data_7FB6
# 
_entry.id   7FB6 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.361 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   7FB6         pdb_00007fb6 10.2210/pdb7fb6/pdb 
WWPDB D_1300023207 ?            ?                   
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        7FB6 
_pdbx_database_status.recvd_initial_deposition_date   2021-07-08 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Baek, Y.'  1 0000-0001-5119-1829 
'Ha, N.-C.' 2 0000-0003-4813-748X 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Commun Biol' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2399-3642 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            5 
_citation.language                  ? 
_citation.page_first                1085 
_citation.page_last                 1085 
_citation.title                     
'Structural analysis of the overoxidized Cu/Zn-superoxide dismutase in ROS-induced ALS filament formation.' 
_citation.year                      2022 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s42003-022-04017-0 
_citation.pdbx_database_id_PubMed   36224351 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Baek, Y.'   1 ?                   
primary 'Woo, T.G.'  2 ?                   
primary 'Ahn, J.'    3 0000-0002-4175-5181 
primary 'Lee, D.'    4 ?                   
primary 'Kwon, Y.'   5 0000-0003-3252-7846 
primary 'Park, B.J.' 6 0000-0002-6037-7219 
primary 'Ha, N.C.'   7 0000-0003-4813-748X 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   93.168 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     7FB6 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     49.319 
_cell.length_a_esd                 ? 
_cell.length_b                     48.554 
_cell.length_b_esd                 ? 
_cell.length_c                     55.015 
_cell.length_c_esd                 ? 
_cell.volume                       131539.501 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         7FB6 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            'P 2yb' 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_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 'Superoxide dismutase [Cu-Zn]' 16746.461 2   1.15.1.1 C57D/C146D ? ? 
2 non-polymer syn 'ZINC ION'                     65.409    2   ?        ?          ? ? 
3 non-polymer syn 'COPPER (II) ION'              63.546    2   ?        ?          ? ? 
4 non-polymer syn 'CHLORIDE ION'                 35.453    1   ?        ?          ? ? 
5 water       nat water                          18.015    155 ?        ?          ? ? 
# 
_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                   yes 
_entity_poly.pdbx_seq_one_letter_code       
;GAMDPEFMATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGDTSAGPHFNPLSRKHG
GPKDEERHVGDLGNVTADKDGVADVSIEDSVISLSGDH(CSO)IIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLADGV
IGIAQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GAMDPEFMATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGDTSAGPHFNPLSRKHG
GPKDEERHVGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLADGVIGIA
Q
;
_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   GLY n 
1 2   ALA n 
1 3   MET n 
1 4   ASP n 
1 5   PRO n 
1 6   GLU n 
1 7   PHE n 
1 8   MET n 
1 9   ALA n 
1 10  THR n 
1 11  LYS n 
1 12  ALA n 
1 13  VAL n 
1 14  CYS n 
1 15  VAL n 
1 16  LEU n 
1 17  LYS n 
1 18  GLY n 
1 19  ASP n 
1 20  GLY n 
1 21  PRO n 
1 22  VAL n 
1 23  GLN n 
1 24  GLY n 
1 25  ILE n 
1 26  ILE n 
1 27  ASN n 
1 28  PHE n 
1 29  GLU n 
1 30  GLN n 
1 31  LYS n 
1 32  GLU n 
1 33  SER n 
1 34  ASN n 
1 35  GLY n 
1 36  PRO n 
1 37  VAL n 
1 38  LYS n 
1 39  VAL n 
1 40  TRP n 
1 41  GLY n 
1 42  SER n 
1 43  ILE n 
1 44  LYS n 
1 45  GLY n 
1 46  LEU n 
1 47  THR n 
1 48  GLU n 
1 49  GLY n 
1 50  LEU n 
1 51  HIS n 
1 52  GLY n 
1 53  PHE n 
1 54  HIS n 
1 55  VAL n 
1 56  HIS n 
1 57  GLU n 
1 58  PHE n 
1 59  GLY n 
1 60  ASP n 
1 61  ASN n 
1 62  THR n 
1 63  ALA n 
1 64  GLY n 
1 65  ASP n 
1 66  THR n 
1 67  SER n 
1 68  ALA n 
1 69  GLY n 
1 70  PRO n 
1 71  HIS n 
1 72  PHE n 
1 73  ASN n 
1 74  PRO n 
1 75  LEU n 
1 76  SER n 
1 77  ARG n 
1 78  LYS n 
1 79  HIS n 
1 80  GLY n 
1 81  GLY n 
1 82  PRO n 
1 83  LYS n 
1 84  ASP n 
1 85  GLU n 
1 86  GLU n 
1 87  ARG n 
1 88  HIS n 
1 89  VAL n 
1 90  GLY n 
1 91  ASP n 
1 92  LEU n 
1 93  GLY n 
1 94  ASN n 
1 95  VAL n 
1 96  THR n 
1 97  ALA n 
1 98  ASP n 
1 99  LYS n 
1 100 ASP n 
1 101 GLY n 
1 102 VAL n 
1 103 ALA n 
1 104 ASP n 
1 105 VAL n 
1 106 SER n 
1 107 ILE n 
1 108 GLU n 
1 109 ASP n 
1 110 SER n 
1 111 VAL n 
1 112 ILE n 
1 113 SER n 
1 114 LEU n 
1 115 SER n 
1 116 GLY n 
1 117 ASP n 
1 118 HIS n 
1 119 CSO n 
1 120 ILE n 
1 121 ILE n 
1 122 GLY n 
1 123 ARG n 
1 124 THR n 
1 125 LEU n 
1 126 VAL n 
1 127 VAL n 
1 128 HIS n 
1 129 GLU n 
1 130 LYS n 
1 131 ALA n 
1 132 ASP n 
1 133 ASP n 
1 134 LEU n 
1 135 GLY n 
1 136 LYS n 
1 137 GLY n 
1 138 GLY n 
1 139 ASN n 
1 140 GLU n 
1 141 GLU n 
1 142 SER n 
1 143 THR n 
1 144 LYS n 
1 145 THR n 
1 146 GLY n 
1 147 ASN n 
1 148 ALA n 
1 149 GLY n 
1 150 SER n 
1 151 ARG n 
1 152 LEU n 
1 153 ALA n 
1 154 ASP n 
1 155 GLY n 
1 156 VAL n 
1 157 ILE n 
1 158 GLY n 
1 159 ILE n 
1 160 ALA n 
1 161 GLN n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   161 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 SOD1 
_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      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    SODC_HUMAN 
_struct_ref.pdbx_db_accession          P00441 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEER
HVGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7FB6 A 8 ? 161 ? P00441 1 ? 154 ? 0 153 
2 1 7FB6 B 8 ? 161 ? P00441 1 ? 154 ? 0 153 
# 
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 7FB6 GLY A 1   ? UNP P00441 ?   ?   'expression tag'      -7  1  
1 7FB6 ALA A 2   ? UNP P00441 ?   ?   'expression tag'      -6  2  
1 7FB6 MET A 3   ? UNP P00441 ?   ?   'expression tag'      -5  3  
1 7FB6 ASP A 4   ? UNP P00441 ?   ?   'expression tag'      -4  4  
1 7FB6 PRO A 5   ? UNP P00441 ?   ?   'expression tag'      -3  5  
1 7FB6 GLU A 6   ? UNP P00441 ?   ?   'expression tag'      -2  6  
1 7FB6 PHE A 7   ? UNP P00441 ?   ?   'expression tag'      -1  7  
1 7FB6 ASP A 65  ? UNP P00441 CYS 58  'engineered mutation' 57  8  
1 7FB6 ASP A 154 ? UNP P00441 CYS 147 'engineered mutation' 146 9  
2 7FB6 GLY B 1   ? UNP P00441 ?   ?   'expression tag'      -7  10 
2 7FB6 ALA B 2   ? UNP P00441 ?   ?   'expression tag'      -6  11 
2 7FB6 MET B 3   ? UNP P00441 ?   ?   'expression tag'      -5  12 
2 7FB6 ASP B 4   ? UNP P00441 ?   ?   'expression tag'      -4  13 
2 7FB6 PRO B 5   ? UNP P00441 ?   ?   'expression tag'      -3  14 
2 7FB6 GLU B 6   ? UNP P00441 ?   ?   'expression tag'      -2  15 
2 7FB6 PHE B 7   ? UNP P00441 ?   ?   'expression tag'      -1  16 
2 7FB6 ASP B 65  ? UNP P00441 CYS 58  'engineered mutation' 57  17 
2 7FB6 ASP B 154 ? UNP P00441 CYS 147 'engineered mutation' 146 18 
# 
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 
CL  non-polymer         . 'CHLORIDE ION'    ? 'Cl -1'          35.453  
CSO 'L-peptide linking' n S-HYDROXYCYSTEINE ? 'C3 H7 N O3 S'   137.158 
CU  non-polymer         . 'COPPER (II) ION' ? 'Cu 2'           63.546  
CYS 'L-peptide linking' y CYSTEINE          ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE         ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'   ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE           ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE         ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER             ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE        ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE           ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE            ? 'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE        ? 'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE     ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE           ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE            ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE         ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN        ? 'C11 H12 N2 O2'  204.225 
VAL 'L-peptide linking' y VALINE            ? 'C5 H11 N O2'    117.146 
ZN  non-polymer         . 'ZINC ION'        ? 'Zn 2'           65.409  
# 
_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                   7FB6 
_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             1.96 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          37.36 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING 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            287.15 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.2M MgCl2, 22% (w/v) PEG 3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100.15 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'ADSC QUANTUM 315' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-04-02 
_diffrn_detector.pdbx_frequency               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.97949 
_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                        'PAL/PLS BEAMLINE 5C (4A)' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97949 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   '5C (4A)' 
_diffrn_source.pdbx_synchrotron_site       PAL/PLS 
# 
_reflns.B_iso_Wilson_estimate                          16.95 
_reflns.entry_id                                       7FB6 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.80 
_reflns.d_resolution_low                               50.00 
_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                                     23316 
_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                           96.7 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                4.8 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          11.9671 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.972 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.113 
_reflns.pdbx_Rpim_I_all                                0.045 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.976 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
_reflns.pdbx_CC_split_method                           ? 
# 
_reflns_shell.d_res_high                                    1.80 
_reflns_shell.d_res_low                                     1.83 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           3.79 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             996 
_reflns_shell.percent_possible_all                          84.2 
_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                                  ? 
_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                               3.3 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_chi_squared                              1.133 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               0.297 
_reflns_shell.pdbx_Rpim_I_all                               0.139 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.925 
_reflns_shell.pdbx_CC_star                                  0.980 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               20.86 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 7FB6 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.80 
_refine.ls_d_res_low                             36.38 
_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                     21300 
_refine.ls_number_reflns_R_free                  1024 
_refine.ls_number_reflns_R_work                  20276 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    88.15 
_refine.ls_percent_reflns_R_free                 4.81 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1856 
_refine.ls_R_factor_R_free                       0.2130 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1843 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.52 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      1PU0 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1100 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 20.5725 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.1690 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.80 
_refine_hist.d_res_low                        36.38 
_refine_hist.number_atoms_solvent             155 
_refine_hist.number_atoms_total               2351 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        2191 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         5 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0084  ? 2241 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.1041  ? 3023 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0744  ? 330  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0072  ? 410  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 14.8000 ? 810  ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
'X-RAY DIFFRACTION' 1.80 1.90  . . 90  1910 58.46 . . . 0.2498 . 0.2090 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 1.90 2.02  . . 142 2359 73.32 . . . 0.2083 . 0.1938 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 2.02 2.17  . . 159 2942 90.17 . . . 0.2611 . 0.1987 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 2.17 2.39  . . 143 3192 97.06 . . . 0.2259 . 0.2016 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 2.39 2.74  . . 149 3271 98.90 . . . 0.2594 . 0.2043 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 2.74 3.45  . . 195 3257 99.48 . . . 0.2174 . 0.1946 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 3.45 36.38 . . 146 3345 99.12 . . . 0.1596 . 0.1547 . . . . . . . . . . . 
# 
_struct.entry_id                     7FB6 
_struct.title                        'C57D/C146D mutant of Human Cu, Zn Superoxide Dismutase (SOD1)' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        7FB6 
_struct_keywords.text            'Superoxide, oxidation, metalloprotein, hydrogen peroxide, filament, ALS, 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 3 ? 
E N N 4 ? 
F N N 2 ? 
G N N 3 ? 
H N N 5 ? 
I N N 5 ? 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 ASP A 65  ? GLY A 69  ? ASP A 57  GLY A 61  5 ? 5 
HELX_P HELX_P2 AA2 GLU A 140 ? LYS A 144 ? GLU A 132 LYS A 136 5 ? 5 
HELX_P HELX_P3 AA3 GLU B 141 ? GLY B 146 ? GLU B 133 GLY B 138 1 ? 6 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
covale1  covale both ? A HIS 118 C   ? ? ? 1_555 A CSO 119 N  ? ? A HIS 110 A CSO 111 1_555 ? ? ? ? ? ? ? 1.328 ? ? 
covale2  covale both ? A CSO 119 C   ? ? ? 1_555 A ILE 120 N  ? ? A CSO 111 A ILE 112 1_555 ? ? ? ? ? ? ? 1.331 ? ? 
covale3  covale both ? B HIS 118 C   ? ? ? 1_555 B CSO 119 N  ? ? B HIS 110 B CSO 111 1_555 ? ? ? ? ? ? ? 1.327 ? ? 
covale4  covale both ? B CSO 119 C   ? ? ? 1_555 B ILE 120 N  ? ? B CSO 111 B ILE 112 1_555 ? ? ? ? ? ? ? 1.334 ? ? 
metalc1  metalc ?    ? A HIS 54  ND1 ? ? ? 1_555 D CU  .   CU ? ? A HIS 46  A CU  155 1_555 ? ? ? ? ? ? ? 2.386 ? ? 
metalc2  metalc ?    ? A HIS 56  NE2 ? ? ? 1_555 D CU  .   CU ? ? A HIS 48  A CU  155 1_555 ? ? ? ? ? ? ? 2.249 ? ? 
metalc3  metalc ?    ? A HIS 71  ND1 ? ? ? 1_555 C ZN  .   ZN ? ? A HIS 63  A ZN  154 1_555 ? ? ? ? ? ? ? 2.064 ? ? 
metalc4  metalc ?    ? A HIS 79  ND1 ? ? ? 1_555 C ZN  .   ZN ? ? A HIS 71  A ZN  154 1_555 ? ? ? ? ? ? ? 2.130 ? ? 
metalc5  metalc ?    ? A HIS 88  ND1 ? ? ? 1_555 C ZN  .   ZN ? ? A HIS 80  A ZN  154 1_555 ? ? ? ? ? ? ? 2.161 ? ? 
metalc6  metalc ?    ? A ASP 91  OD1 ? ? ? 1_555 C ZN  .   ZN ? ? A ASP 83  A ZN  154 1_555 ? ? ? ? ? ? ? 1.998 ? ? 
metalc7  metalc ?    ? A HIS 128 NE2 ? ? ? 1_555 D CU  .   CU ? ? A HIS 120 A CU  155 1_555 ? ? ? ? ? ? ? 2.011 ? ? 
metalc8  metalc ?    ? B HIS 54  ND1 ? ? ? 1_555 G CU  .   CU ? ? B HIS 46  B CU  155 1_555 ? ? ? ? ? ? ? 2.258 ? ? 
metalc9  metalc ?    ? B HIS 56  NE2 ? ? ? 1_555 G CU  .   CU ? ? B HIS 48  B CU  155 1_555 ? ? ? ? ? ? ? 2.210 ? ? 
metalc10 metalc ?    ? B HIS 71  ND1 ? ? ? 1_555 F ZN  .   ZN ? ? B HIS 63  B ZN  154 1_555 ? ? ? ? ? ? ? 2.248 ? ? 
metalc11 metalc ?    ? B HIS 71  NE2 ? ? ? 1_555 G CU  .   CU ? ? B HIS 63  B CU  155 1_555 ? ? ? ? ? ? ? 2.545 ? ? 
metalc12 metalc ?    ? B HIS 79  ND1 ? ? ? 1_555 F ZN  .   ZN ? ? B HIS 71  B ZN  154 1_555 ? ? ? ? ? ? ? 2.244 ? ? 
metalc13 metalc ?    ? B HIS 88  ND1 ? ? ? 1_555 F ZN  .   ZN ? ? B HIS 80  B ZN  154 1_555 ? ? ? ? ? ? ? 2.254 ? ? 
metalc14 metalc ?    ? B ASP 91  OD1 ? ? ? 1_555 F ZN  .   ZN ? ? B ASP 83  B ZN  154 1_555 ? ? ? ? ? ? ? 1.965 ? ? 
metalc15 metalc ?    ? B HIS 128 NE2 ? ? ? 1_555 G CU  .   CU ? ? B HIS 120 B CU  155 1_555 ? ? ? ? ? ? ? 2.131 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
covale ? ? 
metalc ? ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 5 ? 
AA2 ? 4 ? 
AA3 ? 5 ? 
AA4 ? 4 ? 
# 
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 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? 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 ALA A 103 ? ASP A 109 ? ALA A 95  ASP A 101 
AA1 2 VAL A 37  ? LYS A 44  ? VAL A 29  LYS A 36  
AA1 3 GLN A 23  ? GLU A 29  ? GLN A 15  GLU A 21  
AA1 4 LYS A 11  ? LYS A 17  ? LYS A 3   LYS A 9   
AA1 5 GLY A 158 ? ILE A 159 ? GLY A 150 ILE A 151 
AA2 1 ASP A 91  ? ALA A 97  ? ASP A 83  ALA A 89  
AA2 2 GLY A 49  ? HIS A 56  ? GLY A 41  HIS A 48  
AA2 3 THR A 124 ? HIS A 128 ? THR A 116 HIS A 120 
AA2 4 ARG A 151 ? VAL A 156 ? ARG A 143 VAL A 148 
AA3 1 ALA B 103 ? ASP B 109 ? ALA B 95  ASP B 101 
AA3 2 VAL B 37  ? LYS B 44  ? VAL B 29  LYS B 36  
AA3 3 GLN B 23  ? GLU B 29  ? GLN B 15  GLU B 21  
AA3 4 LYS B 11  ? LEU B 16  ? LYS B 3   LEU B 8   
AA3 5 GLY B 158 ? ILE B 159 ? GLY B 150 ILE B 151 
AA4 1 ASP B 91  ? ALA B 97  ? ASP B 83  ALA B 89  
AA4 2 GLY B 49  ? HIS B 56  ? GLY B 41  HIS B 48  
AA4 3 THR B 124 ? HIS B 128 ? THR B 116 HIS B 120 
AA4 4 ARG B 151 ? VAL B 156 ? ARG B 143 VAL B 148 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O ILE A 107 ? O ILE A 99  N VAL A 39  ? N VAL A 31  
AA1 2 3 O LYS A 44  ? O LYS A 36  N GLN A 23  ? N GLN A 15  
AA1 3 4 O PHE A 28  ? O PHE A 20  N ALA A 12  ? N ALA A 4   
AA1 4 5 N VAL A 13  ? N VAL A 5   O GLY A 158 ? O GLY A 150 
AA2 1 2 O ALA A 97  ? O ALA A 89  N GLY A 49  ? N GLY A 41  
AA2 2 3 N HIS A 56  ? N HIS A 48  O THR A 124 ? O THR A 116 
AA2 3 4 N LEU A 125 ? N LEU A 117 O GLY A 155 ? O GLY A 147 
AA3 1 2 O ILE B 107 ? O ILE B 99  N VAL B 39  ? N VAL B 31  
AA3 2 3 O TRP B 40  ? O TRP B 32  N ASN B 27  ? N ASN B 19  
AA3 3 4 O PHE B 28  ? O PHE B 20  N ALA B 12  ? N ALA B 4   
AA3 4 5 N VAL B 13  ? N VAL B 5   O GLY B 158 ? O GLY B 150 
AA4 1 2 O ALA B 97  ? O ALA B 89  N GLY B 49  ? N GLY B 41  
AA4 2 3 N HIS B 56  ? N HIS B 48  O THR B 124 ? O THR B 116 
AA4 3 4 N VAL B 127 ? N VAL B 119 O LEU B 152 ? O LEU B 144 
# 
_atom_sites.entry_id                    7FB6 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.fract_transf_matrix[1][1]   0.020276 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.001122 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.020596 
_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]   0.018205 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C  ? ? 3.54356  2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
CL ? ? 9.50761  7.44341 ? ? 1.04373  23.83732 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
CU ? ? 23.42449 5.47274 ? ? 2.18335  24.96234 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N  ? ? 4.01032  2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O  ? ? 4.49882  3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S  ? ? 9.55732  6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
ZN ? ? 24.64596 5.25405 ? ? 2.14387  29.76375 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . PHE A 1 7   ? -3.46100  -11.41300 38.01800 1.000 38.83844 ? -1  PHE A N   1 
ATOM   2    C  CA  . PHE A 1 7   ? -3.63300  -10.09500 37.41900 1.000 26.50853 ? -1  PHE A CA  1 
ATOM   3    C  C   . PHE A 1 7   ? -3.13600  -10.06900 35.97700 1.000 30.89084 ? -1  PHE A C   1 
ATOM   4    O  O   . PHE A 1 7   ? -2.18400  -10.76200 35.61500 1.000 31.59467 ? -1  PHE A O   1 
ATOM   5    C  CB  . PHE A 1 7   ? -2.90700  -9.02800  38.24400 1.000 29.23888 ? -1  PHE A CB  1 
ATOM   6    C  CG  . PHE A 1 7   ? -2.90000  -7.66900  37.60300 1.000 24.72155 ? -1  PHE A CG  1 
ATOM   7    C  CD1 . PHE A 1 7   ? -4.01800  -6.85600  37.66300 1.000 26.40578 ? -1  PHE A CD1 1 
ATOM   8    C  CD2 . PHE A 1 7   ? -1.77600  -7.20700  36.93800 1.000 24.07929 ? -1  PHE A CD2 1 
ATOM   9    C  CE1 . PHE A 1 7   ? -4.01500  -5.61000  37.07400 1.000 27.92603 ? -1  PHE A CE1 1 
ATOM   10   C  CE2 . PHE A 1 7   ? -1.76800  -5.96000  36.34600 1.000 21.79799 ? -1  PHE A CE2 1 
ATOM   11   C  CZ  . PHE A 1 7   ? -2.88800  -5.16100  36.41400 1.000 24.57292 ? -1  PHE A CZ  1 
ATOM   12   N  N   . MET A 1 8   ? -3.78900  -9.24700  35.16100 1.000 29.41337 ? 0   MET A N   1 
ATOM   13   C  CA  . MET A 1 8   ? -3.48300  -9.14200  33.73800 1.000 28.48230 ? 0   MET A CA  1 
ATOM   14   C  C   . MET A 1 8   ? -3.49700  -7.67000  33.36200 1.000 26.24238 ? 0   MET A C   1 
ATOM   15   O  O   . MET A 1 8   ? -4.56600  -7.05600  33.29200 1.000 27.05947 ? 0   MET A O   1 
ATOM   16   C  CB  . MET A 1 8   ? -4.49400  -9.92500  32.90700 1.000 29.84483 ? 0   MET A CB  1 
ATOM   17   C  CG  . MET A 1 8   ? -4.41000  -9.65700  31.42800 1.000 29.34516 ? 0   MET A CG  1 
ATOM   18   S  SD  . MET A 1 8   ? -4.90000  -11.12900 30.53200 1.000 45.97870 ? 0   MET A SD  1 
ATOM   19   C  CE  . MET A 1 8   ? -3.87800  -12.33400 31.37200 1.000 27.50793 ? 0   MET A CE  1 
ATOM   20   N  N   . ALA A 1 9   ? -2.32000  -7.10300  33.12500 1.000 20.39026 ? 1   ALA A N   1 
ATOM   21   C  CA  . ALA A 1 9   ? -2.24500  -5.68600  32.80900 1.000 17.40260 ? 1   ALA A CA  1 
ATOM   22   C  C   . ALA A 1 9   ? -2.81600  -5.41100  31.42600 1.000 17.18316 ? 1   ALA A C   1 
ATOM   23   O  O   . ALA A 1 9   ? -2.57800  -6.16200  30.47500 1.000 19.48551 ? 1   ALA A O   1 
ATOM   24   C  CB  . ALA A 1 9   ? -0.80100  -5.19900  32.87800 1.000 19.15325 ? 1   ALA A CB  1 
ATOM   25   N  N   . THR A 1 10  ? -3.59000  -4.32800  31.32700 1.000 19.27704 ? 2   THR A N   1 
ATOM   26   C  CA  . THR A 1 10  ? -4.05300  -3.80500  30.05200 1.000 19.20136 ? 2   THR A CA  1 
ATOM   27   C  C   . THR A 1 10  ? -3.34800  -2.52000  29.64600 1.000 13.47891 ? 2   THR A C   1 
ATOM   28   O  O   . THR A 1 10  ? -3.38200  -2.16700  28.46400 1.000 18.30650 ? 2   THR A O   1 
ATOM   29   C  CB  . THR A 1 10  ? -5.56700  -3.54200  30.09200 1.000 17.32092 ? 2   THR A CB  1 
ATOM   30   O  OG1 . THR A 1 10  ? -5.89900  -2.84500  31.29600 1.000 25.31122 ? 2   THR A OG1 1 
ATOM   31   C  CG2 . THR A 1 10  ? -6.34400  -4.84600  30.04200 1.000 20.55263 ? 2   THR A CG2 1 
ATOM   32   N  N   . LYS A 1 11  ? -2.72400  -1.81400  30.58800 1.000 15.67445 ? 3   LYS A N   1 
ATOM   33   C  CA  . LYS A 1 11  ? -1.99800  -0.58800  30.28900 1.000 18.49938 ? 3   LYS A CA  1 
ATOM   34   C  C   . LYS A 1 11  ? -0.71000  -0.53600  31.09700 1.000 15.92181 ? 3   LYS A C   1 
ATOM   35   O  O   . LYS A 1 11  ? -0.62600  -1.07000  32.20900 1.000 12.51587 ? 3   LYS A O   1 
ATOM   36   C  CB  . LYS A 1 11  ? -2.83300  0.66400   30.58100 1.000 18.96660 ? 3   LYS A CB  1 
ATOM   37   C  CG  . LYS A 1 11  ? -4.15900  0.71600   29.84400 1.000 25.00556 ? 3   LYS A CG  1 
ATOM   38   C  CD  . LYS A 1 11  ? -4.51600  2.14000   29.45800 1.000 34.23236 ? 3   LYS A CD  1 
ATOM   39   C  CE  . LYS A 1 11  ? -5.89800  2.52200   29.95200 1.000 34.51293 ? 3   LYS A CE  1 
ATOM   40   N  NZ  . LYS A 1 11  ? -6.41000  3.73800   29.26300 1.000 35.94794 ? 3   LYS A NZ  1 
ATOM   41   N  N   . ALA A 1 12  ? 0.29200   0.11900   30.51800 1.000 15.70230 ? 4   ALA A N   1 
ATOM   42   C  CA  . ALA A 1 12  ? 1.58300   0.32700   31.15500 1.000 15.86987 ? 4   ALA A CA  1 
ATOM   43   C  C   . ALA A 1 12  ? 2.09600   1.71200   30.78000 1.000 16.42944 ? 4   ALA A C   1 
ATOM   44   O  O   . ALA A 1 12  ? 1.61800   2.33400   29.82900 1.000 15.43673 ? 4   ALA A O   1 
ATOM   45   C  CB  . ALA A 1 12  ? 2.59100   -0.75400  30.74300 1.000 13.78279 ? 4   ALA A CB  1 
ATOM   46   N  N   . VAL A 1 13  ? 3.06800   2.20400   31.54900 1.000 14.67591 ? 5   VAL A N   1 
ATOM   47   C  CA  . VAL A 1 13  ? 3.65600   3.51600   31.30200 1.000 15.37786 ? 5   VAL A CA  1 
ATOM   48   C  C   . VAL A 1 13  ? 5.14800   3.44500   31.59300 1.000 12.30688 ? 5   VAL A C   1 
ATOM   49   O  O   . VAL A 1 13  ? 5.59800   2.65600   32.42800 1.000 14.23005 ? 5   VAL A O   1 
ATOM   50   C  CB  . VAL A 1 13  ? 2.98500   4.61800   32.15200 1.000 14.70943 ? 5   VAL A CB  1 
ATOM   51   C  CG1 . VAL A 1 13  ? 3.25600   4.38800   33.63000 1.000 14.05134 ? 5   VAL A CG1 1 
ATOM   52   C  CG2 . VAL A 1 13  ? 3.45200   6.00600   31.71400 1.000 12.31517 ? 5   VAL A CG2 1 
ATOM   53   N  N   . CYS A 1 14  ? 5.92100   4.27000   30.89000 1.000 15.59049 ? 6   CYS A N   1 
ATOM   54   C  CA  . CYS A 1 14  ? 7.35600   4.37100   31.13200 1.000 9.64816  ? 6   CYS A CA  1 
ATOM   55   C  C   . CYS A 1 14  ? 7.77400   5.83000   31.06300 1.000 12.51341 ? 6   CYS A C   1 
ATOM   56   O  O   . CYS A 1 14  ? 7.55300   6.49700   30.04800 1.000 12.15714 ? 6   CYS A O   1 
ATOM   57   C  CB  . CYS A 1 14  ? 8.15800   3.54000   30.13200 1.000 12.51156 ? 6   CYS A CB  1 
ATOM   58   S  SG  . CYS A 1 14  ? 9.93600   3.60200   30.44100 1.000 14.32591 ? 6   CYS A SG  1 
ATOM   59   N  N   . VAL A 1 15  ? 8.37500   6.31400   32.14400 1.000 13.76993 ? 7   VAL A N   1 
ATOM   60   C  CA  . VAL A 1 15  ? 8.94800   7.65200   32.20000 1.000 14.41621 ? 7   VAL A CA  1 
ATOM   61   C  C   . VAL A 1 15  ? 10.42200  7.55300   31.82700 1.000 12.03288 ? 7   VAL A C   1 
ATOM   62   O  O   . VAL A 1 15  ? 11.20400  6.92500   32.54600 1.000 13.12322 ? 7   VAL A O   1 
ATOM   63   C  CB  . VAL A 1 15  ? 8.77700   8.26400   33.59900 1.000 16.77271 ? 7   VAL A CB  1 
ATOM   64   C  CG1 . VAL A 1 15  ? 9.40100   9.65100   33.65200 1.000 16.19656 ? 7   VAL A CG1 1 
ATOM   65   C  CG2 . VAL A 1 15  ? 7.30400   8.30100   33.98800 1.000 15.07901 ? 7   VAL A CG2 1 
ATOM   66   N  N   . LEU A 1 16  ? 10.80300  8.16700   30.70600 1.000 15.73266 ? 8   LEU A N   1 
ATOM   67   C  CA  . LEU A 1 16  ? 12.18000  8.12500   30.21400 1.000 13.22736 ? 8   LEU A CA  1 
ATOM   68   C  C   . LEU A 1 16  ? 12.96300  9.33800   30.71200 1.000 18.46782 ? 8   LEU A C   1 
ATOM   69   O  O   . LEU A 1 16  ? 12.56400  10.48200  30.46900 1.000 17.50769 ? 8   LEU A O   1 
ATOM   70   C  CB  . LEU A 1 16  ? 12.20800  8.08800   28.68600 1.000 12.54141 ? 8   LEU A CB  1 
ATOM   71   C  CG  . LEU A 1 16  ? 11.55400  6.90800   27.97500 1.000 14.79139 ? 8   LEU A CG  1 
ATOM   72   C  CD1 . LEU A 1 16  ? 11.46800  7.19900   26.48200 1.000 11.62147 ? 8   LEU A CD1 1 
ATOM   73   C  CD2 . LEU A 1 16  ? 12.34400  5.63700   28.21900 1.000 14.57427 ? 8   LEU A CD2 1 
ATOM   74   N  N   . LYS A 1 17  ? 14.08900  9.09100   31.38400 1.000 16.32866 ? 9   LYS A N   1 
ATOM   75   C  CA  . LYS A 1 17  ? 14.96300  10.16300  31.84300 1.000 16.91097 ? 9   LYS A CA  1 
ATOM   76   C  C   . LYS A 1 17  ? 16.41800  9.78000   31.60900 1.000 16.50393 ? 9   LYS A C   1 
ATOM   77   O  O   . LYS A 1 17  ? 16.77600  8.60000   31.56100 1.000 15.74866 ? 9   LYS A O   1 
ATOM   78   C  CB  . LYS A 1 17  ? 14.76500  10.47600  33.33200 1.000 16.90215 ? 9   LYS A CB  1 
ATOM   79   C  CG  . LYS A 1 17  ? 13.34900  10.82700  33.73800 1.000 27.59798 ? 9   LYS A CG  1 
ATOM   80   C  CD  . LYS A 1 17  ? 13.31300  11.26500  35.19900 1.000 30.16515 ? 9   LYS A CD  1 
ATOM   81   C  CE  . LYS A 1 17  ? 11.88900  11.48500  35.68200 1.000 36.50825 ? 9   LYS A CE  1 
ATOM   82   N  NZ  . LYS A 1 17  ? 11.55300  10.59500  36.83100 1.000 35.51695 ? 9   LYS A NZ  1 
ATOM   83   N  N   . GLY A 1 18  ? 17.26200  10.80100  31.50000 1.000 17.18554 ? 10  GLY A N   1 
ATOM   84   C  CA  . GLY A 1 18  ? 18.68500  10.59100  31.32900 1.000 24.41454 ? 10  GLY A CA  1 
ATOM   85   C  C   . GLY A 1 18  ? 19.52000  11.70800  31.91700 1.000 26.63173 ? 10  GLY A C   1 
ATOM   86   O  O   . GLY A 1 18  ? 19.00400  12.56100  32.64700 1.000 25.78758 ? 10  GLY A O   1 
ATOM   87   N  N   . ASP A 1 19  ? 20.81600  11.71800  31.60200 1.000 26.90889 ? 11  ASP A N   1 
ATOM   88   C  CA  . ASP A 1 19  ? 21.72000  12.73100  32.13500 1.000 28.71112 ? 11  ASP A CA  1 
ATOM   89   C  C   . ASP A 1 19  ? 21.64200  14.05400  31.38600 1.000 28.72869 ? 11  ASP A C   1 
ATOM   90   O  O   . ASP A 1 19  ? 22.23900  15.03500  31.84200 1.000 30.30157 ? 11  ASP A O   1 
ATOM   91   C  CB  . ASP A 1 19  ? 23.16300  12.21500  32.10800 1.000 36.83599 ? 11  ASP A CB  1 
ATOM   92   C  CG  . ASP A 1 19  ? 23.30900  10.85300  32.76500 1.000 43.29976 ? 11  ASP A CG  1 
ATOM   93   O  OD1 . ASP A 1 19  ? 22.34500  10.39900  33.42200 1.000 48.29487 ? 11  ASP A OD1 1 
ATOM   94   O  OD2 . ASP A 1 19  ? 24.38300  10.23000  32.61700 1.000 48.58621 ? 11  ASP A OD2 1 
ATOM   95   N  N   . GLY A 1 20  ? 20.92500  14.11100  30.26500 1.000 22.05256 ? 12  GLY A N   1 
ATOM   96   C  CA  . GLY A 1 20  ? 20.86400  15.30800  29.46300 1.000 21.39897 ? 12  GLY A CA  1 
ATOM   97   C  C   . GLY A 1 20  ? 19.45300  15.81100  29.24900 1.000 21.99631 ? 12  GLY A C   1 
ATOM   98   O  O   . GLY A 1 20  ? 18.58000  15.67200  30.11100 1.000 25.77120 ? 12  GLY A O   1 
ATOM   99   N  N   . PRO A 1 21  ? 19.20400  16.41700  28.08400 1.000 21.64886 ? 13  PRO A N   1 
ATOM   100  C  CA  . PRO A 1 21  ? 17.88400  17.00700  27.81700 1.000 24.95967 ? 13  PRO A CA  1 
ATOM   101  C  C   . PRO A 1 21  ? 16.81700  16.01500  27.39400 1.000 24.17399 ? 13  PRO A C   1 
ATOM   102  O  O   . PRO A 1 21  ? 15.64800  16.41100  27.28800 1.000 24.76835 ? 13  PRO A O   1 
ATOM   103  C  CB  . PRO A 1 21  ? 18.17500  17.99200  26.67900 1.000 26.27712 ? 13  PRO A CB  1 
ATOM   104  C  CG  . PRO A 1 21  ? 19.31700  17.37100  25.95000 1.000 25.65897 ? 13  PRO A CG  1 
ATOM   105  C  CD  . PRO A 1 21  ? 20.16900  16.71700  27.01100 1.000 26.09655 ? 13  PRO A CD  1 
ATOM   106  N  N   . VAL A 1 22  ? 17.16300  14.75900  27.13800 1.000 20.29826 ? 14  VAL A N   1 
ATOM   107  C  CA  . VAL A 1 22  ? 16.20700  13.81600  26.57100 1.000 19.00004 ? 14  VAL A CA  1 
ATOM   108  C  C   . VAL A 1 22  ? 15.28600  13.29600  27.66600 1.000 17.51132 ? 14  VAL A C   1 
ATOM   109  O  O   . VAL A 1 22  ? 15.74500  12.78100  28.69100 1.000 18.45315 ? 14  VAL A O   1 
ATOM   110  C  CB  . VAL A 1 22  ? 16.93000  12.66000  25.86700 1.000 15.22104 ? 14  VAL A CB  1 
ATOM   111  C  CG1 . VAL A 1 22  ? 15.90600  11.70800  25.27300 1.000 15.58697 ? 14  VAL A CG1 1 
ATOM   112  C  CG2 . VAL A 1 22  ? 17.87100  13.19600  24.79200 1.000 12.91179 ? 14  VAL A CG2 1 
ATOM   113  N  N   . GLN A 1 23  ? 13.98100  13.41600  27.44100 1.000 16.83226 ? 15  GLN A N   1 
ATOM   114  C  CA  . GLN A 1 23  ? 12.98900  12.92700  28.38700 1.000 16.31681 ? 15  GLN A CA  1 
ATOM   115  C  C   . GLN A 1 23  ? 11.66900  12.74500  27.65300 1.000 12.05334 ? 15  GLN A C   1 
ATOM   116  O  O   . GLN A 1 23  ? 11.43400  13.35200  26.60600 1.000 17.40469 ? 15  GLN A O   1 
ATOM   117  C  CB  . GLN A 1 23  ? 12.83300  13.88300  29.57600 1.000 23.65409 ? 15  GLN A CB  1 
ATOM   118  C  CG  . GLN A 1 23  ? 12.47000  15.30400  29.18600 1.000 26.29962 ? 15  GLN A CG  1 
ATOM   119  C  CD  . GLN A 1 23  ? 12.39800  16.23200  30.38400 1.000 41.51326 ? 15  GLN A CD  1 
ATOM   120  O  OE1 . GLN A 1 23  ? 12.81600  17.38900  30.31300 1.000 50.30570 ? 15  GLN A OE1 1 
ATOM   121  N  NE2 . GLN A 1 23  ? 11.86400  15.72900  31.49200 1.000 42.09952 ? 15  GLN A NE2 1 
ATOM   122  N  N   . GLY A 1 24  ? 10.81000  11.90000  28.21000 1.000 17.84234 ? 16  GLY A N   1 
ATOM   123  C  CA  . GLY A 1 24  ? 9.52400   11.65100  27.58100 1.000 19.08848 ? 16  GLY A CA  1 
ATOM   124  C  C   . GLY A 1 24  ? 8.69800   10.67600  28.39000 1.000 16.90134 ? 16  GLY A C   1 
ATOM   125  O  O   . GLY A 1 24  ? 9.15700   10.10600  29.38500 1.000 14.95200 ? 16  GLY A O   1 
ATOM   126  N  N   . ILE A 1 25  ? 7.45600   10.50100  27.94400 1.000 16.68015 ? 17  ILE A N   1 
ATOM   127  C  CA  . ILE A 1 25  ? 6.50200   9.58300   28.55500 1.000 15.35553 ? 17  ILE A CA  1 
ATOM   128  C  C   . ILE A 1 25  ? 5.99300   8.65200   27.46700 1.000 15.11736 ? 17  ILE A C   1 
ATOM   129  O  O   . ILE A 1 25  ? 5.55300   9.11800   26.41000 1.000 14.56214 ? 17  ILE A O   1 
ATOM   130  C  CB  . ILE A 1 25  ? 5.32000   10.32800  29.20800 1.000 22.84305 ? 17  ILE A CB  1 
ATOM   131  C  CG1 . ILE A 1 25  ? 5.80900   11.32400  30.26500 1.000 21.06089 ? 17  ILE A CG1 1 
ATOM   132  C  CG2 . ILE A 1 25  ? 4.31800   9.33500   29.80000 1.000 18.44110 ? 17  ILE A CG2 1 
ATOM   133  C  CD1 . ILE A 1 25  ? 6.20000   10.67900  31.56600 1.000 26.18916 ? 17  ILE A CD1 1 
ATOM   134  N  N   . ILE A 1 26  ? 6.04200   7.34600   27.72100 1.000 13.50701 ? 18  ILE A N   1 
ATOM   135  C  CA  . ILE A 1 26  ? 5.60500   6.34100   26.75800 1.000 13.75595 ? 18  ILE A CA  1 
ATOM   136  C  C   . ILE A 1 26  ? 4.48400   5.51800   27.37800 1.000 15.20738 ? 18  ILE A C   1 
ATOM   137  O  O   . ILE A 1 26  ? 4.63600   4.98200   28.48300 1.000 13.43543 ? 18  ILE A O   1 
ATOM   138  C  CB  . ILE A 1 26  ? 6.76200   5.43100   26.31000 1.000 14.27052 ? 18  ILE A CB  1 
ATOM   139  C  CG1 . ILE A 1 26  ? 7.86200   6.26600   25.65900 1.000 13.12655 ? 18  ILE A CG1 1 
ATOM   140  C  CG2 . ILE A 1 26  ? 6.25500   4.38200   25.33100 1.000 12.46772 ? 18  ILE A CG2 1 
ATOM   141  C  CD1 . ILE A 1 26  ? 7.40300   6.99900   24.41600 1.000 13.89472 ? 18  ILE A CD1 1 
ATOM   142  N  N   . ASN A 1 27  ? 3.36900   5.41800   26.66100 1.000 14.19604 ? 19  ASN A N   1 
ATOM   143  C  CA  . ASN A 1 27  ? 2.19800   4.67600   27.10000 1.000 13.95083 ? 19  ASN A CA  1 
ATOM   144  C  C   . ASN A 1 27  ? 2.08100   3.37700   26.31700 1.000 12.24064 ? 19  ASN A C   1 
ATOM   145  O  O   . ASN A 1 27  ? 2.38300   3.33200   25.12000 1.000 14.65848 ? 19  ASN A O   1 
ATOM   146  C  CB  . ASN A 1 27  ? 0.92300   5.50300   26.91700 1.000 15.22818 ? 19  ASN A CB  1 
ATOM   147  C  CG  . ASN A 1 27  ? 0.97000   6.81200   27.67500 1.000 19.43330 ? 19  ASN A CG  1 
ATOM   148  O  OD1 . ASN A 1 27  ? 0.86500   6.83400   28.90300 1.000 17.62879 ? 19  ASN A OD1 1 
ATOM   149  N  ND2 . ASN A 1 27  ? 1.13200   7.91300   26.94700 1.000 18.60888 ? 19  ASN A ND2 1 
ATOM   150  N  N   . PHE A 1 28  ? 1.64300   2.32400   27.00300 1.000 14.67185 ? 20  PHE A N   1 
ATOM   151  C  CA  . PHE A 1 28  ? 1.40100   1.02000   26.40400 1.000 13.63544 ? 20  PHE A CA  1 
ATOM   152  C  C   . PHE A 1 28  ? -0.04100  0.61100   26.66600 1.000 14.70979 ? 20  PHE A C   1 
ATOM   153  O  O   . PHE A 1 28  ? -0.55900  0.81800   27.76600 1.000 15.08115 ? 20  PHE A O   1 
ATOM   154  C  CB  . PHE A 1 28  ? 2.33600   -0.04400  26.97900 1.000 13.71720 ? 20  PHE A CB  1 
ATOM   155  C  CG  . PHE A 1 28  ? 3.79800   0.24600   26.77800 1.000 16.25599 ? 20  PHE A CG  1 
ATOM   156  C  CD1 . PHE A 1 28  ? 4.48700   1.05900   27.66400 1.000 13.22209 ? 20  PHE A CD1 1 
ATOM   157  C  CD2 . PHE A 1 28  ? 4.49000   -0.32600  25.72300 1.000 16.13292 ? 20  PHE A CD2 1 
ATOM   158  C  CE1 . PHE A 1 28  ? 5.84200   1.30900   27.48900 1.000 13.62232 ? 20  PHE A CE1 1 
ATOM   159  C  CE2 . PHE A 1 28  ? 5.83800   -0.07900  25.54200 1.000 17.74656 ? 20  PHE A CE2 1 
ATOM   160  C  CZ  . PHE A 1 28  ? 6.51300   0.74300   26.42400 1.000 16.96140 ? 20  PHE A CZ  1 
ATOM   161  N  N   . GLU A 1 29  ? -0.68000  0.01300   25.66300 1.000 16.27829 ? 21  GLU A N   1 
ATOM   162  C  CA  . GLU A 1 29  ? -2.06300  -0.42400  25.78800 1.000 19.75878 ? 21  GLU A CA  1 
ATOM   163  C  C   . GLU A 1 29  ? -2.23700  -1.76900  25.10000 1.000 20.49078 ? 21  GLU A C   1 
ATOM   164  O  O   . GLU A 1 29  ? -1.73800  -1.97200  23.99200 1.000 18.68907 ? 21  GLU A O   1 
ATOM   165  C  CB  . GLU A 1 29  ? -3.02700  0.60900   25.18600 1.000 22.37472 ? 21  GLU A CB  1 
ATOM   166  C  CG  . GLU A 1 29  ? -4.49800  0.28400   25.37000 1.000 35.78924 ? 21  GLU A CG  1 
ATOM   167  C  CD  . GLU A 1 29  ? -5.39900  1.29800   24.69100 1.000 44.29338 ? 21  GLU A CD  1 
ATOM   168  O  OE1 . GLU A 1 29  ? -5.32900  2.49300   25.05400 1.000 44.71271 ? 21  GLU A OE1 1 
ATOM   169  O  OE2 . GLU A 1 29  ? -6.16200  0.90100   23.78300 1.000 39.68939 ? 21  GLU A OE2 1 
ATOM   170  N  N   . GLN A 1 30  ? -2.95100  -2.68400  25.76100 1.000 17.19619 ? 22  GLN A N   1 
ATOM   171  C  CA  . GLN A 1 30  ? -3.19000  -4.01700  25.19800 1.000 17.64588 ? 22  GLN A CA  1 
ATOM   172  C  C   . GLN A 1 30  ? -4.50300  -4.54500  25.78400 1.000 20.75349 ? 22  GLN A C   1 
ATOM   173  O  O   . GLN A 1 30  ? -4.51200  -5.16700  26.84800 1.000 17.06490 ? 22  GLN A O   1 
ATOM   174  C  CB  . GLN A 1 30  ? -2.02900  -4.95500  25.49200 1.000 18.03430 ? 22  GLN A CB  1 
ATOM   175  C  CG  . GLN A 1 30  ? -2.05500  -6.22600  24.66800 1.000 19.71620 ? 22  GLN A CG  1 
ATOM   176  C  CD  . GLN A 1 30  ? -1.12200  -7.29300  25.20000 1.000 21.82100 ? 22  GLN A CD  1 
ATOM   177  O  OE1 . GLN A 1 30  ? -0.75900  -7.29100  26.37900 1.000 20.49024 ? 22  GLN A OE1 1 
ATOM   178  N  NE2 . GLN A 1 30  ? -0.73200  -8.22000  24.33200 1.000 18.77028 ? 22  GLN A NE2 1 
ATOM   179  N  N   . LYS A 1 31  ? -5.60700  -4.29600  25.07000 1.000 23.74158 ? 23  LYS A N   1 
ATOM   180  C  CA  . LYS A 1 31  ? -6.92000  -4.68700  25.58100 1.000 27.86894 ? 23  LYS A CA  1 
ATOM   181  C  C   . LYS A 1 31  ? -7.11700  -6.19800  25.57700 1.000 29.13451 ? 23  LYS A C   1 
ATOM   182  O  O   . LYS A 1 31  ? -7.85700  -6.72400  26.41500 1.000 25.90002 ? 23  LYS A O   1 
ATOM   183  C  CB  . LYS A 1 31  ? -8.02800  -4.01900  24.76900 1.000 30.19245 ? 23  LYS A CB  1 
ATOM   184  C  CG  . LYS A 1 31  ? -8.28400  -2.56600  25.12500 1.000 35.92494 ? 23  LYS A CG  1 
ATOM   185  C  CD  . LYS A 1 31  ? -9.55900  -2.06700  24.45500 1.000 42.64637 ? 23  LYS A CD  1 
ATOM   186  C  CE  . LYS A 1 31  ? -9.44100  -0.60500  24.05100 1.000 41.44393 ? 23  LYS A CE  1 
ATOM   187  N  NZ  . LYS A 1 31  ? -9.18100  0.28800   25.21600 1.000 41.87853 ? 23  LYS A NZ  1 
ATOM   188  N  N   . GLU A 1 32  ? -6.48500  -6.90700  24.64300 1.000 27.20862 ? 24  GLU A N   1 
ATOM   189  C  CA  . GLU A 1 32  ? -6.57200  -8.35700  24.55700 1.000 25.82075 ? 24  GLU A CA  1 
ATOM   190  C  C   . GLU A 1 32  ? -5.20100  -8.96100  24.81600 1.000 27.13653 ? 24  GLU A C   1 
ATOM   191  O  O   . GLU A 1 32  ? -4.19700  -8.49200  24.27300 1.000 25.03976 ? 24  GLU A O   1 
ATOM   192  C  CB  . GLU A 1 32  ? -7.07800  -8.80700  23.18400 1.000 32.31707 ? 24  GLU A CB  1 
ATOM   193  C  CG  . GLU A 1 32  ? -8.36100  -8.13100  22.73500 1.000 35.94773 ? 24  GLU A CG  1 
ATOM   194  C  CD  . GLU A 1 32  ? -8.71700  -8.47300  21.30200 1.000 44.87449 ? 24  GLU A CD  1 
ATOM   195  O  OE1 . GLU A 1 32  ? -7.92500  -8.14400  20.39200 1.000 42.68407 ? 24  GLU A OE1 1 
ATOM   196  O  OE2 . GLU A 1 32  ? -9.78600  -9.08200  21.08900 1.000 47.49749 ? 24  GLU A OE2 1 
ATOM   197  N  N   . SER A 1 33  ? -5.16500  -10.01200 25.63900 1.000 28.41453 ? 25  SER A N   1 
ATOM   198  C  CA  . SER A 1 33  ? -3.89800  -10.65300 25.96900 1.000 27.28531 ? 25  SER A CA  1 
ATOM   199  C  C   . SER A 1 33  ? -3.23900  -11.29200 24.75300 1.000 29.89507 ? 25  SER A C   1 
ATOM   200  O  O   . SER A 1 33  ? -2.01700  -11.47700 24.75000 1.000 32.99698 ? 25  SER A O   1 
ATOM   201  C  CB  . SER A 1 33  ? -4.10700  -11.70300 27.06600 1.000 31.69590 ? 25  SER A CB  1 
ATOM   202  O  OG  . SER A 1 33  ? -4.34400  -12.99200 26.52500 1.000 26.87543 ? 25  SER A OG  1 
ATOM   203  N  N   . ASN A 1 34  ? -4.01200  -11.62800 23.72100 1.000 29.95222 ? 26  ASN A N   1 
ATOM   204  C  CA  . ASN A 1 34  ? -3.47500  -12.21200 22.50000 1.000 36.42949 ? 26  ASN A CA  1 
ATOM   205  C  C   . ASN A 1 34  ? -3.42800  -11.21200 21.34800 1.000 34.25774 ? 26  ASN A C   1 
ATOM   206  O  O   . ASN A 1 34  ? -3.33800  -11.61800 20.18400 1.000 37.43854 ? 26  ASN A O   1 
ATOM   207  C  CB  . ASN A 1 34  ? -4.29000  -13.44700 22.10200 1.000 33.03194 ? 26  ASN A CB  1 
ATOM   208  C  CG  . ASN A 1 34  ? -5.68200  -13.10000 21.59400 1.000 38.54482 ? 26  ASN A CG  1 
ATOM   209  O  OD1 . ASN A 1 34  ? -6.18000  -11.99100 21.79900 1.000 37.80758 ? 26  ASN A OD1 1 
ATOM   210  N  ND2 . ASN A 1 34  ? -6.32200  -14.06000 20.93000 1.000 40.40200 ? 26  ASN A ND2 1 
ATOM   211  N  N   . GLY A 1 35  ? -3.49200  -9.91800  21.64800 1.000 25.95211 ? 27  GLY A N   1 
ATOM   212  C  CA  . GLY A 1 35  ? -3.53100  -8.90400  20.62400 1.000 27.33045 ? 27  GLY A CA  1 
ATOM   213  C  C   . GLY A 1 35  ? -2.30700  -8.01100  20.62900 1.000 25.31437 ? 27  GLY A C   1 
ATOM   214  O  O   . GLY A 1 35  ? -1.40300  -8.14800  21.46000 1.000 20.19438 ? 27  GLY A O   1 
ATOM   215  N  N   . PRO A 1 36  ? -2.26600  -7.05700  19.70500 1.000 25.19873 ? 28  PRO A N   1 
ATOM   216  C  CA  . PRO A 1 36  ? -1.09900  -6.18100  19.61300 1.000 20.89273 ? 28  PRO A CA  1 
ATOM   217  C  C   . PRO A 1 36  ? -1.08400  -5.16200  20.74000 1.000 21.17239 ? 28  PRO A C   1 
ATOM   218  O  O   . PRO A 1 36  ? -2.10400  -4.85400  21.36200 1.000 18.81984 ? 28  PRO A O   1 
ATOM   219  C  CB  . PRO A 1 36  ? -1.26600  -5.50400  18.24800 1.000 22.49874 ? 28  PRO A CB  1 
ATOM   220  C  CG  . PRO A 1 36  ? -2.73800  -5.61800  17.92000 1.000 29.50862 ? 28  PRO A CG  1 
ATOM   221  C  CD  . PRO A 1 36  ? -3.39600  -6.55300  18.90800 1.000 26.26316 ? 28  PRO A CD  1 
ATOM   222  N  N   . VAL A 1 37  ? 0.11100   -4.65000  21.00600 1.000 18.72008 ? 29  VAL A N   1 
ATOM   223  C  CA  . VAL A 1 37  ? 0.32000   -3.59900  21.98900 1.000 16.79323 ? 29  VAL A CA  1 
ATOM   224  C  C   . VAL A 1 37  ? 0.44600   -2.28200  21.24000 1.000 18.22476 ? 29  VAL A C   1 
ATOM   225  O  O   . VAL A 1 37  ? 1.27700   -2.15100  20.33400 1.000 17.40778 ? 29  VAL A O   1 
ATOM   226  C  CB  . VAL A 1 37  ? 1.56800   -3.86900  22.84600 1.000 16.68453 ? 29  VAL A CB  1 
ATOM   227  C  CG1 . VAL A 1 37  ? 1.76900   -2.74600  23.86300 1.000 14.48678 ? 29  VAL A CG1 1 
ATOM   228  C  CG2 . VAL A 1 37  ? 1.46300   -5.22700  23.53700 1.000 14.76267 ? 29  VAL A CG2 1 
ATOM   229  N  N   . LYS A 1 38  ? -0.39300  -1.31600  21.59800 1.000 19.73421 ? 30  LYS A N   1 
ATOM   230  C  CA  . LYS A 1 38  ? -0.24200  0.04400   21.10100 1.000 17.90467 ? 30  LYS A CA  1 
ATOM   231  C  C   . LYS A 1 38  ? 0.76300   0.78300   21.97600 1.000 19.23362 ? 30  LYS A C   1 
ATOM   232  O  O   . LYS A 1 38  ? 0.66700   0.75100   23.20700 1.000 18.82506 ? 30  LYS A O   1 
ATOM   233  C  CB  . LYS A 1 38  ? -1.58500  0.78300   21.09700 1.000 20.25863 ? 30  LYS A CB  1 
ATOM   234  C  CG  . LYS A 1 38  ? -2.80500  -0.01900  20.61300 1.000 29.75468 ? 30  LYS A CG  1 
ATOM   235  C  CD  . LYS A 1 38  ? -3.46100  -0.80500  21.75700 1.000 35.74912 ? 30  LYS A CD  1 
ATOM   236  C  CE  . LYS A 1 38  ? -4.83900  -1.36100  21.39700 1.000 39.73041 ? 30  LYS A CE  1 
ATOM   237  N  NZ  . LYS A 1 38  ? -5.40200  -2.21800  22.49500 1.000 33.70318 ? 30  LYS A NZ  1 
ATOM   238  N  N   . VAL A 1 39  ? 1.73600   1.43200   21.34300 1.000 17.85336 ? 31  VAL A N   1 
ATOM   239  C  CA  . VAL A 1 39  ? 2.76700   2.20200   22.03100 1.000 15.76272 ? 31  VAL A CA  1 
ATOM   240  C  C   . VAL A 1 39  ? 2.68700   3.63700   21.52900 1.000 15.05136 ? 31  VAL A C   1 
ATOM   241  O  O   . VAL A 1 39  ? 2.85400   3.88600   20.32800 1.000 21.31079 ? 31  VAL A O   1 
ATOM   242  C  CB  . VAL A 1 39  ? 4.17000   1.62200   21.79200 1.000 14.65787 ? 31  VAL A CB  1 
ATOM   243  C  CG1 . VAL A 1 39  ? 5.18000   2.30900   22.68900 1.000 15.42972 ? 31  VAL A CG1 1 
ATOM   244  C  CG2 . VAL A 1 39  ? 4.18300   0.11800   22.01500 1.000 16.30084 ? 31  VAL A CG2 1 
ATOM   245  N  N   . TRP A 1 40  ? 2.44500   4.58000   22.43900 1.000 13.86674 ? 32  TRP A N   1 
ATOM   246  C  CA  . TRP A 1 40  ? 2.24300   5.96600   22.03300 1.000 17.11609 ? 32  TRP A CA  1 
ATOM   247  C  C   . TRP A 1 40  ? 2.76800   6.91300   23.10300 1.000 13.75458 ? 32  TRP A C   1 
ATOM   248  O  O   . TRP A 1 40  ? 2.77100   6.59500   24.29500 1.000 18.37155 ? 32  TRP A O   1 
ATOM   249  C  CB  . TRP A 1 40  ? 0.76400   6.26500   21.74800 1.000 16.38155 ? 32  TRP A CB  1 
ATOM   250  C  CG  . TRP A 1 40  ? -0.15100  6.16600   22.93700 1.000 19.00823 ? 32  TRP A CG  1 
ATOM   251  C  CD1 . TRP A 1 40  ? -0.72800  5.03100   23.43300 1.000 21.30686 ? 32  TRP A CD1 1 
ATOM   252  C  CD2 . TRP A 1 40  ? -0.62100  7.24400   23.76000 1.000 22.90289 ? 32  TRP A CD2 1 
ATOM   253  N  NE1 . TRP A 1 40  ? -1.51500  5.33500   24.51800 1.000 20.77494 ? 32  TRP A NE1 1 
ATOM   254  C  CE2 . TRP A 1 40  ? -1.46700  6.68500   24.73900 1.000 21.37160 ? 32  TRP A CE2 1 
ATOM   255  C  CE3 . TRP A 1 40  ? -0.40300  8.62500   23.76800 1.000 25.17188 ? 32  TRP A CE3 1 
ATOM   256  C  CZ2 . TRP A 1 40  ? -2.09500  7.45800   25.71800 1.000 33.05621 ? 32  TRP A CZ2 1 
ATOM   257  C  CZ3 . TRP A 1 40  ? -1.03200  9.39200   24.74100 1.000 33.35686 ? 32  TRP A CZ3 1 
ATOM   258  C  CH2 . TRP A 1 40  ? -1.86600  8.80600   25.70100 1.000 27.56490 ? 32  TRP A CH2 1 
ATOM   259  N  N   . GLY A 1 41  ? 3.19800   8.08500   22.66200 1.000 12.81643 ? 33  GLY A N   1 
ATOM   260  C  CA  . GLY A 1 41  ? 3.76300   9.06500   23.56800 1.000 18.27848 ? 33  GLY A CA  1 
ATOM   261  C  C   . GLY A 1 41  ? 4.64500   10.03100  22.79900 1.000 14.82915 ? 33  GLY A C   1 
ATOM   262  O  O   . GLY A 1 41  ? 4.54400   10.14400  21.58000 1.000 18.23724 ? 33  GLY A O   1 
ATOM   263  N  N   . SER A 1 42  ? 5.50600   10.72200  23.54300 1.000 15.23161 ? 34  SER A N   1 
ATOM   264  C  CA  . SER A 1 42  ? 6.42700   11.66600  22.92700 1.000 19.49936 ? 34  SER A CA  1 
ATOM   265  C  C   . SER A 1 42  ? 7.72300   11.69400  23.72100 1.000 16.53823 ? 34  SER A C   1 
ATOM   266  O  O   . SER A 1 42  ? 7.73300   11.46800  24.93400 1.000 21.55369 ? 34  SER A O   1 
ATOM   267  C  CB  . SER A 1 42  ? 5.83000   13.07800  22.83900 1.000 22.89288 ? 34  SER A CB  1 
ATOM   268  O  OG  . SER A 1 42  ? 6.17600   13.85200  23.97100 1.000 31.34929 ? 34  SER A OG  1 
ATOM   269  N  N   . ILE A 1 43  ? 8.81800   11.96200  23.01600 1.000 16.70968 ? 35  ILE A N   1 
ATOM   270  C  CA  . ILE A 1 43  ? 10.13900  12.10900  23.61500 1.000 16.28926 ? 35  ILE A CA  1 
ATOM   271  C  C   . ILE A 1 43  ? 10.71800  13.43300  23.13900 1.000 18.11770 ? 35  ILE A C   1 
ATOM   272  O  O   . ILE A 1 43  ? 10.69400  13.72800  21.93800 1.000 20.20120 ? 35  ILE A O   1 
ATOM   273  C  CB  . ILE A 1 43  ? 11.08200  10.94900  23.24100 1.000 16.89825 ? 35  ILE A CB  1 
ATOM   274  C  CG1 . ILE A 1 43  ? 10.45500  9.59500   23.57200 1.000 14.26755 ? 35  ILE A CG1 1 
ATOM   275  C  CG2 . ILE A 1 43  ? 12.42100  11.08800  23.96800 1.000 14.96442 ? 35  ILE A CG2 1 
ATOM   276  C  CD1 . ILE A 1 43  ? 11.27100  8.43300   23.02900 1.000 16.74223 ? 35  ILE A CD1 1 
ATOM   277  N  N   . LYS A 1 44  ? 11.23400  14.22500  24.07200 1.000 16.26428 ? 36  LYS A N   1 
ATOM   278  C  CA  . LYS A 1 44  ? 11.73900  15.55400  23.77200 1.000 18.19073 ? 36  LYS A CA  1 
ATOM   279  C  C   . LYS A 1 44  ? 13.25400  15.59700  23.91500 1.000 17.29326 ? 36  LYS A C   1 
ATOM   280  O  O   . LYS A 1 44  ? 13.86800  14.73700  24.55100 1.000 16.39913 ? 36  LYS A O   1 
ATOM   281  C  CB  . LYS A 1 44  ? 11.10200  16.59500  24.69800 1.000 20.16126 ? 36  LYS A CB  1 
ATOM   282  C  CG  . LYS A 1 44  ? 9.61300   16.39800  24.91000 1.000 30.12495 ? 36  LYS A CG  1 
ATOM   283  C  CD  . LYS A 1 44  ? 9.09200   17.34900  25.97100 1.000 35.08354 ? 36  LYS A CD  1 
ATOM   284  C  CE  . LYS A 1 44  ? 7.75100   16.89000  26.51800 1.000 39.75143 ? 36  LYS A CE  1 
ATOM   285  N  NZ  . LYS A 1 44  ? 7.66900   17.15100  27.98200 1.000 38.06461 ? 36  LYS A NZ  1 
ATOM   286  N  N   . GLY A 1 45  ? 13.85300  16.62500  23.31500 1.000 16.29833 ? 37  GLY A N   1 
ATOM   287  C  CA  . GLY A 1 45  ? 15.26500  16.89000  23.50400 1.000 17.17525 ? 37  GLY A CA  1 
ATOM   288  C  C   . GLY A 1 45  ? 16.19700  16.09100  22.63000 1.000 18.03279 ? 37  GLY A C   1 
ATOM   289  O  O   . GLY A 1 45  ? 17.39900  16.04500  22.90700 1.000 17.93401 ? 37  GLY A O   1 
ATOM   290  N  N   . LEU A 1 46  ? 15.68400  15.46900  21.57500 1.000 17.76548 ? 38  LEU A N   1 
ATOM   291  C  CA  . LEU A 1 46  ? 16.47700  14.62500  20.69600 1.000 19.94835 ? 38  LEU A CA  1 
ATOM   292  C  C   . LEU A 1 46  ? 17.02100  15.42400  19.52100 1.000 20.92063 ? 38  LEU A C   1 
ATOM   293  O  O   . LEU A 1 46  ? 16.45100  16.43900  19.11900 1.000 17.77146 ? 38  LEU A O   1 
ATOM   294  C  CB  . LEU A 1 46  ? 15.63000  13.46700  20.16800 1.000 15.50149 ? 38  LEU A CB  1 
ATOM   295  C  CG  . LEU A 1 46  ? 15.15800  12.44200  21.19300 1.000 18.34782 ? 38  LEU A CG  1 
ATOM   296  C  CD1 . LEU A 1 46  ? 14.01600  11.62600  20.61300 1.000 16.48863 ? 38  LEU A CD1 1 
ATOM   297  C  CD2 . LEU A 1 46  ? 16.31400  11.54700  21.59400 1.000 14.54016 ? 38  LEU A CD2 1 
ATOM   298  N  N   . THR A 1 47  ? 18.13500  14.95100  18.96700 1.000 19.77302 ? 39  THR A N   1 
ATOM   299  C  CA  . THR A 1 47  ? 18.57900  15.46400  17.68100 1.000 15.10698 ? 39  THR A CA  1 
ATOM   300  C  C   . THR A 1 47  ? 17.62000  14.99800  16.59700 1.000 17.84895 ? 39  THR A C   1 
ATOM   301  O  O   . THR A 1 47  ? 17.08200  13.88600  16.65800 1.000 19.04977 ? 39  THR A O   1 
ATOM   302  C  CB  . THR A 1 47  ? 19.99600  14.99300  17.35500 1.000 15.14837 ? 39  THR A CB  1 
ATOM   303  O  OG1 . THR A 1 47  ? 20.01200  13.56500  17.22300 1.000 16.85164 ? 39  THR A OG1 1 
ATOM   304  C  CG2 . THR A 1 47  ? 20.95600  15.41000  18.45000 1.000 20.30040 ? 39  THR A CG2 1 
ATOM   305  N  N   . GLU A 1 48  ? 17.39900  15.86100  15.61000 1.000 16.03793 ? 40  GLU A N   1 
ATOM   306  C  CA  . GLU A 1 48  ? 16.50800  15.52800  14.50800 1.000 20.93890 ? 40  GLU A CA  1 
ATOM   307  C  C   . GLU A 1 48  ? 16.97300  14.24500  13.83000 1.000 16.32628 ? 40  GLU A C   1 
ATOM   308  O  O   . GLU A 1 48  ? 18.16600  14.06600  13.56900 1.000 16.91076 ? 40  GLU A O   1 
ATOM   309  C  CB  . GLU A 1 48  ? 16.46900  16.68800  13.51100 1.000 17.97572 ? 40  GLU A CB  1 
ATOM   310  C  CG  . GLU A 1 48  ? 15.60000  16.43900  12.29700 1.000 18.70616 ? 40  GLU A CG  1 
ATOM   311  C  CD  . GLU A 1 48  ? 15.55400  17.62900  11.36200 1.000 28.97373 ? 40  GLU A CD  1 
ATOM   312  O  OE1 . GLU A 1 48  ? 16.08900  18.69900  11.72700 1.000 26.61216 ? 40  GLU A OE1 1 
ATOM   313  O  OE2 . GLU A 1 48  ? 14.98400  17.49100  10.26000 1.000 25.35569 ? 40  GLU A OE2 1 
ATOM   314  N  N   . GLY A 1 49  ? 16.03500  13.32300  13.58900 1.000 18.49503 ? 41  GLY A N   1 
ATOM   315  C  CA  . GLY A 1 49  ? 16.35600  12.09900  12.88900 1.000 15.76436 ? 41  GLY A CA  1 
ATOM   316  C  C   . GLY A 1 49  ? 15.94300  10.86900  13.67900 1.000 17.01996 ? 41  GLY A C   1 
ATOM   317  O  O   . GLY A 1 49  ? 15.14000  10.94700  14.61500 1.000 15.09069 ? 41  GLY A O   1 
ATOM   318  N  N   . LEU A 1 50  ? 16.52300  9.73000   13.29100 1.000 15.95018 ? 42  LEU A N   1 
ATOM   319  C  CA  . LEU A 1 50  ? 16.14900  8.41600   13.80300 1.000 13.81328 ? 42  LEU A CA  1 
ATOM   320  C  C   . LEU A 1 50  ? 16.91900  8.06800   15.06900 1.000 14.86634 ? 42  LEU A C   1 
ATOM   321  O  O   . LEU A 1 50  ? 18.11000  8.37300   15.18800 1.000 13.93245 ? 42  LEU A O   1 
ATOM   322  C  CB  . LEU A 1 50  ? 16.40800  7.34300   12.74200 1.000 12.16097 ? 42  LEU A CB  1 
ATOM   323  C  CG  . LEU A 1 50  ? 15.61800  7.50000   11.44800 1.000 17.68218 ? 42  LEU A CG  1 
ATOM   324  C  CD1 . LEU A 1 50  ? 16.19400  6.60900   10.36000 1.000 21.72223 ? 42  LEU A CD1 1 
ATOM   325  C  CD2 . LEU A 1 50  ? 14.16400  7.16700   11.70600 1.000 14.79428 ? 42  LEU A CD2 1 
ATOM   326  N  N   . HIS A 1 51  ? 16.23900  7.39600   16.00000 1.000 9.98977  ? 43  HIS A N   1 
ATOM   327  C  CA  . HIS A 1 51  ? 16.83800  6.98600   17.26700 1.000 10.14438 ? 43  HIS A CA  1 
ATOM   328  C  C   . HIS A 1 51  ? 16.38100  5.58300   17.63700 1.000 10.81312 ? 43  HIS A C   1 
ATOM   329  O  O   . HIS A 1 51  ? 15.17600  5.30700   17.65700 1.000 11.48184 ? 43  HIS A O   1 
ATOM   330  C  CB  . HIS A 1 51  ? 16.47500  7.96500   18.39000 1.000 11.06301 ? 43  HIS A CB  1 
ATOM   331  C  CG  . HIS A 1 51  ? 17.01400  9.34600   18.18200 1.000 13.51789 ? 43  HIS A CG  1 
ATOM   332  N  ND1 . HIS A 1 51  ? 18.26100  9.73400   18.62400 1.000 15.35776 ? 43  HIS A ND1 1 
ATOM   333  C  CD2 . HIS A 1 51  ? 16.47900  10.42900  17.56800 1.000 16.20259 ? 43  HIS A CD2 1 
ATOM   334  C  CE1 . HIS A 1 51  ? 18.46900  10.99700  18.29600 1.000 13.49400 ? 43  HIS A CE1 1 
ATOM   335  N  NE2 . HIS A 1 51  ? 17.40400  11.44200  17.65400 1.000 16.07321 ? 43  HIS A NE2 1 
ATOM   336  N  N   . GLY A 1 52  ? 17.33900  4.71300   17.95000 1.000 11.61234 ? 44  GLY A N   1 
ATOM   337  C  CA  . GLY A 1 52  ? 16.99500  3.35500   18.34700 1.000 10.21748 ? 44  GLY A CA  1 
ATOM   338  C  C   . GLY A 1 52  ? 16.10300  3.33600   19.57800 1.000 11.19264 ? 44  GLY A C   1 
ATOM   339  O  O   . GLY A 1 52  ? 16.24700  4.15300   20.49000 1.000 11.89228 ? 44  GLY A O   1 
ATOM   340  N  N   . PHE A 1 53  ? 15.18600  2.37100   19.60800 1.000 10.56409 ? 45  PHE A N   1 
ATOM   341  C  CA  . PHE A 1 53  ? 14.09600  2.31900   20.58300 1.000 12.52449 ? 45  PHE A CA  1 
ATOM   342  C  C   . PHE A 1 53  ? 13.89800  0.86200   20.97600 1.000 11.13078 ? 45  PHE A C   1 
ATOM   343  O  O   . PHE A 1 53  ? 13.36700  0.08200   20.18000 1.000 13.38128 ? 45  PHE A O   1 
ATOM   344  C  CB  . PHE A 1 53  ? 12.82400  2.90100   19.96700 1.000 12.27776 ? 45  PHE A CB  1 
ATOM   345  C  CG  . PHE A 1 53  ? 11.73300  3.19400   20.95000 1.000 10.98551 ? 45  PHE A CG  1 
ATOM   346  C  CD1 . PHE A 1 53  ? 11.97400  3.98200   22.06000 1.000 12.09226 ? 45  PHE A CD1 1 
ATOM   347  C  CD2 . PHE A 1 53  ? 10.44900  2.72400   20.73200 1.000 13.88795 ? 45  PHE A CD2 1 
ATOM   348  C  CE1 . PHE A 1 53  ? 10.95600  4.27800   22.95500 1.000 14.59774 ? 45  PHE A CE1 1 
ATOM   349  C  CE2 . PHE A 1 53  ? 9.43100   3.01300   21.62100 1.000 16.76705 ? 45  PHE A CE2 1 
ATOM   350  C  CZ  . PHE A 1 53  ? 9.68700   3.79000   22.73600 1.000 12.62262 ? 45  PHE A CZ  1 
ATOM   351  N  N   . HIS A 1 54  ? 14.32100  0.48200   22.18700 1.000 9.86548  ? 46  HIS A N   1 
ATOM   352  C  CA  . HIS A 1 54  ? 14.41800  -0.93100  22.53600 1.000 12.21526 ? 46  HIS A CA  1 
ATOM   353  C  C   . HIS A 1 54  ? 13.94900  -1.18800  23.95900 1.000 10.02760 ? 46  HIS A C   1 
ATOM   354  O  O   . HIS A 1 54  ? 14.09600  -0.34600  24.84700 1.000 9.83070  ? 46  HIS A O   1 
ATOM   355  C  CB  . HIS A 1 54  ? 15.86000  -1.46000  22.43100 1.000 14.41789 ? 46  HIS A CB  1 
ATOM   356  C  CG  . HIS A 1 54  ? 16.53800  -1.13900  21.13800 1.000 17.35140 ? 46  HIS A CG  1 
ATOM   357  N  ND1 . HIS A 1 54  ? 17.83900  -0.68900  21.07800 1.000 16.60335 ? 46  HIS A ND1 1 
ATOM   358  C  CD2 . HIS A 1 54  ? 16.10900  -1.22200  19.85700 1.000 13.84364 ? 46  HIS A CD2 1 
ATOM   359  C  CE1 . HIS A 1 54  ? 18.18000  -0.50100  19.81600 1.000 14.41589 ? 46  HIS A CE1 1 
ATOM   360  N  NE2 . HIS A 1 54  ? 17.14600  -0.81200  19.05600 1.000 14.91205 ? 46  HIS A NE2 1 
ATOM   361  N  N   . VAL A 1 55  ? 13.42200  -2.38700  24.17400 1.000 10.67001 ? 47  VAL A N   1 
ATOM   362  C  CA  . VAL A 1 55  ? 13.18300  -2.91100  25.51300 1.000 12.23007 ? 47  VAL A CA  1 
ATOM   363  C  C   . VAL A 1 55  ? 14.36400  -3.80600  25.86900 1.000 12.81390 ? 47  VAL A C   1 
ATOM   364  O  O   . VAL A 1 55  ? 14.64100  -4.79100  25.17200 1.000 10.54120 ? 47  VAL A O   1 
ATOM   365  C  CB  . VAL A 1 55  ? 11.85600  -3.68300  25.59700 1.000 13.71321 ? 47  VAL A CB  1 
ATOM   366  C  CG1 . VAL A 1 55  ? 11.69800  -4.32400  26.98100 1.000 11.64137 ? 47  VAL A CG1 1 
ATOM   367  C  CG2 . VAL A 1 55  ? 10.67700  -2.76100  25.30300 1.000 11.70076 ? 47  VAL A CG2 1 
ATOM   368  N  N   . HIS A 1 56  ? 15.07700  -3.44800  26.93000 1.000 13.46243 ? 48  HIS A N   1 
ATOM   369  C  CA  . HIS A 1 56  ? 16.17100  -4.26200  27.43300 1.000 18.76227 ? 48  HIS A CA  1 
ATOM   370  C  C   . HIS A 1 56  ? 15.65800  -5.22000  28.50400 1.000 15.54791 ? 48  HIS A C   1 
ATOM   371  O  O   . HIS A 1 56  ? 14.56500  -5.05100  29.04900 1.000 15.75947 ? 48  HIS A O   1 
ATOM   372  C  CB  . HIS A 1 56  ? 17.29400  -3.38300  27.98600 1.000 15.14091 ? 48  HIS A CB  1 
ATOM   373  C  CG  . HIS A 1 56  ? 18.04700  -2.63500  26.93100 1.000 19.02287 ? 48  HIS A CG  1 
ATOM   374  N  ND1 . HIS A 1 56  ? 19.40800  -2.76800  26.75000 1.000 22.60570 ? 48  HIS A ND1 1 
ATOM   375  C  CD2 . HIS A 1 56  ? 17.62700  -1.75300  25.99300 1.000 16.94005 ? 48  HIS A CD2 1 
ATOM   376  C  CE1 . HIS A 1 56  ? 19.79400  -1.99400  25.75200 1.000 29.02517 ? 48  HIS A CE1 1 
ATOM   377  N  NE2 . HIS A 1 56  ? 18.73400  -1.36500  25.27700 1.000 18.32339 ? 48  HIS A NE2 1 
ATOM   378  N  N   . GLU A 1 57  ? 16.47200  -6.23300  28.80700 1.000 14.96620 ? 49  GLU A N   1 
ATOM   379  C  CA  . GLU A 1 57  ? 15.96600  -7.39000  29.54000 1.000 17.15124 ? 49  GLU A CA  1 
ATOM   380  C  C   . GLU A 1 57  ? 15.58300  -7.04800  30.97900 1.000 16.47765 ? 49  GLU A C   1 
ATOM   381  O  O   . GLU A 1 57  ? 14.56500  -7.53800  31.48000 1.000 21.65371 ? 49  GLU A O   1 
ATOM   382  C  CB  . GLU A 1 57  ? 16.99500  -8.52400  29.52100 1.000 19.15697 ? 49  GLU A CB  1 
ATOM   383  C  CG  . GLU A 1 57  ? 16.48300  -9.79400  30.19600 1.000 21.23303 ? 49  GLU A CG  1 
ATOM   384  C  CD  . GLU A 1 57  ? 17.46600  -10.94800 30.14600 1.000 31.48293 ? 49  GLU A CD  1 
ATOM   385  O  OE1 . GLU A 1 57  ? 18.55200  -10.78600 29.54900 1.000 29.09653 ? 49  GLU A OE1 1 
ATOM   386  O  OE2 . GLU A 1 57  ? 17.14800  -12.02000 30.71200 1.000 30.28708 ? 49  GLU A OE2 1 
ATOM   387  N  N   . PHE A 1 58  ? 16.37300  -6.21900  31.63600 1.000 20.03741 ? 50  PHE A N   1 
ATOM   388  C  CA  . PHE A 1 58  ? 16.15300  -5.99100  33.09100 1.000 22.94747 ? 50  PHE A CA  1 
ATOM   389  C  C   . PHE A 1 58  ? 15.77400  -4.55200  33.45700 1.000 21.60231 ? 50  PHE A C   1 
ATOM   390  O  O   . PHE A 1 58  ? 16.34600  -3.64800  32.87600 1.000 22.53561 ? 50  PHE A O   1 
ATOM   391  C  CB  . PHE A 1 58  ? 17.41600  -6.34800  33.87500 1.000 23.13700 ? 50  PHE A CB  1 
ATOM   392  C  CG  . PHE A 1 58  ? 17.91100  -7.75300  33.65100 1.000 23.27286 ? 50  PHE A CG  1 
ATOM   393  C  CD1 . PHE A 1 58  ? 17.24400  -8.83500  34.19700 1.000 22.55631 ? 50  PHE A CD1 1 
ATOM   394  C  CD2 . PHE A 1 58  ? 19.03900  -7.99400  32.88600 1.000 28.65726 ? 50  PHE A CD2 1 
ATOM   395  C  CE1 . PHE A 1 58  ? 17.69500  -10.12800 33.98700 1.000 30.31270 ? 50  PHE A CE1 1 
ATOM   396  C  CE2 . PHE A 1 58  ? 19.48600  -9.28700  32.67400 1.000 25.73600 ? 50  PHE A CE2 1 
ATOM   397  C  CZ  . PHE A 1 58  ? 18.82100  -10.35000 33.23200 1.000 26.79586 ? 50  PHE A CZ  1 
ATOM   398  N  N   . GLY A 1 59  ? 14.87100  -4.39500  34.43100 1.000 18.47922 ? 51  GLY A N   1 
ATOM   399  C  CA  . GLY A 1 59  ? 14.49100  -3.06000  34.93200 1.000 19.71155 ? 51  GLY A CA  1 
ATOM   400  C  C   . GLY A 1 59  ? 15.46000  -2.63600  36.00800 1.000 22.05027 ? 51  GLY A C   1 
ATOM   401  O  O   . GLY A 1 59  ? 15.03000  -2.40600  37.12300 1.000 21.73112 ? 51  GLY A O   1 
ATOM   402  N  N   . ASP A 1 60  ? 16.73200  -2.55300  35.63000 1.000 28.88291 ? 52  ASP A N   1 
ATOM   403  C  CA  . ASP A 1 60  ? 17.80800  -2.28600  36.59700 1.000 26.38518 ? 52  ASP A CA  1 
ATOM   404  C  C   . ASP A 1 60  ? 18.90900  -1.41600  35.98300 1.000 33.97509 ? 52  ASP A C   1 
ATOM   405  O  O   . ASP A 1 60  ? 19.30000  -1.69200  34.85600 1.000 35.58619 ? 52  ASP A O   1 
ATOM   406  C  CB  . ASP A 1 60  ? 18.44000  -3.62200  36.94700 1.000 29.52501 ? 52  ASP A CB  1 
ATOM   407  C  CG  . ASP A 1 60  ? 19.42600  -3.59300  38.09800 1.000 30.24826 ? 52  ASP A CG  1 
ATOM   408  O  OD1 . ASP A 1 60  ? 19.73100  -2.50200  38.56700 1.000 31.31513 ? 52  ASP A OD1 1 
ATOM   409  O  OD2 . ASP A 1 60  ? 19.85300  -4.67500  38.52100 1.000 26.88082 ? 52  ASP A OD2 1 
ATOM   410  N  N   . ASN A 1 61  ? 19.41400  -0.44100  36.72900 1.000 39.50062 ? 53  ASN A N   1 
ATOM   411  C  CA  . ASN A 1 61  ? 20.60300  0.35700   36.31400 1.000 44.84997 ? 53  ASN A CA  1 
ATOM   412  C  C   . ASN A 1 61  ? 21.57900  0.38000   37.50500 1.000 48.96458 ? 53  ASN A C   1 
ATOM   413  O  O   . ASN A 1 61  ? 22.27600  1.39100   37.67900 1.000 46.44298 ? 53  ASN A O   1 
ATOM   414  C  CB  . ASN A 1 61  ? 20.21300  1.75100   35.83100 1.000 46.76616 ? 53  ASN A CB  1 
ATOM   415  C  CG  . ASN A 1 61  ? 19.12400  2.37500   36.67800 1.000 45.68461 ? 53  ASN A CG  1 
ATOM   416  O  OD1 . ASN A 1 61  ? 17.96100  1.98800   36.58400 1.000 48.46734 ? 53  ASN A OD1 1 
ATOM   417  N  ND2 . ASN A 1 61  ? 19.48700  3.35000   37.49400 1.000 34.75505 ? 53  ASN A ND2 1 
ATOM   418  N  N   . THR A 1 62  ? 21.63100  -0.70900  38.27800 1.000 46.63717 ? 54  THR A N   1 
ATOM   419  C  CA  . THR A 1 62  ? 22.50500  -0.80600  39.47800 1.000 47.38891 ? 54  THR A CA  1 
ATOM   420  C  C   . THR A 1 62  ? 23.91100  -0.32200  39.12500 1.000 51.27067 ? 54  THR A C   1 
ATOM   421  O  O   . THR A 1 62  ? 24.41200  0.58700   39.78400 1.000 51.00782 ? 54  THR A O   1 
ATOM   422  C  CB  . THR A 1 62  ? 22.53700  -2.24200  40.02600 1.000 48.95392 ? 54  THR A CB  1 
ATOM   423  O  OG1 . THR A 1 62  ? 23.59600  -2.32500  40.98000 1.000 58.44613 ? 54  THR A OG1 1 
ATOM   424  C  CG2 . THR A 1 62  ? 22.77000  -3.31400  38.98700 1.000 46.48203 ? 54  THR A CG2 1 
ATOM   425  N  N   . ALA A 1 63  ? 24.49100  -0.91600  38.09800 1.000 51.69723 ? 55  ALA A N   1 
ATOM   426  C  CA  . ALA A 1 63  ? 25.83300  -0.51800  37.65400 1.000 54.36317 ? 55  ALA A CA  1 
ATOM   427  C  C   . ALA A 1 63  ? 25.65400  0.53200   36.55800 1.000 58.49204 ? 55  ALA A C   1 
ATOM   428  O  O   . ALA A 1 63  ? 26.37100  1.54400   36.58800 1.000 61.45518 ? 55  ALA A O   1 
ATOM   429  C  CB  . ALA A 1 63  ? 26.57600  -1.74200  37.18100 1.000 46.96946 ? 55  ALA A CB  1 
ATOM   430  N  N   . GLY A 1 64  ? 24.72700  0.29500   35.62900 1.000 57.09444 ? 56  GLY A N   1 
ATOM   431  C  CA  . GLY A 1 64  ? 24.56400  1.22800   34.50200 1.000 53.30535 ? 56  GLY A CA  1 
ATOM   432  C  C   . GLY A 1 64  ? 23.89100  0.59300   33.30400 1.000 51.80618 ? 56  GLY A C   1 
ATOM   433  O  O   . GLY A 1 64  ? 22.78400  0.08600   33.44200 1.000 51.66379 ? 56  GLY A O   1 
ATOM   434  N  N   . ASP A 1 65  ? 24.53600  0.67600   32.14500 1.000 56.99530 ? 57  ASP A N   1 
ATOM   435  C  CA  . ASP A 1 65  ? 23.91600  0.16400   30.90000 1.000 55.20056 ? 57  ASP A CA  1 
ATOM   436  C  C   . ASP A 1 65  ? 23.87700  -1.35500  30.95800 1.000 49.08656 ? 57  ASP A C   1 
ATOM   437  O  O   . ASP A 1 65  ? 22.84900  -1.91800  30.56400 1.000 51.59869 ? 57  ASP A O   1 
ATOM   438  C  CB  . ASP A 1 65  ? 24.61200  0.73000   29.66000 1.000 50.26481 ? 57  ASP A CB  1 
ATOM   439  C  CG  . ASP A 1 65  ? 24.48800  2.24400   29.55700 1.000 50.12431 ? 57  ASP A CG  1 
ATOM   440  O  OD1 . ASP A 1 65  ? 23.96300  2.85600   30.50400 1.000 50.38573 ? 57  ASP A OD1 1 
ATOM   441  O  OD2 . ASP A 1 65  ? 24.90400  2.79900   28.52600 1.000 52.19142 ? 57  ASP A OD2 1 
ATOM   442  N  N   . THR A 1 66  ? 24.94300  -1.96500  31.46400 1.000 49.97719 ? 58  THR A N   1 
ATOM   443  C  CA  . THR A 1 66  ? 25.02200  -3.44900  31.53200 1.000 49.24896 ? 58  THR A CA  1 
ATOM   444  C  C   . THR A 1 66  ? 23.89500  -4.00100  32.39700 1.000 46.66129 ? 58  THR A C   1 
ATOM   445  O  O   . THR A 1 66  ? 23.38000  -5.05300  32.05400 1.000 48.20496 ? 58  THR A O   1 
ATOM   446  C  CB  . THR A 1 66  ? 26.35800  -3.91800  32.10200 1.000 47.51253 ? 58  THR A CB  1 
ATOM   447  O  OG1 . THR A 1 66  ? 26.21900  -5.28500  32.48900 1.000 51.61230 ? 58  THR A OG1 1 
ATOM   448  C  CG2 . THR A 1 66  ? 26.81300  -3.10500  33.29600 1.000 47.92123 ? 58  THR A CG2 1 
ATOM   449  N  N   . SER A 1 67  ? 23.56900  -3.32400  33.49400 1.000 48.07270 ? 59  SER A N   1 
ATOM   450  C  CA  . SER A 1 67  ? 22.53500  -3.82900  34.43800 1.000 42.46382 ? 59  SER A CA  1 
ATOM   451  C  C   . SER A 1 67  ? 21.16500  -3.94100  33.76100 1.000 37.19146 ? 59  SER A C   1 
ATOM   452  O  O   . SER A 1 67  ? 20.35900  -4.74500  34.25200 1.000 34.01555 ? 59  SER A O   1 
ATOM   453  C  CB  . SER A 1 67  ? 22.47900  -2.95900  35.65100 1.000 40.35764 ? 59  SER A CB  1 
ATOM   454  O  OG  . SER A 1 67  ? 22.69600  -1.60900  35.31400 1.000 46.08947 ? 59  SER A OG  1 
ATOM   455  N  N   . ALA A 1 68  ? 20.90000  -3.13900  32.72100 1.000 36.95987 ? 60  ALA A N   1 
ATOM   456  C  CA  . ALA A 1 68  ? 19.64900  -3.24500  31.93400 1.000 31.66000 ? 60  ALA A CA  1 
ATOM   457  C  C   . ALA A 1 68  ? 19.74600  -4.48700  31.04200 1.000 35.16872 ? 60  ALA A C   1 
ATOM   458  O  O   . ALA A 1 68  ? 18.72700  -4.94800  30.52200 1.000 28.87509 ? 60  ALA A O   1 
ATOM   459  C  CB  . ALA A 1 68  ? 19.44900  -2.00200  31.13500 1.000 29.76238 ? 60  ALA A CB  1 
ATOM   460  N  N   . GLY A 1 69  ? 20.96100  -4.99600  30.88300 1.000 34.17196 ? 61  GLY A N   1 
ATOM   461  C  CA  . GLY A 1 69  ? 21.15600  -6.22300  30.10700 1.000 30.41011 ? 61  GLY A CA  1 
ATOM   462  C  C   . GLY A 1 69  ? 21.05700  -5.96700  28.61800 1.000 28.21708 ? 61  GLY A C   1 
ATOM   463  O  O   . GLY A 1 69  ? 20.91600  -4.81400  28.20400 1.000 28.43767 ? 61  GLY A O   1 
ATOM   464  N  N   . PRO A 1 70  ? 21.11500  -7.02700  27.80600 1.000 25.10430 ? 62  PRO A N   1 
ATOM   465  C  CA  . PRO A 1 70  ? 20.93100  -6.84800  26.39200 1.000 20.89377 ? 62  PRO A CA  1 
ATOM   466  C  C   . PRO A 1 70  ? 19.45500  -6.59600  26.03500 1.000 25.95149 ? 62  PRO A C   1 
ATOM   467  O  O   . PRO A 1 70  ? 18.65100  -6.50600  26.92300 1.000 22.73910 ? 62  PRO A O   1 
ATOM   468  C  CB  . PRO A 1 70  ? 21.32600  -8.22500  25.86500 1.000 20.06001 ? 62  PRO A CB  1 
ATOM   469  C  CG  . PRO A 1 70  ? 21.03800  -9.19000  26.98100 1.000 24.17756 ? 62  PRO A CG  1 
ATOM   470  C  CD  . PRO A 1 70  ? 21.31200  -8.40300  28.23900 1.000 22.65636 ? 62  PRO A CD  1 
ATOM   471  N  N   . HIS A 1 71  ? 19.15700  -6.48100  24.73900 1.000 18.76562 ? 63  HIS A N   1 
ATOM   472  C  CA  . HIS A 1 71  ? 17.74700  -6.36400  24.30400 1.000 16.68851 ? 63  HIS A CA  1 
ATOM   473  C  C   . HIS A 1 71  ? 16.96800  -7.57000  24.83300 1.000 21.29929 ? 63  HIS A C   1 
ATOM   474  O  O   . HIS A 1 71  ? 17.50100  -8.68600  24.80500 1.000 17.53561 ? 63  HIS A O   1 
ATOM   475  C  CB  . HIS A 1 71  ? 17.65000  -6.26200  22.77500 1.000 15.56409 ? 63  HIS A CB  1 
ATOM   476  C  CG  . HIS A 1 71  ? 18.34200  -5.07500  22.20800 1.000 16.77702 ? 63  HIS A CG  1 
ATOM   477  N  ND1 . HIS A 1 71  ? 18.38900  -4.83500  20.86000 1.000 18.97131 ? 63  HIS A ND1 1 
ATOM   478  C  CD2 . HIS A 1 71  ? 19.01700  -4.07000  22.79900 1.000 19.07048 ? 63  HIS A CD2 1 
ATOM   479  C  CE1 . HIS A 1 71  ? 19.06200  -3.73100  20.64000 1.000 15.49933 ? 63  HIS A CE1 1 
ATOM   480  N  NE2 . HIS A 1 71  ? 19.46000  -3.24500  21.81100 1.000 17.63364 ? 63  HIS A NE2 1 
ATOM   481  N  N   . PHE A 1 72  ? 15.73300  -7.33800  25.25700 1.000 16.29696 ? 64  PHE A N   1 
ATOM   482  C  CA  . PHE A 1 72  ? 14.88200  -8.45000  25.74100 1.000 16.99528 ? 64  PHE A CA  1 
ATOM   483  C  C   . PHE A 1 72  ? 14.84400  -9.50500  24.63900 1.000 19.39792 ? 64  PHE A C   1 
ATOM   484  O  O   . PHE A 1 72  ? 14.40000  -9.19400  23.54200 1.000 18.36875 ? 64  PHE A O   1 
ATOM   485  C  CB  . PHE A 1 72  ? 13.51000  -7.93700  26.16800 1.000 16.61713 ? 64  PHE A CB  1 
ATOM   486  C  CG  . PHE A 1 72  ? 12.58900  -8.97800  26.74200 1.000 16.50529 ? 64  PHE A CG  1 
ATOM   487  C  CD1 . PHE A 1 72  ? 13.07500  -9.98800  27.55200 1.000 19.75950 ? 64  PHE A CD1 1 
ATOM   488  C  CD2 . PHE A 1 72  ? 11.23100  -8.93700  26.48200 1.000 16.38660 ? 64  PHE A CD2 1 
ATOM   489  C  CE1 . PHE A 1 72  ? 12.22300  -10.94800 28.07200 1.000 19.10674 ? 64  PHE A CE1 1 
ATOM   490  C  CE2 . PHE A 1 72  ? 10.38100  -9.89100  27.01100 1.000 16.50024 ? 64  PHE A CE2 1 
ATOM   491  C  CZ  . PHE A 1 72  ? 10.87800  -10.89500 27.80300 1.000 20.24228 ? 64  PHE A CZ  1 
ATOM   492  N  N   . ASN A 1 73  ? 15.22700  -10.73300 24.97700 1.000 17.22836 ? 65  ASN A N   1 
ATOM   493  C  CA  . ASN A 1 73  ? 15.39100  -11.77200 23.93500 1.000 19.15695 ? 65  ASN A CA  1 
ATOM   494  C  C   . ASN A 1 73  ? 15.08100  -13.16600 24.49600 1.000 22.81077 ? 65  ASN A C   1 
ATOM   495  O  O   . ASN A 1 73  ? 15.99200  -13.98800 24.56500 1.000 24.93177 ? 65  ASN A O   1 
ATOM   496  C  CB  . ASN A 1 73  ? 16.80500  -11.69900 23.35600 1.000 15.32039 ? 65  ASN A CB  1 
ATOM   497  C  CG  . ASN A 1 73  ? 17.01100  -12.54800 22.12100 1.000 20.45361 ? 65  ASN A CG  1 
ATOM   498  O  OD1 . ASN A 1 73  ? 16.05700  -12.96300 21.47200 1.000 19.43856 ? 65  ASN A OD1 1 
ATOM   499  N  ND2 . ASN A 1 73  ? 18.26300  -12.80700 21.79400 1.000 19.32678 ? 65  ASN A ND2 1 
ATOM   500  N  N   . PRO A 1 74  ? 13.82300  -13.45700 24.86700 1.000 20.72586 ? 66  PRO A N   1 
ATOM   501  C  CA  . PRO A 1 74  ? 13.45100  -14.78500 25.35200 1.000 25.01643 ? 66  PRO A CA  1 
ATOM   502  C  C   . PRO A 1 74  ? 13.60600  -15.90100 24.30600 1.000 28.66356 ? 66  PRO A C   1 
ATOM   503  O  O   . PRO A 1 74  ? 13.84200  -17.01100 24.69800 1.000 31.38840 ? 66  PRO A O   1 
ATOM   504  C  CB  . PRO A 1 74  ? 11.95800  -14.63100 25.66900 1.000 20.11402 ? 66  PRO A CB  1 
ATOM   505  C  CG  . PRO A 1 74  ? 11.50100  -13.45000 24.87500 1.000 20.79287 ? 66  PRO A CG  1 
ATOM   506  C  CD  . PRO A 1 74  ? 12.69700  -12.53100 24.85300 1.000 19.63145 ? 66  PRO A CD  1 
ATOM   507  N  N   . LEU A 1 75  ? 13.45300  -15.58400 23.01800 1.000 24.79182 ? 67  LEU A N   1 
ATOM   508  C  CA  . LEU A 1 75  ? 13.49300  -16.62100 21.95200 1.000 21.93972 ? 67  LEU A CA  1 
ATOM   509  C  C   . LEU A 1 75  ? 14.91300  -16.83500 21.40400 1.000 23.96669 ? 67  LEU A C   1 
ATOM   510  O  O   . LEU A 1 75  ? 15.04600  -17.57100 20.43100 1.000 30.86788 ? 67  LEU A O   1 
ATOM   511  C  CB  . LEU A 1 75  ? 12.51400  -16.22400 20.84500 1.000 21.07877 ? 67  LEU A CB  1 
ATOM   512  C  CG  . LEU A 1 75  ? 11.03700  -16.23200 21.22600 1.000 21.65197 ? 67  LEU A CG  1 
ATOM   513  C  CD1 . LEU A 1 75  ? 10.18000  -15.80400 20.04800 1.000 24.44657 ? 67  LEU A CD1 1 
ATOM   514  C  CD2 . LEU A 1 75  ? 10.61300  -17.60400 21.71400 1.000 29.22965 ? 67  LEU A CD2 1 
ATOM   515  N  N   . SER A 1 76  ? 15.91700  -16.21000 21.99700 1.000 24.90806 ? 68  SER A N   1 
ATOM   516  C  CA  . SER A 1 76  ? 17.32700  -16.43500 21.58900 1.000 27.43609 ? 68  SER A CA  1 
ATOM   517  C  C   . SER A 1 76  ? 17.53000  -16.18900 20.09000 1.000 28.84581 ? 68  SER A C   1 
ATOM   518  O  O   . SER A 1 76  ? 18.13700  -17.02000 19.42800 1.000 26.21133 ? 68  SER A O   1 
ATOM   519  C  CB  . SER A 1 76  ? 17.79000  -17.80100 21.99700 1.000 31.87998 ? 68  SER A CB  1 
ATOM   520  O  OG  . SER A 1 76  ? 18.99300  -17.71900 22.74500 1.000 41.28603 ? 68  SER A OG  1 
ATOM   521  N  N   . ARG A 1 77  ? 17.07000  -15.03600 19.61100 1.000 29.15526 ? 69  ARG A N   1 
ATOM   522  C  CA  . ARG A 1 77  ? 17.21100  -14.70400 18.17300 1.000 22.72208 ? 69  ARG A CA  1 
ATOM   523  C  C   . ARG A 1 77  ? 18.21200  -13.56800 18.00000 1.000 22.82487 ? 69  ARG A C   1 
ATOM   524  O  O   . ARG A 1 77  ? 18.71400  -13.07300 19.01200 1.000 24.90231 ? 69  ARG A O   1 
ATOM   525  C  CB  . ARG A 1 77  ? 15.83600  -14.39400 17.57500 1.000 24.32629 ? 69  ARG A CB  1 
ATOM   526  C  CG  . ARG A 1 77  ? 14.97700  -15.62800 17.34900 1.000 27.77589 ? 69  ARG A CG  1 
ATOM   527  C  CD  . ARG A 1 77  ? 13.66100  -15.30400 16.68400 1.000 33.84136 ? 69  ARG A CD  1 
ATOM   528  N  NE  . ARG A 1 77  ? 12.68500  -16.36400 16.87100 1.000 37.51904 ? 69  ARG A NE  1 
ATOM   529  C  CZ  . ARG A 1 77  ? 11.42800  -16.30800 16.45100 1.000 41.16099 ? 69  ARG A CZ  1 
ATOM   530  N  NH1 . ARG A 1 77  ? 10.99100  -15.23800 15.81100 1.000 40.42670 ? 69  ARG A NH1 1 
ATOM   531  N  NH2 . ARG A 1 77  ? 10.61100  -17.32300 16.66500 1.000 39.39172 ? 69  ARG A NH2 1 
ATOM   532  N  N   . LYS A 1 78  ? 18.49100  -13.19900 16.75000 1.000 20.06711 ? 70  LYS A N   1 
ATOM   533  C  CA  . LYS A 1 78  ? 19.39700  -12.06300 16.48500 1.000 18.09026 ? 70  LYS A CA  1 
ATOM   534  C  C   . LYS A 1 78  ? 18.61100  -10.76700 16.30700 1.000 16.45871 ? 70  LYS A C   1 
ATOM   535  O  O   . LYS A 1 78  ? 17.41400  -10.81600 16.09800 1.000 17.81573 ? 70  LYS A O   1 
ATOM   536  C  CB  . LYS A 1 78  ? 20.24300  -12.30900 15.23700 1.000 27.53001 ? 70  LYS A CB  1 
ATOM   537  C  CG  . LYS A 1 78  ? 21.20800  -13.48400 15.33300 1.000 30.47992 ? 70  LYS A CG  1 
ATOM   538  C  CD  . LYS A 1 78  ? 22.15500  -13.37300 16.50700 1.000 31.68025 ? 70  LYS A CD  1 
ATOM   539  C  CE  . LYS A 1 78  ? 23.25300  -14.41500 16.51400 1.000 37.80970 ? 70  LYS A CE  1 
ATOM   540  N  NZ  . LYS A 1 78  ? 24.38500  -14.03800 15.63500 1.000 42.37175 ? 70  LYS A NZ  1 
ATOM   541  N  N   . HIS A 1 79  ? 19.33300  -9.66100  16.40100 1.000 17.51287 ? 71  HIS A N   1 
ATOM   542  C  CA  . HIS A 1 79  ? 18.70600  -8.33300  16.28400 1.000 17.00329 ? 71  HIS A CA  1 
ATOM   543  C  C   . HIS A 1 79  ? 18.09900  -8.10200  14.91500 1.000 16.52818 ? 71  HIS A C   1 
ATOM   544  O  O   . HIS A 1 79  ? 18.68300  -8.50000  13.91500 1.000 15.94330 ? 71  HIS A O   1 
ATOM   545  C  CB  . HIS A 1 79  ? 19.71900  -7.24400  16.62200 1.000 18.11550 ? 71  HIS A CB  1 
ATOM   546  C  CG  . HIS A 1 79  ? 19.16500  -5.86500  16.56900 1.000 18.61364 ? 71  HIS A CG  1 
ATOM   547  N  ND1 . HIS A 1 79  ? 18.36900  -5.32200  17.56200 1.000 18.49612 ? 71  HIS A ND1 1 
ATOM   548  C  CD2 . HIS A 1 79  ? 19.28900  -4.91300  15.62600 1.000 19.30473 ? 71  HIS A CD2 1 
ATOM   549  C  CE1 . HIS A 1 79  ? 18.03500  -4.10400  17.22200 1.000 15.35574 ? 71  HIS A CE1 1 
ATOM   550  N  NE2 . HIS A 1 79  ? 18.58700  -3.83100  16.05100 1.000 16.50770 ? 71  HIS A NE2 1 
ATOM   551  N  N   . GLY A 1 80  ? 16.96300  -7.42900  14.92600 1.000 19.82337 ? 72  GLY A N   1 
ATOM   552  C  CA  . GLY A 1 80  ? 16.33100  -7.04600  13.66400 1.000 18.63276 ? 72  GLY A CA  1 
ATOM   553  C  C   . GLY A 1 80  ? 15.39300  -5.87600  13.86600 1.000 17.53346 ? 72  GLY A C   1 
ATOM   554  O  O   . GLY A 1 80  ? 15.42500  -5.26500  14.93900 1.000 14.92814 ? 72  GLY A O   1 
ATOM   555  N  N   . GLY A 1 81  ? 14.61400  -5.58000  12.83900 1.000 16.83373 ? 73  GLY A N   1 
ATOM   556  C  CA  . GLY A 1 81  ? 13.58900  -4.55100  12.97500 1.000 18.68320 ? 73  GLY A CA  1 
ATOM   557  C  C   . GLY A 1 81  ? 12.30000  -5.15100  13.50400 1.000 16.70405 ? 73  GLY A C   1 
ATOM   558  O  O   . GLY A 1 81  ? 12.16800  -6.37100  13.51900 1.000 17.90645 ? 73  GLY A O   1 
ATOM   559  N  N   . PRO A 1 82  ? 11.35500  -4.30800  13.92800 1.000 17.09706 ? 74  PRO A N   1 
ATOM   560  C  CA  . PRO A 1 82  ? 10.10100  -4.78900  14.49700 1.000 15.86717 ? 74  PRO A CA  1 
ATOM   561  C  C   . PRO A 1 82  ? 9.27200   -5.67100  13.54500 1.000 16.26586 ? 74  PRO A C   1 
ATOM   562  O  O   . PRO A 1 82  ? 8.54100   -6.48900  14.00700 1.000 18.53389 ? 74  PRO A O   1 
ATOM   563  C  CB  . PRO A 1 82  ? 9.36800   -3.48700  14.82000 1.000 14.72220 ? 74  PRO A CB  1 
ATOM   564  C  CG  . PRO A 1 82  ? 10.02100  -2.42600  13.97900 1.000 14.19230 ? 74  PRO A CG  1 
ATOM   565  C  CD  . PRO A 1 82  ? 11.46500  -2.85500  13.90000 1.000 16.39780 ? 74  PRO A CD  1 
ATOM   566  N  N   . LYS A 1 83  ? 9.43000   -5.46400  12.23900 1.000 18.20776 ? 75  LYS A N   1 
ATOM   567  C  CA  . LYS A 1 83  ? 8.64400   -6.22700  11.23000 1.000 20.65684 ? 75  LYS A CA  1 
ATOM   568  C  C   . LYS A 1 83  ? 9.34200   -7.52300  10.79400 1.000 23.35295 ? 75  LYS A C   1 
ATOM   569  O  O   . LYS A 1 83  ? 8.72700   -8.30400  10.07600 1.000 21.73664 ? 75  LYS A O   1 
ATOM   570  C  CB  . LYS A 1 83  ? 8.36800   -5.33300  10.02300 1.000 20.08533 ? 75  LYS A CB  1 
ATOM   571  C  CG  . LYS A 1 83  ? 6.97300   -4.73300  9.95900  1.000 27.78851 ? 75  LYS A CG  1 
ATOM   572  C  CD  . LYS A 1 83  ? 6.55000   -4.05000  11.23300 1.000 23.67631 ? 75  LYS A CD  1 
ATOM   573  C  CE  . LYS A 1 83  ? 5.06000   -4.15600  11.46900 1.000 39.72913 ? 75  LYS A CE  1 
ATOM   574  N  NZ  . LYS A 1 83  ? 4.64200   -3.43100  12.69100 1.000 36.83089 ? 75  LYS A NZ  1 
ATOM   575  N  N   . ASP A 1 84  ? 10.59100  -7.71000  11.20200 1.000 20.31491 ? 76  ASP A N   1 
ATOM   576  C  CA  . ASP A 1 84  ? 11.35000  -8.91400  10.80000 1.000 21.90051 ? 76  ASP A CA  1 
ATOM   577  C  C   . ASP A 1 84  ? 10.95600  -10.12600 11.65100 1.000 23.30850 ? 76  ASP A C   1 
ATOM   578  O  O   . ASP A 1 84  ? 10.71400  -9.94200  12.83800 1.000 24.47541 ? 76  ASP A O   1 
ATOM   579  C  CB  . ASP A 1 84  ? 12.85700  -8.68400  10.89400 1.000 17.71102 ? 76  ASP A CB  1 
ATOM   580  C  CG  . ASP A 1 84  ? 13.33900  -7.57700  9.98900  1.000 22.55269 ? 76  ASP A CG  1 
ATOM   581  O  OD1 . ASP A 1 84  ? 12.77700  -7.42900  8.89000  1.000 27.12627 ? 76  ASP A OD1 1 
ATOM   582  O  OD2 . ASP A 1 84  ? 14.25700  -6.88200  10.40200 1.000 24.08151 ? 76  ASP A OD2 1 
ATOM   583  N  N   . GLU A 1 85  ? 10.91400  -11.31200 11.04500 1.000 23.75594 ? 77  GLU A N   1 
ATOM   584  C  CA  . GLU A 1 85  ? 10.64500  -12.55400 11.81200 1.000 26.83269 ? 77  GLU A CA  1 
ATOM   585  C  C   . GLU A 1 85  ? 11.82300  -12.82500 12.74100 1.000 26.31164 ? 77  GLU A C   1 
ATOM   586  O  O   . GLU A 1 85  ? 11.59100  -13.25400 13.86400 1.000 24.82936 ? 77  GLU A O   1 
ATOM   587  C  CB  . GLU A 1 85  ? 10.47500  -13.73100 10.85500 1.000 30.17316 ? 77  GLU A CB  1 
ATOM   588  C  CG  . GLU A 1 85  ? 9.14700   -14.44500 10.98900 1.000 43.15005 ? 77  GLU A CG  1 
ATOM   589  C  CD  . GLU A 1 85  ? 9.12600   -15.53800 12.04000 1.000 50.41914 ? 77  GLU A CD  1 
ATOM   590  O  OE1 . GLU A 1 85  ? 10.21300  -15.96000 12.47300 1.000 53.90291 ? 77  GLU A OE1 1 
ATOM   591  O  OE2 . GLU A 1 85  ? 8.02200   -15.95900 12.42300 1.000 57.50625 ? 77  GLU A OE2 1 
ATOM   592  N  N   . GLU A 1 86  ? 13.03200  -12.56100 12.25400 1.000 22.33543 ? 78  GLU A N   1 
ATOM   593  C  CA  . GLU A 1 86  ? 14.23400  -12.71000 13.09100 1.000 19.14519 ? 78  GLU A CA  1 
ATOM   594  C  C   . GLU A 1 86  ? 14.45700  -11.38500 13.81100 1.000 21.18329 ? 78  GLU A C   1 
ATOM   595  O  O   . GLU A 1 86  ? 15.01400  -10.46800 13.21700 1.000 19.96997 ? 78  GLU A O   1 
ATOM   596  C  CB  . GLU A 1 86  ? 15.44000  -13.12800 12.25200 1.000 23.07870 ? 78  GLU A CB  1 
ATOM   597  C  CG  . GLU A 1 86  ? 16.66600  -13.47300 13.07400 1.000 22.12240 ? 78  GLU A CG  1 
ATOM   598  C  CD  . GLU A 1 86  ? 16.63600  -14.81100 13.79400 1.000 26.88987 ? 78  GLU A CD  1 
ATOM   599  O  OE1 . GLU A 1 86  ? 15.72300  -15.61400 13.52800 1.000 30.99460 ? 78  GLU A OE1 1 
ATOM   600  O  OE2 . GLU A 1 86  ? 17.53200  -15.04900 14.60700 1.000 23.66670 ? 78  GLU A OE2 1 
ATOM   601  N  N   . ARG A 1 87  ? 14.00200  -11.33600 15.05800 1.000 21.62445 ? 79  ARG A N   1 
ATOM   602  C  CA  . ARG A 1 87  ? 14.21300  -10.13200 15.87200 1.000 16.60939 ? 79  ARG A CA  1 
ATOM   603  C  C   . ARG A 1 87  ? 14.21000  -10.48100 17.35600 1.000 16.82588 ? 79  ARG A C   1 
ATOM   604  O  O   . ARG A 1 87  ? 13.75700  -11.56200 17.69600 1.000 17.08579 ? 79  ARG A O   1 
ATOM   605  C  CB  . ARG A 1 87  ? 13.06400  -9.14600  15.65300 1.000 14.38525 ? 79  ARG A CB  1 
ATOM   606  C  CG  . ARG A 1 87  ? 11.68000  -9.70800  15.92500 1.000 15.12132 ? 79  ARG A CG  1 
ATOM   607  C  CD  . ARG A 1 87  ? 10.64300  -8.60600  15.91400 1.000 15.88322 ? 79  ARG A CD  1 
ATOM   608  N  NE  . ARG A 1 87  ? 10.47300  -8.00700  17.22800 1.000 16.45953 ? 79  ARG A NE  1 
ATOM   609  C  CZ  . ARG A 1 87  ? 9.47200   -7.20900  17.56600 1.000 14.90037 ? 79  ARG A CZ  1 
ATOM   610  N  NH1 . ARG A 1 87  ? 8.54500   -6.90500  16.68000 1.000 15.77324 ? 79  ARG A NH1 1 
ATOM   611  N  NH2 . ARG A 1 87  ? 9.38900   -6.72700  18.79100 1.000 14.12171 ? 79  ARG A NH2 1 
ATOM   612  N  N   . HIS A 1 88  ? 14.77200  -9.59600  18.16100 1.000 15.19233 ? 80  HIS A N   1 
ATOM   613  C  CA  . HIS A 1 88  ? 14.62100  -9.70600  19.62800 1.000 16.42674 ? 80  HIS A CA  1 
ATOM   614  C  C   . HIS A 1 88  ? 13.18700  -9.24400  19.97200 1.000 18.09209 ? 80  HIS A C   1 
ATOM   615  O  O   . HIS A 1 88  ? 12.66800  -8.37500  19.28300 1.000 14.72894 ? 80  HIS A O   1 
ATOM   616  C  CB  . HIS A 1 88  ? 15.64700  -8.81100  20.28900 1.000 13.67963 ? 80  HIS A CB  1 
ATOM   617  C  CG  . HIS A 1 88  ? 17.06200  -9.16000  20.01000 1.000 13.43441 ? 80  HIS A CG  1 
ATOM   618  N  ND1 . HIS A 1 88  ? 18.05000  -8.20900  19.92900 1.000 14.26401 ? 80  HIS A ND1 1 
ATOM   619  C  CD2 . HIS A 1 88  ? 17.65500  -10.35300 19.82300 1.000 16.12576 ? 80  HIS A CD2 1 
ATOM   620  C  CE1 . HIS A 1 88  ? 19.19800  -8.80600  19.71200 1.000 18.58938 ? 80  HIS A CE1 1 
ATOM   621  N  NE2 . HIS A 1 88  ? 18.98300  -10.11800 19.64000 1.000 14.13734 ? 80  HIS A NE2 1 
ATOM   622  N  N   . VAL A 1 89  ? 12.57200  -9.78100  21.01800 1.000 13.94359 ? 81  VAL A N   1 
ATOM   623  C  CA  . VAL A 1 89  ? 11.21800  -9.29200  21.40800 1.000 12.65299 ? 81  VAL A CA  1 
ATOM   624  C  C   . VAL A 1 89  ? 11.27900  -7.77800  21.67300 1.000 11.77540 ? 81  VAL A C   1 
ATOM   625  O  O   . VAL A 1 89  ? 10.29000  -7.11900  21.43600 1.000 12.74219 ? 81  VAL A O   1 
ATOM   626  C  CB  . VAL A 1 89  ? 10.63200  -10.08500 22.59500 1.000 10.72067 ? 81  VAL A CB  1 
ATOM   627  C  CG1 . VAL A 1 89  ? 9.41100   -9.43500  23.21400 1.000 12.51930 ? 81  VAL A CG1 1 
ATOM   628  C  CG2 . VAL A 1 89  ? 10.34300  -11.52400 22.20000 1.000 15.53542 ? 81  VAL A CG2 1 
ATOM   629  N  N   . GLY A 1 90  ? 12.41700  -7.27500  22.13500 1.000 11.46579 ? 82  GLY A N   1 
ATOM   630  C  CA  . GLY A 1 90  ? 12.52400  -5.85400  22.51500 1.000 13.81994 ? 82  GLY A CA  1 
ATOM   631  C  C   . GLY A 1 90  ? 12.88900  -4.92800  21.36000 1.000 13.08083 ? 82  GLY A C   1 
ATOM   632  O  O   . GLY A 1 90  ? 13.09600  -3.75600  21.61400 1.000 12.62336 ? 82  GLY A O   1 
ATOM   633  N  N   . ASP A 1 91  ? 12.93400  -5.45600  20.13900 1.000 14.93257 ? 83  ASP A N   1 
ATOM   634  C  CA  . ASP A 1 91  ? 13.29600  -4.66100  18.94000 1.000 15.79295 ? 83  ASP A CA  1 
ATOM   635  C  C   . ASP A 1 91  ? 12.11200  -3.83800  18.43400 1.000 13.11425 ? 83  ASP A C   1 
ATOM   636  O  O   . ASP A 1 91  ? 11.34700  -4.36900  17.64000 1.000 14.95876 ? 83  ASP A O   1 
ATOM   637  C  CB  . ASP A 1 91  ? 13.84000  -5.57800  17.85000 1.000 13.99831 ? 83  ASP A CB  1 
ATOM   638  C  CG  . ASP A 1 91  ? 15.19700  -6.15900  18.20800 1.000 15.69729 ? 83  ASP A CG  1 
ATOM   639  O  OD1 . ASP A 1 91  ? 15.76200  -5.72000  19.21000 1.000 11.77981 ? 83  ASP A OD1 1 
ATOM   640  O  OD2 . ASP A 1 91  ? 15.67000  -7.04400  17.47900 1.000 14.98235 ? 83  ASP A OD2 1 
ATOM   641  N  N   . LEU A 1 92  ? 12.01600  -2.58900  18.88800 1.000 11.94227 ? 84  LEU A N   1 
ATOM   642  C  CA  . LEU A 1 92  ? 10.88400  -1.70600  18.48300 1.000 14.78348 ? 84  LEU A CA  1 
ATOM   643  C  C   . LEU A 1 92  ? 11.31900  -0.70200  17.40900 1.000 11.84261 ? 84  LEU A C   1 
ATOM   644  O  O   . LEU A 1 92  ? 10.59000  0.23900   17.17400 1.000 14.09241 ? 84  LEU A O   1 
ATOM   645  C  CB  . LEU A 1 92  ? 10.30800  -1.01000  19.72100 1.000 12.67759 ? 84  LEU A CB  1 
ATOM   646  C  CG  . LEU A 1 92  ? 9.69500   -1.95400  20.74900 1.000 15.60994 ? 84  LEU A CG  1 
ATOM   647  C  CD1 . LEU A 1 92  ? 9.09800   -1.18000  21.91200 1.000 13.59357 ? 84  LEU A CD1 1 
ATOM   648  C  CD2 . LEU A 1 92  ? 8.65100   -2.85100  20.10200 1.000 16.99025 ? 84  LEU A CD2 1 
ATOM   649  N  N   . GLY A 1 93  ? 12.49700  -0.90400  16.83600 1.000 12.18078 ? 85  GLY A N   1 
ATOM   650  C  CA  . GLY A 1 93  ? 12.95200  -0.07700  15.71500 1.000 13.65965 ? 85  GLY A CA  1 
ATOM   651  C  C   . GLY A 1 93  ? 13.41500  1.31300   16.07900 1.000 11.25650 ? 85  GLY A C   1 
ATOM   652  O  O   . GLY A 1 93  ? 14.16400  1.45900   17.02200 1.000 11.89845 ? 85  GLY A O   1 
ATOM   653  N  N   . ASN A 1 94  ? 12.98200  2.27600   15.27400 1.000 10.61787 ? 86  ASN A N   1 
ATOM   654  C  CA  . ASN A 1 94  ? 13.41700  3.66300   15.48900 1.000 10.86934 ? 86  ASN A CA  1 
ATOM   655  C  C   . ASN A 1 94  ? 12.25400  4.63300   15.70000 1.000 13.54946 ? 86  ASN A C   1 
ATOM   656  O  O   . ASN A 1 94  ? 11.20100  4.41800   15.13500 1.000 11.11977 ? 86  ASN A O   1 
ATOM   657  C  CB  . ASN A 1 94  ? 14.17100  4.19600   14.27500 1.000 12.04050 ? 86  ASN A CB  1 
ATOM   658  C  CG  . ASN A 1 94  ? 15.53700  3.58200   14.09400 1.000 14.84899 ? 86  ASN A CG  1 
ATOM   659  O  OD1 . ASN A 1 94  ? 16.43600  3.85500   14.87500 1.000 14.07626 ? 86  ASN A OD1 1 
ATOM   660  N  ND2 . ASN A 1 94  ? 15.69900  2.77600   13.06100 1.000 12.71024 ? 86  ASN A ND2 1 
ATOM   661  N  N   . VAL A 1 95  ? 12.48600  5.61400   16.55500 1.000 12.99534 ? 87  VAL A N   1 
ATOM   662  C  CA  . VAL A 1 95  ? 11.53900  6.73600   16.69800 1.000 11.69239 ? 87  VAL A CA  1 
ATOM   663  C  C   . VAL A 1 95  ? 12.15300  7.86200   15.85800 1.000 15.34477 ? 87  VAL A C   1 
ATOM   664  O  O   . VAL A 1 95  ? 13.37600  7.86700   15.67200 1.000 13.86683 ? 87  VAL A O   1 
ATOM   665  C  CB  . VAL A 1 95  ? 11.32700  7.10400   18.17400 1.000 13.70798 ? 87  VAL A CB  1 
ATOM   666  C  CG1 . VAL A 1 95  ? 10.62700  5.99600   18.93700 1.000 13.73418 ? 87  VAL A CG1 1 
ATOM   667  C  CG2 . VAL A 1 95  ? 12.61400  7.51800   18.86100 1.000 13.72954 ? 87  VAL A CG2 1 
ATOM   668  N  N   . THR A 1 96  ? 11.30600  8.75000   15.36200 1.000 15.58234 ? 88  THR A N   1 
ATOM   669  C  CA  . THR A 1 96  ? 11.77300  9.85700   14.50900 1.000 15.28496 ? 88  THR A CA  1 
ATOM   670  C  C   . THR A 1 96  ? 11.56400  11.19800  15.22700 1.000 14.20021 ? 88  THR A C   1 
ATOM   671  O  O   . THR A 1 96  ? 10.43300  11.50400  15.57400 1.000 14.35584 ? 88  THR A O   1 
ATOM   672  C  CB  . THR A 1 96  ? 11.10900  9.80700   13.12700 1.000 14.51868 ? 88  THR A CB  1 
ATOM   673  O  OG1 . THR A 1 96  ? 11.44400  8.57400   12.49700 1.000 18.62092 ? 88  THR A OG1 1 
ATOM   674  C  CG2 . THR A 1 96  ? 11.53500  10.96300  12.24700 1.000 14.88443 ? 88  THR A CG2 1 
ATOM   675  N  N   . ALA A 1 97  ? 12.64700  11.94100  15.41900 1.000 12.52084 ? 89  ALA A N   1 
ATOM   676  C  CA  . ALA A 1 97  ? 12.54900  13.28600  16.01500 1.000 14.47746 ? 89  ALA A CA  1 
ATOM   677  C  C   . ALA A 1 97  ? 12.45800  14.33700  14.89800 1.000 17.04461 ? 89  ALA A C   1 
ATOM   678  O  O   . ALA A 1 97  ? 13.17800  14.23400  13.91400 1.000 15.05637 ? 89  ALA A O   1 
ATOM   679  C  CB  . ALA A 1 97  ? 13.69200  13.58400  16.94400 1.000 17.37652 ? 89  ALA A CB  1 
ATOM   680  N  N   . ASP A 1 98  ? 11.57500  15.30500  15.10300 1.000 18.50205 ? 90  ASP A N   1 
ATOM   681  C  CA  . ASP A 1 98  ? 11.40000  16.38800  14.12100 1.000 20.70266 ? 90  ASP A CA  1 
ATOM   682  C  C   . ASP A 1 98  ? 12.49200  17.44500  14.29900 1.000 21.19787 ? 90  ASP A C   1 
ATOM   683  O  O   . ASP A 1 98  ? 13.41400  17.22600  15.07800 1.000 20.58166 ? 90  ASP A O   1 
ATOM   684  C  CB  . ASP A 1 98  ? 10.01600  17.01700  14.26500 1.000 20.68932 ? 90  ASP A CB  1 
ATOM   685  C  CG  . ASP A 1 98  ? 9.68500   17.62100  15.61800 1.000 21.91042 ? 90  ASP A CG  1 
ATOM   686  O  OD1 . ASP A 1 98  ? 10.60800  17.97500  16.35700 1.000 23.69204 ? 90  ASP A OD1 1 
ATOM   687  O  OD2 . ASP A 1 98  ? 8.48800   17.73000  15.91500 1.000 25.86618 ? 90  ASP A OD2 1 
ATOM   688  N  N   . LYS A 1 99  ? 12.32300  18.57700  13.62100 1.000 21.50199 ? 91  LYS A N   1 
ATOM   689  C  CA  . LYS A 1 99  ? 13.34000  19.65700  13.67900 1.000 22.91412 ? 91  LYS A CA  1 
ATOM   690  C  C   . LYS A 1 99  ? 13.41400  20.26400  15.07800 1.000 21.82129 ? 91  LYS A C   1 
ATOM   691  O  O   . LYS A 1 99  ? 14.45000  20.83200  15.40000 1.000 26.31265 ? 91  LYS A O   1 
ATOM   692  C  CB  . LYS A 1 99  ? 13.00200  20.74900  12.66300 1.000 22.94034 ? 91  LYS A CB  1 
ATOM   693  C  CG  . LYS A 1 99  ? 11.66400  21.44400  12.85400 1.000 25.23412 ? 91  LYS A CG  1 
ATOM   694  C  CD  . LYS A 1 99  ? 11.47300  22.61500  11.91700 1.000 32.08843 ? 91  LYS A CD  1 
ATOM   695  C  CE  . LYS A 1 99  ? 10.18000  23.36500  12.14800 1.000 39.71409 ? 91  LYS A CE  1 
ATOM   696  N  NZ  . LYS A 1 99  ? 10.17200  24.05700  13.45900 1.000 41.64007 ? 91  LYS A NZ  1 
ATOM   697  N  N   . ASP A 1 100 ? 12.33600  20.16000  15.84800 1.000 21.32954 ? 92  ASP A N   1 
ATOM   698  C  CA  . ASP A 1 100 ? 12.29300  20.75700  17.20400 1.000 23.13242 ? 92  ASP A CA  1 
ATOM   699  C  C   . ASP A 1 100 ? 12.75200  19.74400  18.26300 1.000 19.27511 ? 92  ASP A C   1 
ATOM   700  O  O   . ASP A 1 100 ? 12.68300  20.08100  19.43900 1.000 22.83630 ? 92  ASP A O   1 
ATOM   701  C  CB  . ASP A 1 100 ? 10.89600  21.29600  17.49600 1.000 27.19312 ? 92  ASP A CB  1 
ATOM   702  C  CG  . ASP A 1 100 ? 10.46100  22.36000  16.50600 1.000 29.70015 ? 92  ASP A CG  1 
ATOM   703  O  OD1 . ASP A 1 100 ? 11.33100  23.09400  16.02800 1.000 29.57278 ? 92  ASP A OD1 1 
ATOM   704  O  OD2 . ASP A 1 100 ? 9.26300   22.42400  16.21100 1.000 37.63158 ? 92  ASP A OD2 1 
ATOM   705  N  N   . GLY A 1 101 ? 13.19600  18.56400  17.84600 1.000 17.37598 ? 93  GLY A N   1 
ATOM   706  C  CA  . GLY A 1 101 ? 13.69300  17.54000  18.78200 1.000 20.14258 ? 93  GLY A CA  1 
ATOM   707  C  C   . GLY A 1 101 ? 12.60300  16.69600  19.44600 1.000 20.70155 ? 93  GLY A C   1 
ATOM   708  O  O   . GLY A 1 101 ? 12.90700  16.01800  20.41600 1.000 17.54092 ? 93  GLY A O   1 
ATOM   709  N  N   . VAL A 1 102 ? 11.39400  16.73900  18.90000 1.000 17.64884 ? 94  VAL A N   1 
ATOM   710  C  CA  . VAL A 1 102 ? 10.26800  15.96300  19.48200 1.000 16.34492 ? 94  VAL A CA  1 
ATOM   711  C  C   . VAL A 1 102 ? 10.00100  14.73200  18.62100 1.000 16.82586 ? 94  VAL A C   1 
ATOM   712  O  O   . VAL A 1 102 ? 9.86600   14.88600  17.41900 1.000 17.29784 ? 94  VAL A O   1 
ATOM   713  C  CB  . VAL A 1 102 ? 8.98900   16.80300  19.64800 1.000 23.72557 ? 94  VAL A CB  1 
ATOM   714  C  CG1 . VAL A 1 102 ? 7.90100   16.02500  20.36700 1.000 18.25622 ? 94  VAL A CG1 1 
ATOM   715  C  CG2 . VAL A 1 102 ? 9.27400   18.11100  20.36400 1.000 19.80822 ? 94  VAL A CG2 1 
ATOM   716  N  N   . ALA A 1 103 ? 9.99700   13.56700  19.25500 1.000 18.78964 ? 95  ALA A N   1 
ATOM   717  C  CA  . ALA A 1 103 ? 9.64200   12.31500  18.56400 1.000 14.79040 ? 95  ALA A CA  1 
ATOM   718  C  C   . ALA A 1 103 ? 8.24100   11.91700  19.01400 1.000 17.47888 ? 95  ALA A C   1 
ATOM   719  O  O   . ALA A 1 103 ? 8.08300   11.58600  20.17800 1.000 20.12267 ? 95  ALA A O   1 
ATOM   720  C  CB  . ALA A 1 103 ? 10.60800  11.21900  18.90300 1.000 14.10507 ? 95  ALA A CB  1 
ATOM   721  N  N   . ASP A 1 104 ? 7.27900   12.00900  18.11300 1.000 16.31901 ? 96  ASP A N   1 
ATOM   722  C  CA  . ASP A 1 104 ? 5.91700   11.51800  18.43300 1.000 22.59855 ? 96  ASP A CA  1 
ATOM   723  C  C   . ASP A 1 104 ? 5.89900   10.02300  18.15800 1.000 20.09312 ? 96  ASP A C   1 
ATOM   724  O  O   . ASP A 1 104 ? 6.07200   9.62900   17.01800 1.000 22.80349 ? 96  ASP A O   1 
ATOM   725  C  CB  . ASP A 1 104 ? 4.83300   12.24800  17.65000 1.000 26.68629 ? 96  ASP A CB  1 
ATOM   726  C  CG  . ASP A 1 104 ? 4.79200   13.72100  18.00900 1.000 36.81824 ? 96  ASP A CG  1 
ATOM   727  O  OD1 . ASP A 1 104 ? 4.77700   14.02600  19.21300 1.000 41.40793 ? 96  ASP A OD1 1 
ATOM   728  O  OD2 . ASP A 1 104 ? 4.81500   14.54800  17.08500 1.000 50.67127 ? 96  ASP A OD2 1 
ATOM   729  N  N   . VAL A 1 105 ? 5.71000   9.25300   19.20900 1.000 20.61963 ? 97  VAL A N   1 
ATOM   730  C  CA  . VAL A 1 105 ? 5.76900   7.78300   19.05300 1.000 19.91989 ? 97  VAL A CA  1 
ATOM   731  C  C   . VAL A 1 105 ? 4.37100   7.24100   18.75200 1.000 20.81761 ? 97  VAL A C   1 
ATOM   732  O  O   . VAL A 1 105 ? 3.43700   7.59500   19.46800 1.000 17.77548 ? 97  VAL A O   1 
ATOM   733  C  CB  . VAL A 1 105 ? 6.39200   7.11200   20.29000 1.000 16.29707 ? 97  VAL A CB  1 
ATOM   734  C  CG1 . VAL A 1 105 ? 6.49000   5.60400   20.13600 1.000 18.35797 ? 97  VAL A CG1 1 
ATOM   735  C  CG2 . VAL A 1 105 ? 7.74900   7.70900   20.62200 1.000 18.53871 ? 97  VAL A CG2 1 
ATOM   736  N  N   . SER A 1 106 ? 4.28400   6.41600   17.71200 1.000 23.62625 ? 98  SER A N   1 
ATOM   737  C  CA  . SER A 1 106 ? 3.01300   5.74900   17.36000 1.000 25.77962 ? 98  SER A CA  1 
ATOM   738  C  C   . SER A 1 106 ? 3.37500   4.37900   16.81300 1.000 29.21084 ? 98  SER A C   1 
ATOM   739  O  O   . SER A 1 106 ? 3.73700   4.28900   15.64100 1.000 29.63441 ? 98  SER A O   1 
ATOM   740  C  CB  . SER A 1 106 ? 2.21300   6.52400   16.36000 1.000 32.38011 ? 98  SER A CB  1 
ATOM   741  O  OG  . SER A 1 106 ? 0.91000   5.98200   16.23900 1.000 37.75383 ? 98  SER A OG  1 
ATOM   742  N  N   . ILE A 1 107 ? 3.26900   3.36100   17.64900 1.000 21.47401 ? 99  ILE A N   1 
ATOM   743  C  CA  . ILE A 1 107 ? 3.72200   2.02000   17.21900 1.000 22.23557 ? 99  ILE A CA  1 
ATOM   744  C  C   . ILE A 1 107 ? 2.67300   0.97500   17.59200 1.000 17.21461 ? 99  ILE A C   1 
ATOM   745  O  O   . ILE A 1 107 ? 2.02900   1.13200   18.61600 1.000 18.47051 ? 99  ILE A O   1 
ATOM   746  C  CB  . ILE A 1 107 ? 5.07100   1.66700   17.89600 1.000 18.04093 ? 99  ILE A CB  1 
ATOM   747  C  CG1 . ILE A 1 107 ? 6.20200   2.63900   17.56300 1.000 23.79240 ? 99  ILE A CG1 1 
ATOM   748  C  CG2 . ILE A 1 107 ? 5.48800   0.23300   17.61400 1.000 23.47165 ? 99  ILE A CG2 1 
ATOM   749  C  CD1 . ILE A 1 107 ? 7.51400   2.24200   18.18600 1.000 19.25738 ? 99  ILE A CD1 1 
ATOM   750  N  N   . GLU A 1 108 ? 2.51400   -0.02800  16.74300 1.000 21.14645 ? 100 GLU A N   1 
ATOM   751  C  CA  . GLU A 1 108 ? 1.68500   -1.19000  17.12600 1.000 20.85845 ? 100 GLU A CA  1 
ATOM   752  C  C   . GLU A 1 108 ? 2.59900   -2.40200  16.93000 1.000 19.02930 ? 100 GLU A C   1 
ATOM   753  O  O   . GLU A 1 108 ? 3.12600   -2.56400  15.84000 1.000 24.29212 ? 100 GLU A O   1 
ATOM   754  C  CB  . GLU A 1 108 ? 0.37600   -1.27800  16.35000 1.000 26.79441 ? 100 GLU A CB  1 
ATOM   755  C  CG  . GLU A 1 108 ? -0.77000  -0.51600  16.98600 1.000 31.22265 ? 100 GLU A CG  1 
ATOM   756  C  CD  . GLU A 1 108 ? -2.14300  -0.83200  16.41700 1.000 41.60254 ? 100 GLU A CD  1 
ATOM   757  O  OE1 . GLU A 1 108 ? -2.26500  -1.82800  15.67600 1.000 38.14385 ? 100 GLU A OE1 1 
ATOM   758  O  OE2 . GLU A 1 108 ? -3.09000  -0.08200  16.71800 1.000 40.08482 ? 100 GLU A OE2 1 
ATOM   759  N  N   . ASP A 1 109 ? 2.78000   -3.18800  17.98200 1.000 16.53865 ? 101 ASP A N   1 
ATOM   760  C  CA  . ASP A 1 109 ? 3.66300   -4.37300  17.90200 1.000 19.24681 ? 101 ASP A CA  1 
ATOM   761  C  C   . ASP A 1 109 ? 2.88800   -5.59300  18.39000 1.000 18.76370 ? 101 ASP A C   1 
ATOM   762  O  O   . ASP A 1 109 ? 2.30300   -5.49600  19.46400 1.000 21.63419 ? 101 ASP A O   1 
ATOM   763  C  CB  . ASP A 1 109 ? 4.97300   -4.15600  18.64900 1.000 19.29493 ? 101 ASP A CB  1 
ATOM   764  C  CG  . ASP A 1 109 ? 6.01800   -5.19200  18.29500 1.000 18.38559 ? 101 ASP A CG  1 
ATOM   765  O  OD1 . ASP A 1 109 ? 6.53800   -5.11800  17.18000 1.000 22.28513 ? 101 ASP A OD1 1 
ATOM   766  O  OD2 . ASP A 1 109 ? 6.27400   -6.07000  19.12400 1.000 17.36290 ? 101 ASP A OD2 1 
ATOM   767  N  N   A SER A 1 110 ? 3.16200   -6.75600  17.79600 0.408 22.47724 ? 102 SER A N   1 
ATOM   768  N  N   B SER A 1 110 ? 3.16100   -6.75500  17.79500 0.592 22.49436 ? 102 SER A N   1 
ATOM   769  C  CA  A SER A 1 110 ? 2.42700   -7.99100  18.16800 0.408 22.24134 ? 102 SER A CA  1 
ATOM   770  C  CA  B SER A 1 110 ? 2.42700   -7.99000  18.16700 0.592 22.23571 ? 102 SER A CA  1 
ATOM   771  C  C   A SER A 1 110 ? 3.37300   -9.01500  18.80700 0.408 22.52343 ? 102 SER A C   1 
ATOM   772  C  C   B SER A 1 110 ? 3.37300   -9.01300  18.80700 0.592 22.55056 ? 102 SER A C   1 
ATOM   773  O  O   A SER A 1 110 ? 2.98200   -10.18800 18.88200 0.408 22.80154 ? 102 SER A O   1 
ATOM   774  O  O   B SER A 1 110 ? 2.98300   -10.18400 18.87800 0.592 22.82352 ? 102 SER A O   1 
ATOM   775  C  CB  A SER A 1 110 ? 1.72900   -8.56300  16.96000 0.408 26.14641 ? 102 SER A CB  1 
ATOM   776  C  CB  B SER A 1 110 ? 1.73300   -8.55800  16.95400 0.592 26.17358 ? 102 SER A CB  1 
ATOM   777  O  OG  A SER A 1 110 ? 0.74600   -7.66600  16.46700 0.408 30.03900 ? 102 SER A OG  1 
ATOM   778  O  OG  B SER A 1 110 ? 0.72700   -7.67700  16.48300 0.592 30.11242 ? 102 SER A OG  1 
ATOM   779  N  N   . VAL A 1 111 ? 4.64400   -8.64300  18.98900 1.000 17.63976 ? 103 VAL A N   1 
ATOM   780  C  CA  . VAL A 1 111 ? 5.64200   -9.57100  19.58800 1.000 18.04866 ? 103 VAL A CA  1 
ATOM   781  C  C   . VAL A 1 111 ? 5.79100   -9.23200  21.07000 1.000 17.25736 ? 103 VAL A C   1 
ATOM   782  O  O   . VAL A 1 111 ? 5.80700   -10.14900 21.86500 1.000 15.21618 ? 103 VAL A O   1 
ATOM   783  C  CB  . VAL A 1 111 ? 6.99200   -9.49800  18.86100 1.000 16.62506 ? 103 VAL A CB  1 
ATOM   784  C  CG1 . VAL A 1 111 ? 8.04000   -10.39700 19.48200 1.000 15.45637 ? 103 VAL A CG1 1 
ATOM   785  C  CG2 . VAL A 1 111 ? 6.82400   -9.81000  17.38100 1.000 18.54935 ? 103 VAL A CG2 1 
ATOM   786  N  N   . ILE A 1 112 ? 5.91800   -7.94600  21.38400 1.000 16.12935 ? 104 ILE A N   1 
ATOM   787  C  CA  . ILE A 1 112 ? 5.93500   -7.55600  22.82000 1.000 12.54481 ? 104 ILE A CA  1 
ATOM   788  C  C   . ILE A 1 112 ? 4.55000   -7.84700  23.40000 1.000 17.42630 ? 104 ILE A C   1 
ATOM   789  O  O   . ILE A 1 112 ? 3.60400   -7.96100  22.63000 1.000 17.29495 ? 104 ILE A O   1 
ATOM   790  C  CB  . ILE A 1 112 ? 6.27800   -6.06800  23.01000 1.000 13.45544 ? 104 ILE A CB  1 
ATOM   791  C  CG1 . ILE A 1 112 ? 5.27200   -5.14700  22.31900 1.000 15.56100 ? 104 ILE A CG1 1 
ATOM   792  C  CG2 . ILE A 1 112 ? 7.70300   -5.77400  22.57400 1.000 18.11239 ? 104 ILE A CG2 1 
ATOM   793  C  CD1 . ILE A 1 112 ? 5.43000   -3.69600  22.68700 1.000 15.23119 ? 104 ILE A CD1 1 
ATOM   794  N  N   . SER A 1 113 ? 4.45600   -7.89600  24.72700 1.000 15.42372 ? 105 SER A N   1 
ATOM   795  C  CA  . SER A 1 113 ? 3.14700   -8.10400  25.39600 1.000 15.98017 ? 105 SER A CA  1 
ATOM   796  C  C   . SER A 1 113 ? 3.17600   -7.50200  26.80700 1.000 16.33361 ? 105 SER A C   1 
ATOM   797  O  O   . SER A 1 113 ? 4.26400   -7.22100  27.29100 1.000 14.18119 ? 105 SER A O   1 
ATOM   798  C  CB  . SER A 1 113 ? 2.71100   -9.55300  25.44300 1.000 15.66223 ? 105 SER A CB  1 
ATOM   799  O  OG  . SER A 1 113 ? 1.40500   -9.69000  25.96600 1.000 15.94940 ? 105 SER A OG  1 
ATOM   800  N  N   . LEU A 1 114 ? 1.99500   -7.27900  27.37400 1.000 12.83900 ? 106 LEU A N   1 
ATOM   801  C  CA  . LEU A 1 114 ? 1.90100   -6.80300  28.77100 1.000 12.38505 ? 106 LEU A CA  1 
ATOM   802  C  C   . LEU A 1 114 ? 1.56600   -8.00200  29.66500 1.000 19.21998 ? 106 LEU A C   1 
ATOM   803  O  O   . LEU A 1 114 ? 1.36400   -7.78600  30.84700 1.000 21.19510 ? 106 LEU A O   1 
ATOM   804  C  CB  . LEU A 1 114 ? 0.84400   -5.70300  28.86000 1.000 14.73547 ? 106 LEU A CB  1 
ATOM   805  C  CG  . LEU A 1 114 ? 1.08000   -4.47800  27.98000 1.000 17.44934 ? 106 LEU A CG  1 
ATOM   806  C  CD1 . LEU A 1 114 ? 0.08200   -3.38300  28.30800 1.000 14.97778 ? 106 LEU A CD1 1 
ATOM   807  C  CD2 . LEU A 1 114 ? 2.50300   -3.96000  28.12600 1.000 14.52755 ? 106 LEU A CD2 1 
ATOM   808  N  N   . SER A 1 115 ? 1.54600   -9.20900  29.08700 1.000 18.22539 ? 107 SER A N   1 
ATOM   809  C  CA  . SER A 1 115 ? 1.25100   -10.46200 29.82800 1.000 20.15216 ? 107 SER A CA  1 
ATOM   810  C  C   . SER A 1 115 ? 1.97900   -11.62800 29.15000 1.000 22.77646 ? 107 SER A C   1 
ATOM   811  O  O   . SER A 1 115 ? 2.35900   -11.49900 27.99100 1.000 22.51401 ? 107 SER A O   1 
ATOM   812  C  CB  . SER A 1 115 ? -0.24500  -10.71200 29.89800 1.000 19.58545 ? 107 SER A CB  1 
ATOM   813  O  OG  . SER A 1 115 ? -0.78400  -10.99200 28.62700 1.000 24.43304 ? 107 SER A OG  1 
ATOM   814  N  N   . GLY A 1 116 ? 2.22100   -12.70400 29.88200 1.000 24.19574 ? 108 GLY A N   1 
ATOM   815  C  CA  . GLY A 1 116 ? 2.82400   -13.90000 29.28500 1.000 20.79341 ? 108 GLY A CA  1 
ATOM   816  C  C   . GLY A 1 116 ? 4.32700   -13.87700 29.16100 1.000 21.00693 ? 108 GLY A C   1 
ATOM   817  O  O   . GLY A 1 116 ? 4.95200   -13.07400 29.82500 1.000 19.20793 ? 108 GLY A O   1 
ATOM   818  N  N   . ASP A 1 117 ? 4.86100   -14.76700 28.32900 1.000 23.00300 ? 109 ASP A N   1 
ATOM   819  C  CA  . ASP A 1 117 ? 6.32000   -14.94200 28.13100 1.000 20.49630 ? 109 ASP A CA  1 
ATOM   820  C  C   . ASP A 1 117 ? 6.98000   -13.70500 27.51500 1.000 23.76363 ? 109 ASP A C   1 
ATOM   821  O  O   . ASP A 1 117 ? 8.17400   -13.52400 27.73500 1.000 26.65403 ? 109 ASP A O   1 
ATOM   822  C  CB  . ASP A 1 117 ? 6.55000   -16.14100 27.21800 1.000 23.23156 ? 109 ASP A CB  1 
ATOM   823  C  CG  . ASP A 1 117 ? 6.14300   -17.47500 27.82700 1.000 36.48133 ? 109 ASP A CG  1 
ATOM   824  O  OD1 . ASP A 1 117 ? 6.18800   -17.59600 29.06200 1.000 25.21115 ? 109 ASP A OD1 1 
ATOM   825  O  OD2 . ASP A 1 117 ? 5.79100   -18.38400 27.05300 1.000 38.52311 ? 109 ASP A OD2 1 
ATOM   826  N  N   . HIS A 1 118 ? 6.23400   -12.94400 26.72600 1.000 18.82726 ? 110 HIS A N   1 
ATOM   827  C  CA  . HIS A 1 118 ? 6.80200   -11.74400 26.05900 1.000 21.93655 ? 110 HIS A CA  1 
ATOM   828  C  C   . HIS A 1 118 ? 6.47000   -10.47900 26.86600 1.000 18.82798 ? 110 HIS A C   1 
ATOM   829  O  O   . HIS A 1 118 ? 6.59500   -9.39400  26.33100 1.000 20.35268 ? 110 HIS A O   1 
ATOM   830  C  CB  . HIS A 1 118 ? 6.34900   -11.69000 24.59600 1.000 20.32230 ? 110 HIS A CB  1 
ATOM   831  C  CG  . HIS A 1 118 ? 6.92500   -12.77500 23.75400 1.000 23.69860 ? 110 HIS A CG  1 
ATOM   832  N  ND1 . HIS A 1 118 ? 6.75100   -12.81700 22.38800 1.000 20.05701 ? 110 HIS A ND1 1 
ATOM   833  C  CD2 . HIS A 1 118 ? 7.67800   -13.84600 24.07200 1.000 20.07285 ? 110 HIS A CD2 1 
ATOM   834  C  CE1 . HIS A 1 118 ? 7.36400   -13.87300 21.90600 1.000 24.57402 ? 110 HIS A CE1 1 
ATOM   835  N  NE2 . HIS A 1 118 ? 7.93900   -14.51900 22.91700 1.000 20.02123 ? 110 HIS A NE2 1 
HETATM 836  N  N   . CSO A 1 119 ? 6.04300   -10.65600 28.11100 1.000 18.04803 ? 111 CSO A N   1 
HETATM 837  C  CA  . CSO A 1 119 ? 5.71100   -9.50200  28.97600 1.000 15.42473 ? 111 CSO A CA  1 
HETATM 838  C  CB  . CSO A 1 119 ? 5.22500   -9.96700  30.31900 1.000 20.54663 ? 111 CSO A CB  1 
HETATM 839  S  SG  . CSO A 1 119 ? 4.63000   -8.62700  31.38100 1.000 20.98981 ? 111 CSO A SG  1 
HETATM 840  C  C   . CSO A 1 119 ? 6.92500   -8.58200  29.15200 1.000 15.39858 ? 111 CSO A C   1 
HETATM 841  O  O   . CSO A 1 119 ? 7.99000   -9.09800  29.47900 1.000 15.99564 ? 111 CSO A O   1 
HETATM 842  O  OD  . CSO A 1 119 ? 3.64300   -9.21500  32.56200 1.000 27.05781 ? 111 CSO A OD  1 
ATOM   843  N  N   . ILE A 1 120 ? 6.73600   -7.28200  28.93900 1.000 12.93271 ? 112 ILE A N   1 
ATOM   844  C  CA  . ILE A 1 120 ? 7.84000   -6.27800  29.05000 1.000 10.20212 ? 112 ILE A CA  1 
ATOM   845  C  C   . ILE A 1 120 ? 7.69700   -5.46100  30.35000 1.000 13.49804 ? 112 ILE A C   1 
ATOM   846  O  O   . ILE A 1 120 ? 8.51800   -4.59800  30.61300 1.000 13.09353 ? 112 ILE A O   1 
ATOM   847  C  CB  . ILE A 1 120 ? 7.84800   -5.37400  27.80500 1.000 12.41440 ? 112 ILE A CB  1 
ATOM   848  C  CG1 . ILE A 1 120 ? 6.57700   -4.52900  27.70300 1.000 11.89332 ? 112 ILE A CG1 1 
ATOM   849  C  CG2 . ILE A 1 120 ? 8.07900   -6.20000  26.55300 1.000 11.59961 ? 112 ILE A CG2 1 
ATOM   850  C  CD1 . ILE A 1 120 ? 6.57700   -3.55800  26.54800 1.000 14.29418 ? 112 ILE A CD1 1 
ATOM   851  N  N   . ILE A 1 121 ? 6.67600   -5.77300  31.13400 1.000 12.68055 ? 113 ILE A N   1 
ATOM   852  C  CA  . ILE A 1 121 ? 6.47500   -5.06300  32.42100 1.000 12.85415 ? 113 ILE A CA  1 
ATOM   853  C  C   . ILE A 1 121 ? 7.62600   -5.40300  33.37300 1.000 10.51082 ? 113 ILE A C   1 
ATOM   854  O  O   . ILE A 1 121 ? 7.99100   -6.55300  33.46700 1.000 14.20711 ? 113 ILE A O   1 
ATOM   855  C  CB  . ILE A 1 121 ? 5.07300   -5.34000  32.99700 1.000 11.47937 ? 113 ILE A CB  1 
ATOM   856  C  CG1 . ILE A 1 121 ? 4.01900   -4.62200  32.15700 1.000 11.10997 ? 113 ILE A CG1 1 
ATOM   857  C  CG2 . ILE A 1 121 ? 4.98300   -4.93700  34.45500 1.000 14.27772 ? 113 ILE A CG2 1 
ATOM   858  C  CD1 . ILE A 1 121 ? 2.61200   -4.87500  32.59400 1.000 19.62502 ? 113 ILE A CD1 1 
ATOM   859  N  N   . GLY A 1 122 ? 8.17500   -4.37700  34.00600 1.000 9.98611  ? 114 GLY A N   1 
ATOM   860  C  CA  . GLY A 1 122 ? 9.31700   -4.57000  34.91800 1.000 13.71175 ? 114 GLY A CA  1 
ATOM   861  C  C   . GLY A 1 122 ? 10.66000  -4.53100  34.18900 1.000 14.43023 ? 114 GLY A C   1 
ATOM   862  O  O   . GLY A 1 122 ? 11.69000  -4.75700  34.82800 1.000 12.32604 ? 114 GLY A O   1 
ATOM   863  N  N   . ARG A 1 123 ? 10.61500  -4.25100  32.89400 1.000 12.49544 ? 115 ARG A N   1 
ATOM   864  C  CA  . ARG A 1 123 ? 11.84900  -4.21600  32.07600 1.000 13.21240 ? 115 ARG A CA  1 
ATOM   865  C  C   . ARG A 1 123 ? 12.16500  -2.76900  31.68100 1.000 14.88139 ? 115 ARG A C   1 
ATOM   866  O  O   . ARG A 1 123 ? 11.39000  -1.88800  32.00500 1.000 15.49656 ? 115 ARG A O   1 
ATOM   867  C  CB  . ARG A 1 123 ? 11.72400  -5.18400  30.89300 1.000 11.15340 ? 115 ARG A CB  1 
ATOM   868  C  CG  . ARG A 1 123 ? 11.41700  -6.61500  31.30400 1.000 13.32018 ? 115 ARG A CG  1 
ATOM   869  C  CD  . ARG A 1 123 ? 11.60200  -7.63400  30.20200 1.000 18.49651 ? 115 ARG A CD  1 
ATOM   870  N  NE  . ARG A 1 123 ? 11.06000  -8.92900  30.57800 1.000 18.32208 ? 115 ARG A NE  1 
ATOM   871  C  CZ  . ARG A 1 123 ? 11.71800  -9.88200  31.22700 1.000 19.96275 ? 115 ARG A CZ  1 
ATOM   872  N  NH1 . ARG A 1 123 ? 12.97800  -9.71100  31.57900 1.000 20.13670 ? 115 ARG A NH1 1 
ATOM   873  N  NH2 . ARG A 1 123 ? 11.11300  -11.01900 31.50700 1.000 18.80414 ? 115 ARG A NH2 1 
ATOM   874  N  N   . THR A 1 124 ? 13.27500  -2.56600  30.98500 1.000 12.24538 ? 116 THR A N   1 
ATOM   875  C  CA  . THR A 1 124 ? 13.72300  -1.17700  30.72700 1.000 15.82778 ? 116 THR A CA  1 
ATOM   876  C  C   . THR A 1 124 ? 13.49800  -0.76900  29.27400 1.000 13.48219 ? 116 THR A C   1 
ATOM   877  O  O   . THR A 1 124 ? 13.82900  -1.54600  28.40400 1.000 16.08869 ? 116 THR A O   1 
ATOM   878  C  CB  . THR A 1 124 ? 15.20600  -0.98500  31.09500 1.000 18.08995 ? 116 THR A CB  1 
ATOM   879  O  OG1 . THR A 1 124 ? 15.38900  -1.21900  32.49000 1.000 16.88265 ? 116 THR A OG1 1 
ATOM   880  C  CG2 . THR A 1 124 ? 15.72600  0.39500   30.76200 1.000 17.33532 ? 116 THR A CG2 1 
ATOM   881  N  N   . LEU A 1 125 ? 12.90400  0.40300   29.08100 1.000 12.77123 ? 117 LEU A N   1 
ATOM   882  C  CA  . LEU A 1 125 ? 12.76700  0.96100   27.71700 1.000 9.99717  ? 117 LEU A CA  1 
ATOM   883  C  C   . LEU A 1 125 ? 13.90000  1.97500   27.56100 1.000 12.79843 ? 117 LEU A C   1 
ATOM   884  O  O   . LEU A 1 125 ? 14.10200  2.77300   28.47000 1.000 12.10830 ? 117 LEU A O   1 
ATOM   885  C  CB  . LEU A 1 125 ? 11.41700  1.65200   27.55000 1.000 10.52445 ? 117 LEU A CB  1 
ATOM   886  C  CG  . LEU A 1 125 ? 11.09700  2.21600   26.17400 1.000 11.81510 ? 117 LEU A CG  1 
ATOM   887  C  CD1 . LEU A 1 125 ? 10.91500  1.09400   25.16800 1.000 13.26007 ? 117 LEU A CD1 1 
ATOM   888  C  CD2 . LEU A 1 125 ? 9.84000   3.05900   26.25500 1.000 12.21830 ? 117 LEU A CD2 1 
ATOM   889  N  N   . VAL A 1 126 ? 14.54100  1.95000   26.40900 1.000 11.86289 ? 118 VAL A N   1 
ATOM   890  C  CA  . VAL A 1 126 ? 15.67800  2.86200   26.13600 1.000 8.84130  ? 118 VAL A CA  1 
ATOM   891  C  C   . VAL A 1 126 ? 15.53300  3.56400   24.78100 1.000 10.70660 ? 118 VAL A C   1 
ATOM   892  O  O   . VAL A 1 126 ? 15.13200  2.91600   23.82700 1.000 12.12561 ? 118 VAL A O   1 
ATOM   893  C  CB  . VAL A 1 126 ? 17.01400  2.09200   26.18100 1.000 12.61882 ? 118 VAL A CB  1 
ATOM   894  C  CG1 . VAL A 1 126 ? 18.19200  2.99000   25.86400 1.000 15.29860 ? 118 VAL A CG1 1 
ATOM   895  C  CG2 . VAL A 1 126 ? 17.22900  1.38500   27.50600 1.000 15.74799 ? 118 VAL A CG2 1 
ATOM   896  N  N   . VAL A 1 127 ? 15.89500  4.84500   24.76100 1.000 10.27340 ? 119 VAL A N   1 
ATOM   897  C  CA  . VAL A 1 127 ? 15.97000  5.59700   23.48000 1.000 11.29666 ? 119 VAL A CA  1 
ATOM   898  C  C   . VAL A 1 127 ? 17.46000  5.87700   23.27100 1.000 11.53659 ? 119 VAL A C   1 
ATOM   899  O  O   . VAL A 1 127 ? 18.11000  6.31800   24.21900 1.000 13.14967 ? 119 VAL A O   1 
ATOM   900  C  CB  . VAL A 1 127 ? 15.14200  6.89400   23.45000 1.000 11.81272 ? 119 VAL A CB  1 
ATOM   901  C  CG1 . VAL A 1 127 ? 15.47500  7.85800   24.57100 1.000 12.31621 ? 119 VAL A CG1 1 
ATOM   902  C  CG2 . VAL A 1 127 ? 15.18000  7.57400   22.09200 1.000 11.81654 ? 119 VAL A CG2 1 
ATOM   903  N  N   . HIS A 1 128 ? 17.95900  5.61300   22.07800 1.000 11.59390 ? 120 HIS A N   1 
ATOM   904  C  CA  . HIS A 1 128 ? 19.42000  5.70800   21.85800 1.000 14.36277 ? 120 HIS A CA  1 
ATOM   905  C  C   . HIS A 1 128 ? 19.86500  6.95800   21.10400 1.000 15.07775 ? 120 HIS A C   1 
ATOM   906  O  O   . HIS A 1 128 ? 19.03100  7.63100   20.53300 1.000 13.91254 ? 120 HIS A O   1 
ATOM   907  C  CB  . HIS A 1 128 ? 19.93600  4.45700   21.14100 1.000 15.34010 ? 120 HIS A CB  1 
ATOM   908  C  CG  . HIS A 1 128 ? 19.89600  3.21600   21.95700 1.000 13.97486 ? 120 HIS A CG  1 
ATOM   909  N  ND1 . HIS A 1 128 ? 21.00300  2.73900   22.61000 1.000 18.78677 ? 120 HIS A ND1 1 
ATOM   910  C  CD2 . HIS A 1 128 ? 18.90100  2.33900   22.20300 1.000 16.11524 ? 120 HIS A CD2 1 
ATOM   911  C  CE1 . HIS A 1 128 ? 20.69500  1.62500   23.23500 1.000 19.91415 ? 120 HIS A CE1 1 
ATOM   912  N  NE2 . HIS A 1 128 ? 19.40900  1.36200   23.00800 1.000 21.29491 ? 120 HIS A NE2 1 
ATOM   913  N  N   . GLU A 1 129 ? 21.17600  7.19800   21.11300 1.000 13.07914 ? 121 GLU A N   1 
ATOM   914  C  CA  . GLU A 1 129 ? 21.81300  8.34100   20.44400 1.000 15.32766 ? 121 GLU A CA  1 
ATOM   915  C  C   . GLU A 1 129 ? 21.67200  8.27200   18.92900 1.000 16.37677 ? 121 GLU A C   1 
ATOM   916  O  O   . GLU A 1 129 ? 21.51300  9.31300   18.29500 1.000 16.01666 ? 121 GLU A O   1 
ATOM   917  C  CB  . GLU A 1 129 ? 23.30700  8.14100   20.71300 1.000 17.26203 ? 121 GLU A CB  1 
ATOM   918  C  CG  . GLU A 1 129 ? 24.18300  9.34600   20.47500 1.000 27.90691 ? 121 GLU A CG  1 
ATOM   919  C  CD  . GLU A 1 129 ? 25.64800  9.01700   20.70100 1.000 39.06277 ? 121 GLU A CD  1 
ATOM   920  O  OE1 . GLU A 1 129 ? 26.00800  7.81700   20.62200 1.000 32.72516 ? 121 GLU A OE1 1 
ATOM   921  O  OE2 . GLU A 1 129 ? 26.42200  9.95400   20.95200 1.000 40.52452 ? 121 GLU A OE2 1 
ATOM   922  N  N   . LYS A 1 130 ? 21.77500  7.06500   18.40300 1.000 13.52292 ? 122 LYS A N   1 
ATOM   923  C  CA  . LYS A 1 130 ? 21.82600  6.90300   16.94700 1.000 16.71044 ? 122 LYS A CA  1 
ATOM   924  C  C   . LYS A 1 130 ? 20.71700  5.99000   16.44300 1.000 13.18704 ? 122 LYS A C   1 
ATOM   925  O  O   . LYS A 1 130 ? 20.06700  5.32200   17.22300 1.000 15.80720 ? 122 LYS A O   1 
ATOM   926  C  CB  . LYS A 1 130 ? 23.15800  6.25600   16.53600 1.000 15.36784 ? 122 LYS A CB  1 
ATOM   927  C  CG  . LYS A 1 130 ? 24.42900  6.88000   17.09100 1.000 22.97223 ? 122 LYS A CG  1 
ATOM   928  C  CD  . LYS A 1 130 ? 25.67000  6.17400   16.59900 1.000 22.86604 ? 122 LYS A CD  1 
ATOM   929  C  CE  . LYS A 1 130 ? 26.94900  6.69000   17.22000 1.000 35.53320 ? 122 LYS A CE  1 
ATOM   930  N  NZ  . LYS A 1 130 ? 27.24400  8.07900   16.79500 1.000 40.52541 ? 122 LYS A NZ  1 
ATOM   931  N  N   . ALA A 1 131 ? 20.57800  5.98500   15.13200 1.000 13.43330 ? 123 ALA A N   1 
ATOM   932  C  CA  . ALA A 1 131 ? 19.55800  5.14200   14.50500 1.000 13.86892 ? 123 ALA A CA  1 
ATOM   933  C  C   . ALA A 1 131 ? 19.87300  3.66400   14.68700 1.000 15.16450 ? 123 ALA A C   1 
ATOM   934  O  O   . ALA A 1 131 ? 21.04400  3.30000   14.70400 1.000 13.05205 ? 123 ALA A O   1 
ATOM   935  C  CB  . ALA A 1 131 ? 19.48000  5.45400   13.04600 1.000 15.44545 ? 123 ALA A CB  1 
ATOM   936  N  N   . ASP A 1 132 ? 18.82400  2.86500   14.76800 1.000 11.38251 ? 124 ASP A N   1 
ATOM   937  C  CA  . ASP A 1 132 ? 19.00000  1.40600   14.78600 1.000 14.22745 ? 124 ASP A CA  1 
ATOM   938  C  C   . ASP A 1 132 ? 19.09100  0.97000   13.31200 1.000 14.65552 ? 124 ASP A C   1 
ATOM   939  O  O   . ASP A 1 132 ? 18.20100  1.30600   12.55600 1.000 14.16794 ? 124 ASP A O   1 
ATOM   940  C  CB  . ASP A 1 132 ? 17.86200  0.76100   15.57800 1.000 12.39135 ? 124 ASP A CB  1 
ATOM   941  C  CG  . ASP A 1 132 ? 17.84900  -0.75700  15.58300 1.000 17.28644 ? 124 ASP A CG  1 
ATOM   942  O  OD1 . ASP A 1 132 ? 18.69200  -1.36500  14.91100 1.000 14.63703 ? 124 ASP A OD1 1 
ATOM   943  O  OD2 . ASP A 1 132 ? 16.98900  -1.31000  16.26500 1.000 18.73298 ? 124 ASP A OD2 1 
ATOM   944  N  N   . ASP A 1 133 ? 20.15000  0.25900   12.95500 1.000 14.02237 ? 125 ASP A N   1 
ATOM   945  C  CA  . ASP A 1 133 ? 20.36400  -0.18600  11.55200 1.000 12.77388 ? 125 ASP A CA  1 
ATOM   946  C  C   . ASP A 1 133 ? 19.51600  -1.42900  11.23200 1.000 15.79340 ? 125 ASP A C   1 
ATOM   947  O  O   . ASP A 1 133 ? 19.67800  -1.96200  10.14400 1.000 16.60019 ? 125 ASP A O   1 
ATOM   948  C  CB  . ASP A 1 133 ? 21.85500  -0.36200  11.24400 1.000 16.20152 ? 125 ASP A CB  1 
ATOM   949  C  CG  . ASP A 1 133 ? 22.57100  -1.50700  11.94200 1.000 18.64784 ? 125 ASP A CG  1 
ATOM   950  O  OD1 . ASP A 1 133 ? 21.90200  -2.42300  12.42100 1.000 15.44328 ? 125 ASP A OD1 1 
ATOM   951  O  OD2 . ASP A 1 133 ? 23.80500  -1.47000  11.98400 1.000 17.38907 ? 125 ASP A OD2 1 
ATOM   952  N  N   . LEU A 1 134 ? 18.74100  -1.91800  12.19100 1.000 15.58559 ? 126 LEU A N   1 
ATOM   953  C  CA  . LEU A 1 134 ? 17.78100  -3.03900  11.96200 1.000 14.06258 ? 126 LEU A CA  1 
ATOM   954  C  C   . LEU A 1 134 ? 18.49900  -4.36600  11.64800 1.000 17.72791 ? 126 LEU A C   1 
ATOM   955  O  O   . LEU A 1 134 ? 17.85100  -5.25400  11.12400 1.000 19.25351 ? 126 LEU A O   1 
ATOM   956  C  CB  . LEU A 1 134 ? 16.79700  -2.64300  10.85800 1.000 16.36606 ? 126 LEU A CB  1 
ATOM   957  C  CG  . LEU A 1 134 ? 16.18000  -1.25200  11.00300 1.000 18.67955 ? 126 LEU A CG  1 
ATOM   958  C  CD1 . LEU A 1 134 ? 15.21800  -0.96000  9.86700  1.000 20.95692 ? 126 LEU A CD1 1 
ATOM   959  C  CD2 . LEU A 1 134 ? 15.49200  -1.09500  12.34800 1.000 16.25512 ? 126 LEU A CD2 1 
ATOM   960  N  N   . GLY A 1 135 ? 19.76200  -4.49600  12.04100 1.000 15.89838 ? 127 GLY A N   1 
ATOM   961  C  CA  . GLY A 1 135 ? 20.49800  -5.74900  11.81300 1.000 19.90410 ? 127 GLY A CA  1 
ATOM   962  C  C   . GLY A 1 135 ? 21.10700  -5.79800  10.43000 1.000 17.17813 ? 127 GLY A C   1 
ATOM   963  O  O   . GLY A 1 135 ? 21.66600  -6.83200  10.09000 1.000 23.77722 ? 127 GLY A O   1 
ATOM   964  N  N   . LYS A 1 136 ? 21.03700  -4.69100  9.70500  1.000 19.38333 ? 128 LYS A N   1 
ATOM   965  C  CA  . LYS A 1 136 ? 21.50000  -4.64600  8.29700  1.000 20.63371 ? 128 LYS A CA  1 
ATOM   966  C  C   . LYS A 1 136 ? 22.81800  -3.87700  8.16000  1.000 19.53083 ? 128 LYS A C   1 
ATOM   967  O  O   . LYS A 1 136 ? 23.15000  -3.50600  7.03800  1.000 22.67711 ? 128 LYS A O   1 
ATOM   968  C  CB  . LYS A 1 136 ? 20.35000  -4.04200  7.48900  1.000 22.59301 ? 128 LYS A CB  1 
ATOM   969  C  CG  . LYS A 1 136 ? 19.15200  -4.96000  7.30800  1.000 22.37111 ? 128 LYS A CG  1 
ATOM   970  C  CD  . LYS A 1 136 ? 17.94000  -4.26100  6.73600  1.000 29.21803 ? 128 LYS A CD  1 
ATOM   971  C  CE  . LYS A 1 136 ? 18.20300  -3.57400  5.41400  1.000 26.14694 ? 128 LYS A CE  1 
ATOM   972  N  NZ  . LYS A 1 136 ? 17.00500  -2.83900  4.94600  1.000 27.92129 ? 128 LYS A NZ  1 
ATOM   973  N  N   . GLY A 1 137 ? 23.55900  -3.69400  9.24900  1.000 18.18835 ? 129 GLY A N   1 
ATOM   974  C  CA  . GLY A 1 137 ? 24.79600  -2.89300  9.21000  1.000 20.13686 ? 129 GLY A CA  1 
ATOM   975  C  C   . GLY A 1 137 ? 26.02200  -3.64500  8.69600  1.000 21.52697 ? 129 GLY A C   1 
ATOM   976  O  O   . GLY A 1 137 ? 27.03400  -3.01400  8.46000  1.000 22.61918 ? 129 GLY A O   1 
ATOM   977  N  N   . GLY A 1 138 ? 25.90800  -4.95800  8.54900  1.000 21.14255 ? 130 GLY A N   1 
ATOM   978  C  CA  . GLY A 1 138 ? 27.03300  -5.74400  8.01900  1.000 20.87757 ? 130 GLY A CA  1 
ATOM   979  C  C   . GLY A 1 138 ? 28.17200  -5.84000  9.00100  1.000 22.60630 ? 130 GLY A C   1 
ATOM   980  O  O   . GLY A 1 138 ? 29.32300  -5.79500  8.56600  1.000 26.08663 ? 130 GLY A O   1 
ATOM   981  N  N   . ASN A 1 139 ? 27.84400  -5.98600  10.27800 1.000 23.19921 ? 131 ASN A N   1 
ATOM   982  C  CA  . ASN A 1 139 ? 28.88200  -6.19300  11.31600 1.000 23.22671 ? 131 ASN A CA  1 
ATOM   983  C  C   . ASN A 1 139 ? 28.26900  -6.91900  12.51500 1.000 23.60008 ? 131 ASN A C   1 
ATOM   984  O  O   . ASN A 1 139 ? 27.05600  -7.04000  12.58400 1.000 27.29901 ? 131 ASN A O   1 
ATOM   985  C  CB  . ASN A 1 139 ? 29.62200  -4.91300  11.68700 1.000 22.76037 ? 131 ASN A CB  1 
ATOM   986  C  CG  . ASN A 1 139 ? 28.70200  -3.78600  12.09900 1.000 28.62940 ? 131 ASN A CG  1 
ATOM   987  O  OD1 . ASN A 1 139 ? 27.83200  -3.97100  12.93900 1.000 27.22427 ? 131 ASN A OD1 1 
ATOM   988  N  ND2 . ASN A 1 139 ? 28.89600  -2.61700  11.51700 1.000 23.51663 ? 131 ASN A ND2 1 
ATOM   989  N  N   . GLU A 1 140 ? 29.11600  -7.36100  13.42900 1.000 32.11287 ? 132 GLU A N   1 
ATOM   990  C  CA  . GLU A 1 140 ? 28.65200  -8.18300  14.57700 1.000 31.94179 ? 132 GLU A CA  1 
ATOM   991  C  C   . GLU A 1 140 ? 27.72800  -7.36300  15.47700 1.000 24.08793 ? 132 GLU A C   1 
ATOM   992  O  O   . GLU A 1 140 ? 26.68200  -7.85700  15.82500 1.000 27.22130 ? 132 GLU A O   1 
ATOM   993  C  CB  . GLU A 1 140 ? 29.88000  -8.72400  15.32200 1.000 37.10490 ? 132 GLU A CB  1 
ATOM   994  C  CG  . GLU A 1 140 ? 29.54700  -9.53300  16.56500 1.000 44.81865 ? 132 GLU A CG  1 
ATOM   995  C  CD  . GLU A 1 140 ? 30.72300  -10.04500 17.38600 1.000 56.54266 ? 132 GLU A CD  1 
ATOM   996  O  OE1 . GLU A 1 140 ? 31.87400  -9.65700  17.09600 1.000 47.26042 ? 132 GLU A OE1 1 
ATOM   997  O  OE2 . GLU A 1 140 ? 30.48200  -10.84000 18.32000 1.000 55.96686 ? 132 GLU A OE2 1 
ATOM   998  N  N   . GLU A 1 141 ? 28.12500  -6.14100  15.79300 1.000 27.82641 ? 133 GLU A N   1 
ATOM   999  C  CA  . GLU A 1 141 ? 27.30700  -5.27600  16.67700 1.000 25.82898 ? 133 GLU A CA  1 
ATOM   1000 C  C   . GLU A 1 141 ? 25.90600  -5.07100  16.08500 1.000 25.20034 ? 133 GLU A C   1 
ATOM   1001 O  O   . GLU A 1 141 ? 24.97000  -4.97200  16.85300 1.000 22.41537 ? 133 GLU A O   1 
ATOM   1002 C  CB  . GLU A 1 141 ? 27.98000  -3.92800  16.87800 1.000 28.15435 ? 133 GLU A CB  1 
ATOM   1003 C  CG  . GLU A 1 141 ? 27.56000  -3.24000  18.15800 1.000 31.14211 ? 133 GLU A CG  1 
ATOM   1004 C  CD  . GLU A 1 141 ? 27.72200  -4.10900  19.39300 1.000 38.66563 ? 133 GLU A CD  1 
ATOM   1005 O  OE1 . GLU A 1 141 ? 28.76700  -4.76700  19.52400 1.000 42.19162 ? 133 GLU A OE1 1 
ATOM   1006 O  OE2 . GLU A 1 141 ? 26.79700  -4.13400  20.21100 1.000 43.19815 ? 133 GLU A OE2 1 
ATOM   1007 N  N   . SER A 1 142 ? 25.80600  -5.00500  14.75600 1.000 19.98091 ? 134 SER A N   1 
ATOM   1008 C  CA  . SER A 1 142 ? 24.48900  -4.83200  14.10100 1.000 21.87953 ? 134 SER A CA  1 
ATOM   1009 C  C   . SER A 1 142 ? 23.58200  -5.99800  14.48800 1.000 20.68169 ? 134 SER A C   1 
ATOM   1010 O  O   . SER A 1 142 ? 22.40300  -5.77300  14.71200 1.000 17.67059 ? 134 SER A O   1 
ATOM   1011 C  CB  . SER A 1 142 ? 24.63400  -4.71600  12.60900 1.000 16.43651 ? 134 SER A CB  1 
ATOM   1012 O  OG  . SER A 1 142 ? 23.37900  -4.56500  11.98300 1.000 24.01640 ? 134 SER A OG  1 
ATOM   1013 N  N   . THR A 1 143 ? 24.15400  -7.19300  14.61100 1.000 20.41387 ? 135 THR A N   1 
ATOM   1014 C  CA  . THR A 1 143 ? 23.35200  -8.41700  14.89700 1.000 20.71375 ? 135 THR A CA  1 
ATOM   1015 C  C   . THR A 1 143 ? 22.92400  -8.48500  16.37000 1.000 20.30723 ? 135 THR A C   1 
ATOM   1016 O  O   . THR A 1 143 ? 22.19900  -9.39700  16.70900 1.000 18.44294 ? 135 THR A O   1 
ATOM   1017 C  CB  . THR A 1 143 ? 24.14400  -9.68300  14.53700 1.000 23.67255 ? 135 THR A CB  1 
ATOM   1018 O  OG1 . THR A 1 143 ? 25.25700  -9.83500  15.41600 1.000 26.25569 ? 135 THR A OG1 1 
ATOM   1019 C  CG2 . THR A 1 143 ? 24.62400  -9.66500  13.10200 1.000 21.37629 ? 135 THR A CG2 1 
ATOM   1020 N  N   . LYS A 1 144 ? 23.40000  -7.54800  17.18600 1.000 21.33067 ? 136 LYS A N   1 
ATOM   1021 C  CA  . LYS A 1 144 ? 23.06900  -7.54500  18.63200 1.000 22.55420 ? 136 LYS A CA  1 
ATOM   1022 C  C   . LYS A 1 144 ? 22.31100  -6.26500  19.04500 1.000 23.58212 ? 136 LYS A C   1 
ATOM   1023 O  O   . LYS A 1 144 ? 21.25800  -6.39800  19.65700 1.000 21.23309 ? 136 LYS A O   1 
ATOM   1024 C  CB  . LYS A 1 144 ? 24.36200  -7.65700  19.44700 1.000 25.07367 ? 136 LYS A CB  1 
ATOM   1025 C  CG  . LYS A 1 144 ? 25.43700  -8.58200  18.89600 1.000 29.94094 ? 136 LYS A CG  1 
ATOM   1026 C  CD  . LYS A 1 144 ? 26.51100  -8.92700  19.90300 1.000 31.00792 ? 136 LYS A CD  1 
ATOM   1027 C  CE  . LYS A 1 144 ? 26.95400  -7.74800  20.73900 1.000 36.52537 ? 136 LYS A CE  1 
ATOM   1028 N  NZ  . LYS A 1 144 ? 27.82000  -8.16800  21.86500 1.000 34.05888 ? 136 LYS A NZ  1 
ATOM   1029 N  N   . THR A 1 145 ? 22.83600  -5.08400  18.69800 1.000 21.09575 ? 137 THR A N   1 
ATOM   1030 C  CA  . THR A 1 145 ? 22.25900  -3.78400  19.14900 1.000 22.41556 ? 137 THR A CA  1 
ATOM   1031 C  C   . THR A 1 145 ? 21.78100  -2.88200  18.00200 1.000 18.92566 ? 137 THR A C   1 
ATOM   1032 O  O   . THR A 1 145 ? 21.15000  -1.87500  18.28500 1.000 20.46235 ? 137 THR A O   1 
ATOM   1033 C  CB  . THR A 1 145 ? 23.32000  -3.01700  19.94400 1.000 23.58210 ? 137 THR A CB  1 
ATOM   1034 O  OG1 . THR A 1 145 ? 24.46100  -2.83400  19.10800 1.000 27.10779 ? 137 THR A OG1 1 
ATOM   1035 C  CG2 . THR A 1 145 ? 23.70100  -3.73100  21.22100 1.000 23.75791 ? 137 THR A CG2 1 
ATOM   1036 N  N   . GLY A 1 146 ? 22.11800  -3.21900  16.76200 1.000 18.52491 ? 138 GLY A N   1 
ATOM   1037 C  CA  . GLY A 1 146 ? 21.75100  -2.34300  15.63600 1.000 17.48424 ? 138 GLY A CA  1 
ATOM   1038 C  C   . GLY A 1 146 ? 22.62900  -1.10600  15.56700 1.000 16.36675 ? 138 GLY A C   1 
ATOM   1039 O  O   . GLY A 1 146 ? 22.25600  -0.18400  14.84800 1.000 16.69892 ? 138 GLY A O   1 
ATOM   1040 N  N   . ASN A 1 147 ? 23.74500  -1.10000  16.29600 1.000 18.16516 ? 139 ASN A N   1 
ATOM   1041 C  CA  . ASN A 1 147 ? 24.70800  0.03400   16.28900 1.000 19.95759 ? 139 ASN A CA  1 
ATOM   1042 C  C   . ASN A 1 147 ? 24.02700  1.35600   16.69600 1.000 17.12293 ? 139 ASN A C   1 
ATOM   1043 O  O   . ASN A 1 147 ? 24.41200  2.39800   16.17500 1.000 15.67597 ? 139 ASN A O   1 
ATOM   1044 C  CB  . ASN A 1 147 ? 25.38200  0.15500   14.93100 1.000 20.45137 ? 139 ASN A CB  1 
ATOM   1045 C  CG  . ASN A 1 147 ? 26.39000  -0.94000  14.65900 1.000 24.62389 ? 139 ASN A CG  1 
ATOM   1046 O  OD1 . ASN A 1 147 ? 27.39900  -1.04100  15.34300 1.000 21.56670 ? 139 ASN A OD1 1 
ATOM   1047 N  ND2 . ASN A 1 147 ? 26.13300  -1.74300  13.64300 1.000 19.38612 ? 139 ASN A ND2 1 
ATOM   1048 N  N   . ALA A 1 148 ? 23.03900  1.28800   17.59100 1.000 15.32316 ? 140 ALA A N   1 
ATOM   1049 C  CA  . ALA A 1 148 ? 22.26700  2.50000   17.97200 1.000 15.42270 ? 140 ALA A CA  1 
ATOM   1050 C  C   . ALA A 1 148 ? 23.04300  3.37000   18.97200 1.000 18.01714 ? 140 ALA A C   1 
ATOM   1051 O  O   . ALA A 1 148 ? 22.56100  4.43200   19.33200 1.000 16.70758 ? 140 ALA A O   1 
ATOM   1052 C  CB  . ALA A 1 148 ? 20.92900  2.09900   18.50800 1.000 14.90776 ? 140 ALA A CB  1 
ATOM   1053 N  N   . GLY A 1 149 ? 24.19000  2.88400   19.41700 1.000 20.95116 ? 141 GLY A N   1 
ATOM   1054 C  CA  . GLY A 1 149 ? 25.03700  3.71300   20.27400 1.000 19.74148 ? 141 GLY A CA  1 
ATOM   1055 C  C   . GLY A 1 149 ? 24.56100  3.86000   21.70500 1.000 20.34896 ? 141 GLY A C   1 
ATOM   1056 O  O   . GLY A 1 149 ? 23.86700  2.97500   22.19600 1.000 20.95324 ? 141 GLY A O   1 
ATOM   1057 N  N   . SER A 1 150 ? 24.92500  4.97200   22.32400 1.000 19.00063 ? 142 SER A N   1 
ATOM   1058 C  CA  . SER A 1 150 ? 24.66000  5.18800   23.75600 1.000 18.27280 ? 142 SER A CA  1 
ATOM   1059 C  C   . SER A 1 150 ? 23.18200  5.36300   24.10100 1.000 17.72862 ? 142 SER A C   1 
ATOM   1060 O  O   . SER A 1 150 ? 22.40400  5.73700   23.23200 1.000 18.75213 ? 142 SER A O   1 
ATOM   1061 C  CB  . SER A 1 150 ? 25.45100  6.39100   24.23100 1.000 23.12594 ? 142 SER A CB  1 
ATOM   1062 O  OG  . SER A 1 150 ? 24.85000  7.60800   23.83400 1.000 29.00729 ? 142 SER A OG  1 
ATOM   1063 N  N   . ARG A 1 151 ? 22.86200  5.15600   25.37200 1.000 19.25202 ? 143 ARG A N   1 
ATOM   1064 C  CA  . ARG A 1 151 ? 21.49100  5.38900   25.86700 1.000 20.21581 ? 143 ARG A CA  1 
ATOM   1065 C  C   . ARG A 1 151 ? 21.38900  6.86600   26.19800 1.000 19.88643 ? 143 ARG A C   1 
ATOM   1066 O  O   . ARG A 1 151 ? 22.25700  7.35100   26.91400 1.000 24.10391 ? 143 ARG A O   1 
ATOM   1067 C  CB  . ARG A 1 151 ? 21.23700  4.57600   27.13400 1.000 23.07455 ? 143 ARG A CB  1 
ATOM   1068 C  CG  . ARG A 1 151 ? 21.87500  3.19700   27.13800 1.000 32.48935 ? 143 ARG A CG  1 
ATOM   1069 C  CD  . ARG A 1 151 ? 20.95900  2.21500   27.84300 1.000 34.49447 ? 143 ARG A CD  1 
ATOM   1070 N  NE  . ARG A 1 151 ? 21.47700  0.89100   28.15000 1.000 44.42504 ? 143 ARG A NE  1 
ATOM   1071 C  CZ  . ARG A 1 151 ? 21.94400  0.00900   27.27300 1.000 41.89226 ? 143 ARG A CZ  1 
ATOM   1072 N  NH1 . ARG A 1 151 ? 22.00800  0.30200   25.98700 1.000 35.78121 ? 143 ARG A NH1 1 
ATOM   1073 N  NH2 . ARG A 1 151 ? 22.36900  -1.16700  27.69400 1.000 43.37644 ? 143 ARG A NH2 1 
ATOM   1074 N  N   . LEU A 1 152 ? 20.37500  7.53700   25.66900 1.000 14.16537 ? 144 LEU A N   1 
ATOM   1075 C  CA  . LEU A 1 152 ? 20.16700  8.96900   25.98900 1.000 14.30272 ? 144 LEU A CA  1 
ATOM   1076 C  C   . LEU A 1 152 ? 19.16900  9.07200   27.14400 1.000 15.86639 ? 144 LEU A C   1 
ATOM   1077 O  O   . LEU A 1 152 ? 19.25500  10.00400  27.93500 1.000 15.38355 ? 144 LEU A O   1 
ATOM   1078 C  CB  . LEU A 1 152 ? 19.63800  9.67300   24.74100 1.000 12.85780 ? 144 LEU A CB  1 
ATOM   1079 C  CG  . LEU A 1 152 ? 20.63200  9.87100   23.60500 1.000 18.11609 ? 144 LEU A CG  1 
ATOM   1080 C  CD1 . LEU A 1 152 ? 19.96500  10.61000  22.46000 1.000 20.67425 ? 144 LEU A CD1 1 
ATOM   1081 C  CD2 . LEU A 1 152 ? 21.85000  10.63300  24.08500 1.000 22.80941 ? 144 LEU A CD2 1 
ATOM   1082 N  N   . ALA A 1 153 ? 18.21500  8.15200   27.15500 1.000 15.38611 ? 145 ALA A N   1 
ATOM   1083 C  CA  . ALA A 1 153 ? 17.23400  8.12400   28.25200 1.000 11.51651 ? 145 ALA A CA  1 
ATOM   1084 C  C   . ALA A 1 153 ? 16.66000  6.71600   28.42600 1.000 14.03272 ? 145 ALA A C   1 
ATOM   1085 O  O   . ALA A 1 153 ? 16.59700  5.96000   27.46100 1.000 10.82610 ? 145 ALA A O   1 
ATOM   1086 C  CB  . ALA A 1 153 ? 16.15200  9.12300   27.97900 1.000 11.63659 ? 145 ALA A CB  1 
ATOM   1087 N  N   . ASP A 1 154 ? 16.26100  6.42800   29.65500 1.000 12.60482 ? 146 ASP A N   1 
ATOM   1088 C  CA  . ASP A 1 154 ? 15.65900  5.11100   29.93700 1.000 14.97698 ? 146 ASP A CA  1 
ATOM   1089 C  C   . ASP A 1 154 ? 14.68500  5.19200   31.11600 1.000 13.93336 ? 146 ASP A C   1 
ATOM   1090 O  O   . ASP A 1 154 ? 14.55100  6.24100   31.72000 1.000 14.96171 ? 146 ASP A O   1 
ATOM   1091 C  CB  . ASP A 1 154 ? 16.71500  4.03100   30.14600 1.000 14.90663 ? 146 ASP A CB  1 
ATOM   1092 C  CG  . ASP A 1 154 ? 17.68200  4.26400   31.29300 1.000 24.02636 ? 146 ASP A CG  1 
ATOM   1093 O  OD1 . ASP A 1 154 ? 17.40500  5.11800   32.14000 1.000 24.98141 ? 146 ASP A OD1 1 
ATOM   1094 O  OD2 . ASP A 1 154 ? 18.71200  3.57800   31.31900 1.000 27.15708 ? 146 ASP A OD2 1 
ATOM   1095 N  N   . GLY A 1 155 ? 14.02600  4.07900   31.36500 1.000 16.56188 ? 147 GLY A N   1 
ATOM   1096 C  CA  . GLY A 1 155 ? 13.08300  4.01300   32.46300 1.000 13.55113 ? 147 GLY A CA  1 
ATOM   1097 C  C   . GLY A 1 155 ? 12.50900  2.61600   32.53400 1.000 13.46424 ? 147 GLY A C   1 
ATOM   1098 O  O   . GLY A 1 155 ? 12.58500  1.84000   31.57700 1.000 16.28121 ? 147 GLY A O   1 
ATOM   1099 N  N   . VAL A 1 156 ? 11.93500  2.30900   33.68600 1.000 11.68766 ? 148 VAL A N   1 
ATOM   1100 C  CA  . VAL A 1 156 ? 11.36200  0.99100   33.93000 1.000 10.48295 ? 148 VAL A CA  1 
ATOM   1101 C  C   . VAL A 1 156 ? 9.87500   1.02600   33.59500 1.000 13.02854 ? 148 VAL A C   1 
ATOM   1102 O  O   . VAL A 1 156 ? 9.16600   1.97600   33.94900 1.000 13.77782 ? 148 VAL A O   1 
ATOM   1103 C  CB  . VAL A 1 156 ? 11.60900  0.55700   35.38600 1.000 11.50005 ? 148 VAL A CB  1 
ATOM   1104 C  CG1 . VAL A 1 156 ? 11.09800  -0.86000  35.62100 1.000 13.25451 ? 148 VAL A CG1 1 
ATOM   1105 C  CG2 . VAL A 1 156 ? 13.09200  0.65000   35.70000 1.000 14.14535 ? 148 VAL A CG2 1 
ATOM   1106 N  N   . ILE A 1 157 ? 9.40300   -0.00500  32.89700 1.000 12.31378 ? 149 ILE A N   1 
ATOM   1107 C  CA  . ILE A 1 157 ? 8.01800   -0.05500  32.43600 1.000 9.79691  ? 149 ILE A CA  1 
ATOM   1108 C  C   . ILE A 1 157 ? 7.12500   -0.51700  33.58200 1.000 10.90931 ? 149 ILE A C   1 
ATOM   1109 O  O   . ILE A 1 157 ? 7.26800   -1.63600  34.08300 1.000 12.02476 ? 149 ILE A O   1 
ATOM   1110 C  CB  . ILE A 1 157 ? 7.87600   -0.97800  31.21800 1.000 11.89908 ? 149 ILE A CB  1 
ATOM   1111 C  CG1 . ILE A 1 157 ? 8.72000   -0.45400  30.05200 1.000 10.98925 ? 149 ILE A CG1 1 
ATOM   1112 C  CG2 . ILE A 1 157 ? 6.41200   -1.10500  30.81500 1.000 13.54931 ? 149 ILE A CG2 1 
ATOM   1113 C  CD1 . ILE A 1 157 ? 8.98600   -1.49100  28.96700 1.000 10.84333 ? 149 ILE A CD1 1 
ATOM   1114 N  N   . GLY A 1 158 ? 6.19100   0.34000   33.98900 1.000 12.25891 ? 150 GLY A N   1 
ATOM   1115 C  CA  . GLY A 1 158 ? 5.32900   0.02900   35.11200 1.000 12.38624 ? 150 GLY A CA  1 
ATOM   1116 C  C   . GLY A 1 158 ? 3.87300   -0.13600  34.73200 1.000 12.09276 ? 150 GLY A C   1 
ATOM   1117 O  O   . GLY A 1 158 ? 3.43600   0.35500   33.69000 1.000 12.18856 ? 150 GLY A O   1 
ATOM   1118 N  N   . ILE A 1 159 ? 3.11600   -0.82300  35.58700 1.000 11.22810 ? 151 ILE A N   1 
ATOM   1119 C  CA  . ILE A 1 159 ? 1.69000   -1.02900  35.36800 1.000 13.75996 ? 151 ILE A CA  1 
ATOM   1120 C  C   . ILE A 1 159 ? 0.95200   0.29300   35.53300 1.000 14.29154 ? 151 ILE A C   1 
ATOM   1121 O  O   . ILE A 1 159 ? 1.18500   1.03600   36.49600 1.000 15.30539 ? 151 ILE A O   1 
ATOM   1122 C  CB  . ILE A 1 159 ? 1.15800   -2.09100  36.34300 1.000 13.17522 ? 151 ILE A CB  1 
ATOM   1123 C  CG1 . ILE A 1 159 ? 1.80800   -3.44700  36.05600 1.000 12.26326 ? 151 ILE A CG1 1 
ATOM   1124 C  CG2 . ILE A 1 159 ? -0.36500  -2.19500  36.27200 1.000 17.31594 ? 151 ILE A CG2 1 
ATOM   1125 C  CD1 . ILE A 1 159 ? 1.55200   -4.49000  37.13300 1.000 16.70817 ? 151 ILE A CD1 1 
ATOM   1126 N  N   . ALA A 1 160 ? 0.06200   0.59700   34.58300 1.000 16.23945 ? 152 ALA A N   1 
ATOM   1127 C  CA  . ALA A 1 160 ? -0.78800  1.77900   34.64200 1.000 17.11473 ? 152 ALA A CA  1 
ATOM   1128 C  C   . ALA A 1 160 ? -2.27300  1.46000   34.75200 1.000 17.49231 ? 152 ALA A C   1 
ATOM   1129 O  O   . ALA A 1 160 ? -3.03100  2.30600   35.24200 1.000 22.58826 ? 152 ALA A O   1 
ATOM   1130 C  CB  . ALA A 1 160 ? -0.56500  2.66300   33.40300 1.000 17.17906 ? 152 ALA A CB  1 
ATOM   1131 N  N   . GLN A 1 161 ? -2.70500  0.28100   34.31400 1.000 18.32372 ? 153 GLN A N   1 
ATOM   1132 C  CA  . GLN A 1 161 ? -4.09400  -0.15100  34.46000 1.000 31.24804 ? 153 GLN A CA  1 
ATOM   1133 C  C   . GLN A 1 161 ? -4.21000  -1.67000  34.32400 1.000 31.29386 ? 153 GLN A C   1 
ATOM   1134 O  O   . GLN A 1 161 ? -5.07600  -2.27900  34.95600 1.000 33.07536 ? 153 GLN A O   1 
ATOM   1135 C  CB  . GLN A 1 161 ? -4.98700  0.54700   33.43000 1.000 31.02115 ? 153 GLN A CB  1 
ATOM   1136 C  CG  . GLN A 1 161 ? -6.47600  0.47100   33.72700 1.000 34.05376 ? 153 GLN A CG  1 
ATOM   1137 C  CD  . GLN A 1 161 ? -7.28300  1.44900   32.89100 1.000 42.73439 ? 153 GLN A CD  1 
ATOM   1138 O  OE1 . GLN A 1 161 ? -7.96000  1.05700   31.93900 1.000 43.61655 ? 153 GLN A OE1 1 
ATOM   1139 N  NE2 . GLN A 1 161 ? -7.21500  2.73200   33.24300 1.000 36.13571 ? 153 GLN A NE2 1 
ATOM   1140 O  OXT . GLN A 1 161 ? -3.44600  -2.32300  33.59600 1.000 22.56555 ? 153 GLN A OXT 1 
ATOM   1141 N  N   . ALA B 1 9   ? 10.49400  -15.20300 38.26400 1.000 39.49954 ? 1   ALA B N   1 
ATOM   1142 C  CA  . ALA B 1 9   ? 11.31100  -14.11000 38.78600 1.000 31.71948 ? 1   ALA B CA  1 
ATOM   1143 C  C   . ALA B 1 9   ? 11.72300  -14.37000 40.23200 1.000 26.77959 ? 1   ALA B C   1 
ATOM   1144 O  O   . ALA B 1 9   ? 10.89900  -14.73800 41.06500 1.000 32.49661 ? 1   ALA B O   1 
ATOM   1145 C  CB  . ALA B 1 9   ? 10.56300  -12.79100 38.68000 1.000 27.77962 ? 1   ALA B CB  1 
ATOM   1146 N  N   . THR B 1 10  ? 13.00600  -14.18000 40.53200 1.000 21.02848 ? 2   THR B N   1 
ATOM   1147 C  CA  . THR B 1 10  ? 13.50000  -14.35500 41.88700 1.000 20.05480 ? 2   THR B CA  1 
ATOM   1148 C  C   . THR B 1 10  ? 14.17100  -13.11400 42.45500 1.000 22.03323 ? 2   THR B C   1 
ATOM   1149 O  O   . THR B 1 10  ? 14.42800  -13.07600 43.66300 1.000 19.92963 ? 2   THR B O   1 
ATOM   1150 C  CB  . THR B 1 10  ? 14.49000  -15.53000 41.95300 1.000 20.11760 ? 2   THR B CB  1 
ATOM   1151 O  OG1 . THR B 1 10  ? 15.58300  -15.29000 41.05900 1.000 27.21703 ? 2   THR B OG1 1 
ATOM   1152 C  CG2 . THR B 1 10  ? 13.80400  -16.82400 41.55500 1.000 27.56839 ? 2   THR B CG2 1 
ATOM   1153 N  N   . LYS B 1 11  ? 14.45800  -12.10600 41.63300 1.000 15.65947 ? 3   LYS B N   1 
ATOM   1154 C  CA  . LYS B 1 11  ? 15.16000  -10.91000 42.07300 1.000 16.79055 ? 3   LYS B CA  1 
ATOM   1155 C  C   . LYS B 1 11  ? 14.51000  -9.68600  41.44600 1.000 14.59416 ? 3   LYS B C   1 
ATOM   1156 O  O   . LYS B 1 11  ? 14.10500  -9.72100  40.28100 1.000 18.27097 ? 3   LYS B O   1 
ATOM   1157 C  CB  . LYS B 1 11  ? 16.65000  -10.94800 41.68400 1.000 23.36595 ? 3   LYS B CB  1 
ATOM   1158 C  CG  . LYS B 1 11  ? 17.34900  -12.28200 41.93100 1.000 35.24608 ? 3   LYS B CG  1 
ATOM   1159 C  CD  . LYS B 1 11  ? 18.85900  -12.16500 41.72800 1.000 43.65803 ? 3   LYS B CD  1 
ATOM   1160 C  CE  . LYS B 1 11  ? 19.58200  -13.45900 42.09700 1.000 49.96684 ? 3   LYS B CE  1 
ATOM   1161 N  NZ  . LYS B 1 11  ? 19.81500  -14.35000 40.92300 1.000 48.45445 ? 3   LYS B NZ  1 
ATOM   1162 N  N   . ALA B 1 12  ? 14.42800  -8.60200  42.21500 1.000 14.67369 ? 4   ALA B N   1 
ATOM   1163 C  CA  . ALA B 1 12  ? 13.90200  -7.34000  41.71700 1.000 10.71625 ? 4   ALA B CA  1 
ATOM   1164 C  C   . ALA B 1 12  ? 14.70300  -6.19800  42.32300 1.000 13.03181 ? 4   ALA B C   1 
ATOM   1165 O  O   . ALA B 1 12  ? 15.42600  -6.37600  43.30600 1.000 13.91538 ? 4   ALA B O   1 
ATOM   1166 C  CB  . ALA B 1 12  ? 12.40700  -7.18100  42.03400 1.000 13.44140 ? 4   ALA B CB  1 
ATOM   1167 N  N   . VAL B 1 13  ? 14.57100  -5.01200  41.72900 1.000 11.36457 ? 5   VAL B N   1 
ATOM   1168 C  CA  . VAL B 1 13  ? 15.33300  -3.85200  42.17600 1.000 13.59497 ? 5   VAL B CA  1 
ATOM   1169 C  C   . VAL B 1 13  ? 14.52600  -2.59500  41.88500 1.000 12.56741 ? 5   VAL B C   1 
ATOM   1170 O  O   . VAL B 1 13  ? 13.75600  -2.54000  40.92300 1.000 15.51151 ? 5   VAL B O   1 
ATOM   1171 C  CB  . VAL B 1 13  ? 16.72700  -3.80200  41.50300 1.000 14.66139 ? 5   VAL B CB  1 
ATOM   1172 C  CG1 . VAL B 1 13  ? 16.58900  -3.57800  40.01100 1.000 17.66000 ? 5   VAL B CG1 1 
ATOM   1173 C  CG2 . VAL B 1 13  ? 17.59400  -2.72500  42.13000 1.000 17.38707 ? 5   VAL B CG2 1 
ATOM   1174 N  N   . CYS B 1 14  ? 14.69900  -1.58300  42.73200 1.000 14.08024 ? 6   CYS B N   1 
ATOM   1175 C  CA  . CYS B 1 14  ? 14.00000  -0.31500  42.57100 1.000 14.95452 ? 6   CYS B CA  1 
ATOM   1176 C  C   . CYS B 1 14  ? 14.93800  0.83700   42.89900 1.000 14.18447 ? 6   CYS B C   1 
ATOM   1177 O  O   . CYS B 1 14  ? 15.56500  0.85000   43.96200 1.000 13.09255 ? 6   CYS B O   1 
ATOM   1178 C  CB  . CYS B 1 14  ? 12.75800  -0.25800  43.46500 1.000 13.27117 ? 6   CYS B CB  1 
ATOM   1179 S  SG  . CYS B 1 14  ? 11.81200  1.27200   43.34300 1.000 16.15639 ? 6   CYS B SG  1 
ATOM   1180 N  N   . VAL B 1 15  ? 15.03700  1.79700   41.98800 1.000 15.12721 ? 7   VAL B N   1 
ATOM   1181 C  CA  . VAL B 1 15  ? 15.76000  3.03900   42.23400 1.000 15.98050 ? 7   VAL B CA  1 
ATOM   1182 C  C   . VAL B 1 15  ? 14.73800  4.09500   42.61900 1.000 14.44581 ? 7   VAL B C   1 
ATOM   1183 O  O   . VAL B 1 15  ? 13.82000  4.39500   41.84400 1.000 15.59412 ? 7   VAL B O   1 
ATOM   1184 C  CB  . VAL B 1 15  ? 16.57800  3.47900   41.01000 1.000 15.95329 ? 7   VAL B CB  1 
ATOM   1185 C  CG1 . VAL B 1 15  ? 17.24600  4.81300   41.28700 1.000 18.16900 ? 7   VAL B CG1 1 
ATOM   1186 C  CG2 . VAL B 1 15  ? 17.61900  2.42500   40.65600 1.000 17.73190 ? 7   VAL B CG2 1 
ATOM   1187 N  N   . LEU B 1 16  ? 14.88800  4.64900   43.81800 1.000 13.31134 ? 8   LEU B N   1 
ATOM   1188 C  CA  . LEU B 1 16  ? 13.97100  5.64200   44.35700 1.000 14.90566 ? 8   LEU B CA  1 
ATOM   1189 C  C   . LEU B 1 16  ? 14.52100  7.03600   44.07900 1.000 17.95378 ? 8   LEU B C   1 
ATOM   1190 O  O   . LEU B 1 16  ? 15.61700  7.37400   44.53600 1.000 15.30018 ? 8   LEU B O   1 
ATOM   1191 C  CB  . LEU B 1 16  ? 13.78300  5.43800   45.86000 1.000 17.53102 ? 8   LEU B CB  1 
ATOM   1192 C  CG  . LEU B 1 16  ? 13.14600  4.12400   46.31000 1.000 15.90795 ? 8   LEU B CG  1 
ATOM   1193 C  CD1 . LEU B 1 16  ? 13.34100  3.92800   47.80500 1.000 18.33508 ? 8   LEU B CD1 1 
ATOM   1194 C  CD2 . LEU B 1 16  ? 11.66700  4.12800   45.96200 1.000 13.02011 ? 8   LEU B CD2 1 
ATOM   1195 N  N   . LYS B 1 17  ? 13.76600  7.84000   43.33300 1.000 18.54758 ? 9   LYS B N   1 
ATOM   1196 C  CA  . LYS B 1 17  ? 14.15600  9.21800   43.07700 1.000 16.39380 ? 9   LYS B CA  1 
ATOM   1197 C  C   . LYS B 1 17  ? 12.92900  10.11500  43.15100 1.000 19.20952 ? 9   LYS B C   1 
ATOM   1198 O  O   . LYS B 1 17  ? 11.78800  9.65400   43.06600 1.000 18.65844 ? 9   LYS B O   1 
ATOM   1199 C  CB  . LYS B 1 17  ? 14.86000  9.36700   41.71700 1.000 22.63293 ? 9   LYS B CB  1 
ATOM   1200 C  CG  . LYS B 1 17  ? 16.19300  8.62300   41.63800 1.000 31.00095 ? 9   LYS B CG  1 
ATOM   1201 C  CD  . LYS B 1 17  ? 17.31900  9.46700   41.04000 1.000 40.67160 ? 9   LYS B CD  1 
ATOM   1202 C  CE  . LYS B 1 17  ? 17.16500  9.64600   39.53700 1.000 43.92875 ? 9   LYS B CE  1 
ATOM   1203 N  NZ  . LYS B 1 17  ? 18.41400  10.18000  38.92000 1.000 42.73691 ? 9   LYS B NZ  1 
ATOM   1204 N  N   . GLY B 1 18  ? 13.18100  11.40300  43.32600 1.000 18.19517 ? 10  GLY B N   1 
ATOM   1205 C  CA  . GLY B 1 18  ? 12.13000  12.39000  43.37800 1.000 20.92482 ? 10  GLY B CA  1 
ATOM   1206 C  C   . GLY B 1 18  ? 12.65600  13.74200  42.95200 1.000 25.09987 ? 10  GLY B C   1 
ATOM   1207 O  O   . GLY B 1 18  ? 13.73400  13.85300  42.36700 1.000 23.54923 ? 10  GLY B O   1 
ATOM   1208 N  N   . ASP B 1 19  ? 11.88200  14.77900  43.25400 1.000 29.99328 ? 11  ASP B N   1 
ATOM   1209 C  CA  . ASP B 1 19  ? 12.25700  16.14800  42.92900 1.000 30.76464 ? 11  ASP B CA  1 
ATOM   1210 C  C   . ASP B 1 19  ? 13.02300  16.82500  44.05600 1.000 30.54040 ? 11  ASP B C   1 
ATOM   1211 O  O   . ASP B 1 19  ? 13.27300  18.03300  43.98400 1.000 30.16443 ? 11  ASP B O   1 
ATOM   1212 C  CB  . ASP B 1 19  ? 11.01000  16.96100  42.58200 1.000 38.36146 ? 11  ASP B CB  1 
ATOM   1213 C  CG  . ASP B 1 19  ? 10.22800  16.35700  41.43400 1.000 41.36797 ? 11  ASP B CG  1 
ATOM   1214 O  OD1 . ASP B 1 19  ? 10.81700  16.16700  40.34700 1.000 51.02350 ? 11  ASP B OD1 1 
ATOM   1215 O  OD2 . ASP B 1 19  ? 9.03100   16.05600  41.62300 1.000 48.11854 ? 11  ASP B OD2 1 
ATOM   1216 N  N   . GLY B 1 20  ? 13.39400  16.07800  45.09300 1.000 25.85874 ? 12  GLY B N   1 
ATOM   1217 C  CA  . GLY B 1 20  ? 14.13100  16.62400  46.20300 1.000 23.16295 ? 12  GLY B CA  1 
ATOM   1218 C  C   . GLY B 1 20  ? 15.38500  15.83000  46.49400 1.000 20.10411 ? 12  GLY B C   1 
ATOM   1219 O  O   . GLY B 1 20  ? 15.96600  15.19300  45.61000 1.000 20.76071 ? 12  GLY B O   1 
ATOM   1220 N  N   . PRO B 1 21  ? 15.82100  15.84700  47.75600 1.000 18.97503 ? 13  PRO B N   1 
ATOM   1221 C  CA  . PRO B 1 21  ? 17.10000  15.21700  48.10900 1.000 18.59555 ? 13  PRO B CA  1 
ATOM   1222 C  C   . PRO B 1 21  ? 17.01900  13.72000  48.35500 1.000 20.36907 ? 13  PRO B C   1 
ATOM   1223 O  O   . PRO B 1 21  ? 18.06900  13.07700  48.47100 1.000 18.25274 ? 13  PRO B O   1 
ATOM   1224 C  CB  . PRO B 1 21  ? 17.50100  15.95400  49.39200 1.000 19.39118 ? 13  PRO B CB  1 
ATOM   1225 C  CG  . PRO B 1 21  ? 16.19600  16.32000  50.01800 1.000 25.98031 ? 13  PRO B CG  1 
ATOM   1226 C  CD  . PRO B 1 21  ? 15.21000  16.55100  48.89700 1.000 19.42433 ? 13  PRO B CD  1 
ATOM   1227 N  N   . VAL B 1 22  ? 15.82400  13.14600  48.43000 1.000 18.89641 ? 14  VAL B N   1 
ATOM   1228 C  CA  . VAL B 1 22  ? 15.67900  11.74800  48.82000 1.000 19.71042 ? 14  VAL B CA  1 
ATOM   1229 C  C   . VAL B 1 22  ? 15.97800  10.85300  47.62900 1.000 20.52500 ? 14  VAL B C   1 
ATOM   1230 O  O   . VAL B 1 22  ? 15.36600  10.98900  46.56300 1.000 21.36237 ? 14  VAL B O   1 
ATOM   1231 C  CB  . VAL B 1 22  ? 14.27000  11.47900  49.37100 1.000 15.86455 ? 14  VAL B CB  1 
ATOM   1232 C  CG1 . VAL B 1 22  ? 14.13600  10.01500  49.76700 1.000 17.45878 ? 14  VAL B CG1 1 
ATOM   1233 C  CG2 . VAL B 1 22  ? 13.98600  12.38900  50.55600 1.000 18.84086 ? 14  VAL B CG2 1 
ATOM   1234 N  N   . GLN B 1 23  ? 16.91600  9.92700   47.81100 1.000 19.71677 ? 15  GLN B N   1 
ATOM   1235 C  CA  . GLN B 1 23  ? 17.22600  8.93800   46.79100 1.000 21.69412 ? 15  GLN B CA  1 
ATOM   1236 C  C   . GLN B 1 23  ? 17.69100  7.66100   47.47700 1.000 21.77982 ? 15  GLN B C   1 
ATOM   1237 O  O   . GLN B 1 23  ? 18.18500  7.68700   48.60600 1.000 22.34689 ? 15  GLN B O   1 
ATOM   1238 C  CB  . GLN B 1 23  ? 18.28800  9.45000   45.81100 1.000 27.63206 ? 15  GLN B CB  1 
ATOM   1239 C  CG  . GLN B 1 23  ? 19.69400  9.48600   46.37600 1.000 32.49714 ? 15  GLN B CG  1 
ATOM   1240 C  CD  . GLN B 1 23  ? 20.70500  9.99600   45.36600 1.000 36.96617 ? 15  GLN B CD  1 
ATOM   1241 O  OE1 . GLN B 1 23  ? 21.73500  9.36500   45.12900 1.000 44.92969 ? 15  GLN B OE1 1 
ATOM   1242 N  NE2 . GLN B 1 23  ? 20.41400  11.14400  44.76600 1.000 34.36595 ? 15  GLN B NE2 1 
ATOM   1243 N  N   . GLY B 1 24  ? 17.52300  6.53900   46.78800 1.000 17.05960 ? 16  GLY B N   1 
ATOM   1244 C  CA  . GLY B 1 24  ? 17.90800  5.26900   47.37500 1.000 17.42672 ? 16  GLY B CA  1 
ATOM   1245 C  C   . GLY B 1 24  ? 17.85200  4.14800   46.36400 1.000 16.85138 ? 16  GLY B C   1 
ATOM   1246 O  O   . GLY B 1 24  ? 17.39400  4.32000   45.23000 1.000 16.16130 ? 16  GLY B O   1 
ATOM   1247 N  N   . ILE B 1 25  ? 18.33200  2.98600   46.80200 1.000 16.75460 ? 17  ILE B N   1 
ATOM   1248 C  CA  . ILE B 1 25  ? 18.34300  1.76500   46.00400 1.000 16.11094 ? 17  ILE B CA  1 
ATOM   1249 C  C   . ILE B 1 25  ? 17.85500  0.62300   46.88400 1.000 16.55212 ? 17  ILE B C   1 
ATOM   1250 O  O   . ILE B 1 25  ? 18.35000  0.44600   48.00300 1.000 16.83439 ? 17  ILE B O   1 
ATOM   1251 C  CB  . ILE B 1 25  ? 19.74600  1.45500   45.44600 1.000 15.90302 ? 17  ILE B CB  1 
ATOM   1252 C  CG1 . ILE B 1 25  ? 20.17500  2.52600   44.44000 1.000 20.99418 ? 17  ILE B CG1 1 
ATOM   1253 C  CG2 . ILE B 1 25  ? 19.77900  0.07000   44.81700 1.000 21.06276 ? 17  ILE B CG2 1 
ATOM   1254 C  CD1 . ILE B 1 25  ? 21.53900  2.27600   43.83000 1.000 26.72679 ? 17  ILE B CD1 1 
ATOM   1255 N  N   . ILE B 1 26  ? 16.89100  -0.14900  46.38400 1.000 13.48970 ? 18  ILE B N   1 
ATOM   1256 C  CA  . ILE B 1 26  ? 16.22000  -1.18100  47.16600 1.000 13.49367 ? 18  ILE B CA  1 
ATOM   1257 C  C   . ILE B 1 26  ? 16.23000  -2.48300  46.37800 1.000 15.80930 ? 18  ILE B C   1 
ATOM   1258 O  O   . ILE B 1 26  ? 15.82900  -2.51000  45.21000 1.000 15.95938 ? 18  ILE B O   1 
ATOM   1259 C  CB  . ILE B 1 26  ? 14.77500  -0.77900  47.51600 1.000 11.99887 ? 18  ILE B CB  1 
ATOM   1260 C  CG1 . ILE B 1 26  ? 14.76000  0.49300   48.36600 1.000 13.54501 ? 18  ILE B CG1 1 
ATOM   1261 C  CG2 . ILE B 1 26  ? 14.07600  -1.90200  48.24900 1.000 11.67202 ? 18  ILE B CG2 1 
ATOM   1262 C  CD1 . ILE B 1 26  ? 15.33400  0.29500   49.75200 1.000 17.17181 ? 18  ILE B CD1 1 
ATOM   1263 N  N   . ASN B 1 27  ? 16.66300  -3.56300  47.02500 1.000 12.86560 ? 19  ASN B N   1 
ATOM   1264 C  CA  . ASN B 1 27  ? 16.73900  -4.87900  46.41200 1.000 14.94432 ? 19  ASN B CA  1 
ATOM   1265 C  C   . ASN B 1 27  ? 15.67800  -5.79800  46.99900 1.000 13.99206 ? 19  ASN B C   1 
ATOM   1266 O  O   . ASN B 1 27  ? 15.36900  -5.72800  48.19100 1.000 17.53631 ? 19  ASN B O   1 
ATOM   1267 C  CB  . ASN B 1 27  ? 18.11800  -5.50700  46.61900 1.000 15.30411 ? 19  ASN B CB  1 
ATOM   1268 C  CG  . ASN B 1 27  ? 19.23100  -4.65000  46.07000 1.000 19.40341 ? 19  ASN B CG  1 
ATOM   1269 O  OD1 . ASN B 1 27  ? 19.45300  -4.60200  44.85900 1.000 20.43906 ? 19  ASN B OD1 1 
ATOM   1270 N  ND2 . ASN B 1 27  ? 19.94400  -3.96500  46.95800 1.000 25.78462 ? 19  ASN B ND2 1 
ATOM   1271 N  N   . PHE B 1 28  ? 15.13600  -6.67200  46.15000 1.000 14.64595 ? 20  PHE B N   1 
ATOM   1272 C  CA  . PHE B 1 28  ? 14.17300  -7.68700  46.55500 1.000 15.31769 ? 20  PHE B CA  1 
ATOM   1273 C  C   . PHE B 1 28  ? 14.65900  -9.05600  46.10000 1.000 14.77834 ? 20  PHE B C   1 
ATOM   1274 O  O   . PHE B 1 28  ? 15.15200  -9.20600  44.97800 1.000 15.98424 ? 20  PHE B O   1 
ATOM   1275 C  CB  . PHE B 1 28  ? 12.78100  -7.44200  45.94800 1.000 13.78056 ? 20  PHE B CB  1 
ATOM   1276 C  CG  . PHE B 1 28  ? 12.21900  -6.07800  46.22200 1.000 13.87648 ? 20  PHE B CG  1 
ATOM   1277 C  CD1 . PHE B 1 28  ? 12.59000  -4.98900  45.44300 1.000 11.77917 ? 20  PHE B CD1 1 
ATOM   1278 C  CD2 . PHE B 1 28  ? 11.28800  -5.89000  47.23100 1.000 14.83748 ? 20  PHE B CD2 1 
ATOM   1279 C  CE1 . PHE B 1 28  ? 12.06300  -3.73400  45.68400 1.000 12.06585 ? 20  PHE B CE1 1 
ATOM   1280 C  CE2 . PHE B 1 28  ? 10.75200  -4.62800  47.47500 1.000 13.60954 ? 20  PHE B CE2 1 
ATOM   1281 C  CZ  . PHE B 1 28  ? 11.14200  -3.55400  46.70200 1.000 11.21621 ? 20  PHE B CZ  1 
ATOM   1282 N  N   . GLU B 1 29  ? 14.49100  -10.06000 46.95600 1.000 15.45201 ? 21  GLU B N   1 
ATOM   1283 C  CA  . GLU B 1 29  ? 14.87800  -11.41900 46.60500 1.000 19.01102 ? 21  GLU B CA  1 
ATOM   1284 C  C   . GLU B 1 29  ? 13.87500  -12.40200 47.18400 1.000 16.37432 ? 21  GLU B C   1 
ATOM   1285 O  O   . GLU B 1 29  ? 13.48500  -12.28600 48.34900 1.000 13.72051 ? 21  GLU B O   1 
ATOM   1286 C  CB  . GLU B 1 29  ? 16.29100  -11.74400 47.10600 1.000 20.86232 ? 21  GLU B CB  1 
ATOM   1287 C  CG  . GLU B 1 29  ? 16.71300  -13.18800 46.85700 1.000 32.84124 ? 21  GLU B CG  1 
ATOM   1288 C  CD  . GLU B 1 29  ? 18.01000  -13.29700 46.07600 1.000 44.71079 ? 21  GLU B CD  1 
ATOM   1289 O  OE1 . GLU B 1 29  ? 18.60400  -12.24400 45.75400 1.000 42.54995 ? 21  GLU B OE1 1 
ATOM   1290 O  OE2 . GLU B 1 29  ? 18.43400  -14.43800 45.78300 1.000 42.01819 ? 21  GLU B OE2 1 
ATOM   1291 N  N   . GLN B 1 30  ? 13.45700  -13.36400 46.36300 1.000 15.13326 ? 22  GLN B N   1 
ATOM   1292 C  CA  . GLN B 1 30  ? 12.55000  -14.43400 46.78000 1.000 17.57815 ? 22  GLN B CA  1 
ATOM   1293 C  C   . GLN B 1 30  ? 13.11200  -15.72100 46.17600 1.000 21.33943 ? 22  GLN B C   1 
ATOM   1294 O  O   . GLN B 1 30  ? 12.74100  -16.11300 45.06700 1.000 23.46973 ? 22  GLN B O   1 
ATOM   1295 C  CB  . GLN B 1 30  ? 11.12200  -14.16000 46.32700 1.000 14.98864 ? 22  GLN B CB  1 
ATOM   1296 C  CG  . GLN B 1 30  ? 10.09200  -15.11900 46.89400 1.000 18.69729 ? 22  GLN B CG  1 
ATOM   1297 C  CD  . GLN B 1 30  ? 8.69100   -14.82400 46.38900 1.000 18.02912 ? 22  GLN B CD  1 
ATOM   1298 O  OE1 . GLN B 1 30  ? 8.51400   -14.26100 45.30500 1.000 18.35941 ? 22  GLN B OE1 1 
ATOM   1299 N  NE2 . GLN B 1 30  ? 7.68800   -15.19500 47.17500 1.000 14.73762 ? 22  GLN B NE2 1 
ATOM   1300 N  N   . LYS B 1 31  ? 14.02100  -16.36900 46.90800 1.000 25.96537 ? 23  LYS B N   1 
ATOM   1301 C  CA  . LYS B 1 31  ? 14.76700  -17.47700 46.31900 1.000 33.66381 ? 23  LYS B CA  1 
ATOM   1302 C  C   . LYS B 1 31  ? 13.89100  -18.70500 46.09500 1.000 33.65876 ? 23  LYS B C   1 
ATOM   1303 O  O   . LYS B 1 31  ? 14.09600  -19.43700 45.12100 1.000 33.94852 ? 23  LYS B O   1 
ATOM   1304 C  CB  . LYS B 1 31  ? 15.97500  -17.82800 47.18900 1.000 39.77119 ? 23  LYS B CB  1 
ATOM   1305 C  CG  . LYS B 1 31  ? 15.72500  -17.71300 48.68300 1.000 44.04107 ? 23  LYS B CG  1 
ATOM   1306 C  CD  . LYS B 1 31  ? 16.82800  -18.38700 49.49800 1.000 41.86465 ? 23  LYS B CD  1 
ATOM   1307 C  CE  . LYS B 1 31  ? 18.18900  -17.74600 49.26200 1.000 39.83353 ? 23  LYS B CE  1 
ATOM   1308 N  NZ  . LYS B 1 31  ? 19.14000  -18.03400 50.38100 1.000 39.81322 ? 23  LYS B NZ  1 
ATOM   1309 N  N   . GLU B 1 32  ? 12.91300  -18.94200 46.96300 1.000 34.02220 ? 24  GLU B N   1 
ATOM   1310 C  CA  . GLU B 1 32  ? 12.04200  -20.10200 46.85200 1.000 37.78129 ? 24  GLU B CA  1 
ATOM   1311 C  C   . GLU B 1 32  ? 10.62500  -19.67500 46.49800 1.000 31.31244 ? 24  GLU B C   1 
ATOM   1312 O  O   . GLU B 1 32  ? 10.16800  -18.59600 46.88200 1.000 25.51673 ? 24  GLU B O   1 
ATOM   1313 C  CB  . GLU B 1 32  ? 12.02500  -20.90800 48.15600 1.000 39.76761 ? 24  GLU B CB  1 
ATOM   1314 C  CG  . GLU B 1 32  ? 13.28300  -21.72500 48.39400 1.000 46.52323 ? 24  GLU B CG  1 
ATOM   1315 C  CD  . GLU B 1 32  ? 13.99600  -21.33700 49.67300 1.000 54.92473 ? 24  GLU B CD  1 
ATOM   1316 O  OE1 . GLU B 1 32  ? 13.40100  -20.60300 50.49000 1.000 63.78972 ? 24  GLU B OE1 1 
ATOM   1317 O  OE2 . GLU B 1 32  ? 15.15500  -21.76500 49.85900 1.000 63.26189 ? 24  GLU B OE2 1 
ATOM   1318 N  N   . SER B 1 33  ? 9.93600   -20.53500 45.75200 1.000 34.70144 ? 25  SER B N   1 
ATOM   1319 C  CA  . SER B 1 33  ? 8.52400   -20.31000 45.48400 1.000 36.98097 ? 25  SER B CA  1 
ATOM   1320 C  C   . SER B 1 33  ? 7.73900   -20.38400 46.78700 1.000 34.96102 ? 25  SER B C   1 
ATOM   1321 O  O   . SER B 1 33  ? 8.00700   -21.23100 47.64600 1.000 28.25048 ? 25  SER B O   1 
ATOM   1322 C  CB  . SER B 1 33  ? 7.99500   -21.33600 44.47800 1.000 42.64702 ? 25  SER B CB  1 
ATOM   1323 O  OG  . SER B 1 33  ? 8.32100   -20.96400 43.14800 1.000 46.69043 ? 25  SER B OG  1 
ATOM   1324 N  N   . ASN B 1 34  ? 6.77500   -19.47400 46.93700 1.000 23.93058 ? 26  ASN B N   1 
ATOM   1325 C  CA  . ASN B 1 34  ? 6.01300   -19.27900 48.16700 1.000 24.70783 ? 26  ASN B CA  1 
ATOM   1326 C  C   . ASN B 1 34  ? 6.88800   -18.84900 49.33500 1.000 22.44467 ? 26  ASN B C   1 
ATOM   1327 O  O   . ASN B 1 34  ? 6.45400   -18.92900 50.49000 1.000 25.92496 ? 26  ASN B O   1 
ATOM   1328 C  CB  . ASN B 1 34  ? 5.23200   -20.53900 48.56700 1.000 29.14980 ? 26  ASN B CB  1 
ATOM   1329 C  CG  . ASN B 1 34  ? 4.27500   -20.99900 47.49600 1.000 31.78458 ? 26  ASN B CG  1 
ATOM   1330 O  OD1 . ASN B 1 34  ? 4.28700   -22.16200 47.09600 1.000 34.42522 ? 26  ASN B OD1 1 
ATOM   1331 N  ND2 . ASN B 1 34  ? 3.43100   -20.09000 47.02700 1.000 36.40693 ? 26  ASN B ND2 1 
ATOM   1332 N  N   . GLY B 1 35  ? 8.11600   -18.41600 49.07500 1.000 17.90789 ? 27  GLY B N   1 
ATOM   1333 C  CA  . GLY B 1 35  ? 9.00200   -18.01000 50.13600 1.000 21.76941 ? 27  GLY B CA  1 
ATOM   1334 C  C   . GLY B 1 35  ? 8.81600   -16.55100 50.48700 1.000 18.45370 ? 27  GLY B C   1 
ATOM   1335 O  O   . GLY B 1 35  ? 8.21600   -15.77700 49.73200 1.000 15.39562 ? 27  GLY B O   1 
ATOM   1336 N  N   . PRO B 1 36  ? 9.32600   -16.14400 51.64400 1.000 21.82669 ? 28  PRO B N   1 
ATOM   1337 C  CA  . PRO B 1 36  ? 9.29600   -14.72300 51.99600 1.000 19.77206 ? 28  PRO B CA  1 
ATOM   1338 C  C   . PRO B 1 36  ? 10.16400  -13.92200 51.04100 1.000 16.82038 ? 28  PRO B C   1 
ATOM   1339 O  O   . PRO B 1 36  ? 11.08600  -14.44200 50.41000 1.000 16.17543 ? 28  PRO B O   1 
ATOM   1340 C  CB  . PRO B 1 36  ? 9.86000   -14.69400 53.41900 1.000 16.04792 ? 28  PRO B CB  1 
ATOM   1341 C  CG  . PRO B 1 36  ? 10.73400  -15.90000 53.48800 1.000 21.81240 ? 28  PRO B CG  1 
ATOM   1342 C  CD  . PRO B 1 36  ? 10.06900  -16.94400 52.63300 1.000 17.74511 ? 28  PRO B CD  1 
ATOM   1343 N  N   . VAL B 1 37  ? 9.83900   -12.64000 50.92000 1.000 13.07980 ? 29  VAL B N   1 
ATOM   1344 C  CA  . VAL B 1 37  ? 10.62200  -11.70900 50.11800 1.000 15.88711 ? 29  VAL B CA  1 
ATOM   1345 C  C   . VAL B 1 37  ? 11.52500  -10.93800 51.06500 1.000 15.58577 ? 29  VAL B C   1 
ATOM   1346 O  O   . VAL B 1 37  ? 11.05100  -10.34900 52.04300 1.000 15.75358 ? 29  VAL B O   1 
ATOM   1347 C  CB  . VAL B 1 37  ? 9.72800   -10.75900 49.30700 1.000 14.61560 ? 29  VAL B CB  1 
ATOM   1348 C  CG1 . VAL B 1 37  ? 10.57800  -9.84400  48.43400 1.000 15.31530 ? 29  VAL B CG1 1 
ATOM   1349 C  CG2 . VAL B 1 37  ? 8.74700   -11.55100 48.46400 1.000 14.39681 ? 29  VAL B CG2 1 
ATOM   1350 N  N   . LYS B 1 38  ? 12.82600  -10.96800 50.80000 1.000 14.67364 ? 30  LYS B N   1 
ATOM   1351 C  CA  . LYS B 1 38  ? 13.77800  -10.17500 51.56200 1.000 15.03823 ? 30  LYS B CA  1 
ATOM   1352 C  C   . LYS B 1 38  ? 13.97600  -8.84400  50.85300 1.000 16.74522 ? 30  LYS B C   1 
ATOM   1353 O  O   . LYS B 1 38  ? 14.09800  -8.80200  49.62600 1.000 16.21120 ? 30  LYS B O   1 
ATOM   1354 C  CB  . LYS B 1 38  ? 15.10600  -10.91800 51.71600 1.000 17.53620 ? 30  LYS B CB  1 
ATOM   1355 C  CG  . LYS B 1 38  ? 15.00800  -12.22300 52.51900 1.000 24.42573 ? 30  LYS B CG  1 
ATOM   1356 C  CD  . LYS B 1 38  ? 16.36900  -12.91800 52.60500 1.000 28.40279 ? 30  LYS B CD  1 
ATOM   1357 C  CE  . LYS B 1 38  ? 16.38600  -14.06000 53.61400 1.000 28.68369 ? 30  LYS B CE  1 
ATOM   1358 N  NZ  . LYS B 1 38  ? 15.63100  -15.24600 53.13500 1.000 39.94729 ? 30  LYS B NZ  1 
ATOM   1359 N  N   . VAL B 1 39  ? 13.97400  -7.75900  51.62100 1.000 14.01023 ? 31  VAL B N   1 
ATOM   1360 C  CA  . VAL B 1 39  ? 14.07800  -6.40300  51.09500 1.000 11.34922 ? 31  VAL B CA  1 
ATOM   1361 C  C   . VAL B 1 39  ? 15.24100  -5.72400  51.79800 1.000 19.77995 ? 31  VAL B C   1 
ATOM   1362 O  O   . VAL B 1 39  ? 15.23000  -5.59600  53.02800 1.000 21.06204 ? 31  VAL B O   1 
ATOM   1363 C  CB  . VAL B 1 39  ? 12.78200  -5.60500  51.32000 1.000 15.19020 ? 31  VAL B CB  1 
ATOM   1364 C  CG1 . VAL B 1 39  ? 12.84200  -4.26800  50.59900 1.000 14.92275 ? 31  VAL B CG1 1 
ATOM   1365 C  CG2 . VAL B 1 39  ? 11.57100  -6.41800  50.88700 1.000 13.54200 ? 31  VAL B CG2 1 
ATOM   1366 N  N   . TRP B 1 40  ? 16.23400  -5.27400  51.03400 1.000 16.45671 ? 32  TRP B N   1 
ATOM   1367 C  CA  . TRP B 1 40  ? 17.37400  -4.60800  51.65100 1.000 20.51996 ? 32  TRP B CA  1 
ATOM   1368 C  C   . TRP B 1 40  ? 17.88700  -3.48700  50.76100 1.000 20.84909 ? 32  TRP B C   1 
ATOM   1369 O  O   . TRP B 1 40  ? 17.80100  -3.55900  49.53200 1.000 19.24569 ? 32  TRP B O   1 
ATOM   1370 C  CB  . TRP B 1 40  ? 18.50500  -5.60100  51.97500 1.000 20.26589 ? 32  TRP B CB  1 
ATOM   1371 C  CG  . TRP B 1 40  ? 19.20200  -6.19200  50.79600 1.000 21.46196 ? 32  TRP B CG  1 
ATOM   1372 C  CD1 . TRP B 1 40  ? 20.33700  -5.73100  50.19600 1.000 24.13657 ? 32  TRP B CD1 1 
ATOM   1373 C  CD2 . TRP B 1 40  ? 18.83600  -7.38600  50.09700 1.000 22.63173 ? 32  TRP B CD2 1 
ATOM   1374 N  NE1 . TRP B 1 40  ? 20.69000  -6.55700  49.15400 1.000 23.15719 ? 32  TRP B NE1 1 
ATOM   1375 C  CE2 . TRP B 1 40  ? 19.78400  -7.58000  49.07300 1.000 21.29602 ? 32  TRP B CE2 1 
ATOM   1376 C  CE3 . TRP B 1 40  ? 17.78900  -8.30200  50.22900 1.000 23.15477 ? 32  TRP B CE3 1 
ATOM   1377 C  CZ2 . TRP B 1 40  ? 19.71700  -8.65300  48.19000 1.000 23.63101 ? 32  TRP B CZ2 1 
ATOM   1378 C  CZ3 . TRP B 1 40  ? 17.72500  -9.36600  49.35300 1.000 27.19007 ? 32  TRP B CZ3 1 
ATOM   1379 C  CH2 . TRP B 1 40  ? 18.68300  -9.53400  48.34700 1.000 27.56184 ? 32  TRP B CH2 1 
ATOM   1380 N  N   . GLY B 1 41  ? 18.41200  -2.44200  51.40200 1.000 16.34022 ? 33  GLY B N   1 
ATOM   1381 C  CA  . GLY B 1 41  ? 18.95900  -1.31200  50.67600 1.000 17.08659 ? 33  GLY B CA  1 
ATOM   1382 C  C   . GLY B 1 41  ? 19.16800  -0.13200  51.60500 1.000 20.66724 ? 33  GLY B C   1 
ATOM   1383 O  O   . GLY B 1 41  ? 19.20800  -0.29300  52.82700 1.000 18.31491 ? 33  GLY B O   1 
ATOM   1384 N  N   A SER B 1 42  ? 19.30200  1.04800   51.00400 0.468 18.94502 ? 34  SER B N   1 
ATOM   1385 N  N   B SER B 1 42  ? 19.32200  1.04700   51.00600 0.532 18.95561 ? 34  SER B N   1 
ATOM   1386 C  CA  A SER B 1 42  ? 19.54700  2.26300   51.76700 0.468 17.38367 ? 34  SER B CA  1 
ATOM   1387 C  CA  B SER B 1 42  ? 19.53000  2.25900   51.78300 0.532 17.39308 ? 34  SER B CA  1 
ATOM   1388 C  C   A SER B 1 42  ? 18.87100  3.43800   51.08000 0.468 16.96803 ? 34  SER B C   1 
ATOM   1389 C  C   B SER B 1 42  ? 18.85900  3.43100   51.08700 0.532 16.94132 ? 34  SER B C   1 
ATOM   1390 O  O   A SER B 1 42  ? 18.75700  3.47400   49.85200 0.468 18.64161 ? 34  SER B O   1 
ATOM   1391 O  O   B SER B 1 42  ? 18.73900  3.45800   49.85900 0.532 18.64989 ? 34  SER B O   1 
ATOM   1392 C  CB  A SER B 1 42  ? 21.04700  2.52800   51.92000 0.468 18.39447 ? 34  SER B CB  1 
ATOM   1393 C  CB  B SER B 1 42  ? 21.02100  2.54900   51.98400 0.532 18.37994 ? 34  SER B CB  1 
ATOM   1394 O  OG  A SER B 1 42  ? 21.27000  3.70000   52.67400 0.468 17.74988 ? 34  SER B OG  1 
ATOM   1395 O  OG  B SER B 1 42  ? 21.63500  2.88400   50.75200 0.532 20.94620 ? 34  SER B OG  1 
ATOM   1396 N  N   . ILE B 1 43  ? 18.41200  4.39300   51.88700 1.000 16.18425 ? 35  ILE B N   1 
ATOM   1397 C  CA  . ILE B 1 43  ? 17.79100  5.61500   51.39700 1.000 16.24664 ? 35  ILE B CA  1 
ATOM   1398 C  C   . ILE B 1 43  ? 18.44900  6.77500   52.12200 1.000 16.74145 ? 35  ILE B C   1 
ATOM   1399 O  O   . ILE B 1 43  ? 18.63700  6.71100   53.34000 1.000 17.35264 ? 35  ILE B O   1 
ATOM   1400 C  CB  . ILE B 1 43  ? 16.27100  5.64000   51.64200 1.000 16.88741 ? 35  ILE B CB  1 
ATOM   1401 C  CG1 . ILE B 1 43  ? 15.61900  4.32000   51.23400 1.000 15.52382 ? 35  ILE B CG1 1 
ATOM   1402 C  CG2 . ILE B 1 43  ? 15.63700  6.82900   50.92000 1.000 17.25035 ? 35  ILE B CG2 1 
ATOM   1403 C  CD1 . ILE B 1 43  ? 14.13600  4.28400   51.52400 1.000 13.83052 ? 35  ILE B CD1 1 
ATOM   1404 N  N   . LYS B 1 44  ? 18.78700  7.83200   51.38800 1.000 19.35890 ? 36  LYS B N   1 
ATOM   1405 C  CA  . LYS B 1 44  ? 19.41300  9.00700   51.98100 1.000 19.44426 ? 36  LYS B CA  1 
ATOM   1406 C  C   . LYS B 1 44  ? 18.60800  10.26000  51.65800 1.000 19.32702 ? 36  LYS B C   1 
ATOM   1407 O  O   . LYS B 1 44  ? 17.69800  10.24100  50.82900 1.000 18.39257 ? 36  LYS B O   1 
ATOM   1408 C  CB  . LYS B 1 44  ? 20.85900  9.16300   51.49800 1.000 21.33065 ? 36  LYS B CB  1 
ATOM   1409 C  CG  . LYS B 1 44  ? 21.00100  9.52700   50.03000 1.000 29.19258 ? 36  LYS B CG  1 
ATOM   1410 C  CD  . LYS B 1 44  ? 22.36000  9.08900   49.51200 1.000 34.44729 ? 36  LYS B CD  1 
ATOM   1411 C  CE  . LYS B 1 44  ? 22.77200  9.86500   48.27400 1.000 42.28774 ? 36  LYS B CE  1 
ATOM   1412 N  NZ  . LYS B 1 44  ? 24.02400  9.30700   47.68100 1.000 53.66155 ? 36  LYS B NZ  1 
ATOM   1413 N  N   . GLY B 1 45  ? 18.95400  11.35500  52.33800 1.000 17.56227 ? 37  GLY B N   1 
ATOM   1414 C  CA  . GLY B 1 45  ? 18.28700  12.63100  52.16900 1.000 18.14364 ? 37  GLY B CA  1 
ATOM   1415 C  C   . GLY B 1 45  ? 17.01600  12.81100  52.96700 1.000 14.83439 ? 37  GLY B C   1 
ATOM   1416 O  O   . GLY B 1 45  ? 16.26700  13.75800  52.70000 1.000 18.15024 ? 37  GLY B O   1 
ATOM   1417 N  N   . LEU B 1 46  ? 16.75000  11.94300  53.93800 1.000 15.98527 ? 38  LEU B N   1 
ATOM   1418 C  CA  . LEU B 1 46  ? 15.50500  11.93900  54.69200 1.000 17.14175 ? 38  LEU B CA  1 
ATOM   1419 C  C   . LEU B 1 46  ? 15.64000  12.72500  55.98700 1.000 18.40541 ? 38  LEU B C   1 
ATOM   1420 O  O   . LEU B 1 46  ? 16.72600  12.85400  56.55400 1.000 19.89471 ? 38  LEU B O   1 
ATOM   1421 C  CB  . LEU B 1 46  ? 15.08200  10.51000  55.03200 1.000 19.06274 ? 38  LEU B CB  1 
ATOM   1422 C  CG  . LEU B 1 46  ? 14.71400  9.58100   53.88000 1.000 15.83132 ? 38  LEU B CG  1 
ATOM   1423 C  CD1 . LEU B 1 46  ? 14.82900  8.12200   54.31000 1.000 13.71531 ? 38  LEU B CD1 1 
ATOM   1424 C  CD2 . LEU B 1 46  ? 13.30600  9.88600   53.40500 1.000 15.03503 ? 38  LEU B CD2 1 
ATOM   1425 N  N   . THR B 1 47  ? 14.50900  13.23100  56.46400 1.000 16.74329 ? 39  THR B N   1 
ATOM   1426 C  CA  . THR B 1 47  ? 14.47100  13.78900  57.80400 1.000 15.55512 ? 39  THR B CA  1 
ATOM   1427 C  C   . THR B 1 47  ? 14.57700  12.66900  58.83100 1.000 22.57014 ? 39  THR B C   1 
ATOM   1428 O  O   . THR B 1 47  ? 14.15800  11.53400  58.59500 1.000 19.85940 ? 39  THR B O   1 
ATOM   1429 C  CB  . THR B 1 47  ? 13.19200  14.59400  58.03800 1.000 23.56736 ? 39  THR B CB  1 
ATOM   1430 O  OG1 . THR B 1 47  ? 12.04700  13.75100  57.87500 1.000 18.53525 ? 39  THR B OG1 1 
ATOM   1431 C  CG2 . THR B 1 47  ? 13.10300  15.77200  57.08300 1.000 20.66324 ? 39  THR B CG2 1 
ATOM   1432 N  N   . GLU B 1 48  ? 15.15900  13.00200  59.97800 1.000 19.55878 ? 40  GLU B N   1 
ATOM   1433 C  CA  . GLU B 1 48  ? 15.36200  12.03100  61.04300 1.000 22.77113 ? 40  GLU B CA  1 
ATOM   1434 C  C   . GLU B 1 48  ? 14.04200  11.39500  61.45500 1.000 21.16921 ? 40  GLU B C   1 
ATOM   1435 O  O   . GLU B 1 48  ? 13.03000  12.08100  61.60100 1.000 21.71816 ? 40  GLU B O   1 
ATOM   1436 C  CB  . GLU B 1 48  ? 16.00700  12.73300  62.23800 1.000 20.82000 ? 40  GLU B CB  1 
ATOM   1437 C  CG  . GLU B 1 48  ? 16.24900  11.87700  63.45900 1.000 27.60731 ? 40  GLU B CG  1 
ATOM   1438 C  CD  . GLU B 1 48  ? 16.83100  12.67200  64.62400 1.000 31.98590 ? 40  GLU B CD  1 
ATOM   1439 O  OE1 . GLU B 1 48  ? 17.35800  13.78900  64.41100 1.000 26.54419 ? 40  GLU B OE1 1 
ATOM   1440 O  OE2 . GLU B 1 48  ? 16.75500  12.16800  65.76200 1.000 38.17108 ? 40  GLU B OE2 1 
ATOM   1441 N  N   . GLY B 1 49  ? 14.05300  10.07300  61.62800 1.000 24.84397 ? 41  GLY B N   1 
ATOM   1442 C  CA  . GLY B 1 49  ? 12.88100  9.38300   62.13800 1.000 21.96468 ? 41  GLY B CA  1 
ATOM   1443 C  C   . GLY B 1 49  ? 12.21200  8.40400   61.19000 1.000 23.93971 ? 41  GLY B C   1 
ATOM   1444 O  O   . GLY B 1 49  ? 12.83900  7.90200   60.25300 1.000 16.75176 ? 41  GLY B O   1 
ATOM   1445 N  N   . LEU B 1 50  ? 10.92700  8.13300   61.42700 1.000 16.03994 ? 42  LEU B N   1 
ATOM   1446 C  CA  . LEU B 1 50  ? 10.20500  7.11800   60.67000 1.000 14.51772 ? 42  LEU B CA  1 
ATOM   1447 C  C   . LEU B 1 50  ? 9.63800   7.68900   59.37900 1.000 13.80771 ? 42  LEU B C   1 
ATOM   1448 O  O   . LEU B 1 50  ? 9.18200   8.83500   59.33300 1.000 15.25203 ? 42  LEU B O   1 
ATOM   1449 C  CB  . LEU B 1 50  ? 9.06900   6.53600   61.50700 1.000 14.59599 ? 42  LEU B CB  1 
ATOM   1450 C  CG  . LEU B 1 50  ? 9.43500   5.85000   62.81900 1.000 16.55531 ? 42  LEU B CG  1 
ATOM   1451 C  CD1 . LEU B 1 50  ? 8.16200   5.54700   63.57000 1.000 23.31053 ? 42  LEU B CD1 1 
ATOM   1452 C  CD2 . LEU B 1 50  ? 10.23700  4.57900   62.57800 1.000 20.77250 ? 42  LEU B CD2 1 
ATOM   1453 N  N   . HIS B 1 51  ? 9.65300   6.86800   58.33200 1.000 15.04726 ? 43  HIS B N   1 
ATOM   1454 C  CA  . HIS B 1 51  ? 9.09200   7.22800   57.03800 1.000 13.19618 ? 43  HIS B CA  1 
ATOM   1455 C  C   . HIS B 1 51  ? 8.32200   6.04700   56.47500 1.000 11.18299 ? 43  HIS B C   1 
ATOM   1456 O  O   . HIS B 1 51  ? 8.85400   4.93900   56.39000 1.000 11.08559 ? 43  HIS B O   1 
ATOM   1457 C  CB  . HIS B 1 51  ? 10.19500  7.65000   56.06600 1.000 14.92297 ? 43  HIS B CB  1 
ATOM   1458 C  CG  . HIS B 1 51  ? 10.87200  8.92600   56.45000 1.000 14.84729 ? 43  HIS B CG  1 
ATOM   1459 N  ND1 . HIS B 1 51  ? 10.40100  10.16000  56.06000 1.000 17.79350 ? 43  HIS B ND1 1 
ATOM   1460 C  CD2 . HIS B 1 51  ? 11.96700  9.16100   57.20900 1.000 18.62687 ? 43  HIS B CD2 1 
ATOM   1461 C  CE1 . HIS B 1 51  ? 11.18400  11.10300  56.55400 1.000 19.79228 ? 43  HIS B CE1 1 
ATOM   1462 N  NE2 . HIS B 1 51  ? 12.14200  10.52300  57.25500 1.000 21.26702 ? 43  HIS B NE2 1 
ATOM   1463 N  N   . GLY B 1 52  ? 7.06600   6.29300   56.08800 1.000 12.55905 ? 44  GLY B N   1 
ATOM   1464 C  CA  . GLY B 1 52  ? 6.26300   5.24100   55.49600 1.000 12.76913 ? 44  GLY B CA  1 
ATOM   1465 C  C   . GLY B 1 52  ? 6.90400   4.68600   54.22900 1.000 10.64713 ? 44  GLY B C   1 
ATOM   1466 O  O   . GLY B 1 52  ? 7.51000   5.41600   53.44200 1.000 12.47238 ? 44  GLY B O   1 
ATOM   1467 N  N   . PHE B 1 53  ? 6.74000   3.37900   54.03400 1.000 11.32879 ? 45  PHE B N   1 
ATOM   1468 C  CA  . PHE B 1 53  ? 7.45500   2.62000   53.00600 1.000 13.40518 ? 45  PHE B CA  1 
ATOM   1469 C  C   . PHE B 1 53  ? 6.43000   1.67100   52.39000 1.000 16.28990 ? 45  PHE B C   1 
ATOM   1470 O  O   . PHE B 1 53  ? 6.07400   0.66400   53.00900 1.000 11.38099 ? 45  PHE B O   1 
ATOM   1471 C  CB  . PHE B 1 53  ? 8.62700   1.87800   53.64300 1.000 13.33526 ? 45  PHE B CB  1 
ATOM   1472 C  CG  . PHE B 1 53  ? 9.60200   1.28400   52.67000 1.000 14.83236 ? 45  PHE B CG  1 
ATOM   1473 C  CD1 . PHE B 1 53  ? 10.29200  2.08500   51.77800 1.000 13.16346 ? 45  PHE B CD1 1 
ATOM   1474 C  CD2 . PHE B 1 53  ? 9.87000   -0.07800  52.69000 1.000 16.61782 ? 45  PHE B CD2 1 
ATOM   1475 C  CE1 . PHE B 1 53  ? 11.21400  1.53300   50.89800 1.000 14.00791 ? 45  PHE B CE1 1 
ATOM   1476 C  CE2 . PHE B 1 53  ? 10.78900  -0.63900  51.81200 1.000 17.68010 ? 45  PHE B CE2 1 
ATOM   1477 C  CZ  . PHE B 1 53  ? 11.46200  0.16700   50.91500 1.000 12.30163 ? 45  PHE B CZ  1 
ATOM   1478 N  N   . HIS B 1 54  ? 5.94000   1.99800   51.18900 1.000 12.77066 ? 46  HIS B N   1 
ATOM   1479 C  CA  . HIS B 1 54  ? 4.77100   1.32400   50.63500 1.000 12.77260 ? 46  HIS B CA  1 
ATOM   1480 C  C   . HIS B 1 54  ? 4.96300   0.99200   49.16400 1.000 12.02432 ? 46  HIS B C   1 
ATOM   1481 O  O   . HIS B 1 54  ? 5.62500   1.72300   48.42300 1.000 11.55037 ? 46  HIS B O   1 
ATOM   1482 C  CB  . HIS B 1 54  ? 3.50700   2.18700   50.76600 1.000 14.86076 ? 46  HIS B CB  1 
ATOM   1483 C  CG  . HIS B 1 54  ? 3.22500   2.63100   52.16300 1.000 14.14632 ? 46  HIS B CG  1 
ATOM   1484 N  ND1 . HIS B 1 54  ? 2.79800   3.90500   52.46700 1.000 15.38742 ? 46  HIS B ND1 1 
ATOM   1485 C  CD2 . HIS B 1 54  ? 3.30400   1.96800   53.34100 1.000 12.34922 ? 46  HIS B CD2 1 
ATOM   1486 C  CE1 . HIS B 1 54  ? 2.63300   4.01000   53.77300 1.000 15.98472 ? 46  HIS B CE1 1 
ATOM   1487 N  NE2 . HIS B 1 54  ? 2.93500   2.85000   54.32700 1.000 14.57564 ? 46  HIS B NE2 1 
ATOM   1488 N  N   . VAL B 1 55  ? 4.34200   -0.10800  48.74500 1.000 9.29027  ? 47  VAL B N   1 
ATOM   1489 C  CA  . VAL B 1 55  ? 4.16100   -0.41600  47.33000 1.000 8.38363  ? 47  VAL B CA  1 
ATOM   1490 C  C   . VAL B 1 55  ? 2.79100   0.10100   46.90600 1.000 12.42317 ? 47  VAL B C   1 
ATOM   1491 O  O   . VAL B 1 55  ? 1.76400   -0.31000  47.45900 1.000 8.52909  ? 47  VAL B O   1 
ATOM   1492 C  CB  . VAL B 1 55  ? 4.27800   -1.92300  47.05900 1.000 9.10301  ? 47  VAL B CB  1 
ATOM   1493 C  CG1 . VAL B 1 55  ? 4.18500   -2.19300  45.55900 1.000 8.24637  ? 47  VAL B CG1 1 
ATOM   1494 C  CG2 . VAL B 1 55  ? 5.56700   -2.49100  47.65500 1.000 12.54535 ? 47  VAL B CG2 1 
ATOM   1495 N  N   . HIS B 1 56  ? 2.77300   0.99200   45.92100 1.000 12.78527 ? 48  HIS B N   1 
ATOM   1496 C  CA  . HIS B 1 56  ? 1.54800   1.58800   45.41100 1.000 11.24733 ? 48  HIS B CA  1 
ATOM   1497 C  C   . HIS B 1 56  ? 1.08600   0.88300   44.14000 1.000 12.17409 ? 48  HIS B C   1 
ATOM   1498 O  O   . HIS B 1 56  ? 1.87300   0.26600   43.41800 1.000 12.63556 ? 48  HIS B O   1 
ATOM   1499 C  CB  . HIS B 1 56  ? 1.75000   3.07800   45.14000 1.000 14.07416 ? 48  HIS B CB  1 
ATOM   1500 C  CG  . HIS B 1 56  ? 1.88400   3.89700   46.38300 1.000 14.33325 ? 48  HIS B CG  1 
ATOM   1501 N  ND1 . HIS B 1 56  ? 1.18300   5.06500   46.58300 1.000 16.40411 ? 48  HIS B ND1 1 
ATOM   1502 C  CD2 . HIS B 1 56  ? 2.62900   3.70900   47.49700 1.000 15.41242 ? 48  HIS B CD2 1 
ATOM   1503 C  CE1 . HIS B 1 56  ? 1.49000   5.56400   47.76700 1.000 12.99595 ? 48  HIS B CE1 1 
ATOM   1504 N  NE2 . HIS B 1 56  ? 2.37200   4.76400   48.33900 1.000 15.35166 ? 48  HIS B NE2 1 
ATOM   1505 N  N   . GLU B 1 57  ? -0.21900  0.99100   43.87400 1.000 10.13406 ? 49  GLU B N   1 
ATOM   1506 C  CA  . GLU B 1 57  ? -0.82600  0.24700   42.77600 1.000 12.21082 ? 49  GLU B CA  1 
ATOM   1507 C  C   . GLU B 1 57  ? -0.35100  0.75700   41.41900 1.000 17.97361 ? 49  GLU B C   1 
ATOM   1508 O  O   . GLU B 1 57  ? -0.07300  -0.03800  40.51300 1.000 17.26946 ? 49  GLU B O   1 
ATOM   1509 C  CB  . GLU B 1 57  ? -2.35100  0.32700   42.87500 1.000 16.98644 ? 49  GLU B CB  1 
ATOM   1510 C  CG  . GLU B 1 57  ? -3.08100  -0.43900  41.78900 1.000 16.20394 ? 49  GLU B CG  1 
ATOM   1511 C  CD  . GLU B 1 57  ? -4.59100  -0.31300  41.88800 1.000 21.49583 ? 49  GLU B CD  1 
ATOM   1512 O  OE1 . GLU B 1 57  ? -5.07100  0.52900   42.67300 1.000 19.44881 ? 49  GLU B OE1 1 
ATOM   1513 O  OE2 . GLU B 1 57  ? -5.29800  -1.05700  41.17400 1.000 24.93210 ? 49  GLU B OE2 1 
ATOM   1514 N  N   . PHE B 1 58  ? -0.26600  2.07500   41.25700 1.000 18.87548 ? 50  PHE B N   1 
ATOM   1515 C  CA  . PHE B 1 58  ? 0.17600   2.69500   40.01800 1.000 23.07957 ? 50  PHE B CA  1 
ATOM   1516 C  C   . PHE B 1 58  ? 1.20600   3.77300   40.33600 1.000 24.96537 ? 50  PHE B C   1 
ATOM   1517 O  O   . PHE B 1 58  ? 1.43300   4.12900   41.49600 1.000 27.87473 ? 50  PHE B O   1 
ATOM   1518 C  CB  . PHE B 1 58  ? -0.99900  3.31200   39.24300 1.000 24.37728 ? 50  PHE B CB  1 
ATOM   1519 C  CG  . PHE B 1 58  ? -2.15200  2.37400   39.02500 1.000 20.91306 ? 50  PHE B CG  1 
ATOM   1520 C  CD1 . PHE B 1 58  ? -2.00300  1.23600   38.24700 1.000 21.91568 ? 50  PHE B CD1 1 
ATOM   1521 C  CD2 . PHE B 1 58  ? -3.39600  2.64600   39.57900 1.000 20.27149 ? 50  PHE B CD2 1 
ATOM   1522 C  CE1 . PHE B 1 58  ? -3.06500  0.37200   38.04000 1.000 21.80527 ? 50  PHE B CE1 1 
ATOM   1523 C  CE2 . PHE B 1 58  ? -4.46700  1.79000   39.36900 1.000 21.06172 ? 50  PHE B CE2 1 
ATOM   1524 C  CZ  . PHE B 1 58  ? -4.30000  0.65000   38.59800 1.000 21.89516 ? 50  PHE B CZ  1 
ATOM   1525 N  N   . GLY B 1 59  ? 1.82300   4.30700   39.28600 1.000 27.16773 ? 51  GLY B N   1 
ATOM   1526 C  CA  . GLY B 1 59  ? 2.73600   5.42600   39.43500 1.000 27.95688 ? 51  GLY B CA  1 
ATOM   1527 C  C   . GLY B 1 59  ? 2.00100   6.75000   39.56100 1.000 29.48494 ? 51  GLY B C   1 
ATOM   1528 O  O   . GLY B 1 59  ? 2.46400   7.67300   40.23100 1.000 34.20596 ? 51  GLY B O   1 
ATOM   1529 N  N   . GLY B 1 69  ? -0.43100  7.15100   44.35300 1.000 29.72233 ? 61  GLY B N   1 
ATOM   1530 C  CA  . GLY B 1 69  ? -1.85300  6.86700   44.46500 1.000 37.26413 ? 61  GLY B CA  1 
ATOM   1531 C  C   . GLY B 1 69  ? -2.19400  5.98000   45.65000 1.000 29.26447 ? 61  GLY B C   1 
ATOM   1532 O  O   . GLY B 1 69  ? -1.54400  6.06000   46.69400 1.000 34.76322 ? 61  GLY B O   1 
ATOM   1533 N  N   . PRO B 1 70  ? -3.21400  5.13800   45.50800 1.000 28.09061 ? 62  PRO B N   1 
ATOM   1534 C  CA  . PRO B 1 70  ? -3.53700  4.19200   46.57700 1.000 20.74430 ? 62  PRO B CA  1 
ATOM   1535 C  C   . PRO B 1 70  ? -2.53200  3.05100   46.62200 1.000 19.91565 ? 62  PRO B C   1 
ATOM   1536 O  O   . PRO B 1 70  ? -1.83900  2.74400   45.64800 1.000 15.59209 ? 62  PRO B O   1 
ATOM   1537 C  CB  . PRO B 1 70  ? -4.93000  3.68600   46.19400 1.000 30.11893 ? 62  PRO B CB  1 
ATOM   1538 C  CG  . PRO B 1 70  ? -4.92500  3.75500   44.69000 1.000 30.47486 ? 62  PRO B CG  1 
ATOM   1539 C  CD  . PRO B 1 70  ? -4.09900  4.97400   44.33900 1.000 31.41451 ? 62  PRO B CD  1 
ATOM   1540 N  N   . HIS B 1 71  ? -2.46000  2.42400   47.78900 1.000 15.55209 ? 63  HIS B N   1 
ATOM   1541 C  CA  . HIS B 1 71  ? -1.49800  1.35600   47.99000 1.000 13.56708 ? 63  HIS B CA  1 
ATOM   1542 C  C   . HIS B 1 71  ? -1.90200  0.12200   47.19900 1.000 13.74688 ? 63  HIS B C   1 
ATOM   1543 O  O   . HIS B 1 71  ? -3.07900  -0.10100  46.90400 1.000 12.11294 ? 63  HIS B O   1 
ATOM   1544 C  CB  . HIS B 1 71  ? -1.37800  1.03000   49.47600 1.000 13.21296 ? 63  HIS B CB  1 
ATOM   1545 C  CG  . HIS B 1 71  ? -0.87900  2.17800   50.29500 1.000 17.95698 ? 63  HIS B CG  1 
ATOM   1546 N  ND1 . HIS B 1 71  ? -0.74200  2.11800   51.66400 1.000 13.76674 ? 63  HIS B ND1 1 
ATOM   1547 C  CD2 . HIS B 1 71  ? -0.47600  3.41900   49.93300 1.000 14.99985 ? 63  HIS B CD2 1 
ATOM   1548 C  CE1 . HIS B 1 71  ? -0.28000  3.27100   52.11200 1.000 18.15456 ? 63  HIS B CE1 1 
ATOM   1549 N  NE2 . HIS B 1 71  ? -0.11000  4.07800   51.08100 1.000 11.98220 ? 63  HIS B NE2 1 
ATOM   1550 N  N   . PHE B 1 72  ? -0.90500  -0.67700  46.83700 1.000 11.72982 ? 64  PHE B N   1 
ATOM   1551 C  CA  . PHE B 1 72  ? -1.17700  -1.92400  46.13700 1.000 11.92464 ? 64  PHE B CA  1 
ATOM   1552 C  C   . PHE B 1 72  ? -2.04400  -2.80800  47.01700 1.000 12.11053 ? 64  PHE B C   1 
ATOM   1553 O  O   . PHE B 1 72  ? -1.64400  -3.17700  48.12300 1.000 13.62760 ? 64  PHE B O   1 
ATOM   1554 C  CB  . PHE B 1 72  ? 0.13500   -2.61700  45.78000 1.000 13.01297 ? 64  PHE B CB  1 
ATOM   1555 C  CG  . PHE B 1 72  ? -0.04000  -3.91600  45.04300 1.000 13.26655 ? 64  PHE B CG  1 
ATOM   1556 C  CD1 . PHE B 1 72  ? -0.85400  -3.99100  43.92400 1.000 14.13957 ? 64  PHE B CD1 1 
ATOM   1557 C  CD2 . PHE B 1 72  ? 0.63700   -5.05500  45.45400 1.000 13.55069 ? 64  PHE B CD2 1 
ATOM   1558 C  CE1 . PHE B 1 72  ? -1.00800  -5.18200  43.23800 1.000 13.97687 ? 64  PHE B CE1 1 
ATOM   1559 C  CE2 . PHE B 1 72  ? 0.48800   -6.24900  44.77000 1.000 14.27205 ? 64  PHE B CE2 1 
ATOM   1560 C  CZ  . PHE B 1 72  ? -0.33700  -6.31100  43.66200 1.000 14.80987 ? 64  PHE B CZ  1 
ATOM   1561 N  N   . ASN B 1 73  ? -3.24500  -3.12200  46.54000 1.000 12.05706 ? 65  ASN B N   1 
ATOM   1562 C  CA  . ASN B 1 73  ? -4.25300  -3.69600  47.42200 1.000 16.30133 ? 65  ASN B CA  1 
ATOM   1563 C  C   . ASN B 1 73  ? -5.12900  -4.69700  46.67500 1.000 15.42773 ? 65  ASN B C   1 
ATOM   1564 O  O   . ASN B 1 73  ? -6.35300  -4.51900  46.60800 1.000 14.40910 ? 65  ASN B O   1 
ATOM   1565 C  CB  . ASN B 1 73  ? -5.09800  -2.56800  48.02500 1.000 15.63549 ? 65  ASN B CB  1 
ATOM   1566 C  CG  . ASN B 1 73  ? -6.10300  -3.05600  49.05600 1.000 15.90392 ? 65  ASN B CG  1 
ATOM   1567 O  OD1 . ASN B 1 73  ? -5.92900  -4.10500  49.68300 1.000 13.75241 ? 65  ASN B OD1 1 
ATOM   1568 N  ND2 . ASN B 1 73  ? -7.16300  -2.28200  49.24300 1.000 14.43770 ? 65  ASN B ND2 1 
ATOM   1569 N  N   . PRO B 1 74  ? -4.55400  -5.76800  46.12000 1.000 14.65167 ? 66  PRO B N   1 
ATOM   1570 C  CA  . PRO B 1 74  ? -5.36800  -6.69500  45.31700 1.000 17.04851 ? 66  PRO B CA  1 
ATOM   1571 C  C   . PRO B 1 74  ? -6.41100  -7.44800  46.12300 1.000 18.26656 ? 66  PRO B C   1 
ATOM   1572 O  O   . PRO B 1 74  ? -7.35400  -7.98000  45.52600 1.000 21.09737 ? 66  PRO B O   1 
ATOM   1573 C  CB  . PRO B 1 74  ? -4.32700  -7.65100  44.72200 1.000 15.49808 ? 66  PRO B CB  1 
ATOM   1574 C  CG  . PRO B 1 74  ? -3.21200  -7.62700  45.71200 1.000 15.47063 ? 66  PRO B CG  1 
ATOM   1575 C  CD  . PRO B 1 74  ? -3.15300  -6.21500  46.21600 1.000 13.97669 ? 66  PRO B CD  1 
ATOM   1576 N  N   . LEU B 1 75  ? -6.28500  -7.50700  47.44700 1.000 16.43791 ? 67  LEU B N   1 
ATOM   1577 C  CA  . LEU B 1 75  ? -7.25000  -8.20100  48.28900 1.000 19.17437 ? 67  LEU B CA  1 
ATOM   1578 C  C   . LEU B 1 75  ? -8.33300  -7.28200  48.84000 1.000 17.30744 ? 67  LEU B C   1 
ATOM   1579 O  O   . LEU B 1 75  ? -9.20600  -7.75300  49.57600 1.000 17.23971 ? 67  LEU B O   1 
ATOM   1580 C  CB  . LEU B 1 75  ? -6.52700  -8.90000  49.44300 1.000 19.66320 ? 67  LEU B CB  1 
ATOM   1581 C  CG  . LEU B 1 75  ? -5.48300  -9.92000  48.99200 1.000 21.54716 ? 67  LEU B CG  1 
ATOM   1582 C  CD1 . LEU B 1 75  ? -4.67100  -10.42300 50.17600 1.000 20.59180 ? 67  LEU B CD1 1 
ATOM   1583 C  CD2 . LEU B 1 75  ? -6.16200  -11.07200 48.27200 1.000 24.69767 ? 67  LEU B CD2 1 
ATOM   1584 N  N   . SER B 1 76  ? -8.29500  -5.99400  48.50100 1.000 18.11136 ? 68  SER B N   1 
ATOM   1585 C  CA  . SER B 1 76  ? -9.29700  -5.01900  48.93800 1.000 16.88100 ? 68  SER B CA  1 
ATOM   1586 C  C   . SER B 1 76  ? -9.46400  -5.03000  50.45700 1.000 15.95357 ? 68  SER B C   1 
ATOM   1587 O  O   . SER B 1 76  ? -10.56800 -5.15700  50.98700 1.000 16.35942 ? 68  SER B O   1 
ATOM   1588 C  CB  . SER B 1 76  ? -10.63800 -5.25700  48.24000 1.000 18.12076 ? 68  SER B CB  1 
ATOM   1589 O  OG  . SER B 1 76  ? -10.51100 -5.15300  46.83200 1.000 25.69543 ? 68  SER B OG  1 
ATOM   1590 N  N   . ARG B 1 77  ? -8.34400  -4.90200  51.16000 1.000 14.36399 ? 69  ARG B N   1 
ATOM   1591 C  CA  . ARG B 1 77  ? -8.33600  -4.79600  52.60700 1.000 14.59614 ? 69  ARG B CA  1 
ATOM   1592 C  C   . ARG B 1 77  ? -8.08700  -3.34700  53.00700 1.000 14.72926 ? 69  ARG B C   1 
ATOM   1593 O  O   . ARG B 1 77  ? -7.92000  -2.45600  52.17000 1.000 14.63099 ? 69  ARG B O   1 
ATOM   1594 C  CB  . ARG B 1 77  ? -7.26500  -5.69700  53.22400 1.000 16.37910 ? 69  ARG B CB  1 
ATOM   1595 C  CG  . ARG B 1 77  ? -7.02100  -7.00700  52.50900 1.000 21.47052 ? 69  ARG B CG  1 
ATOM   1596 C  CD  . ARG B 1 77  ? -7.83400  -8.14700  53.09000 1.000 23.56113 ? 69  ARG B CD  1 
ATOM   1597 N  NE  . ARG B 1 77  ? -7.84100  -8.21500  54.54900 1.000 27.23539 ? 69  ARG B NE  1 
ATOM   1598 C  CZ  . ARG B 1 77  ? -6.86400  -8.70700  55.30300 1.000 22.70043 ? 69  ARG B CZ  1 
ATOM   1599 N  NH1 . ARG B 1 77  ? -5.69500  -9.05500  54.78900 1.000 28.70529 ? 69  ARG B NH1 1 
ATOM   1600 N  NH2 . ARG B 1 77  ? -7.06700  -8.85600  56.61000 1.000 28.50240 ? 69  ARG B NH2 1 
ATOM   1601 N  N   . LYS B 1 78  ? -8.04000  -3.11400  54.30900 1.000 13.09528 ? 70  LYS B N   1 
ATOM   1602 C  CA  . LYS B 1 78  ? -7.69700  -1.80400  54.83500 1.000 16.75077 ? 70  LYS B CA  1 
ATOM   1603 C  C   . LYS B 1 78  ? -6.22000  -1.76400  55.21400 1.000 14.00334 ? 70  LYS B C   1 
ATOM   1604 O  O   . LYS B 1 78  ? -5.54500  -2.79100  55.30300 1.000 12.51118 ? 70  LYS B O   1 
ATOM   1605 C  CB  . LYS B 1 78  ? -8.60200  -1.45400  56.01900 1.000 20.67474 ? 70  LYS B CB  1 
ATOM   1606 C  CG  . LYS B 1 78  ? -9.92400  -0.86300  55.55300 1.000 25.54630 ? 70  LYS B CG  1 
ATOM   1607 C  CD  . LYS B 1 78  ? -11.12500 -1.48000  56.24000 1.000 35.81842 ? 70  LYS B CD  1 
ATOM   1608 C  CE  . LYS B 1 78  ? -11.39300 -0.83400  57.58100 1.000 35.46791 ? 70  LYS B CE  1 
ATOM   1609 N  NZ  . LYS B 1 78  ? -12.84400 -0.90000  57.91400 1.000 47.41407 ? 70  LYS B NZ  1 
ATOM   1610 N  N   . HIS B 1 79  ? -5.71500  -0.54800  55.40100 1.000 13.65509 ? 71  HIS B N   1 
ATOM   1611 C  CA  . HIS B 1 79  ? -4.29800  -0.34400  55.66300 1.000 10.93271 ? 71  HIS B CA  1 
ATOM   1612 C  C   . HIS B 1 79  ? -3.91200  -0.88300  57.03600 1.000 9.94800  ? 71  HIS B C   1 
ATOM   1613 O  O   . HIS B 1 79  ? -4.69100  -0.84100  57.99100 1.000 13.66380 ? 71  HIS B O   1 
ATOM   1614 C  CB  . HIS B 1 79  ? -3.96200  1.14800   55.57100 1.000 12.37220 ? 71  HIS B CB  1 
ATOM   1615 C  CG  . HIS B 1 79  ? -2.53700  1.47700   55.89600 1.000 13.37688 ? 71  HIS B CG  1 
ATOM   1616 N  ND1 . HIS B 1 79  ? -1.51600  1.35600   54.98100 1.000 10.14365 ? 71  HIS B ND1 1 
ATOM   1617 C  CD2 . HIS B 1 79  ? -1.96700  1.94700   57.03000 1.000 14.18982 ? 71  HIS B CD2 1 
ATOM   1618 C  CE1 . HIS B 1 79  ? -0.37600  1.71500   55.53800 1.000 12.27047 ? 71  HIS B CE1 1 
ATOM   1619 N  NE2 . HIS B 1 79  ? -0.62200  2.08200   56.78300 1.000 9.62712  ? 71  HIS B NE2 1 
ATOM   1620 N  N   . GLY B 1 80  ? -2.68300  -1.37900  57.13200 1.000 10.63688 ? 72  GLY B N   1 
ATOM   1621 C  CA  . GLY B 1 80  ? -2.15100  -1.80700  58.40900 1.000 9.92017  ? 72  GLY B CA  1 
ATOM   1622 C  C   . GLY B 1 80  ? -0.64100  -1.79000  58.35000 1.000 12.31242 ? 72  GLY B C   1 
ATOM   1623 O  O   . GLY B 1 80  ? -0.04000  -1.35500  57.36600 1.000 14.35603 ? 72  GLY B O   1 
ATOM   1624 N  N   . GLY B 1 81  ? -0.03000  -2.25900  59.43300 1.000 13.36267 ? 73  GLY B N   1 
ATOM   1625 C  CA  . GLY B 1 81  ? 1.39200   -2.50000  59.44900 1.000 12.48449 ? 73  GLY B CA  1 
ATOM   1626 C  C   . GLY B 1 81  ? 1.68200   -3.85400  58.83800 1.000 10.36941 ? 73  GLY B C   1 
ATOM   1627 O  O   . GLY B 1 81  ? 0.78400   -4.68400  58.67800 1.000 13.69536 ? 73  GLY B O   1 
ATOM   1628 N  N   . PRO B 1 82  ? 2.94000   -4.10100  58.47300 1.000 11.51147 ? 74  PRO B N   1 
ATOM   1629 C  CA  . PRO B 1 82  ? 3.26400   -5.36400  57.78700 1.000 12.47658 ? 74  PRO B CA  1 
ATOM   1630 C  C   . PRO B 1 82  ? 3.02600   -6.60000  58.63100 1.000 14.29413 ? 74  PRO B C   1 
ATOM   1631 O  O   . PRO B 1 82  ? 2.74600   -7.66400  58.07000 1.000 11.98122 ? 74  PRO B O   1 
ATOM   1632 C  CB  . PRO B 1 82  ? 4.75100   -5.20500  57.43000 1.000 12.00386 ? 74  PRO B CB  1 
ATOM   1633 C  CG  . PRO B 1 82  ? 5.25800   -4.13100  58.34400 1.000 16.05290 ? 74  PRO B CG  1 
ATOM   1634 C  CD  . PRO B 1 82  ? 4.09900   -3.20000  58.55000 1.000 15.77242 ? 74  PRO B CD  1 
ATOM   1635 N  N   . LYS B 1 83  ? 3.13300   -6.51000  59.95400 1.000 14.99194 ? 75  LYS B N   1 
ATOM   1636 C  CA  . LYS B 1 83  ? 2.85900   -7.65400  60.81300 1.000 19.41198 ? 75  LYS B CA  1 
ATOM   1637 C  C   . LYS B 1 83  ? 1.42700   -7.66300  61.32800 1.000 20.25366 ? 75  LYS B C   1 
ATOM   1638 O  O   . LYS B 1 83  ? 1.08800   -8.49500  62.17400 1.000 23.90620 ? 75  LYS B O   1 
ATOM   1639 C  CB  . LYS B 1 83  ? 3.84000   -7.69600  61.98800 1.000 18.09827 ? 75  LYS B CB  1 
ATOM   1640 C  CG  . LYS B 1 83  ? 5.30500   -7.75200  61.58400 1.000 22.09675 ? 75  LYS B CG  1 
ATOM   1641 C  CD  . LYS B 1 83  ? 5.61100   -8.97800  60.74800 1.000 22.93959 ? 75  LYS B CD  1 
ATOM   1642 C  CE  . LYS B 1 83  ? 7.05900   -8.97300  60.28400 1.000 29.19182 ? 75  LYS B CE  1 
ATOM   1643 N  NZ  . LYS B 1 83  ? 8.00700   -8.84300  61.43100 1.000 30.40398 ? 75  LYS B NZ  1 
ATOM   1644 N  N   . ASP B 1 84  ? 0.58300   -6.75900  60.84500 1.000 17.21749 ? 76  ASP B N   1 
ATOM   1645 C  CA  . ASP B 1 84  ? -0.82800  -6.79800  61.19400 1.000 18.24724 ? 76  ASP B CA  1 
ATOM   1646 C  C   . ASP B 1 84  ? -1.55500  -7.81700  60.32700 1.000 21.45987 ? 76  ASP B C   1 
ATOM   1647 O  O   . ASP B 1 84  ? -1.16200  -8.08800  59.18700 1.000 19.70358 ? 76  ASP B O   1 
ATOM   1648 C  CB  . ASP B 1 84  ? -1.47100  -5.41900  61.03300 1.000 18.57610 ? 76  ASP B CB  1 
ATOM   1649 C  CG  . ASP B 1 84  ? -1.02400  -4.44300  62.10100 1.000 27.92823 ? 76  ASP B CG  1 
ATOM   1650 O  OD1 . ASP B 1 84  ? -0.59700  -4.90500  63.18200 1.000 34.86540 ? 76  ASP B OD1 1 
ATOM   1651 O  OD2 . ASP B 1 84  ? -1.10200  -3.21700  61.87100 1.000 19.27192 ? 76  ASP B OD2 1 
ATOM   1652 N  N   . GLU B 1 85  ? -2.62300  -8.39300  60.88700 1.000 28.32875 ? 77  GLU B N   1 
ATOM   1653 C  CA  . GLU B 1 85  ? -3.43700  -9.33200  60.12200 1.000 25.07352 ? 77  GLU B CA  1 
ATOM   1654 C  C   . GLU B 1 85  ? -4.16400  -8.62700  58.98700 1.000 17.57862 ? 77  GLU B C   1 
ATOM   1655 O  O   . GLU B 1 85  ? -4.21700  -9.14400  57.86500 1.000 21.16921 ? 77  GLU B O   1 
ATOM   1656 C  CB  . GLU B 1 85  ? -4.43400  -10.04500 61.03700 1.000 35.39091 ? 77  GLU B CB  1 
ATOM   1657 C  CG  . GLU B 1 85  ? -3.79300  -10.91500 62.10800 1.000 50.05509 ? 77  GLU B CG  1 
ATOM   1658 C  CD  . GLU B 1 85  ? -4.81100  -11.48500 63.08200 1.000 61.19084 ? 77  GLU B CD  1 
ATOM   1659 O  OE1 . GLU B 1 85  ? -6.02400  -11.27500 62.86600 1.000 65.82841 ? 77  GLU B OE1 1 
ATOM   1660 O  OE2 . GLU B 1 85  ? -4.39700  -12.13900 64.06400 1.000 56.39003 ? 77  GLU B OE2 1 
ATOM   1661 N  N   . GLU B 1 86  ? -4.72200  -7.44600  59.24500 1.000 18.70760 ? 78  GLU B N   1 
ATOM   1662 C  CA  . GLU B 1 86  ? -5.34100  -6.65100  58.19300 1.000 18.01395 ? 78  GLU B CA  1 
ATOM   1663 C  C   . GLU B 1 86  ? -4.33100  -5.64200  57.66400 1.000 16.92664 ? 78  GLU B C   1 
ATOM   1664 O  O   . GLU B 1 86  ? -3.84200  -4.79000  58.41400 1.000 14.27337 ? 78  GLU B O   1 
ATOM   1665 C  CB  . GLU B 1 86  ? -6.60300  -5.93300  58.66800 1.000 20.95457 ? 78  GLU B CB  1 
ATOM   1666 C  CG  . GLU B 1 86  ? -7.15200  -5.01500  57.58400 1.000 23.92170 ? 78  GLU B CG  1 
ATOM   1667 C  CD  . GLU B 1 86  ? -8.66200  -5.04900  57.46000 1.000 33.62748 ? 78  GLU B CD  1 
ATOM   1668 O  OE1 . GLU B 1 86  ? -9.35100  -4.79900  58.47500 1.000 30.54018 ? 78  GLU B OE1 1 
ATOM   1669 O  OE2 . GLU B 1 86  ? -9.15600  -5.31600  56.33700 1.000 30.19141 ? 78  GLU B OE2 1 
ATOM   1670 N  N   . ARG B 1 87  ? -4.02800  -5.74300  56.37400 1.000 12.14212 ? 79  ARG B N   1 
ATOM   1671 C  CA  . ARG B 1 87  ? -3.10500  -4.83100  55.71800 1.000 10.13504 ? 79  ARG B CA  1 
ATOM   1672 C  C   . ARG B 1 87  ? -3.31900  -4.93400  54.21900 1.000 13.46253 ? 79  ARG B C   1 
ATOM   1673 O  O   . ARG B 1 87  ? -3.89600  -5.90600  53.71800 1.000 13.52668 ? 79  ARG B O   1 
ATOM   1674 C  CB  . ARG B 1 87  ? -1.64500  -5.14900  56.06500 1.000 11.35150 ? 79  ARG B CB  1 
ATOM   1675 C  CG  . ARG B 1 87  ? -1.27300  -6.60000  55.80400 1.000 10.45837 ? 79  ARG B CG  1 
ATOM   1676 C  CD  . ARG B 1 87  ? 0.23800   -6.82600  55.85300 1.000 12.05628 ? 79  ARG B CD  1 
ATOM   1677 N  NE  . ARG B 1 87  ? 0.89600   -6.50900  54.59100 1.000 10.70211 ? 79  ARG B NE  1 
ATOM   1678 C  CZ  . ARG B 1 87  ? 2.14100   -6.86300  54.30000 1.000 12.16556 ? 79  ARG B CZ  1 
ATOM   1679 N  NH1 . ARG B 1 87  ? 2.89100   -7.52400  55.17100 1.000 10.10184 ? 79  ARG B NH1 1 
ATOM   1680 N  NH2 . ARG B 1 87  ? 2.64000   -6.56500  53.10200 1.000 10.47334 ? 79  ARG B NH2 1 
ATOM   1681 N  N   . HIS B 1 88  ? -2.85300  -3.90800  53.51300 1.000 10.02212 ? 80  HIS B N   1 
ATOM   1682 C  CA  . HIS B 1 88  ? -2.70900  -4.00100  52.07500 1.000 11.47971 ? 80  HIS B CA  1 
ATOM   1683 C  C   . HIS B 1 88  ? -1.46700  -4.82600  51.76200 1.000 7.80933  ? 80  HIS B C   1 
ATOM   1684 O  O   . HIS B 1 88  ? -0.54900  -4.93400  52.57600 1.000 10.68397 ? 80  HIS B O   1 
ATOM   1685 C  CB  . HIS B 1 88  ? -2.58800  -2.60800  51.45000 1.000 10.08266 ? 80  HIS B CB  1 
ATOM   1686 C  CG  . HIS B 1 88  ? -3.73100  -1.68700  51.76700 1.000 9.94395  ? 80  HIS B CG  1 
ATOM   1687 N  ND1 . HIS B 1 88  ? -3.55400  -0.34900  52.05400 1.000 12.79599 ? 80  HIS B ND1 1 
ATOM   1688 C  CD2 . HIS B 1 88  ? -5.06700  -1.90200  51.81000 1.000 11.00173 ? 80  HIS B CD2 1 
ATOM   1689 C  CE1 . HIS B 1 88  ? -4.72700  0.21600   52.27400 1.000 9.80683  ? 80  HIS B CE1 1 
ATOM   1690 N  NE2 . HIS B 1 88  ? -5.66400  -0.70400  52.12600 1.000 10.45892 ? 80  HIS B NE2 1 
ATOM   1691 N  N   . VAL B 1 89  ? -1.44800  -5.43100  50.57500 1.000 9.13255  ? 81  VAL B N   1 
ATOM   1692 C  CA  . VAL B 1 89  ? -0.26000  -6.17600  50.17000 1.000 9.91848  ? 81  VAL B CA  1 
ATOM   1693 C  C   . VAL B 1 89  ? 0.95900   -5.26400  50.16800 1.000 8.04706  ? 81  VAL B C   1 
ATOM   1694 O  O   . VAL B 1 89  ? 2.06400   -5.67700  50.53800 1.000 11.03724 ? 81  VAL B O   1 
ATOM   1695 C  CB  . VAL B 1 89  ? -0.48000  -6.84200  48.80000 1.000 11.53851 ? 81  VAL B CB  1 
ATOM   1696 C  CG1 . VAL B 1 89  ? 0.83800   -7.35600  48.23400 1.000 10.70289 ? 81  VAL B CG1 1 
ATOM   1697 C  CG2 . VAL B 1 89  ? -1.47600  -7.98800  48.93500 1.000 14.51981 ? 81  VAL B CG2 1 
ATOM   1698 N  N   . GLY B 1 90  ? 0.78000   -4.00800  49.76900 1.000 8.43243  ? 82  GLY B N   1 
ATOM   1699 C  CA  . GLY B 1 90  ? 1.91900   -3.12100  49.67300 1.000 10.20661 ? 82  GLY B CA  1 
ATOM   1700 C  C   . GLY B 1 90  ? 2.37500   -2.46900  50.96100 1.000 11.82739 ? 82  GLY B C   1 
ATOM   1701 O  O   . GLY B 1 90  ? 3.20100   -1.55300  50.91400 1.000 10.73267 ? 82  GLY B O   1 
ATOM   1702 N  N   . ASP B 1 91  ? 1.88400   -2.91400  52.11700 1.000 10.32867 ? 83  ASP B N   1 
ATOM   1703 C  CA  . ASP B 1 91  ? 2.14400   -2.23000  53.38600 1.000 8.01501  ? 83  ASP B CA  1 
ATOM   1704 C  C   . ASP B 1 91  ? 3.41500   -2.78400  54.01600 1.000 10.67094 ? 83  ASP B C   1 
ATOM   1705 O  O   . ASP B 1 91  ? 3.38600   -3.81300  54.69500 1.000 9.65722  ? 83  ASP B O   1 
ATOM   1706 C  CB  . ASP B 1 91  ? 0.95600   -2.38300  54.32600 1.000 8.31353  ? 83  ASP B CB  1 
ATOM   1707 C  CG  . ASP B 1 91  ? -0.23700  -1.57100  53.88200 1.000 9.97199  ? 83  ASP B CG  1 
ATOM   1708 O  OD1 . ASP B 1 91  ? -0.04900  -0.64700  53.06700 1.000 12.19873 ? 83  ASP B OD1 1 
ATOM   1709 O  OD2 . ASP B 1 91  ? -1.35600  -1.85100  54.35200 1.000 10.19855 ? 83  ASP B OD2 1 
ATOM   1710 N  N   . LEU B 1 92  ? 4.53600   -2.09100  53.80900 1.000 8.94943  ? 84  LEU B N   1 
ATOM   1711 C  CA  . LEU B 1 92  ? 5.81800   -2.50300  54.36800 1.000 12.20086 ? 84  LEU B CA  1 
ATOM   1712 C  C   . LEU B 1 92  ? 6.25400   -1.63900  55.55500 1.000 13.32185 ? 84  LEU B C   1 
ATOM   1713 O  O   . LEU B 1 92  ? 7.43500   -1.64100  55.91300 1.000 12.12373 ? 84  LEU B O   1 
ATOM   1714 C  CB  . LEU B 1 92  ? 6.89200   -2.50200  53.27800 1.000 11.57651 ? 84  LEU B CB  1 
ATOM   1715 C  CG  . LEU B 1 92  ? 6.70500   -3.52700  52.14600 1.000 11.96640 ? 84  LEU B CG  1 
ATOM   1716 C  CD1 . LEU B 1 92  ? 7.83000   -3.43400  51.12300 1.000 8.46909  ? 84  LEU B CD1 1 
ATOM   1717 C  CD2 . LEU B 1 92  ? 6.58100   -4.95500  52.68700 1.000 12.32375 ? 84  LEU B CD2 1 
ATOM   1718 N  N   . GLY B 1 93  ? 5.33300   -0.90000  56.16500 1.000 10.39981 ? 85  GLY B N   1 
ATOM   1719 C  CA  . GLY B 1 93  ? 5.61800   -0.25000  57.43100 1.000 13.93963 ? 85  GLY B CA  1 
ATOM   1720 C  C   . GLY B 1 93  ? 6.46300   1.00300   57.33300 1.000 18.06645 ? 85  GLY B C   1 
ATOM   1721 O  O   . GLY B 1 93  ? 6.22100   1.85200   56.46900 1.000 13.09950 ? 85  GLY B O   1 
ATOM   1722 N  N   . ASN B 1 94  ? 7.45200   1.13200   58.22000 1.000 11.68887 ? 86  ASN B N   1 
ATOM   1723 C  CA  . ASN B 1 94  ? 8.31500   2.30200   58.27600 1.000 13.40717 ? 86  ASN B CA  1 
ATOM   1724 C  C   . ASN B 1 94  ? 9.77400   1.90700   58.11300 1.000 12.28149 ? 86  ASN B C   1 
ATOM   1725 O  O   . ASN B 1 94  ? 10.21200  0.87100   58.62300 1.000 16.31653 ? 86  ASN B O   1 
ATOM   1726 C  CB  . ASN B 1 94  ? 8.15300   3.06400   59.60600 1.000 12.35413 ? 86  ASN B CB  1 
ATOM   1727 C  CG  . ASN B 1 94  ? 6.83700   3.80800   59.70100 1.000 11.70679 ? 86  ASN B CG  1 
ATOM   1728 O  OD1 . ASN B 1 94  ? 6.60900   4.79100   58.99500 1.000 13.21917 ? 86  ASN B OD1 1 
ATOM   1729 N  ND2 . ASN B 1 94  ? 5.97000   3.35300   60.59300 1.000 14.40385 ? 86  ASN B ND2 1 
ATOM   1730 N  N   . VAL B 1 95  ? 10.51800  2.74500   57.40600 1.000 13.06717 ? 87  VAL B N   1 
ATOM   1731 C  CA  . VAL B 1 95  ? 11.97300  2.73900   57.45100 1.000 15.24577 ? 87  VAL B CA  1 
ATOM   1732 C  C   . VAL B 1 95  ? 12.40800  3.86500   58.38100 1.000 17.91106 ? 87  VAL B C   1 
ATOM   1733 O  O   . VAL B 1 95  ? 11.67800  4.84100   58.58600 1.000 16.33640 ? 87  VAL B O   1 
ATOM   1734 C  CB  . VAL B 1 95  ? 12.57400  2.88300   56.03700 1.000 14.37399 ? 87  VAL B CB  1 
ATOM   1735 C  CG1 . VAL B 1 95  ? 12.13100  1.71200   55.16600 1.000 16.68843 ? 87  VAL B CG1 1 
ATOM   1736 C  CG2 . VAL B 1 95  ? 12.16100  4.20600   55.41400 1.000 14.45633 ? 87  VAL B CG2 1 
ATOM   1737 N  N   . THR B 1 96  ? 13.59100  3.72300   58.97800 1.000 14.71796 ? 88  THR B N   1 
ATOM   1738 C  CA  . THR B 1 96  ? 14.05700  4.63900   60.01400 1.000 14.04807 ? 88  THR B CA  1 
ATOM   1739 C  C   . THR B 1 96  ? 15.34000  5.31300   59.55600 1.000 16.32132 ? 88  THR B C   1 
ATOM   1740 O  O   . THR B 1 96  ? 16.34300  4.63600   59.31000 1.000 15.67519 ? 88  THR B O   1 
ATOM   1741 C  CB  . THR B 1 96  ? 14.30600  3.90600   61.33600 1.000 20.17766 ? 88  THR B CB  1 
ATOM   1742 O  OG1 . THR B 1 96  ? 13.10100  3.26700   61.76900 1.000 18.46779 ? 88  THR B OG1 1 
ATOM   1743 C  CG2 . THR B 1 96  ? 14.76300  4.88800   62.40000 1.000 21.48027 ? 88  THR B CG2 1 
ATOM   1744 N  N   . ALA B 1 97  ? 15.31200  6.64200   59.47900 1.000 21.72120 ? 89  ALA B N   1 
ATOM   1745 C  CA  . ALA B 1 97  ? 16.46600  7.43800   59.08600 1.000 21.14821 ? 89  ALA B CA  1 
ATOM   1746 C  C   . ALA B 1 97  ? 17.18400  7.95100   60.32500 1.000 20.86819 ? 89  ALA B C   1 
ATOM   1747 O  O   . ALA B 1 97  ? 16.54700  8.47200   61.24700 1.000 23.82160 ? 89  ALA B O   1 
ATOM   1748 C  CB  . ALA B 1 97  ? 16.04100  8.61300   58.20400 1.000 18.91382 ? 89  ALA B CB  1 
ATOM   1749 N  N   . ASP B 1 98  ? 18.50700  7.81500   60.33400 1.000 25.46960 ? 90  ASP B N   1 
ATOM   1750 C  CA  . ASP B 1 98  ? 19.32800  8.35700   61.40500 1.000 28.48233 ? 90  ASP B CA  1 
ATOM   1751 C  C   . ASP B 1 98  ? 19.34300  9.88400   61.35300 1.000 28.63288 ? 90  ASP B C   1 
ATOM   1752 O  O   . ASP B 1 98  ? 18.66900  10.52300  60.53800 1.000 20.49256 ? 90  ASP B O   1 
ATOM   1753 C  CB  . ASP B 1 98  ? 20.74700  7.81000   61.31300 1.000 28.44188 ? 90  ASP B CB  1 
ATOM   1754 C  CG  . ASP B 1 98  ? 20.81400  6.34000   61.61400 1.000 35.74087 ? 90  ASP B CG  1 
ATOM   1755 O  OD1 . ASP B 1 98  ? 19.96000  5.86600   62.39200 1.000 42.60287 ? 90  ASP B OD1 1 
ATOM   1756 O  OD2 . ASP B 1 98  ? 21.71300  5.65800   61.07600 1.000 44.84756 ? 90  ASP B OD2 1 
ATOM   1757 N  N   . LYS B 1 99  ? 20.14200  10.47600  62.24300 1.000 25.92989 ? 91  LYS B N   1 
ATOM   1758 C  CA  . LYS B 1 99  ? 20.23000  11.92900  62.29000 1.000 25.16149 ? 91  LYS B CA  1 
ATOM   1759 C  C   . LYS B 1 99  ? 20.86900  12.48900  61.02700 1.000 25.56231 ? 91  LYS B C   1 
ATOM   1760 O  O   . LYS B 1 99  ? 20.52600  13.59800  60.60000 1.000 24.54396 ? 91  LYS B O   1 
ATOM   1761 C  CB  . LYS B 1 99  ? 21.00400  12.36500  63.53600 1.000 28.76847 ? 91  LYS B CB  1 
ATOM   1762 C  CG  . LYS B 1 99  ? 20.31300  11.98000  64.83600 1.000 35.21034 ? 91  LYS B CG  1 
ATOM   1763 C  CD  . LYS B 1 99  ? 21.02000  12.56000  66.05200 1.000 40.72243 ? 91  LYS B CD  1 
ATOM   1764 C  CE  . LYS B 1 99  ? 20.32200  12.14900  67.34400 1.000 39.09679 ? 91  LYS B CE  1 
ATOM   1765 N  NZ  . LYS B 1 99  ? 18.90200  12.60900  67.38800 1.000 33.33880 ? 91  LYS B NZ  1 
ATOM   1766 N  N   . ASP B 1 100 ? 21.77300  11.73700  60.40400 1.000 22.81876 ? 92  ASP B N   1 
ATOM   1767 C  CA  . ASP B 1 100 ? 22.38600  12.17000  59.15700 1.000 24.06406 ? 92  ASP B CA  1 
ATOM   1768 C  C   . ASP B 1 100 ? 21.46900  12.00100  57.95200 1.000 27.44583 ? 92  ASP B C   1 
ATOM   1769 O  O   . ASP B 1 100 ? 21.84500  12.41300  56.84900 1.000 26.35184 ? 92  ASP B O   1 
ATOM   1770 C  CB  . ASP B 1 100 ? 23.70200  11.42000  58.92400 1.000 22.94122 ? 92  ASP B CB  1 
ATOM   1771 C  CG  . ASP B 1 100 ? 23.51600  9.92000   58.74300 1.000 28.13278 ? 92  ASP B CG  1 
ATOM   1772 O  OD1 . ASP B 1 100 ? 22.37500  9.41500   58.82000 1.000 27.55492 ? 92  ASP B OD1 1 
ATOM   1773 O  OD2 . ASP B 1 100 ? 24.53300  9.23700   58.51600 1.000 26.81774 ? 92  ASP B OD2 1 
ATOM   1774 N  N   . GLY B 1 101 ? 20.28900  11.40900  58.12700 1.000 22.89895 ? 93  GLY B N   1 
ATOM   1775 C  CA  . GLY B 1 101 ? 19.32800  11.29300  57.05000 1.000 24.20904 ? 93  GLY B CA  1 
ATOM   1776 C  C   . GLY B 1 101 ? 19.37500  10.01000  56.25000 1.000 21.59756 ? 93  GLY B C   1 
ATOM   1777 O  O   . GLY B 1 101 ? 18.70000  9.92100   55.21600 1.000 19.79288 ? 93  GLY B O   1 
ATOM   1778 N  N   . VAL B 1 102 ? 20.13700  9.01300   56.68900 1.000 19.17794 ? 94  VAL B N   1 
ATOM   1779 C  CA  . VAL B 1 102 ? 20.26800  7.74900   55.97200 1.000 21.68494 ? 94  VAL B CA  1 
ATOM   1780 C  C   . VAL B 1 102 ? 19.41800  6.69800   56.67200 1.000 24.62284 ? 94  VAL B C   1 
ATOM   1781 O  O   . VAL B 1 102 ? 19.43600  6.58900   57.90600 1.000 21.66950 ? 94  VAL B O   1 
ATOM   1782 C  CB  . VAL B 1 102 ? 21.73800  7.30500   55.88500 1.000 20.43209 ? 94  VAL B CB  1 
ATOM   1783 C  CG1 . VAL B 1 102 ? 21.84600  5.93200   55.23800 1.000 17.32854 ? 94  VAL B CG1 1 
ATOM   1784 C  CG2 . VAL B 1 102 ? 22.55100  8.32800   55.10900 1.000 19.67715 ? 94  VAL B CG2 1 
ATOM   1785 N  N   . ALA B 1 103 ? 18.66800  5.92800   55.88800 1.000 19.61410 ? 95  ALA B N   1 
ATOM   1786 C  CA  . ALA B 1 103 ? 17.85200  4.83500   56.40000 1.000 18.58718 ? 95  ALA B CA  1 
ATOM   1787 C  C   . ALA B 1 103 ? 18.38900  3.52800   55.84500 1.000 18.07573 ? 95  ALA B C   1 
ATOM   1788 O  O   . ALA B 1 103 ? 18.42100  3.33400   54.62500 1.000 18.83807 ? 95  ALA B O   1 
ATOM   1789 C  CB  . ALA B 1 103 ? 16.38200  5.01700   56.01700 1.000 16.15844 ? 95  ALA B CB  1 
ATOM   1790 N  N   . ASP B 1 104 ? 18.81800  2.63900   56.73600 1.000 18.97554 ? 96  ASP B N   1 
ATOM   1791 C  CA  . ASP B 1 104 ? 19.17200  1.28000   56.35100 1.000 20.42201 ? 96  ASP B CA  1 
ATOM   1792 C  C   . ASP B 1 104 ? 17.90500  0.43200   56.30200 1.000 19.43390 ? 96  ASP B C   1 
ATOM   1793 O  O   . ASP B 1 104 ? 17.16700  0.35500   57.28900 1.000 21.46191 ? 96  ASP B O   1 
ATOM   1794 C  CB  . ASP B 1 104 ? 20.18500  0.69300   57.33200 1.000 26.66640 ? 96  ASP B CB  1 
ATOM   1795 C  CG  . ASP B 1 104 ? 21.61500  1.08400   57.00100 1.000 36.03034 ? 96  ASP B CG  1 
ATOM   1796 O  OD1 . ASP B 1 104 ? 21.85500  2.26700   56.68100 1.000 31.72912 ? 96  ASP B OD1 1 
ATOM   1797 O  OD2 . ASP B 1 104 ? 22.50000  0.20600   57.06600 1.000 50.10632 ? 96  ASP B OD2 1 
ATOM   1798 N  N   . VAL B 1 105 ? 17.64800  -0.19800  55.15900 1.000 17.77755 ? 97  VAL B N   1 
ATOM   1799 C  CA  . VAL B 1 105 ? 16.41700  -0.95200  54.94400 1.000 12.75499 ? 97  VAL B CA  1 
ATOM   1800 C  C   . VAL B 1 105 ? 16.73700  -2.43600  55.03100 1.000 18.87518 ? 97  VAL B C   1 
ATOM   1801 O  O   . VAL B 1 105 ? 17.56700  -2.94800  54.27200 1.000 16.99583 ? 97  VAL B O   1 
ATOM   1802 C  CB  . VAL B 1 105 ? 15.77100  -0.60400  53.59100 1.000 13.91830 ? 97  VAL B CB  1 
ATOM   1803 C  CG1 . VAL B 1 105 ? 14.51800  -1.44100  53.37400 1.000 16.95572 ? 97  VAL B CG1 1 
ATOM   1804 C  CG2 . VAL B 1 105 ? 15.45000  0.88500   53.50900 1.000 15.24222 ? 97  VAL B CG2 1 
ATOM   1805 N  N   . SER B 1 106 ? 16.07400  -3.12800  55.95400 1.000 18.03517 ? 98  SER B N   1 
ATOM   1806 C  CA  . SER B 1 106 ? 16.20500  -4.57500  56.09100 1.000 20.10255 ? 98  SER B CA  1 
ATOM   1807 C  C   . SER B 1 106 ? 14.84500  -5.12000  56.50000 1.000 19.26514 ? 98  SER B C   1 
ATOM   1808 O  O   . SER B 1 106 ? 14.42700  -4.94700  57.65000 1.000 23.61281 ? 98  SER B O   1 
ATOM   1809 C  CB  . SER B 1 106 ? 17.27600  -4.94600  57.11500 1.000 24.20751 ? 98  SER B CB  1 
ATOM   1810 O  OG  . SER B 1 106 ? 17.40400  -6.35300  57.22100 1.000 28.23255 ? 98  SER B OG  1 
ATOM   1811 N  N   . ILE B 1 107 ? 14.15400  -5.76300  55.56400 1.000 17.28529 ? 99  ILE B N   1 
ATOM   1812 C  CA  . ILE B 1 107 ? 12.79000  -6.23600  55.76900 1.000 19.17805 ? 99  ILE B CA  1 
ATOM   1813 C  C   . ILE B 1 107 ? 12.67700  -7.65500  55.22900 1.000 18.45830 ? 99  ILE B C   1 
ATOM   1814 O  O   . ILE B 1 107 ? 13.25800  -7.98600  54.19000 1.000 16.78734 ? 99  ILE B O   1 
ATOM   1815 C  CB  . ILE B 1 107 ? 11.76300  -5.30700  55.08000 1.000 16.96159 ? 99  ILE B CB  1 
ATOM   1816 C  CG1 . ILE B 1 107 ? 11.77400  -3.91900  55.71900 1.000 18.79988 ? 99  ILE B CG1 1 
ATOM   1817 C  CG2 . ILE B 1 107 ? 10.35600  -5.87900  55.15900 1.000 19.41221 ? 99  ILE B CG2 1 
ATOM   1818 C  CD1 . ILE B 1 107 ? 11.00700  -2.88300  54.91600 1.000 18.64063 ? 99  ILE B CD1 1 
ATOM   1819 N  N   . GLU B 1 108 ? 11.94200  -8.49800  55.94400 1.000 15.66739 ? 100 GLU B N   1 
ATOM   1820 C  CA  . GLU B 1 108 ? 11.47300  -9.77000  55.41900 1.000 15.61061 ? 100 GLU B CA  1 
ATOM   1821 C  C   . GLU B 1 108 ? 9.95400   -9.76900  55.51800 1.000 19.52378 ? 100 GLU B C   1 
ATOM   1822 O  O   . GLU B 1 108 ? 9.40500   -9.47400  56.58500 1.000 16.08592 ? 100 GLU B O   1 
ATOM   1823 C  CB  . GLU B 1 108 ? 12.07800  -10.94300 56.19200 1.000 19.20243 ? 100 GLU B CB  1 
ATOM   1824 C  CG  . GLU B 1 108 ? 11.86700  -12.28400 55.54100 1.000 21.98628 ? 100 GLU B CG  1 
ATOM   1825 C  CD  . GLU B 1 108 ? 12.82800  -13.33500 56.06500 1.000 26.94049 ? 100 GLU B CD  1 
ATOM   1826 O  OE1 . GLU B 1 108 ? 13.85800  -12.96200 56.66400 1.000 39.28497 ? 100 GLU B OE1 1 
ATOM   1827 O  OE2 . GLU B 1 108 ? 12.55500  -14.53400 55.87400 1.000 33.16788 ? 100 GLU B OE2 1 
ATOM   1828 N  N   . ASP B 1 109 ? 9.27300   -10.05800 54.40600 1.000 14.29578 ? 101 ASP B N   1 
ATOM   1829 C  CA  . ASP B 1 109 ? 7.81900   -9.96600  54.37200 1.000 14.87498 ? 101 ASP B CA  1 
ATOM   1830 C  C   . ASP B 1 109 ? 7.20300   -11.20100 53.73300 1.000 15.78816 ? 101 ASP B C   1 
ATOM   1831 O  O   . ASP B 1 109 ? 7.73300   -11.74200 52.75800 1.000 13.53824 ? 101 ASP B O   1 
ATOM   1832 C  CB  . ASP B 1 109 ? 7.34500   -8.72500  53.61500 1.000 16.03936 ? 101 ASP B CB  1 
ATOM   1833 C  CG  . ASP B 1 109 ? 5.88500   -8.41700  53.87700 1.000 17.30129 ? 101 ASP B CG  1 
ATOM   1834 O  OD1 . ASP B 1 109 ? 5.56000   -8.02300  55.02200 1.000 16.79785 ? 101 ASP B OD1 1 
ATOM   1835 O  OD2 . ASP B 1 109 ? 5.06400   -8.57800  52.95000 1.000 12.49819 ? 101 ASP B OD2 1 
ATOM   1836 N  N   . SER B 1 110 ? 6.05700   -11.61700 54.27700 1.000 16.20850 ? 102 SER B N   1 
ATOM   1837 C  CA  . SER B 1 110 ? 5.36800   -12.82300 53.84400 1.000 13.70766 ? 102 SER B CA  1 
ATOM   1838 C  C   . SER B 1 110 ? 4.19900   -12.56000 52.90200 1.000 15.85356 ? 102 SER B C   1 
ATOM   1839 O  O   . SER B 1 110 ? 3.62900   -13.52200 52.37900 1.000 16.38627 ? 102 SER B O   1 
ATOM   1840 C  CB  . SER B 1 110 ? 4.85600   -13.59700 55.06500 1.000 18.80664 ? 102 SER B CB  1 
ATOM   1841 O  OG  . SER B 1 110 ? 5.92000   -13.91100 55.94300 1.000 20.31619 ? 102 SER B OG  1 
ATOM   1842 N  N   . VAL B 1 111 ? 3.82300   -11.30400 52.66700 1.000 11.58929 ? 103 VAL B N   1 
ATOM   1843 C  CA  . VAL B 1 111 ? 2.62000   -10.98800 51.91100 1.000 12.71579 ? 103 VAL B CA  1 
ATOM   1844 C  C   . VAL B 1 111 ? 2.94600   -10.51500 50.49900 1.000 14.76497 ? 103 VAL B C   1 
ATOM   1845 O  O   . VAL B 1 111 ? 2.30600   -10.94900 49.53700 1.000 13.48951 ? 103 VAL B O   1 
ATOM   1846 C  CB  . VAL B 1 111 ? 1.74700   -9.95700  52.66200 1.000 11.36437 ? 103 VAL B CB  1 
ATOM   1847 C  CG1 . VAL B 1 111 ? 0.46700   -9.67700  51.89500 1.000 11.74245 ? 103 VAL B CG1 1 
ATOM   1848 C  CG2 . VAL B 1 111 ? 1.41100   -10.47300 54.05900 1.000 12.33688 ? 103 VAL B CG2 1 
ATOM   1849 N  N   . ILE B 1 112 ? 3.94200   -9.63400  50.34400 1.000 9.68732  ? 104 ILE B N   1 
ATOM   1850 C  CA  . ILE B 1 112 ? 4.41400   -9.33600  49.00000 1.000 10.69748 ? 104 ILE B CA  1 
ATOM   1851 C  C   . ILE B 1 112 ? 5.03800   -10.59200 48.38800 1.000 10.54319 ? 104 ILE B C   1 
ATOM   1852 O  O   . ILE B 1 112 ? 5.38300   -11.55900 49.08200 1.000 13.67831 ? 104 ILE B O   1 
ATOM   1853 C  CB  . ILE B 1 112 ? 5.41900   -8.17200  48.99000 1.000 8.18818  ? 104 ILE B CB  1 
ATOM   1854 C  CG1 . ILE B 1 112 ? 6.68400   -8.55100  49.75900 1.000 11.83657 ? 104 ILE B CG1 1 
ATOM   1855 C  CG2 . ILE B 1 112 ? 4.78900   -6.92300  49.56300 1.000 12.14882 ? 104 ILE B CG2 1 
ATOM   1856 C  CD1 . ILE B 1 112 ? 7.82600   -7.55600  49.59300 1.000 15.93933 ? 104 ILE B CD1 1 
ATOM   1857 N  N   . SER B 1 113 ? 5.17100   -10.57400 47.06600 1.000 11.63943 ? 105 SER B N   1 
ATOM   1858 C  CA  . SER B 1 113 ? 5.81500   -11.66700 46.35000 1.000 14.69203 ? 105 SER B CA  1 
ATOM   1859 C  C   . SER B 1 113 ? 6.36500   -11.12700 45.04000 1.000 15.17604 ? 105 SER B C   1 
ATOM   1860 O  O   . SER B 1 113 ? 5.97900   -10.04800 44.58400 1.000 14.04024 ? 105 SER B O   1 
ATOM   1861 C  CB  . SER B 1 113 ? 4.84500   -12.82800 46.09800 1.000 16.85806 ? 105 SER B CB  1 
ATOM   1862 O  OG  . SER B 1 113 ? 5.51300   -13.94100 45.53000 1.000 18.77515 ? 105 SER B OG  1 
ATOM   1863 N  N   . LEU B 1 114 ? 7.28800   -11.88200 44.44800 1.000 12.98280 ? 106 LEU B N   1 
ATOM   1864 C  CA  . LEU B 1 114 ? 7.80900   -11.56500 43.12600 1.000 17.47676 ? 106 LEU B CA  1 
ATOM   1865 C  C   . LEU B 1 114 ? 7.17100   -12.41700 42.03600 1.000 19.65875 ? 106 LEU B C   1 
ATOM   1866 O  O   . LEU B 1 114 ? 7.65500   -12.42000 40.90000 1.000 21.17657 ? 106 LEU B O   1 
ATOM   1867 C  CB  . LEU B 1 114 ? 9.33200   -11.72000 43.10000 1.000 15.63710 ? 106 LEU B CB  1 
ATOM   1868 C  CG  . LEU B 1 114 ? 10.11800  -10.80800 44.04500 1.000 13.17585 ? 106 LEU B CG  1 
ATOM   1869 C  CD1 . LEU B 1 114 ? 11.61100  -10.97900 43.83400 1.000 15.89312 ? 106 LEU B CD1 1 
ATOM   1870 C  CD2 . LEU B 1 114 ? 9.71200   -9.34500  43.85800 1.000 14.53467 ? 106 LEU B CD2 1 
ATOM   1871 N  N   . SER B 1 115 ? 6.09600   -13.13100 42.36000 1.000 19.82066 ? 107 SER B N   1 
ATOM   1872 C  CA  . SER B 1 115 ? 5.35000   -13.94200 41.41000 1.000 22.49884 ? 107 SER B CA  1 
ATOM   1873 C  C   . SER B 1 115 ? 3.96600   -14.19000 41.99100 1.000 27.94572 ? 107 SER B C   1 
ATOM   1874 O  O   . SER B 1 115 ? 3.78600   -14.16900 43.21100 1.000 23.77549 ? 107 SER B O   1 
ATOM   1875 C  CB  . SER B 1 115 ? 6.05400   -15.27400 41.12200 1.000 22.66163 ? 107 SER B CB  1 
ATOM   1876 O  OG  . SER B 1 115 ? 6.29600   -15.99200 42.31800 1.000 28.54614 ? 107 SER B OG  1 
ATOM   1877 N  N   . GLY B 1 116 ? 2.99400   -14.41500 41.11200 1.000 22.92064 ? 108 GLY B N   1 
ATOM   1878 C  CA  . GLY B 1 116 ? 1.65600   -14.77300 41.54800 1.000 21.21845 ? 108 GLY B CA  1 
ATOM   1879 C  C   . GLY B 1 116 ? 0.74000   -13.57800 41.74500 1.000 21.85136 ? 108 GLY B C   1 
ATOM   1880 O  O   . GLY B 1 116 ? 1.00700   -12.45900 41.30300 1.000 21.68278 ? 108 GLY B O   1 
ATOM   1881 N  N   . ASP B 1 117 ? -0.37100  -13.84000 42.44400 1.000 28.23974 ? 109 ASP B N   1 
ATOM   1882 C  CA  . ASP B 1 117 ? -1.40400  -12.82600 42.65100 1.000 22.87647 ? 109 ASP B CA  1 
ATOM   1883 C  C   . ASP B 1 117 ? -0.84400  -11.54700 43.26900 1.000 23.82415 ? 109 ASP B C   1 
ATOM   1884 O  O   . ASP B 1 117 ? -1.29300  -10.44100 42.94600 1.000 25.50330 ? 109 ASP B O   1 
ATOM   1885 C  CB  . ASP B 1 117 ? -2.51000  -13.38100 43.55400 1.000 28.61428 ? 109 ASP B CB  1 
ATOM   1886 C  CG  . ASP B 1 117 ? -3.02000  -14.74000 43.10900 1.000 32.48302 ? 109 ASP B CG  1 
ATOM   1887 O  OD1 . ASP B 1 117 ? -2.70200  -15.16900 41.98100 1.000 28.91925 ? 109 ASP B OD1 1 
ATOM   1888 O  OD2 . ASP B 1 117 ? -3.74300  -15.38300 43.90400 1.000 32.63422 ? 109 ASP B OD2 1 
ATOM   1889 N  N   . HIS B 1 118 ? 0.12200   -11.67500 44.16900 1.000 19.79147 ? 110 HIS B N   1 
ATOM   1890 C  CA  . HIS B 1 118 ? 0.56900   -10.53500 44.96100 1.000 17.13786 ? 110 HIS B CA  1 
ATOM   1891 C  C   . HIS B 1 118 ? 1.93900   -10.05700 44.51100 1.000 18.84611 ? 110 HIS B C   1 
ATOM   1892 O  O   . HIS B 1 118 ? 2.68100   -9.43600  45.27300 1.000 16.56024 ? 110 HIS B O   1 
ATOM   1893 C  CB  . HIS B 1 118 ? 0.57600   -10.91100 46.44000 1.000 19.43490 ? 110 HIS B CB  1 
ATOM   1894 C  CG  . HIS B 1 118 ? -0.65900  -11.64200 46.86200 1.000 24.82230 ? 110 HIS B CG  1 
ATOM   1895 N  ND1 . HIS B 1 118 ? -0.70000  -13.01300 47.00100 1.000 30.80061 ? 110 HIS B ND1 1 
ATOM   1896 C  CD2 . HIS B 1 118 ? -1.91100  -11.20000 47.12200 1.000 23.37390 ? 110 HIS B CD2 1 
ATOM   1897 C  CE1 . HIS B 1 118 ? -1.91800  -13.38000 47.35600 1.000 23.78310 ? 110 HIS B CE1 1 
ATOM   1898 N  NE2 . HIS B 1 118 ? -2.67100  -12.29900 47.43900 1.000 22.94048 ? 110 HIS B NE2 1 
HETATM 1899 N  N   . CSO B 1 119 ? 2.25300   -10.35400 43.25600 1.000 21.21372 ? 111 CSO B N   1 
HETATM 1900 C  CA  . CSO B 1 119 ? 3.53100   -9.99600  42.66800 1.000 18.91174 ? 111 CSO B CA  1 
HETATM 1901 C  CB  . CSO B 1 119 ? 3.66200   -10.63400 41.28200 1.000 18.73498 ? 111 CSO B CB  1 
HETATM 1902 S  SG  . CSO B 1 119 ? 4.96700   -9.86300  40.31100 1.000 22.55326 ? 111 CSO B SG  1 
HETATM 1903 C  C   . CSO B 1 119 ? 3.61900   -8.46900  42.60500 1.000 16.47974 ? 111 CSO B C   1 
HETATM 1904 O  O   . CSO B 1 119 ? 2.65000   -7.81300  42.22600 1.000 16.09231 ? 111 CSO B O   1 
HETATM 1905 O  OD  . CSO B 1 119 ? 5.54800   -10.98500 39.05100 1.000 27.26089 ? 111 CSO B OD  1 
ATOM   1906 N  N   . ILE B 1 120 ? 4.76300   -7.90400  42.99400 1.000 13.41421 ? 112 ILE B N   1 
ATOM   1907 C  CA  . ILE B 1 120 ? 4.90500   -6.44800  43.07100 1.000 16.78923 ? 112 ILE B CA  1 
ATOM   1908 C  C   . ILE B 1 120 ? 5.76600   -5.87300  41.95300 1.000 13.43401 ? 112 ILE B C   1 
ATOM   1909 O  O   . ILE B 1 120 ? 5.96700   -4.66200  41.88500 1.000 13.85060 ? 112 ILE B O   1 
ATOM   1910 C  CB  . ILE B 1 120 ? 5.48700   -6.01100  44.43500 1.000 13.32563 ? 112 ILE B CB  1 
ATOM   1911 C  CG1 . ILE B 1 120 ? 6.84800   -6.67700  44.66600 1.000 18.12567 ? 112 ILE B CG1 1 
ATOM   1912 C  CG2 . ILE B 1 120 ? 4.50200   -6.30800  45.55600 1.000 12.82722 ? 112 ILE B CG2 1 
ATOM   1913 C  CD1 . ILE B 1 120 ? 7.64200   -6.09000  45.81800 1.000 16.37742 ? 112 ILE B CD1 1 
ATOM   1914 N  N   . ILE B 1 121 ? 6.29400   -6.73100  41.08000 1.000 16.84213 ? 113 ILE B N   1 
ATOM   1915 C  CA  . ILE B 1 121 ? 7.06600   -6.23500  39.94800 1.000 16.22756 ? 113 ILE B CA  1 
ATOM   1916 C  C   . ILE B 1 121 ? 6.14400   -5.45300  39.02500 1.000 15.80019 ? 113 ILE B C   1 
ATOM   1917 O  O   . ILE B 1 121 ? 5.00500   -5.86200  38.76000 1.000 16.73551 ? 113 ILE B O   1 
ATOM   1918 C  CB  . ILE B 1 121 ? 7.76200   -7.39400  39.21600 1.000 16.36061 ? 113 ILE B CB  1 
ATOM   1919 C  CG1 . ILE B 1 121 ? 8.88100   -7.95900  40.09400 1.000 15.98792 ? 113 ILE B CG1 1 
ATOM   1920 C  CG2 . ILE B 1 121 ? 8.31000   -6.93000  37.87400 1.000 16.30043 ? 113 ILE B CG2 1 
ATOM   1921 C  CD1 . ILE B 1 121 ? 9.39700   -9.30400  39.64500 1.000 19.10973 ? 113 ILE B CD1 1 
ATOM   1922 N  N   . GLY B 1 122 ? 6.61900   -4.29900  38.56000 1.000 14.07051 ? 114 GLY B N   1 
ATOM   1923 C  CA  . GLY B 1 122 ? 5.80200   -3.40000  37.78100 1.000 13.16698 ? 114 GLY B CA  1 
ATOM   1924 C  C   . GLY B 1 122 ? 5.02900   -2.38700  38.59500 1.000 11.84452 ? 114 GLY B C   1 
ATOM   1925 O  O   . GLY B 1 122 ? 4.42000   -1.48700  38.00900 1.000 10.02847 ? 114 GLY B O   1 
ATOM   1926 N  N   . ARG B 1 123 ? 5.03100   -2.50600  39.92400 1.000 11.87939 ? 115 ARG B N   1 
ATOM   1927 C  CA  . ARG B 1 123 ? 4.37000   -1.54700  40.79600 1.000 10.40868 ? 115 ARG B CA  1 
ATOM   1928 C  C   . ARG B 1 123 ? 5.37500   -0.47600  41.22300 1.000 10.59371 ? 115 ARG B C   1 
ATOM   1929 O  O   . ARG B 1 123 ? 6.55900   -0.53600  40.89000 1.000 11.24587 ? 115 ARG B O   1 
ATOM   1930 C  CB  . ARG B 1 123 ? 3.75100   -2.26600  41.99400 1.000 10.53874 ? 115 ARG B CB  1 
ATOM   1931 C  CG  . ARG B 1 123 ? 2.79600   -3.41300  41.61800 1.000 14.87915 ? 115 ARG B CG  1 
ATOM   1932 C  CD  . ARG B 1 123 ? 1.51200   -2.90600  40.95600 1.000 15.34085 ? 115 ARG B CD  1 
ATOM   1933 N  NE  . ARG B 1 123 ? 0.67300   -3.99800  40.47100 1.000 12.13456 ? 115 ARG B NE  1 
ATOM   1934 C  CZ  . ARG B 1 123 ? -0.58300  -3.86000  40.06300 1.000 18.05090 ? 115 ARG B CZ  1 
ATOM   1935 N  NH1 . ARG B 1 123 ? -1.18200  -2.67900  40.04500 1.000 15.90831 ? 115 ARG B NH1 1 
ATOM   1936 N  NH2 . ARG B 1 123 ? -1.25900  -4.93600  39.66900 1.000 20.35071 ? 115 ARG B NH2 1 
ATOM   1937 N  N   . THR B 1 124 ? 4.90400   0.52700   41.95900 1.000 10.46722 ? 116 THR B N   1 
ATOM   1938 C  CA  . THR B 1 124 ? 5.72200   1.68000   42.32700 1.000 13.28456 ? 116 THR B CA  1 
ATOM   1939 C  C   . THR B 1 124 ? 5.98400   1.66100   43.82800 1.000 14.19178 ? 116 THR B C   1 
ATOM   1940 O  O   . THR B 1 124 ? 5.04100   1.68700   44.62500 1.000 12.68853 ? 116 THR B O   1 
ATOM   1941 C  CB  . THR B 1 124 ? 5.04500   2.98700   41.91200 1.000 14.94108 ? 116 THR B CB  1 
ATOM   1942 O  OG1 . THR B 1 124 ? 5.05100   3.08600   40.48200 1.000 13.10418 ? 116 THR B OG1 1 
ATOM   1943 C  CG2 . THR B 1 124 ? 5.77800   4.20000   42.48900 1.000 14.18598 ? 116 THR B CG2 1 
ATOM   1944 N  N   . LEU B 1 125 ? 7.26000   1.61200   44.20300 1.000 8.30309  ? 117 LEU B N   1 
ATOM   1945 C  CA  . LEU B 1 125 ? 7.67600   1.69400   45.59500 1.000 9.17975  ? 117 LEU B CA  1 
ATOM   1946 C  C   . LEU B 1 125 ? 7.87100   3.15400   45.98400 1.000 10.36685 ? 117 LEU B C   1 
ATOM   1947 O  O   . LEU B 1 125 ? 8.41500   3.94600   45.21100 1.000 13.63569 ? 117 LEU B O   1 
ATOM   1948 C  CB  . LEU B 1 125 ? 8.97300   0.91200   45.80900 1.000 10.62538 ? 117 LEU B CB  1 
ATOM   1949 C  CG  . LEU B 1 125 ? 9.54900   0.90000   47.22800 1.000 12.66908 ? 117 LEU B CG  1 
ATOM   1950 C  CD1 . LEU B 1 125 ? 8.71500   0.02000   48.14200 1.000 13.27436 ? 117 LEU B CD1 1 
ATOM   1951 C  CD2 . LEU B 1 125 ? 11.00500  0.44200   47.19900 1.000 10.09187 ? 117 LEU B CD2 1 
ATOM   1952 N  N   . VAL B 1 126 ? 7.42200   3.51000   47.18400 1.000 11.61113 ? 118 VAL B N   1 
ATOM   1953 C  CA  . VAL B 1 126 ? 7.37200   4.90400   47.61900 1.000 11.36635 ? 118 VAL B CA  1 
ATOM   1954 C  C   . VAL B 1 126 ? 7.90700   5.00200   49.04300 1.000 10.19137 ? 118 VAL B C   1 
ATOM   1955 O  O   . VAL B 1 126 ? 7.56600   4.18100   49.90000 1.000 11.86181 ? 118 VAL B O   1 
ATOM   1956 C  CB  . VAL B 1 126 ? 5.93000   5.45800   47.53900 1.000 10.65337 ? 118 VAL B CB  1 
ATOM   1957 C  CG1 . VAL B 1 126 ? 5.86200   6.89200   48.05300 1.000 16.97540 ? 118 VAL B CG1 1 
ATOM   1958 C  CG2 . VAL B 1 126 ? 5.39300   5.37400   46.10600 1.000 12.88666 ? 118 VAL B CG2 1 
ATOM   1959 N  N   . VAL B 1 127 ? 8.74600   6.00700   49.29700 1.000 11.34605 ? 119 VAL B N   1 
ATOM   1960 C  CA  . VAL B 1 127 ? 9.12600   6.39800   50.65300 1.000 12.55094 ? 119 VAL B CA  1 
ATOM   1961 C  C   . VAL B 1 127 ? 8.46600   7.73900   50.95600 1.000 13.38442 ? 119 VAL B C   1 
ATOM   1962 O  O   . VAL B 1 127 ? 8.45500   8.64400   50.11200 1.000 13.56632 ? 119 VAL B O   1 
ATOM   1963 C  CB  . VAL B 1 127 ? 10.66000  6.45100   50.83500 1.000 13.04146 ? 119 VAL B CB  1 
ATOM   1964 C  CG1 . VAL B 1 127 ? 11.30400  7.42300   49.87100 1.000 16.83013 ? 119 VAL B CG1 1 
ATOM   1965 C  CG2 . VAL B 1 127 ? 11.02500  6.78300   52.28100 1.000 15.67462 ? 119 VAL B CG2 1 
ATOM   1966 N  N   . HIS B 1 128 ? 7.89300   7.86000   52.14900 1.000 12.47291 ? 120 HIS B N   1 
ATOM   1967 C  CA  . HIS B 1 128 ? 6.93700   8.92300   52.42600 1.000 14.94961 ? 120 HIS B CA  1 
ATOM   1968 C  C   . HIS B 1 128 ? 7.49800   9.98800   53.36100 1.000 14.70014 ? 120 HIS B C   1 
ATOM   1969 O  O   . HIS B 1 128 ? 8.49800   9.78900   54.05600 1.000 16.35625 ? 120 HIS B O   1 
ATOM   1970 C  CB  . HIS B 1 128 ? 5.64400   8.35400   53.02000 1.000 14.70041 ? 120 HIS B CB  1 
ATOM   1971 C  CG  . HIS B 1 128 ? 4.70800   7.79700   51.99300 1.000 16.31508 ? 120 HIS B CG  1 
ATOM   1972 N  ND1 . HIS B 1 128 ? 3.76900   8.57100   51.34500 1.000 16.40463 ? 120 HIS B ND1 1 
ATOM   1973 C  CD2 . HIS B 1 128 ? 4.57400   6.54600   51.49300 1.000 16.16249 ? 120 HIS B CD2 1 
ATOM   1974 C  CE1 . HIS B 1 128 ? 3.09200   7.81900   50.49500 1.000 17.96505 ? 120 HIS B CE1 1 
ATOM   1975 N  NE2 . HIS B 1 128 ? 3.56500   6.58800   50.56100 1.000 18.79316 ? 120 HIS B NE2 1 
ATOM   1976 N  N   . GLU B 1 129 ? 6.79500   11.12700  53.36100 1.000 15.43757 ? 121 GLU B N   1 
ATOM   1977 C  CA  . GLU B 1 129 ? 7.17700   12.29600  54.14800 1.000 15.74658 ? 121 GLU B CA  1 
ATOM   1978 C  C   . GLU B 1 129 ? 7.14300   12.01100  55.64500 1.000 20.18837 ? 121 GLU B C   1 
ATOM   1979 O  O   . GLU B 1 129 ? 8.06400   12.39200  56.37800 1.000 16.21406 ? 121 GLU B O   1 
ATOM   1980 C  CB  . GLU B 1 129 ? 6.23200   13.45000  53.80500 1.000 18.21525 ? 121 GLU B CB  1 
ATOM   1981 C  CG  . GLU B 1 129 ? 6.40700   14.70900  54.62600 1.000 25.94794 ? 121 GLU B CG  1 
ATOM   1982 C  CD  . GLU B 1 129 ? 5.17800   15.60600  54.57800 1.000 29.44918 ? 121 GLU B CD  1 
ATOM   1983 O  OE1 . GLU B 1 129 ? 4.15200   15.19300  53.99200 1.000 23.56431 ? 121 GLU B OE1 1 
ATOM   1984 O  OE2 . GLU B 1 129 ? 5.23300   16.72300  55.13300 1.000 33.82392 ? 121 GLU B OE2 1 
ATOM   1985 N  N   . LYS B 1 130 ? 6.08800   11.35600  56.11900 1.000 17.80611 ? 122 LYS B N   1 
ATOM   1986 C  CA  . LYS B 1 130 ? 5.82900   11.17800  57.54200 1.000 15.49728 ? 122 LYS B CA  1 
ATOM   1987 C  C   . LYS B 1 130 ? 5.81600   9.69500   57.89400 1.000 16.22985 ? 122 LYS B C   1 
ATOM   1988 O  O   . LYS B 1 130 ? 5.89900   8.82200   57.02700 1.000 13.11776 ? 122 LYS B O   1 
ATOM   1989 C  CB  . LYS B 1 130 ? 4.49900   11.83000  57.93000 1.000 19.27653 ? 122 LYS B CB  1 
ATOM   1990 C  CG  . LYS B 1 130 ? 4.41700   13.30800  57.58400 1.000 20.12922 ? 122 LYS B CG  1 
ATOM   1991 C  CD  . LYS B 1 130 ? 5.46400   14.10600  58.34000 1.000 15.81898 ? 122 LYS B CD  1 
ATOM   1992 C  CE  . LYS B 1 130 ? 5.30200   15.59900  58.08000 1.000 21.97723 ? 122 LYS B CE  1 
ATOM   1993 N  NZ  . LYS B 1 130 ? 6.18100   16.43900  58.93800 1.000 24.44029 ? 122 LYS B NZ  1 
ATOM   1994 N  N   . ALA B 1 131 ? 5.69300   9.41800   59.18800 1.000 12.64287 ? 123 ALA B N   1 
ATOM   1995 C  CA  . ALA B 1 131 ? 5.63900   8.04100   59.64800 1.000 10.58535 ? 123 ALA B CA  1 
ATOM   1996 C  C   . ALA B 1 131 ? 4.30700   7.40100   59.27600 1.000 14.77866 ? 123 ALA B C   1 
ATOM   1997 O  O   . ALA B 1 131 ? 3.26200   8.05700   59.25600 1.000 13.10502 ? 123 ALA B O   1 
ATOM   1998 C  CB  . ALA B 1 131 ? 5.84100   7.97000   61.16300 1.000 14.56450 ? 123 ALA B CB  1 
ATOM   1999 N  N   . ASP B 1 132 ? 4.35900   6.11200   58.96900 1.000 12.59813 ? 124 ASP B N   1 
ATOM   2000 C  CA  . ASP B 1 132 ? 3.15200   5.30600   58.84800 1.000 14.32907 ? 124 ASP B CA  1 
ATOM   2001 C  C   . ASP B 1 132 ? 2.61000   5.01300   60.24600 1.000 13.18797 ? 124 ASP B C   1 
ATOM   2002 O  O   . ASP B 1 132 ? 3.32100   4.43300   61.07500 1.000 15.15173 ? 124 ASP B O   1 
ATOM   2003 C  CB  . ASP B 1 132 ? 3.49900   4.01400   58.10700 1.000 12.02856 ? 124 ASP B CB  1 
ATOM   2004 C  CG  . ASP B 1 132 ? 2.28400   3.20900   57.70400 1.000 17.15853 ? 124 ASP B CG  1 
ATOM   2005 O  OD1 . ASP B 1 132 ? 1.20700   3.38600   58.30500 1.000 13.51116 ? 124 ASP B OD1 1 
ATOM   2006 O  OD2 . ASP B 1 132 ? 2.41900   2.37700   56.77800 1.000 22.19522 ? 124 ASP B OD2 1 
ATOM   2007 N  N   . ASP B 1 133 ? 1.35900   5.40900   60.52500 1.000 13.56644 ? 125 ASP B N   1 
ATOM   2008 C  CA  . ASP B 1 133 ? 0.78300   5.08900   61.83100 1.000 15.91174 ? 125 ASP B CA  1 
ATOM   2009 C  C   . ASP B 1 133 ? 0.21400   3.67500   61.88500 1.000 13.94811 ? 125 ASP B C   1 
ATOM   2010 O  O   . ASP B 1 133 ? -0.40000  3.30300   62.89100 1.000 13.05696 ? 125 ASP B O   1 
ATOM   2011 C  CB  . ASP B 1 133 ? -0.27500  6.13300   62.25300 1.000 16.77605 ? 125 ASP B CB  1 
ATOM   2012 C  CG  . ASP B 1 133 ? -1.54300  6.12800   61.38900 1.000 16.87772 ? 125 ASP B CG  1 
ATOM   2013 O  OD1 . ASP B 1 133 ? -1.83500  5.14700   60.67700 1.000 15.20721 ? 125 ASP B OD1 1 
ATOM   2014 O  OD2 . ASP B 1 133 ? -2.27100  7.14200   61.43500 1.000 16.84255 ? 125 ASP B OD2 1 
ATOM   2015 N  N   . LEU B 1 134 ? 0.41300   2.89000   60.82200 1.000 16.49490 ? 126 LEU B N   1 
ATOM   2016 C  CA  . LEU B 1 134 ? 0.10600   1.46300   60.77200 1.000 13.07274 ? 126 LEU B CA  1 
ATOM   2017 C  C   . LEU B 1 134 ? -1.38000  1.17200   60.90100 1.000 14.13083 ? 126 LEU B C   1 
ATOM   2018 O  O   . LEU B 1 134 ? -1.76200  0.07300   61.31000 1.000 14.62448 ? 126 LEU B O   1 
ATOM   2019 C  CB  . LEU B 1 134 ? 0.88300   0.68900   61.84600 1.000 13.40184 ? 126 LEU B CB  1 
ATOM   2020 C  CG  . LEU B 1 134 ? 2.39500   0.94600   61.89400 1.000 12.88611 ? 126 LEU B CG  1 
ATOM   2021 C  CD1 . LEU B 1 134 ? 3.04900   0.07000   62.95700 1.000 17.08478 ? 126 LEU B CD1 1 
ATOM   2022 C  CD2 . LEU B 1 134 ? 3.03700   0.72000   60.52700 1.000 16.29402 ? 126 LEU B CD2 1 
ATOM   2023 N  N   . GLY B 1 135 ? -2.23100  2.12900   60.55000 1.000 12.05422 ? 127 GLY B N   1 
ATOM   2024 C  CA  . GLY B 1 135 ? -3.66000  1.92300   60.61600 1.000 12.53078 ? 127 GLY B CA  1 
ATOM   2025 C  C   . GLY B 1 135 ? -4.28600  2.17800   61.96500 1.000 13.86449 ? 127 GLY B C   1 
ATOM   2026 O  O   . GLY B 1 135 ? -5.48300  1.92100   62.12600 1.000 20.38606 ? 127 GLY B O   1 
ATOM   2027 N  N   . LYS B 1 136 ? -3.52800  2.69600   62.93500 1.000 14.34281 ? 128 LYS B N   1 
ATOM   2028 C  CA  . LYS B 1 136 ? -4.02300  2.91100   64.29100 1.000 18.61758 ? 128 LYS B CA  1 
ATOM   2029 C  C   . LYS B 1 136 ? -4.17200  4.39300   64.63500 1.000 22.73635 ? 128 LYS B C   1 
ATOM   2030 O  O   . LYS B 1 136 ? -4.13100  4.77100   65.80900 1.000 22.42537 ? 128 LYS B O   1 
ATOM   2031 C  CB  . LYS B 1 136 ? -3.10800  2.22500   65.30400 1.000 19.60534 ? 128 LYS B CB  1 
ATOM   2032 C  CG  . LYS B 1 136 ? -3.31600  0.72000   65.42300 1.000 27.49600 ? 128 LYS B CG  1 
ATOM   2033 C  CD  . LYS B 1 136 ? -2.52700  -0.02900  64.37300 1.000 30.62656 ? 128 LYS B CD  1 
ATOM   2034 C  CE  . LYS B 1 136 ? -2.37200  -1.50000  64.72500 1.000 32.14178 ? 128 LYS B CE  1 
ATOM   2035 N  NZ  . LYS B 1 136 ? -1.17300  -2.06300  64.04100 1.000 30.91959 ? 128 LYS B NZ  1 
ATOM   2036 N  N   . GLY B 1 137 ? -4.35300  5.24300   63.62400 1.000 20.80283 ? 129 GLY B N   1 
ATOM   2037 C  CA  . GLY B 1 137 ? -4.46900  6.67000   63.85500 1.000 15.74701 ? 129 GLY B CA  1 
ATOM   2038 C  C   . GLY B 1 137 ? -5.85000  7.15700   64.23100 1.000 18.42992 ? 129 GLY B C   1 
ATOM   2039 O  O   . GLY B 1 137 ? -5.99100  8.31000   64.64600 1.000 20.08780 ? 129 GLY B O   1 
ATOM   2040 N  N   . GLY B 1 138 ? -6.87400  6.32400   64.08300 1.000 18.18397 ? 130 GLY B N   1 
ATOM   2041 C  CA  . GLY B 1 138 ? -8.20000  6.68400   64.53400 1.000 18.55890 ? 130 GLY B CA  1 
ATOM   2042 C  C   . GLY B 1 138 ? -9.03200  7.50500   63.57200 1.000 19.43004 ? 130 GLY B C   1 
ATOM   2043 O  O   . GLY B 1 138 ? -10.14500 7.90200   63.93400 1.000 20.28593 ? 130 GLY B O   1 
ATOM   2044 N  N   . ASN B 1 139 ? -8.54300  7.77700   62.36700 1.000 18.91330 ? 131 ASN B N   1 
ATOM   2045 C  CA  . ASN B 1 139 ? -9.33200  8.46200   61.35200 1.000 17.50738 ? 131 ASN B CA  1 
ATOM   2046 C  C   . ASN B 1 139 ? -9.42900  7.58100   60.11300 1.000 17.41307 ? 131 ASN B C   1 
ATOM   2047 O  O   . ASN B 1 139 ? -8.74900  6.55900   60.00200 1.000 18.13197 ? 131 ASN B O   1 
ATOM   2048 C  CB  . ASN B 1 139 ? -8.74000  9.84400   61.01900 1.000 15.65703 ? 131 ASN B CB  1 
ATOM   2049 C  CG  . ASN B 1 139 ? -7.33500  9.77500   60.43800 1.000 18.63827 ? 131 ASN B CG  1 
ATOM   2050 O  OD1 . ASN B 1 139 ? -6.68800  8.73400   60.45000 1.000 17.61615 ? 131 ASN B OD1 1 
ATOM   2051 N  ND2 . ASN B 1 139 ? -6.85500  10.90600  59.93200 1.000 17.76341 ? 131 ASN B ND2 1 
ATOM   2052 N  N   . GLU B 1 140 ? -10.30100 7.97300   59.17700 1.000 15.86169 ? 132 GLU B N   1 
ATOM   2053 C  CA  . GLU B 1 140 ? -10.45600 7.17500   57.96400 1.000 20.03491 ? 132 GLU B CA  1 
ATOM   2054 C  C   . GLU B 1 140 ? -9.17700  7.14700   57.14700 1.000 20.39712 ? 132 GLU B C   1 
ATOM   2055 O  O   . GLU B 1 140 ? -8.85700  6.12300   56.53100 1.000 16.13341 ? 132 GLU B O   1 
ATOM   2056 C  CB  . GLU B 1 140 ? -11.60300 7.69500   57.09600 1.000 17.05494 ? 132 GLU B CB  1 
ATOM   2057 C  CG  . GLU B 1 140 ? -11.90000 6.74800   55.92900 1.000 21.81917 ? 132 GLU B CG  1 
ATOM   2058 C  CD  . GLU B 1 140 ? -13.05400 7.18800   55.05200 1.000 26.48638 ? 132 GLU B CD  1 
ATOM   2059 O  OE1 . GLU B 1 140 ? -13.17400 8.39700   54.76800 1.000 27.32964 ? 132 GLU B OE1 1 
ATOM   2060 O  OE2 . GLU B 1 140 ? -13.84000 6.30900   54.63500 1.000 31.08231 ? 132 GLU B OE2 1 
ATOM   2061 N  N   . GLU B 1 141 ? -8.43600  8.25600   57.13400 1.000 16.83356 ? 133 GLU B N   1 
ATOM   2062 C  CA  . GLU B 1 141 ? -7.20000  8.31100   56.36600 1.000 20.04401 ? 133 GLU B CA  1 
ATOM   2063 C  C   . GLU B 1 141 ? -6.18200  7.29800   56.86900 1.000 16.75004 ? 133 GLU B C   1 
ATOM   2064 O  O   . GLU B 1 141 ? -5.37700  6.78300   56.08500 1.000 14.72416 ? 133 GLU B O   1 
ATOM   2065 C  CB  . GLU B 1 141 ? -6.62400  9.72600   56.41700 1.000 21.30099 ? 133 GLU B CB  1 
ATOM   2066 C  CG  . GLU B 1 141 ? -5.49700  9.96600   55.43500 1.000 16.68742 ? 133 GLU B CG  1 
ATOM   2067 C  CD  . GLU B 1 141 ? -5.92200  9.71100   54.00300 1.000 24.00057 ? 133 GLU B CD  1 
ATOM   2068 O  OE1 . GLU B 1 141 ? -7.05100  10.10800  53.62900 1.000 23.86773 ? 133 GLU B OE1 1 
ATOM   2069 O  OE2 . GLU B 1 141 ? -5.13100  9.09600   53.26000 1.000 20.12182 ? 133 GLU B OE2 1 
ATOM   2070 N  N   . SER B 1 142 ? -6.20600  6.99000   58.16600 1.000 15.09562 ? 134 SER B N   1 
ATOM   2071 C  CA  . SER B 1 142 ? -5.28800  5.99200   58.70100 1.000 14.65071 ? 134 SER B CA  1 
ATOM   2072 C  C   . SER B 1 142 ? -5.51700  4.63300   58.05300 1.000 13.94837 ? 134 SER B C   1 
ATOM   2073 O  O   . SER B 1 142 ? -4.55800  3.90600   57.76600 1.000 12.17721 ? 134 SER B O   1 
ATOM   2074 C  CB  . SER B 1 142 ? -5.44100  5.89700   60.21900 1.000 15.30200 ? 134 SER B CB  1 
ATOM   2075 O  OG  . SER B 1 142 ? -4.52400  4.96800   60.76500 1.000 13.83190 ? 134 SER B OG  1 
ATOM   2076 N  N   . THR B 1 143 ? -6.77900  4.28300   57.79500 1.000 13.85603 ? 135 THR B N   1 
ATOM   2077 C  CA  . THR B 1 143 ? -7.14000  3.02600   57.14900 1.000 15.32411 ? 135 THR B CA  1 
ATOM   2078 C  C   . THR B 1 143 ? -6.87400  3.01700   55.65100 1.000 18.21162 ? 135 THR B C   1 
ATOM   2079 O  O   . THR B 1 143 ? -7.11400  1.98800   55.00900 1.000 15.13250 ? 135 THR B O   1 
ATOM   2080 C  CB  . THR B 1 143 ? -8.62000  2.71000   57.37800 1.000 18.57854 ? 135 THR B CB  1 
ATOM   2081 O  OG1 . THR B 1 143 ? -9.42300  3.55400   56.54100 1.000 17.30566 ? 135 THR B OG1 1 
ATOM   2082 C  CG2 . THR B 1 143 ? -8.99200  2.93900   58.82400 1.000 22.01977 ? 135 THR B CG2 1 
ATOM   2083 N  N   . LYS B 1 144 ? -6.40900  4.12700   55.07700 1.000 13.35564 ? 136 LYS B N   1 
ATOM   2084 C  CA  . LYS B 1 144 ? -6.02100  4.20000   53.67600 1.000 13.98134 ? 136 LYS B CA  1 
ATOM   2085 C  C   . LYS B 1 144 ? -4.51300  4.25300   53.48800 1.000 13.97078 ? 136 LYS B C   1 
ATOM   2086 O  O   . LYS B 1 144 ? -3.95100  3.43600   52.75300 1.000 15.09144 ? 136 LYS B O   1 
ATOM   2087 C  CB  . LYS B 1 144 ? -6.65000  5.43300   53.01300 1.000 16.80448 ? 136 LYS B CB  1 
ATOM   2088 C  CG  . LYS B 1 144 ? -8.16300  5.49000   53.07800 1.000 24.92123 ? 136 LYS B CG  1 
ATOM   2089 C  CD  . LYS B 1 144 ? -8.65600  6.85500   52.63200 1.000 27.24163 ? 136 LYS B CD  1 
ATOM   2090 C  CE  . LYS B 1 144 ? -10.13800 6.82400   52.31300 1.000 37.72551 ? 136 LYS B CE  1 
ATOM   2091 N  NZ  . LYS B 1 144 ? -10.43100 5.80600   51.26500 1.000 43.12813 ? 136 LYS B NZ  1 
ATOM   2092 N  N   . THR B 1 145 ? -3.84100  5.20200   54.14700 1.000 14.41767 ? 137 THR B N   1 
ATOM   2093 C  CA  . THR B 1 145 ? -2.43600  5.49200   53.90100 1.000 10.54991 ? 137 THR B CA  1 
ATOM   2094 C  C   . THR B 1 145 ? -1.58700  5.50800   55.16000 1.000 14.80860 ? 137 THR B C   1 
ATOM   2095 O  O   . THR B 1 145 ? -0.37800  5.75300   55.06700 1.000 15.76879 ? 137 THR B O   1 
ATOM   2096 C  CB  . THR B 1 145 ? -2.28700  6.85500   53.21500 1.000 15.59811 ? 137 THR B CB  1 
ATOM   2097 O  OG1 . THR B 1 145 ? -2.79500  7.87000   54.09200 1.000 15.08735 ? 137 THR B OG1 1 
ATOM   2098 C  CG2 . THR B 1 145 ? -3.05300  6.88200   51.89700 1.000 19.46841 ? 137 THR B CG2 1 
ATOM   2099 N  N   . GLY B 1 146 ? -2.18000  5.28500   56.33000 1.000 13.78395 ? 138 GLY B N   1 
ATOM   2100 C  CA  . GLY B 1 146 ? -1.44200  5.43000   57.56700 1.000 16.57637 ? 138 GLY B CA  1 
ATOM   2101 C  C   . GLY B 1 146 ? -0.99600  6.84400   57.86900 1.000 15.65192 ? 138 GLY B C   1 
ATOM   2102 O  O   . GLY B 1 146 ? -0.09500  7.03400   58.68900 1.000 14.30727 ? 138 GLY B O   1 
ATOM   2103 N  N   . ASN B 1 147 ? -1.59500  7.84200   57.21400 1.000 14.35326 ? 139 ASN B N   1 
ATOM   2104 C  CA  . ASN B 1 147 ? -1.24000  9.25100   57.40800 1.000 13.35147 ? 139 ASN B CA  1 
ATOM   2105 C  C   . ASN B 1 147 ? 0.25100   9.49500   57.16800 1.000 15.79151 ? 139 ASN B C   1 
ATOM   2106 O  O   . ASN B 1 147 ? 0.88900   10.30200  57.84600 1.000 15.64710 ? 139 ASN B O   1 
ATOM   2107 C  CB  . ASN B 1 147 ? -1.65600  9.73800   58.80100 1.000 13.07881 ? 139 ASN B CB  1 
ATOM   2108 C  CG  . ASN B 1 147 ? -3.16500  9.77000   58.98200 1.000 15.84083 ? 139 ASN B CG  1 
ATOM   2109 O  OD1 . ASN B 1 147 ? -3.86100  10.54100  58.32400 1.000 14.12205 ? 139 ASN B OD1 1 
ATOM   2110 N  ND2 . ASN B 1 147 ? -3.67500  8.94000   59.88300 1.000 14.82540 ? 139 ASN B ND2 1 
ATOM   2111 N  N   . ALA B 1 148 ? 0.81600   8.79600   56.18300 1.000 15.00162 ? 140 ALA B N   1 
ATOM   2112 C  CA  . ALA B 1 148 ? 2.24400   8.91800   55.91500 1.000 13.11206 ? 140 ALA B CA  1 
ATOM   2113 C  C   . ALA B 1 148 ? 2.58400   10.13400  55.06300 1.000 14.82448 ? 140 ALA B C   1 
ATOM   2114 O  O   . ALA B 1 148 ? 3.77000   10.42800  54.87900 1.000 14.66079 ? 140 ALA B O   1 
ATOM   2115 C  CB  . ALA B 1 148 ? 2.76800   7.64500   55.24500 1.000 11.95228 ? 140 ALA B CB  1 
ATOM   2116 N  N   . GLY B 1 149 ? 1.58800   10.84500  54.54300 1.000 14.29440 ? 141 GLY B N   1 
ATOM   2117 C  CA  . GLY B 1 149 ? 1.86200   12.10100  53.86600 1.000 19.58662 ? 141 GLY B CA  1 
ATOM   2118 C  C   . GLY B 1 149 ? 2.37400   11.93000  52.44500 1.000 17.74013 ? 141 GLY B C   1 
ATOM   2119 O  O   . GLY B 1 149 ? 2.09400   10.93900  51.76800 1.000 15.91260 ? 141 GLY B O   1 
ATOM   2120 N  N   . SER B 1 150 ? 3.15400   12.91400  52.00000 1.000 15.29682 ? 142 SER B N   1 
ATOM   2121 C  CA  . SER B 1 150 ? 3.51400   13.02900  50.59300 1.000 15.93067 ? 142 SER B CA  1 
ATOM   2122 C  C   . SER B 1 150 ? 4.59600   12.03700  50.19100 1.000 15.89935 ? 142 SER B C   1 
ATOM   2123 O  O   . SER B 1 150 ? 5.40700   11.59600  51.01100 1.000 17.47133 ? 142 SER B O   1 
ATOM   2124 C  CB  . SER B 1 150 ? 3.99700   14.44400  50.28200 1.000 18.69219 ? 142 SER B CB  1 
ATOM   2125 O  OG  . SER B 1 150 ? 3.08800   15.40700  50.77700 1.000 19.71120 ? 142 SER B OG  1 
ATOM   2126 N  N   . ARG B 1 151 ? 4.61400   11.70300  48.90100 1.000 16.52349 ? 143 ARG B N   1 
ATOM   2127 C  CA  . ARG B 1 151 ? 5.69500   10.89500  48.35500 1.000 15.39646 ? 143 ARG B CA  1 
ATOM   2128 C  C   . ARG B 1 151 ? 6.96700   11.72800  48.28400 1.000 14.66352 ? 143 ARG B C   1 
ATOM   2129 O  O   . ARG B 1 151 ? 6.96500   12.82600  47.72400 1.000 20.22082 ? 143 ARG B O   1 
ATOM   2130 C  CB  . ARG B 1 151 ? 5.32700   10.37700  46.96300 1.000 23.23989 ? 143 ARG B CB  1 
ATOM   2131 C  CG  . ARG B 1 151 ? 3.90700   9.84400   46.85000 1.000 29.01678 ? 143 ARG B CG  1 
ATOM   2132 C  CD  . ARG B 1 151 ? 3.64900   9.22000   45.48600 1.000 41.40972 ? 143 ARG B CD  1 
ATOM   2133 N  NE  . ARG B 1 151 ? 4.03500   10.10700  44.39300 1.000 51.19247 ? 143 ARG B NE  1 
ATOM   2134 C  CZ  . ARG B 1 151 ? 3.23900   11.01300  43.84200 1.000 57.37114 ? 143 ARG B CZ  1 
ATOM   2135 N  NH1 . ARG B 1 151 ? 1.99400   11.18800  44.26100 1.000 48.07686 ? 143 ARG B NH1 1 
ATOM   2136 N  NH2 . ARG B 1 151 ? 3.70200   11.76200  42.84500 1.000 57.92588 ? 143 ARG B NH2 1 
ATOM   2137 N  N   . LEU B 1 152 ? 8.05400   11.21100  48.85600 1.000 15.47424 ? 144 LEU B N   1 
ATOM   2138 C  CA  . LEU B 1 152 ? 9.34800   11.87900  48.76100 1.000 15.89873 ? 144 LEU B CA  1 
ATOM   2139 C  C   . LEU B 1 152 ? 10.16200  11.37400  47.58100 1.000 20.25197 ? 144 LEU B C   1 
ATOM   2140 O  O   . LEU B 1 152 ? 10.80000  12.16600  46.87700 1.000 18.54368 ? 144 LEU B O   1 
ATOM   2141 C  CB  . LEU B 1 152 ? 10.14900  11.68100  50.05000 1.000 15.35061 ? 144 LEU B CB  1 
ATOM   2142 C  CG  . LEU B 1 152 ? 9.53000   12.27500  51.31300 1.000 21.87945 ? 144 LEU B CG  1 
ATOM   2143 C  CD1 . LEU B 1 152 ? 10.44800  12.05600  52.49800 1.000 21.71808 ? 144 LEU B CD1 1 
ATOM   2144 C  CD2 . LEU B 1 152 ? 9.24200   13.75000  51.12600 1.000 18.73836 ? 144 LEU B CD2 1 
ATOM   2145 N  N   . ALA B 1 153 ? 10.16100  10.06300  47.36700 1.000 12.48615 ? 145 ALA B N   1 
ATOM   2146 C  CA  . ALA B 1 153 ? 10.83200  9.45400   46.23200 1.000 14.49098 ? 145 ALA B CA  1 
ATOM   2147 C  C   . ALA B 1 153 ? 10.08100  8.18500   45.87000 1.000 15.95610 ? 145 ALA B C   1 
ATOM   2148 O  O   . ALA B 1 153 ? 9.44700   7.55800   46.72500 1.000 13.79209 ? 145 ALA B O   1 
ATOM   2149 C  CB  . ALA B 1 153 ? 12.30100  9.13600   46.53400 1.000 16.21203 ? 145 ALA B CB  1 
ATOM   2150 N  N   . ASP B 1 154 ? 10.14500  7.81600   44.59500 1.000 15.55879 ? 146 ASP B N   1 
ATOM   2151 C  CA  . ASP B 1 154 ? 9.46500   6.61000   44.15100 1.000 14.78304 ? 146 ASP B CA  1 
ATOM   2152 C  C   . ASP B 1 154 ? 10.23300  5.99200   42.99400 1.000 14.29231 ? 146 ASP B C   1 
ATOM   2153 O  O   . ASP B 1 154 ? 11.19200  6.56800   42.47500 1.000 17.31221 ? 146 ASP B O   1 
ATOM   2154 C  CB  . ASP B 1 154 ? 7.99300   6.88900   43.78500 1.000 17.75292 ? 146 ASP B CB  1 
ATOM   2155 C  CG  . ASP B 1 154 ? 7.82400   7.78800   42.56000 1.000 26.65362 ? 146 ASP B CG  1 
ATOM   2156 O  OD1 . ASP B 1 154 ? 8.81100   8.11700   41.87100 1.000 26.55488 ? 146 ASP B OD1 1 
ATOM   2157 O  OD2 . ASP B 1 154 ? 6.66900   8.17200   42.28400 1.000 33.46756 ? 146 ASP B OD2 1 
ATOM   2158 N  N   . GLY B 1 155 ? 9.79800   4.80400   42.60200 1.000 11.70049 ? 147 GLY B N   1 
ATOM   2159 C  CA  . GLY B 1 155 ? 10.37500  4.13600   41.45400 1.000 12.46169 ? 147 GLY B CA  1 
ATOM   2160 C  C   . GLY B 1 155 ? 9.60500   2.87400   41.14200 1.000 13.35433 ? 147 GLY B C   1 
ATOM   2161 O  O   . GLY B 1 155 ? 8.94900   2.29700   42.01100 1.000 11.49655 ? 147 GLY B O   1 
ATOM   2162 N  N   . VAL B 1 156 ? 9.68700   2.45800   39.88400 1.000 9.65990  ? 148 VAL B N   1 
ATOM   2163 C  CA  . VAL B 1 156 ? 9.05600   1.21100   39.47000 1.000 10.61067 ? 148 VAL B CA  1 
ATOM   2164 C  C   . VAL B 1 156 ? 9.92800   0.04200   39.90500 1.000 12.35990 ? 148 VAL B C   1 
ATOM   2165 O  O   . VAL B 1 156 ? 11.15200  0.06000   39.72500 1.000 12.80399 ? 148 VAL B O   1 
ATOM   2166 C  CB  . VAL B 1 156 ? 8.82500   1.20300   37.94800 1.000 10.12303 ? 148 VAL B CB  1 
ATOM   2167 C  CG1 . VAL B 1 156 ? 8.09300   -0.06100  37.53000 1.000 12.84693 ? 148 VAL B CG1 1 
ATOM   2168 C  CG2 . VAL B 1 156 ? 8.05600   2.44400   37.53100 1.000 13.20069 ? 148 VAL B CG2 1 
ATOM   2169 N  N   . ILE B 1 157 ? 9.30300   -0.98300  40.47900 1.000 11.48655 ? 149 ILE B N   1 
ATOM   2170 C  CA  . ILE B 1 157 ? 10.01300  -2.20300  40.84400 1.000 10.89659 ? 149 ILE B CA  1 
ATOM   2171 C  C   . ILE B 1 157 ? 10.26600  -3.01100  39.57600 1.000 12.79934 ? 149 ILE B C   1 
ATOM   2172 O  O   . ILE B 1 157 ? 9.32400   -3.46900  38.91700 1.000 13.17082 ? 149 ILE B O   1 
ATOM   2173 C  CB  . ILE B 1 157 ? 9.22300   -3.01600  41.87900 1.000 13.78272 ? 149 ILE B CB  1 
ATOM   2174 C  CG1 . ILE B 1 157 ? 8.90900   -2.14600  43.10100 1.000 10.41929 ? 149 ILE B CG1 1 
ATOM   2175 C  CG2 . ILE B 1 157 ? 10.00000  -4.26900  42.29000 1.000 10.62112 ? 149 ILE B CG2 1 
ATOM   2176 C  CD1 . ILE B 1 157 ? 7.90700   -2.76700  44.06200 1.000 11.57024 ? 149 ILE B CD1 1 
ATOM   2177 N  N   . GLY B 1 158 ? 11.54000  -3.18700  39.23100 1.000 10.75640 ? 150 GLY B N   1 
ATOM   2178 C  CA  . GLY B 1 158 ? 11.90200  -3.88600  38.01100 1.000 11.73502 ? 150 GLY B CA  1 
ATOM   2179 C  C   . GLY B 1 158 ? 12.52800  -5.24600  38.23500 1.000 14.62165 ? 150 GLY B C   1 
ATOM   2180 O  O   . GLY B 1 158 ? 13.02200  -5.54000  39.32700 1.000 12.41030 ? 150 GLY B O   1 
ATOM   2181 N  N   . ILE B 1 159 ? 12.49600  -6.08900  37.20300 1.000 11.06968 ? 151 ILE B N   1 
ATOM   2182 C  CA  . ILE B 1 159 ? 13.15200  -7.38900  37.25300 1.000 15.15780 ? 151 ILE B CA  1 
ATOM   2183 C  C   . ILE B 1 159 ? 14.65600  -7.17400  37.30100 1.000 15.85648 ? 151 ILE B C   1 
ATOM   2184 O  O   . ILE B 1 159 ? 15.20600  -6.37500  36.53500 1.000 17.93697 ? 151 ILE B O   1 
ATOM   2185 C  CB  . ILE B 1 159 ? 12.75000  -8.23500  36.03500 1.000 20.50578 ? 151 ILE B CB  1 
ATOM   2186 C  CG1 . ILE B 1 159 ? 11.23200  -8.44700  36.00400 1.000 22.06114 ? 151 ILE B CG1 1 
ATOM   2187 C  CG2 . ILE B 1 159 ? 13.47800  -9.57500  36.03900 1.000 24.11544 ? 151 ILE B CG2 1 
ATOM   2188 C  CD1 . ILE B 1 159 ? 10.70400  -8.94700  34.65000 1.000 19.52315 ? 151 ILE B CD1 1 
ATOM   2189 N  N   . ALA B 1 160 ? 15.33000  -7.88100  38.20300 1.000 16.96063 ? 152 ALA B N   1 
ATOM   2190 C  CA  . ALA B 1 160 ? 16.74700  -7.65700  38.44500 1.000 20.99950 ? 152 ALA B CA  1 
ATOM   2191 C  C   . ALA B 1 160 ? 17.58500  -8.78700  37.86600 1.000 22.36811 ? 152 ALA B C   1 
ATOM   2192 O  O   . ALA B 1 160 ? 17.15000  -9.94100  37.78400 1.000 20.65613 ? 152 ALA B O   1 
ATOM   2193 C  CB  . ALA B 1 160 ? 17.04600  -7.51500  39.94100 1.000 19.93455 ? 152 ALA B CB  1 
ATOM   2194 N  N   . GLN B 1 161 ? 18.80000  -8.42500  37.47300 1.000 32.89186 ? 153 GLN B N   1 
ATOM   2195 C  CA  . GLN B 1 161 ? 19.77900  -9.35100  36.93200 1.000 33.03955 ? 153 GLN B CA  1 
ATOM   2196 C  C   . GLN B 1 161 ? 20.23200  -10.34500 37.99700 1.000 39.82584 ? 153 GLN B C   1 
ATOM   2197 O  O   . GLN B 1 161 ? 20.69700  -9.95600  39.07100 1.000 44.02362 ? 153 GLN B O   1 
ATOM   2198 C  CB  . GLN B 1 161 ? 20.97200  -8.56300  36.38800 1.000 33.79735 ? 153 GLN B CB  1 
ATOM   2199 C  CG  . GLN B 1 161 ? 21.67200  -9.18300  35.19900 1.000 39.85371 ? 153 GLN B CG  1 
ATOM   2200 C  CD  . GLN B 1 161 ? 22.56200  -8.18400  34.48300 1.000 34.36195 ? 153 GLN B CD  1 
ATOM   2201 O  OE1 . GLN B 1 161 ? 22.98000  -7.17900  35.06500 1.000 40.45218 ? 153 GLN B OE1 1 
ATOM   2202 N  NE2 . GLN B 1 161 ? 22.84800  -8.44800  33.21400 1.000 45.53074 ? 153 GLN B NE2 1 
ATOM   2203 O  OXT . GLN B 1 161 ? 20.14900  -11.56000 37.81000 1.000 46.85108 ? 153 GLN B OXT 1 
HETATM 2204 ZN ZN  . ZN  C 2 .   ? 17.70500  -6.13900  19.41400 1.000 16.01705 ? 154 ZN  A ZN  1 
HETATM 2205 CU CU  . CU  D 3 .   ? 18.96800  -0.59300  23.17800 1.000 39.70253 ? 155 CU  A CU  1 
HETATM 2206 CL CL  . CL  E 4 .   ? 6.85200   -3.98000  6.86800  1.000 27.77968 ? 156 CL  A CL  1 
HETATM 2207 ZN ZN  . ZN  F 2 .   ? -1.64700  0.48600   52.91700 1.000 12.45088 ? 154 ZN  B ZN  1 
HETATM 2208 CU CU  . CU  G 3 .   ? 2.22600   4.93000   50.53800 1.000 39.96867 ? 155 CU  B CU  1 
HETATM 2209 O  O   . HOH H 5 .   ? 14.81200  -2.69700  16.29100 1.000 12.24865 ? 157 HOH A O   1 
HETATM 2210 O  O   . HOH H 5 .   ? 10.68000  1.49200   13.34000 1.000 13.86076 ? 158 HOH A O   1 
HETATM 2211 O  O   . HOH H 5 .   ? 13.34400  2.37900   10.99400 1.000 14.29809 ? 159 HOH A O   1 
HETATM 2212 O  O   . HOH H 5 .   ? 8.62000   4.55100   34.48900 1.000 15.87406 ? 160 HOH A O   1 
HETATM 2213 O  O   . HOH H 5 .   ? 13.46200  -12.95600 21.53400 1.000 16.42868 ? 161 HOH A O   1 
HETATM 2214 O  O   . HOH H 5 .   ? 8.77200   0.95000   15.26400 1.000 16.49001 ? 162 HOH A O   1 
HETATM 2215 O  O   . HOH H 5 .   ? 11.72800  4.46500   35.48400 1.000 16.86685 ? 163 HOH A O   1 
HETATM 2216 O  O   . HOH H 5 .   ? 8.61200   3.79100   15.29000 1.000 16.48326 ? 164 HOH A O   1 
HETATM 2217 O  O   . HOH H 5 .   ? 16.99000  -1.45600  2.35800  1.000 17.23863 ? 165 HOH A O   1 
HETATM 2218 O  O   . HOH H 5 .   ? 15.57500  -0.25000  38.58500 1.000 17.86038 ? 166 HOH A O   1 
HETATM 2219 O  O   . HOH H 5 .   ? 5.75600   -2.96400  15.31700 1.000 17.89312 ? 167 HOH A O   1 
HETATM 2220 O  O   . HOH H 5 .   ? 19.60000  13.22100  20.66800 1.000 17.96581 ? 168 HOH A O   1 
HETATM 2221 O  O   . HOH H 5 .   ? 11.34500  -3.62300  10.70100 1.000 18.64668 ? 169 HOH A O   1 
HETATM 2222 O  O   . HOH H 5 .   ? 10.94000  3.79200   11.80100 1.000 19.20901 ? 170 HOH A O   1 
HETATM 2223 O  O   . HOH H 5 .   ? 10.38000  8.81400   9.75200  1.000 19.81915 ? 171 HOH A O   1 
HETATM 2224 O  O   . HOH H 5 .   ? 25.21600  0.42100   10.97700 1.000 20.22294 ? 172 HOH A O   1 
HETATM 2225 O  O   . HOH H 5 .   ? 8.52500   8.27200   15.83100 1.000 20.49039 ? 173 HOH A O   1 
HETATM 2226 O  O   . HOH H 5 .   ? 4.19900   3.22900   36.59700 1.000 20.56900 ? 174 HOH A O   1 
HETATM 2227 O  O   . HOH H 5 .   ? 18.17000  2.00400   9.84500  1.000 20.48482 ? 175 HOH A O   1 
HETATM 2228 O  O   . HOH H 5 .   ? 11.56600  -0.39200  11.34900 1.000 20.78165 ? 176 HOH A O   1 
HETATM 2229 O  O   . HOH H 5 .   ? 6.94500   -0.63500  14.32300 1.000 20.79927 ? 177 HOH A O   1 
HETATM 2230 O  O   . HOH H 5 .   ? 10.32700  6.11100   12.81800 1.000 21.21034 ? 178 HOH A O   1 
HETATM 2231 O  O   . HOH H 5 .   ? 0.38200   -8.62800  33.21100 1.000 21.39218 ? 179 HOH A O   1 
HETATM 2232 O  O   . HOH H 5 .   ? 12.21200  -12.81300 19.35100 1.000 21.53466 ? 180 HOH A O   1 
HETATM 2233 O  O   . HOH H 5 .   ? 16.15400  -11.56100 27.38800 1.000 21.81258 ? 181 HOH A O   1 
HETATM 2234 O  O   . HOH H 5 .   ? -0.29800  4.70200   30.04800 1.000 21.96384 ? 182 HOH A O   1 
HETATM 2235 O  O   . HOH H 5 .   ? 12.73100  19.12500  22.10700 1.000 21.94914 ? 183 HOH A O   1 
HETATM 2236 O  O   . HOH H 5 .   ? 13.77900  -11.95800 9.28300  1.000 22.13465 ? 184 HOH A O   1 
HETATM 2237 O  O   . HOH H 5 .   ? 16.85100  0.95600   33.88300 1.000 22.11325 ? 185 HOH A O   1 
HETATM 2238 O  O   . HOH H 5 .   ? 21.86300  11.99700  19.42600 1.000 22.72746 ? 186 HOH A O   1 
HETATM 2239 O  O   . HOH H 5 .   ? 1.75300   3.61800   36.71700 1.000 22.56745 ? 187 HOH A O   1 
HETATM 2240 O  O   . HOH H 5 .   ? 18.74200  -0.02800  8.15900  1.000 23.31536 ? 188 HOH A O   1 
HETATM 2241 O  O   . HOH H 5 .   ? -4.68700  -5.85800  22.16500 1.000 23.32009 ? 189 HOH A O   1 
HETATM 2242 O  O   . HOH H 5 .   ? 21.94300  7.85500   13.12600 1.000 24.05415 ? 190 HOH A O   1 
HETATM 2243 O  O   . HOH H 5 .   ? 6.93400   5.87200   16.42300 1.000 23.55156 ? 191 HOH A O   1 
HETATM 2244 O  O   . HOH H 5 .   ? 3.57700   -12.87200 25.85000 1.000 23.66534 ? 192 HOH A O   1 
HETATM 2245 O  O   . HOH H 5 .   ? 4.03900   0.04600   14.17100 1.000 23.35015 ? 193 HOH A O   1 
HETATM 2246 O  O   . HOH H 5 .   ? 7.97600   6.79800   12.41700 1.000 23.84720 ? 194 HOH A O   1 
HETATM 2247 O  O   . HOH H 5 .   ? 18.80200  18.55500  15.89700 1.000 23.83146 ? 195 HOH A O   1 
HETATM 2248 O  O   . HOH H 5 .   ? 19.99600  9.85700   13.81200 1.000 24.15405 ? 196 HOH A O   1 
HETATM 2249 O  O   . HOH H 5 .   ? 23.64100  3.69800   13.53700 1.000 24.28777 ? 197 HOH A O   1 
HETATM 2250 O  O   . HOH H 5 .   ? 15.78700  -5.55900  9.07800  1.000 24.06745 ? 198 HOH A O   1 
HETATM 2251 O  O   . HOH H 5 .   ? -1.94900  -8.71000  28.33200 1.000 25.45030 ? 199 HOH A O   1 
HETATM 2252 O  O   . HOH H 5 .   ? 21.61100  -10.85000 19.26700 1.000 25.77080 ? 200 HOH A O   1 
HETATM 2253 O  O   . HOH H 5 .   ? 8.62100   -11.95100 30.25800 1.000 25.46613 ? 201 HOH A O   1 
HETATM 2254 O  O   . HOH H 5 .   ? 17.56000  -10.12800 11.81000 1.000 25.56892 ? 202 HOH A O   1 
HETATM 2255 O  O   . HOH H 5 .   ? 2.78900   -16.52900 26.97200 1.000 25.97541 ? 203 HOH A O   1 
HETATM 2256 O  O   . HOH H 5 .   ? 30.85600  -4.92300  15.10600 1.000 26.03095 ? 204 HOH A O   1 
HETATM 2257 O  O   . HOH H 5 .   ? 21.07500  -11.69700 29.87600 1.000 26.42871 ? 205 HOH A O   1 
HETATM 2258 O  O   . HOH H 5 .   ? 19.51400  -9.75500  23.28400 1.000 26.17262 ? 206 HOH A O   1 
HETATM 2259 O  O   . HOH H 5 .   ? 19.39100  12.90600  27.93700 1.000 26.44511 ? 207 HOH A O   1 
HETATM 2260 O  O   . HOH H 5 .   ? 12.62300  14.13300  11.30400 1.000 26.11335 ? 208 HOH A O   1 
HETATM 2261 O  O   . HOH H 5 .   ? 0.33000   9.00600   30.35900 1.000 26.02024 ? 209 HOH A O   1 
HETATM 2262 O  O   . HOH H 5 .   ? -4.50500  -7.58300  28.08200 1.000 25.96439 ? 210 HOH A O   1 
HETATM 2263 O  O   . HOH H 5 .   ? 23.39100  0.46900   21.41700 1.000 26.32929 ? 211 HOH A O   1 
HETATM 2264 O  O   . HOH H 5 .   ? 20.04900  15.43800  22.48700 1.000 26.63415 ? 212 HOH A O   1 
HETATM 2265 O  O   . HOH H 5 .   ? 10.18000  12.33300  31.77200 1.000 26.87976 ? 213 HOH A O   1 
HETATM 2266 O  O   . HOH H 5 .   ? 4.62300   -6.49200  15.28400 1.000 26.61879 ? 214 HOH A O   1 
HETATM 2267 O  O   . HOH H 5 .   ? -7.36900  -10.29200 27.52900 1.000 26.45353 ? 215 HOH A O   1 
HETATM 2268 O  O   . HOH H 5 .   ? 21.66700  13.40500  26.85700 1.000 26.92058 ? 216 HOH A O   1 
HETATM 2269 O  O   . HOH H 5 .   ? 21.07800  -6.87600  22.26200 1.000 27.03874 ? 217 HOH A O   1 
HETATM 2270 O  O   . HOH H 5 .   ? 10.52300  18.33900  11.28000 1.000 28.06889 ? 218 HOH A O   1 
HETATM 2271 O  O   . HOH H 5 .   ? 12.59000  16.68700  10.27900 1.000 27.12539 ? 219 HOH A O   1 
HETATM 2272 O  O   . HOH H 5 .   ? 25.20900  0.01600   19.58200 1.000 28.35542 ? 220 HOH A O   1 
HETATM 2273 O  O   . HOH H 5 .   ? 11.05600  -11.49400 8.21700  1.000 27.89063 ? 221 HOH A O   1 
HETATM 2274 O  O   . HOH H 5 .   ? -5.94700  -2.38000  37.29600 1.000 28.31498 ? 222 HOH A O   1 
HETATM 2275 O  O   . HOH H 5 .   ? 3.61500   11.20900  26.39800 1.000 28.45217 ? 223 HOH A O   1 
HETATM 2276 O  O   . HOH H 5 .   ? 19.74900  12.38300  14.92200 1.000 28.81892 ? 224 HOH A O   1 
HETATM 2277 O  O   . HOH H 5 .   ? 14.30000  11.67700  9.87100  1.000 29.13659 ? 225 HOH A O   1 
HETATM 2278 O  O   . HOH H 5 .   ? 7.66500   19.86700  17.23300 1.000 29.30580 ? 226 HOH A O   1 
HETATM 2279 O  O   . HOH H 5 .   ? 8.09600   -10.17200 13.69000 1.000 29.08181 ? 227 HOH A O   1 
HETATM 2280 O  O   . HOH H 5 .   ? 12.18000  6.77700   34.95300 1.000 29.35442 ? 228 HOH A O   1 
HETATM 2281 O  O   . HOH H 5 .   ? 7.05400   3.93300   13.21700 1.000 30.86373 ? 229 HOH A O   1 
HETATM 2282 O  O   . HOH H 5 .   ? 21.57600  9.90500   29.58100 1.000 31.56445 ? 230 HOH A O   1 
HETATM 2283 O  O   . HOH H 5 .   ? 1.26600   -12.86000 32.56100 1.000 31.96385 ? 231 HOH A O   1 
HETATM 2284 O  O   . HOH H 5 .   ? -6.99800  -8.11500  28.83100 1.000 32.32589 ? 232 HOH A O   1 
HETATM 2285 O  O   . HOH H 5 .   ? 14.75300  -12.38200 31.98700 1.000 32.38584 ? 233 HOH A O   1 
HETATM 2286 O  O   . HOH H 5 .   ? 10.36400  7.72400   36.82500 1.000 33.95812 ? 234 HOH A O   1 
HETATM 2287 O  O   . HOH I 5 .   ? 2.44500   -0.46900  56.42200 1.000 10.22363 ? 156 HOH B O   1 
HETATM 2288 O  O   . HOH I 5 .   ? -4.41900  -6.30800  49.55400 1.000 12.16430 ? 157 HOH B O   1 
HETATM 2289 O  O   . HOH I 5 .   ? 13.57100  1.37200   39.53100 1.000 13.87253 ? 158 HOH B O   1 
HETATM 2290 O  O   . HOH I 5 .   ? -4.34700  3.16600   49.90100 1.000 14.35662 ? 159 HOH B O   1 
HETATM 2291 O  O   . HOH I 5 .   ? 8.48400   -5.53600  58.73900 1.000 16.20784 ? 160 HOH B O   1 
HETATM 2292 O  O   . HOH I 5 .   ? -7.74300  10.27100  64.71300 1.000 16.11642 ? 161 HOH B O   1 
HETATM 2293 O  O   . HOH I 5 .   ? 5.18100   -10.26700 56.81400 1.000 16.78150 ? 162 HOH B O   1 
HETATM 2294 O  O   . HOH I 5 .   ? 8.79500   -2.71600  57.92200 1.000 16.85280 ? 163 HOH B O   1 
HETATM 2295 O  O   . HOH I 5 .   ? 7.49300   -7.58700  56.99300 1.000 17.32546 ? 164 HOH B O   1 
HETATM 2296 O  O   . HOH I 5 .   ? 7.06600   1.41200   62.79900 1.000 18.12477 ? 165 HOH B O   1 
HETATM 2297 O  O   . HOH I 5 .   ? 2.13800   10.23500  60.36700 1.000 17.55314 ? 166 HOH B O   1 
HETATM 2298 O  O   . HOH I 5 .   ? 5.88100   -14.15900 49.91500 1.000 18.19099 ? 167 HOH B O   1 
HETATM 2299 O  O   . HOH I 5 .   ? -6.91600  0.38700   59.14200 1.000 18.52360 ? 168 HOH B O   1 
HETATM 2300 O  O   . HOH I 5 .   ? 7.64400   -1.26800  60.13000 1.000 18.91330 ? 169 HOH B O   1 
HETATM 2301 O  O   . HOH I 5 .   ? 11.77900  3.92100   38.35500 1.000 18.98969 ? 170 HOH B O   1 
HETATM 2302 O  O   . HOH I 5 .   ? 15.22900  10.01700  65.90300 1.000 18.73559 ? 171 HOH B O   1 
HETATM 2303 O  O   . HOH I 5 .   ? 9.61500   9.69200   63.49500 1.000 19.36587 ? 172 HOH B O   1 
HETATM 2304 O  O   . HOH I 5 .   ? 14.81100  1.19200   58.56000 1.000 18.83706 ? 173 HOH B O   1 
HETATM 2305 O  O   . HOH I 5 .   ? -4.17400  -2.58300  44.20200 1.000 19.47511 ? 174 HOH B O   1 
HETATM 2306 O  O   . HOH I 5 .   ? 0.23300   8.94100   52.00900 1.000 19.49930 ? 175 HOH B O   1 
HETATM 2307 O  O   . HOH I 5 .   ? -7.03600  -14.50700 47.13700 1.000 19.70608 ? 176 HOH B O   1 
HETATM 2308 O  O   . HOH I 5 .   ? -7.95400  0.99700   51.97600 1.000 19.90894 ? 177 HOH B O   1 
HETATM 2309 O  O   . HOH I 5 .   ? 2.24700   -6.66900  39.84200 1.000 19.95751 ? 178 HOH B O   1 
HETATM 2310 O  O   . HOH I 5 .   ? 3.87600   1.22000   38.78700 1.000 20.02777 ? 179 HOH B O   1 
HETATM 2311 O  O   . HOH I 5 .   ? -3.82700  -7.65100  51.88300 1.000 19.98875 ? 180 HOH B O   1 
HETATM 2312 O  O   . HOH I 5 .   ? -5.22000  -2.60900  59.91600 1.000 20.43707 ? 181 HOH B O   1 
HETATM 2313 O  O   . HOH I 5 .   ? 4.41800   5.06500   63.57500 1.000 20.81131 ? 182 HOH B O   1 
HETATM 2314 O  O   . HOH I 5 .   ? 11.39900  -1.52600  58.27400 1.000 20.69231 ? 183 HOH B O   1 
HETATM 2315 O  O   . HOH I 5 .   ? 9.49800   1.13800   63.15100 1.000 21.60447 ? 184 HOH B O   1 
HETATM 2316 O  O   . HOH I 5 .   ? 12.35000  13.56700  54.60500 1.000 21.46896 ? 185 HOH B O   1 
HETATM 2317 O  O   . HOH I 5 .   ? -1.32400  10.58300  54.43400 1.000 21.30663 ? 186 HOH B O   1 
HETATM 2318 O  O   . HOH I 5 .   ? 13.94000  15.30600  53.05700 1.000 21.67313 ? 187 HOH B O   1 
HETATM 2319 O  O   . HOH I 5 .   ? -1.77400  9.01800   63.07600 1.000 22.00976 ? 188 HOH B O   1 
HETATM 2320 O  O   . HOH I 5 .   ? 18.15600  2.64400   59.55700 1.000 22.80708 ? 189 HOH B O   1 
HETATM 2321 O  O   . HOH I 5 .   ? -2.46600  12.23600  56.69100 1.000 22.58368 ? 190 HOH B O   1 
HETATM 2322 O  O   . HOH I 5 .   ? 18.17600  3.43400   64.85200 1.000 22.85780 ? 191 HOH B O   1 
HETATM 2323 O  O   . HOH I 5 .   ? -1.91600  -10.00100 56.36200 1.000 23.19237 ? 192 HOH B O   1 
HETATM 2324 O  O   . HOH I 5 .   ? 13.15400  5.91100   39.80500 1.000 23.22664 ? 193 HOH B O   1 
HETATM 2325 O  O   . HOH I 5 .   ? 21.43700  12.02800  54.12500 1.000 23.07094 ? 194 HOH B O   1 
HETATM 2326 O  O   . HOH I 5 .   ? 10.14500  14.44800  55.92500 1.000 23.68080 ? 195 HOH B O   1 
HETATM 2327 O  O   . HOH I 5 .   ? 17.33400  -1.46700  59.41100 1.000 23.77077 ? 196 HOH B O   1 
HETATM 2328 O  O   . HOH I 5 .   ? -4.90100  -6.36200  62.03900 1.000 23.57948 ? 197 HOH B O   1 
HETATM 2329 O  O   . HOH I 5 .   ? -3.98900  -3.05000  39.77000 1.000 24.11262 ? 198 HOH B O   1 
HETATM 2330 O  O   . HOH I 5 .   ? 6.16800   5.10800   35.95300 1.000 24.05907 ? 199 HOH B O   1 
HETATM 2331 O  O   . HOH I 5 .   ? 16.24500  15.54800  60.34800 1.000 24.49769 ? 200 HOH B O   1 
HETATM 2332 O  O   . HOH I 5 .   ? 3.87000   -0.53100  66.33100 1.000 24.02461 ? 201 HOH B O   1 
HETATM 2333 O  O   . HOH I 5 .   ? 2.85000   -10.78700 57.74900 1.000 24.66109 ? 202 HOH B O   1 
HETATM 2334 O  O   . HOH I 5 .   ? 11.22600  -7.72200  58.88800 1.000 24.31737 ? 203 HOH B O   1 
HETATM 2335 O  O   . HOH I 5 .   ? 20.74400  14.75600  45.63300 1.000 25.09419 ? 204 HOH B O   1 
HETATM 2336 O  O   . HOH I 5 .   ? 15.53500  12.48500  44.52300 1.000 24.65910 ? 205 HOH B O   1 
HETATM 2337 O  O   . HOH I 5 .   ? 0.17000   5.29300   36.02800 1.000 25.21346 ? 206 HOH B O   1 
HETATM 2338 O  O   . HOH I 5 .   ? -3.01600  -9.60700  53.64000 1.000 25.11015 ? 207 HOH B O   1 
HETATM 2339 O  O   . HOH I 5 .   ? 6.18100   11.35900  61.26500 1.000 25.72303 ? 208 HOH B O   1 
HETATM 2340 O  O   . HOH I 5 .   ? 11.69700  1.19800   60.68300 1.000 25.42395 ? 209 HOH B O   1 
HETATM 2341 O  O   . HOH I 5 .   ? -1.23000  3.78400   42.94900 1.000 25.62591 ? 210 HOH B O   1 
HETATM 2342 O  O   . HOH I 5 .   ? 12.84400  13.98600  47.13100 1.000 25.69475 ? 211 HOH B O   1 
HETATM 2343 O  O   . HOH I 5 .   ? -6.98400  2.59900   49.85000 1.000 25.60392 ? 212 HOH B O   1 
HETATM 2344 O  O   . HOH I 5 .   ? 1.16900   -20.80400 46.31000 1.000 26.40971 ? 213 HOH B O   1 
HETATM 2345 O  O   . HOH I 5 .   ? 16.04300  8.17500   64.12500 1.000 26.38117 ? 214 HOH B O   1 
HETATM 2346 O  O   . HOH I 5 .   ? 6.40800   5.01700   39.20100 1.000 26.71754 ? 215 HOH B O   1 
HETATM 2347 O  O   . HOH I 5 .   ? 6.21700   -18.06000 44.89800 1.000 26.60497 ? 216 HOH B O   1 
HETATM 2348 O  O   . HOH I 5 .   ? 3.47000   2.40000   66.20500 1.000 26.86483 ? 217 HOH B O   1 
HETATM 2349 O  O   . HOH I 5 .   ? 18.88900  15.13600  61.95900 1.000 27.39885 ? 218 HOH B O   1 
HETATM 2350 O  O   . HOH I 5 .   ? 10.09400  -10.20600 59.61900 1.000 27.47775 ? 219 HOH B O   1 
HETATM 2351 O  O   . HOH I 5 .   ? 8.71200   11.25000  60.88100 1.000 28.63700 ? 220 HOH B O   1 
HETATM 2352 O  O   . HOH I 5 .   ? 14.71100  -12.60500 38.65400 1.000 28.80242 ? 221 HOH B O   1 
HETATM 2353 O  O   . HOH I 5 .   ? 6.00200   2.93900   64.79500 1.000 29.04171 ? 222 HOH B O   1 
HETATM 2354 O  O   . HOH I 5 .   ? 12.48600  2.85200   64.44000 1.000 28.83498 ? 223 HOH B O   1 
HETATM 2355 O  O   . HOH I 5 .   ? 24.60700  -9.34800  30.66200 1.000 29.65960 ? 224 HOH B O   1 
HETATM 2356 O  O   . HOH I 5 .   ? 18.44000  14.62300  44.48000 1.000 29.04521 ? 225 HOH B O   1 
HETATM 2357 O  O   . HOH I 5 .   ? 5.87300   -2.43900  61.87100 1.000 27.84680 ? 226 HOH B O   1 
HETATM 2358 O  O   . HOH I 5 .   ? 7.23000   -4.85300  61.20000 1.000 29.88982 ? 227 HOH B O   1 
HETATM 2359 O  O   . HOH I 5 .   ? 1.20600   -0.92900  65.66600 1.000 29.81613 ? 228 HOH B O   1 
HETATM 2360 O  O   . HOH I 5 .   ? 1.01200   13.19500  57.43500 1.000 30.25684 ? 229 HOH B O   1 
HETATM 2361 O  O   . HOH I 5 .   ? 11.63700  15.65200  48.68900 1.000 31.29050 ? 230 HOH B O   1 
HETATM 2362 O  O   . HOH I 5 .   ? -8.19300  -3.39200  60.13200 1.000 30.64754 ? 231 HOH B O   1 
HETATM 2363 O  O   . HOH I 5 .   ? -7.72100  -3.54400  43.17000 1.000 33.00960 ? 232 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   GLY 1   -7  ?   ?   ?   A . n 
A 1 2   ALA 2   -6  ?   ?   ?   A . n 
A 1 3   MET 3   -5  ?   ?   ?   A . n 
A 1 4   ASP 4   -4  ?   ?   ?   A . n 
A 1 5   PRO 5   -3  ?   ?   ?   A . n 
A 1 6   GLU 6   -2  ?   ?   ?   A . n 
A 1 7   PHE 7   -1  -1  PHE PHE A . n 
A 1 8   MET 8   0   0   MET MET A . n 
A 1 9   ALA 9   1   1   ALA ALA A . n 
A 1 10  THR 10  2   2   THR THR A . n 
A 1 11  LYS 11  3   3   LYS LYS A . n 
A 1 12  ALA 12  4   4   ALA ALA A . n 
A 1 13  VAL 13  5   5   VAL VAL A . n 
A 1 14  CYS 14  6   6   CYS CYS A . n 
A 1 15  VAL 15  7   7   VAL VAL A . n 
A 1 16  LEU 16  8   8   LEU LEU A . n 
A 1 17  LYS 17  9   9   LYS LYS A . n 
A 1 18  GLY 18  10  10  GLY GLY A . n 
A 1 19  ASP 19  11  11  ASP ASP A . n 
A 1 20  GLY 20  12  12  GLY GLY A . n 
A 1 21  PRO 21  13  13  PRO PRO A . n 
A 1 22  VAL 22  14  14  VAL VAL A . n 
A 1 23  GLN 23  15  15  GLN GLN A . n 
A 1 24  GLY 24  16  16  GLY GLY A . n 
A 1 25  ILE 25  17  17  ILE ILE A . n 
A 1 26  ILE 26  18  18  ILE ILE A . n 
A 1 27  ASN 27  19  19  ASN ASN A . n 
A 1 28  PHE 28  20  20  PHE PHE A . n 
A 1 29  GLU 29  21  21  GLU GLU A . n 
A 1 30  GLN 30  22  22  GLN GLN A . n 
A 1 31  LYS 31  23  23  LYS LYS A . n 
A 1 32  GLU 32  24  24  GLU GLU A . n 
A 1 33  SER 33  25  25  SER SER A . n 
A 1 34  ASN 34  26  26  ASN ASN A . n 
A 1 35  GLY 35  27  27  GLY GLY A . n 
A 1 36  PRO 36  28  28  PRO PRO A . n 
A 1 37  VAL 37  29  29  VAL VAL A . n 
A 1 38  LYS 38  30  30  LYS LYS A . n 
A 1 39  VAL 39  31  31  VAL VAL A . n 
A 1 40  TRP 40  32  32  TRP TRP A . n 
A 1 41  GLY 41  33  33  GLY GLY A . n 
A 1 42  SER 42  34  34  SER SER A . n 
A 1 43  ILE 43  35  35  ILE ILE A . n 
A 1 44  LYS 44  36  36  LYS LYS A . n 
A 1 45  GLY 45  37  37  GLY GLY A . n 
A 1 46  LEU 46  38  38  LEU LEU A . n 
A 1 47  THR 47  39  39  THR THR A . n 
A 1 48  GLU 48  40  40  GLU GLU A . n 
A 1 49  GLY 49  41  41  GLY GLY A . n 
A 1 50  LEU 50  42  42  LEU LEU A . n 
A 1 51  HIS 51  43  43  HIS HIS A . n 
A 1 52  GLY 52  44  44  GLY GLY A . n 
A 1 53  PHE 53  45  45  PHE PHE A . n 
A 1 54  HIS 54  46  46  HIS HIS A . n 
A 1 55  VAL 55  47  47  VAL VAL A . n 
A 1 56  HIS 56  48  48  HIS HIS A . n 
A 1 57  GLU 57  49  49  GLU GLU A . n 
A 1 58  PHE 58  50  50  PHE PHE A . n 
A 1 59  GLY 59  51  51  GLY GLY A . n 
A 1 60  ASP 60  52  52  ASP ASP A . n 
A 1 61  ASN 61  53  53  ASN ASN A . n 
A 1 62  THR 62  54  54  THR THR A . n 
A 1 63  ALA 63  55  55  ALA ALA A . n 
A 1 64  GLY 64  56  56  GLY GLY A . n 
A 1 65  ASP 65  57  57  ASP ASP A . n 
A 1 66  THR 66  58  58  THR THR A . n 
A 1 67  SER 67  59  59  SER SER A . n 
A 1 68  ALA 68  60  60  ALA ALA A . n 
A 1 69  GLY 69  61  61  GLY GLY A . n 
A 1 70  PRO 70  62  62  PRO PRO A . n 
A 1 71  HIS 71  63  63  HIS HIS A . n 
A 1 72  PHE 72  64  64  PHE PHE A . n 
A 1 73  ASN 73  65  65  ASN ASN A . n 
A 1 74  PRO 74  66  66  PRO PRO A . n 
A 1 75  LEU 75  67  67  LEU LEU A . n 
A 1 76  SER 76  68  68  SER SER A . n 
A 1 77  ARG 77  69  69  ARG ARG A . n 
A 1 78  LYS 78  70  70  LYS LYS A . n 
A 1 79  HIS 79  71  71  HIS HIS A . n 
A 1 80  GLY 80  72  72  GLY GLY A . n 
A 1 81  GLY 81  73  73  GLY GLY A . n 
A 1 82  PRO 82  74  74  PRO PRO A . n 
A 1 83  LYS 83  75  75  LYS LYS A . n 
A 1 84  ASP 84  76  76  ASP ASP A . n 
A 1 85  GLU 85  77  77  GLU GLU A . n 
A 1 86  GLU 86  78  78  GLU GLU A . n 
A 1 87  ARG 87  79  79  ARG ARG A . n 
A 1 88  HIS 88  80  80  HIS HIS A . n 
A 1 89  VAL 89  81  81  VAL VAL A . n 
A 1 90  GLY 90  82  82  GLY GLY A . n 
A 1 91  ASP 91  83  83  ASP ASP A . n 
A 1 92  LEU 92  84  84  LEU LEU A . n 
A 1 93  GLY 93  85  85  GLY GLY A . n 
A 1 94  ASN 94  86  86  ASN ASN A . n 
A 1 95  VAL 95  87  87  VAL VAL A . n 
A 1 96  THR 96  88  88  THR THR A . n 
A 1 97  ALA 97  89  89  ALA ALA A . n 
A 1 98  ASP 98  90  90  ASP ASP A . n 
A 1 99  LYS 99  91  91  LYS LYS A . n 
A 1 100 ASP 100 92  92  ASP ASP A . n 
A 1 101 GLY 101 93  93  GLY GLY A . n 
A 1 102 VAL 102 94  94  VAL VAL A . n 
A 1 103 ALA 103 95  95  ALA ALA A . n 
A 1 104 ASP 104 96  96  ASP ASP A . n 
A 1 105 VAL 105 97  97  VAL VAL A . n 
A 1 106 SER 106 98  98  SER SER A . n 
A 1 107 ILE 107 99  99  ILE ILE A . n 
A 1 108 GLU 108 100 100 GLU GLU A . n 
A 1 109 ASP 109 101 101 ASP ASP A . n 
A 1 110 SER 110 102 102 SER SER A . n 
A 1 111 VAL 111 103 103 VAL VAL A . n 
A 1 112 ILE 112 104 104 ILE ILE A . n 
A 1 113 SER 113 105 105 SER SER A . n 
A 1 114 LEU 114 106 106 LEU LEU A . n 
A 1 115 SER 115 107 107 SER SER A . n 
A 1 116 GLY 116 108 108 GLY GLY A . n 
A 1 117 ASP 117 109 109 ASP ASP A . n 
A 1 118 HIS 118 110 110 HIS HIS A . n 
A 1 119 CSO 119 111 111 CSO CSO A . n 
A 1 120 ILE 120 112 112 ILE ILE A . n 
A 1 121 ILE 121 113 113 ILE ILE A . n 
A 1 122 GLY 122 114 114 GLY GLY A . n 
A 1 123 ARG 123 115 115 ARG ARG A . n 
A 1 124 THR 124 116 116 THR THR A . n 
A 1 125 LEU 125 117 117 LEU LEU A . n 
A 1 126 VAL 126 118 118 VAL VAL A . n 
A 1 127 VAL 127 119 119 VAL VAL A . n 
A 1 128 HIS 128 120 120 HIS HIS A . n 
A 1 129 GLU 129 121 121 GLU GLU A . n 
A 1 130 LYS 130 122 122 LYS LYS A . n 
A 1 131 ALA 131 123 123 ALA ALA A . n 
A 1 132 ASP 132 124 124 ASP ASP A . n 
A 1 133 ASP 133 125 125 ASP ASP A . n 
A 1 134 LEU 134 126 126 LEU LEU A . n 
A 1 135 GLY 135 127 127 GLY GLY A . n 
A 1 136 LYS 136 128 128 LYS LYS A . n 
A 1 137 GLY 137 129 129 GLY GLY A . n 
A 1 138 GLY 138 130 130 GLY GLY A . n 
A 1 139 ASN 139 131 131 ASN ASN A . n 
A 1 140 GLU 140 132 132 GLU GLU A . n 
A 1 141 GLU 141 133 133 GLU GLU A . n 
A 1 142 SER 142 134 134 SER SER A . n 
A 1 143 THR 143 135 135 THR THR A . n 
A 1 144 LYS 144 136 136 LYS LYS A . n 
A 1 145 THR 145 137 137 THR THR A . n 
A 1 146 GLY 146 138 138 GLY GLY A . n 
A 1 147 ASN 147 139 139 ASN ASN A . n 
A 1 148 ALA 148 140 140 ALA ALA A . n 
A 1 149 GLY 149 141 141 GLY GLY A . n 
A 1 150 SER 150 142 142 SER SER A . n 
A 1 151 ARG 151 143 143 ARG ARG A . n 
A 1 152 LEU 152 144 144 LEU LEU A . n 
A 1 153 ALA 153 145 145 ALA ALA A . n 
A 1 154 ASP 154 146 146 ASP ASP A . n 
A 1 155 GLY 155 147 147 GLY GLY A . n 
A 1 156 VAL 156 148 148 VAL VAL A . n 
A 1 157 ILE 157 149 149 ILE ILE A . n 
A 1 158 GLY 158 150 150 GLY GLY A . n 
A 1 159 ILE 159 151 151 ILE ILE A . n 
A 1 160 ALA 160 152 152 ALA ALA A . n 
A 1 161 GLN 161 153 153 GLN GLN A . n 
B 1 1   GLY 1   -7  ?   ?   ?   B . n 
B 1 2   ALA 2   -6  ?   ?   ?   B . n 
B 1 3   MET 3   -5  ?   ?   ?   B . n 
B 1 4   ASP 4   -4  ?   ?   ?   B . n 
B 1 5   PRO 5   -3  ?   ?   ?   B . n 
B 1 6   GLU 6   -2  ?   ?   ?   B . n 
B 1 7   PHE 7   -1  ?   ?   ?   B . n 
B 1 8   MET 8   0   ?   ?   ?   B . n 
B 1 9   ALA 9   1   1   ALA ALA B . n 
B 1 10  THR 10  2   2   THR THR B . n 
B 1 11  LYS 11  3   3   LYS LYS B . n 
B 1 12  ALA 12  4   4   ALA ALA B . n 
B 1 13  VAL 13  5   5   VAL VAL B . n 
B 1 14  CYS 14  6   6   CYS CYS B . n 
B 1 15  VAL 15  7   7   VAL VAL B . n 
B 1 16  LEU 16  8   8   LEU LEU B . n 
B 1 17  LYS 17  9   9   LYS LYS B . n 
B 1 18  GLY 18  10  10  GLY GLY B . n 
B 1 19  ASP 19  11  11  ASP ASP B . n 
B 1 20  GLY 20  12  12  GLY GLY B . n 
B 1 21  PRO 21  13  13  PRO PRO B . n 
B 1 22  VAL 22  14  14  VAL VAL B . n 
B 1 23  GLN 23  15  15  GLN GLN B . n 
B 1 24  GLY 24  16  16  GLY GLY B . n 
B 1 25  ILE 25  17  17  ILE ILE B . n 
B 1 26  ILE 26  18  18  ILE ILE B . n 
B 1 27  ASN 27  19  19  ASN ASN B . n 
B 1 28  PHE 28  20  20  PHE PHE B . n 
B 1 29  GLU 29  21  21  GLU GLU B . n 
B 1 30  GLN 30  22  22  GLN GLN B . n 
B 1 31  LYS 31  23  23  LYS LYS B . n 
B 1 32  GLU 32  24  24  GLU GLU B . n 
B 1 33  SER 33  25  25  SER SER B . n 
B 1 34  ASN 34  26  26  ASN ASN B . n 
B 1 35  GLY 35  27  27  GLY GLY B . n 
B 1 36  PRO 36  28  28  PRO PRO B . n 
B 1 37  VAL 37  29  29  VAL VAL B . n 
B 1 38  LYS 38  30  30  LYS LYS B . n 
B 1 39  VAL 39  31  31  VAL VAL B . n 
B 1 40  TRP 40  32  32  TRP TRP B . n 
B 1 41  GLY 41  33  33  GLY GLY B . n 
B 1 42  SER 42  34  34  SER SER B . n 
B 1 43  ILE 43  35  35  ILE ILE B . n 
B 1 44  LYS 44  36  36  LYS LYS B . n 
B 1 45  GLY 45  37  37  GLY GLY B . n 
B 1 46  LEU 46  38  38  LEU LEU B . n 
B 1 47  THR 47  39  39  THR THR B . n 
B 1 48  GLU 48  40  40  GLU GLU B . n 
B 1 49  GLY 49  41  41  GLY GLY B . n 
B 1 50  LEU 50  42  42  LEU LEU B . n 
B 1 51  HIS 51  43  43  HIS HIS B . n 
B 1 52  GLY 52  44  44  GLY GLY B . n 
B 1 53  PHE 53  45  45  PHE PHE B . n 
B 1 54  HIS 54  46  46  HIS HIS B . n 
B 1 55  VAL 55  47  47  VAL VAL B . n 
B 1 56  HIS 56  48  48  HIS HIS B . n 
B 1 57  GLU 57  49  49  GLU GLU B . n 
B 1 58  PHE 58  50  50  PHE PHE B . n 
B 1 59  GLY 59  51  51  GLY GLY B . n 
B 1 60  ASP 60  52  ?   ?   ?   B . n 
B 1 61  ASN 61  53  ?   ?   ?   B . n 
B 1 62  THR 62  54  ?   ?   ?   B . n 
B 1 63  ALA 63  55  ?   ?   ?   B . n 
B 1 64  GLY 64  56  ?   ?   ?   B . n 
B 1 65  ASP 65  57  ?   ?   ?   B . n 
B 1 66  THR 66  58  ?   ?   ?   B . n 
B 1 67  SER 67  59  ?   ?   ?   B . n 
B 1 68  ALA 68  60  ?   ?   ?   B . n 
B 1 69  GLY 69  61  61  GLY GLY B . n 
B 1 70  PRO 70  62  62  PRO PRO B . n 
B 1 71  HIS 71  63  63  HIS HIS B . n 
B 1 72  PHE 72  64  64  PHE PHE B . n 
B 1 73  ASN 73  65  65  ASN ASN B . n 
B 1 74  PRO 74  66  66  PRO PRO B . n 
B 1 75  LEU 75  67  67  LEU LEU B . n 
B 1 76  SER 76  68  68  SER SER B . n 
B 1 77  ARG 77  69  69  ARG ARG B . n 
B 1 78  LYS 78  70  70  LYS LYS B . n 
B 1 79  HIS 79  71  71  HIS HIS B . n 
B 1 80  GLY 80  72  72  GLY GLY B . n 
B 1 81  GLY 81  73  73  GLY GLY B . n 
B 1 82  PRO 82  74  74  PRO PRO B . n 
B 1 83  LYS 83  75  75  LYS LYS B . n 
B 1 84  ASP 84  76  76  ASP ASP B . n 
B 1 85  GLU 85  77  77  GLU GLU B . n 
B 1 86  GLU 86  78  78  GLU GLU B . n 
B 1 87  ARG 87  79  79  ARG ARG B . n 
B 1 88  HIS 88  80  80  HIS HIS B . n 
B 1 89  VAL 89  81  81  VAL VAL B . n 
B 1 90  GLY 90  82  82  GLY GLY B . n 
B 1 91  ASP 91  83  83  ASP ASP B . n 
B 1 92  LEU 92  84  84  LEU LEU B . n 
B 1 93  GLY 93  85  85  GLY GLY B . n 
B 1 94  ASN 94  86  86  ASN ASN B . n 
B 1 95  VAL 95  87  87  VAL VAL B . n 
B 1 96  THR 96  88  88  THR THR B . n 
B 1 97  ALA 97  89  89  ALA ALA B . n 
B 1 98  ASP 98  90  90  ASP ASP B . n 
B 1 99  LYS 99  91  91  LYS LYS B . n 
B 1 100 ASP 100 92  92  ASP ASP B . n 
B 1 101 GLY 101 93  93  GLY GLY B . n 
B 1 102 VAL 102 94  94  VAL VAL B . n 
B 1 103 ALA 103 95  95  ALA ALA B . n 
B 1 104 ASP 104 96  96  ASP ASP B . n 
B 1 105 VAL 105 97  97  VAL VAL B . n 
B 1 106 SER 106 98  98  SER SER B . n 
B 1 107 ILE 107 99  99  ILE ILE B . n 
B 1 108 GLU 108 100 100 GLU GLU B . n 
B 1 109 ASP 109 101 101 ASP ASP B . n 
B 1 110 SER 110 102 102 SER SER B . n 
B 1 111 VAL 111 103 103 VAL VAL B . n 
B 1 112 ILE 112 104 104 ILE ILE B . n 
B 1 113 SER 113 105 105 SER SER B . n 
B 1 114 LEU 114 106 106 LEU LEU B . n 
B 1 115 SER 115 107 107 SER SER B . n 
B 1 116 GLY 116 108 108 GLY GLY B . n 
B 1 117 ASP 117 109 109 ASP ASP B . n 
B 1 118 HIS 118 110 110 HIS HIS B . n 
B 1 119 CSO 119 111 111 CSO CSO B . n 
B 1 120 ILE 120 112 112 ILE ILE B . n 
B 1 121 ILE 121 113 113 ILE ILE B . n 
B 1 122 GLY 122 114 114 GLY GLY B . n 
B 1 123 ARG 123 115 115 ARG ARG B . n 
B 1 124 THR 124 116 116 THR THR B . n 
B 1 125 LEU 125 117 117 LEU LEU B . n 
B 1 126 VAL 126 118 118 VAL VAL B . n 
B 1 127 VAL 127 119 119 VAL VAL B . n 
B 1 128 HIS 128 120 120 HIS HIS B . n 
B 1 129 GLU 129 121 121 GLU GLU B . n 
B 1 130 LYS 130 122 122 LYS LYS B . n 
B 1 131 ALA 131 123 123 ALA ALA B . n 
B 1 132 ASP 132 124 124 ASP ASP B . n 
B 1 133 ASP 133 125 125 ASP ASP B . n 
B 1 134 LEU 134 126 126 LEU LEU B . n 
B 1 135 GLY 135 127 127 GLY GLY B . n 
B 1 136 LYS 136 128 128 LYS LYS B . n 
B 1 137 GLY 137 129 129 GLY GLY B . n 
B 1 138 GLY 138 130 130 GLY GLY B . n 
B 1 139 ASN 139 131 131 ASN ASN B . n 
B 1 140 GLU 140 132 132 GLU GLU B . n 
B 1 141 GLU 141 133 133 GLU GLU B . n 
B 1 142 SER 142 134 134 SER SER B . n 
B 1 143 THR 143 135 135 THR THR B . n 
B 1 144 LYS 144 136 136 LYS LYS B . n 
B 1 145 THR 145 137 137 THR THR B . n 
B 1 146 GLY 146 138 138 GLY GLY B . n 
B 1 147 ASN 147 139 139 ASN ASN B . n 
B 1 148 ALA 148 140 140 ALA ALA B . n 
B 1 149 GLY 149 141 141 GLY GLY B . n 
B 1 150 SER 150 142 142 SER SER B . n 
B 1 151 ARG 151 143 143 ARG ARG B . n 
B 1 152 LEU 152 144 144 LEU LEU B . n 
B 1 153 ALA 153 145 145 ALA ALA B . n 
B 1 154 ASP 154 146 146 ASP ASP B . n 
B 1 155 GLY 155 147 147 GLY GLY B . n 
B 1 156 VAL 156 148 148 VAL VAL B . n 
B 1 157 ILE 157 149 149 ILE ILE B . n 
B 1 158 GLY 158 150 150 GLY GLY B . n 
B 1 159 ILE 159 151 151 ILE ILE B . n 
B 1 160 ALA 160 152 152 ALA ALA B . n 
B 1 161 GLN 161 153 153 GLN GLN B . n 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              hanc210@snu.ac.kr 
_pdbx_contact_author.name_first         Nam-Chul 
_pdbx_contact_author.name_last          Ha 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-4813-748X 
# 
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 ZN  1  154 154 ZN  ZN  A . 
D 3 CU  1  155 155 CU  CU  A . 
E 4 CL  1  156 156 CL  CL  A . 
F 2 ZN  1  154 154 ZN  ZN  B . 
G 3 CU  1  155 155 CU  CU  B . 
H 5 HOH 1  157 157 HOH HOH A . 
H 5 HOH 2  158 158 HOH HOH A . 
H 5 HOH 3  159 159 HOH HOH A . 
H 5 HOH 4  160 160 HOH HOH A . 
H 5 HOH 5  161 161 HOH HOH A . 
H 5 HOH 6  162 162 HOH HOH A . 
H 5 HOH 7  163 163 HOH HOH A . 
H 5 HOH 8  164 164 HOH HOH A . 
H 5 HOH 9  165 165 HOH HOH A . 
H 5 HOH 10 166 166 HOH HOH A . 
H 5 HOH 11 167 167 HOH HOH A . 
H 5 HOH 12 168 168 HOH HOH A . 
H 5 HOH 13 169 169 HOH HOH A . 
H 5 HOH 14 170 170 HOH HOH A . 
H 5 HOH 15 171 171 HOH HOH A . 
H 5 HOH 16 172 172 HOH HOH A . 
H 5 HOH 17 173 173 HOH HOH A . 
H 5 HOH 18 174 174 HOH HOH A . 
H 5 HOH 19 175 175 HOH HOH A . 
H 5 HOH 20 176 176 HOH HOH A . 
H 5 HOH 21 177 177 HOH HOH A . 
H 5 HOH 22 178 178 HOH HOH A . 
H 5 HOH 23 179 179 HOH HOH A . 
H 5 HOH 24 180 180 HOH HOH A . 
H 5 HOH 25 181 181 HOH HOH A . 
H 5 HOH 26 182 182 HOH HOH A . 
H 5 HOH 27 183 183 HOH HOH A . 
H 5 HOH 28 184 184 HOH HOH A . 
H 5 HOH 29 185 185 HOH HOH A . 
H 5 HOH 30 186 186 HOH HOH A . 
H 5 HOH 31 187 187 HOH HOH A . 
H 5 HOH 32 188 188 HOH HOH A . 
H 5 HOH 33 189 189 HOH HOH A . 
H 5 HOH 34 190 190 HOH HOH A . 
H 5 HOH 35 191 191 HOH HOH A . 
H 5 HOH 36 192 192 HOH HOH A . 
H 5 HOH 37 193 193 HOH HOH A . 
H 5 HOH 38 194 194 HOH HOH A . 
H 5 HOH 39 195 195 HOH HOH A . 
H 5 HOH 40 196 196 HOH HOH A . 
H 5 HOH 41 197 197 HOH HOH A . 
H 5 HOH 42 198 198 HOH HOH A . 
H 5 HOH 43 199 199 HOH HOH A . 
H 5 HOH 44 200 200 HOH HOH A . 
H 5 HOH 45 201 201 HOH HOH A . 
H 5 HOH 46 202 202 HOH HOH A . 
H 5 HOH 47 203 203 HOH HOH A . 
H 5 HOH 48 204 204 HOH HOH A . 
H 5 HOH 49 205 205 HOH HOH A . 
H 5 HOH 50 206 206 HOH HOH A . 
H 5 HOH 51 207 207 HOH HOH A . 
H 5 HOH 52 208 208 HOH HOH A . 
H 5 HOH 53 209 209 HOH HOH A . 
H 5 HOH 54 210 210 HOH HOH A . 
H 5 HOH 55 211 211 HOH HOH A . 
H 5 HOH 56 212 212 HOH HOH A . 
H 5 HOH 57 213 213 HOH HOH A . 
H 5 HOH 58 214 214 HOH HOH A . 
H 5 HOH 59 215 215 HOH HOH A . 
H 5 HOH 60 216 216 HOH HOH A . 
H 5 HOH 61 217 217 HOH HOH A . 
H 5 HOH 62 218 218 HOH HOH A . 
H 5 HOH 63 219 219 HOH HOH A . 
H 5 HOH 64 220 220 HOH HOH A . 
H 5 HOH 65 221 221 HOH HOH A . 
H 5 HOH 66 222 222 HOH HOH A . 
H 5 HOH 67 223 223 HOH HOH A . 
H 5 HOH 68 224 224 HOH HOH A . 
H 5 HOH 69 225 225 HOH HOH A . 
H 5 HOH 70 226 226 HOH HOH A . 
H 5 HOH 71 227 227 HOH HOH A . 
H 5 HOH 72 228 228 HOH HOH A . 
H 5 HOH 73 229 229 HOH HOH A . 
H 5 HOH 74 230 230 HOH HOH A . 
H 5 HOH 75 231 231 HOH HOH A . 
H 5 HOH 76 232 232 HOH HOH A . 
H 5 HOH 77 233 233 HOH HOH A . 
H 5 HOH 78 234 234 HOH HOH A . 
I 5 HOH 1  156 156 HOH HOH B . 
I 5 HOH 2  157 157 HOH HOH B . 
I 5 HOH 3  158 158 HOH HOH B . 
I 5 HOH 4  159 159 HOH HOH B . 
I 5 HOH 5  160 160 HOH HOH B . 
I 5 HOH 6  161 161 HOH HOH B . 
I 5 HOH 7  162 162 HOH HOH B . 
I 5 HOH 8  163 163 HOH HOH B . 
I 5 HOH 9  164 164 HOH HOH B . 
I 5 HOH 10 165 165 HOH HOH B . 
I 5 HOH 11 166 166 HOH HOH B . 
I 5 HOH 12 167 167 HOH HOH B . 
I 5 HOH 13 168 168 HOH HOH B . 
I 5 HOH 14 169 169 HOH HOH B . 
I 5 HOH 15 170 170 HOH HOH B . 
I 5 HOH 16 171 171 HOH HOH B . 
I 5 HOH 17 172 172 HOH HOH B . 
I 5 HOH 18 173 173 HOH HOH B . 
I 5 HOH 19 174 174 HOH HOH B . 
I 5 HOH 20 175 175 HOH HOH B . 
I 5 HOH 21 176 176 HOH HOH B . 
I 5 HOH 22 177 177 HOH HOH B . 
I 5 HOH 23 178 178 HOH HOH B . 
I 5 HOH 24 179 179 HOH HOH B . 
I 5 HOH 25 180 180 HOH HOH B . 
I 5 HOH 26 181 181 HOH HOH B . 
I 5 HOH 27 182 182 HOH HOH B . 
I 5 HOH 28 183 183 HOH HOH B . 
I 5 HOH 29 184 184 HOH HOH B . 
I 5 HOH 30 185 185 HOH HOH B . 
I 5 HOH 31 186 186 HOH HOH B . 
I 5 HOH 32 187 187 HOH HOH B . 
I 5 HOH 33 188 188 HOH HOH B . 
I 5 HOH 34 189 189 HOH HOH B . 
I 5 HOH 35 190 190 HOH HOH B . 
I 5 HOH 36 191 191 HOH HOH B . 
I 5 HOH 37 192 192 HOH HOH B . 
I 5 HOH 38 193 193 HOH HOH B . 
I 5 HOH 39 194 194 HOH HOH B . 
I 5 HOH 40 195 195 HOH HOH B . 
I 5 HOH 41 196 196 HOH HOH B . 
I 5 HOH 42 197 197 HOH HOH B . 
I 5 HOH 43 198 198 HOH HOH B . 
I 5 HOH 44 199 199 HOH HOH B . 
I 5 HOH 45 200 200 HOH HOH B . 
I 5 HOH 46 201 201 HOH HOH B . 
I 5 HOH 47 202 202 HOH HOH B . 
I 5 HOH 48 203 203 HOH HOH B . 
I 5 HOH 49 204 204 HOH HOH B . 
I 5 HOH 50 205 205 HOH HOH B . 
I 5 HOH 51 206 206 HOH HOH B . 
I 5 HOH 52 207 207 HOH HOH B . 
I 5 HOH 53 208 208 HOH HOH B . 
I 5 HOH 54 209 209 HOH HOH B . 
I 5 HOH 55 210 210 HOH HOH B . 
I 5 HOH 56 211 211 HOH HOH B . 
I 5 HOH 57 212 212 HOH HOH B . 
I 5 HOH 58 213 213 HOH HOH B . 
I 5 HOH 59 214 214 HOH HOH B . 
I 5 HOH 60 215 215 HOH HOH B . 
I 5 HOH 61 216 216 HOH HOH B . 
I 5 HOH 62 217 217 HOH HOH B . 
I 5 HOH 63 218 218 HOH HOH B . 
I 5 HOH 64 219 219 HOH HOH B . 
I 5 HOH 65 220 220 HOH HOH B . 
I 5 HOH 66 221 221 HOH HOH B . 
I 5 HOH 67 222 222 HOH HOH B . 
I 5 HOH 68 223 223 HOH HOH B . 
I 5 HOH 69 224 224 HOH HOH B . 
I 5 HOH 70 225 225 HOH HOH B . 
I 5 HOH 71 226 226 HOH HOH B . 
I 5 HOH 72 227 227 HOH HOH B . 
I 5 HOH 73 228 228 HOH HOH B . 
I 5 HOH 74 229 229 HOH HOH B . 
I 5 HOH 75 230 230 HOH HOH B . 
I 5 HOH 76 231 231 HOH HOH B . 
I 5 HOH 77 232 232 HOH HOH B . 
# 
loop_
_pdbx_struct_mod_residue.id 
_pdbx_struct_mod_residue.label_asym_id 
_pdbx_struct_mod_residue.label_comp_id 
_pdbx_struct_mod_residue.label_seq_id 
_pdbx_struct_mod_residue.auth_asym_id 
_pdbx_struct_mod_residue.auth_comp_id 
_pdbx_struct_mod_residue.auth_seq_id 
_pdbx_struct_mod_residue.PDB_ins_code 
_pdbx_struct_mod_residue.parent_comp_id 
_pdbx_struct_mod_residue.details 
1 A CSO 119 A CSO 111 ? CYS 'modified residue' 
2 B CSO 119 B CSO 111 ? CYS 'modified residue' 
# 
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_and_software_defined_assembly PISA monomeric 1 
2 author_and_software_defined_assembly PISA 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,D,E,H 
2 1 B,F,G,I   
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 130  ? 
1 MORE         -13  ? 
1 'SSA (A^2)'  7750 ? 
2 'ABSA (A^2)' 120  ? 
2 MORE         -13  ? 
2 'SSA (A^2)'  7440 ? 
# 
_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_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  ND1 ? A HIS 54 ? A HIS 46 ? 1_555 CU ? D CU . ? A CU 155 ? 1_555 NE2 ? A HIS 56  ? A HIS 48  ? 1_555 139.3 ? 
2  ND1 ? A HIS 54 ? A HIS 46 ? 1_555 CU ? D CU . ? A CU 155 ? 1_555 NE2 ? A HIS 128 ? A HIS 120 ? 1_555 93.9  ? 
3  NE2 ? A HIS 56 ? A HIS 48 ? 1_555 CU ? D CU . ? A CU 155 ? 1_555 NE2 ? A HIS 128 ? A HIS 120 ? 1_555 115.8 ? 
4  ND1 ? A HIS 71 ? A HIS 63 ? 1_555 ZN ? C ZN . ? A ZN 154 ? 1_555 ND1 ? A HIS 79  ? A HIS 71  ? 1_555 105.3 ? 
5  ND1 ? A HIS 71 ? A HIS 63 ? 1_555 ZN ? C ZN . ? A ZN 154 ? 1_555 ND1 ? A HIS 88  ? A HIS 80  ? 1_555 112.7 ? 
6  ND1 ? A HIS 79 ? A HIS 71 ? 1_555 ZN ? C ZN . ? A ZN 154 ? 1_555 ND1 ? A HIS 88  ? A HIS 80  ? 1_555 121.7 ? 
7  ND1 ? A HIS 71 ? A HIS 63 ? 1_555 ZN ? C ZN . ? A ZN 154 ? 1_555 OD1 ? A ASP 91  ? A ASP 83  ? 1_555 105.1 ? 
8  ND1 ? A HIS 79 ? A HIS 71 ? 1_555 ZN ? C ZN . ? A ZN 154 ? 1_555 OD1 ? A ASP 91  ? A ASP 83  ? 1_555 97.7  ? 
9  ND1 ? A HIS 88 ? A HIS 80 ? 1_555 ZN ? C ZN . ? A ZN 154 ? 1_555 OD1 ? A ASP 91  ? A ASP 83  ? 1_555 112.4 ? 
10 ND1 ? B HIS 54 ? B HIS 46 ? 1_555 CU ? G CU . ? B CU 155 ? 1_555 NE2 ? B HIS 56  ? B HIS 48  ? 1_555 143.0 ? 
11 ND1 ? B HIS 54 ? B HIS 46 ? 1_555 CU ? G CU . ? B CU 155 ? 1_555 NE2 ? B HIS 71  ? B HIS 63  ? 1_555 84.2  ? 
12 NE2 ? B HIS 56 ? B HIS 48 ? 1_555 CU ? G CU . ? B CU 155 ? 1_555 NE2 ? B HIS 71  ? B HIS 63  ? 1_555 104.3 ? 
13 ND1 ? B HIS 54 ? B HIS 46 ? 1_555 CU ? G CU . ? B CU 155 ? 1_555 NE2 ? B HIS 128 ? B HIS 120 ? 1_555 100.6 ? 
14 NE2 ? B HIS 56 ? B HIS 48 ? 1_555 CU ? G CU . ? B CU 155 ? 1_555 NE2 ? B HIS 128 ? B HIS 120 ? 1_555 91.6  ? 
15 NE2 ? B HIS 71 ? B HIS 63 ? 1_555 CU ? G CU . ? B CU 155 ? 1_555 NE2 ? B HIS 128 ? B HIS 120 ? 1_555 146.6 ? 
16 ND1 ? B HIS 71 ? B HIS 63 ? 1_555 ZN ? F ZN . ? B ZN 154 ? 1_555 ND1 ? B HIS 79  ? B HIS 71  ? 1_555 102.0 ? 
17 ND1 ? B HIS 71 ? B HIS 63 ? 1_555 ZN ? F ZN . ? B ZN 154 ? 1_555 ND1 ? B HIS 88  ? B HIS 80  ? 1_555 113.3 ? 
18 ND1 ? B HIS 79 ? B HIS 71 ? 1_555 ZN ? F ZN . ? B ZN 154 ? 1_555 ND1 ? B HIS 88  ? B HIS 80  ? 1_555 123.0 ? 
19 ND1 ? B HIS 71 ? B HIS 63 ? 1_555 ZN ? F ZN . ? B ZN 154 ? 1_555 OD1 ? B ASP 91  ? B ASP 83  ? 1_555 97.7  ? 
20 ND1 ? B HIS 79 ? B HIS 71 ? 1_555 ZN ? F ZN . ? B ZN 154 ? 1_555 OD1 ? B ASP 91  ? B ASP 83  ? 1_555 96.1  ? 
21 ND1 ? B HIS 88 ? B HIS 80 ? 1_555 ZN ? F ZN . ? B ZN 154 ? 1_555 OD1 ? B ASP 91  ? B ASP 83  ? 1_555 120.3 ? 
# 
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 2022-10-12 
2 'Structure model' 1 1 2022-10-26 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  2 'Structure model' '_citation.country'                 
2  2 'Structure model' '_citation.journal_abbrev'          
3  2 'Structure model' '_citation.journal_id_CSD'          
4  2 'Structure model' '_citation.journal_id_ISSN'         
5  2 'Structure model' '_citation.journal_volume'          
6  2 'Structure model' '_citation.page_first'              
7  2 'Structure model' '_citation.page_last'               
8  2 'Structure model' '_citation.pdbx_database_id_DOI'    
9  2 'Structure model' '_citation.pdbx_database_id_PubMed' 
10 2 'Structure model' '_citation.title'                   
11 2 'Structure model' '_citation.year'                    
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z       
2 -x,y+1/2,-z 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? 1.19.1_4122 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP   ? ? ? .           4 
# 
_pdbx_entry_details.entry_id                 7FB6 
_pdbx_entry_details.nonpolymer_details       ? 
_pdbx_entry_details.sequence_details         ? 
_pdbx_entry_details.compound_details         ? 
_pdbx_entry_details.source_details           ? 
_pdbx_entry_details.has_ligand_of_interest   Y 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    ASP 
_pdbx_validate_torsion.auth_asym_id    B 
_pdbx_validate_torsion.auth_seq_id     90 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             -69.42 
_pdbx_validate_torsion.psi             -175.75 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLY -7 ? A GLY 1  
2  1 Y 1 A ALA -6 ? A ALA 2  
3  1 Y 1 A MET -5 ? A MET 3  
4  1 Y 1 A ASP -4 ? A ASP 4  
5  1 Y 1 A PRO -3 ? A PRO 5  
6  1 Y 1 A GLU -2 ? A GLU 6  
7  1 Y 1 B GLY -7 ? B GLY 1  
8  1 Y 1 B ALA -6 ? B ALA 2  
9  1 Y 1 B MET -5 ? B MET 3  
10 1 Y 1 B ASP -4 ? B ASP 4  
11 1 Y 1 B PRO -3 ? B PRO 5  
12 1 Y 1 B GLU -2 ? B GLU 6  
13 1 Y 1 B PHE -1 ? B PHE 7  
14 1 Y 1 B MET 0  ? B MET 8  
15 1 Y 1 B ASP 52 ? B ASP 60 
16 1 Y 1 B ASN 53 ? B ASN 61 
17 1 Y 1 B THR 54 ? B THR 62 
18 1 Y 1 B ALA 55 ? B ALA 63 
19 1 Y 1 B GLY 56 ? B GLY 64 
20 1 Y 1 B ASP 57 ? B ASP 65 
21 1 Y 1 B THR 58 ? B THR 66 
22 1 Y 1 B SER 59 ? B SER 67 
23 1 Y 1 B ALA 60 ? B ALA 68 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
loop_
_pdbx_entity_instance_feature.ordinal 
_pdbx_entity_instance_feature.comp_id 
_pdbx_entity_instance_feature.asym_id 
_pdbx_entity_instance_feature.seq_num 
_pdbx_entity_instance_feature.auth_comp_id 
_pdbx_entity_instance_feature.auth_asym_id 
_pdbx_entity_instance_feature.auth_seq_num 
_pdbx_entity_instance_feature.feature_type 
_pdbx_entity_instance_feature.details 
1 CU ? ? CU ? ? 'SUBJECT OF INVESTIGATION' ? 
2 ZN ? ? ZN ? ? 'SUBJECT OF INVESTIGATION' ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'        ZN  
3 'COPPER (II) ION' CU  
4 'CHLORIDE ION'    CL  
5 water             HOH 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'light scattering' 
_pdbx_struct_assembly_auth_evidence.details                
'Multi-angle light scattering combined with size exclusion chromatography' 
# 
_space_group.name_H-M_alt     'P 1 21 1' 
_space_group.name_Hall        'P 2yb' 
_space_group.IT_number        4 
_space_group.crystal_system   monoclinic 
_space_group.id               1 
# 
