data_5O3Y
# 
_entry.id   5O3Y 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.302 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   5O3Y         
WWPDB D_1200005016 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        5O3Y 
_pdbx_database_status.recvd_initial_deposition_date   2017-05-25 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Capper, M.J.'   1 ? 
'Wright, G.S.A.' 2 ? 
'Antonyuk, S.V.' 3 ? 
'Hasnain, S.S.'  4 ? 
# 
_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            'Nat Commun' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2041-1723 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            9 
_citation.language                  ? 
_citation.page_first                1693 
_citation.page_last                 1693 
_citation.title                     'The cysteine-reactive small molecule ebselen facilitates effective SOD1 maturation.' 
_citation.year                      2018 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41467-018-04114-x 
_citation.pdbx_database_id_PubMed   29703933 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Capper, M.J.'   1  ? 
primary 'Wright, G.S.A.' 2  ? 
primary 'Barbieri, L.'   3  ? 
primary 'Luchinat, E.'   4  ? 
primary 'Mercatelli, E.' 5  ? 
primary 'McAlary, L.'    6  ? 
primary 'Yerbury, J.J.'  7  ? 
primary 
;O'Neill, P.M.
;
8  ? 
primary 'Antonyuk, S.V.' 9  ? 
primary 'Banci, L.'      10 ? 
primary 'Hasnain, S.S.'  11 ? 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   106.73 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     5O3Y 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     38.050 
_cell.length_a_esd                 ? 
_cell.length_b                     67.960 
_cell.length_b_esd                 ? 
_cell.length_c                     51.180 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_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             ? 
# 
_symmetry.entry_id                         5O3Y 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_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]'     15827.561 2   1.15.1.1 ? ? ? 
2 non-polymer syn 'ZINC ION'                         65.409    4   ?        ? ? ? 
3 non-polymer syn '~{N}-phenyl-2-sulfanyl-benzamide' 229.298   2   ?        ? ? ? 
4 non-polymer syn 'SULFATE ION'                      96.063    2   ?        ? ? ? 
5 water       nat water                              18.015    313 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Superoxide dismutase 1,hSod1' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_entity_poly.pdbx_strand_id                 A,F 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ALA n 
1 2   THR n 
1 3   LYS n 
1 4   ALA n 
1 5   VAL n 
1 6   CYS n 
1 7   VAL n 
1 8   LEU n 
1 9   LYS n 
1 10  GLY n 
1 11  ASP n 
1 12  GLY n 
1 13  PRO n 
1 14  VAL n 
1 15  GLN n 
1 16  GLY n 
1 17  ILE n 
1 18  ILE n 
1 19  ASN n 
1 20  PHE n 
1 21  GLU n 
1 22  GLN n 
1 23  LYS n 
1 24  GLU n 
1 25  SER n 
1 26  ASN n 
1 27  GLY n 
1 28  PRO n 
1 29  VAL n 
1 30  LYS n 
1 31  VAL n 
1 32  TRP n 
1 33  GLY n 
1 34  SER n 
1 35  ILE n 
1 36  LYS n 
1 37  GLY n 
1 38  LEU n 
1 39  THR n 
1 40  GLU n 
1 41  GLY n 
1 42  LEU n 
1 43  HIS n 
1 44  GLY n 
1 45  PHE n 
1 46  HIS n 
1 47  VAL n 
1 48  HIS n 
1 49  GLU n 
1 50  PHE n 
1 51  GLY n 
1 52  ASP n 
1 53  ASN n 
1 54  THR n 
1 55  ALA n 
1 56  GLY n 
1 57  CYS n 
1 58  THR n 
1 59  SER n 
1 60  ALA n 
1 61  GLY n 
1 62  PRO n 
1 63  HIS n 
1 64  PHE n 
1 65  ASN n 
1 66  PRO n 
1 67  LEU n 
1 68  SER n 
1 69  ARG n 
1 70  LYS n 
1 71  HIS n 
1 72  GLY n 
1 73  GLY n 
1 74  PRO n 
1 75  LYS n 
1 76  ASP n 
1 77  GLU n 
1 78  GLU n 
1 79  ARG n 
1 80  HIS n 
1 81  VAL n 
1 82  GLY n 
1 83  ASP n 
1 84  LEU n 
1 85  GLY n 
1 86  ASN n 
1 87  VAL n 
1 88  THR n 
1 89  ALA n 
1 90  ASP n 
1 91  LYS n 
1 92  ASP n 
1 93  GLY n 
1 94  VAL n 
1 95  ALA n 
1 96  ASP n 
1 97  VAL n 
1 98  SER n 
1 99  ILE n 
1 100 GLU n 
1 101 ASP n 
1 102 SER n 
1 103 VAL n 
1 104 ILE n 
1 105 SER n 
1 106 LEU n 
1 107 SER n 
1 108 GLY n 
1 109 ASP n 
1 110 HIS n 
1 111 CYS n 
1 112 ILE n 
1 113 ILE n 
1 114 GLY n 
1 115 ARG n 
1 116 THR n 
1 117 LEU n 
1 118 VAL n 
1 119 VAL n 
1 120 HIS n 
1 121 GLU n 
1 122 LYS n 
1 123 ALA n 
1 124 ASP n 
1 125 ASP n 
1 126 LEU n 
1 127 GLY n 
1 128 LYS n 
1 129 GLY n 
1 130 GLY n 
1 131 ASN n 
1 132 GLU n 
1 133 GLU n 
1 134 SER n 
1 135 THR n 
1 136 LYS n 
1 137 THR n 
1 138 GLY n 
1 139 ASN n 
1 140 ALA n 
1 141 GLY n 
1 142 SER n 
1 143 ARG n 
1 144 LEU n 
1 145 ALA n 
1 146 CYS n 
1 147 GLY n 
1 148 VAL n 
1 149 ILE n 
1 150 GLY n 
1 151 ILE n 
1 152 ALA n 
1 153 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                   153 
_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                       pET26b 
_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   
;ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_struct_ref.pdbx_align_begin           2 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 5O3Y A 1 ? 153 ? P00441 2 ? 154 ? 1 153 
2 1 5O3Y F 1 ? 153 ? P00441 2 ? 154 ? 1 153 
# 
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 
9JK non-polymer         . '~{N}-phenyl-2-sulfanyl-benzamide' ? 'C13 H11 N O S'  229.298 
ALA 'L-peptide linking' y ALANINE                            ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE                           ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE                         ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                    ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE                           ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE                          ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                    ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                            ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE                          ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                              ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE                         ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                            ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                             ? 'C6 H15 N2 O2 1' 147.195 
PHE 'L-peptide linking' y PHENYLALANINE                      ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE                            ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE                             ? 'C3 H7 N O3'     105.093 
SO4 non-polymer         . 'SULFATE ION'                      ? 'O4 S -2'        96.063  
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                   5O3Y 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                      ? 
_exptl_crystal.density_diffrn              ? 
_exptl_crystal.density_Matthews            2.00 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         38.56 
_exptl_crystal.description                 Plates 
_exptl_crystal.F_000                       ? 
_exptl_crystal.id                          1 
_exptl_crystal.preparation                 ? 
_exptl_crystal.size_max                    ? 
_exptl_crystal.size_mid                    ? 
_exptl_crystal.size_min                    ? 
_exptl_crystal.size_rad                    ? 
_exptl_crystal.colour_lustre               ? 
_exptl_crystal.colour_modifier             ? 
_exptl_crystal.colour_primary              ? 
_exptl_crystal.density_meas                ? 
_exptl_crystal.density_meas_esd            ? 
_exptl_crystal.density_meas_gt             ? 
_exptl_crystal.density_meas_lt             ? 
_exptl_crystal.density_meas_temp           ? 
_exptl_crystal.density_meas_temp_esd       ? 
_exptl_crystal.density_meas_temp_gt        ? 
_exptl_crystal.density_meas_temp_lt        ? 
_exptl_crystal.pdbx_crystal_image_url      ? 
_exptl_crystal.pdbx_crystal_image_format   ? 
_exptl_crystal.pdbx_mosaicity              ? 
_exptl_crystal.pdbx_mosaicity_esd          ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              3.75 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp            293 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '100 mM NaAct pH 3.75, 100 mM NaCl, 2.8 M AmSO4' 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.ambient_environment    ? 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.ambient_temp_esd       ? 
_diffrn.crystal_id             1 
_diffrn.crystal_support        ? 
_diffrn.crystal_treatment      ? 
_diffrn.details                ? 
_diffrn.id                     1 
_diffrn.ambient_pressure       ? 
_diffrn.ambient_pressure_esd   ? 
_diffrn.ambient_pressure_gt    ? 
_diffrn.ambient_pressure_lt    ? 
_diffrn.ambient_temp_gt        ? 
_diffrn.ambient_temp_lt        ? 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS 6M-F' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2016-01-24 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    'Double crystal' 
_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   0.987 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'DIAMOND BEAMLINE I02' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.987 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I02 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate            ? 
_reflns.entry_id                         5O3Y 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                1.3 
_reflns.d_resolution_low                 67.84 
_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                       60537 
_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             98.8 
_reflns.R_free_details                   ? 
_reflns.Rmerge_F_all                     ? 
_reflns.Rmerge_F_obs                     ? 
_reflns.Friedel_coverage                 ? 
_reflns.number_gt                        ? 
_reflns.threshold_expression             ? 
_reflns.pdbx_redundancy                  3 
_reflns.pdbx_Rmerge_I_obs                0.064 
_reflns.pdbx_Rmerge_I_all                ? 
_reflns.pdbx_Rsym_value                  ? 
_reflns.pdbx_netI_over_av_sigmaI         ? 
_reflns.pdbx_netI_over_sigmaI            7.1 
_reflns.pdbx_res_netI_over_av_sigmaI_2   ? 
_reflns.pdbx_res_netI_over_sigmaI_2      ? 
_reflns.pdbx_chi_squared                 ? 
_reflns.pdbx_scaling_rejects             ? 
_reflns.pdbx_d_res_high_opt              ? 
_reflns.pdbx_d_res_low_opt               ? 
_reflns.pdbx_d_res_opt_method            ? 
_reflns.phase_calculation_details        ? 
_reflns.pdbx_Rrim_I_all                  ? 
_reflns.pdbx_Rpim_I_all                  ? 
_reflns.pdbx_d_opt                       ? 
_reflns.pdbx_number_measured_all         ? 
_reflns.pdbx_diffrn_id                   1 
_reflns.pdbx_ordinal                     1 
_reflns.pdbx_CC_half                     ? 
_reflns.pdbx_R_split                     ? 
# 
_reflns_shell.d_res_high                  1.3 
_reflns_shell.d_res_low                   1.33 
_reflns_shell.meanI_over_sigI_all         ? 
_reflns_shell.meanI_over_sigI_obs         1.4 
_reflns_shell.number_measured_all         ? 
_reflns_shell.number_measured_obs         ? 
_reflns_shell.number_possible             ? 
_reflns_shell.number_unique_all           ? 
_reflns_shell.number_unique_obs           ? 
_reflns_shell.percent_possible_all        97.7 
_reflns_shell.percent_possible_obs        ? 
_reflns_shell.Rmerge_F_all                ? 
_reflns_shell.Rmerge_F_obs                ? 
_reflns_shell.Rmerge_I_all                ? 
_reflns_shell.Rmerge_I_obs                0.566 
_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             2.8 
_reflns_shell.pdbx_Rsym_value             ? 
_reflns_shell.pdbx_chi_squared            ? 
_reflns_shell.pdbx_netI_over_sigmaI_all   ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs   ? 
_reflns_shell.pdbx_Rrim_I_all             ? 
_reflns_shell.pdbx_Rpim_I_all             ? 
_reflns_shell.pdbx_rejects                ? 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_CC_half                ? 
_reflns_shell.pdbx_R_split                ? 
# 
_refine.aniso_B[1][1]                            -0.81 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            -0.63 
_refine.aniso_B[2][2]                            0.95 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            0.20 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               15.110 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.975 
_refine.correlation_coeff_Fo_to_Fc_free          0.964 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_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                                 5O3Y 
_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                            1.30 
_refine.ls_d_res_low                             49.01 
_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                     57561 
_refine.ls_number_reflns_R_free                  2943 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.71 
_refine.ls_percent_reflns_R_free                 4.9 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.15308 
_refine.ls_R_factor_R_free                       0.18566 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.15144 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      2v0a 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.056 
_refine.pdbx_overall_ESU_R_Free                  0.053 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             2.328 
_refine.overall_SU_ML                            0.042 
_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                         1 
_refine_hist.pdbx_number_atoms_protein        2220 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         46 
_refine_hist.number_atoms_solvent             313 
_refine_hist.number_atoms_total               2579 
_refine_hist.d_res_high                       1.30 
_refine_hist.d_res_low                        49.01 
# 
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' ? 0.010  0.019  2377 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.002  0.020  2086 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.425  1.949  3239 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 1.541  2.998  4836 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.475  5.000  326  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 38.755 24.947 95   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 11.118 15.000 349  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 10.068 15.000 10   ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.078  0.200  349  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.005  0.020  2806 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.002  0.020  472  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 1.434  1.312  1277 ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 1.424  1.312  1276 ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 1.999  1.987  1612 ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 2.001  1.987  1613 ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 2.004  1.555  1100 ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.002  1.555  1097 ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 2.515  2.238  1622 ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 5.305  18.654 2593 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 4.345  17.701 2525 ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? 3.541  3.000  4451 ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? 30.637 5.000  181  ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? 12.458 5.000  4519 ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.300 
_refine_ls_shell.d_res_low                        1.334 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             218 
_refine_ls_shell.number_reflns_R_work             4198 
_refine_ls_shell.percent_reflns_obs               97.59 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free                  0.322 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.299 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
# 
_struct.entry_id                     5O3Y 
_struct.title                        'SOD1 bound to Ebsulfur' 
_struct.pdbx_descriptor              'Superoxide dismutase [Cu-Zn] (E.C.1.15.1.1)' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        5O3Y 
_struct_keywords.text            'OXIDOREDUCTASE Drug discovery ALS MND, 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 2 ? 
F N N 4 ? 
G N N 2 ? 
H N N 2 ? 
I N N 3 ? 
J N N 4 ? 
K N N 5 ? 
L 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 ALA A 55  ? GLY A 61  ? ALA A 55  GLY A 61  5 ? 7 
HELX_P HELX_P2 AA2 ASN A 131 ? LYS A 136 ? ASN A 131 LYS A 136 5 ? 6 
HELX_P HELX_P3 AA3 ALA B 55  ? GLY B 61  ? ALA F 55  GLY F 61  5 ? 7 
HELX_P HELX_P4 AA4 SER B 107 ? CYS B 111 ? SER F 107 CYS F 111 5 ? 5 
HELX_P HELX_P5 AA5 ASN B 131 ? LYS B 136 ? ASN F 131 LYS F 136 5 ? 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 
disulf1  disulf ?    ? A CYS 57  SG  ? ? ? 1_555 A CYS 146 SG  ? ? A CYS 57  A CYS 146 1_555 ? ? ? ? ? ? ? 2.106 ? 
disulf2  disulf ?    ? B CYS 57  SG  ? ? ? 1_555 B CYS 146 SG  ? ? F CYS 57  F CYS 146 1_555 ? ? ? ? ? ? ? 2.087 ? 
metalc1  metalc ?    ? A HIS 46  ND1 ? ? ? 1_555 E ZN  .   ZN  ? ? A HIS 46  A ZN  503 1_555 ? ? ? ? ? ? ? 2.169 ? 
metalc2  metalc ?    ? A HIS 48  NE2 ? ? ? 1_555 E ZN  .   ZN  ? ? A HIS 48  A ZN  503 1_555 ? ? ? ? ? ? ? 2.059 ? 
metalc3  metalc ?    ? A HIS 63  ND1 ? ? ? 1_555 C ZN  .   ZN  ? ? A HIS 63  A ZN  501 1_555 ? ? ? ? ? ? ? 2.018 ? 
metalc4  metalc ?    ? A HIS 71  ND1 ? ? ? 1_555 C ZN  .   ZN  ? ? A HIS 71  A ZN  501 1_555 ? ? ? ? ? ? ? 2.052 ? 
metalc5  metalc ?    ? A HIS 80  ND1 ? ? ? 1_555 C ZN  .   ZN  ? ? A HIS 80  A ZN  501 1_555 ? ? ? ? ? ? ? 2.024 ? 
metalc6  metalc ?    ? A ASP 83  OD1 ? ? ? 1_555 C ZN  .   ZN  ? ? A ASP 83  A ZN  501 1_555 ? ? ? ? ? ? ? 1.953 ? 
covale1  covale none ? A CYS 111 SG  ? ? ? 1_555 D 9JK .   S01 ? ? A CYS 111 A 9JK 502 1_555 ? ? ? ? ? ? ? 2.030 ? 
metalc7  metalc ?    ? A HIS 120 NE2 ? ? ? 1_555 E ZN  .   ZN  ? ? A HIS 120 A ZN  503 1_555 ? ? ? ? ? ? ? 1.964 ? 
metalc8  metalc ?    ? B HIS 46  ND1 ? ? ? 1_555 H ZN  .   ZN  ? ? F HIS 46  F ZN  502 1_555 ? ? ? ? ? ? ? 2.249 ? 
metalc9  metalc ?    ? B HIS 48  NE2 ? ? ? 1_555 H ZN  .   ZN  ? ? F HIS 48  F ZN  502 1_555 ? ? ? ? ? ? ? 2.063 ? 
metalc10 metalc ?    ? B HIS 63  ND1 ? ? ? 1_555 G ZN  .   ZN  ? ? F HIS 63  F ZN  501 1_555 ? ? ? ? ? ? ? 2.052 ? 
metalc11 metalc ?    ? B HIS 71  ND1 ? ? ? 1_555 G ZN  .   ZN  ? ? F HIS 71  F ZN  501 1_555 ? ? ? ? ? ? ? 2.050 ? 
metalc12 metalc ?    ? B HIS 80  ND1 ? ? ? 1_555 G ZN  .   ZN  ? ? F HIS 80  F ZN  501 1_555 ? ? ? ? ? ? ? 2.023 ? 
metalc13 metalc ?    ? B ASP 83  OD1 ? ? ? 1_555 G ZN  .   ZN  ? ? F ASP 83  F ZN  501 1_555 ? ? ? ? ? ? ? 1.955 ? 
covale2  covale none ? B CYS 111 SG  ? ? ? 1_555 I 9JK .   S01 ? ? F CYS 111 F 9JK 503 1_555 ? ? ? ? ? ? ? 2.046 ? 
metalc14 metalc ?    ? B HIS 120 NE2 ? ? ? 1_555 H ZN  .   ZN  ? ? F HIS 120 F ZN  502 1_555 ? ? ? ? ? ? ? 1.861 ? 
metalc15 metalc ?    ? E ZN  .   ZN  ? ? ? 1_555 F SO4 .   O4  ? ? A ZN  503 A SO4 504 1_555 ? ? ? ? ? ? ? 1.982 ? 
metalc16 metalc ?    ? H ZN  .   ZN  ? ? ? 1_555 J SO4 .   O1  ? ? F ZN  502 F SO4 504 1_555 ? ? ? ? ? ? ? 2.043 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
covale ? ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          GLY 
_struct_mon_prot_cis.label_seq_id           12 
_struct_mon_prot_cis.label_asym_id          B 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           GLY 
_struct_mon_prot_cis.auth_seq_id            12 
_struct_mon_prot_cis.auth_asym_id           F 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    13 
_struct_mon_prot_cis.pdbx_label_asym_id_2   B 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     13 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    F 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       0.06 
# 
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 95  ? ASP A 101 ? ALA A 95  ASP A 101 
AA1 2 VAL A 29  ? LYS A 36  ? VAL A 29  LYS A 36  
AA1 3 GLN A 15  ? GLN A 22  ? GLN A 15  GLN A 22  
AA1 4 THR A 2   ? LEU A 8   ? THR A 2   LEU A 8   
AA1 5 GLY A 150 ? ALA A 152 ? GLY A 150 ALA A 152 
AA2 1 ASP A 83  ? ALA A 89  ? ASP A 83  ALA A 89  
AA2 2 GLY A 41  ? HIS A 48  ? GLY A 41  HIS A 48  
AA2 3 THR A 116 ? HIS A 120 ? THR A 116 HIS A 120 
AA2 4 ARG A 143 ? VAL A 148 ? ARG A 143 VAL A 148 
AA3 1 ALA B 95  ? ASP B 101 ? ALA F 95  ASP F 101 
AA3 2 VAL B 29  ? LYS B 36  ? VAL F 29  LYS F 36  
AA3 3 VAL B 14  ? GLN B 22  ? VAL F 14  GLN F 22  
AA3 4 THR B 2   ? GLY B 10  ? THR F 2   GLY F 10  
AA3 5 GLY B 150 ? ILE B 151 ? GLY F 150 ILE F 151 
AA4 1 ASP B 83  ? ALA B 89  ? ASP F 83  ALA F 89  
AA4 2 GLY B 41  ? HIS B 48  ? GLY F 41  HIS F 48  
AA4 3 THR B 116 ? HIS B 120 ? THR F 116 HIS F 120 
AA4 4 ARG B 143 ? VAL B 148 ? ARG F 143 VAL F 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 ALA A 95  ? O ALA A 95  N ILE A 35  ? N ILE A 35  
AA1 2 3 O TRP A 32  ? O TRP A 32  N ASN A 19  ? N ASN A 19  
AA1 3 4 O GLN A 22  ? O GLN A 22  N THR A 2   ? N THR A 2   
AA1 4 5 N VAL A 5   ? N VAL A 5   O GLY A 150 ? O GLY A 150 
AA2 1 2 O ALA A 89  ? O ALA A 89  N GLY A 41  ? N GLY A 41  
AA2 2 3 N HIS A 48  ? N HIS A 48  O THR A 116 ? O THR A 116 
AA2 3 4 N VAL A 119 ? N VAL A 119 O ALA A 145 ? O ALA A 145 
AA3 1 2 O ILE B 99  ? O ILE F 99  N VAL B 31  ? N VAL F 31  
AA3 2 3 O TRP B 32  ? O TRP F 32  N ASN B 19  ? N ASN F 19  
AA3 3 4 O GLN B 22  ? O GLN F 22  N THR B 2   ? N THR F 2   
AA3 4 5 N VAL B 5   ? N VAL F 5   O GLY B 150 ? O GLY F 150 
AA4 1 2 O ALA B 89  ? O ALA F 89  N GLY B 41  ? N GLY F 41  
AA4 2 3 N HIS B 48  ? N HIS F 48  O THR B 116 ? O THR F 116 
AA4 3 4 N VAL B 119 ? N VAL F 119 O ALA B 145 ? O ALA F 145 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software A ZN  501 ? 4  'binding site for residue ZN A 501'                   
AC2 Software A 9JK 502 ? 9  'binding site for residue 9JK A 502'                  
AC3 Software A ZN  503 ? 5  'binding site for residue ZN A 503'                   
AC4 Software A SO4 504 ? 11 'binding site for residue SO4 A 504'                  
AC5 Software F ZN  501 ? 4  'binding site for residue ZN F 501'                   
AC6 Software F ZN  502 ? 5  'binding site for residue ZN F 502'                   
AC7 Software F SO4 504 ? 10 'binding site for residue SO4 F 504'                  
AC8 Software F ARG 69  ? 12 'binding site for Di-peptide ARG F 69 and GLU F 78'   
AC9 Software F 9JK 503 ? 15 'binding site for Di-peptide 9JK F 503 and CYS F 111' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 4  HIS A 63  ? HIS A 63  . ? 1_555 ? 
2  AC1 4  HIS A 71  ? HIS A 71  . ? 1_555 ? 
3  AC1 4  HIS A 80  ? HIS A 80  . ? 1_555 ? 
4  AC1 4  ASP A 83  ? ASP A 83  . ? 1_555 ? 
5  AC2 9  GLN A 15  ? GLN A 15  . ? 1_655 ? 
6  AC2 9  LYS A 36  ? LYS A 36  . ? 1_655 ? 
7  AC2 9  LEU A 106 ? LEU A 106 . ? 1_555 ? 
8  AC2 9  SER A 107 ? SER A 107 . ? 1_555 ? 
9  AC2 9  GLY A 108 ? GLY A 108 . ? 1_555 ? 
10 AC2 9  CYS A 111 ? CYS A 111 . ? 1_555 ? 
11 AC2 9  ILE A 113 ? ILE A 113 . ? 1_555 ? 
12 AC2 9  HOH K .   ? HOH A 683 . ? 1_555 ? 
13 AC2 9  9JK I .   ? 9JK F 503 . ? 1_555 ? 
14 AC3 5  HIS A 46  ? HIS A 46  . ? 1_555 ? 
15 AC3 5  HIS A 48  ? HIS A 48  . ? 1_555 ? 
16 AC3 5  HIS A 63  ? HIS A 63  . ? 1_555 ? 
17 AC3 5  HIS A 120 ? HIS A 120 . ? 1_555 ? 
18 AC3 5  SO4 F .   ? SO4 A 504 . ? 1_555 ? 
19 AC4 11 HIS A 46  ? HIS A 46  . ? 1_555 ? 
20 AC4 11 HIS A 48  ? HIS A 48  . ? 1_555 ? 
21 AC4 11 HIS A 63  ? HIS A 63  . ? 1_555 ? 
22 AC4 11 HIS A 120 ? HIS A 120 . ? 1_555 ? 
23 AC4 11 THR A 137 ? THR A 137 . ? 1_555 ? 
24 AC4 11 ARG A 143 ? ARG A 143 . ? 1_555 ? 
25 AC4 11 ZN  E .   ? ZN  A 503 . ? 1_555 ? 
26 AC4 11 HOH K .   ? HOH A 604 . ? 1_555 ? 
27 AC4 11 HOH K .   ? HOH A 609 . ? 1_555 ? 
28 AC4 11 HOH K .   ? HOH A 621 . ? 1_555 ? 
29 AC4 11 HOH K .   ? HOH A 637 . ? 1_555 ? 
30 AC5 4  HIS B 63  ? HIS F 63  . ? 1_555 ? 
31 AC5 4  HIS B 71  ? HIS F 71  . ? 1_555 ? 
32 AC5 4  HIS B 80  ? HIS F 80  . ? 1_555 ? 
33 AC5 4  ASP B 83  ? ASP F 83  . ? 1_555 ? 
34 AC6 5  HIS B 46  ? HIS F 46  . ? 1_555 ? 
35 AC6 5  HIS B 48  ? HIS F 48  . ? 1_555 ? 
36 AC6 5  HIS B 63  ? HIS F 63  . ? 1_555 ? 
37 AC6 5  HIS B 120 ? HIS F 120 . ? 1_555 ? 
38 AC6 5  SO4 J .   ? SO4 F 504 . ? 1_555 ? 
39 AC7 10 HIS B 46  ? HIS F 46  . ? 1_555 ? 
40 AC7 10 HIS B 48  ? HIS F 48  . ? 1_555 ? 
41 AC7 10 HIS B 63  ? HIS F 63  . ? 1_555 ? 
42 AC7 10 HIS B 120 ? HIS F 120 . ? 1_555 ? 
43 AC7 10 THR B 137 ? THR F 137 . ? 1_555 ? 
44 AC7 10 ARG B 143 ? ARG F 143 . ? 1_555 ? 
45 AC7 10 ZN  H .   ? ZN  F 502 . ? 1_555 ? 
46 AC7 10 HOH L .   ? HOH F 609 . ? 1_555 ? 
47 AC7 10 HOH L .   ? HOH F 614 . ? 1_555 ? 
48 AC7 10 HOH L .   ? HOH F 617 . ? 1_555 ? 
49 AC8 12 ASN B 65  ? ASN F 65  . ? 1_555 ? 
50 AC8 12 LEU B 67  ? LEU F 67  . ? 1_555 ? 
51 AC8 12 SER B 68  ? SER F 68  . ? 1_555 ? 
52 AC8 12 LYS B 70  ? LYS F 70  . ? 1_555 ? 
53 AC8 12 GLY B 72  ? GLY F 72  . ? 1_555 ? 
54 AC8 12 ASP B 76  ? ASP F 76  . ? 1_555 ? 
55 AC8 12 GLU B 77  ? GLU F 77  . ? 1_555 ? 
56 AC8 12 ARG B 79  ? ARG F 79  . ? 1_555 ? 
57 AC8 12 HIS B 80  ? HIS F 80  . ? 1_555 ? 
58 AC8 12 HOH L .   ? HOH F 635 . ? 1_555 ? 
59 AC8 12 HOH L .   ? HOH F 678 . ? 1_555 ? 
60 AC8 12 HOH L .   ? HOH F 682 . ? 1_555 ? 
61 AC9 15 ILE A 113 ? ILE A 113 . ? 1_555 ? 
62 AC9 15 9JK D .   ? 9JK A 502 . ? 1_555 ? 
63 AC9 15 PHE B 64  ? PHE F 64  . ? 1_555 ? 
64 AC9 15 SER B 105 ? SER F 105 . ? 1_555 ? 
65 AC9 15 LEU B 106 ? LEU F 106 . ? 1_555 ? 
66 AC9 15 SER B 107 ? SER F 107 . ? 1_555 ? 
67 AC9 15 GLY B 108 ? GLY F 108 . ? 1_555 ? 
68 AC9 15 ASP B 109 ? ASP F 109 . ? 1_555 ? 
69 AC9 15 HIS B 110 ? HIS F 110 . ? 1_555 ? 
70 AC9 15 ILE B 112 ? ILE F 112 . ? 1_555 ? 
71 AC9 15 ILE B 113 ? ILE F 113 . ? 1_555 ? 
72 AC9 15 ARG B 115 ? ARG F 115 . ? 1_555 ? 
73 AC9 15 HOH L .   ? HOH F 612 . ? 1_555 ? 
74 AC9 15 HOH L .   ? HOH F 663 . ? 1_555 ? 
75 AC9 15 HOH L .   ? HOH F 668 . ? 1_555 ? 
# 
_atom_sites.entry_id                    5O3Y 
_atom_sites.fract_transf_matrix[1][1]   0.026281 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.007900 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.014714 
_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]   0.020402 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . ALA A 1 1   ? 27.541 5.927   30.647  0.60 25.08 ? 1   ALA A N   1 
ATOM   2    C  CA  . ALA A 1 1   ? 26.635 4.807   30.238  0.60 21.99 ? 1   ALA A CA  1 
ATOM   3    C  C   . ALA A 1 1   ? 26.273 4.878   28.760  0.60 17.99 ? 1   ALA A C   1 
ATOM   4    O  O   . ALA A 1 1   ? 26.249 5.950   28.169  0.60 20.56 ? 1   ALA A O   1 
ATOM   5    C  CB  . ALA A 1 1   ? 25.364 4.808   31.074  0.60 24.57 ? 1   ALA A CB  1 
ATOM   6    N  N   . THR A 1 2   ? 25.977 3.719   28.183  0.70 16.31 ? 2   THR A N   1 
ATOM   7    C  CA  . THR A 1 2   ? 25.527 3.616   26.802  0.70 14.95 ? 2   THR A CA  1 
ATOM   8    C  C   . THR A 1 2   ? 24.087 3.133   26.829  0.90 10.99 ? 2   THR A C   1 
ATOM   9    O  O   . THR A 1 2   ? 23.713 2.349   27.707  0.80 10.34 ? 2   THR A O   1 
ATOM   10   C  CB  . THR A 1 2   ? 26.419 2.664   25.987  0.70 17.28 ? 2   THR A CB  1 
ATOM   11   O  OG1 . THR A 1 2   ? 27.788 3.064   26.126  0.70 19.43 ? 2   THR A OG1 1 
ATOM   12   C  CG2 . THR A 1 2   ? 26.055 2.694   24.508  0.70 18.04 ? 2   THR A CG2 1 
ATOM   13   N  N   . LYS A 1 3   ? 23.284 3.622   25.891  1.00 11.15 ? 3   LYS A N   1 
ATOM   14   C  CA  . LYS A 1 3   ? 21.886 3.234   25.781  1.00 11.26 ? 3   LYS A CA  1 
ATOM   15   C  C   . LYS A 1 3   ? 21.562 2.900   24.355  1.00 9.56  ? 3   LYS A C   1 
ATOM   16   O  O   . LYS A 1 3   ? 22.131 3.495   23.424  1.00 9.84  ? 3   LYS A O   1 
ATOM   17   C  CB  . LYS A 1 3   ? 20.975 4.358   26.272  1.00 13.69 ? 3   LYS A CB  1 
ATOM   18   C  CG  . LYS A 1 3   ? 21.125 4.652   27.749  1.00 17.62 ? 3   LYS A CG  1 
ATOM   19   C  CD  . LYS A 1 3   ? 20.134 5.713   28.208  1.00 20.27 ? 3   LYS A CD  1 
ATOM   20   C  CE  . LYS A 1 3   ? 20.207 5.943   29.706  1.00 23.44 ? 3   LYS A CE  1 
ATOM   21   N  NZ  . LYS A 1 3   ? 21.510 6.514   30.155  0.10 22.45 ? 3   LYS A NZ  1 
ATOM   22   N  N   . ALA A 1 4   ? 20.624 1.987   24.182  1.00 9.24  ? 4   ALA A N   1 
ATOM   23   C  CA  . ALA A 1 4   ? 20.143 1.613   22.863  1.00 9.00  ? 4   ALA A CA  1 
ATOM   24   C  C   . ALA A 1 4   ? 18.654 1.358   22.934  1.00 8.25  ? 4   ALA A C   1 
ATOM   25   O  O   . ALA A 1 4   ? 18.083 1.242   24.018  1.00 8.93  ? 4   ALA A O   1 
ATOM   26   C  CB  . ALA A 1 4   ? 20.910 0.410   22.303  1.00 8.42  ? 4   ALA A CB  1 
ATOM   27   N  N   . VAL A 1 5   ? 18.017 1.262   21.778  1.00 8.98  ? 5   VAL A N   1 
ATOM   28   C  CA  . VAL A 1 5   ? 16.569 1.105   21.735  1.00 9.61  ? 5   VAL A CA  1 
ATOM   29   C  C   . VAL A 1 5   ? 16.197 0.357   20.467  1.00 8.34  ? 5   VAL A C   1 
ATOM   30   O  O   . VAL A 1 5   ? 16.953 0.371   19.486  1.00 9.72  ? 5   VAL A O   1 
ATOM   31   C  CB  . VAL A 1 5   ? 15.860 2.483   21.845  1.00 10.77 ? 5   VAL A CB  1 
ATOM   32   C  CG1 . VAL A 1 5   ? 16.143 3.359   20.628  1.00 11.33 ? 5   VAL A CG1 1 
ATOM   33   C  CG2 . VAL A 1 5   ? 14.364 2.321   22.077  1.00 13.35 ? 5   VAL A CG2 1 
ATOM   34   N  N   . CYS A 1 6   ? 15.047 -0.301  20.488  1.00 9.11  ? 6   CYS A N   1 
ATOM   35   C  CA  . CYS A 1 6   ? 14.573 -1.054  19.360  1.00 9.03  ? 6   CYS A CA  1 
ATOM   36   C  C   . CYS A 1 6   ? 13.063 -1.023  19.308  1.00 9.01  ? 6   CYS A C   1 
ATOM   37   O  O   . CYS A 1 6   ? 12.412 -1.268  20.314  1.00 9.95  ? 6   CYS A O   1 
ATOM   38   C  CB  . CYS A 1 6   ? 15.056 -2.500  19.488  1.00 9.65  ? 6   CYS A CB  1 
ATOM   39   S  SG  . CYS A 1 6   ? 14.628 -3.546  18.099  1.00 11.36 ? 6   CYS A SG  1 
ATOM   40   N  N   . VAL A 1 7   ? 12.508 -0.722  18.146  1.00 9.05  ? 7   VAL A N   1 
ATOM   41   C  CA  . VAL A 1 7   ? 11.079 -0.805  17.897  1.00 10.25 ? 7   VAL A CA  1 
ATOM   42   C  C   . VAL A 1 7   ? 10.817 -2.108  17.179  1.00 9.99  ? 7   VAL A C   1 
ATOM   43   O  O   . VAL A 1 7   ? 11.342 -2.336  16.087  1.00 11.03 ? 7   VAL A O   1 
ATOM   44   C  CB  . VAL A 1 7   ? 10.599 0.341   17.000  1.00 12.60 ? 7   VAL A CB  1 
ATOM   45   C  CG1 . VAL A 1 7   ? 9.102  0.232   16.743  1.00 15.47 ? 7   VAL A CG1 1 
ATOM   46   C  CG2 . VAL A 1 7   ? 10.934 1.669   17.639  1.00 13.43 ? 7   VAL A CG2 1 
ATOM   47   N  N   . LEU A 1 8   ? 10.011 -2.963  17.791  1.00 9.98  ? 8   LEU A N   1 
ATOM   48   C  CA  . LEU A 1 8   ? 9.631  -4.235  17.182  1.00 9.98  ? 8   LEU A CA  1 
ATOM   49   C  C   . LEU A 1 8   ? 8.337  -4.101  16.406  1.00 10.20 ? 8   LEU A C   1 
ATOM   50   O  O   . LEU A 1 8   ? 7.324  -3.693  16.973  1.00 11.64 ? 8   LEU A O   1 
ATOM   51   C  CB  . LEU A 1 8   ? 9.455  -5.297  18.267  1.00 10.50 ? 8   LEU A CB  1 
ATOM   52   C  CG  . LEU A 1 8   ? 10.687 -5.644  19.107  1.00 11.84 ? 8   LEU A CG  1 
ATOM   53   C  CD1 . LEU A 1 8   ? 10.310 -6.545  20.286  1.00 12.53 ? 8   LEU A CD1 1 
ATOM   54   C  CD2 . LEU A 1 8   ? 11.728 -6.342  18.255  1.00 13.59 ? 8   LEU A CD2 1 
ATOM   55   N  N   . LYS A 1 9   ? 8.389  -4.423  15.116  1.00 10.53 ? 9   LYS A N   1 
ATOM   56   C  CA  . LYS A 1 9   ? 7.233  -4.409  14.224  1.00 12.24 ? 9   LYS A CA  1 
ATOM   57   C  C   . LYS A 1 9   ? 7.248  -5.658  13.360  1.00 12.26 ? 9   LYS A C   1 
ATOM   58   O  O   . LYS A 1 9   ? 8.307  -6.217  13.084  1.00 12.83 ? 9   LYS A O   1 
ATOM   59   C  CB  . LYS A 1 9   ? 7.274  -3.194  13.290  1.00 14.37 ? 9   LYS A CB  1 
ATOM   60   C  CG  . LYS A 1 9   ? 7.294  -1.857  13.992  0.50 15.24 ? 9   LYS A CG  1 
ATOM   61   C  CD  . LYS A 1 9   ? 6.848  -0.677  13.036  0.00 21.93 ? 9   LYS A CD  1 
ATOM   62   C  CE  . LYS A 1 9   ? 6.913  0.686   13.681  0.00 21.64 ? 9   LYS A CE  1 
ATOM   63   N  NZ  . LYS A 1 9   ? 5.754  0.927   14.564  0.00 25.50 ? 9   LYS A NZ  1 
ATOM   64   N  N   . GLY A 1 10  ? 6.074  -6.080  12.915  1.00 14.21 ? 10  GLY A N   1 
ATOM   65   C  CA  . GLY A 1 10  ? 5.975  -7.179  11.961  1.00 16.73 ? 10  GLY A CA  1 
ATOM   66   C  C   . GLY A 1 10  ? 4.751  -7.097  11.080  1.00 18.58 ? 10  GLY A C   1 
ATOM   67   O  O   . GLY A 1 10  ? 4.132  -6.042  10.954  1.00 23.94 ? 10  GLY A O   1 
ATOM   68   N  N   . ASP A 1 11  ? 4.411  -8.223  10.463  1.00 20.97 ? 11  ASP A N   1 
ATOM   69   C  CA  . ASP A 1 11  ? 3.275  -8.295  9.536   1.00 23.65 ? 11  ASP A CA  1 
ATOM   70   C  C   . ASP A 1 11  ? 1.920  -8.480  10.221  1.00 23.35 ? 11  ASP A C   1 
ATOM   71   O  O   . ASP A 1 11  ? 0.888  -8.411  9.555   1.00 29.88 ? 11  ASP A O   1 
ATOM   72   C  CB  . ASP A 1 11  ? 3.487  -9.430  8.525   1.00 27.13 ? 11  ASP A CB  1 
ATOM   73   C  CG  . ASP A 1 11  ? 4.697  -9.209  7.636   0.50 28.68 ? 11  ASP A CG  1 
ATOM   74   O  OD1 . ASP A 1 11  ? 5.148  -8.050  7.494   0.50 30.76 ? 11  ASP A OD1 1 
ATOM   75   O  OD2 . ASP A 1 11  ? 5.196  -10.203 7.073   0.50 30.19 ? 11  ASP A OD2 1 
ATOM   76   N  N   . GLY A 1 12  ? 1.919  -8.710  11.533  1.00 21.35 ? 12  GLY A N   1 
ATOM   77   C  CA  . GLY A 1 12  ? 0.699  -9.015  12.271  1.00 20.44 ? 12  GLY A CA  1 
ATOM   78   C  C   . GLY A 1 12  ? 0.514  -8.136  13.492  1.00 19.28 ? 12  GLY A C   1 
ATOM   79   O  O   . GLY A 1 12  ? 0.954  -6.985  13.492  1.00 20.71 ? 12  GLY A O   1 
ATOM   80   N  N   . PRO A 1 13  ? -0.135 -8.673  14.546  1.00 19.27 ? 13  PRO A N   1 
ATOM   81   C  CA  . PRO A 1 13  ? -0.467 -7.862  15.726  1.00 20.03 ? 13  PRO A CA  1 
ATOM   82   C  C   . PRO A 1 13  ? 0.698  -7.502  16.651  1.00 17.26 ? 13  PRO A C   1 
ATOM   83   O  O   . PRO A 1 13  ? 0.541  -6.608  17.487  1.00 18.81 ? 13  PRO A O   1 
ATOM   84   C  CB  . PRO A 1 13  ? -1.463 -8.750  16.484  1.00 23.50 ? 13  PRO A CB  1 
ATOM   85   C  CG  . PRO A 1 13  ? -1.054 -10.131 16.125  1.00 22.69 ? 13  PRO A CG  1 
ATOM   86   C  CD  . PRO A 1 13  ? -0.658 -10.050 14.678  1.00 21.55 ? 13  PRO A CD  1 
ATOM   87   N  N   . VAL A 1 14  ? 1.845  -8.169  16.518  1.00 15.20 ? 14  VAL A N   1 
ATOM   88   C  CA  . VAL A 1 14  ? 2.907  -8.023  17.503  1.00 14.09 ? 14  VAL A CA  1 
ATOM   89   C  C   . VAL A 1 14  ? 3.690  -6.726  17.279  1.00 13.51 ? 14  VAL A C   1 
ATOM   90   O  O   . VAL A 1 14  ? 4.161  -6.439  16.174  1.00 14.87 ? 14  VAL A O   1 
ATOM   91   C  CB  . VAL A 1 14  ? 3.851  -9.246  17.533  1.00 14.04 ? 14  VAL A CB  1 
ATOM   92   C  CG1 . VAL A 1 14  ? 4.932  -9.070  18.585  1.00 14.00 ? 14  VAL A CG1 1 
ATOM   93   C  CG2 . VAL A 1 14  ? 3.070  -10.525 17.808  1.00 13.88 ? 14  VAL A CG2 1 
ATOM   94   N  N   . GLN A 1 15  ? 3.825  -5.951  18.347  1.00 12.65 ? 15  GLN A N   1 
ATOM   95   C  CA  . GLN A 1 15  ? 4.679  -4.780  18.328  1.00 12.95 ? 15  GLN A CA  1 
ATOM   96   C  C   . GLN A 1 15  ? 5.216  -4.523  19.715  1.00 11.88 ? 15  GLN A C   1 
ATOM   97   O  O   . GLN A 1 15  ? 4.616  -4.940  20.706  1.00 12.57 ? 15  GLN A O   1 
ATOM   98   C  CB  . GLN A 1 15  ? 3.920  -3.559  17.822  1.00 15.64 ? 15  GLN A CB  1 
ATOM   99   C  CG  . GLN A 1 15  ? 2.784  -3.135  18.723  1.00 17.09 ? 15  GLN A CG  1 
ATOM   100  C  CD  . GLN A 1 15  ? 2.063  -1.926  18.188  0.50 17.72 ? 15  GLN A CD  1 
ATOM   101  O  OE1 . GLN A 1 15  ? 1.411  -1.990  17.152  0.50 17.61 ? 15  GLN A OE1 1 
ATOM   102  N  NE2 . GLN A 1 15  ? 2.175  -0.812  18.894  0.50 19.35 ? 15  GLN A NE2 1 
ATOM   103  N  N   . GLY A 1 16  ? 6.337  -3.833  19.796  1.00 10.43 ? 16  GLY A N   1 
ATOM   104  C  CA  . GLY A 1 16  ? 6.926  -3.535  21.077  1.00 10.87 ? 16  GLY A CA  1 
ATOM   105  C  C   . GLY A 1 16  ? 7.995  -2.483  21.037  1.00 8.26  ? 16  GLY A C   1 
ATOM   106  O  O   . GLY A 1 16  ? 8.389  -2.010  19.968  1.00 9.84  ? 16  GLY A O   1 
ATOM   107  N  N   . ILE A 1 17  ? 8.459  -2.125  22.225  1.00 8.63  ? 17  ILE A N   1 
ATOM   108  C  CA  . ILE A 1 17  ? 9.549  -1.172  22.404  1.00 9.55  ? 17  ILE A CA  1 
ATOM   109  C  C   . ILE A 1 17  ? 10.481 -1.760  23.439  1.00 8.46  ? 17  ILE A C   1 
ATOM   110  O  O   . ILE A 1 17  ? 10.026 -2.121  24.534  1.00 9.08  ? 17  ILE A O   1 
ATOM   111  C  CB  . ILE A 1 17  ? 9.044  0.186   22.939  1.00 11.55 ? 17  ILE A CB  1 
ATOM   112  C  CG1 . ILE A 1 17  ? 8.016  0.831   22.001  1.00 15.19 ? 17  ILE A CG1 1 
ATOM   113  C  CG2 . ILE A 1 17  ? 10.219 1.113   23.226  1.00 11.61 ? 17  ILE A CG2 1 
ATOM   114  C  CD1 . ILE A 1 17  ? 8.571  1.408   20.727  1.00 16.88 ? 17  ILE A CD1 1 
ATOM   115  N  N   . ILE A 1 18  ? 11.767 -1.873  23.102  1.00 8.45  ? 18  ILE A N   1 
ATOM   116  C  CA  . ILE A 1 18  ? 12.742 -2.444  24.009  1.00 7.91  ? 18  ILE A CA  1 
ATOM   117  C  C   . ILE A 1 18  ? 13.913 -1.498  24.168  1.00 7.71  ? 18  ILE A C   1 
ATOM   118  O  O   . ILE A 1 18  ? 14.463 -1.015  23.166  1.00 9.08  ? 18  ILE A O   1 
ATOM   119  C  CB  . ILE A 1 18  ? 13.228 -3.819  23.510  1.00 8.65  ? 18  ILE A CB  1 
ATOM   120  C  CG1 . ILE A 1 18  ? 12.048 -4.795  23.394  1.00 9.99  ? 18  ILE A CG1 1 
ATOM   121  C  CG2 . ILE A 1 18  ? 14.321 -4.348  24.417  1.00 9.28  ? 18  ILE A CG2 1 
ATOM   122  C  CD1 . ILE A 1 18  ? 11.436 -5.236  24.713  1.00 11.18 ? 18  ILE A CD1 1 
ATOM   123  N  N   . ASN A 1 19  ? 14.290 -1.267  25.418  1.00 8.03  ? 19  ASN A N   1 
ATOM   124  C  CA  . ASN A 1 19  ? 15.391 -0.397  25.798  1.00 8.27  ? 19  ASN A CA  1 
ATOM   125  C  C   . ASN A 1 19  ? 16.552 -1.207  26.328  1.00 7.81  ? 19  ASN A C   1 
ATOM   126  O  O   . ASN A 1 19  ? 16.339 -2.229  26.969  1.00 9.11  ? 19  ASN A O   1 
ATOM   127  C  CB  . ASN A 1 19  ? 14.939 0.534   26.915  1.00 9.04  ? 19  ASN A CB  1 
ATOM   128  C  CG  . ASN A 1 19  ? 13.701 1.308   26.559  1.00 9.57  ? 19  ASN A CG  1 
ATOM   129  O  OD1 . ASN A 1 19  ? 12.583 0.941   26.932  1.00 13.59 ? 19  ASN A OD1 1 
ATOM   130  N  ND2 . ASN A 1 19  ? 13.885 2.353   25.806  1.00 10.07 ? 19  ASN A ND2 1 
ATOM   131  N  N   . PHE A 1 20  ? 17.767 -0.740  26.069  1.00 8.79  ? 20  PHE A N   1 
ATOM   132  C  CA  . PHE A 1 20  ? 18.984 -1.355  26.574  1.00 7.96  ? 20  PHE A CA  1 
ATOM   133  C  C   . PHE A 1 20  ? 19.822 -0.303  27.273  1.00 8.26  ? 20  PHE A C   1 
ATOM   134  O  O   . PHE A 1 20  ? 19.953 0.810   26.761  1.00 9.62  ? 20  PHE A O   1 
ATOM   135  C  CB  . PHE A 1 20  ? 19.826 -1.923  25.429  1.00 8.45  ? 20  PHE A CB  1 
ATOM   136  C  CG  . PHE A 1 20  ? 19.126 -2.942  24.568  1.00 9.17  ? 20  PHE A CG  1 
ATOM   137  C  CD1 . PHE A 1 20  ? 18.276 -2.545  23.545  1.00 10.94 ? 20  PHE A CD1 1 
ATOM   138  C  CD2 . PHE A 1 20  ? 19.342 -4.312  24.767  1.00 9.98  ? 20  PHE A CD2 1 
ATOM   139  C  CE1 . PHE A 1 20  ? 17.645 -3.486  22.735  1.00 11.47 ? 20  PHE A CE1 1 
ATOM   140  C  CE2 . PHE A 1 20  ? 18.713 -5.252  23.960  1.00 11.20 ? 20  PHE A CE2 1 
ATOM   141  C  CZ  . PHE A 1 20  ? 17.862 -4.842  22.950  1.00 12.01 ? 20  PHE A CZ  1 
ATOM   142  N  N   . GLU A 1 21  ? 20.423 -0.646  28.402  1.00 8.92  ? 21  GLU A N   1 
ATOM   143  C  CA  . GLU A 1 21  ? 21.316 0.281   29.118  1.00 9.99  ? 21  GLU A CA  1 
ATOM   144  C  C   . GLU A 1 21  ? 22.503 -0.465  29.691  1.00 9.41  ? 21  GLU A C   1 
ATOM   145  O  O   . GLU A 1 21  ? 22.349 -1.512  30.302  1.00 11.27 ? 21  GLU A O   1 
ATOM   146  C  CB  . GLU A 1 21  ? 20.588 1.048   30.228  1.00 12.76 ? 21  GLU A CB  1 
ATOM   147  C  CG  . GLU A 1 21  ? 21.479 2.069   30.942  1.00 16.03 ? 21  GLU A CG  1 
ATOM   148  C  CD  . GLU A 1 21  ? 20.722 3.038   31.835  0.50 20.41 ? 21  GLU A CD  1 
ATOM   149  O  OE1 . GLU A 1 21  ? 19.481 2.943   31.935  0.50 20.58 ? 21  GLU A OE1 1 
ATOM   150  O  OE2 . GLU A 1 21  ? 21.380 3.915   32.437  0.50 23.60 ? 21  GLU A OE2 1 
ATOM   151  N  N   . GLN A 1 22  ? 23.688 0.097   29.522  1.00 10.20 ? 22  GLN A N   1 
ATOM   152  C  CA  . GLN A 1 22  ? 24.919 -0.486  30.028  1.00 10.84 ? 22  GLN A CA  1 
ATOM   153  C  C   . GLN A 1 22  ? 25.694 0.624   30.716  1.00 12.59 ? 22  GLN A C   1 
ATOM   154  O  O   . GLN A 1 22  ? 26.136 1.563   30.065  1.00 16.30 ? 22  GLN A O   1 
ATOM   155  C  CB  . GLN A 1 22  ? 25.716 -1.088  28.879  1.00 11.91 ? 22  GLN A CB  1 
ATOM   156  C  CG  . GLN A 1 22  ? 26.891 -1.931  29.327  1.00 12.08 ? 22  GLN A CG  1 
ATOM   157  C  CD  . GLN A 1 22  ? 27.641 -2.543  28.165  1.00 12.48 ? 22  GLN A CD  1 
ATOM   158  O  OE1 . GLN A 1 22  ? 27.669 -1.984  27.067  1.00 14.36 ? 22  GLN A OE1 1 
ATOM   159  N  NE2 . GLN A 1 22  ? 28.282 -3.685  28.401  1.00 13.94 ? 22  GLN A NE2 1 
ATOM   160  N  N   . LYS A 1 23  ? 25.846 0.513   32.031  1.00 15.00 ? 23  LYS A N   1 
ATOM   161  C  CA  . LYS A 1 23  ? 26.449 1.581   32.830  1.00 21.50 ? 23  LYS A CA  1 
ATOM   162  C  C   . LYS A 1 23  ? 27.962 1.637   32.664  1.00 21.12 ? 23  LYS A C   1 
ATOM   163  O  O   . LYS A 1 23  ? 28.546 2.723   32.612  1.00 25.32 ? 23  LYS A O   1 
ATOM   164  C  CB  . LYS A 1 23  ? 26.089 1.432   34.313  1.00 31.42 ? 23  LYS A CB  1 
ATOM   165  C  CG  . LYS A 1 23  ? 24.597 1.494   34.599  1.00 51.80 ? 23  LYS A CG  1 
ATOM   166  C  CD  . LYS A 1 23  ? 24.217 1.567   36.054  0.00 29.12 ? 23  LYS A CD  1 
ATOM   167  C  CE  . LYS A 1 23  ? 24.410 0.157   36.570  0.00 26.18 ? 23  LYS A CE  1 
ATOM   168  N  NZ  . LYS A 1 23  ? 23.661 -0.190  37.828  0.00 31.27 ? 23  LYS A NZ  1 
ATOM   169  N  N   . GLU A 1 24  ? 28.585 0.480   32.579  1.00 23.66 ? 24  GLU A N   1 
ATOM   170  C  CA  . GLU A 1 24  ? 30.028 0.340   32.454  1.00 28.18 ? 24  GLU A CA  1 
ATOM   171  C  C   . GLU A 1 24  ? 30.389 -0.401  31.190  1.00 25.88 ? 24  GLU A C   1 
ATOM   172  O  O   . GLU A 1 24  ? 29.705 -1.347  30.797  1.00 25.08 ? 24  GLU A O   1 
ATOM   173  C  CB  . GLU A 1 24  ? 30.588 -0.423  33.656  1.00 30.81 ? 24  GLU A CB  1 
ATOM   174  C  CG  . GLU A 1 24  ? 30.550 0.360   34.954  1.00 35.24 ? 24  GLU A CG  1 
ATOM   175  C  CD  . GLU A 1 24  ? 31.047 -0.451  36.073  0.00 32.08 ? 24  GLU A CD  1 
ATOM   176  O  OE1 . GLU A 1 24  ? 31.209 -1.682  35.934  0.00 25.10 ? 24  GLU A OE1 1 
ATOM   177  O  OE2 . GLU A 1 24  ? 31.265 0.147   37.148  0.00 34.11 ? 24  GLU A OE2 1 
ATOM   178  N  N   . SER A 1 25  ? 31.508 0.019   30.600  1.00 28.19 ? 25  SER A N   1 
ATOM   179  C  CA  . SER A 1 25  ? 32.121 -0.746  29.534  1.00 29.21 ? 25  SER A CA  1 
ATOM   180  C  C   . SER A 1 25  ? 32.351 -2.143  30.086  1.00 32.75 ? 25  SER A C   1 
ATOM   181  O  O   . SER A 1 25  ? 32.904 -2.305  31.181  1.00 38.17 ? 25  SER A O   1 
ATOM   182  C  CB  . SER A 1 25  ? 33.451 -0.126  29.096  0.50 31.68 ? 25  SER A CB  1 
ATOM   183  O  OG  . SER A 1 25  ? 34.182 -1.153  28.348  0.00 38.29 ? 25  SER A OG  1 
ATOM   184  N  N   . ASN A 1 26  ? 31.863 -3.136  29.353  1.00 30.12 ? 26  ASN A N   1 
ATOM   185  C  CA  . ASN A 1 26  ? 31.962 -4.542  29.739  1.00 30.22 ? 26  ASN A CA  1 
ATOM   186  C  C   . ASN A 1 26  ? 31.183 -4.915  31.024  1.00 30.56 ? 26  ASN A C   1 
ATOM   187  O  O   . ASN A 1 26  ? 31.472 -5.943  31.640  1.00 38.15 ? 26  ASN A O   1 
ATOM   188  C  CB  . ASN A 1 26  ? 33.441 -4.966  29.873  1.00 31.73 ? 26  ASN A CB  1 
ATOM   189  C  CG  . ASN A 1 26  ? 34.293 -4.546  28.686  0.50 28.19 ? 26  ASN A CG  1 
ATOM   190  O  OD1 . ASN A 1 26  ? 34.027 -4.928  27.549  0.50 28.70 ? 26  ASN A OD1 1 
ATOM   191  N  ND2 . ASN A 1 26  ? 35.337 -3.769  28.952  0.50 26.36 ? 26  ASN A ND2 1 
ATOM   192  N  N   . GLY A 1 27  ? 30.201 -4.097  31.419  1.00 23.27 ? 27  GLY A N   1 
ATOM   193  C  CA  . GLY A 1 27  ? 29.297 -4.421  32.537  1.00 20.45 ? 27  GLY A CA  1 
ATOM   194  C  C   . GLY A 1 27  ? 28.028 -5.055  31.981  1.00 17.62 ? 27  GLY A C   1 
ATOM   195  O  O   . GLY A 1 27  ? 27.875 -5.143  30.768  1.00 18.31 ? 27  GLY A O   1 
ATOM   196  N  N   . PRO A 1 28  ? 27.098 -5.484  32.854  1.00 15.52 ? 28  PRO A N   1 
ATOM   197  C  CA  . PRO A 1 28  ? 25.862 -6.087  32.347  1.00 14.89 ? 28  PRO A CA  1 
ATOM   198  C  C   . PRO A 1 28  ? 24.973 -5.090  31.626  1.00 11.32 ? 28  PRO A C   1 
ATOM   199  O  O   . PRO A 1 28  ? 25.043 -3.882  31.876  1.00 12.99 ? 28  PRO A O   1 
ATOM   200  C  CB  . PRO A 1 28  ? 25.160 -6.598  33.612  1.00 17.94 ? 28  PRO A CB  1 
ATOM   201  C  CG  . PRO A 1 28  ? 25.697 -5.751  34.697  1.00 20.75 ? 28  PRO A CG  1 
ATOM   202  C  CD  . PRO A 1 28  ? 27.118 -5.446  34.326  1.00 18.66 ? 28  PRO A CD  1 
ATOM   203  N  N   . VAL A 1 29  ? 24.124 -5.599  30.748  1.00 10.34 ? 29  VAL A N   1 
ATOM   204  C  CA  . VAL A 1 29  ? 23.181 -4.771  30.009  1.00 10.09 ? 29  VAL A CA  1 
ATOM   205  C  C   . VAL A 1 29  ? 21.791 -5.035  30.569  1.00 9.24  ? 29  VAL A C   1 
ATOM   206  O  O   . VAL A 1 29  ? 21.347 -6.182  30.651  1.00 10.57 ? 29  VAL A O   1 
ATOM   207  C  CB  . VAL A 1 29  ? 23.209 -5.092  28.505  1.00 9.95  ? 29  VAL A CB  1 
ATOM   208  C  CG1 . VAL A 1 29  ? 22.236 -4.206  27.739  1.00 9.75  ? 29  VAL A CG1 1 
ATOM   209  C  CG2 . VAL A 1 29  ? 24.620 -4.934  27.940  1.00 10.72 ? 29  VAL A CG2 1 
ATOM   210  N  N   . LYS A 1 30  ? 21.103 -3.975  30.963  1.00 9.45  ? 30  LYS A N   1 
ATOM   211  C  CA  . LYS A 1 30  ? 19.707 -4.063  31.350  1.00 10.04 ? 30  LYS A CA  1 
ATOM   212  C  C   . LYS A 1 30  ? 18.828 -3.921  30.124  1.00 8.95  ? 30  LYS A C   1 
ATOM   213  O  O   . LYS A 1 30  ? 19.064 -3.037  29.300  1.00 10.16 ? 30  LYS A O   1 
ATOM   214  C  CB  . LYS A 1 30  ? 19.379 -2.969  32.373  1.00 12.53 ? 30  LYS A CB  1 
ATOM   215  C  CG  . LYS A 1 30  ? 20.074 -3.172  33.706  1.00 18.51 ? 30  LYS A CG  1 
ATOM   216  C  CD  . LYS A 1 30  ? 19.458 -2.429  34.847  0.00 14.93 ? 30  LYS A CD  1 
ATOM   217  C  CE  . LYS A 1 30  ? 20.104 -2.710  36.198  0.00 13.81 ? 30  LYS A CE  1 
ATOM   218  N  NZ  . LYS A 1 30  ? 19.904 -1.517  37.052  0.00 13.26 ? 30  LYS A NZ  1 
ATOM   219  N  N   . VAL A 1 31  ? 17.841 -4.798  29.993  1.00 9.61  ? 31  VAL A N   1 
ATOM   220  C  CA  . VAL A 1 31  ? 16.939 -4.825  28.845  1.00 10.90 ? 31  VAL A CA  1 
ATOM   221  C  C   . VAL A 1 31  ? 15.543 -4.704  29.411  1.00 9.71  ? 31  VAL A C   1 
ATOM   222  O  O   . VAL A 1 31  ? 15.153 -5.514  30.229  1.00 12.26 ? 31  VAL A O   1 
ATOM   223  C  CB  . VAL A 1 31  ? 17.072 -6.150  28.054  1.00 11.33 ? 31  VAL A CB  1 
ATOM   224  C  CG1 . VAL A 1 31  ? 16.201 -6.128  26.808  1.00 11.38 ? 31  VAL A CG1 1 
ATOM   225  C  CG2 . VAL A 1 31  ? 18.533 -6.432  27.710  1.00 10.38 ? 31  VAL A CG2 1 
ATOM   226  N  N   A TRP A 1 32  ? 14.787 -3.702  28.987  0.50 11.18 ? 32  TRP A N   1 
ATOM   227  N  N   B TRP A 1 32  ? 14.796 -3.688  28.991  0.50 11.53 ? 32  TRP A N   1 
ATOM   228  C  CA  A TRP A 1 32  ? 13.426 -3.563  29.489  0.50 10.57 ? 32  TRP A CA  1 
ATOM   229  C  CA  B TRP A 1 32  ? 13.449 -3.473  29.523  0.50 10.93 ? 32  TRP A CA  1 
ATOM   230  C  C   A TRP A 1 32  ? 12.522 -2.882  28.493  0.50 8.13  ? 32  TRP A C   1 
ATOM   231  C  C   B TRP A 1 32  ? 12.522 -2.863  28.494  0.50 8.25  ? 32  TRP A C   1 
ATOM   232  O  O   A TRP A 1 32  ? 12.962 -2.101  27.647  0.50 8.85  ? 32  TRP A O   1 
ATOM   233  O  O   B TRP A 1 32  ? 12.950 -2.106  27.621  0.50 8.98  ? 32  TRP A O   1 
ATOM   234  C  CB  A TRP A 1 32  ? 13.398 -2.815  30.822  0.50 10.16 ? 32  TRP A CB  1 
ATOM   235  C  CB  B TRP A 1 32  ? 13.479 -2.601  30.785  0.50 11.04 ? 32  TRP A CB  1 
ATOM   236  C  CG  A TRP A 1 32  ? 13.589 -1.351  30.681  0.50 11.70 ? 32  TRP A CG  1 
ATOM   237  C  CG  B TRP A 1 32  ? 13.963 -1.182  30.578  0.50 12.56 ? 32  TRP A CG  1 
ATOM   238  C  CD1 A TRP A 1 32  ? 12.623 -0.391  30.747  0.50 12.35 ? 32  TRP A CD1 1 
ATOM   239  C  CD1 B TRP A 1 32  ? 15.248 -0.733  30.671  0.50 13.32 ? 32  TRP A CD1 1 
ATOM   240  C  CD2 A TRP A 1 32  ? 14.822 -0.667  30.457  0.50 11.08 ? 32  TRP A CD2 1 
ATOM   241  C  CD2 B TRP A 1 32  ? 13.157 -0.028  30.292  0.50 14.26 ? 32  TRP A CD2 1 
ATOM   242  N  NE1 A TRP A 1 32  ? 13.179 0.851   30.576  0.50 13.79 ? 32  TRP A NE1 1 
ATOM   243  N  NE1 B TRP A 1 32  ? 15.293 0.625   30.451  0.50 14.94 ? 32  TRP A NE1 1 
ATOM   244  C  CE2 A TRP A 1 32  ? 14.531 0.712   30.402  0.50 11.51 ? 32  TRP A CE2 1 
ATOM   245  C  CE2 B TRP A 1 32  ? 14.024 1.079   30.207  0.50 14.88 ? 32  TRP A CE2 1 
ATOM   246  C  CE3 A TRP A 1 32  ? 16.146 -1.083  30.306  0.50 11.87 ? 32  TRP A CE3 1 
ATOM   247  C  CE3 B TRP A 1 32  ? 11.788 0.173   30.089  0.50 14.89 ? 32  TRP A CE3 1 
ATOM   248  C  CZ2 A TRP A 1 32  ? 15.514 1.671   30.183  0.50 13.42 ? 32  TRP A CZ2 1 
ATOM   249  C  CZ2 B TRP A 1 32  ? 13.568 2.366   29.928  0.50 16.14 ? 32  TRP A CZ2 1 
ATOM   250  C  CZ3 A TRP A 1 32  ? 17.118 -0.133  30.091  0.50 12.05 ? 32  TRP A CZ3 1 
ATOM   251  C  CZ3 B TRP A 1 32  ? 11.338 1.454   29.810  0.50 15.20 ? 32  TRP A CZ3 1 
ATOM   252  C  CH2 A TRP A 1 32  ? 16.801 1.229   30.035  0.50 13.33 ? 32  TRP A CH2 1 
ATOM   253  C  CH2 B TRP A 1 32  ? 12.225 2.532   29.734  0.50 17.11 ? 32  TRP A CH2 1 
ATOM   254  N  N   . GLY A 1 33  ? 11.241 -3.182  28.607  1.00 8.39  ? 33  GLY A N   1 
ATOM   255  C  CA  . GLY A 1 33  ? 10.250 -2.636  27.716  1.00 9.03  ? 33  GLY A CA  1 
ATOM   256  C  C   . GLY A 1 33  ? 8.997  -3.452  27.736  1.00 8.28  ? 33  GLY A C   1 
ATOM   257  O  O   . GLY A 1 33  ? 8.701  -4.123  28.737  1.00 8.90  ? 33  GLY A O   1 
ATOM   258  N  N   A SER A 1 34  ? 8.254  -3.399  26.637  0.50 9.00  ? 34  SER A N   1 
ATOM   259  N  N   B SER A 1 34  ? 8.247  -3.401  26.648  0.50 9.24  ? 34  SER A N   1 
ATOM   260  C  CA  A SER A 1 34  ? 6.952  -4.029  26.542  0.50 10.31 ? 34  SER A CA  1 
ATOM   261  C  CA  B SER A 1 34  ? 6.996  -4.115  26.567  0.50 10.65 ? 34  SER A CA  1 
ATOM   262  C  C   A SER A 1 34  ? 6.726  -4.516  25.125  0.50 9.73  ? 34  SER A C   1 
ATOM   263  C  C   B SER A 1 34  ? 6.728  -4.524  25.138  0.50 9.88  ? 34  SER A C   1 
ATOM   264  O  O   A SER A 1 34  ? 7.145  -3.867  24.166  0.50 10.88 ? 34  SER A O   1 
ATOM   265  O  O   B SER A 1 34  ? 7.116  -3.836  24.192  0.50 11.09 ? 34  SER A O   1 
ATOM   266  C  CB  A SER A 1 34  ? 5.859  -3.032  26.926  0.50 11.10 ? 34  SER A CB  1 
ATOM   267  C  CB  B SER A 1 34  ? 5.857  -3.250  27.093  0.50 12.61 ? 34  SER A CB  1 
ATOM   268  O  OG  A SER A 1 34  ? 4.608  -3.680  27.069  0.50 13.64 ? 34  SER A OG  1 
ATOM   269  O  OG  B SER A 1 34  ? 5.656  -2.139  26.247  0.50 14.90 ? 34  SER A OG  1 
ATOM   270  N  N   . ILE A 1 35  ? 6.070  -5.669  25.002  1.00 10.09 ? 35  ILE A N   1 
ATOM   271  C  CA  . ILE A 1 35  ? 5.677  -6.213  23.707  1.00 9.99  ? 35  ILE A CA  1 
ATOM   272  C  C   . ILE A 1 35  ? 4.226  -6.634  23.847  1.00 10.24 ? 35  ILE A C   1 
ATOM   273  O  O   . ILE A 1 35  ? 3.858  -7.257  24.848  1.00 12.05 ? 35  ILE A O   1 
ATOM   274  C  CB  . ILE A 1 35  ? 6.534  -7.430  23.292  1.00 10.07 ? 35  ILE A CB  1 
ATOM   275  C  CG1 . ILE A 1 35  ? 8.034  -7.105  23.376  1.00 9.65  ? 35  ILE A CG1 1 
ATOM   276  C  CG2 . ILE A 1 35  ? 6.130  -7.905  21.892  1.00 10.56 ? 35  ILE A CG2 1 
ATOM   277  C  CD1 . ILE A 1 35  ? 8.943  -8.305  23.209  1.00 10.19 ? 35  ILE A CD1 1 
ATOM   278  N  N   . LYS A 1 36  ? 3.398  -6.296  22.870  1.00 10.48 ? 36  LYS A N   1 
ATOM   279  C  CA  . LYS A 1 36  ? 1.983  -6.678  22.909  1.00 11.45 ? 36  LYS A CA  1 
ATOM   280  C  C   . LYS A 1 36  ? 1.577  -7.403  21.639  1.00 10.26 ? 36  LYS A C   1 
ATOM   281  O  O   . LYS A 1 36  ? 2.347  -7.450  20.663  1.00 12.65 ? 36  LYS A O   1 
ATOM   282  C  CB  . LYS A 1 36  ? 1.093  -5.474  23.196  1.00 13.36 ? 36  LYS A CB  1 
ATOM   283  C  CG  . LYS A 1 36  ? 1.073  -4.427  22.120  1.00 15.16 ? 36  LYS A CG  1 
ATOM   284  C  CD  . LYS A 1 36  ? 0.434  -3.152  22.637  0.50 14.83 ? 36  LYS A CD  1 
ATOM   285  C  CE  . LYS A 1 36  ? 0.716  -1.996  21.710  0.50 16.39 ? 36  LYS A CE  1 
ATOM   286  N  NZ  . LYS A 1 36  ? -0.067 -0.795  22.111  0.50 18.54 ? 36  LYS A NZ  1 
ATOM   287  N  N   . GLY A 1 37  ? 0.382  -7.994  21.673  1.00 11.18 ? 37  GLY A N   1 
ATOM   288  C  CA  . GLY A 1 37  ? -0.151 -8.751  20.544  1.00 11.33 ? 37  GLY A CA  1 
ATOM   289  C  C   . GLY A 1 37  ? 0.290  -10.201 20.489  1.00 11.71 ? 37  GLY A C   1 
ATOM   290  O  O   . GLY A 1 37  ? 0.140  -10.841 19.452  1.00 12.78 ? 37  GLY A O   1 
ATOM   291  N  N   . LEU A 1 38  ? 0.816  -10.715 21.600  1.00 11.26 ? 38  LEU A N   1 
ATOM   292  C  CA  . LEU A 1 38  ? 1.350  -12.072 21.682  1.00 11.66 ? 38  LEU A CA  1 
ATOM   293  C  C   . LEU A 1 38  ? 0.322  -13.047 22.232  1.00 12.75 ? 38  LEU A C   1 
ATOM   294  O  O   . LEU A 1 38  ? -0.569 -12.661 22.978  1.00 14.25 ? 38  LEU A O   1 
ATOM   295  C  CB  . LEU A 1 38  ? 2.564  -12.077 22.605  1.00 11.94 ? 38  LEU A CB  1 
ATOM   296  C  CG  . LEU A 1 38  ? 3.778  -11.317 22.083  1.00 11.82 ? 38  LEU A CG  1 
ATOM   297  C  CD1 . LEU A 1 38  ? 4.759  -11.066 23.214  1.00 12.81 ? 38  LEU A CD1 1 
ATOM   298  C  CD2 . LEU A 1 38  ? 4.446  -12.097 20.968  1.00 11.20 ? 38  LEU A CD2 1 
ATOM   299  N  N   . THR A 1 39  ? 0.477  -14.324 21.901  1.00 12.49 ? 39  THR A N   1 
ATOM   300  C  CA  . THR A 1 39  ? -0.255 -15.372 22.595  1.00 11.77 ? 39  THR A CA  1 
ATOM   301  C  C   . THR A 1 39  ? 0.354  -15.540 23.981  1.00 11.61 ? 39  THR A C   1 
ATOM   302  O  O   . THR A 1 39  ? 1.561  -15.365 24.168  1.00 12.17 ? 39  THR A O   1 
ATOM   303  C  CB  . THR A 1 39  ? -0.199 -16.700 21.830  1.00 15.38 ? 39  THR A CB  1 
ATOM   304  O  OG1 . THR A 1 39  ? 1.164  -17.064 21.592  1.00 17.20 ? 39  THR A OG1 1 
ATOM   305  C  CG2 . THR A 1 39  ? -0.924 -16.560 20.505  1.00 18.53 ? 39  THR A CG2 1 
ATOM   306  N  N   . GLU A 1 40  ? -0.483 -15.887 24.948  1.00 11.64 ? 40  GLU A N   1 
ATOM   307  C  CA  . GLU A 1 40  ? -0.002 -16.099 26.309  1.00 11.48 ? 40  GLU A CA  1 
ATOM   308  C  C   . GLU A 1 40  ? 1.036  -17.234 26.332  1.00 10.16 ? 40  GLU A C   1 
ATOM   309  O  O   . GLU A 1 40  ? 0.854  -18.258 25.666  1.00 12.37 ? 40  GLU A O   1 
ATOM   310  C  CB  . GLU A 1 40  ? -1.191 -16.374 27.232  1.00 13.33 ? 40  GLU A CB  1 
ATOM   311  C  CG  . GLU A 1 40  ? -0.889 -16.262 28.715  1.00 14.65 ? 40  GLU A CG  1 
ATOM   312  C  CD  . GLU A 1 40  ? -0.694 -17.600 29.369  1.00 15.02 ? 40  GLU A CD  1 
ATOM   313  O  OE1 . GLU A 1 40  ? -0.203 -18.533 28.701  1.00 16.82 ? 40  GLU A OE1 1 
ATOM   314  O  OE2 . GLU A 1 40  ? -1.055 -17.729 30.560  1.00 15.96 ? 40  GLU A OE2 1 
ATOM   315  N  N   . GLY A 1 41  ? 2.124  -17.017 27.071  1.00 10.02 ? 41  GLY A N   1 
ATOM   316  C  CA  . GLY A 1 41  ? 3.205  -17.986 27.232  1.00 9.70  ? 41  GLY A CA  1 
ATOM   317  C  C   . GLY A 1 41  ? 4.561  -17.430 26.853  1.00 9.60  ? 41  GLY A C   1 
ATOM   318  O  O   . GLY A 1 41  ? 4.762  -16.212 26.799  1.00 10.70 ? 41  GLY A O   1 
ATOM   319  N  N   . LEU A 1 42  ? 5.494  -18.332 26.593  1.00 10.50 ? 42  LEU A N   1 
ATOM   320  C  CA  . LEU A 1 42  ? 6.870  -17.975 26.305  1.00 9.79  ? 42  LEU A CA  1 
ATOM   321  C  C   . LEU A 1 42  ? 7.094  -17.730 24.826  1.00 9.27  ? 42  LEU A C   1 
ATOM   322  O  O   . LEU A 1 42  ? 6.595  -18.464 23.985  1.00 10.36 ? 42  LEU A O   1 
ATOM   323  C  CB  . LEU A 1 42  ? 7.815  -19.075 26.794  1.00 9.98  ? 42  LEU A CB  1 
ATOM   324  C  CG  . LEU A 1 42  ? 7.773  -19.312 28.314  1.00 11.79 ? 42  LEU A CG  1 
ATOM   325  C  CD1 . LEU A 1 42  ? 8.694  -20.459 28.680  1.00 14.59 ? 42  LEU A CD1 1 
ATOM   326  C  CD2 . LEU A 1 42  ? 8.157  -18.073 29.104  1.00 14.44 ? 42  LEU A CD2 1 
ATOM   327  N  N   . HIS A 1 43  ? 7.894  -16.711 24.526  1.00 8.51  ? 43  HIS A N   1 
ATOM   328  C  CA  . HIS A 1 43  ? 8.257  -16.370 23.155  1.00 8.45  ? 43  HIS A CA  1 
ATOM   329  C  C   . HIS A 1 43  ? 9.748  -16.160 23.043  1.00 7.66  ? 43  HIS A C   1 
ATOM   330  O  O   . HIS A 1 43  ? 10.312 -15.346 23.785  1.00 8.78  ? 43  HIS A O   1 
ATOM   331  C  CB  . HIS A 1 43  ? 7.514  -15.100 22.754  1.00 9.24  ? 43  HIS A CB  1 
ATOM   332  C  CG  . HIS A 1 43  ? 6.050  -15.318 22.623  1.00 9.55  ? 43  HIS A CG  1 
ATOM   333  N  ND1 . HIS A 1 43  ? 5.473  -15.774 21.461  1.00 11.22 ? 43  HIS A ND1 1 
ATOM   334  C  CD2 . HIS A 1 43  ? 5.055  -15.249 23.536  1.00 9.28  ? 43  HIS A CD2 1 
ATOM   335  C  CE1 . HIS A 1 43  ? 4.176  -15.923 21.646  1.00 12.29 ? 43  HIS A CE1 1 
ATOM   336  N  NE2 . HIS A 1 43  ? 3.895  -15.609 22.897  1.00 10.78 ? 43  HIS A NE2 1 
ATOM   337  N  N   . GLY A 1 44  ? 10.381 -16.865 22.102  1.00 7.91  ? 44  GLY A N   1 
ATOM   338  C  CA  . GLY A 1 44  ? 11.814 -16.740 21.901  1.00 7.94  ? 44  GLY A CA  1 
ATOM   339  C  C   . GLY A 1 44  ? 12.216 -15.290 21.623  1.00 7.53  ? 44  GLY A C   1 
ATOM   340  O  O   . GLY A 1 44  ? 11.497 -14.565 20.949  1.00 8.18  ? 44  GLY A O   1 
ATOM   341  N  N   . PHE A 1 45  ? 13.355 -14.888 22.164  1.00 7.50  ? 45  PHE A N   1 
ATOM   342  C  CA  . PHE A 1 45  ? 13.793 -13.482 22.150  1.00 7.45  ? 45  PHE A CA  1 
ATOM   343  C  C   . PHE A 1 45  ? 15.262 -13.504 21.824  1.00 7.79  ? 45  PHE A C   1 
ATOM   344  O  O   . PHE A 1 45  ? 16.074 -13.915 22.642  1.00 8.75  ? 45  PHE A O   1 
ATOM   345  C  CB  . PHE A 1 45  ? 13.528 -12.903 23.543  1.00 7.72  ? 45  PHE A CB  1 
ATOM   346  C  CG  . PHE A 1 45  ? 13.604 -11.393 23.649  1.00 8.45  ? 45  PHE A CG  1 
ATOM   347  C  CD1 . PHE A 1 45  ? 12.834 -10.576 22.846  1.00 9.33  ? 45  PHE A CD1 1 
ATOM   348  C  CD2 . PHE A 1 45  ? 14.358 -10.813 24.655  1.00 9.07  ? 45  PHE A CD2 1 
ATOM   349  C  CE1 . PHE A 1 45  ? 12.869 -9.188  23.000  1.00 10.12 ? 45  PHE A CE1 1 
ATOM   350  C  CE2 . PHE A 1 45  ? 14.400 -9.427  24.818  1.00 9.14  ? 45  PHE A CE2 1 
ATOM   351  C  CZ  . PHE A 1 45  ? 13.643 -8.627  23.995  1.00 11.14 ? 45  PHE A CZ  1 
ATOM   352  N  N   . HIS A 1 46  ? 15.604 -13.057 20.616  1.00 7.65  ? 46  HIS A N   1 
ATOM   353  C  CA  . HIS A 1 46  ? 16.951 -13.232 20.084  1.00 7.91  ? 46  HIS A CA  1 
ATOM   354  C  C   . HIS A 1 46  ? 17.488 -11.967 19.436  1.00 7.07  ? 46  HIS A C   1 
ATOM   355  O  O   . HIS A 1 46  ? 16.749 -11.242 18.767  1.00 7.55  ? 46  HIS A O   1 
ATOM   356  C  CB  . HIS A 1 46  ? 16.978 -14.275 18.961  1.00 8.81  ? 46  HIS A CB  1 
ATOM   357  C  CG  . HIS A 1 46  ? 16.447 -15.618 19.339  1.00 10.96 ? 46  HIS A CG  1 
ATOM   358  N  ND1 . HIS A 1 46  ? 15.787 -16.440 18.442  1.00 12.10 ? 46  HIS A ND1 1 
ATOM   359  C  CD2 . HIS A 1 46  ? 16.506 -16.298 20.505  1.00 10.29 ? 46  HIS A CD2 1 
ATOM   360  C  CE1 . HIS A 1 46  ? 15.448 -17.561 19.058  1.00 14.29 ? 46  HIS A CE1 1 
ATOM   361  N  NE2 . HIS A 1 46  ? 15.854 -17.492 20.314  1.00 12.94 ? 46  HIS A NE2 1 
ATOM   362  N  N   . VAL A 1 47  ? 18.792 -11.764 19.569  1.00 7.27  ? 47  VAL A N   1 
ATOM   363  C  CA  . VAL A 1 47  ? 19.507 -10.859 18.659  1.00 6.66  ? 47  VAL A CA  1 
ATOM   364  C  C   . VAL A 1 47  ? 20.018 -11.696 17.486  1.00 7.45  ? 47  VAL A C   1 
ATOM   365  O  O   . VAL A 1 47  ? 20.778 -12.647 17.675  1.00 8.09  ? 47  VAL A O   1 
ATOM   366  C  CB  . VAL A 1 47  ? 20.659 -10.096 19.332  1.00 7.80  ? 47  VAL A CB  1 
ATOM   367  C  CG1 . VAL A 1 47  ? 21.300 -9.113  18.352  1.00 8.21  ? 47  VAL A CG1 1 
ATOM   368  C  CG2 . VAL A 1 47  ? 20.137 -9.367  20.567  1.00 9.18  ? 47  VAL A CG2 1 
ATOM   369  N  N   . HIS A 1 48  ? 19.563 -11.342 16.287  1.00 7.26  ? 48  HIS A N   1 
ATOM   370  C  CA  . HIS A 1 48  ? 19.997 -11.946 15.044  1.00 7.81  ? 48  HIS A CA  1 
ATOM   371  C  C   . HIS A 1 48  ? 21.117 -11.115 14.428  1.00 7.64  ? 48  HIS A C   1 
ATOM   372  O  O   . HIS A 1 48  ? 21.267 -9.930  14.742  1.00 9.66  ? 48  HIS A O   1 
ATOM   373  C  CB  . HIS A 1 48  ? 18.799 -12.097 14.111  1.00 8.61  ? 48  HIS A CB  1 
ATOM   374  C  CG  . HIS A 1 48  ? 17.904 -13.256 14.466  1.00 8.97  ? 48  HIS A CG  1 
ATOM   375  N  ND1 . HIS A 1 48  ? 17.822 -14.358 13.650  1.00 10.57 ? 48  HIS A ND1 1 
ATOM   376  C  CD2 . HIS A 1 48  ? 17.085 -13.517 15.522  1.00 10.30 ? 48  HIS A CD2 1 
ATOM   377  C  CE1 . HIS A 1 48  ? 16.991 -15.237 14.162  1.00 12.77 ? 48  HIS A CE1 1 
ATOM   378  N  NE2 . HIS A 1 48  ? 16.522 -14.763 15.296  1.00 11.41 ? 48  HIS A NE2 1 
ATOM   379  N  N   . GLU A 1 49  ? 21.899 -11.735 13.558  1.00 8.41  ? 49  GLU A N   1 
ATOM   380  C  CA  . GLU A 1 49  ? 23.191 -11.192 13.163  1.00 8.87  ? 49  GLU A CA  1 
ATOM   381  C  C   . GLU A 1 49  ? 23.128 -9.869  12.401  1.00 8.81  ? 49  GLU A C   1 
ATOM   382  O  O   . GLU A 1 49  ? 23.970 -8.992  12.624  1.00 10.34 ? 49  GLU A O   1 
ATOM   383  C  CB  . GLU A 1 49  ? 23.953 -12.217 12.325  1.00 10.61 ? 49  GLU A CB  1 
ATOM   384  C  CG  A GLU A 1 49  ? 25.365 -11.789 11.955  0.70 11.40 ? 49  GLU A CG  1 
ATOM   385  C  CG  B GLU A 1 49  ? 25.375 -11.804 11.962  0.30 11.03 ? 49  GLU A CG  1 
ATOM   386  C  CD  A GLU A 1 49  ? 26.105 -12.816 11.135  0.70 13.61 ? 49  GLU A CD  1 
ATOM   387  C  CD  B GLU A 1 49  ? 26.098 -12.834 11.122  0.30 12.22 ? 49  GLU A CD  1 
ATOM   388  O  OE1 A GLU A 1 49  ? 25.533 -13.898 10.872  0.70 15.53 ? 49  GLU A OE1 1 
ATOM   389  O  OE1 B GLU A 1 49  ? 25.495 -13.883 10.806  0.30 12.68 ? 49  GLU A OE1 1 
ATOM   390  O  OE2 A GLU A 1 49  ? 27.262 -12.529 10.755  0.70 15.85 ? 49  GLU A OE2 1 
ATOM   391  O  OE2 B GLU A 1 49  ? 27.273 -12.586 10.774  0.30 13.08 ? 49  GLU A OE2 1 
ATOM   392  N  N   . PHE A 1 50  ? 22.179 -9.745  11.482  1.00 8.68  ? 50  PHE A N   1 
ATOM   393  C  CA  . PHE A 1 50  ? 22.164 -8.591  10.576  1.00 9.00  ? 50  PHE A CA  1 
ATOM   394  C  C   . PHE A 1 50  ? 21.056 -7.641  10.965  1.00 9.20  ? 50  PHE A C   1 
ATOM   395  O  O   . PHE A 1 50  ? 19.935 -8.074  11.244  1.00 9.86  ? 50  PHE A O   1 
ATOM   396  C  CB  . PHE A 1 50  ? 21.975 -9.025  9.123   1.00 10.56 ? 50  PHE A CB  1 
ATOM   397  C  CG  . PHE A 1 50  ? 22.933 -10.088 8.697   1.00 11.85 ? 50  PHE A CG  1 
ATOM   398  C  CD1 . PHE A 1 50  ? 24.305 -9.900  8.836   1.00 12.60 ? 50  PHE A CD1 1 
ATOM   399  C  CD2 . PHE A 1 50  ? 22.472 -11.294 8.173   1.00 12.42 ? 50  PHE A CD2 1 
ATOM   400  C  CE1 . PHE A 1 50  ? 25.199 -10.908 8.453   1.00 12.93 ? 50  PHE A CE1 1 
ATOM   401  C  CE2 . PHE A 1 50  ? 23.355 -12.288 7.793   1.00 13.71 ? 50  PHE A CE2 1 
ATOM   402  C  CZ  . PHE A 1 50  ? 24.717 -12.107 7.946   1.00 18.05 ? 50  PHE A CZ  1 
ATOM   403  N  N   . GLY A 1 51  ? 21.355 -6.346  10.923  1.00 9.19  ? 51  GLY A N   1 
ATOM   404  C  CA  . GLY A 1 51  ? 20.339 -5.300  11.073  1.00 9.98  ? 51  GLY A CA  1 
ATOM   405  C  C   . GLY A 1 51  ? 19.717 -4.985  9.741   1.00 9.77  ? 51  GLY A C   1 
ATOM   406  O  O   . GLY A 1 51  ? 19.625 -3.836  9.346   1.00 11.23 ? 51  GLY A O   1 
ATOM   407  N  N   . ASP A 1 52  ? 19.331 -6.020  9.013   1.00 11.83 ? 52  ASP A N   1 
ATOM   408  C  CA  . ASP A 1 52  ? 18.839 -5.904  7.659   1.00 12.72 ? 52  ASP A CA  1 
ATOM   409  C  C   . ASP A 1 52  ? 17.388 -6.289  7.749   1.00 12.43 ? 52  ASP A C   1 
ATOM   410  O  O   . ASP A 1 52  ? 17.071 -7.467  7.963   1.00 13.74 ? 52  ASP A O   1 
ATOM   411  C  CB  . ASP A 1 52  ? 19.608 -6.843  6.730   1.00 12.97 ? 52  ASP A CB  1 
ATOM   412  C  CG  . ASP A 1 52  ? 19.173 -6.730  5.294   1.00 14.93 ? 52  ASP A CG  1 
ATOM   413  O  OD1 . ASP A 1 52  ? 18.026 -6.298  5.061   1.00 15.07 ? 52  ASP A OD1 1 
ATOM   414  O  OD2 . ASP A 1 52  ? 19.975 -7.083  4.394   1.00 18.19 ? 52  ASP A OD2 1 
ATOM   415  N  N   . ASN A 1 53  ? 16.503 -5.308  7.643   1.00 13.28 ? 53  ASN A N   1 
ATOM   416  C  CA  . ASN A 1 53  ? 15.064 -5.570  7.667   1.00 15.69 ? 53  ASN A CA  1 
ATOM   417  C  C   . ASN A 1 53  ? 14.415 -5.225  6.324   1.00 14.71 ? 53  ASN A C   1 
ATOM   418  O  O   . ASN A 1 53  ? 13.214 -4.960  6.240   1.00 15.84 ? 53  ASN A O   1 
ATOM   419  C  CB  . ASN A 1 53  ? 14.414 -4.845  8.849   1.00 18.05 ? 53  ASN A CB  1 
ATOM   420  C  CG  . ASN A 1 53  ? 14.810 -5.445  10.209  1.00 20.36 ? 53  ASN A CG  1 
ATOM   421  O  OD1 . ASN A 1 53  ? 15.395 -6.542  10.312  1.00 23.26 ? 53  ASN A OD1 1 
ATOM   422  N  ND2 . ASN A 1 53  ? 14.484 -4.725  11.262  1.00 22.41 ? 53  ASN A ND2 1 
ATOM   423  N  N   . THR A 1 54  ? 15.213 -5.297  5.263   1.00 14.20 ? 54  THR A N   1 
ATOM   424  C  CA  . THR A 1 54  ? 14.742 -4.956  3.925   1.00 16.32 ? 54  THR A CA  1 
ATOM   425  C  C   . THR A 1 54  ? 13.617 -5.862  3.435   1.00 14.78 ? 54  THR A C   1 
ATOM   426  O  O   . THR A 1 54  ? 12.739 -5.405  2.718   1.00 16.57 ? 54  THR A O   1 
ATOM   427  C  CB  . THR A 1 54  ? 15.887 -4.937  2.904   1.00 17.03 ? 54  THR A CB  1 
ATOM   428  O  OG1 . THR A 1 54  ? 16.576 -6.183  2.929   1.00 17.97 ? 54  THR A OG1 1 
ATOM   429  C  CG2 . THR A 1 54  ? 16.877 -3.817  3.219   1.00 17.55 ? 54  THR A CG2 1 
ATOM   430  N  N   . ALA A 1 55  ? 13.640 -7.137  3.830   1.00 15.44 ? 55  ALA A N   1 
ATOM   431  C  CA  . ALA A 1 55  ? 12.522 -8.037  3.550   1.00 18.25 ? 55  ALA A CA  1 
ATOM   432  C  C   . ALA A 1 55  ? 11.803 -8.424  4.840   1.00 19.86 ? 55  ALA A C   1 
ATOM   433  O  O   . ALA A 1 55  ? 11.313 -9.545  4.977   1.00 26.19 ? 55  ALA A O   1 
ATOM   434  C  CB  . ALA A 1 55  ? 13.009 -9.268  2.807   1.00 20.77 ? 55  ALA A CB  1 
ATOM   435  N  N   . GLY A 1 56  ? 11.716 -7.482  5.773   1.00 17.59 ? 56  GLY A N   1 
ATOM   436  C  CA  . GLY A 1 56  ? 11.168 -7.750  7.092   1.00 18.56 ? 56  GLY A CA  1 
ATOM   437  C  C   . GLY A 1 56  ? 12.139 -8.573  7.905   1.00 17.68 ? 56  GLY A C   1 
ATOM   438  O  O   . GLY A 1 56  ? 13.358 -8.520  7.705   1.00 19.05 ? 56  GLY A O   1 
ATOM   439  N  N   . CYS A 1 57  ? 11.602 -9.391  8.796   1.00 13.71 ? 57  CYS A N   1 
ATOM   440  C  CA  . CYS A 1 57  ? 12.454 -10.137 9.715   1.00 13.15 ? 57  CYS A CA  1 
ATOM   441  C  C   . CYS A 1 57  ? 13.258 -11.252 9.070   1.00 13.79 ? 57  CYS A C   1 
ATOM   442  O  O   . CYS A 1 57  ? 14.241 -11.705 9.651   1.00 15.31 ? 57  CYS A O   1 
ATOM   443  C  CB  . CYS A 1 57  ? 11.624 -10.686 10.868  1.00 14.20 ? 57  CYS A CB  1 
ATOM   444  S  SG  . CYS A 1 57  ? 10.654 -9.408  11.699  1.00 18.53 ? 57  CYS A SG  1 
ATOM   445  N  N   . THR A 1 58  ? 12.879 -11.667 7.864   1.00 13.45 ? 58  THR A N   1 
ATOM   446  C  CA  . THR A 1 58  ? 13.587 -12.775 7.213   1.00 17.02 ? 58  THR A CA  1 
ATOM   447  C  C   . THR A 1 58  ? 15.020 -12.453 6.770   1.00 16.51 ? 58  THR A C   1 
ATOM   448  O  O   . THR A 1 58  ? 15.828 -13.358 6.631   1.00 26.10 ? 58  THR A O   1 
ATOM   449  C  CB  . THR A 1 58  ? 12.772 -13.381 6.054   1.00 21.72 ? 58  THR A CB  1 
ATOM   450  O  OG1 . THR A 1 58  ? 13.369 -14.619 5.644   1.00 27.92 ? 58  THR A OG1 1 
ATOM   451  C  CG2 . THR A 1 58  ? 12.705 -12.462 4.871   1.00 21.79 ? 58  THR A CG2 1 
ATOM   452  N  N   A SER A 1 59  ? 15.316 -11.174 6.556   0.50 13.69 ? 59  SER A N   1 
ATOM   453  N  N   B SER A 1 59  ? 15.322 -11.178 6.545   0.50 12.00 ? 59  SER A N   1 
ATOM   454  C  CA  A SER A 1 59  ? 16.650 -10.734 6.161   0.50 14.41 ? 59  SER A CA  1 
ATOM   455  C  CA  B SER A 1 59  ? 16.665 -10.766 6.148   0.50 12.50 ? 59  SER A CA  1 
ATOM   456  C  C   A SER A 1 59  ? 17.648 -10.645 7.316   0.50 11.97 ? 59  SER A C   1 
ATOM   457  C  C   B SER A 1 59  ? 17.650 -10.640 7.315   0.50 11.03 ? 59  SER A C   1 
ATOM   458  O  O   A SER A 1 59  ? 18.822 -10.372 7.085   0.50 11.77 ? 59  SER A O   1 
ATOM   459  O  O   B SER A 1 59  ? 18.819 -10.348 7.090   0.50 11.13 ? 59  SER A O   1 
ATOM   460  C  CB  A SER A 1 59  ? 16.550 -9.369  5.483   0.50 15.60 ? 59  SER A CB  1 
ATOM   461  C  CB  B SER A 1 59  ? 16.603 -9.452  5.362   0.50 11.33 ? 59  SER A CB  1 
ATOM   462  O  OG  A SER A 1 59  ? 15.668 -9.418  4.386   0.50 14.51 ? 59  SER A OG  1 
ATOM   463  O  OG  B SER A 1 59  ? 15.592 -8.598  5.855   0.50 11.00 ? 59  SER A OG  1 
ATOM   464  N  N   . ALA A 1 60  ? 17.197 -10.882 8.551   1.00 10.62 ? 60  ALA A N   1 
ATOM   465  C  CA  . ALA A 1 60  ? 18.046 -10.674 9.727   1.00 11.24 ? 60  ALA A CA  1 
ATOM   466  C  C   . ALA A 1 60  ? 19.111 -11.744 9.952   1.00 10.07 ? 60  ALA A C   1 
ATOM   467  O  O   . ALA A 1 60  ? 20.025 -11.549 10.738  1.00 11.03 ? 60  ALA A O   1 
ATOM   468  C  CB  . ALA A 1 60  ? 17.192 -10.529 10.969  1.00 11.39 ? 60  ALA A CB  1 
ATOM   469  N  N   . GLY A 1 61  ? 19.018 -12.857 9.234   1.00 9.32  ? 61  GLY A N   1 
ATOM   470  C  CA  . GLY A 1 61  ? 20.041 -13.878 9.335   1.00 9.47  ? 61  GLY A CA  1 
ATOM   471  C  C   . GLY A 1 61  ? 19.929 -14.716 10.584  1.00 10.26 ? 61  GLY A C   1 
ATOM   472  O  O   . GLY A 1 61  ? 18.895 -14.716 11.236  1.00 11.16 ? 61  GLY A O   1 
ATOM   473  N  N   . PRO A 1 62  ? 20.996 -15.465 10.887  1.00 11.04 ? 62  PRO A N   1 
ATOM   474  C  CA  . PRO A 1 62  ? 20.972 -16.383 12.008  1.00 11.42 ? 62  PRO A CA  1 
ATOM   475  C  C   . PRO A 1 62  ? 21.166 -15.669 13.338  1.00 10.17 ? 62  PRO A C   1 
ATOM   476  O  O   . PRO A 1 62  ? 21.301 -14.447 13.388  1.00 10.79 ? 62  PRO A O   1 
ATOM   477  C  CB  . PRO A 1 62  ? 22.156 -17.296 11.716  1.00 14.18 ? 62  PRO A CB  1 
ATOM   478  C  CG  . PRO A 1 62  ? 23.117 -16.433 10.992  1.00 14.50 ? 62  PRO A CG  1 
ATOM   479  C  CD  . PRO A 1 62  ? 22.278 -15.520 10.157  1.00 13.00 ? 62  PRO A CD  1 
ATOM   480  N  N   . HIS A 1 63  ? 21.199 -16.430 14.426  1.00 11.73 ? 63  HIS A N   1 
ATOM   481  C  CA  . HIS A 1 63  ? 21.455 -15.839 15.739  1.00 10.56 ? 63  HIS A CA  1 
ATOM   482  C  C   . HIS A 1 63  ? 22.841 -15.202 15.735  1.00 9.34  ? 63  HIS A C   1 
ATOM   483  O  O   . HIS A 1 63  ? 23.777 -15.744 15.174  1.00 11.53 ? 63  HIS A O   1 
ATOM   484  C  CB  . HIS A 1 63  ? 21.392 -16.882 16.854  1.00 11.02 ? 63  HIS A CB  1 
ATOM   485  C  CG  . HIS A 1 63  ? 20.053 -17.527 17.001  1.00 13.42 ? 63  HIS A CG  1 
ATOM   486  N  ND1 . HIS A 1 63  ? 19.734 -18.340 18.066  1.00 10.74 ? 63  HIS A ND1 1 
ATOM   487  C  CD2 . HIS A 1 63  ? 18.955 -17.498 16.208  1.00 16.76 ? 63  HIS A CD2 1 
ATOM   488  C  CE1 . HIS A 1 63  ? 18.501 -18.785 17.916  1.00 12.54 ? 63  HIS A CE1 1 
ATOM   489  N  NE2 . HIS A 1 63  ? 18.004 -18.286 16.801  1.00 14.95 ? 63  HIS A NE2 1 
ATOM   490  N  N   . PHE A 1 64  ? 22.966 -14.056 16.389  1.00 9.26  ? 64  PHE A N   1 
ATOM   491  C  CA  . PHE A 1 64  ? 24.237 -13.370 16.483  1.00 9.45  ? 64  PHE A CA  1 
ATOM   492  C  C   . PHE A 1 64  ? 25.178 -14.240 17.307  1.00 9.80  ? 64  PHE A C   1 
ATOM   493  O  O   . PHE A 1 64  ? 24.900 -14.543 18.466  1.00 9.92  ? 64  PHE A O   1 
ATOM   494  C  CB  . PHE A 1 64  ? 24.030 -11.990 17.110  1.00 8.93  ? 64  PHE A CB  1 
ATOM   495  C  CG  . PHE A 1 64  ? 25.298 -11.208 17.317  1.00 10.00 ? 64  PHE A CG  1 
ATOM   496  C  CD1 . PHE A 1 64  ? 26.252 -11.099 16.303  1.00 10.85 ? 64  PHE A CD1 1 
ATOM   497  C  CD2 . PHE A 1 64  ? 25.532 -10.554 18.517  1.00 10.82 ? 64  PHE A CD2 1 
ATOM   498  C  CE1 . PHE A 1 64  ? 27.427 -10.386 16.505  1.00 13.33 ? 64  PHE A CE1 1 
ATOM   499  C  CE2 . PHE A 1 64  ? 26.696 -9.824  18.713  1.00 12.15 ? 64  PHE A CE2 1 
ATOM   500  C  CZ  . PHE A 1 64  ? 27.646 -9.739  17.703  1.00 14.44 ? 64  PHE A CZ  1 
ATOM   501  N  N   . ASN A 1 65  ? 26.256 -14.689 16.674  1.00 10.70 ? 65  ASN A N   1 
ATOM   502  C  CA  . ASN A 1 65  ? 27.109 -15.724 17.235  1.00 10.90 ? 65  ASN A CA  1 
ATOM   503  C  C   . ASN A 1 65  ? 28.582 -15.475 16.910  1.00 12.23 ? 65  ASN A C   1 
ATOM   504  O  O   . ASN A 1 65  ? 29.238 -16.306 16.268  1.00 12.56 ? 65  ASN A O   1 
ATOM   505  C  CB  . ASN A 1 65  ? 26.636 -17.080 16.700  1.00 10.51 ? 65  ASN A CB  1 
ATOM   506  C  CG  . ASN A 1 65  ? 27.362 -18.265 17.325  1.00 11.42 ? 65  ASN A CG  1 
ATOM   507  O  OD1 . ASN A 1 65  ? 27.870 -18.204 18.453  1.00 11.40 ? 65  ASN A OD1 1 
ATOM   508  N  ND2 . ASN A 1 65  ? 27.398 -19.369 16.585  1.00 11.85 ? 65  ASN A ND2 1 
ATOM   509  N  N   . PRO A 1 66  ? 29.124 -14.340 17.376  1.00 11.35 ? 66  PRO A N   1 
ATOM   510  C  CA  . PRO A 1 66  ? 30.505 -14.009 17.017  1.00 13.15 ? 66  PRO A CA  1 
ATOM   511  C  C   . PRO A 1 66  ? 31.545 -14.951 17.629  1.00 13.15 ? 66  PRO A C   1 
ATOM   512  O  O   . PRO A 1 66  ? 32.655 -15.009 17.120  1.00 16.29 ? 66  PRO A O   1 
ATOM   513  C  CB  . PRO A 1 66  ? 30.670 -12.589 17.559  1.00 13.36 ? 66  PRO A CB  1 
ATOM   514  C  CG  . PRO A 1 66  ? 29.734 -12.537 18.710  1.00 12.34 ? 66  PRO A CG  1 
ATOM   515  C  CD  . PRO A 1 66  ? 28.544 -13.347 18.299  1.00 12.25 ? 66  PRO A CD  1 
ATOM   516  N  N   . LEU A 1 67  ? 31.186 -15.681 18.697  1.00 13.77 ? 67  LEU A N   1 
ATOM   517  C  CA  . LEU A 1 67  ? 32.116 -16.583 19.383  1.00 15.41 ? 67  LEU A CA  1 
ATOM   518  C  C   . LEU A 1 67  ? 31.940 -18.051 18.974  1.00 15.36 ? 67  LEU A C   1 
ATOM   519  O  O   . LEU A 1 67  ? 32.546 -18.934 19.578  1.00 17.45 ? 67  LEU A O   1 
ATOM   520  C  CB  . LEU A 1 67  ? 31.984 -16.412 20.904  1.00 17.19 ? 67  LEU A CB  1 
ATOM   521  C  CG  . LEU A 1 67  ? 32.140 -14.964 21.400  1.00 21.07 ? 67  LEU A CG  1 
ATOM   522  C  CD1 . LEU A 1 67  ? 31.696 -14.800 22.842  1.00 21.04 ? 67  LEU A CD1 1 
ATOM   523  C  CD2 . LEU A 1 67  ? 33.573 -14.480 21.230  1.00 26.03 ? 67  LEU A CD2 1 
ATOM   524  N  N   . SER A 1 68  ? 31.137 -18.304 17.940  1.00 15.08 ? 68  SER A N   1 
ATOM   525  C  CA  . SER A 1 68  ? 31.020 -19.632 17.327  1.00 15.26 ? 68  SER A CA  1 
ATOM   526  C  C   . SER A 1 68  ? 30.671 -20.728 18.331  1.00 14.89 ? 68  SER A C   1 
ATOM   527  O  O   . SER A 1 68  ? 31.365 -21.746 18.414  1.00 17.84 ? 68  SER A O   1 
ATOM   528  C  CB  . SER A 1 68  ? 32.307 -20.002 16.562  1.00 16.78 ? 68  SER A CB  1 
ATOM   529  O  OG  . SER A 1 68  ? 32.550 -19.085 15.516  1.00 18.91 ? 68  SER A OG  1 
ATOM   530  N  N   A ARG A 1 69  ? 29.606 -20.506 19.096  0.50 13.70 ? 69  ARG A N   1 
ATOM   531  N  N   B ARG A 1 69  ? 29.607 -20.493 19.101  0.50 13.67 ? 69  ARG A N   1 
ATOM   532  C  CA  A ARG A 1 69  ? 29.103 -21.499 20.038  0.50 13.97 ? 69  ARG A CA  1 
ATOM   533  C  CA  B ARG A 1 69  ? 29.074 -21.470 20.051  0.50 13.78 ? 69  ARG A CA  1 
ATOM   534  C  C   A ARG A 1 69  ? 27.778 -22.039 19.541  0.50 12.64 ? 69  ARG A C   1 
ATOM   535  C  C   B ARG A 1 69  ? 27.789 -22.060 19.515  0.50 12.60 ? 69  ARG A C   1 
ATOM   536  O  O   A ARG A 1 69  ? 27.240 -21.562 18.540  0.50 13.05 ? 69  ARG A O   1 
ATOM   537  O  O   B ARG A 1 69  ? 27.270 -21.617 18.488  0.50 13.13 ? 69  ARG A O   1 
ATOM   538  C  CB  A ARG A 1 69  ? 28.968 -20.883 21.430  0.50 14.52 ? 69  ARG A CB  1 
ATOM   539  C  CB  B ARG A 1 69  ? 28.762 -20.809 21.389  0.50 14.04 ? 69  ARG A CB  1 
ATOM   540  C  CG  A ARG A 1 69  ? 30.284 -20.322 21.947  0.50 16.91 ? 69  ARG A CG  1 
ATOM   541  C  CG  B ARG A 1 69  ? 29.875 -19.963 21.971  0.50 15.78 ? 69  ARG A CG  1 
ATOM   542  C  CD  A ARG A 1 69  ? 30.434 -20.380 23.459  0.50 17.84 ? 69  ARG A CD  1 
ATOM   543  C  CD  B ARG A 1 69  ? 31.153 -20.758 22.151  0.50 14.94 ? 69  ARG A CD  1 
ATOM   544  N  NE  A ARG A 1 69  ? 31.828 -20.143 23.834  0.50 18.67 ? 69  ARG A NE  1 
ATOM   545  N  NE  B ARG A 1 69  ? 31.022 -21.900 23.052  0.50 15.48 ? 69  ARG A NE  1 
ATOM   546  C  CZ  A ARG A 1 69  ? 32.314 -18.963 24.213  0.50 18.76 ? 69  ARG A CZ  1 
ATOM   547  C  CZ  B ARG A 1 69  ? 31.087 -21.811 24.379  0.50 17.09 ? 69  ARG A CZ  1 
ATOM   548  N  NH1 A ARG A 1 69  ? 31.513 -17.920 24.291  0.50 16.20 ? 69  ARG A NH1 1 
ATOM   549  N  NH1 B ARG A 1 69  ? 31.238 -20.634 24.958  0.50 17.66 ? 69  ARG A NH1 1 
ATOM   550  N  NH2 A ARG A 1 69  ? 33.597 -18.828 24.527  0.50 20.58 ? 69  ARG A NH2 1 
ATOM   551  N  NH2 B ARG A 1 69  ? 30.988 -22.894 25.134  0.50 17.50 ? 69  ARG A NH2 1 
ATOM   552  N  N   . LYS A 1 70  ? 27.276 -23.056 20.235  1.00 12.48 ? 70  LYS A N   1 
ATOM   553  C  CA  . LYS A 1 70  ? 25.953 -23.604 19.979  1.00 12.00 ? 70  LYS A CA  1 
ATOM   554  C  C   . LYS A 1 70  ? 24.890 -22.774 20.696  1.00 10.24 ? 70  LYS A C   1 
ATOM   555  O  O   . LYS A 1 70  ? 25.184 -21.992 21.604  1.00 11.23 ? 70  LYS A O   1 
ATOM   556  C  CB  . LYS A 1 70  ? 25.877 -25.041 20.480  1.00 12.55 ? 70  LYS A CB  1 
ATOM   557  C  CG  . LYS A 1 70  ? 26.831 -25.993 19.776  1.00 15.51 ? 70  LYS A CG  1 
ATOM   558  C  CD  . LYS A 1 70  ? 26.689 -27.398 20.334  1.00 19.40 ? 70  LYS A CD  1 
ATOM   559  C  CE  . LYS A 1 70  ? 27.729 -28.334 19.688  0.00 32.47 ? 70  LYS A CE  1 
ATOM   560  N  NZ  . LYS A 1 70  ? 27.472 -28.481 18.229  0.00 33.71 ? 70  LYS A NZ  1 
ATOM   561  N  N   . HIS A 1 71  ? 23.647 -22.979 20.300  1.00 9.98  ? 71  HIS A N   1 
ATOM   562  C  CA  . HIS A 1 71  ? 22.512 -22.274 20.876  1.00 10.74 ? 71  HIS A CA  1 
ATOM   563  C  C   . HIS A 1 71  ? 22.235 -22.730 22.304  1.00 10.01 ? 71  HIS A C   1 
ATOM   564  O  O   . HIS A 1 71  ? 22.313 -23.921 22.610  1.00 11.78 ? 71  HIS A O   1 
ATOM   565  C  CB  . HIS A 1 71  ? 21.263 -22.522 20.038  1.00 10.68 ? 71  HIS A CB  1 
ATOM   566  C  CG  . HIS A 1 71  ? 20.053 -21.840 20.567  1.00 9.51  ? 71  HIS A CG  1 
ATOM   567  N  ND1 . HIS A 1 71  ? 19.818 -20.484 20.417  1.00 9.51  ? 71  HIS A ND1 1 
ATOM   568  C  CD2 . HIS A 1 71  ? 19.026 -22.326 21.299  1.00 10.79 ? 71  HIS A CD2 1 
ATOM   569  C  CE1 . HIS A 1 71  ? 18.689 -20.179 21.023  1.00 10.82 ? 71  HIS A CE1 1 
ATOM   570  N  NE2 . HIS A 1 71  ? 18.182 -21.278 21.560  1.00 9.95  ? 71  HIS A NE2 1 
ATOM   571  N  N   . GLY A 1 72  ? 21.895 -21.791 23.181  1.00 10.83 ? 72  GLY A N   1 
ATOM   572  C  CA  . GLY A 1 72  ? 21.448 -22.114 24.532  1.00 10.22 ? 72  GLY A CA  1 
ATOM   573  C  C   . GLY A 1 72  ? 20.549 -21.053 25.096  1.00 10.20 ? 72  GLY A C   1 
ATOM   574  O  O   . GLY A 1 72  ? 20.028 -20.213 24.364  1.00 10.71 ? 72  GLY A O   1 
ATOM   575  N  N   . GLY A 1 73  ? 20.389 -21.108 26.406  1.00 11.36 ? 73  GLY A N   1 
ATOM   576  C  CA  . GLY A 1 73  ? 19.687 -20.089 27.141  1.00 10.49 ? 73  GLY A CA  1 
ATOM   577  C  C   . GLY A 1 73  ? 20.647 -19.053 27.676  1.00 10.32 ? 73  GLY A C   1 
ATOM   578  O  O   . GLY A 1 73  ? 21.869 -19.254 27.683  1.00 10.76 ? 73  GLY A O   1 
ATOM   579  N  N   . PRO A 1 74  ? 20.101 -17.929 28.155  1.00 10.03 ? 74  PRO A N   1 
ATOM   580  C  CA  . PRO A 1 74  ? 20.952 -16.823 28.564  1.00 10.64 ? 74  PRO A CA  1 
ATOM   581  C  C   . PRO A 1 74  ? 21.839 -17.153 29.755  1.00 10.67 ? 74  PRO A C   1 
ATOM   582  O  O   . PRO A 1 74  ? 22.903 -16.580 29.893  1.00 13.89 ? 74  PRO A O   1 
ATOM   583  C  CB  . PRO A 1 74  ? 19.947 -15.701 28.889  1.00 11.59 ? 74  PRO A CB  1 
ATOM   584  C  CG  . PRO A 1 74  ? 18.622 -16.374 28.998  1.00 11.42 ? 74  PRO A CG  1 
ATOM   585  C  CD  . PRO A 1 74  ? 18.692 -17.536 28.062  1.00 10.53 ? 74  PRO A CD  1 
ATOM   586  N  N   . LYS A 1 75  ? 21.411 -18.085 30.609  1.00 11.68 ? 75  LYS A N   1 
ATOM   587  C  CA  . LYS A 1 75  ? 22.205 -18.441 31.775  1.00 14.21 ? 75  LYS A CA  1 
ATOM   588  C  C   . LYS A 1 75  ? 23.069 -19.682 31.548  1.00 14.21 ? 75  LYS A C   1 
ATOM   589  O  O   . LYS A 1 75  ? 23.576 -20.260 32.498  1.00 18.26 ? 75  LYS A O   1 
ATOM   590  C  CB  . LYS A 1 75  ? 21.295 -18.577 32.996  1.00 17.55 ? 75  LYS A CB  1 
ATOM   591  C  CG  . LYS A 1 75  ? 20.523 -17.292 33.329  1.00 20.76 ? 75  LYS A CG  1 
ATOM   592  C  CD  . LYS A 1 75  ? 21.422 -16.072 33.556  1.00 25.03 ? 75  LYS A CD  1 
ATOM   593  C  CE  . LYS A 1 75  ? 20.622 -14.784 33.649  1.00 30.65 ? 75  LYS A CE  1 
ATOM   594  N  NZ  . LYS A 1 75  ? 21.505 -13.582 33.681  1.00 33.72 ? 75  LYS A NZ  1 
ATOM   595  N  N   . ASP A 1 76  ? 23.237 -20.082 30.291  1.00 13.83 ? 76  ASP A N   1 
ATOM   596  C  CA  . ASP A 1 76  ? 24.140 -21.183 29.932  1.00 13.95 ? 76  ASP A CA  1 
ATOM   597  C  C   . ASP A 1 76  ? 25.482 -20.650 29.472  1.00 13.23 ? 76  ASP A C   1 
ATOM   598  O  O   . ASP A 1 76  ? 25.562 -19.577 28.872  1.00 13.99 ? 76  ASP A O   1 
ATOM   599  C  CB  . ASP A 1 76  ? 23.560 -22.011 28.781  1.00 14.45 ? 76  ASP A CB  1 
ATOM   600  C  CG  . ASP A 1 76  ? 22.325 -22.770 29.164  1.00 16.23 ? 76  ASP A CG  1 
ATOM   601  O  OD1 . ASP A 1 76  ? 22.186 -23.155 30.347  1.00 20.70 ? 76  ASP A OD1 1 
ATOM   602  O  OD2 . ASP A 1 76  ? 21.492 -22.991 28.262  1.00 17.73 ? 76  ASP A OD2 1 
ATOM   603  N  N   A GLU A 1 77  ? 26.541 -21.401 29.735  0.50 13.79 ? 77  GLU A N   1 
ATOM   604  N  N   B GLU A 1 77  ? 26.546 -21.400 29.745  0.50 14.23 ? 77  GLU A N   1 
ATOM   605  C  CA  A GLU A 1 77  ? 27.848 -21.072 29.185  0.50 14.57 ? 77  GLU A CA  1 
ATOM   606  C  CA  B GLU A 1 77  ? 27.868 -21.097 29.193  0.50 15.78 ? 77  GLU A CA  1 
ATOM   607  C  C   A GLU A 1 77  ? 27.858 -21.254 27.669  0.50 13.20 ? 77  GLU A C   1 
ATOM   608  C  C   B GLU A 1 77  ? 27.864 -21.260 27.674  0.50 13.67 ? 77  GLU A C   1 
ATOM   609  O  O   A GLU A 1 77  ? 28.401 -20.423 26.927  0.50 13.57 ? 77  GLU A O   1 
ATOM   610  O  O   B GLU A 1 77  ? 28.403 -20.422 26.936  0.50 14.03 ? 77  GLU A O   1 
ATOM   611  C  CB  A GLU A 1 77  ? 28.904 -21.960 29.818  0.50 15.25 ? 77  GLU A CB  1 
ATOM   612  C  CB  B GLU A 1 77  ? 28.908 -22.035 29.801  0.50 17.06 ? 77  GLU A CB  1 
ATOM   613  C  CG  A GLU A 1 77  ? 30.319 -21.555 29.461  0.50 17.08 ? 77  GLU A CG  1 
ATOM   614  C  CG  B GLU A 1 77  ? 30.331 -21.825 29.299  0.50 19.73 ? 77  GLU A CG  1 
ATOM   615  C  CD  A GLU A 1 77  ? 30.762 -22.092 28.116  0.50 18.25 ? 77  GLU A CD  1 
ATOM   616  C  CD  B GLU A 1 77  ? 31.246 -22.999 29.620  0.50 20.99 ? 77  GLU A CD  1 
ATOM   617  O  OE1 A GLU A 1 77  ? 30.245 -23.150 27.694  0.50 19.04 ? 77  GLU A OE1 1 
ATOM   618  O  OE1 B GLU A 1 77  ? 30.813 -24.153 29.439  0.50 26.01 ? 77  GLU A OE1 1 
ATOM   619  O  OE2 A GLU A 1 77  ? 31.634 -21.457 27.485  0.50 20.45 ? 77  GLU A OE2 1 
ATOM   620  O  OE2 B GLU A 1 77  ? 32.398 -22.790 30.053  0.50 22.20 ? 77  GLU A OE2 1 
ATOM   621  N  N   . GLU A 1 78  ? 27.237 -22.338 27.230  1.00 12.67 ? 78  GLU A N   1 
ATOM   622  C  CA  . GLU A 1 78  ? 27.165 -22.641 25.814  1.00 12.52 ? 78  GLU A CA  1 
ATOM   623  C  C   . GLU A 1 78  ? 25.934 -21.950 25.250  1.00 11.93 ? 78  GLU A C   1 
ATOM   624  O  O   . GLU A 1 78  ? 24.816 -22.458 25.349  1.00 13.21 ? 78  GLU A O   1 
ATOM   625  C  CB  . GLU A 1 78  ? 27.092 -24.152 25.572  1.00 14.73 ? 78  GLU A CB  1 
ATOM   626  C  CG  . GLU A 1 78  ? 27.206 -24.523 24.096  1.00 19.72 ? 78  GLU A CG  1 
ATOM   627  C  CD  . GLU A 1 78  ? 28.608 -24.310 23.525  1.00 24.36 ? 78  GLU A CD  1 
ATOM   628  O  OE1 . GLU A 1 78  ? 29.572 -24.245 24.312  1.00 32.68 ? 78  GLU A OE1 1 
ATOM   629  O  OE2 . GLU A 1 78  ? 28.776 -24.223 22.291  1.00 27.53 ? 78  GLU A OE2 1 
ATOM   630  N  N   . ARG A 1 79  ? 26.119 -20.775 24.669  1.00 9.98  ? 79  ARG A N   1 
ATOM   631  C  CA  . ARG A 1 79  ? 25.054 -19.994 24.060  1.00 9.15  ? 79  ARG A CA  1 
ATOM   632  C  C   . ARG A 1 79  ? 25.652 -19.106 22.999  1.00 8.46  ? 79  ARG A C   1 
ATOM   633  O  O   . ARG A 1 79  ? 26.844 -18.809 23.031  1.00 9.92  ? 79  ARG A O   1 
ATOM   634  C  CB  . ARG A 1 79  ? 24.350 -19.086 25.086  1.00 8.75  ? 79  ARG A CB  1 
ATOM   635  C  CG  . ARG A 1 79  ? 25.308 -18.151 25.816  1.00 8.92  ? 79  ARG A CG  1 
ATOM   636  C  CD  . ARG A 1 79  ? 24.600 -17.136 26.700  1.00 8.33  ? 79  ARG A CD  1 
ATOM   637  N  NE  . ARG A 1 79  ? 24.178 -15.958 25.952  1.00 9.14  ? 79  ARG A NE  1 
ATOM   638  C  CZ  . ARG A 1 79  ? 23.710 -14.856 26.525  1.00 8.52  ? 79  ARG A CZ  1 
ATOM   639  N  NH1 . ARG A 1 79  ? 23.582 -14.791 27.843  1.00 9.26  ? 79  ARG A NH1 1 
ATOM   640  N  NH2 . ARG A 1 79  ? 23.380 -13.803 25.769  1.00 8.97  ? 79  ARG A NH2 1 
ATOM   641  N  N   . HIS A 1 80  ? 24.784 -18.631 22.120  1.00 7.63  ? 80  HIS A N   1 
ATOM   642  C  CA  . HIS A 1 80  ? 25.104 -17.530 21.222  1.00 8.02  ? 80  HIS A CA  1 
ATOM   643  C  C   . HIS A 1 80  ? 25.051 -16.210 21.983  1.00 8.00  ? 80  HIS A C   1 
ATOM   644  O  O   . HIS A 1 80  ? 24.259 -16.070 22.930  1.00 8.67  ? 80  HIS A O   1 
ATOM   645  C  CB  . HIS A 1 80  ? 24.066 -17.462 20.123  1.00 8.30  ? 80  HIS A CB  1 
ATOM   646  C  CG  . HIS A 1 80  ? 23.978 -18.710 19.308  1.00 8.61  ? 80  HIS A CG  1 
ATOM   647  N  ND1 . HIS A 1 80  ? 22.800 -19.248 18.840  1.00 9.05  ? 80  HIS A ND1 1 
ATOM   648  C  CD2 . HIS A 1 80  ? 24.961 -19.528 18.876  1.00 8.69  ? 80  HIS A CD2 1 
ATOM   649  C  CE1 . HIS A 1 80  ? 23.074 -20.317 18.110  1.00 8.99  ? 80  HIS A CE1 1 
ATOM   650  N  NE2 . HIS A 1 80  ? 24.375 -20.522 18.139  1.00 9.76  ? 80  HIS A NE2 1 
ATOM   651  N  N   . VAL A 1 81  ? 25.830 -15.212 21.556  1.00 8.45  ? 81  VAL A N   1 
ATOM   652  C  CA  . VAL A 1 81  ? 25.703 -13.893 22.189  1.00 8.12  ? 81  VAL A CA  1 
ATOM   653  C  C   . VAL A 1 81  ? 24.249 -13.427 22.129  1.00 8.29  ? 81  VAL A C   1 
ATOM   654  O  O   . VAL A 1 81  ? 23.739 -12.870 23.096  1.00 9.01  ? 81  VAL A O   1 
ATOM   655  C  CB  . VAL A 1 81  ? 26.663 -12.845 21.587  1.00 8.61  ? 81  VAL A CB  1 
ATOM   656  C  CG1 . VAL A 1 81  ? 26.326 -11.437 22.094  1.00 8.54  ? 81  VAL A CG1 1 
ATOM   657  C  CG2 . VAL A 1 81  ? 28.091 -13.202 21.963  1.00 9.78  ? 81  VAL A CG2 1 
ATOM   658  N  N   . GLY A 1 82  ? 23.583 -13.660 21.001  1.00 8.51  ? 82  GLY A N   1 
ATOM   659  C  CA  . GLY A 1 82  ? 22.213 -13.201 20.824  1.00 9.15  ? 82  GLY A CA  1 
ATOM   660  C  C   . GLY A 1 82  ? 21.120 -13.989 21.541  1.00 8.46  ? 82  GLY A C   1 
ATOM   661  O  O   . GLY A 1 82  ? 19.945 -13.672 21.373  1.00 9.29  ? 82  GLY A O   1 
ATOM   662  N  N   . ASP A 1 83  ? 21.481 -14.986 22.354  1.00 7.19  ? 83  ASP A N   1 
ATOM   663  C  CA  . ASP A 1 83  ? 20.479 -15.833 23.009  1.00 7.34  ? 83  ASP A CA  1 
ATOM   664  C  C   . ASP A 1 83  ? 19.962 -15.219 24.304  1.00 8.34  ? 83  ASP A C   1 
ATOM   665  O  O   . ASP A 1 83  ? 20.514 -15.455 25.386  1.00 10.01 ? 83  ASP A O   1 
ATOM   666  C  CB  . ASP A 1 83  ? 21.066 -17.224 23.300  1.00 7.65  ? 83  ASP A CB  1 
ATOM   667  C  CG  . ASP A 1 83  ? 21.277 -18.046 22.047  1.00 8.03  ? 83  ASP A CG  1 
ATOM   668  O  OD1 . ASP A 1 83  ? 20.740 -17.663 20.986  1.00 8.54  ? 83  ASP A OD1 1 
ATOM   669  O  OD2 . ASP A 1 83  ? 22.011 -19.061 22.103  1.00 8.73  ? 83  ASP A OD2 1 
ATOM   670  N  N   . LEU A 1 84  ? 18.875 -14.463 24.189  1.00 7.51  ? 84  LEU A N   1 
ATOM   671  C  CA  . LEU A 1 84  ? 18.257 -13.827 25.341  1.00 7.91  ? 84  LEU A CA  1 
ATOM   672  C  C   . LEU A 1 84  ? 17.064 -14.603 25.918  1.00 9.03  ? 84  LEU A C   1 
ATOM   673  O  O   . LEU A 1 84  ? 16.323 -14.069 26.757  1.00 11.67 ? 84  LEU A O   1 
ATOM   674  C  CB  . LEU A 1 84  ? 17.874 -12.372 24.989  1.00 9.35  ? 84  LEU A CB  1 
ATOM   675  C  CG  . LEU A 1 84  ? 19.058 -11.458 24.678  1.00 10.80 ? 84  LEU A CG  1 
ATOM   676  C  CD1 . LEU A 1 84  ? 18.527 -10.089 24.283  1.00 10.62 ? 84  LEU A CD1 1 
ATOM   677  C  CD2 . LEU A 1 84  ? 20.029 -11.360 25.847  1.00 12.92 ? 84  LEU A CD2 1 
ATOM   678  N  N   . GLY A 1 85  ? 16.895 -15.858 25.504  1.00 8.88  ? 85  GLY A N   1 
ATOM   679  C  CA  . GLY A 1 85  ? 15.905 -16.738 26.108  1.00 9.95  ? 85  GLY A CA  1 
ATOM   680  C  C   . GLY A 1 85  ? 14.497 -16.456 25.630  1.00 9.32  ? 85  GLY A C   1 
ATOM   681  O  O   . GLY A 1 85  ? 14.245 -16.401 24.431  1.00 10.11 ? 85  GLY A O   1 
ATOM   682  N  N   . ASN A 1 86  ? 13.580 -16.297 26.583  1.00 8.95  ? 86  ASN A N   1 
ATOM   683  C  CA  . ASN A 1 86  ? 12.184 -16.071 26.285  1.00 8.93  ? 86  ASN A CA  1 
ATOM   684  C  C   . ASN A 1 86  ? 11.689 -14.866 27.025  1.00 8.75  ? 86  ASN A C   1 
ATOM   685  O  O   . ASN A 1 86  ? 12.133 -14.585 28.135  1.00 10.81 ? 86  ASN A O   1 
ATOM   686  C  CB  . ASN A 1 86  ? 11.345 -17.263 26.743  1.00 8.59  ? 86  ASN A CB  1 
ATOM   687  C  CG  . ASN A 1 86  ? 11.579 -18.480 25.900  1.00 10.03 ? 86  ASN A CG  1 
ATOM   688  O  OD1 . ASN A 1 86  ? 11.241 -18.486 24.727  1.00 9.86  ? 86  ASN A OD1 1 
ATOM   689  N  ND2 . ASN A 1 86  ? 12.149 -19.525 26.498  1.00 12.03 ? 86  ASN A ND2 1 
ATOM   690  N  N   . VAL A 1 87  ? 10.751 -14.176 26.396  1.00 8.08  ? 87  VAL A N   1 
ATOM   691  C  CA  . VAL A 1 87  ? 9.908  -13.236 27.109  1.00 8.43  ? 87  VAL A CA  1 
ATOM   692  C  C   . VAL A 1 87  ? 8.583  -13.935 27.392  1.00 8.48  ? 87  VAL A C   1 
ATOM   693  O  O   . VAL A 1 87  ? 8.247  -14.920 26.737  1.00 9.89  ? 87  VAL A O   1 
ATOM   694  C  CB  . VAL A 1 87  ? 9.698  -11.909 26.348  1.00 10.07 ? 87  VAL A CB  1 
ATOM   695  C  CG1 . VAL A 1 87  ? 11.028 -11.189 26.181  1.00 10.87 ? 87  VAL A CG1 1 
ATOM   696  C  CG2 . VAL A 1 87  ? 9.022  -12.105 24.998  1.00 11.15 ? 87  VAL A CG2 1 
ATOM   697  N  N   . THR A 1 88  ? 7.828  -13.414 28.352  1.00 9.26  ? 88  THR A N   1 
ATOM   698  C  CA  . THR A 1 88  ? 6.609  -14.072 28.833  1.00 10.98 ? 88  THR A CA  1 
ATOM   699  C  C   . THR A 1 88  ? 5.437  -13.144 28.627  1.00 9.71  ? 88  THR A C   1 
ATOM   700  O  O   . THR A 1 88  ? 5.404  -12.065 29.217  1.00 10.92 ? 88  THR A O   1 
ATOM   701  C  CB  . THR A 1 88  ? 6.709  -14.403 30.335  1.00 12.71 ? 88  THR A CB  1 
ATOM   702  O  OG1 . THR A 1 88  ? 7.833  -15.263 30.543  1.00 14.65 ? 88  THR A OG1 1 
ATOM   703  C  CG2 . THR A 1 88  ? 5.428  -15.072 30.865  1.00 14.51 ? 88  THR A CG2 1 
ATOM   704  N  N   . ALA A 1 89  ? 4.477  -13.559 27.811  1.00 9.97  ? 89  ALA A N   1 
ATOM   705  C  CA  . ALA A 1 89  ? 3.242  -12.821 27.615  1.00 11.65 ? 89  ALA A CA  1 
ATOM   706  C  C   . ALA A 1 89  ? 2.169  -13.351 28.554  1.00 10.52 ? 89  ALA A C   1 
ATOM   707  O  O   . ALA A 1 89  ? 2.018  -14.569 28.727  1.00 11.41 ? 89  ALA A O   1 
ATOM   708  C  CB  . ALA A 1 89  ? 2.782  -12.932 26.176  1.00 13.34 ? 89  ALA A CB  1 
ATOM   709  N  N   . ASP A 1 90  ? 1.420  -12.414 29.135  1.00 11.51 ? 90  ASP A N   1 
ATOM   710  C  CA  . ASP A 1 90  ? 0.289  -12.709 29.997  1.00 11.20 ? 90  ASP A CA  1 
ATOM   711  C  C   . ASP A 1 90  ? -0.979 -12.972 29.165  1.00 11.29 ? 90  ASP A C   1 
ATOM   712  O  O   . ASP A 1 90  ? -0.926 -12.979 27.916  1.00 11.71 ? 90  ASP A O   1 
ATOM   713  C  CB  . ASP A 1 90  ? 0.119  -11.578 31.031  1.00 11.68 ? 90  ASP A CB  1 
ATOM   714  C  CG  . ASP A 1 90  ? -0.278 -10.226 30.423  1.00 13.77 ? 90  ASP A CG  1 
ATOM   715  O  OD1 . ASP A 1 90  ? -0.824 -10.163 29.300  1.00 13.46 ? 90  ASP A OD1 1 
ATOM   716  O  OD2 . ASP A 1 90  ? -0.043 -9.206  31.117  1.00 16.19 ? 90  ASP A OD2 1 
ATOM   717  N  N   . LYS A 1 91  ? -2.111 -13.200 29.841  1.00 11.62 ? 91  LYS A N   1 
ATOM   718  C  CA  . LYS A 1 91  ? -3.365 -13.483 29.130  1.00 11.56 ? 91  LYS A CA  1 
ATOM   719  C  C   . LYS A 1 91  ? -3.943 -12.302 28.348  1.00 13.23 ? 91  LYS A C   1 
ATOM   720  O  O   . LYS A 1 91  ? -4.821 -12.499 27.508  1.00 15.69 ? 91  LYS A O   1 
ATOM   721  C  CB  . LYS A 1 91  ? -4.419 -14.075 30.074  1.00 10.19 ? 91  LYS A CB  1 
ATOM   722  C  CG  . LYS A 1 91  ? -4.176 -15.532 30.449  1.00 11.54 ? 91  LYS A CG  1 
ATOM   723  C  CD  . LYS A 1 91  ? -4.387 -16.511 29.300  1.00 13.90 ? 91  LYS A CD  1 
ATOM   724  C  CE  . LYS A 1 91  ? -5.848 -16.805 29.047  1.00 16.45 ? 91  LYS A CE  1 
ATOM   725  N  NZ  . LYS A 1 91  ? -6.011 -17.683 27.857  1.00 19.73 ? 91  LYS A NZ  1 
ATOM   726  N  N   . ASP A 1 92  ? -3.442 -11.096 28.601  1.00 12.64 ? 92  ASP A N   1 
ATOM   727  C  CA  . ASP A 1 92  ? -3.757 -9.940  27.760  1.00 12.54 ? 92  ASP A CA  1 
ATOM   728  C  C   . ASP A 1 92  ? -2.863 -9.840  26.517  1.00 11.67 ? 92  ASP A C   1 
ATOM   729  O  O   . ASP A 1 92  ? -3.063 -8.946  25.684  1.00 13.93 ? 92  ASP A O   1 
ATOM   730  C  CB  . ASP A 1 92  ? -3.647 -8.649  28.565  1.00 13.95 ? 92  ASP A CB  1 
ATOM   731  C  CG  . ASP A 1 92  ? -4.574 -8.618  29.767  1.00 17.00 ? 92  ASP A CG  1 
ATOM   732  O  OD1 . ASP A 1 92  ? -5.710 -9.134  29.695  1.00 21.82 ? 92  ASP A OD1 1 
ATOM   733  O  OD2 . ASP A 1 92  ? -4.151 -8.072  30.800  1.00 20.94 ? 92  ASP A OD2 1 
ATOM   734  N  N   . GLY A 1 93  ? -1.874 -10.730 26.404  1.00 10.78 ? 93  GLY A N   1 
ATOM   735  C  CA  . GLY A 1 93  ? -0.952 -10.763 25.274  1.00 10.34 ? 93  GLY A CA  1 
ATOM   736  C  C   . GLY A 1 93  ? 0.224  -9.817  25.398  1.00 10.25 ? 93  GLY A C   1 
ATOM   737  O  O   . GLY A 1 93  ? 0.898  -9.523  24.404  1.00 11.18 ? 93  GLY A O   1 
ATOM   738  N  N   . VAL A 1 94  ? 0.482  -9.370  26.625  1.00 10.45 ? 94  VAL A N   1 
ATOM   739  C  CA  . VAL A 1 94  ? 1.505  -8.390  26.916  1.00 10.32 ? 94  VAL A CA  1 
ATOM   740  C  C   . VAL A 1 94  ? 2.658  -9.021  27.650  1.00 9.74  ? 94  VAL A C   1 
ATOM   741  O  O   . VAL A 1 94  ? 2.469  -9.683  28.679  1.00 11.13 ? 94  VAL A O   1 
ATOM   742  C  CB  . VAL A 1 94  ? 0.944  -7.239  27.767  1.00 11.16 ? 94  VAL A CB  1 
ATOM   743  C  CG1 . VAL A 1 94  ? 2.042  -6.242  28.141  1.00 11.22 ? 94  VAL A CG1 1 
ATOM   744  C  CG2 . VAL A 1 94  ? -0.182 -6.553  27.018  1.00 13.16 ? 94  VAL A CG2 1 
ATOM   745  N  N   . ALA A 1 95  ? 3.856  -8.798  27.119  1.00 9.65  ? 95  ALA A N   1 
ATOM   746  C  CA  . ALA A 1 95  ? 5.088  -9.168  27.788  1.00 10.49 ? 95  ALA A CA  1 
ATOM   747  C  C   . ALA A 1 95  ? 5.762  -7.923  28.324  1.00 10.67 ? 95  ALA A C   1 
ATOM   748  O  O   . ALA A 1 95  ? 6.119  -7.040  27.559  1.00 13.16 ? 95  ALA A O   1 
ATOM   749  C  CB  . ALA A 1 95  ? 6.012  -9.884  26.824  1.00 11.00 ? 95  ALA A CB  1 
ATOM   750  N  N   . ASP A 1 96  ? 5.936  -7.865  29.635  1.00 9.88  ? 96  ASP A N   1 
ATOM   751  C  CA  . ASP A 1 96  ? 6.719  -6.817  30.261  1.00 10.97 ? 96  ASP A CA  1 
ATOM   752  C  C   . ASP A 1 96  ? 8.112  -7.381  30.438  1.00 12.15 ? 96  ASP A C   1 
ATOM   753  O  O   . ASP A 1 96  ? 8.318  -8.355  31.150  1.00 15.26 ? 96  ASP A O   1 
ATOM   754  C  CB  . ASP A 1 96  ? 6.068  -6.381  31.564  1.00 13.69 ? 96  ASP A CB  1 
ATOM   755  C  CG  . ASP A 1 96  ? 4.797  -5.579  31.320  1.00 15.74 ? 96  ASP A CG  1 
ATOM   756  O  OD1 . ASP A 1 96  ? 4.845  -4.555  30.577  1.00 18.99 ? 96  ASP A OD1 1 
ATOM   757  O  OD2 . ASP A 1 96  ? 3.748  -5.990  31.844  1.00 22.33 ? 96  ASP A OD2 1 
ATOM   758  N  N   . VAL A 1 97  ? 9.054  -6.814  29.710  1.00 10.17 ? 97  VAL A N   1 
ATOM   759  C  CA  . VAL A 1 97  ? 10.390 -7.373  29.602  1.00 11.15 ? 97  VAL A CA  1 
ATOM   760  C  C   . VAL A 1 97  ? 11.276 -6.714  30.634  1.00 10.35 ? 97  VAL A C   1 
ATOM   761  O  O   . VAL A 1 97  ? 11.313 -5.479  30.726  1.00 10.50 ? 97  VAL A O   1 
ATOM   762  C  CB  . VAL A 1 97  ? 10.944 -7.147  28.188  1.00 11.90 ? 97  VAL A CB  1 
ATOM   763  C  CG1 . VAL A 1 97  ? 12.367 -7.665  28.048  1.00 12.41 ? 97  VAL A CG1 1 
ATOM   764  C  CG2 . VAL A 1 97  ? 10.032 -7.814  27.169  1.00 13.39 ? 97  VAL A CG2 1 
ATOM   765  N  N   . SER A 1 98  ? 12.011 -7.531  31.375  0.90 10.28 ? 98  SER A N   1 
ATOM   766  C  CA  . SER A 1 98  ? 12.982 -7.060  32.340  0.90 10.95 ? 98  SER A CA  1 
ATOM   767  C  C   . SER A 1 98  ? 14.061 -8.127  32.465  0.90 11.26 ? 98  SER A C   1 
ATOM   768  O  O   . SER A 1 98  ? 13.854 -9.156  33.129  0.90 14.13 ? 98  SER A O   1 
ATOM   769  C  CB  . SER A 1 98  ? 12.302 -6.779  33.681  0.90 14.28 ? 98  SER A CB  1 
ATOM   770  O  OG  . SER A 1 98  ? 13.227 -6.241  34.596  0.90 18.39 ? 98  SER A OG  1 
ATOM   771  N  N   . ILE A 1 99  ? 15.187 -7.888  31.802  1.00 11.55 ? 99  ILE A N   1 
ATOM   772  C  CA  . ILE A 1 99  ? 16.298 -8.844  31.671  1.00 12.16 ? 99  ILE A CA  1 
ATOM   773  C  C   . ILE A 1 99  ? 17.581 -8.108  32.054  1.00 11.37 ? 99  ILE A C   1 
ATOM   774  O  O   . ILE A 1 99  ? 17.732 -6.919  31.762  1.00 12.58 ? 99  ILE A O   1 
ATOM   775  C  CB  . ILE A 1 99  ? 16.402 -9.374  30.209  1.00 12.64 ? 99  ILE A CB  1 
ATOM   776  C  CG1 . ILE A 1 99  ? 15.246 -10.341 29.896  1.00 14.33 ? 99  ILE A CG1 1 
ATOM   777  C  CG2 . ILE A 1 99  ? 17.722 -10.091 29.925  1.00 13.68 ? 99  ILE A CG2 1 
ATOM   778  C  CD1 . ILE A 1 99  ? 15.046 -10.610 28.420  1.00 17.05 ? 99  ILE A CD1 1 
ATOM   779  N  N   . GLU A 1 100 ? 18.506 -8.804  32.696  1.00 11.52 ? 100 GLU A N   1 
ATOM   780  C  CA  . GLU A 1 100 ? 19.867 -8.309  32.838  1.00 11.43 ? 100 GLU A CA  1 
ATOM   781  C  C   . GLU A 1 100 ? 20.740 -9.390  32.220  1.00 10.58 ? 100 GLU A C   1 
ATOM   782  O  O   . GLU A 1 100 ? 20.603 -10.558 32.574  1.00 13.54 ? 100 GLU A O   1 
ATOM   783  C  CB  . GLU A 1 100 ? 20.224 -8.095  34.302  1.00 14.33 ? 100 GLU A CB  1 
ATOM   784  C  CG  . GLU A 1 100 ? 21.546 -7.396  34.510  1.00 16.92 ? 100 GLU A CG  1 
ATOM   785  C  CD  . GLU A 1 100 ? 21.803 -7.208  35.930  0.00 14.63 ? 100 GLU A CD  1 
ATOM   786  O  OE1 . GLU A 1 100 ? 20.950 -7.565  36.769  0.00 26.15 ? 100 GLU A OE1 1 
ATOM   787  O  OE2 . GLU A 1 100 ? 22.883 -6.666  36.245  0.00 17.01 ? 100 GLU A OE2 1 
ATOM   788  N  N   . ASP A 1 101 ? 21.633 -9.016  31.306  1.00 10.01 ? 101 ASP A N   1 
ATOM   789  C  CA  . ASP A 1 101 ? 22.479 -9.997  30.623  1.00 11.23 ? 101 ASP A CA  1 
ATOM   790  C  C   . ASP A 1 101 ? 23.926 -9.551  30.633  1.00 10.85 ? 101 ASP A C   1 
ATOM   791  O  O   . ASP A 1 101 ? 24.218 -8.382  30.391  1.00 12.28 ? 101 ASP A O   1 
ATOM   792  C  CB  . ASP A 1 101 ? 22.002 -10.216 29.189  1.00 11.63 ? 101 ASP A CB  1 
ATOM   793  C  CG  . ASP A 1 101 ? 22.611 -11.457 28.563  1.00 11.52 ? 101 ASP A CG  1 
ATOM   794  O  OD1 . ASP A 1 101 ? 22.171 -12.564 28.940  1.00 13.00 ? 101 ASP A OD1 1 
ATOM   795  O  OD2 . ASP A 1 101 ? 23.546 -11.334 27.743  1.00 11.18 ? 101 ASP A OD2 1 
ATOM   796  N  N   . SER A 1 102 ? 24.816 -10.504 30.890  1.00 11.40 ? 102 SER A N   1 
ATOM   797  C  CA  . SER A 1 102 ? 26.234 -10.262 31.064  1.00 13.17 ? 102 SER A CA  1 
ATOM   798  C  C   . SER A 1 102 ? 27.056 -10.544 29.789  1.00 10.92 ? 102 SER A C   1 
ATOM   799  O  O   . SER A 1 102 ? 28.255 -10.269 29.764  1.00 12.84 ? 102 SER A O   1 
ATOM   800  C  CB  . SER A 1 102 ? 26.726 -11.152 32.223  1.00 14.81 ? 102 SER A CB  1 
ATOM   801  O  OG  A SER A 1 102 ? 26.473 -10.382 33.390  0.50 17.90 ? 102 SER A OG  1 
ATOM   802  O  OG  B SER A 1 102 ? 27.025 -12.378 31.589  0.50 18.57 ? 102 SER A OG  1 
ATOM   803  N  N   . VAL A 1 103 ? 26.416 -11.095 28.754  1.00 9.53  ? 103 VAL A N   1 
ATOM   804  C  CA  . VAL A 1 103 ? 27.106 -11.543 27.540  1.00 8.67  ? 103 VAL A CA  1 
ATOM   805  C  C   . VAL A 1 103 ? 26.954 -10.554 26.386  1.00 9.44  ? 103 VAL A C   1 
ATOM   806  O  O   . VAL A 1 103 ? 27.939 -10.219 25.731  1.00 11.44 ? 103 VAL A O   1 
ATOM   807  C  CB  . VAL A 1 103 ? 26.619 -12.945 27.132  1.00 8.62  ? 103 VAL A CB  1 
ATOM   808  C  CG1 . VAL A 1 103 ? 27.200 -13.375 25.788  1.00 9.92  ? 103 VAL A CG1 1 
ATOM   809  C  CG2 . VAL A 1 103 ? 26.988 -13.963 28.193  1.00 9.78  ? 103 VAL A CG2 1 
ATOM   810  N  N   . ILE A 1 104 ? 25.738 -10.071 26.146  1.00 8.57  ? 104 ILE A N   1 
ATOM   811  C  CA  . ILE A 1 104 ? 25.568 -8.955  25.207  1.00 8.85  ? 104 ILE A CA  1 
ATOM   812  C  C   . ILE A 1 104 ? 26.284 -7.713  25.727  1.00 9.60  ? 104 ILE A C   1 
ATOM   813  O  O   . ILE A 1 104 ? 26.540 -7.572  26.922  1.00 10.60 ? 104 ILE A O   1 
ATOM   814  C  CB  . ILE A 1 104 ? 24.089 -8.620  24.926  1.00 9.05  ? 104 ILE A CB  1 
ATOM   815  C  CG1 . ILE A 1 104 ? 23.341 -8.179  26.202  1.00 9.89  ? 104 ILE A CG1 1 
ATOM   816  C  CG2 . ILE A 1 104 ? 23.405 -9.788  24.230  1.00 9.18  ? 104 ILE A CG2 1 
ATOM   817  C  CD1 . ILE A 1 104 ? 21.971 -7.599  25.941  1.00 9.95  ? 104 ILE A CD1 1 
ATOM   818  N  N   . SER A 1 105 ? 26.605 -6.824  24.798  1.00 8.85  ? 105 SER A N   1 
ATOM   819  C  CA  . SER A 1 105 ? 27.195 -5.542  25.142  1.00 9.92  ? 105 SER A CA  1 
ATOM   820  C  C   . SER A 1 105 ? 26.671 -4.476  24.209  1.00 9.42  ? 105 SER A C   1 
ATOM   821  O  O   . SER A 1 105 ? 26.089 -4.777  23.172  1.00 9.49  ? 105 SER A O   1 
ATOM   822  C  CB  . SER A 1 105 ? 28.711 -5.614  25.022  1.00 10.90 ? 105 SER A CB  1 
ATOM   823  O  OG  . SER A 1 105 ? 29.316 -4.490  25.624  1.00 12.62 ? 105 SER A OG  1 
ATOM   824  N  N   . LEU A 1 106 ? 26.888 -3.225  24.599  1.00 10.27 ? 106 LEU A N   1 
ATOM   825  C  CA  . LEU A 1 106 ? 26.603 -2.072  23.733  1.00 10.58 ? 106 LEU A CA  1 
ATOM   826  C  C   . LEU A 1 106 ? 27.880 -1.415  23.196  1.00 12.54 ? 106 LEU A C   1 
ATOM   827  O  O   . LEU A 1 106 ? 27.819 -0.335  22.614  1.00 14.09 ? 106 LEU A O   1 
ATOM   828  C  CB  . LEU A 1 106 ? 25.710 -1.055  24.460  1.00 10.55 ? 106 LEU A CB  1 
ATOM   829  C  CG  . LEU A 1 106 ? 24.372 -1.602  24.963  1.00 10.56 ? 106 LEU A CG  1 
ATOM   830  C  CD1 . LEU A 1 106 ? 23.569 -0.495  25.646  1.00 10.45 ? 106 LEU A CD1 1 
ATOM   831  C  CD2 . LEU A 1 106 ? 23.557 -2.251  23.850  1.00 11.23 ? 106 LEU A CD2 1 
ATOM   832  N  N   . SER A 1 107 ? 29.016 -2.091  23.364  1.00 14.70 ? 107 SER A N   1 
ATOM   833  C  CA  . SER A 1 107 ? 30.265 -1.728  22.701  1.00 17.31 ? 107 SER A CA  1 
ATOM   834  C  C   . SER A 1 107 ? 31.096 -2.982  22.365  1.00 20.65 ? 107 SER A C   1 
ATOM   835  O  O   . SER A 1 107 ? 30.896 -4.043  22.955  1.00 22.64 ? 107 SER A O   1 
ATOM   836  C  CB  . SER A 1 107 ? 31.051 -0.756  23.581  1.00 22.79 ? 107 SER A CB  1 
ATOM   837  O  OG  . SER A 1 107 ? 31.615 -1.416  24.693  1.00 26.19 ? 107 SER A OG  1 
ATOM   838  N  N   . GLY A 1 108 ? 31.994 -2.868  21.390  1.00 18.46 ? 108 GLY A N   1 
ATOM   839  C  CA  . GLY A 1 108 ? 32.942 -3.956  21.075  1.00 19.91 ? 108 GLY A CA  1 
ATOM   840  C  C   . GLY A 1 108 ? 32.400 -5.137  20.277  1.00 20.27 ? 108 GLY A C   1 
ATOM   841  O  O   . GLY A 1 108 ? 31.365 -5.038  19.646  1.00 19.75 ? 108 GLY A O   1 
ATOM   842  N  N   . ASP A 1 109 ? 33.108 -6.265  20.281  1.00 18.07 ? 109 ASP A N   1 
ATOM   843  C  CA  . ASP A 1 109 ? 32.698 -7.395  19.419  1.00 17.69 ? 109 ASP A CA  1 
ATOM   844  C  C   . ASP A 1 109 ? 31.455 -8.165  19.892  1.00 15.90 ? 109 ASP A C   1 
ATOM   845  O  O   . ASP A 1 109 ? 30.862 -8.887  19.073  1.00 16.94 ? 109 ASP A O   1 
ATOM   846  C  CB  . ASP A 1 109 ? 33.859 -8.349  19.116  1.00 22.51 ? 109 ASP A CB  1 
ATOM   847  C  CG  . ASP A 1 109 ? 34.262 -9.183  20.293  1.00 24.56 ? 109 ASP A CG  1 
ATOM   848  O  OD1 . ASP A 1 109 ? 34.234 -8.664  21.431  1.00 29.01 ? 109 ASP A OD1 1 
ATOM   849  O  OD2 . ASP A 1 109 ? 34.645 -10.355 20.065  1.00 30.39 ? 109 ASP A OD2 1 
ATOM   850  N  N   . HIS A 1 110 ? 31.059 -8.017  21.170  1.00 13.00 ? 110 HIS A N   1 
ATOM   851  C  CA  . HIS A 1 110 ? 29.762 -8.555  21.638  1.00 12.01 ? 110 HIS A CA  1 
ATOM   852  C  C   . HIS A 1 110 ? 28.640 -7.532  21.427  1.00 11.44 ? 110 HIS A C   1 
ATOM   853  O  O   . HIS A 1 110 ? 27.515 -7.757  21.891  1.00 10.72 ? 110 HIS A O   1 
ATOM   854  C  CB  . HIS A 1 110 ? 29.762 -8.921  23.132  1.00 12.37 ? 110 HIS A CB  1 
ATOM   855  C  CG  . HIS A 1 110 ? 30.768 -9.952  23.525  1.00 14.44 ? 110 HIS A CG  1 
ATOM   856  N  ND1 . HIS A 1 110 ? 30.556 -10.810 24.578  1.00 17.91 ? 110 HIS A ND1 1 
ATOM   857  C  CD2 . HIS A 1 110 ? 31.998 -10.245 23.040  1.00 15.67 ? 110 HIS A CD2 1 
ATOM   858  C  CE1 . HIS A 1 110 ? 31.607 -11.602 24.714  1.00 19.12 ? 110 HIS A CE1 1 
ATOM   859  N  NE2 . HIS A 1 110 ? 32.502 -11.270 23.803  1.00 17.01 ? 110 HIS A NE2 1 
ATOM   860  N  N   . CYS A 1 111 ? 28.938 -6.418  20.753  1.00 12.04 ? 111 CYS A N   1 
ATOM   861  C  CA  . CYS A 1 111 ? 27.976 -5.340  20.580  1.00 11.83 ? 111 CYS A CA  1 
ATOM   862  C  C   . CYS A 1 111 ? 26.793 -5.752  19.724  1.00 10.14 ? 111 CYS A C   1 
ATOM   863  O  O   . CYS A 1 111 ? 26.958 -6.368  18.674  1.00 11.79 ? 111 CYS A O   1 
ATOM   864  C  CB  . CYS A 1 111 ? 28.617 -4.098  19.967  1.00 12.57 ? 111 CYS A CB  1 
ATOM   865  S  SG  . CYS A 1 111 ? 27.504 -2.689  20.027  1.00 14.96 ? 111 CYS A SG  1 
ATOM   866  N  N   . ILE A 1 112 ? 25.603 -5.423  20.205  1.00 9.01  ? 112 ILE A N   1 
ATOM   867  C  CA  . ILE A 1 112 ? 24.362 -5.724  19.507  1.00 8.79  ? 112 ILE A CA  1 
ATOM   868  C  C   . ILE A 1 112 ? 23.740 -4.535  18.767  1.00 8.38  ? 112 ILE A C   1 
ATOM   869  O  O   . ILE A 1 112 ? 22.755 -4.694  18.061  1.00 8.14  ? 112 ILE A O   1 
ATOM   870  C  CB  . ILE A 1 112 ? 23.334 -6.374  20.454  1.00 8.10  ? 112 ILE A CB  1 
ATOM   871  C  CG1 . ILE A 1 112 ? 22.889 -5.405  21.561  1.00 8.86  ? 112 ILE A CG1 1 
ATOM   872  C  CG2 . ILE A 1 112 ? 23.909 -7.666  21.042  1.00 8.63  ? 112 ILE A CG2 1 
ATOM   873  C  CD1 . ILE A 1 112 ? 21.778 -5.925  22.439  1.00 10.49 ? 112 ILE A CD1 1 
ATOM   874  N  N   . ILE A 1 113 ? 24.341 -3.352  18.906  1.00 8.58  ? 113 ILE A N   1 
ATOM   875  C  CA  . ILE A 1 113 ? 23.858 -2.192  18.163  1.00 8.90  ? 113 ILE A CA  1 
ATOM   876  C  C   . ILE A 1 113 ? 24.061 -2.458  16.663  1.00 9.42  ? 113 ILE A C   1 
ATOM   877  O  O   . ILE A 1 113 ? 25.100 -2.971  16.243  1.00 10.95 ? 113 ILE A O   1 
ATOM   878  C  CB  . ILE A 1 113 ? 24.539 -0.879  18.614  1.00 9.18  ? 113 ILE A CB  1 
ATOM   879  C  CG1 . ILE A 1 113 ? 24.093 -0.562  20.048  1.00 10.40 ? 113 ILE A CG1 1 
ATOM   880  C  CG2 . ILE A 1 113 ? 24.191 0.256   17.653  1.00 9.71  ? 113 ILE A CG2 1 
ATOM   881  C  CD1 . ILE A 1 113 ? 24.870 0.525   20.750  1.00 11.53 ? 113 ILE A CD1 1 
ATOM   882  N  N   . GLY A 1 114 ? 23.046 -2.126  15.872  1.00 8.66  ? 114 GLY A N   1 
ATOM   883  C  CA  . GLY A 1 114 ? 23.070 -2.368  14.443  1.00 8.46  ? 114 GLY A CA  1 
ATOM   884  C  C   . GLY A 1 114 ? 22.643 -3.767  14.031  1.00 8.83  ? 114 GLY A C   1 
ATOM   885  O  O   . GLY A 1 114 ? 22.680 -4.099  12.854  1.00 9.47  ? 114 GLY A O   1 
ATOM   886  N  N   . ARG A 1 115 ? 22.247 -4.594  15.004  1.00 8.44  ? 115 ARG A N   1 
ATOM   887  C  CA  . ARG A 1 115 ? 21.763 -5.952  14.726  1.00 8.93  ? 115 ARG A CA  1 
ATOM   888  C  C   . ARG A 1 115 ? 20.263 -5.948  14.940  1.00 8.15  ? 115 ARG A C   1 
ATOM   889  O  O   . ARG A 1 115 ? 19.697 -4.908  15.252  1.00 9.57  ? 115 ARG A O   1 
ATOM   890  C  CB  . ARG A 1 115 ? 22.529 -6.943  15.593  1.00 10.15 ? 115 ARG A CB  1 
ATOM   891  C  CG  . ARG A 1 115 ? 24.016 -6.699  15.416  1.00 12.48 ? 115 ARG A CG  1 
ATOM   892  C  CD  . ARG A 1 115 ? 24.887 -7.845  15.835  1.00 13.35 ? 115 ARG A CD  1 
ATOM   893  N  NE  . ARG A 1 115 ? 26.303 -7.521  15.653  1.00 15.21 ? 115 ARG A NE  1 
ATOM   894  C  CZ  . ARG A 1 115 ? 27.050 -7.828  14.583  1.00 14.37 ? 115 ARG A CZ  1 
ATOM   895  N  NH1 . ARG A 1 115 ? 26.543 -8.466  13.533  1.00 13.65 ? 115 ARG A NH1 1 
ATOM   896  N  NH2 . ARG A 1 115 ? 28.338 -7.508  14.580  1.00 15.24 ? 115 ARG A NH2 1 
ATOM   897  N  N   . THR A 1 116 ? 19.601 -7.076  14.718  1.00 8.26  ? 116 THR A N   1 
ATOM   898  C  CA  . THR A 1 116 ? 18.144 -7.150  14.781  1.00 8.45  ? 116 THR A CA  1 
ATOM   899  C  C   . THR A 1 116 ? 17.666 -7.917  16.005  1.00 7.71  ? 116 THR A C   1 
ATOM   900  O  O   . THR A 1 116 ? 18.107 -9.037  16.244  1.00 10.09 ? 116 THR A O   1 
ATOM   901  C  CB  . THR A 1 116 ? 17.558 -7.818  13.532  1.00 9.41  ? 116 THR A CB  1 
ATOM   902  O  OG1 . THR A 1 116 ? 17.851 -7.017  12.396  1.00 10.65 ? 116 THR A OG1 1 
ATOM   903  C  CG2 . THR A 1 116 ? 16.049 -7.979  13.614  1.00 11.48 ? 116 THR A CG2 1 
ATOM   904  N  N   . LEU A 1 117 ? 16.771 -7.315  16.780  1.00 6.84  ? 117 LEU A N   1 
ATOM   905  C  CA  . LEU A 1 117 ? 16.070 -8.008  17.861  1.00 6.54  ? 117 LEU A CA  1 
ATOM   906  C  C   . LEU A 1 117 ? 14.811 -8.620  17.287  1.00 7.08  ? 117 LEU A C   1 
ATOM   907  O  O   . LEU A 1 117 ? 14.096 -7.959  16.547  1.00 7.36  ? 117 LEU A O   1 
ATOM   908  C  CB  . LEU A 1 117 ? 15.695 -6.991  18.948  1.00 6.23  ? 117 LEU A CB  1 
ATOM   909  C  CG  . LEU A 1 117 ? 15.146 -7.556  20.247  1.00 6.92  ? 117 LEU A CG  1 
ATOM   910  C  CD1 . LEU A 1 117 ? 16.165 -8.405  20.995  1.00 8.55  ? 117 LEU A CD1 1 
ATOM   911  C  CD2 . LEU A 1 117 ? 14.664 -6.419  21.134  1.00 8.38  ? 117 LEU A CD2 1 
ATOM   912  N  N   . VAL A 1 118 ? 14.550 -9.881  17.639  1.00 6.92  ? 118 VAL A N   1 
ATOM   913  C  CA  . VAL A 1 118 ? 13.419 -10.616 17.091  1.00 7.05  ? 118 VAL A CA  1 
ATOM   914  C  C   . VAL A 1 118 ? 12.656 -11.281 18.226  1.00 7.47  ? 118 VAL A C   1 
ATOM   915  O  O   . VAL A 1 118 ? 13.262 -11.897 19.118  1.00 8.15  ? 118 VAL A O   1 
ATOM   916  C  CB  . VAL A 1 118 ? 13.882 -11.705 16.098  1.00 7.66  ? 118 VAL A CB  1 
ATOM   917  C  CG1 . VAL A 1 118 ? 12.712 -12.506 15.541  1.00 9.64  ? 118 VAL A CG1 1 
ATOM   918  C  CG2 . VAL A 1 118 ? 14.713 -11.106 14.976  1.00 9.42  ? 118 VAL A CG2 1 
ATOM   919  N  N   . VAL A 1 119 ? 11.333 -11.165 18.174  1.00 7.53  ? 119 VAL A N   1 
ATOM   920  C  CA  . VAL A 1 119 ? 10.461 -11.932 19.060  1.00 7.24  ? 119 VAL A CA  1 
ATOM   921  C  C   . VAL A 1 119 ? 9.727  -12.991 18.229  1.00 8.53  ? 119 VAL A C   1 
ATOM   922  O  O   . VAL A 1 119 ? 9.211  -12.710 17.150  1.00 8.66  ? 119 VAL A O   1 
ATOM   923  C  CB  . VAL A 1 119 ? 9.496  -11.053 19.883  1.00 8.10  ? 119 VAL A CB  1 
ATOM   924  C  CG1 . VAL A 1 119 ? 8.565  -10.222 19.017  1.00 9.02  ? 119 VAL A CG1 1 
ATOM   925  C  CG2 . VAL A 1 119 ? 8.726  -11.905 20.893  1.00 7.92  ? 119 VAL A CG2 1 
ATOM   926  N  N   . HIS A 1 120 ? 9.711  -14.212 18.761  1.00 8.23  ? 120 HIS A N   1 
ATOM   927  C  CA  . HIS A 1 120 ? 9.279  -15.392 18.025  1.00 8.59  ? 120 HIS A CA  1 
ATOM   928  C  C   . HIS A 1 120 ? 7.892  -15.893 18.432  1.00 8.84  ? 120 HIS A C   1 
ATOM   929  O  O   . HIS A 1 120 ? 7.375  -15.572 19.498  1.00 9.98  ? 120 HIS A O   1 
ATOM   930  C  CB  . HIS A 1 120 ? 10.290 -16.506 18.235  1.00 8.71  ? 120 HIS A CB  1 
ATOM   931  C  CG  . HIS A 1 120 ? 11.492 -16.381 17.375  1.00 9.64  ? 120 HIS A CG  1 
ATOM   932  N  ND1 . HIS A 1 120 ? 11.542 -16.937 16.119  1.00 11.21 ? 120 HIS A ND1 1 
ATOM   933  C  CD2 . HIS A 1 120 ? 12.684 -15.772 17.575  1.00 9.69  ? 120 HIS A CD2 1 
ATOM   934  C  CE1 . HIS A 1 120 ? 12.708 -16.662 15.574  1.00 12.39 ? 120 HIS A CE1 1 
ATOM   935  N  NE2 . HIS A 1 120 ? 13.428 -15.971 16.438  1.00 11.26 ? 120 HIS A NE2 1 
ATOM   936  N  N   . GLU A 1 121 ? 7.325  -16.722 17.563  1.00 10.56 ? 121 GLU A N   1 
ATOM   937  C  CA  . GLU A 1 121 ? 5.991  -17.297 17.738  1.00 12.32 ? 121 GLU A CA  1 
ATOM   938  C  C   . GLU A 1 121 ? 5.907  -18.298 18.884  1.00 11.83 ? 121 GLU A C   1 
ATOM   939  O  O   . GLU A 1 121 ? 4.923  -18.303 19.620  1.00 12.70 ? 121 GLU A O   1 
ATOM   940  C  CB  . GLU A 1 121 ? 5.533  -17.980 16.440  1.00 16.54 ? 121 GLU A CB  1 
ATOM   941  C  CG  . GLU A 1 121 ? 4.098  -18.500 16.460  1.00 21.29 ? 121 GLU A CG  1 
ATOM   942  C  CD  . GLU A 1 121 ? 3.585  -18.938 15.097  1.00 31.44 ? 121 GLU A CD  1 
ATOM   943  O  OE1 . GLU A 1 121 ? 3.657  -18.140 14.140  1.00 36.46 ? 121 GLU A OE1 1 
ATOM   944  O  OE2 . GLU A 1 121 ? 3.094  -20.085 14.982  1.00 40.96 ? 121 GLU A OE2 1 
ATOM   945  N  N   . LYS A 1 122 ? 6.934  -19.136 19.014  1.00 11.93 ? 122 LYS A N   1 
ATOM   946  C  CA  . LYS A 1 122 ? 6.963  -20.220 19.988  1.00 12.19 ? 122 LYS A CA  1 
ATOM   947  C  C   . LYS A 1 122 ? 8.038  -19.973 21.010  1.00 10.40 ? 122 LYS A C   1 
ATOM   948  O  O   . LYS A 1 122 ? 8.835  -19.030 20.896  1.00 11.31 ? 122 LYS A O   1 
ATOM   949  C  CB  . LYS A 1 122 ? 7.209  -21.571 19.288  1.00 14.28 ? 122 LYS A CB  1 
ATOM   950  C  CG  . LYS A 1 122 ? 6.176  -21.922 18.227  1.00 17.74 ? 122 LYS A CG  1 
ATOM   951  C  CD  . LYS A 1 122 ? 6.313  -23.358 17.733  1.00 21.06 ? 122 LYS A CD  1 
ATOM   952  C  CE  . LYS A 1 122 ? 7.570  -23.590 16.915  1.00 22.78 ? 122 LYS A CE  1 
ATOM   953  N  NZ  . LYS A 1 122 ? 7.742  -25.011 16.502  1.00 27.54 ? 122 LYS A NZ  1 
ATOM   954  N  N   . ALA A 1 123 ? 8.060  -20.822 22.025  1.00 10.56 ? 123 ALA A N   1 
ATOM   955  C  CA  . ALA A 1 123 ? 9.078  -20.761 23.052  1.00 11.55 ? 123 ALA A CA  1 
ATOM   956  C  C   . ALA A 1 123 ? 10.410 -21.234 22.487  1.00 10.62 ? 123 ALA A C   1 
ATOM   957  O  O   . ALA A 1 123 ? 10.465 -22.158 21.661  1.00 12.71 ? 123 ALA A O   1 
ATOM   958  C  CB  . ALA A 1 123 ? 8.677  -21.617 24.244  1.00 12.32 ? 123 ALA A CB  1 
ATOM   959  N  N   . ASP A 1 124 ? 11.487 -20.584 22.904  1.00 10.72 ? 124 ASP A N   1 
ATOM   960  C  CA  . ASP A 1 124 ? 12.837 -21.077 22.697  1.00 9.34  ? 124 ASP A CA  1 
ATOM   961  C  C   . ASP A 1 124 ? 13.045 -22.186 23.724  1.00 10.15 ? 124 ASP A C   1 
ATOM   962  O  O   . ASP A 1 124 ? 12.885 -21.976 24.926  1.00 11.11 ? 124 ASP A O   1 
ATOM   963  C  CB  . ASP A 1 124 ? 13.803 -19.908 22.906  1.00 9.35  ? 124 ASP A CB  1 
ATOM   964  C  CG  . ASP A 1 124 ? 15.253 -20.226 22.613  1.00 10.12 ? 124 ASP A CG  1 
ATOM   965  O  OD1 . ASP A 1 124 ? 15.681 -21.399 22.678  1.00 10.67 ? 124 ASP A OD1 1 
ATOM   966  O  OD2 . ASP A 1 124 ? 16.002 -19.250 22.350  1.00 12.18 ? 124 ASP A OD2 1 
ATOM   967  N  N   . ASP A 1 125 ? 13.402 -23.373 23.234  1.00 9.87  ? 125 ASP A N   1 
ATOM   968  C  CA  . ASP A 1 125 ? 13.650 -24.508 24.127  1.00 10.33 ? 125 ASP A CA  1 
ATOM   969  C  C   . ASP A 1 125 ? 15.029 -24.469 24.805  1.00 10.34 ? 125 ASP A C   1 
ATOM   970  O  O   . ASP A 1 125 ? 15.380 -25.382 25.560  1.00 12.19 ? 125 ASP A O   1 
ATOM   971  C  CB  . ASP A 1 125 ? 13.372 -25.857 23.419  1.00 10.36 ? 125 ASP A CB  1 
ATOM   972  C  CG  . ASP A 1 125 ? 14.333 -26.173 22.283  1.00 12.12 ? 125 ASP A CG  1 
ATOM   973  O  OD1 . ASP A 1 125 ? 15.496 -25.708 22.299  1.00 12.29 ? 125 ASP A OD1 1 
ATOM   974  O  OD2 . ASP A 1 125 ? 13.919 -26.950 21.387  1.00 13.09 ? 125 ASP A OD2 1 
ATOM   975  N  N   . LEU A 1 126 ? 15.814 -23.426 24.516  1.00 11.31 ? 126 LEU A N   1 
ATOM   976  C  CA  . LEU A 1 126 ? 17.087 -23.156 25.179  1.00 13.27 ? 126 LEU A CA  1 
ATOM   977  C  C   . LEU A 1 126 ? 18.121 -24.256 24.961  1.00 12.61 ? 126 LEU A C   1 
ATOM   978  O  O   . LEU A 1 126 ? 19.016 -24.449 25.793  1.00 14.39 ? 126 LEU A O   1 
ATOM   979  C  CB  . LEU A 1 126 ? 16.877 -22.877 26.679  1.00 13.33 ? 126 LEU A CB  1 
ATOM   980  C  CG  . LEU A 1 126 ? 15.770 -21.873 27.012  1.00 12.10 ? 126 LEU A CG  1 
ATOM   981  C  CD1 . LEU A 1 126 ? 15.718 -21.644 28.512  1.00 14.76 ? 126 LEU A CD1 1 
ATOM   982  C  CD2 . LEU A 1 126 ? 15.952 -20.537 26.301  1.00 10.46 ? 126 LEU A CD2 1 
ATOM   983  N  N   . GLY A 1 127 ? 18.001 -24.962 23.832  1.00 10.85 ? 127 GLY A N   1 
ATOM   984  C  CA  . GLY A 1 127 ? 18.869 -26.107 23.529  1.00 11.29 ? 127 GLY A CA  1 
ATOM   985  C  C   . GLY A 1 127 ? 18.510 -27.410 24.225  1.00 12.80 ? 127 GLY A C   1 
ATOM   986  O  O   . GLY A 1 127 ? 19.302 -28.350 24.193  1.00 17.14 ? 127 GLY A O   1 
ATOM   987  N  N   . LYS A 1 128 ? 17.310 -27.485 24.798  1.00 12.34 ? 128 LYS A N   1 
ATOM   988  C  CA  . LYS A 1 128 ? 16.849 -28.661 25.547  1.00 15.19 ? 128 LYS A CA  1 
ATOM   989  C  C   . LYS A 1 128 ? 15.554 -29.222 24.941  1.00 14.42 ? 128 LYS A C   1 
ATOM   990  O  O   . LYS A 1 128 ? 14.629 -29.598 25.660  1.00 18.59 ? 128 LYS A O   1 
ATOM   991  C  CB  . LYS A 1 128 ? 16.615 -28.293 27.022  1.00 20.11 ? 128 LYS A CB  1 
ATOM   992  C  CG  . LYS A 1 128 ? 17.807 -27.644 27.712  1.00 23.74 ? 128 LYS A CG  1 
ATOM   993  C  CD  . LYS A 1 128 ? 18.899 -28.668 27.970  1.00 24.32 ? 128 LYS A CD  1 
ATOM   994  C  CE  . LYS A 1 128 ? 18.420 -29.816 28.958  0.00 14.26 ? 128 LYS A CE  1 
ATOM   995  N  NZ  . LYS A 1 128 ? 19.511 -30.723 29.372  0.00 14.62 ? 128 LYS A NZ  1 
ATOM   996  N  N   . GLY A 1 129 ? 15.510 -29.299 23.619  0.70 10.46 ? 129 GLY A N   1 
ATOM   997  C  CA  . GLY A 1 129 ? 14.323 -29.756 22.892  0.70 9.67  ? 129 GLY A CA  1 
ATOM   998  C  C   . GLY A 1 129 ? 14.378 -31.198 22.393  0.70 9.37  ? 129 GLY A C   1 
ATOM   999  O  O   . GLY A 1 129 ? 13.357 -31.755 22.002  0.70 11.95 ? 129 GLY A O   1 
ATOM   1000 N  N   . GLY A 1 130 ? 15.563 -31.793 22.381  0.70 9.31  ? 130 GLY A N   1 
ATOM   1001 C  CA  . GLY A 1 130 ? 15.718 -33.198 21.981  0.70 9.73  ? 130 GLY A CA  1 
ATOM   1002 C  C   . GLY A 1 130 ? 15.766 -33.456 20.480  0.70 11.10 ? 130 GLY A C   1 
ATOM   1003 O  O   . GLY A 1 130 ? 15.496 -34.572 20.040  0.70 11.63 ? 130 GLY A O   1 
ATOM   1004 N  N   . ASN A 1 131 ? 16.099 -32.434 19.681  1.00 14.17 ? 131 ASN A N   1 
ATOM   1005 C  CA  . ASN A 1 131 ? 16.402 -32.606 18.250  1.00 15.77 ? 131 ASN A CA  1 
ATOM   1006 C  C   . ASN A 1 131 ? 17.613 -31.744 17.864  1.00 15.52 ? 131 ASN A C   1 
ATOM   1007 O  O   . ASN A 1 131 ? 18.099 -30.955 18.673  1.00 16.58 ? 131 ASN A O   1 
ATOM   1008 C  CB  . ASN A 1 131 ? 15.156 -32.324 17.377  1.00 18.53 ? 131 ASN A CB  1 
ATOM   1009 C  CG  . ASN A 1 131 ? 14.728 -30.861 17.377  1.00 17.30 ? 131 ASN A CG  1 
ATOM   1010 O  OD1 . ASN A 1 131 ? 15.346 -30.031 18.006  1.00 16.81 ? 131 ASN A OD1 1 
ATOM   1011 N  ND2 . ASN A 1 131 ? 13.656 -30.551 16.654  1.00 19.94 ? 131 ASN A ND2 1 
ATOM   1012 N  N   . GLU A 1 132 ? 18.111 -31.905 16.643  1.00 16.50 ? 132 GLU A N   1 
ATOM   1013 C  CA  . GLU A 1 132 ? 19.300 -31.160 16.187  1.00 17.38 ? 132 GLU A CA  1 
ATOM   1014 C  C   . GLU A 1 132 ? 19.059 -29.660 16.133  1.00 16.44 ? 132 GLU A C   1 
ATOM   1015 O  O   . GLU A 1 132 ? 19.934 -28.866 16.504  1.00 18.75 ? 132 GLU A O   1 
ATOM   1016 C  CB  . GLU A 1 132 ? 19.746 -31.647 14.805  1.00 19.57 ? 132 GLU A CB  1 
ATOM   1017 C  CG  . GLU A 1 132 ? 20.909 -30.873 14.184  1.00 26.02 ? 132 GLU A CG  1 
ATOM   1018 C  CD  . GLU A 1 132 ? 22.201 -31.152 14.815  0.00 37.20 ? 132 GLU A CD  1 
ATOM   1019 O  OE1 . GLU A 1 132 ? 22.301 -32.072 15.682  0.00 39.51 ? 132 GLU A OE1 1 
ATOM   1020 O  OE2 . GLU A 1 132 ? 23.213 -30.460 14.456  0.00 42.83 ? 132 GLU A OE2 1 
ATOM   1021 N  N   . GLU A 1 133 ? 17.876 -29.277 15.664  1.00 16.37 ? 133 GLU A N   1 
ATOM   1022 C  CA  . GLU A 1 133 ? 17.509 -27.857 15.555  1.00 14.15 ? 133 GLU A CA  1 
ATOM   1023 C  C   . GLU A 1 133 ? 17.535 -27.145 16.908  1.00 13.25 ? 133 GLU A C   1 
ATOM   1024 O  O   . GLU A 1 133 ? 17.796 -25.948 16.968  1.00 14.74 ? 133 GLU A O   1 
ATOM   1025 C  CB  . GLU A 1 133 ? 16.114 -27.714 14.941  1.00 17.66 ? 133 GLU A CB  1 
ATOM   1026 C  CG  . GLU A 1 133 ? 16.044 -28.063 13.466  1.00 21.23 ? 133 GLU A CG  1 
ATOM   1027 C  CD  . GLU A 1 133 ? 14.677 -28.093 12.884  0.00 28.55 ? 133 GLU A CD  1 
ATOM   1028 O  OE1 . GLU A 1 133 ? 13.718 -27.879 13.655  0.00 36.42 ? 133 GLU A OE1 1 
ATOM   1029 O  OE2 . GLU A 1 133 ? 14.539 -28.242 11.652  0.00 43.22 ? 133 GLU A OE2 1 
ATOM   1030 N  N   . SER A 1 134 ? 17.281 -27.869 17.996  1.00 14.07 ? 134 SER A N   1 
ATOM   1031 C  CA  . SER A 1 134 ? 17.281 -27.267 19.327  1.00 12.54 ? 134 SER A CA  1 
ATOM   1032 C  C   . SER A 1 134 ? 18.594 -26.556 19.668  1.00 12.42 ? 134 SER A C   1 
ATOM   1033 O  O   . SER A 1 134 ? 18.563 -25.469 20.237  1.00 13.19 ? 134 SER A O   1 
ATOM   1034 C  CB  . SER A 1 134 ? 16.946 -28.321 20.387  1.00 12.58 ? 134 SER A CB  1 
ATOM   1035 O  OG  . SER A 1 134 ? 16.998 -27.770 21.679  1.00 13.59 ? 134 SER A OG  1 
ATOM   1036 N  N   . THR A 1 135 ? 19.740 -27.141 19.303  1.00 15.34 ? 135 THR A N   1 
ATOM   1037 C  CA  . THR A 1 135 ? 21.039 -26.519 19.608  1.00 15.97 ? 135 THR A CA  1 
ATOM   1038 C  C   . THR A 1 135 ? 21.559 -25.593 18.499  1.00 13.52 ? 135 THR A C   1 
ATOM   1039 O  O   . THR A 1 135 ? 22.715 -25.183 18.534  1.00 15.32 ? 135 THR A O   1 
ATOM   1040 C  CB  . THR A 1 135 ? 22.092 -27.562 19.983  1.00 19.04 ? 135 THR A CB  1 
ATOM   1041 O  OG1 . THR A 1 135 ? 22.188 -28.513 18.929  1.00 25.40 ? 135 THR A OG1 1 
ATOM   1042 C  CG2 . THR A 1 135 ? 21.712 -28.252 21.291  1.00 23.61 ? 135 THR A CG2 1 
ATOM   1043 N  N   . LYS A 1 136 ? 20.692 -25.242 17.553  1.00 13.22 ? 136 LYS A N   1 
ATOM   1044 C  CA  . LYS A 1 136 ? 20.970 -24.209 16.549  1.00 13.59 ? 136 LYS A CA  1 
ATOM   1045 C  C   . LYS A 1 136 ? 20.041 -23.008 16.714  1.00 13.95 ? 136 LYS A C   1 
ATOM   1046 O  O   . LYS A 1 136 ? 20.513 -21.884 16.804  1.00 16.55 ? 136 LYS A O   1 
ATOM   1047 C  CB  . LYS A 1 136 ? 20.844 -24.784 15.141  1.00 15.97 ? 136 LYS A CB  1 
ATOM   1048 C  CG  . LYS A 1 136 ? 21.915 -25.808 14.813  1.00 19.02 ? 136 LYS A CG  1 
ATOM   1049 C  CD  . LYS A 1 136 ? 22.213 -26.088 13.420  0.00 22.70 ? 136 LYS A CD  1 
ATOM   1050 C  CE  . LYS A 1 136 ? 23.325 -27.105 13.108  0.00 18.91 ? 136 LYS A CE  1 
ATOM   1051 N  NZ  . LYS A 1 136 ? 24.771 -26.628 13.287  0.00 16.20 ? 136 LYS A NZ  1 
ATOM   1052 N  N   . THR A 1 137 ? 18.730 -23.237 16.742  1.00 14.41 ? 137 THR A N   1 
ATOM   1053 C  CA  . THR A 1 137 ? 17.758 -22.146 16.826  1.00 15.08 ? 137 THR A CA  1 
ATOM   1054 C  C   . THR A 1 137 ? 16.881 -22.149 18.075  1.00 12.42 ? 137 THR A C   1 
ATOM   1055 O  O   . THR A 1 137 ? 16.228 -21.151 18.357  1.00 14.21 ? 137 THR A O   1 
ATOM   1056 C  CB  . THR A 1 137 ? 16.796 -22.161 15.629  1.00 15.31 ? 137 THR A CB  1 
ATOM   1057 O  OG1 . THR A 1 137 ? 15.923 -23.292 15.745  1.00 14.64 ? 137 THR A OG1 1 
ATOM   1058 C  CG2 . THR A 1 137 ? 17.553 -22.199 14.311  1.00 18.32 ? 137 THR A CG2 1 
ATOM   1059 N  N   . GLY A 1 138 ? 16.816 -23.265 18.802  1.00 11.49 ? 138 GLY A N   1 
ATOM   1060 C  CA  . GLY A 1 138 ? 15.881 -23.393 19.914  1.00 11.69 ? 138 GLY A CA  1 
ATOM   1061 C  C   . GLY A 1 138 ? 14.433 -23.652 19.531  1.00 10.45 ? 138 GLY A C   1 
ATOM   1062 O  O   . GLY A 1 138 ? 13.562 -23.633 20.390  1.00 10.85 ? 138 GLY A O   1 
ATOM   1063 N  N   . ASN A 1 139 ? 14.160 -23.894 18.252  1.00 11.77 ? 139 ASN A N   1 
ATOM   1064 C  CA  . ASN A 1 139 ? 12.816 -24.286 17.781  1.00 11.55 ? 139 ASN A CA  1 
ATOM   1065 C  C   . ASN A 1 139 ? 11.746 -23.253 18.114  1.00 11.28 ? 139 ASN A C   1 
ATOM   1066 O  O   . ASN A 1 139 ? 10.630 -23.610 18.433  1.00 11.94 ? 139 ASN A O   1 
ATOM   1067 C  CB  . ASN A 1 139 ? 12.405 -25.672 18.330  1.00 11.38 ? 139 ASN A CB  1 
ATOM   1068 C  CG  . ASN A 1 139 ? 13.225 -26.793 17.755  1.00 13.78 ? 139 ASN A CG  1 
ATOM   1069 O  OD1 . ASN A 1 139 ? 13.171 -27.056 16.559  1.00 17.74 ? 139 ASN A OD1 1 
ATOM   1070 N  ND2 . ASN A 1 139 ? 13.996 -27.454 18.600  1.00 14.20 ? 139 ASN A ND2 1 
ATOM   1071 N  N   . ALA A 1 140 ? 12.082 -21.967 18.017  1.00 11.09 ? 140 ALA A N   1 
ATOM   1072 C  CA  . ALA A 1 140 ? 11.134 -20.903 18.426  1.00 10.66 ? 140 ALA A CA  1 
ATOM   1073 C  C   . ALA A 1 140 ? 10.169 -20.453 17.325  1.00 10.96 ? 140 ALA A C   1 
ATOM   1074 O  O   . ALA A 1 140 ? 9.376  -19.547 17.538  1.00 11.98 ? 140 ALA A O   1 
ATOM   1075 C  CB  . ALA A 1 140 ? 11.871 -19.710 19.025  1.00 11.29 ? 140 ALA A CB  1 
ATOM   1076 N  N   . GLY A 1 141 ? 10.200 -21.094 16.163  1.00 12.15 ? 141 GLY A N   1 
ATOM   1077 C  CA  . GLY A 1 141 ? 9.201  -20.839 15.148  1.00 12.72 ? 141 GLY A CA  1 
ATOM   1078 C  C   . GLY A 1 141 ? 9.353  -19.494 14.466  1.00 12.43 ? 141 GLY A C   1 
ATOM   1079 O  O   . GLY A 1 141 ? 10.449 -18.897 14.440  1.00 14.11 ? 141 GLY A O   1 
ATOM   1080 N  N   A SER A 1 142 ? 8.227  -19.012 13.944  0.50 12.05 ? 142 SER A N   1 
ATOM   1081 N  N   B SER A 1 142 ? 8.246  -19.004 13.922  0.50 12.38 ? 142 SER A N   1 
ATOM   1082 C  CA  A SER A 1 142 ? 8.169  -17.825 13.095  0.50 12.18 ? 142 SER A CA  1 
ATOM   1083 C  CA  B SER A 1 142 ? 8.284  -17.846 13.041  0.50 12.67 ? 142 SER A CA  1 
ATOM   1084 C  C   A SER A 1 142 ? 8.667  -16.556 13.787  0.50 11.49 ? 142 SER A C   1 
ATOM   1085 C  C   B SER A 1 142 ? 8.673  -16.566 13.769  0.50 11.68 ? 142 SER A C   1 
ATOM   1086 O  O   A SER A 1 142 ? 8.608  -16.442 15.007  0.50 11.82 ? 142 SER A O   1 
ATOM   1087 O  O   B SER A 1 142 ? 8.549  -16.454 14.985  0.50 12.08 ? 142 SER A O   1 
ATOM   1088 C  CB  A SER A 1 142 ? 6.732  -17.619 12.615  0.50 14.22 ? 142 SER A CB  1 
ATOM   1089 C  CB  B SER A 1 142 ? 6.944  -17.670 12.335  0.50 15.93 ? 142 SER A CB  1 
ATOM   1090 O  OG  A SER A 1 142 ? 6.277  -18.718 11.836  0.50 16.42 ? 142 SER A OG  1 
ATOM   1091 O  OG  B SER A 1 142 ? 5.992  -17.074 13.188  0.50 17.82 ? 142 SER A OG  1 
ATOM   1092 N  N   . ARG A 1 143 ? 9.159  -15.610 12.987  1.00 10.99 ? 143 ARG A N   1 
ATOM   1093 C  CA  . ARG A 1 143 ? 9.603  -14.316 13.487  1.00 10.46 ? 143 ARG A CA  1 
ATOM   1094 C  C   . ARG A 1 143 ? 8.402  -13.388 13.434  1.00 10.48 ? 143 ARG A C   1 
ATOM   1095 O  O   . ARG A 1 143 ? 7.947  -13.031 12.351  1.00 13.90 ? 143 ARG A O   1 
ATOM   1096 C  CB  . ARG A 1 143 ? 10.731 -13.789 12.622  1.00 10.78 ? 143 ARG A CB  1 
ATOM   1097 C  CG  . ARG A 1 143 ? 11.924 -14.710 12.637  1.00 10.07 ? 143 ARG A CG  1 
ATOM   1098 C  CD  . ARG A 1 143 ? 13.078 -14.216 11.785  1.00 10.61 ? 143 ARG A CD  1 
ATOM   1099 N  NE  . ARG A 1 143 ? 14.134 -15.223 11.758  1.00 11.65 ? 143 ARG A NE  1 
ATOM   1100 C  CZ  . ARG A 1 143 ? 15.275 -15.131 11.102  1.00 11.04 ? 143 ARG A CZ  1 
ATOM   1101 N  NH1 . ARG A 1 143 ? 15.568 -14.044 10.409  1.00 14.67 ? 143 ARG A NH1 1 
ATOM   1102 N  NH2 . ARG A 1 143 ? 16.150 -16.124 11.155  1.00 12.13 ? 143 ARG A NH2 1 
ATOM   1103 N  N   . LEU A 1 144 ? 7.854  -13.030 14.592  1.00 9.42  ? 144 LEU A N   1 
ATOM   1104 C  CA  . LEU A 1 144 ? 6.603  -12.268 14.610  1.00 9.98  ? 144 LEU A CA  1 
ATOM   1105 C  C   . LEU A 1 144 ? 6.831  -10.770 14.488  1.00 9.35  ? 144 LEU A C   1 
ATOM   1106 O  O   . LEU A 1 144 ? 6.003  -10.054 13.904  1.00 10.89 ? 144 LEU A O   1 
ATOM   1107 C  CB  . LEU A 1 144 ? 5.770  -12.562 15.861  1.00 11.65 ? 144 LEU A CB  1 
ATOM   1108 C  CG  . LEU A 1 144 ? 5.293  -14.001 16.046  1.00 14.14 ? 144 LEU A CG  1 
ATOM   1109 C  CD1 . LEU A 1 144 ? 4.369  -14.077 17.247  1.00 17.50 ? 144 LEU A CD1 1 
ATOM   1110 C  CD2 . LEU A 1 144 ? 4.577  -14.512 14.808  1.00 18.95 ? 144 LEU A CD2 1 
ATOM   1111 N  N   . ALA A 1 145 ? 7.921  -10.288 15.073  1.00 8.96  ? 145 ALA A N   1 
ATOM   1112 C  CA  . ALA A 1 145 ? 8.254  -8.865  14.999  1.00 8.33  ? 145 ALA A CA  1 
ATOM   1113 C  C   . ALA A 1 145 ? 9.729  -8.683  15.247  1.00 8.09  ? 145 ALA A C   1 
ATOM   1114 O  O   . ALA A 1 145 ? 10.366 -9.501  15.900  1.00 8.75  ? 145 ALA A O   1 
ATOM   1115 C  CB  . ALA A 1 145 ? 7.438  -8.053  15.995  1.00 8.98  ? 145 ALA A CB  1 
ATOM   1116 N  N   . CYS A 1 146 ? 10.276 -7.627  14.667  1.00 8.66  ? 146 CYS A N   1 
ATOM   1117 C  CA  . CYS A 1 146 ? 11.693 -7.356  14.794  1.00 8.40  ? 146 CYS A CA  1 
ATOM   1118 C  C   . CYS A 1 146 ? 11.968 -5.891  14.553  1.00 8.10  ? 146 CYS A C   1 
ATOM   1119 O  O   . CYS A 1 146 ? 11.106 -5.136  14.089  1.00 9.18  ? 146 CYS A O   1 
ATOM   1120 C  CB  . CYS A 1 146 ? 12.482 -8.184  13.784  1.00 11.39 ? 146 CYS A CB  1 
ATOM   1121 S  SG  . CYS A 1 146 ? 12.028 -7.855  12.066  1.00 15.08 ? 146 CYS A SG  1 
ATOM   1122 N  N   . GLY A 1 147 ? 13.185 -5.500  14.895  1.00 7.99  ? 147 GLY A N   1 
ATOM   1123 C  CA  . GLY A 1 147 ? 13.669 -4.169  14.572  1.00 8.23  ? 147 GLY A CA  1 
ATOM   1124 C  C   . GLY A 1 147 ? 15.160 -4.082  14.730  1.00 7.33  ? 147 GLY A C   1 
ATOM   1125 O  O   . GLY A 1 147 ? 15.778 -4.948  15.333  1.00 8.56  ? 147 GLY A O   1 
ATOM   1126 N  N   . VAL A 1 148 ? 15.733 -3.024  14.178  1.00 8.14  ? 148 VAL A N   1 
ATOM   1127 C  CA  . VAL A 1 148 ? 17.159 -2.803  14.251  1.00 8.03  ? 148 VAL A CA  1 
ATOM   1128 C  C   . VAL A 1 148 ? 17.442 -2.104  15.579  1.00 7.34  ? 148 VAL A C   1 
ATOM   1129 O  O   . VAL A 1 148 ? 16.746 -1.162  15.965  1.00 9.98  ? 148 VAL A O   1 
ATOM   1130 C  CB  . VAL A 1 148 ? 17.652 -1.992  13.046  1.00 9.38  ? 148 VAL A CB  1 
ATOM   1131 C  CG1 . VAL A 1 148 ? 19.152 -1.821  13.107  1.00 10.16 ? 148 VAL A CG1 1 
ATOM   1132 C  CG2 . VAL A 1 148 ? 17.256 -2.693  11.749  1.00 10.21 ? 148 VAL A CG2 1 
ATOM   1133 N  N   . ILE A 1 149 ? 18.471 -2.558  16.275  1.00 7.22  ? 149 ILE A N   1 
ATOM   1134 C  CA  . ILE A 1 149 ? 18.838 -1.973  17.563  1.00 7.88  ? 149 ILE A CA  1 
ATOM   1135 C  C   . ILE A 1 149 ? 19.669 -0.713  17.274  1.00 8.40  ? 149 ILE A C   1 
ATOM   1136 O  O   . ILE A 1 149 ? 20.723 -0.785  16.645  1.00 9.30  ? 149 ILE A O   1 
ATOM   1137 C  CB  . ILE A 1 149 ? 19.621 -2.990  18.426  1.00 8.38  ? 149 ILE A CB  1 
ATOM   1138 C  CG1 . ILE A 1 149 ? 18.759 -4.228  18.716  1.00 8.23  ? 149 ILE A CG1 1 
ATOM   1139 C  CG2 . ILE A 1 149 ? 20.113 -2.346  19.721  1.00 8.78  ? 149 ILE A CG2 1 
ATOM   1140 C  CD1 . ILE A 1 149 ? 19.526 -5.384  19.325  1.00 9.34  ? 149 ILE A CD1 1 
ATOM   1141 N  N   . GLY A 1 150 ? 19.193 0.431   17.762  1.00 7.56  ? 150 GLY A N   1 
ATOM   1142 C  CA  . GLY A 1 150 ? 19.823 1.720   17.497  1.00 8.37  ? 150 GLY A CA  1 
ATOM   1143 C  C   . GLY A 1 150 ? 20.394 2.368   18.718  1.00 8.51  ? 150 GLY A C   1 
ATOM   1144 O  O   . GLY A 1 150 ? 19.995 2.063   19.831  1.00 9.72  ? 150 GLY A O   1 
ATOM   1145 N  N   . ILE A 1 151 ? 21.335 3.272   18.487  1.00 9.36  ? 151 ILE A N   1 
ATOM   1146 C  CA  . ILE A 1 151 ? 21.923 4.078   19.546  1.00 9.63  ? 151 ILE A CA  1 
ATOM   1147 C  C   . ILE A 1 151 ? 20.856 5.025   20.065  1.00 9.67  ? 151 ILE A C   1 
ATOM   1148 O  O   . ILE A 1 151 ? 20.187 5.705   19.280  1.00 10.95 ? 151 ILE A O   1 
ATOM   1149 C  CB  . ILE A 1 151 ? 23.116 4.907   19.022  1.00 11.38 ? 151 ILE A CB  1 
ATOM   1150 C  CG1 . ILE A 1 151 ? 24.266 3.987   18.627  1.00 12.49 ? 151 ILE A CG1 1 
ATOM   1151 C  CG2 . ILE A 1 151 ? 23.588 5.921   20.058  1.00 13.32 ? 151 ILE A CG2 1 
ATOM   1152 C  CD1 . ILE A 1 151 ? 25.308 4.650   17.755  1.00 13.62 ? 151 ILE A CD1 1 
ATOM   1153 N  N   . ALA A 1 152 ? 20.753 5.111   21.385  1.00 9.63  ? 152 ALA A N   1 
ATOM   1154 C  CA  . ALA A 1 152 ? 19.819 6.009   22.044  1.00 9.96  ? 152 ALA A CA  1 
ATOM   1155 C  C   . ALA A 1 152 ? 20.575 7.080   22.819  1.00 11.00 ? 152 ALA A C   1 
ATOM   1156 O  O   . ALA A 1 152 ? 21.751 6.940   23.161  1.00 12.07 ? 152 ALA A O   1 
ATOM   1157 C  CB  . ALA A 1 152 ? 18.890 5.223   22.963  1.00 9.85  ? 152 ALA A CB  1 
ATOM   1158 N  N   . GLN A 1 153 ? 19.866 8.154   23.112  1.00 12.58 ? 153 GLN A N   1 
ATOM   1159 C  CA  . GLN A 1 153 ? 20.444 9.273   23.830  1.00 15.36 ? 153 GLN A CA  1 
ATOM   1160 C  C   . GLN A 1 153 ? 20.741 8.925   25.279  1.00 19.60 ? 153 GLN A C   1 
ATOM   1161 O  O   . GLN A 1 153 ? 19.960 8.225   25.931  1.00 23.19 ? 153 GLN A O   1 
ATOM   1162 C  CB  . GLN A 1 153 ? 19.472 10.424  23.771  1.00 15.26 ? 153 GLN A CB  1 
ATOM   1163 C  CG  . GLN A 1 153 ? 19.936 11.706  24.408  1.00 15.94 ? 153 GLN A CG  1 
ATOM   1164 C  CD  . GLN A 1 153 ? 18.894 12.782  24.215  1.00 18.75 ? 153 GLN A CD  1 
ATOM   1165 O  OE1 . GLN A 1 153 ? 18.279 12.882  23.155  1.00 20.49 ? 153 GLN A OE1 1 
ATOM   1166 N  NE2 . GLN A 1 153 ? 18.676 13.578  25.236  1.00 18.89 ? 153 GLN A NE2 1 
ATOM   1167 O  OXT . GLN A 1 153 ? 21.769 9.357   25.812  1.00 23.76 ? 153 GLN A OXT 1 
ATOM   1168 N  N   . ALA B 1 1   ? 35.601 -5.956  3.762   1.00 30.53 ? 1   ALA F N   1 
ATOM   1169 C  CA  . ALA B 1 1   ? 34.643 -4.824  3.604   1.00 27.34 ? 1   ALA F CA  1 
ATOM   1170 C  C   . ALA B 1 1   ? 33.528 -4.901  4.631   1.00 24.47 ? 1   ALA F C   1 
ATOM   1171 O  O   . ALA B 1 1   ? 33.163 -5.958  5.078   1.00 37.56 ? 1   ALA F O   1 
ATOM   1172 C  CB  . ALA B 1 1   ? 34.050 -4.804  2.202   1.00 36.21 ? 1   ALA F CB  1 
ATOM   1173 N  N   . THR B 1 2   ? 32.994 -3.742  4.973   1.00 22.32 ? 2   THR F N   1 
ATOM   1174 C  CA  . THR B 1 2   ? 31.854 -3.647  5.854   1.00 20.60 ? 2   THR F CA  1 
ATOM   1175 C  C   . THR B 1 2   ? 30.690 -3.149  5.009   1.00 14.26 ? 2   THR F C   1 
ATOM   1176 O  O   . THR B 1 2   ? 30.866 -2.325  4.108   1.00 15.31 ? 2   THR F O   1 
ATOM   1177 C  CB  . THR B 1 2   ? 32.150 -2.698  7.026   1.00 23.37 ? 2   THR F CB  1 
ATOM   1178 O  OG1 . THR B 1 2   ? 33.335 -3.140  7.698   1.00 25.84 ? 2   THR F OG1 1 
ATOM   1179 C  CG2 . THR B 1 2   ? 31.000 -2.666  8.030   1.00 21.67 ? 2   THR F CG2 1 
ATOM   1180 N  N   . LYS B 1 3   ? 29.506 -3.667  5.314   1.00 13.65 ? 3   LYS F N   1 
ATOM   1181 C  CA  . LYS B 1 3   ? 28.283 -3.313  4.627   1.00 13.12 ? 3   LYS F CA  1 
ATOM   1182 C  C   . LYS B 1 3   ? 27.214 -2.976  5.636   1.00 11.68 ? 3   LYS F C   1 
ATOM   1183 O  O   . LYS B 1 3   ? 27.136 -3.590  6.703   1.00 13.18 ? 3   LYS F O   1 
ATOM   1184 C  CB  . LYS B 1 3   ? 27.814 -4.474  3.756   1.00 15.78 ? 3   LYS F CB  1 
ATOM   1185 C  CG  . LYS B 1 3   ? 26.757 -4.097  2.734   1.00 20.80 ? 3   LYS F CG  1 
ATOM   1186 C  CD  . LYS B 1 3   ? 26.378 -5.472  2.062   0.00 14.10 ? 3   LYS F CD  1 
ATOM   1187 C  CE  . LYS B 1 3   ? 25.025 -5.482  1.495   0.00 11.76 ? 3   LYS F CE  1 
ATOM   1188 N  NZ  . LYS B 1 3   ? 24.769 -6.770  0.760   0.00 15.60 ? 3   LYS F NZ  1 
ATOM   1189 N  N   . ALA B 1 4   ? 26.365 -2.028  5.286   1.00 12.26 ? 4   ALA F N   1 
ATOM   1190 C  CA  . ALA B 1 4   ? 25.228 -1.683  6.111   1.00 11.20 ? 4   ALA F CA  1 
ATOM   1191 C  C   . ALA B 1 4   ? 24.038 -1.443  5.213   1.00 11.01 ? 4   ALA F C   1 
ATOM   1192 O  O   . ALA B 1 4   ? 24.185 -1.333  3.990   1.00 12.46 ? 4   ALA F O   1 
ATOM   1193 C  CB  . ALA B 1 4   ? 25.525 -0.469  6.995   1.00 11.62 ? 4   ALA F CB  1 
ATOM   1194 N  N   . VAL B 1 5   ? 22.862 -1.392  5.813   1.00 11.12 ? 5   VAL F N   1 
ATOM   1195 C  CA  . VAL B 1 5   ? 21.632 -1.215  5.063   1.00 12.02 ? 5   VAL F CA  1 
ATOM   1196 C  C   . VAL B 1 5   ? 20.608 -0.477  5.915   1.00 11.74 ? 5   VAL F C   1 
ATOM   1197 O  O   . VAL B 1 5   ? 20.682 -0.484  7.152   1.00 12.07 ? 5   VAL F O   1 
ATOM   1198 C  CB  . VAL B 1 5   ? 21.117 -2.586  4.566   1.00 13.09 ? 5   VAL F CB  1 
ATOM   1199 C  CG1 . VAL B 1 5   ? 20.686 -3.467  5.726   1.00 12.16 ? 5   VAL F CG1 1 
ATOM   1200 C  CG2 . VAL B 1 5   ? 20.008 -2.440  3.538   1.00 16.67 ? 5   VAL F CG2 1 
ATOM   1201 N  N   . CYS B 1 6   ? 19.671 0.180   5.244   1.00 12.66 ? 6   CYS F N   1 
ATOM   1202 C  CA  . CYS B 1 6   ? 18.643 0.942   5.903   1.00 12.49 ? 6   CYS F CA  1 
ATOM   1203 C  C   . CYS B 1 6   ? 17.360 0.883   5.090   1.00 11.96 ? 6   CYS F C   1 
ATOM   1204 O  O   . CYS B 1 6   ? 17.377 1.094   3.877   1.00 14.69 ? 6   CYS F O   1 
ATOM   1205 C  CB  . CYS B 1 6   ? 19.120 2.388   6.068   1.00 13.13 ? 6   CYS F CB  1 
ATOM   1206 S  SG  . CYS B 1 6   ? 17.962 3.421   6.962   1.00 14.91 ? 6   CYS F SG  1 
ATOM   1207 N  N   . VAL B 1 7   ? 16.253 0.594   5.760   1.00 11.89 ? 7   VAL F N   1 
ATOM   1208 C  CA  . VAL B 1 7   ? 14.924 0.656   5.160   1.00 13.33 ? 7   VAL F CA  1 
ATOM   1209 C  C   . VAL B 1 7   ? 14.295 1.950   5.614   1.00 13.45 ? 7   VAL F C   1 
ATOM   1210 O  O   . VAL B 1 7   ? 14.110 2.154   6.812   1.00 14.15 ? 7   VAL F O   1 
ATOM   1211 C  CB  . VAL B 1 7   ? 14.021 -0.492  5.638   1.00 14.95 ? 7   VAL F CB  1 
ATOM   1212 C  CG1 . VAL B 1 7   ? 12.631 -0.394  5.018   1.00 17.88 ? 7   VAL F CG1 1 
ATOM   1213 C  CG2 . VAL B 1 7   ? 14.650 -1.811  5.286   1.00 15.91 ? 7   VAL F CG2 1 
ATOM   1214 N  N   . LEU B 1 8   ? 13.954 2.801   4.658   1.00 13.21 ? 8   LEU F N   1 
ATOM   1215 C  CA  . LEU B 1 8   ? 13.317 4.082   4.942   1.00 12.79 ? 8   LEU F CA  1 
ATOM   1216 C  C   . LEU B 1 8   ? 11.825 3.920   4.832   1.00 13.36 ? 8   LEU F C   1 
ATOM   1217 O  O   . LEU B 1 8   ? 11.331 3.440   3.808   1.00 16.46 ? 8   LEU F O   1 
ATOM   1218 C  CB  . LEU B 1 8   ? 13.778 5.146   3.947   1.00 13.33 ? 8   LEU F CB  1 
ATOM   1219 C  CG  . LEU B 1 8   ? 15.258 5.508   3.949   1.00 15.20 ? 8   LEU F CG  1 
ATOM   1220 C  CD1 . LEU B 1 8   ? 15.592 6.405   2.759   1.00 16.23 ? 8   LEU F CD1 1 
ATOM   1221 C  CD2 . LEU B 1 8   ? 15.645 6.206   5.239   1.00 17.32 ? 8   LEU F CD2 1 
ATOM   1222 N  N   . LYS B 1 9   ? 11.117 4.284   5.895   1.00 14.10 ? 9   LYS F N   1 
ATOM   1223 C  CA  . LYS B 1 9   ? 9.661  4.223   5.915   1.00 15.73 ? 9   LYS F CA  1 
ATOM   1224 C  C   . LYS B 1 9   ? 9.119  5.511   6.489   1.00 16.85 ? 9   LYS F C   1 
ATOM   1225 O  O   . LYS B 1 9   ? 9.703  6.093   7.411   1.00 16.10 ? 9   LYS F O   1 
ATOM   1226 C  CB  . LYS B 1 9   ? 9.151  3.016   6.708   1.00 16.71 ? 9   LYS F CB  1 
ATOM   1227 C  CG  . LYS B 1 9   ? 9.450  1.687   6.027   1.00 19.87 ? 9   LYS F CG  1 
ATOM   1228 C  CD  . LYS B 1 9   ? 8.681  0.513   6.622   1.00 24.17 ? 9   LYS F CD  1 
ATOM   1229 C  CE  . LYS B 1 9   ? 8.758  -0.721  5.729   1.00 29.04 ? 9   LYS F CE  1 
ATOM   1230 N  NZ  . LYS B 1 9   ? 7.972  -0.591  4.468   0.10 31.11 ? 9   LYS F NZ  1 
ATOM   1231 N  N   . GLY B 1 10  ? 7.988  5.909   5.915   0.80 19.22 ? 10  GLY F N   1 
ATOM   1232 C  CA  . GLY B 1 10  ? 7.371  7.195   6.125   0.80 19.93 ? 10  GLY F CA  1 
ATOM   1233 C  C   . GLY B 1 10  ? 6.123  7.314   5.264   0.80 20.36 ? 10  GLY F C   1 
ATOM   1234 O  O   . GLY B 1 10  ? 5.959  6.587   4.271   0.80 19.94 ? 10  GLY F O   1 
ATOM   1235 N  N   . ASP B 1 11  ? 5.241  8.229   5.645   1.00 21.51 ? 11  ASP F N   1 
ATOM   1236 C  CA  . ASP B 1 11  ? 3.919  8.348   5.023   1.00 22.02 ? 11  ASP F CA  1 
ATOM   1237 C  C   . ASP B 1 11  ? 4.036  8.760   3.560   1.00 21.82 ? 11  ASP F C   1 
ATOM   1238 O  O   . ASP B 1 11  ? 4.878  9.595   3.203   1.00 24.92 ? 11  ASP F O   1 
ATOM   1239 C  CB  . ASP B 1 11  ? 3.055  9.350   5.791   1.00 24.03 ? 11  ASP F CB  1 
ATOM   1240 C  CG  . ASP B 1 11  ? 2.686  8.864   7.178   1.00 28.97 ? 11  ASP F CG  1 
ATOM   1241 O  OD1 . ASP B 1 11  ? 2.736  7.641   7.427   1.00 32.68 ? 11  ASP F OD1 1 
ATOM   1242 O  OD2 . ASP B 1 11  ? 2.341  9.715   8.027   1.00 35.13 ? 11  ASP F OD2 1 
ATOM   1243 N  N   . GLY B 1 12  ? 3.215  8.136   2.718   1.00 18.98 ? 12  GLY F N   1 
ATOM   1244 C  CA  . GLY B 1 12  ? 3.195  8.421   1.295   1.00 20.82 ? 12  GLY F CA  1 
ATOM   1245 C  C   . GLY B 1 12  ? 2.576  7.314   0.450   1.00 22.51 ? 12  GLY F C   1 
ATOM   1246 O  O   . GLY B 1 12  ? 1.573  7.558   -0.223  1.00 24.95 ? 12  GLY F O   1 
ATOM   1247 N  N   . PRO B 1 13  ? 3.133  6.098   0.459   1.00 23.22 ? 13  PRO F N   1 
ATOM   1248 C  CA  . PRO B 1 13  ? 4.316  5.727   1.231   1.00 21.41 ? 13  PRO F CA  1 
ATOM   1249 C  C   . PRO B 1 13  ? 5.574  6.323   0.623   1.00 21.18 ? 13  PRO F C   1 
ATOM   1250 O  O   . PRO B 1 13  ? 5.734  6.271   -0.587  1.00 23.75 ? 13  PRO F O   1 
ATOM   1251 C  CB  . PRO B 1 13  ? 4.356  4.193   1.095   1.00 25.52 ? 13  PRO F CB  1 
ATOM   1252 C  CG  . PRO B 1 13  ? 3.006  3.791   0.634   1.00 27.61 ? 13  PRO F CG  1 
ATOM   1253 C  CD  . PRO B 1 13  ? 2.543  4.928   -0.218  1.00 25.30 ? 13  PRO F CD  1 
ATOM   1254 N  N   . VAL B 1 14  ? 6.423  6.930   1.447   1.00 21.93 ? 14  VAL F N   1 
ATOM   1255 C  CA  . VAL B 1 14  ? 7.797  7.198   1.055   1.00 19.25 ? 14  VAL F CA  1 
ATOM   1256 C  C   . VAL B 1 14  ? 8.544  5.998   1.588   1.00 21.65 ? 14  VAL F C   1 
ATOM   1257 O  O   . VAL B 1 14  ? 8.544  5.730   2.798   1.00 26.41 ? 14  VAL F O   1 
ATOM   1258 C  CB  . VAL B 1 14  ? 8.359  8.518   1.611   1.00 18.50 ? 14  VAL F CB  1 
ATOM   1259 C  CG1 . VAL B 1 14  ? 9.861  8.620   1.358   1.00 18.82 ? 14  VAL F CG1 1 
ATOM   1260 C  CG2 . VAL B 1 14  ? 7.662  9.681   0.934   1.00 19.72 ? 14  VAL F CG2 1 
ATOM   1261 N  N   . GLN B 1 15  ? 9.124  5.242   0.670   1.00 20.14 ? 15  GLN F N   1 
ATOM   1262 C  CA  . GLN B 1 15  ? 9.773  3.991   1.005   1.00 22.76 ? 15  GLN F CA  1 
ATOM   1263 C  C   . GLN B 1 15  ? 11.045 3.925   0.243   1.00 18.58 ? 15  GLN F C   1 
ATOM   1264 O  O   . GLN B 1 15  ? 11.084 4.279   -0.935  1.00 21.35 ? 15  GLN F O   1 
ATOM   1265 C  CB  . GLN B 1 15  ? 8.917  2.800   0.604   1.00 27.01 ? 15  GLN F CB  1 
ATOM   1266 C  CG  . GLN B 1 15  ? 7.473  2.933   1.006   1.00 32.09 ? 15  GLN F CG  1 
ATOM   1267 C  CD  . GLN B 1 15  ? 6.741  1.610   0.983   1.00 40.26 ? 15  GLN F CD  1 
ATOM   1268 O  OE1 . GLN B 1 15  ? 6.765  0.896   -0.017  1.00 45.24 ? 15  GLN F OE1 1 
ATOM   1269 N  NE2 . GLN B 1 15  ? 6.083  1.277   2.089   1.00 45.85 ? 15  GLN F NE2 1 
ATOM   1270 N  N   . GLY B 1 16  ? 12.083 3.451   0.901   1.00 17.15 ? 16  GLY F N   1 
ATOM   1271 C  CA  . GLY B 1 16  ? 13.365 3.351   0.262   1.00 19.37 ? 16  GLY F CA  1 
ATOM   1272 C  C   . GLY B 1 16  ? 14.192 2.247   0.848   1.00 15.44 ? 16  GLY F C   1 
ATOM   1273 O  O   . GLY B 1 16  ? 13.918 1.769   1.954   1.00 17.36 ? 16  GLY F O   1 
ATOM   1274 N  N   . ILE B 1 17  ? 15.199 1.846   0.088   1.00 16.12 ? 17  ILE F N   1 
ATOM   1275 C  CA  . ILE B 1 17  ? 16.205 0.892   0.528   1.00 16.43 ? 17  ILE F CA  1 
ATOM   1276 C  C   . ILE B 1 17  ? 17.520 1.566   0.208   1.00 13.56 ? 17  ILE F C   1 
ATOM   1277 O  O   . ILE B 1 17  ? 17.738 1.957   -0.943  1.00 14.33 ? 17  ILE F O   1 
ATOM   1278 C  CB  . ILE B 1 17  ? 16.133 -0.441  -0.251  1.00 18.67 ? 17  ILE F CB  1 
ATOM   1279 C  CG1 . ILE B 1 17  ? 14.770 -1.121  -0.054  1.00 22.45 ? 17  ILE F CG1 1 
ATOM   1280 C  CG2 . ILE B 1 17  ? 17.292 -1.349  0.147   1.00 18.70 ? 17  ILE F CG2 1 
ATOM   1281 C  CD1 . ILE B 1 17  ? 14.524 -1.672  1.335   1.00 23.14 ? 17  ILE F CD1 1 
ATOM   1282 N  N   . ILE B 1 18  ? 18.379 1.714   1.211   1.00 12.85 ? 18  ILE F N   1 
ATOM   1283 C  CA  . ILE B 1 18  ? 19.689 2.330   1.026   1.00 12.87 ? 18  ILE F CA  1 
ATOM   1284 C  C   . ILE B 1 18  ? 20.766 1.404   1.560   1.00 12.67 ? 18  ILE F C   1 
ATOM   1285 O  O   . ILE B 1 18  ? 20.684 0.919   2.697   1.00 15.19 ? 18  ILE F O   1 
ATOM   1286 C  CB  . ILE B 1 18  ? 19.780 3.717   1.704   1.00 12.06 ? 18  ILE F CB  1 
ATOM   1287 C  CG1 . ILE B 1 18  ? 18.695 4.645   1.141   1.00 13.06 ? 18  ILE F CG1 1 
ATOM   1288 C  CG2 . ILE B 1 18  ? 21.177 4.300   1.544   1.00 13.15 ? 18  ILE F CG2 1 
ATOM   1289 C  CD1 . ILE B 1 18  ? 18.874 5.089   -0.300  1.00 12.99 ? 18  ILE F CD1 1 
ATOM   1290 N  N   . ASN B 1 19  ? 21.753 1.141   0.704   1.00 13.15 ? 19  ASN F N   1 
ATOM   1291 C  CA  . ASN B 1 19  ? 22.895 0.305   1.013   1.00 13.20 ? 19  ASN F CA  1 
ATOM   1292 C  C   . ASN B 1 19  ? 24.127 1.149   1.221   1.00 12.01 ? 19  ASN F C   1 
ATOM   1293 O  O   . ASN B 1 19  ? 24.292 2.191   0.571   1.00 13.16 ? 19  ASN F O   1 
ATOM   1294 C  CB  . ASN B 1 19  ? 23.156 -0.629  -0.156  1.00 13.87 ? 19  ASN F CB  1 
ATOM   1295 C  CG  . ASN B 1 19  ? 21.959 -1.478  -0.481  1.00 14.87 ? 19  ASN F CG  1 
ATOM   1296 O  OD1 . ASN B 1 19  ? 21.720 -2.476  0.182   1.00 17.46 ? 19  ASN F OD1 1 
ATOM   1297 N  ND2 . ASN B 1 19  ? 21.180 -1.070  -1.481  1.00 15.84 ? 19  ASN F ND2 1 
ATOM   1298 N  N   . PHE B 1 20  ? 25.003 0.691   2.101   1.00 11.86 ? 20  PHE F N   1 
ATOM   1299 C  CA  . PHE B 1 20  ? 26.279 1.325   2.383   1.00 13.43 ? 20  PHE F CA  1 
ATOM   1300 C  C   . PHE B 1 20  ? 27.356 0.267   2.260   1.00 13.29 ? 20  PHE F C   1 
ATOM   1301 O  O   . PHE B 1 20  ? 27.193 -0.856  2.758   1.00 15.13 ? 20  PHE F O   1 
ATOM   1302 C  CB  . PHE B 1 20  ? 26.336 1.900   3.801   1.00 12.50 ? 20  PHE F CB  1 
ATOM   1303 C  CG  . PHE B 1 20  ? 25.243 2.885   4.121   1.00 14.65 ? 20  PHE F CG  1 
ATOM   1304 C  CD1 . PHE B 1 20  ? 23.965 2.461   4.478   1.00 14.37 ? 20  PHE F CD1 1 
ATOM   1305 C  CD2 . PHE B 1 20  ? 25.503 4.259   4.081   1.00 14.47 ? 20  PHE F CD2 1 
ATOM   1306 C  CE1 . PHE B 1 20  ? 22.967 3.388   4.770   1.00 14.62 ? 20  PHE F CE1 1 
ATOM   1307 C  CE2 . PHE B 1 20  ? 24.511 5.174   4.379   1.00 15.98 ? 20  PHE F CE2 1 
ATOM   1308 C  CZ  . PHE B 1 20  ? 23.247 4.744   4.727   1.00 14.53 ? 20  PHE F CZ  1 
ATOM   1309 N  N   . GLU B 1 21  ? 28.459 0.607   1.612   1.00 14.19 ? 21  GLU F N   1 
ATOM   1310 C  CA  . GLU B 1 21  ? 29.595 -0.320  1.522   1.00 14.45 ? 21  GLU F CA  1 
ATOM   1311 C  C   . GLU B 1 21  ? 30.892 0.436   1.694   1.00 14.02 ? 21  GLU F C   1 
ATOM   1312 O  O   . GLU B 1 21  ? 31.096 1.463   1.060   1.00 14.89 ? 21  GLU F O   1 
ATOM   1313 C  CB  . GLU B 1 21  ? 29.609 -1.076  0.190   1.00 17.45 ? 21  GLU F CB  1 
ATOM   1314 C  CG  . GLU B 1 21  ? 30.665 -2.177  0.144   0.70 20.52 ? 21  GLU F CG  1 
ATOM   1315 C  CD  . GLU B 1 21  ? 30.553 -3.106  -1.058  0.70 27.54 ? 21  GLU F CD  1 
ATOM   1316 O  OE1 . GLU B 1 21  ? 29.633 -2.945  -1.889  0.50 29.19 ? 21  GLU F OE1 1 
ATOM   1317 O  OE2 . GLU B 1 21  ? 31.405 -4.010  -1.171  0.50 30.40 ? 21  GLU F OE2 1 
ATOM   1318 N  N   . GLN B 1 22  ? 31.775 -0.089  2.525   1.00 14.71 ? 22  GLN F N   1 
ATOM   1319 C  CA  . GLN B 1 22  ? 33.079 0.498   2.772   1.00 14.96 ? 22  GLN F CA  1 
ATOM   1320 C  C   . GLN B 1 22  ? 34.127 -0.606  2.657   1.00 15.73 ? 22  GLN F C   1 
ATOM   1321 O  O   . GLN B 1 22  ? 34.100 -1.578  3.406   1.00 19.74 ? 22  GLN F O   1 
ATOM   1322 C  CB  . GLN B 1 22  ? 33.091 1.133   4.150   1.00 14.39 ? 22  GLN F CB  1 
ATOM   1323 C  CG  . GLN B 1 22  ? 34.319 1.971   4.432   1.00 14.22 ? 22  GLN F CG  1 
ATOM   1324 C  CD  . GLN B 1 22  ? 34.283 2.590   5.815   1.00 14.53 ? 22  GLN F CD  1 
ATOM   1325 O  OE1 . GLN B 1 22  ? 33.700 2.025   6.738   1.00 17.66 ? 22  GLN F OE1 1 
ATOM   1326 N  NE2 . GLN B 1 22  ? 34.903 3.753   5.964   1.00 15.15 ? 22  GLN F NE2 1 
ATOM   1327 N  N   . LYS B 1 23  ? 35.038 -0.455  1.710   1.00 18.57 ? 23  LYS F N   1 
ATOM   1328 C  CA  . LYS B 1 23  ? 36.032 -1.493  1.417   1.00 19.97 ? 23  LYS F CA  1 
ATOM   1329 C  C   . LYS B 1 23  ? 37.146 -1.604  2.462   1.00 21.85 ? 23  LYS F C   1 
ATOM   1330 O  O   . LYS B 1 23  ? 37.628 -2.707  2.729   1.00 26.83 ? 23  LYS F O   1 
ATOM   1331 C  CB  . LYS B 1 23  ? 36.622 -1.269  0.030   1.00 20.56 ? 23  LYS F CB  1 
ATOM   1332 C  CG  . LYS B 1 23  ? 35.622 -1.512  -1.087  1.00 25.26 ? 23  LYS F CG  1 
ATOM   1333 C  CD  . LYS B 1 23  ? 34.917 -2.994  -1.036  0.00 27.62 ? 23  LYS F CD  1 
ATOM   1334 C  CE  . LYS B 1 23  ? 35.777 -4.085  -1.638  0.00 24.97 ? 23  LYS F CE  1 
ATOM   1335 N  NZ  . LYS B 1 23  ? 35.073 -5.392  -1.568  0.00 23.47 ? 23  LYS F NZ  1 
ATOM   1336 N  N   . GLU B 1 24  ? 37.573 -0.470  3.017   1.00 25.49 ? 24  GLU F N   1 
ATOM   1337 C  CA  . GLU B 1 24  ? 38.431 -0.443  4.216   1.00 29.84 ? 24  GLU F CA  1 
ATOM   1338 C  C   . GLU B 1 24  ? 38.034 0.713   5.108   1.00 23.57 ? 24  GLU F C   1 
ATOM   1339 O  O   . GLU B 1 24  ? 37.430 1.667   4.638   1.00 23.52 ? 24  GLU F O   1 
ATOM   1340 C  CB  . GLU B 1 24  ? 39.922 -0.338  3.869   1.00 29.38 ? 24  GLU F CB  1 
ATOM   1341 C  CG  . GLU B 1 24  ? 40.337 0.859   3.027   0.50 29.41 ? 24  GLU F CG  1 
ATOM   1342 C  CD  . GLU B 1 24  ? 40.059 0.664   1.556   0.50 30.95 ? 24  GLU F CD  1 
ATOM   1343 O  OE1 . GLU B 1 24  ? 40.701 -0.204  0.930   0.50 35.17 ? 24  GLU F OE1 1 
ATOM   1344 O  OE2 . GLU B 1 24  ? 39.194 1.386   1.029   0.50 34.97 ? 24  GLU F OE2 1 
ATOM   1345 N  N   . SER B 1 25  ? 38.409 0.643   6.382   0.70 26.21 ? 25  SER F N   1 
ATOM   1346 C  CA  . SER B 1 25  ? 38.051 1.682   7.362   0.70 26.75 ? 25  SER F CA  1 
ATOM   1347 C  C   . SER B 1 25  ? 38.537 3.073   6.967   0.70 23.35 ? 25  SER F C   1 
ATOM   1348 O  O   . SER B 1 25  ? 37.922 4.077   7.329   0.70 21.17 ? 25  SER F O   1 
ATOM   1349 C  CB  . SER B 1 25  ? 38.608 1.331   8.739   0.70 30.37 ? 25  SER F CB  1 
ATOM   1350 O  OG  . SER B 1 25  ? 40.021 1.259   8.699   0.70 32.05 ? 25  SER F OG  1 
ATOM   1351 N  N   . ASN B 1 26  ? 39.610 3.121   6.175   1.00 23.69 ? 26  ASN F N   1 
ATOM   1352 C  CA  . ASN B 1 26  ? 40.115 4.410   5.709   1.00 21.34 ? 26  ASN F CA  1 
ATOM   1353 C  C   . ASN B 1 26  ? 39.476 4.881   4.405   1.00 21.86 ? 26  ASN F C   1 
ATOM   1354 O  O   . ASN B 1 26  ? 39.949 5.835   3.779   1.00 25.71 ? 26  ASN F O   1 
ATOM   1355 C  CB  . ASN B 1 26  ? 41.628 4.330   5.523   1.00 24.85 ? 26  ASN F CB  1 
ATOM   1356 C  CG  . ASN B 1 26  ? 42.258 4.259   6.741   0.00 36.37 ? 26  ASN F CG  1 
ATOM   1357 O  OD1 . ASN B 1 26  ? 41.746 4.565   7.818   0.00 54.54 ? 26  ASN F OD1 1 
ATOM   1358 N  ND2 . ASN B 1 26  ? 43.502 3.806   6.642   0.00 40.68 ? 26  ASN F ND2 1 
ATOM   1359 N  N   . GLY B 1 27  ? 38.486 4.214   3.946   1.00 20.89 ? 27  GLY F N   1 
ATOM   1360 C  CA  . GLY B 1 27  ? 37.983 4.450   2.631   1.00 20.76 ? 27  GLY F CA  1 
ATOM   1361 C  C   . GLY B 1 27  ? 36.652 5.136   2.669   1.00 17.94 ? 27  GLY F C   1 
ATOM   1362 O  O   . GLY B 1 27  ? 35.992 5.199   3.719   1.00 16.09 ? 27  GLY F O   1 
ATOM   1363 N  N   . PRO B 1 28  ? 36.228 5.632   1.503   1.00 17.21 ? 28  PRO F N   1 
ATOM   1364 C  CA  . PRO B 1 28  ? 34.914 6.196   1.373   1.00 16.84 ? 28  PRO F CA  1 
ATOM   1365 C  C   . PRO B 1 28  ? 33.853 5.123   1.484   1.00 15.05 ? 28  PRO F C   1 
ATOM   1366 O  O   . PRO B 1 28  ? 34.120 3.912   1.318   1.00 17.38 ? 28  PRO F O   1 
ATOM   1367 C  CB  . PRO B 1 28  ? 34.926 6.783   -0.036  1.00 20.61 ? 28  PRO F CB  1 
ATOM   1368 C  CG  . PRO B 1 28  ? 35.833 5.887   -0.778  1.00 23.47 ? 28  PRO F CG  1 
ATOM   1369 C  CD  . PRO B 1 28  ? 36.912 5.551   0.201   1.00 20.55 ? 28  PRO F CD  1 
ATOM   1370 N  N   . VAL B 1 29  ? 32.648 5.586   1.740   1.00 14.94 ? 29  VAL F N   1 
ATOM   1371 C  CA  . VAL B 1 29  ? 31.493 4.732   1.815   1.00 15.34 ? 29  VAL F CA  1 
ATOM   1372 C  C   . VAL B 1 29  ? 30.675 4.995   0.562   1.00 14.62 ? 29  VAL F C   1 
ATOM   1373 O  O   . VAL B 1 29  ? 30.327 6.139   0.270   1.00 16.19 ? 29  VAL F O   1 
ATOM   1374 C  CB  . VAL B 1 29  ? 30.665 5.051   3.069   1.00 15.13 ? 29  VAL F CB  1 
ATOM   1375 C  CG1 . VAL B 1 29  ? 29.429 4.158   3.144   1.00 14.22 ? 29  VAL F CG1 1 
ATOM   1376 C  CG2 . VAL B 1 29  ? 31.517 4.874   4.322   1.00 16.17 ? 29  VAL F CG2 1 
ATOM   1377 N  N   A LYS B 1 30  ? 30.408 3.938   -0.202  0.50 14.71 ? 30  LYS F N   1 
ATOM   1378 N  N   B LYS B 1 30  ? 30.392 3.931   -0.183  0.50 14.34 ? 30  LYS F N   1 
ATOM   1379 C  CA  A LYS B 1 30  ? 29.464 3.996   -1.305  0.50 15.68 ? 30  LYS F CA  1 
ATOM   1380 C  CA  B LYS B 1 30  ? 29.474 3.968   -1.306  0.50 16.33 ? 30  LYS F CA  1 
ATOM   1381 C  C   A LYS B 1 30  ? 28.069 3.855   -0.710  0.50 12.33 ? 30  LYS F C   1 
ATOM   1382 C  C   B LYS B 1 30  ? 28.055 3.813   -0.756  0.50 12.39 ? 30  LYS F C   1 
ATOM   1383 O  O   A LYS B 1 30  ? 27.838 2.991   0.139   0.50 14.32 ? 30  LYS F O   1 
ATOM   1384 O  O   B LYS B 1 30  ? 27.789 2.882   0.009   0.50 14.65 ? 30  LYS F O   1 
ATOM   1385 C  CB  A LYS B 1 30  ? 29.733 2.871   -2.309  0.50 14.72 ? 30  LYS F CB  1 
ATOM   1386 C  CB  B LYS B 1 30  ? 29.812 2.820   -2.262  0.50 16.14 ? 30  LYS F CB  1 
ATOM   1387 C  CG  A LYS B 1 30  ? 30.880 2.983   -3.099  0.00 23.27 ? 30  LYS F CG  1 
ATOM   1388 C  CG  B LYS B 1 30  ? 29.110 2.883   -3.604  0.50 17.56 ? 30  LYS F CG  1 
ATOM   1389 C  CD  A LYS B 1 30  ? 31.144 1.768   -3.974  0.00 29.14 ? 30  LYS F CD  1 
ATOM   1390 C  CD  B LYS B 1 30  ? 29.417 1.798   -4.458  0.00 29.14 ? 30  LYS F CD  1 
ATOM   1391 C  CE  A LYS B 1 30  ? 32.363 1.979   -4.857  0.00 30.64 ? 30  LYS F CE  1 
ATOM   1392 C  CE  B LYS B 1 30  ? 28.685 1.995   -5.775  0.00 30.64 ? 30  LYS F CE  1 
ATOM   1393 N  NZ  A LYS B 1 30  ? 32.706 3.422   -4.996  0.00 38.99 ? 30  LYS F NZ  1 
ATOM   1394 N  NZ  B LYS B 1 30  ? 29.005 0.920   -6.754  0.00 38.99 ? 30  LYS F NZ  1 
ATOM   1395 N  N   . VAL B 1 31  ? 27.162 4.722   -1.148  1.00 16.03 ? 31  VAL F N   1 
ATOM   1396 C  CA  . VAL B 1 31  ? 25.783 4.752   -0.665  1.00 15.69 ? 31  VAL F CA  1 
ATOM   1397 C  C   . VAL B 1 31  ? 24.939 4.636   -1.911  1.00 13.84 ? 31  VAL F C   1 
ATOM   1398 O  O   . VAL B 1 31  ? 25.037 5.479   -2.793  1.00 17.46 ? 31  VAL F O   1 
ATOM   1399 C  CB  . VAL B 1 31  ? 25.447 6.087   0.036   1.00 15.49 ? 31  VAL F CB  1 
ATOM   1400 C  CG1 . VAL B 1 31  ? 24.026 6.073   0.589   1.00 16.88 ? 31  VAL F CG1 1 
ATOM   1401 C  CG2 . VAL B 1 31  ? 26.465 6.395   1.118   1.00 15.11 ? 31  VAL F CG2 1 
ATOM   1402 N  N   A TRP B 1 32  ? 24.112 3.603   -1.996  0.50 12.80 ? 32  TRP F N   1 
ATOM   1403 N  N   B TRP B 1 32  ? 24.125 3.588   -1.994  0.50 13.37 ? 32  TRP F N   1 
ATOM   1404 C  CA  A TRP B 1 32  ? 23.266 3.438   -3.171  0.50 14.39 ? 32  TRP F CA  1 
ATOM   1405 C  CA  B TRP B 1 32  ? 23.315 3.344   -3.189  0.50 14.37 ? 32  TRP F CA  1 
ATOM   1406 C  C   A TRP B 1 32  ? 21.966 2.746   -2.843  0.50 12.46 ? 32  TRP F C   1 
ATOM   1407 C  C   B TRP B 1 32  ? 21.973 2.717   -2.853  0.50 12.47 ? 32  TRP F C   1 
ATOM   1408 O  O   A TRP B 1 32  ? 21.880 1.970   -1.888  0.50 13.30 ? 32  TRP F O   1 
ATOM   1409 O  O   B TRP B 1 32  ? 21.864 1.955   -1.890  0.50 13.51 ? 32  TRP F O   1 
ATOM   1410 C  CB  A TRP B 1 32  ? 23.996 2.683   -4.284  0.50 13.85 ? 32  TRP F CB  1 
ATOM   1411 C  CB  B TRP B 1 32  ? 24.073 2.474   -4.202  0.50 14.18 ? 32  TRP F CB  1 
ATOM   1412 C  CG  A TRP B 1 32  ? 24.068 1.212   -4.070  0.50 15.40 ? 32  TRP F CG  1 
ATOM   1413 C  CG  B TRP B 1 32  ? 24.349 1.057   -3.763  0.50 16.01 ? 32  TRP F CG  1 
ATOM   1414 C  CD1 A TRP B 1 32  ? 23.286 0.254   -4.657  0.50 14.18 ? 32  TRP F CD1 1 
ATOM   1415 C  CD1 B TRP B 1 32  ? 25.464 0.597   -3.122  0.50 16.24 ? 32  TRP F CD1 1 
ATOM   1416 C  CD2 A TRP B 1 32  ? 24.975 0.519   -3.209  0.50 15.34 ? 32  TRP F CD2 1 
ATOM   1417 C  CD2 B TRP B 1 32  ? 23.507 -0.087  -3.972  0.50 16.67 ? 32  TRP F CD2 1 
ATOM   1418 N  NE1 A TRP B 1 32  ? 23.648 -0.992  -4.206  0.50 16.50 ? 32  TRP F NE1 1 
ATOM   1419 N  NE1 B TRP B 1 32  ? 25.363 -0.760  -2.908  0.50 17.17 ? 32  TRP F NE1 1 
ATOM   1420 C  CE2 A TRP B 1 32  ? 24.689 -0.859  -3.323  0.50 15.71 ? 32  TRP F CE2 1 
ATOM   1421 C  CE2 B TRP B 1 32  ? 24.169 -1.202  -3.414  0.50 16.03 ? 32  TRP F CE2 1 
ATOM   1422 C  CE3 A TRP B 1 32  ? 26.007 0.926   -2.357  0.50 17.67 ? 32  TRP F CE3 1 
ATOM   1423 C  CE3 B TRP B 1 32  ? 22.254 -0.274  -4.564  0.50 17.39 ? 32  TRP F CE3 1 
ATOM   1424 C  CZ2 A TRP B 1 32  ? 25.390 -1.827  -2.608  0.50 17.25 ? 32  TRP F CZ2 1 
ATOM   1425 C  CZ2 B TRP B 1 32  ? 23.621 -2.484  -3.433  0.50 15.78 ? 32  TRP F CZ2 1 
ATOM   1426 C  CZ3 A TRP B 1 32  ? 26.701 -0.036  -1.648  0.50 17.03 ? 32  TRP F CZ3 1 
ATOM   1427 C  CZ3 B TRP B 1 32  ? 21.712 -1.553  -4.582  0.50 16.36 ? 32  TRP F CZ3 1 
ATOM   1428 C  CH2 A TRP B 1 32  ? 26.392 -1.398  -1.780  0.50 17.49 ? 32  TRP F CH2 1 
ATOM   1429 C  CH2 B TRP B 1 32  ? 22.397 -2.638  -4.021  0.50 17.94 ? 32  TRP F CH2 1 
ATOM   1430 N  N   . GLY B 1 33  ? 20.959 3.024   -3.658  1.00 12.61 ? 33  GLY F N   1 
ATOM   1431 C  CA  . GLY B 1 33  ? 19.637 2.470   -3.458  1.00 15.41 ? 33  GLY F CA  1 
ATOM   1432 C  C   . GLY B 1 33  ? 18.588 3.263   -4.174  1.00 13.53 ? 33  GLY F C   1 
ATOM   1433 O  O   . GLY B 1 33  ? 18.875 3.950   -5.158  1.00 15.79 ? 33  GLY F O   1 
ATOM   1434 N  N   . SER B 1 34  ? 17.365 3.151   -3.685  1.00 14.86 ? 34  SER F N   1 
ATOM   1435 C  CA  . SER B 1 34  ? 16.217 3.765   -4.310  1.00 16.88 ? 34  SER F CA  1 
ATOM   1436 C  C   . SER B 1 34  ? 15.261 4.244   -3.252  1.00 15.67 ? 34  SER F C   1 
ATOM   1437 O  O   . SER B 1 34  ? 15.111 3.603   -2.217  1.00 17.51 ? 34  SER F O   1 
ATOM   1438 C  CB  . SER B 1 34  ? 15.505 2.768   -5.224  1.00 19.70 ? 34  SER F CB  1 
ATOM   1439 O  OG  . SER B 1 34  ? 14.483 3.431   -5.957  1.00 26.60 ? 34  SER F OG  1 
ATOM   1440 N  N   . ILE B 1 35  ? 14.629 5.383   -3.504  1.00 15.22 ? 35  ILE F N   1 
ATOM   1441 C  CA  . ILE B 1 35  ? 13.552 5.895   -2.653  1.00 15.20 ? 35  ILE F CA  1 
ATOM   1442 C  C   . ILE B 1 35  ? 12.409 6.268   -3.579  1.00 14.17 ? 35  ILE F C   1 
ATOM   1443 O  O   . ILE B 1 35  ? 12.631 6.945   -4.580  1.00 16.19 ? 35  ILE F O   1 
ATOM   1444 C  CB  . ILE B 1 35  ? 13.964 7.135   -1.831  1.00 13.93 ? 35  ILE F CB  1 
ATOM   1445 C  CG1 . ILE B 1 35  ? 15.270 6.880   -1.084  1.00 14.71 ? 35  ILE F CG1 1 
ATOM   1446 C  CG2 . ILE B 1 35  ? 12.849 7.526   -0.867  1.00 16.00 ? 35  ILE F CG2 1 
ATOM   1447 C  CD1 . ILE B 1 35  ? 15.877 8.113   -0.446  1.00 14.55 ? 35  ILE F CD1 1 
ATOM   1448 N  N   . LYS B 1 36  ? 11.198 5.838   -3.245  1.00 15.66 ? 36  LYS F N   1 
ATOM   1449 C  CA  . LYS B 1 36  ? 10.021 6.132   -4.044  1.00 16.54 ? 36  LYS F CA  1 
ATOM   1450 C  C   . LYS B 1 36  ? 8.995  6.897   -3.220  1.00 15.60 ? 36  LYS F C   1 
ATOM   1451 O  O   . LYS B 1 36  ? 9.076  6.958   -1.983  1.00 17.04 ? 36  LYS F O   1 
ATOM   1452 C  CB  . LYS B 1 36  ? 9.426  4.856   -4.652  1.00 19.48 ? 36  LYS F CB  1 
ATOM   1453 C  CG  . LYS B 1 36  ? 8.921  3.840   -3.642  1.00 22.89 ? 36  LYS F CG  1 
ATOM   1454 C  CD  . LYS B 1 36  ? 8.366  2.603   -4.328  1.00 27.22 ? 36  LYS F CD  1 
ATOM   1455 C  CE  . LYS B 1 36  ? 8.309  1.437   -3.451  0.00 36.87 ? 36  LYS F CE  1 
ATOM   1456 N  NZ  . LYS B 1 36  ? 8.007  0.186   -4.238  0.00 38.90 ? 36  LYS F NZ  1 
ATOM   1457 N  N   . GLY B 1 37  ? 8.036  7.480   -3.926  1.00 16.51 ? 37  GLY F N   1 
ATOM   1458 C  CA  . GLY B 1 37  ? 6.956  8.241   -3.318  1.00 18.29 ? 37  GLY F CA  1 
ATOM   1459 C  C   . GLY B 1 37  ? 7.298  9.685   -2.995  1.00 18.42 ? 37  GLY F C   1 
ATOM   1460 O  O   . GLY B 1 37  ? 6.564  10.335  -2.259  1.00 19.93 ? 37  GLY F O   1 
ATOM   1461 N  N   . LEU B 1 38  ? 8.399  10.191  -3.547  1.00 16.30 ? 38  LEU F N   1 
ATOM   1462 C  CA  . LEU B 1 38  ? 8.813  11.576  -3.325  1.00 16.30 ? 38  LEU F CA  1 
ATOM   1463 C  C   . LEU B 1 38  ? 8.207  12.521  -4.349  1.00 16.70 ? 38  LEU F C   1 
ATOM   1464 O  O   . LEU B 1 38  ? 7.850  12.113  -5.447  1.00 20.05 ? 38  LEU F O   1 
ATOM   1465 C  CB  . LEU B 1 38  ? 10.332 11.681  -3.408  1.00 17.10 ? 38  LEU F CB  1 
ATOM   1466 C  CG  . LEU B 1 38  ? 11.091 10.910  -2.329  1.00 17.22 ? 38  LEU F CG  1 
ATOM   1467 C  CD1 . LEU B 1 38  ? 12.540 10.739  -2.736  1.00 17.87 ? 38  LEU F CD1 1 
ATOM   1468 C  CD2 . LEU B 1 38  ? 10.982 11.623  -0.987  1.00 16.17 ? 38  LEU F CD2 1 
ATOM   1469 N  N   . THR B 1 39  ? 8.096  13.793  -3.985  1.00 18.25 ? 39  THR F N   1 
ATOM   1470 C  CA  . THR B 1 39  ? 7.819  14.835  -4.979  1.00 19.52 ? 39  THR F CA  1 
ATOM   1471 C  C   . THR B 1 39  ? 9.077  15.075  -5.808  1.00 18.26 ? 39  THR F C   1 
ATOM   1472 O  O   . THR B 1 39  ? 10.193 14.967  -5.303  1.00 17.75 ? 39  THR F O   1 
ATOM   1473 C  CB  . THR B 1 39  ? 7.363  16.150  -4.331  1.00 19.95 ? 39  THR F CB  1 
ATOM   1474 O  OG1 . THR B 1 39  ? 8.335  16.586  -3.377  1.00 20.80 ? 39  THR F OG1 1 
ATOM   1475 C  CG2 . THR B 1 39  ? 6.043  15.954  -3.634  1.00 20.01 ? 39  THR F CG2 1 
ATOM   1476 N  N   . GLU B 1 40  ? 8.889  15.393  -7.083  1.00 16.52 ? 40  GLU F N   1 
ATOM   1477 C  CA  . GLU B 1 40  ? 10.007 15.658  -7.981  1.00 17.92 ? 40  GLU F CA  1 
ATOM   1478 C  C   . GLU B 1 40  ? 10.860 16.793  -7.417  1.00 17.12 ? 40  GLU F C   1 
ATOM   1479 O  O   . GLU B 1 40  ? 10.327 17.804  -6.938  1.00 19.31 ? 40  GLU F O   1 
ATOM   1480 C  CB  . GLU B 1 40  ? 9.487  15.994  -9.384  1.00 19.02 ? 40  GLU F CB  1 
ATOM   1481 C  CG  . GLU B 1 40  ? 10.534 15.942  -10.488 1.00 19.09 ? 40  GLU F CG  1 
ATOM   1482 C  CD  . GLU B 1 40  ? 11.016 17.307  -10.921 1.00 21.15 ? 40  GLU F CD  1 
ATOM   1483 O  OE1 . GLU B 1 40  ? 11.111 18.207  -10.059 1.00 22.67 ? 40  GLU F OE1 1 
ATOM   1484 O  OE2 . GLU B 1 40  ? 11.305 17.471  -12.129 1.00 21.04 ? 40  GLU F OE2 1 
ATOM   1485 N  N   . GLY B 1 41  ? 12.175 16.600  -7.449  1.00 16.59 ? 41  GLY F N   1 
ATOM   1486 C  CA  . GLY B 1 41  ? 13.140 17.608  -7.032  1.00 16.93 ? 41  GLY F CA  1 
ATOM   1487 C  C   . GLY B 1 41  ? 14.097 17.109  -5.972  1.00 13.76 ? 41  GLY F C   1 
ATOM   1488 O  O   . GLY B 1 41  ? 14.306 15.909  -5.812  1.00 17.92 ? 41  GLY F O   1 
ATOM   1489 N  N   . LEU B 1 42  ? 14.666 18.049  -5.232  1.00 13.26 ? 42  LEU F N   1 
ATOM   1490 C  CA  . LEU B 1 42  ? 15.687 17.780  -4.244  1.00 13.00 ? 42  LEU F CA  1 
ATOM   1491 C  C   . LEU B 1 42  ? 15.092 17.541  -2.869  1.00 12.57 ? 42  LEU F C   1 
ATOM   1492 O  O   . LEU B 1 42  ? 14.188 18.262  -2.426  1.00 13.41 ? 42  LEU F O   1 
ATOM   1493 C  CB  . LEU B 1 42  ? 16.677 18.945  -4.188  1.00 13.68 ? 42  LEU F CB  1 
ATOM   1494 C  CG  . LEU B 1 42  ? 17.470 19.182  -5.482  1.00 14.25 ? 42  LEU F CG  1 
ATOM   1495 C  CD1 . LEU B 1 42  ? 18.336 20.419  -5.344  1.00 17.51 ? 42  LEU F CD1 1 
ATOM   1496 C  CD2 . LEU B 1 42  ? 18.339 17.987  -5.823  1.00 16.13 ? 42  LEU F CD2 1 
ATOM   1497 N  N   . HIS B 1 43  ? 15.622 16.530  -2.190  1.00 12.83 ? 43  HIS F N   1 
ATOM   1498 C  CA  . HIS B 1 43  ? 15.205 16.192  -0.836  1.00 11.96 ? 43  HIS F CA  1 
ATOM   1499 C  C   . HIS B 1 43  ? 16.427 16.001  0.044   1.00 10.91 ? 43  HIS F C   1 
ATOM   1500 O  O   . HIS B 1 43  ? 17.316 15.196  -0.273  1.00 12.18 ? 43  HIS F O   1 
ATOM   1501 C  CB  . HIS B 1 43  ? 14.381 14.907  -0.871  1.00 12.92 ? 43  HIS F CB  1 
ATOM   1502 C  CG  . HIS B 1 43  ? 13.067 15.080  -1.553  1.00 14.20 ? 43  HIS F CG  1 
ATOM   1503 N  ND1 . HIS B 1 43  ? 11.933 15.481  -0.884  1.00 16.60 ? 43  HIS F ND1 1 
ATOM   1504 C  CD2 . HIS B 1 43  ? 12.722 14.976  -2.855  1.00 14.87 ? 43  HIS F CD2 1 
ATOM   1505 C  CE1 . HIS B 1 43  ? 10.933 15.577  -1.741  1.00 17.58 ? 43  HIS F CE1 1 
ATOM   1506 N  NE2 . HIS B 1 43  ? 11.388 15.278  -2.946  1.00 16.96 ? 43  HIS F NE2 1 
ATOM   1507 N  N   . GLY B 1 44  ? 16.449 16.712  1.170   1.00 11.07 ? 44  GLY F N   1 
ATOM   1508 C  CA  . GLY B 1 44  ? 17.556 16.606  2.105   1.00 9.69  ? 44  GLY F CA  1 
ATOM   1509 C  C   . GLY B 1 44  ? 17.743 15.177  2.602   1.00 10.05 ? 44  GLY F C   1 
ATOM   1510 O  O   . GLY B 1 44  ? 16.773 14.447  2.808   1.00 11.26 ? 44  GLY F O   1 
ATOM   1511 N  N   . PHE B 1 45  ? 18.994 14.793  2.799   1.00 9.71  ? 45  PHE F N   1 
ATOM   1512 C  CA  . PHE B 1 45  ? 19.358 13.387  3.041   1.00 9.71  ? 45  PHE F CA  1 
ATOM   1513 C  C   . PHE B 1 45  ? 20.419 13.416  4.129   1.00 10.04 ? 45  PHE F C   1 
ATOM   1514 O  O   . PHE B 1 45  ? 21.538 13.843  3.895   1.00 10.84 ? 45  PHE F O   1 
ATOM   1515 C  CB  . PHE B 1 45  ? 19.887 12.810  1.724   1.00 9.50  ? 45  PHE F CB  1 
ATOM   1516 C  CG  . PHE B 1 45  ? 20.044 11.301  1.686   1.00 10.97 ? 45  PHE F CG  1 
ATOM   1517 C  CD1 . PHE B 1 45  ? 18.965 10.460  1.930   1.00 12.04 ? 45  PHE F CD1 1 
ATOM   1518 C  CD2 . PHE B 1 45  ? 21.250 10.734  1.291   1.00 12.49 ? 45  PHE F CD2 1 
ATOM   1519 C  CE1 . PHE B 1 45  ? 19.102 9.080   1.842   1.00 12.99 ? 45  PHE F CE1 1 
ATOM   1520 C  CE2 . PHE B 1 45  ? 21.389 9.352   1.175   1.00 12.46 ? 45  PHE F CE2 1 
ATOM   1521 C  CZ  . PHE B 1 45  ? 20.312 8.533   1.460   1.00 13.45 ? 45  PHE F CZ  1 
ATOM   1522 N  N   . HIS B 1 46  ? 20.050 12.968  5.327   1.00 9.32  ? 46  HIS F N   1 
ATOM   1523 C  CA  . HIS B 1 46  ? 20.885 13.165  6.513   1.00 9.42  ? 46  HIS F CA  1 
ATOM   1524 C  C   . HIS B 1 46  ? 20.983 11.911  7.361   1.00 8.53  ? 46  HIS F C   1 
ATOM   1525 O  O   . HIS B 1 46  ? 20.005 11.175  7.491   1.00 10.09 ? 46  HIS F O   1 
ATOM   1526 C  CB  . HIS B 1 46  ? 20.303 14.233  7.456   1.00 11.34 ? 46  HIS F CB  1 
ATOM   1527 C  CG  . HIS B 1 46  ? 20.028 15.554  6.818   1.00 13.29 ? 46  HIS F CG  1 
ATOM   1528 N  ND1 . HIS B 1 46  ? 18.944 16.341  7.168   1.00 14.77 ? 46  HIS F ND1 1 
ATOM   1529 C  CD2 . HIS B 1 46  ? 20.722 16.245  5.890   1.00 15.57 ? 46  HIS F CD2 1 
ATOM   1530 C  CE1 . HIS B 1 46  ? 18.977 17.447  6.446   1.00 20.55 ? 46  HIS F CE1 1 
ATOM   1531 N  NE2 . HIS B 1 46  ? 20.037 17.409  5.658   1.00 16.57 ? 46  HIS F NE2 1 
ATOM   1532 N  N   . VAL B 1 47  ? 22.141 11.722  7.987   1.00 8.57  ? 47  VAL F N   1 
ATOM   1533 C  CA  . VAL B 1 47  ? 22.267 10.805  9.124   1.00 8.70  ? 47  VAL F CA  1 
ATOM   1534 C  C   . VAL B 1 47  ? 22.048 11.637  10.384  1.00 9.05  ? 47  VAL F C   1 
ATOM   1535 O  O   . VAL B 1 47  ? 22.781 12.601  10.652  1.00 9.72  ? 47  VAL F O   1 
ATOM   1536 C  CB  . VAL B 1 47  ? 23.619 10.082  9.194   1.00 9.34  ? 47  VAL F CB  1 
ATOM   1537 C  CG1 . VAL B 1 47  ? 23.622 9.093   10.353  1.00 8.90  ? 47  VAL F CG1 1 
ATOM   1538 C  CG2 . VAL B 1 47  ? 23.896 9.333   7.898   1.00 10.06 ? 47  VAL F CG2 1 
ATOM   1539 N  N   . HIS B 1 48  ? 21.002 11.270  11.116  1.00 8.93  ? 48  HIS F N   1 
ATOM   1540 C  CA  . HIS B 1 48  ? 20.663 11.868  12.394  1.00 9.89  ? 48  HIS F CA  1 
ATOM   1541 C  C   . HIS B 1 48  ? 21.249 11.006  13.509  1.00 9.36  ? 48  HIS F C   1 
ATOM   1542 O  O   . HIS B 1 48  ? 21.509 9.820   13.317  1.00 11.81 ? 48  HIS F O   1 
ATOM   1543 C  CB  . HIS B 1 48  ? 19.145 12.016  12.485  1.00 11.10 ? 48  HIS F CB  1 
ATOM   1544 C  CG  . HIS B 1 48  ? 18.595 13.182  11.705  1.00 12.05 ? 48  HIS F CG  1 
ATOM   1545 N  ND1 . HIS B 1 48  ? 18.077 14.276  12.350  1.00 13.22 ? 48  HIS F ND1 1 
ATOM   1546 C  CD2 . HIS B 1 48  ? 18.465 13.441  10.374  1.00 12.74 ? 48  HIS F CD2 1 
ATOM   1547 C  CE1 . HIS B 1 48  ? 17.652 15.157  11.472  1.00 15.52 ? 48  HIS F CE1 1 
ATOM   1548 N  NE2 . HIS B 1 48  ? 17.872 14.686  10.265  1.00 14.16 ? 48  HIS F NE2 1 
ATOM   1549 N  N   . GLU B 1 49  ? 21.457 11.625  14.661  1.00 9.22  ? 49  GLU F N   1 
ATOM   1550 C  CA  . GLU B 1 49  ? 22.294 11.062  15.704  1.00 8.91  ? 49  GLU F CA  1 
ATOM   1551 C  C   . GLU B 1 49  ? 21.822 9.727   16.277  1.00 10.41 ? 49  GLU F C   1 
ATOM   1552 O  O   . GLU B 1 49  ? 22.641 8.818   16.472  1.00 11.58 ? 49  GLU F O   1 
ATOM   1553 C  CB  . GLU B 1 49  ? 22.454 12.048  16.841  1.00 9.22  ? 49  GLU F CB  1 
ATOM   1554 C  CG  . GLU B 1 49  ? 23.466 11.618  17.868  0.70 8.19  ? 49  GLU F CG  1 
ATOM   1555 C  CD  . GLU B 1 49  ? 23.606 12.603  18.996  0.70 8.20  ? 49  GLU F CD  1 
ATOM   1556 O  OE1 . GLU B 1 49  ? 22.912 13.648  18.963  0.70 9.39  ? 49  GLU F OE1 1 
ATOM   1557 O  OE2 . GLU B 1 49  ? 24.398 12.308  19.917  0.70 11.27 ? 49  GLU F OE2 1 
ATOM   1558 N  N   . PHE B 1 50  ? 20.535 9.616   16.576  1.00 9.48  ? 50  PHE F N   1 
ATOM   1559 C  CA  . PHE B 1 50  ? 20.050 8.455   17.337  1.00 9.26  ? 50  PHE F CA  1 
ATOM   1560 C  C   . PHE B 1 50  ? 19.340 7.494   16.424  1.00 10.04 ? 50  PHE F C   1 
ATOM   1561 O  O   . PHE B 1 50  ? 18.539 7.914   15.593  1.00 11.60 ? 50  PHE F O   1 
ATOM   1562 C  CB  . PHE B 1 50  ? 19.086 8.895   18.446  1.00 10.46 ? 50  PHE F CB  1 
ATOM   1563 C  CG  . PHE B 1 50  ? 19.644 9.958   19.336  1.00 11.81 ? 50  PHE F CG  1 
ATOM   1564 C  CD1 . PHE B 1 50  ? 20.853 9.767   19.987  1.00 12.91 ? 50  PHE F CD1 1 
ATOM   1565 C  CD2 . PHE B 1 50  ? 18.980 11.170  19.501  1.00 12.82 ? 50  PHE F CD2 1 
ATOM   1566 C  CE1 . PHE B 1 50  ? 21.396 10.771  20.789  1.00 14.23 ? 50  PHE F CE1 1 
ATOM   1567 C  CE2 . PHE B 1 50  ? 19.512 12.169  20.306  1.00 15.79 ? 50  PHE F CE2 1 
ATOM   1568 C  CZ  . PHE B 1 50  ? 20.728 11.974  20.941  1.00 15.22 ? 50  PHE F CZ  1 
ATOM   1569 N  N   . GLY B 1 51  ? 19.580 6.200   16.631  1.00 9.67  ? 51  GLY F N   1 
ATOM   1570 C  CA  . GLY B 1 51  ? 18.811 5.156   15.950  1.00 10.44 ? 51  GLY F CA  1 
ATOM   1571 C  C   . GLY B 1 51  ? 17.554 4.846   16.725  1.00 11.23 ? 51  GLY F C   1 
ATOM   1572 O  O   . GLY B 1 51  ? 17.252 3.684   17.001  1.00 11.83 ? 51  GLY F O   1 
ATOM   1573 N  N   . ASP B 1 52  ? 16.829 5.891   17.102  1.00 13.14 ? 52  ASP F N   1 
ATOM   1574 C  CA  . ASP B 1 52  ? 15.681 5.793   17.965  1.00 12.95 ? 52  ASP F CA  1 
ATOM   1575 C  C   . ASP B 1 52  ? 14.504 6.195   17.119  1.00 12.12 ? 52  ASP F C   1 
ATOM   1576 O  O   . ASP B 1 52  ? 14.367 7.363   16.762  1.00 13.58 ? 52  ASP F O   1 
ATOM   1577 C  CB  . ASP B 1 52  ? 15.850 6.712   19.175  1.00 12.80 ? 52  ASP F CB  1 
ATOM   1578 C  CG  . ASP B 1 52  ? 14.705 6.612   20.145  1.00 14.09 ? 52  ASP F CG  1 
ATOM   1579 O  OD1 . ASP B 1 52  ? 13.610 6.168   19.730  1.00 14.45 ? 52  ASP F OD1 1 
ATOM   1580 O  OD2 . ASP B 1 52  ? 14.898 6.997   21.320  1.00 17.31 ? 52  ASP F OD2 1 
ATOM   1581 N  N   . ASN B 1 53  ? 13.675 5.225   16.757  1.00 12.24 ? 53  ASN F N   1 
ATOM   1582 C  CA  . ASN B 1 53  ? 12.507 5.480   15.923  1.00 15.75 ? 53  ASN F CA  1 
ATOM   1583 C  C   . ASN B 1 53  ? 11.233 5.124   16.700  1.00 13.88 ? 53  ASN F C   1 
ATOM   1584 O  O   . ASN B 1 53  ? 10.189 4.846   16.118  1.00 14.50 ? 53  ASN F O   1 
ATOM   1585 C  CB  . ASN B 1 53  ? 12.633 4.757   14.570  1.00 17.89 ? 53  ASN F CB  1 
ATOM   1586 C  CG  . ASN B 1 53  ? 13.717 5.368   13.648  1.00 19.11 ? 53  ASN F CG  1 
ATOM   1587 O  OD1 . ASN B 1 53  ? 14.276 6.458   13.892  1.00 22.07 ? 53  ASN F OD1 1 
ATOM   1588 N  ND2 . ASN B 1 53  ? 14.011 4.656   12.567  1.00 21.81 ? 53  ASN F ND2 1 
ATOM   1589 N  N   . THR B 1 54  ? 11.311 5.215   18.029  1.00 13.24 ? 54  THR F N   1 
ATOM   1590 C  CA  . THR B 1 54  ? 10.181 4.868   18.882  1.00 15.80 ? 54  THR F CA  1 
ATOM   1591 C  C   . THR B 1 54  ? 8.980  5.772   18.674  1.00 15.96 ? 54  THR F C   1 
ATOM   1592 O  O   . THR B 1 54  ? 7.844  5.314   18.795  1.00 16.46 ? 54  THR F O   1 
ATOM   1593 C  CB  . THR B 1 54  ? 10.560 4.851   20.368  1.00 16.99 ? 54  THR F CB  1 
ATOM   1594 O  OG1 . THR B 1 54  ? 11.128 6.106   20.740  1.00 17.16 ? 54  THR F OG1 1 
ATOM   1595 C  CG2 . THR B 1 54  ? 11.564 3.741   20.661  1.00 18.57 ? 54  THR F CG2 1 
ATOM   1596 N  N   . ALA B 1 55  ? 9.220  7.043   18.349  1.00 16.25 ? 55  ALA F N   1 
ATOM   1597 C  CA  . ALA B 1 55  ? 8.123  7.935   17.974  1.00 18.37 ? 55  ALA F CA  1 
ATOM   1598 C  C   . ALA B 1 55  ? 8.229  8.332   16.509  1.00 20.30 ? 55  ALA F C   1 
ATOM   1599 O  O   . ALA B 1 55  ? 7.873  9.445   16.132  1.00 25.92 ? 55  ALA F O   1 
ATOM   1600 C  CB  . ALA B 1 55  ? 8.092  9.156   18.878  1.00 20.01 ? 55  ALA F CB  1 
ATOM   1601 N  N   . GLY B 1 56  ? 8.675  7.403   15.673  1.00 20.34 ? 56  GLY F N   1 
ATOM   1602 C  CA  . GLY B 1 56  ? 8.947  7.698   14.279  1.00 20.70 ? 56  GLY F CA  1 
ATOM   1603 C  C   . GLY B 1 56  ? 10.221 8.503   14.143  1.00 18.99 ? 56  GLY F C   1 
ATOM   1604 O  O   . GLY B 1 56  ? 11.115 8.448   14.998  1.00 20.69 ? 56  GLY F O   1 
ATOM   1605 N  N   . CYS B 1 57  ? 10.289 9.296   13.085  1.00 15.61 ? 57  CYS F N   1 
ATOM   1606 C  CA  . CYS B 1 57  ? 11.526 9.994   12.754  1.00 15.42 ? 57  CYS F CA  1 
ATOM   1607 C  C   . CYS B 1 57  ? 11.915 11.112  13.710  1.00 16.69 ? 57  CYS F C   1 
ATOM   1608 O  O   . CYS B 1 57  ? 13.083 11.510  13.766  1.00 19.24 ? 57  CYS F O   1 
ATOM   1609 C  CB  . CYS B 1 57  ? 11.446 10.532  11.337  1.00 16.17 ? 57  CYS F CB  1 
ATOM   1610 S  SG  . CYS B 1 57  ? 11.063 9.233   10.138  1.00 20.44 ? 57  CYS F SG  1 
ATOM   1611 N  N   . THR B 1 58  ? 10.964 11.614  14.442  1.00 17.20 ? 58  THR F N   1 
ATOM   1612 C  CA  . THR B 1 58  ? 11.238 12.711  15.375  1.00 19.70 ? 58  THR F CA  1 
ATOM   1613 C  C   . THR B 1 58  ? 12.188 12.335  16.517  1.00 17.28 ? 58  THR F C   1 
ATOM   1614 O  O   . THR B 1 58  ? 12.932 13.170  17.000  1.00 23.72 ? 58  THR F O   1 
ATOM   1615 C  CB  . THR B 1 58  ? 9.934  13.312  15.931  1.00 26.13 ? 58  THR F CB  1 
ATOM   1616 O  OG1 . THR B 1 58  ? 10.224 14.496  16.682  1.00 34.70 ? 58  THR F OG1 1 
ATOM   1617 C  CG2 . THR B 1 58  ? 9.197  12.333  16.822  1.00 25.23 ? 58  THR F CG2 1 
ATOM   1618 N  N   A SER B 1 59  ? 12.139 11.091  16.961  0.50 15.60 ? 59  SER F N   1 
ATOM   1619 N  N   B SER B 1 59  ? 12.136 11.096  16.969  0.50 12.40 ? 59  SER F N   1 
ATOM   1620 C  CA  A SER B 1 59  ? 13.031 10.622  18.015  0.50 16.53 ? 59  SER F CA  1 
ATOM   1621 C  CA  B SER B 1 59  ? 13.031 10.647  18.023  0.50 13.24 ? 59  SER F CA  1 
ATOM   1622 C  C   A SER B 1 59  ? 14.502 10.522  17.608  0.50 13.46 ? 59  SER F C   1 
ATOM   1623 C  C   B SER B 1 59  ? 14.495 10.482  17.600  0.50 11.77 ? 59  SER F C   1 
ATOM   1624 O  O   A SER B 1 59  ? 15.351 10.303  18.469  0.50 13.88 ? 59  SER F O   1 
ATOM   1625 O  O   B SER B 1 59  ? 15.334 10.176  18.441  0.50 12.05 ? 59  SER F O   1 
ATOM   1626 C  CB  A SER B 1 59  ? 12.570 9.255   18.519  0.50 17.79 ? 59  SER F CB  1 
ATOM   1627 C  CB  B SER B 1 59  ? 12.508 9.347   18.638  0.50 10.34 ? 59  SER F CB  1 
ATOM   1628 O  OG  A SER B 1 59  ? 11.201 9.262   18.852  0.50 16.22 ? 59  SER F OG  1 
ATOM   1629 O  OG  B SER B 1 59  ? 11.935 8.492   17.666  0.50 9.78  ? 59  SER F OG  1 
ATOM   1630 N  N   . ALA B 1 60  ? 14.809 10.697  16.319  1.00 12.49 ? 60  ALA F N   1 
ATOM   1631 C  CA  . ALA B 1 60  ? 16.172 10.520  15.816  1.00 14.26 ? 60  ALA F CA  1 
ATOM   1632 C  C   . ALA B 1 60  ? 17.151 11.606  16.226  1.00 11.49 ? 60  ALA F C   1 
ATOM   1633 O  O   . ALA B 1 60  ? 18.354 11.432  16.089  1.00 12.38 ? 60  ALA F O   1 
ATOM   1634 C  CB  . ALA B 1 60  ? 16.161 10.383  14.302  1.00 15.06 ? 60  ALA F CB  1 
ATOM   1635 N  N   . GLY B 1 61  ? 16.651 12.724  16.740  1.00 10.06 ? 61  GLY F N   1 
ATOM   1636 C  CA  . GLY B 1 61  ? 17.533 13.768  17.208  1.00 9.54  ? 61  GLY F CA  1 
ATOM   1637 C  C   . GLY B 1 61  ? 18.116 14.597  16.089  1.00 10.18 ? 61  GLY F C   1 
ATOM   1638 O  O   . GLY B 1 61  ? 17.614 14.574  14.961  1.00 10.65 ? 61  GLY F O   1 
ATOM   1639 N  N   . PRO B 1 62  ? 19.177 15.350  16.408  1.00 9.87  ? 62  PRO F N   1 
ATOM   1640 C  CA  . PRO B 1 62  ? 19.756 16.265  15.451  1.00 9.64  ? 62  PRO F CA  1 
ATOM   1641 C  C   . PRO B 1 62  ? 20.664 15.588  14.442  1.00 9.79  ? 62  PRO F C   1 
ATOM   1642 O  O   . PRO B 1 62  ? 20.849 14.374  14.476  1.00 9.69  ? 62  PRO F O   1 
ATOM   1643 C  CB  . PRO B 1 62  ? 20.556 17.214  16.342  1.00 12.62 ? 62  PRO F CB  1 
ATOM   1644 C  CG  . PRO B 1 62  ? 20.997 16.363  17.463  1.00 13.01 ? 62  PRO F CG  1 
ATOM   1645 C  CD  . PRO B 1 62  ? 19.875 15.406  17.710  1.00 11.99 ? 62  PRO F CD  1 
ATOM   1646 N  N   . HIS B 1 63  ? 21.255 16.367  13.548  1.00 11.25 ? 63  HIS F N   1 
ATOM   1647 C  CA  . HIS B 1 63  ? 22.198 15.809  12.587  1.00 9.49  ? 63  HIS F CA  1 
ATOM   1648 C  C   . HIS B 1 63  ? 23.361 15.206  13.352  1.00 8.16  ? 63  HIS F C   1 
ATOM   1649 O  O   . HIS B 1 63  ? 23.804 15.760  14.352  1.00 9.38  ? 63  HIS F O   1 
ATOM   1650 C  CB  . HIS B 1 63  ? 22.740 16.885  11.637  1.00 10.86 ? 63  HIS F CB  1 
ATOM   1651 C  CG  . HIS B 1 63  ? 21.699 17.489  10.756  1.00 12.41 ? 63  HIS F CG  1 
ATOM   1652 N  ND1 . HIS B 1 63  ? 22.009 18.327  9.705   1.00 11.67 ? 63  HIS F ND1 1 
ATOM   1653 C  CD2 . HIS B 1 63  ? 20.349 17.399  10.781  1.00 14.21 ? 63  HIS F CD2 1 
ATOM   1654 C  CE1 . HIS B 1 63  ? 20.892 18.716  9.120   1.00 13.62 ? 63  HIS F CE1 1 
ATOM   1655 N  NE2 . HIS B 1 63  ? 19.870 18.174  9.756   1.00 16.19 ? 63  HIS F NE2 1 
ATOM   1656 N  N   . PHE B 1 64  ? 23.838 14.053  12.894  1.00 8.63  ? 64  PHE F N   1 
ATOM   1657 C  CA  . PHE B 1 64  ? 25.000 13.432  13.494  1.00 7.98  ? 64  PHE F CA  1 
ATOM   1658 C  C   . PHE B 1 64  ? 26.218 14.339  13.315  1.00 8.05  ? 64  PHE F C   1 
ATOM   1659 O  O   . PHE B 1 64  ? 26.641 14.588  12.185  1.00 8.69  ? 64  PHE F O   1 
ATOM   1660 C  CB  . PHE B 1 64  ? 25.226 12.046  12.881  1.00 8.87  ? 64  PHE F CB  1 
ATOM   1661 C  CG  . PHE B 1 64  ? 26.392 11.315  13.452  1.00 9.44  ? 64  PHE F CG  1 
ATOM   1662 C  CD1 . PHE B 1 64  ? 26.598 11.234  14.820  1.00 10.60 ? 64  PHE F CD1 1 
ATOM   1663 C  CD2 . PHE B 1 64  ? 27.265 10.653  12.610  1.00 9.66  ? 64  PHE F CD2 1 
ATOM   1664 C  CE1 . PHE B 1 64  ? 27.681 10.542  15.325  1.00 11.22 ? 64  PHE F CE1 1 
ATOM   1665 C  CE2 . PHE B 1 64  ? 28.342 9.948   13.112  1.00 10.66 ? 64  PHE F CE2 1 
ATOM   1666 C  CZ  . PHE B 1 64  ? 28.557 9.901   14.470  1.00 11.39 ? 64  PHE F CZ  1 
ATOM   1667 N  N   . ASN B 1 65  ? 26.755 14.821  14.439  1.00 8.37  ? 65  ASN F N   1 
ATOM   1668 C  CA  . ASN B 1 65  ? 27.772 15.872  14.432  1.00 8.65  ? 65  ASN F CA  1 
ATOM   1669 C  C   . ASN B 1 65  ? 28.833 15.618  15.493  1.00 8.56  ? 65  ASN F C   1 
ATOM   1670 O  O   . ASN B 1 65  ? 29.014 16.425  16.408  1.00 9.85  ? 65  ASN F O   1 
ATOM   1671 C  CB  . ASN B 1 65  ? 27.101 17.237  14.640  1.00 8.23  ? 65  ASN F CB  1 
ATOM   1672 C  CG  . ASN B 1 65  ? 28.074 18.406  14.503  1.00 8.97  ? 65  ASN F CG  1 
ATOM   1673 O  OD1 . ASN B 1 65  ? 29.124 18.311  13.850  1.00 8.98  ? 65  ASN F OD1 1 
ATOM   1674 N  ND2 . ASN B 1 65  ? 27.712 19.534  15.120  1.00 9.95  ? 65  ASN F ND2 1 
ATOM   1675 N  N   . PRO B 1 66  ? 29.565 14.509  15.360  1.00 8.61  ? 66  PRO F N   1 
ATOM   1676 C  CA  . PRO B 1 66  ? 30.514 14.164  16.411  1.00 10.10 ? 66  PRO F CA  1 
ATOM   1677 C  C   . PRO B 1 66  ? 31.660 15.155  16.581  1.00 10.70 ? 66  PRO F C   1 
ATOM   1678 O  O   . PRO B 1 66  ? 32.231 15.201  17.652  1.00 12.15 ? 66  PRO F O   1 
ATOM   1679 C  CB  . PRO B 1 66  ? 31.031 12.785  15.969  1.00 10.12 ? 66  PRO F CB  1 
ATOM   1680 C  CG  . PRO B 1 66  ? 30.841 12.781  14.499  1.00 11.08 ? 66  PRO F CG  1 
ATOM   1681 C  CD  . PRO B 1 66  ? 29.561 13.507  14.278  1.00 8.55  ? 66  PRO F CD  1 
ATOM   1682 N  N   . LEU B 1 67  ? 31.965 15.960  15.549  1.00 10.87 ? 67  LEU F N   1 
ATOM   1683 C  CA  . LEU B 1 67  ? 33.094 16.895  15.586  1.00 11.62 ? 67  LEU F CA  1 
ATOM   1684 C  C   . LEU B 1 67  ? 32.685 18.338  15.894  1.00 11.23 ? 67  LEU F C   1 
ATOM   1685 O  O   . LEU B 1 67  ? 33.513 19.251  15.846  1.00 11.88 ? 67  LEU F O   1 
ATOM   1686 C  CB  . LEU B 1 67  ? 33.860 16.844  14.265  1.00 12.78 ? 67  LEU F CB  1 
ATOM   1687 C  CG  . LEU B 1 67  ? 34.678 15.585  14.012  0.50 13.61 ? 67  LEU F CG  1 
ATOM   1688 C  CD1 . LEU B 1 67  ? 35.081 15.514  12.548  0.50 12.53 ? 67  LEU F CD1 1 
ATOM   1689 C  CD2 . LEU B 1 67  ? 35.913 15.562  14.892  0.50 15.43 ? 67  LEU F CD2 1 
ATOM   1690 N  N   . SER B 1 68  ? 31.419 18.548  16.226  1.00 10.85 ? 68  SER F N   1 
ATOM   1691 C  CA  . SER B 1 68  ? 30.956 19.870  16.663  1.00 10.60 ? 68  SER F CA  1 
ATOM   1692 C  C   . SER B 1 68  ? 31.175 20.960  15.613  1.00 11.52 ? 68  SER F C   1 
ATOM   1693 O  O   . SER B 1 68  ? 31.623 22.063  15.934  1.00 14.59 ? 68  SER F O   1 
ATOM   1694 C  CB  . SER B 1 68  ? 31.606 20.264  18.001  1.00 11.44 ? 68  SER F CB  1 
ATOM   1695 O  OG  . SER B 1 68  ? 31.276 19.332  19.017  1.00 12.38 ? 68  SER F OG  1 
ATOM   1696 N  N   A ARG B 1 69  ? 30.858 20.645  14.362  0.50 11.87 ? 69  ARG F N   1 
ATOM   1697 N  N   B ARG B 1 69  ? 30.847 20.639  14.366  0.50 11.46 ? 69  ARG F N   1 
ATOM   1698 C  CA  A ARG B 1 69  ? 30.960 21.598  13.255  0.50 13.10 ? 69  ARG F CA  1 
ATOM   1699 C  CA  B ARG B 1 69  ? 30.937 21.578  13.249  0.50 12.03 ? 69  ARG F CA  1 
ATOM   1700 C  C   A ARG B 1 69  ? 29.580 22.149  12.896  0.50 11.34 ? 69  ARG F C   1 
ATOM   1701 C  C   B ARG B 1 69  ? 29.569 22.156  12.904  0.50 11.11 ? 69  ARG F C   1 
ATOM   1702 O  O   A ARG B 1 69  ? 28.564 21.708  13.426  0.50 11.49 ? 69  ARG F O   1 
ATOM   1703 O  O   B ARG B 1 69  ? 28.550 21.737  13.445  0.50 11.28 ? 69  ARG F O   1 
ATOM   1704 C  CB  A ARG B 1 69  ? 31.585 20.911  12.039  0.50 15.39 ? 69  ARG F CB  1 
ATOM   1705 C  CB  B ARG B 1 69  ? 31.502 20.862  12.026  0.50 12.94 ? 69  ARG F CB  1 
ATOM   1706 C  CG  A ARG B 1 69  ? 32.852 20.117  12.342  0.50 19.07 ? 69  ARG F CG  1 
ATOM   1707 C  CG  B ARG B 1 69  ? 32.866 20.231  12.243  0.50 14.72 ? 69  ARG F CG  1 
ATOM   1708 C  CD  A ARG B 1 69  ? 34.136 20.807  11.897  0.50 23.14 ? 69  ARG F CD  1 
ATOM   1709 C  CD  B ARG B 1 69  ? 33.858 21.221  12.819  0.50 14.64 ? 69  ARG F CD  1 
ATOM   1710 N  NE  A ARG B 1 69  ? 35.285 20.336  12.668  0.50 24.61 ? 69  ARG F NE  1 
ATOM   1711 N  NE  B ARG B 1 69  ? 34.122 22.319  11.896  0.50 18.04 ? 69  ARG F NE  1 
ATOM   1712 C  CZ  A ARG B 1 69  ? 36.268 19.583  12.186  0.50 28.54 ? 69  ARG F CZ  1 
ATOM   1713 C  CZ  B ARG B 1 69  ? 34.878 22.227  10.805  0.50 20.61 ? 69  ARG F CZ  1 
ATOM   1714 N  NH1 A ARG B 1 69  ? 36.265 19.211  10.913  0.50 32.26 ? 69  ARG F NH1 1 
ATOM   1715 N  NH1 B ARG B 1 69  ? 35.461 21.082  10.477  0.50 26.38 ? 69  ARG F NH1 1 
ATOM   1716 N  NH2 A ARG B 1 69  ? 37.260 19.202  12.983  0.50 25.85 ? 69  ARG F NH2 1 
ATOM   1717 N  NH2 B ARG B 1 69  ? 35.048 23.291  10.036  0.50 21.62 ? 69  ARG F NH2 1 
ATOM   1718 N  N   . LYS B 1 70  ? 29.565 23.130  11.995  1.00 11.60 ? 70  LYS F N   1 
ATOM   1719 C  CA  . LYS B 1 70  ? 28.329 23.684  11.449  1.00 11.50 ? 70  LYS F CA  1 
ATOM   1720 C  C   . LYS B 1 70  ? 27.843 22.832  10.285  1.00 9.99  ? 70  LYS F C   1 
ATOM   1721 O  O   . LYS B 1 70  ? 28.599 22.064  9.702   1.00 11.13 ? 70  LYS F O   1 
ATOM   1722 C  CB  . LYS B 1 70  ? 28.547 25.112  10.954  1.00 12.58 ? 70  LYS F CB  1 
ATOM   1723 C  CG  . LYS B 1 70  ? 28.950 26.091  12.049  1.00 16.34 ? 70  LYS F CG  1 
ATOM   1724 C  CD  . LYS B 1 70  ? 29.089 27.517  11.528  1.00 19.68 ? 70  LYS F CD  1 
ATOM   1725 C  CE  . LYS B 1 70  ? 29.409 28.627  12.547  0.00 30.18 ? 70  LYS F CE  1 
ATOM   1726 N  NZ  . LYS B 1 70  ? 28.255 29.584  12.690  0.00 40.74 ? 70  LYS F NZ  1 
ATOM   1727 N  N   . HIS B 1 71  ? 26.567 22.988  9.960   1.00 10.49 ? 71  HIS F N   1 
ATOM   1728 C  CA  . HIS B 1 71  ? 25.934 22.280  8.854   1.00 11.37 ? 71  HIS F CA  1 
ATOM   1729 C  C   . HIS B 1 71  ? 26.502 22.721  7.511   1.00 10.35 ? 71  HIS F C   1 
ATOM   1730 O  O   . HIS B 1 71  ? 26.779 23.903  7.302   1.00 13.01 ? 71  HIS F O   1 
ATOM   1731 C  CB  . HIS B 1 71  ? 24.431 22.519  8.866   1.00 11.93 ? 71  HIS F CB  1 
ATOM   1732 C  CG  . HIS B 1 71  ? 23.705 21.809  7.777   1.00 10.47 ? 71  HIS F CG  1 
ATOM   1733 N  ND1 . HIS B 1 71  ? 23.441 20.449  7.787   1.00 9.73  ? 71  HIS F ND1 1 
ATOM   1734 C  CD2 . HIS B 1 71  ? 23.230 22.280  6.602   1.00 12.24 ? 71  HIS F CD2 1 
ATOM   1735 C  CE1 . HIS B 1 71  ? 22.828 20.130  6.659   1.00 10.96 ? 71  HIS F CE1 1 
ATOM   1736 N  NE2 . HIS B 1 71  ? 22.699 21.218  5.917   1.00 10.89 ? 71  HIS F NE2 1 
ATOM   1737 N  N   . GLY B 1 72  ? 26.672 21.781  6.592   1.00 12.22 ? 72  GLY F N   1 
ATOM   1738 C  CA  . GLY B 1 72  ? 27.090 22.108  5.240   1.00 12.39 ? 72  GLY F CA  1 
ATOM   1739 C  C   . GLY B 1 72  ? 26.647 21.064  4.249   1.00 12.68 ? 72  GLY F C   1 
ATOM   1740 O  O   . GLY B 1 72  ? 25.852 20.185  4.571   1.00 13.71 ? 72  GLY F O   1 
ATOM   1741 N  N   . GLY B 1 73  ? 27.149 21.184  3.029   1.00 13.45 ? 73  GLY F N   1 
ATOM   1742 C  CA  . GLY B 1 73  ? 26.980 20.158  2.018   1.00 14.08 ? 73  GLY F CA  1 
ATOM   1743 C  C   . GLY B 1 73  ? 28.064 19.101  2.142   1.00 14.05 ? 73  GLY F C   1 
ATOM   1744 O  O   . GLY B 1 73  ? 29.099 19.327  2.783   1.00 14.89 ? 73  GLY F O   1 
ATOM   1745 N  N   . PRO B 1 74  ? 27.863 17.949  1.486   1.00 13.88 ? 74  PRO F N   1 
ATOM   1746 C  CA  . PRO B 1 74  ? 28.819 16.851  1.601   1.00 15.25 ? 74  PRO F CA  1 
ATOM   1747 C  C   . PRO B 1 74  ? 30.230 17.184  1.101   1.00 15.93 ? 74  PRO F C   1 
ATOM   1748 O  O   . PRO B 1 74  ? 31.212 16.657  1.630   1.00 16.17 ? 74  PRO F O   1 
ATOM   1749 C  CB  . PRO B 1 74  ? 28.171 15.720  0.783   1.00 17.26 ? 74  PRO F CB  1 
ATOM   1750 C  CG  . PRO B 1 74  ? 27.081 16.352  -0.011  1.00 15.47 ? 74  PRO F CG  1 
ATOM   1751 C  CD  . PRO B 1 74  ? 26.658 17.575  0.735   1.00 14.01 ? 74  PRO F CD  1 
ATOM   1752 N  N   . LYS B 1 75  ? 30.341 18.072  0.115   1.00 15.39 ? 75  LYS F N   1 
ATOM   1753 C  CA  . LYS B 1 75  ? 31.650 18.426  -0.425  1.00 18.65 ? 75  LYS F CA  1 
ATOM   1754 C  C   . LYS B 1 75  ? 32.343 19.541  0.363   1.00 17.55 ? 75  LYS F C   1 
ATOM   1755 O  O   . LYS B 1 75  ? 33.470 19.903  0.031   1.00 23.22 ? 75  LYS F O   1 
ATOM   1756 C  CB  . LYS B 1 75  ? 31.534 18.788  -1.907  1.00 22.63 ? 75  LYS F CB  1 
ATOM   1757 C  CG  . LYS B 1 75  ? 31.025 17.640  -2.764  1.00 24.77 ? 75  LYS F CG  1 
ATOM   1758 C  CD  . LYS B 1 75  ? 31.448 17.939  -4.214  0.00 33.01 ? 75  LYS F CD  1 
ATOM   1759 C  CE  . LYS B 1 75  ? 32.910 17.541  -4.617  0.00 38.76 ? 75  LYS F CE  1 
ATOM   1760 N  NZ  . LYS B 1 75  ? 33.917 18.634  -4.851  0.00 35.24 ? 75  LYS F NZ  1 
ATOM   1761 N  N   . ASP B 1 76  ? 31.695 20.072  1.405   1.00 15.40 ? 76  ASP F N   1 
ATOM   1762 C  CA  . ASP B 1 76  ? 32.284 21.132  2.223   1.00 14.10 ? 76  ASP F CA  1 
ATOM   1763 C  C   . ASP B 1 76  ? 33.153 20.541  3.313   1.00 16.08 ? 76  ASP F C   1 
ATOM   1764 O  O   . ASP B 1 76  ? 32.841 19.491  3.859   1.00 19.86 ? 76  ASP F O   1 
ATOM   1765 C  CB  . ASP B 1 76  ? 31.220 22.004  2.897   1.00 12.43 ? 76  ASP F CB  1 
ATOM   1766 C  CG  . ASP B 1 76  ? 30.350 22.754  1.918   1.00 15.82 ? 76  ASP F CG  1 
ATOM   1767 O  OD1 . ASP B 1 76  ? 30.789 23.022  0.780   1.00 24.01 ? 76  ASP F OD1 1 
ATOM   1768 O  OD2 . ASP B 1 76  ? 29.210 23.090  2.304   1.00 19.93 ? 76  ASP F OD2 1 
ATOM   1769 N  N   . GLU B 1 77  ? 34.221 21.249  3.657   1.00 20.35 ? 77  GLU F N   1 
ATOM   1770 C  CA  . GLU B 1 77  ? 35.037 20.901  4.819   1.00 24.15 ? 77  GLU F CA  1 
ATOM   1771 C  C   . GLU B 1 77  ? 34.218 21.128  6.087   1.00 20.79 ? 77  GLU F C   1 
ATOM   1772 O  O   . GLU B 1 77  ? 34.230 20.303  7.002   1.00 22.25 ? 77  GLU F O   1 
ATOM   1773 C  CB  . GLU B 1 77  ? 36.300 21.759  4.863   1.00 28.07 ? 77  GLU F CB  1 
ATOM   1774 C  CG  . GLU B 1 77  ? 37.294 21.358  5.944   1.00 34.24 ? 77  GLU F CG  1 
ATOM   1775 C  CD  . GLU B 1 77  ? 38.545 22.226  5.898   0.00 42.89 ? 77  GLU F CD  1 
ATOM   1776 O  OE1 . GLU B 1 77  ? 38.628 23.143  5.054   0.00 46.77 ? 77  GLU F OE1 1 
ATOM   1777 O  OE2 . GLU B 1 77  ? 39.451 21.973  6.719   0.00 49.59 ? 77  GLU F OE2 1 
ATOM   1778 N  N   . GLU B 1 78  ? 33.512 22.257  6.135   1.00 18.52 ? 78  GLU F N   1 
ATOM   1779 C  CA  . GLU B 1 78  ? 32.635 22.571  7.254   1.00 16.78 ? 78  GLU F CA  1 
ATOM   1780 C  C   . GLU B 1 78  ? 31.283 21.909  7.023   1.00 14.35 ? 78  GLU F C   1 
ATOM   1781 O  O   . GLU B 1 78  ? 30.442 22.422  6.286   1.00 15.01 ? 78  GLU F O   1 
ATOM   1782 C  CB  . GLU B 1 78  ? 32.480 24.087  7.432   1.00 17.20 ? 78  GLU F CB  1 
ATOM   1783 C  CG  . GLU B 1 78  ? 31.815 24.469  8.748   1.00 20.32 ? 78  GLU F CG  1 
ATOM   1784 C  CD  . GLU B 1 78  ? 32.664 24.157  9.976   0.50 20.49 ? 78  GLU F CD  1 
ATOM   1785 O  OE1 . GLU B 1 78  ? 33.902 23.996  9.853   0.50 24.73 ? 78  GLU F OE1 1 
ATOM   1786 O  OE2 . GLU B 1 78  ? 32.088 24.081  11.079  0.50 20.18 ? 78  GLU F OE2 1 
ATOM   1787 N  N   . ARG B 1 79  ? 31.095 20.753  7.656   1.00 12.21 ? 79  ARG F N   1 
ATOM   1788 C  CA  . ARG B 1 79  ? 29.841 20.026  7.589   1.00 11.09 ? 79  ARG F CA  1 
ATOM   1789 C  C   . ARG B 1 79  ? 29.735 19.160  8.821   1.00 10.76 ? 79  ARG F C   1 
ATOM   1790 O  O   . ARG B 1 79  ? 30.729 18.878  9.496   1.00 11.08 ? 79  ARG F O   1 
ATOM   1791 C  CB  . ARG B 1 79  ? 29.785 19.117  6.347   1.00 11.55 ? 79  ARG F CB  1 
ATOM   1792 C  CG  . ARG B 1 79  ? 30.960 18.151  6.247   1.00 12.74 ? 79  ARG F CG  1 
ATOM   1793 C  CD  . ARG B 1 79  ? 30.804 17.136  5.121   1.00 11.84 ? 79  ARG F CD  1 
ATOM   1794 N  NE  . ARG B 1 79  ? 30.069 15.948  5.543   1.00 12.62 ? 79  ARG F NE  1 
ATOM   1795 C  CZ  . ARG B 1 79  ? 29.962 14.830  4.827   1.00 11.76 ? 79  ARG F CZ  1 
ATOM   1796 N  NH1 . ARG B 1 79  ? 30.545 14.733  3.641   1.00 13.01 ? 79  ARG F NH1 1 
ATOM   1797 N  NH2 . ARG B 1 79  ? 29.293 13.786  5.306   1.00 13.82 ? 79  ARG F NH2 1 
ATOM   1798 N  N   . HIS B 1 80  ? 28.526 18.694  9.067   1.00 9.43  ? 80  HIS F N   1 
ATOM   1799 C  CA  . HIS B 1 80  ? 28.304 17.597  10.012  1.00 8.60  ? 80  HIS F CA  1 
ATOM   1800 C  C   . HIS B 1 80  ? 28.683 16.270  9.354   1.00 10.06 ? 80  HIS F C   1 
ATOM   1801 O  O   . HIS B 1 80  ? 28.525 16.119  8.152   1.00 10.10 ? 80  HIS F O   1 
ATOM   1802 C  CB  . HIS B 1 80  ? 26.831 17.534  10.390  1.00 8.68  ? 80  HIS F CB  1 
ATOM   1803 C  CG  . HIS B 1 80  ? 26.302 18.790  11.000  1.00 9.38  ? 80  HIS F CG  1 
ATOM   1804 N  ND1 . HIS B 1 80  ? 25.041 19.288  10.747  1.00 9.77  ? 80  HIS F ND1 1 
ATOM   1805 C  CD2 . HIS B 1 80  ? 26.864 19.627  11.899  1.00 8.96  ? 80  HIS F CD2 1 
ATOM   1806 C  CE1 . HIS B 1 80  ? 24.844 20.355  11.502  1.00 8.66  ? 80  HIS F CE1 1 
ATOM   1807 N  NE2 . HIS B 1 80  ? 25.937 20.585  12.200  1.00 9.98  ? 80  HIS F NE2 1 
ATOM   1808 N  N   . VAL B 1 81  ? 29.102 15.275  10.138  1.00 9.94  ? 81  VAL F N   1 
ATOM   1809 C  CA  . VAL B 1 81  ? 29.338 13.950  9.551   1.00 9.84  ? 81  VAL F CA  1 
ATOM   1810 C  C   . VAL B 1 81  ? 28.082 13.457  8.837   1.00 10.43 ? 81  VAL F C   1 
ATOM   1811 O  O   . VAL B 1 81  ? 28.169 12.884  7.758   1.00 11.36 ? 81  VAL F O   1 
ATOM   1812 C  CB  . VAL B 1 81  ? 29.841 12.918  10.580  1.00 10.61 ? 81  VAL F CB  1 
ATOM   1813 C  CG1 . VAL B 1 81  ? 29.829 11.497  10.001  1.00 9.62  ? 81  VAL F CG1 1 
ATOM   1814 C  CG2 . VAL B 1 81  ? 31.240 13.276  11.036  1.00 11.90 ? 81  VAL F CG2 1 
ATOM   1815 N  N   . GLY B 1 82  ? 26.909 13.706  9.410   1.00 10.05 ? 82  GLY F N   1 
ATOM   1816 C  CA  . GLY B 1 82  ? 25.659 13.246  8.792   1.00 11.45 ? 82  GLY F CA  1 
ATOM   1817 C  C   . GLY B 1 82  ? 25.139 13.986  7.565   1.00 10.05 ? 82  GLY F C   1 
ATOM   1818 O  O   . GLY B 1 82  ? 24.068 13.654  7.050   1.00 11.98 ? 82  GLY F O   1 
ATOM   1819 N  N   . ASP B 1 83  ? 25.876 14.988  7.089   1.00 9.55  ? 83  ASP F N   1 
ATOM   1820 C  CA  . ASP B 1 83  ? 25.419 15.824  5.989   1.00 9.53  ? 83  ASP F CA  1 
ATOM   1821 C  C   . ASP B 1 83  ? 25.693 15.202  4.625   1.00 10.54 ? 83  ASP F C   1 
ATOM   1822 O  O   . ASP B 1 83  ? 26.751 15.418  4.040   1.00 13.75 ? 83  ASP F O   1 
ATOM   1823 C  CB  . ASP B 1 83  ? 26.093 17.199  6.083   1.00 9.28  ? 83  ASP F CB  1 
ATOM   1824 C  CG  . ASP B 1 83  ? 25.578 18.028  7.240   1.00 9.85  ? 83  ASP F CG  1 
ATOM   1825 O  OD1 . ASP B 1 83  ? 24.532 17.658  7.825   1.00 9.94  ? 83  ASP F OD1 1 
ATOM   1826 O  OD2 . ASP B 1 83  ? 26.234 19.042  7.575   1.00 10.24 ? 83  ASP F OD2 1 
ATOM   1827 N  N   . LEU B 1 84  ? 24.707 14.466  4.114   1.00 10.26 ? 84  LEU F N   1 
ATOM   1828 C  CA  . LEU B 1 84  ? 24.813 13.786  2.826   1.00 10.49 ? 84  LEU F CA  1 
ATOM   1829 C  C   . LEU B 1 84  ? 24.124 14.552  1.696   1.00 11.93 ? 84  LEU F C   1 
ATOM   1830 O  O   . LEU B 1 84  ? 23.980 14.030  0.588   1.00 15.81 ? 84  LEU F O   1 
ATOM   1831 C  CB  . LEU B 1 84  ? 24.306 12.339  2.933   1.00 11.68 ? 84  LEU F CB  1 
ATOM   1832 C  CG  . LEU B 1 84  ? 25.142 11.444  3.848   1.00 13.39 ? 84  LEU F CG  1 
ATOM   1833 C  CD1 . LEU B 1 84  ? 24.499 10.066  3.908   1.00 13.85 ? 84  LEU F CD1 1 
ATOM   1834 C  CD2 . LEU B 1 84  ? 26.595 11.350  3.412   1.00 16.77 ? 84  LEU F CD2 1 
ATOM   1835 N  N   . GLY B 1 85  ? 23.728 15.795  1.966   1.00 13.04 ? 85  GLY F N   1 
ATOM   1836 C  CA  . GLY B 1 85  ? 23.239 16.676  0.916   1.00 14.71 ? 85  GLY F CA  1 
ATOM   1837 C  C   . GLY B 1 85  ? 21.804 16.383  0.544   1.00 12.48 ? 85  GLY F C   1 
ATOM   1838 O  O   . GLY B 1 85  ? 20.939 16.298  1.408   1.00 13.41 ? 85  GLY F O   1 
ATOM   1839 N  N   . ASN B 1 86  ? 21.555 16.260  -0.757  1.00 11.38 ? 86  ASN F N   1 
ATOM   1840 C  CA  . ASN B 1 86  ? 20.228 16.015  -1.293  1.00 11.20 ? 86  ASN F CA  1 
ATOM   1841 C  C   . ASN B 1 86  ? 20.227 14.785  -2.181  1.00 11.31 ? 86  ASN F C   1 
ATOM   1842 O  O   . ASN B 1 86  ? 21.213 14.498  -2.898  1.00 15.40 ? 86  ASN F O   1 
ATOM   1843 C  CB  . ASN B 1 86  ? 19.754 17.195  -2.146  1.00 10.83 ? 86  ASN F CB  1 
ATOM   1844 C  CG  . ASN B 1 86  ? 19.455 18.422  -1.322  1.00 12.12 ? 86  ASN F CG  1 
ATOM   1845 O  OD1 . ASN B 1 86  ? 18.548 18.394  -0.502  1.00 12.43 ? 86  ASN F OD1 1 
ATOM   1846 N  ND2 . ASN B 1 86  ? 20.185 19.521  -1.568  1.00 14.48 ? 86  ASN F ND2 1 
ATOM   1847 N  N   . VAL B 1 87  ? 19.096 14.097  -2.169  1.00 10.53 ? 87  VAL F N   1 
ATOM   1848 C  CA  . VAL B 1 87  ? 18.789 13.127  -3.214  1.00 10.68 ? 87  VAL F CA  1 
ATOM   1849 C  C   . VAL B 1 87  ? 17.815 13.795  -4.182  1.00 10.97 ? 87  VAL F C   1 
ATOM   1850 O  O   . VAL B 1 87  ? 17.146 14.780  -3.831  1.00 12.29 ? 87  VAL F O   1 
ATOM   1851 C  CB  . VAL B 1 87  ? 18.238 11.796  -2.653  1.00 13.29 ? 87  VAL F CB  1 
ATOM   1852 C  CG1 . VAL B 1 87  ? 19.283 11.135  -1.771  1.00 14.68 ? 87  VAL F CG1 1 
ATOM   1853 C  CG2 . VAL B 1 87  ? 16.920 11.994  -1.906  1.00 14.69 ? 87  VAL F CG2 1 
ATOM   1854 N  N   . THR B 1 88  ? 17.737 13.252  -5.393  1.00 11.96 ? 88  THR F N   1 
ATOM   1855 C  CA  . THR B 1 88  ? 16.955 13.854  -6.464  1.00 13.78 ? 88  THR F CA  1 
ATOM   1856 C  C   . THR B 1 88  ? 15.887 12.888  -6.925  1.00 13.08 ? 88  THR F C   1 
ATOM   1857 O  O   . THR B 1 88  ? 16.208 11.801  -7.404  1.00 14.14 ? 88  THR F O   1 
ATOM   1858 C  CB  . THR B 1 88  ? 17.857 14.224  -7.655  1.00 15.39 ? 88  THR F CB  1 
ATOM   1859 O  OG1 . THR B 1 88  ? 18.887 15.107  -7.199  1.00 16.65 ? 88  THR F OG1 1 
ATOM   1860 C  CG2 . THR B 1 88  ? 17.066 14.892  -8.784  1.00 17.63 ? 88  THR F CG2 1 
ATOM   1861 N  N   . ALA B 1 89  ? 14.629 13.291  -6.799  1.00 14.03 ? 89  ALA F N   1 
ATOM   1862 C  CA  . ALA B 1 89  ? 13.504 12.504  -7.271  1.00 15.76 ? 89  ALA F CA  1 
ATOM   1863 C  C   . ALA B 1 89  ? 13.096 12.978  -8.659  1.00 15.60 ? 89  ALA F C   1 
ATOM   1864 O  O   . ALA B 1 89  ? 13.054 14.182  -8.931  1.00 16.28 ? 89  ALA F O   1 
ATOM   1865 C  CB  . ALA B 1 89  ? 12.332 12.635  -6.323  1.00 16.20 ? 89  ALA F CB  1 
ATOM   1866 N  N   . ASP B 1 90  ? 12.798 12.017  -9.528  1.00 17.33 ? 90  ASP F N   1 
ATOM   1867 C  CA  . ASP B 1 90  ? 12.308 12.290  -10.878 1.00 17.52 ? 90  ASP F CA  1 
ATOM   1868 C  C   . ASP B 1 90  ? 10.784 12.528  -10.880 1.00 18.27 ? 90  ASP F C   1 
ATOM   1869 O  O   . ASP B 1 90  ? 10.154 12.541  -9.812  1.00 17.81 ? 90  ASP F O   1 
ATOM   1870 C  CB  . ASP B 1 90  ? 12.761 11.170  -11.837 1.00 17.77 ? 90  ASP F CB  1 
ATOM   1871 C  CG  . ASP B 1 90  ? 12.121 9.807   -11.555 0.80 18.07 ? 90  ASP F CG  1 
ATOM   1872 O  OD1 . ASP B 1 90  ? 11.067 9.710   -10.882 0.80 15.23 ? 90  ASP F OD1 1 
ATOM   1873 O  OD2 . ASP B 1 90  ? 12.698 8.807   -12.042 0.80 19.54 ? 90  ASP F OD2 1 
ATOM   1874 N  N   A LYS B 1 91  ? 10.199 12.718  -12.062 0.70 18.90 ? 91  LYS F N   1 
ATOM   1875 N  N   B LYS B 1 91  ? 10.215 12.716  -12.074 0.30 19.27 ? 91  LYS F N   1 
ATOM   1876 C  CA  A LYS B 1 91  ? 8.758  12.985  -12.170 0.70 19.48 ? 91  LYS F CA  1 
ATOM   1877 C  CA  B LYS B 1 91  ? 8.771  12.931  -12.256 0.30 20.05 ? 91  LYS F CA  1 
ATOM   1878 C  C   A LYS B 1 91  ? 7.860  11.776  -11.818 0.70 20.70 ? 91  LYS F C   1 
ATOM   1879 C  C   B LYS B 1 91  ? 7.881  11.782  -11.776 0.30 21.05 ? 91  LYS F C   1 
ATOM   1880 O  O   A LYS B 1 91  ? 6.656  11.954  -11.640 0.70 22.47 ? 91  LYS F O   1 
ATOM   1881 O  O   B LYS B 1 91  ? 6.711  12.001  -11.460 0.30 21.89 ? 91  LYS F O   1 
ATOM   1882 C  CB  A LYS B 1 91  ? 8.394  13.547  -13.556 0.70 20.20 ? 91  LYS F CB  1 
ATOM   1883 C  CB  B LYS B 1 91  ? 8.462  13.217  -13.727 0.30 21.18 ? 91  LYS F CB  1 
ATOM   1884 C  CG  A LYS B 1 91  ? 8.714  15.032  -13.743 0.70 22.09 ? 91  LYS F CG  1 
ATOM   1885 C  CG  B LYS B 1 91  ? 9.271  12.387  -14.706 0.30 23.36 ? 91  LYS F CG  1 
ATOM   1886 C  CD  A LYS B 1 91  ? 7.774  15.939  -12.946 0.70 21.35 ? 91  LYS F CD  1 
ATOM   1887 C  CD  B LYS B 1 91  ? 8.558  11.139  -15.185 0.30 23.84 ? 91  LYS F CD  1 
ATOM   1888 C  CE  A LYS B 1 91  ? 7.718  17.339  -13.538 0.70 23.75 ? 91  LYS F CE  1 
ATOM   1889 C  CE  B LYS B 1 91  ? 9.161  10.679  -16.502 0.30 23.89 ? 91  LYS F CE  1 
ATOM   1890 N  NZ  A LYS B 1 91  ? 6.855  18.258  -12.751 0.70 28.62 ? 91  LYS F NZ  1 
ATOM   1891 N  NZ  B LYS B 1 91  ? 9.480  9.226   -16.519 0.30 25.56 ? 91  LYS F NZ  1 
ATOM   1892 N  N   . ASP B 1 92  ? 8.433  10.569  -11.733 1.00 20.54 ? 92  ASP F N   1 
ATOM   1893 C  CA  . ASP B 1 92  ? 7.736  9.400   -11.149 1.00 20.21 ? 92  ASP F CA  1 
ATOM   1894 C  C   . ASP B 1 92  ? 7.879  9.302   -9.629  1.00 19.35 ? 92  ASP F C   1 
ATOM   1895 O  O   . ASP B 1 92  ? 7.322  8.389   -9.023  1.00 21.53 ? 92  ASP F O   1 
ATOM   1896 C  CB  . ASP B 1 92  ? 8.241  8.086   -11.763 1.00 22.23 ? 92  ASP F CB  1 
ATOM   1897 C  CG  . ASP B 1 92  ? 7.913  7.959   -13.234 1.00 25.87 ? 92  ASP F CG  1 
ATOM   1898 O  OD1 . ASP B 1 92  ? 6.813  8.381   -13.649 1.00 30.45 ? 92  ASP F OD1 1 
ATOM   1899 O  OD2 . ASP B 1 92  ? 8.757  7.421   -13.975 1.00 31.31 ? 92  ASP F OD2 1 
ATOM   1900 N  N   . GLY B 1 93  ? 8.639  10.210  -9.022  1.00 17.16 ? 93  GLY F N   1 
ATOM   1901 C  CA  . GLY B 1 93  ? 8.795  10.267  -7.578  1.00 17.04 ? 93  GLY F CA  1 
ATOM   1902 C  C   . GLY B 1 93  ? 9.879  9.356   -7.056  1.00 14.96 ? 93  GLY F C   1 
ATOM   1903 O  O   . GLY B 1 93  ? 9.913  9.052   -5.856  1.00 16.15 ? 93  GLY F O   1 
ATOM   1904 N  N   . VAL B 1 94  ? 10.765 8.925   -7.953  1.00 15.59 ? 94  VAL F N   1 
ATOM   1905 C  CA  . VAL B 1 94  ? 11.814 7.978   -7.625  1.00 15.99 ? 94  VAL F CA  1 
ATOM   1906 C  C   . VAL B 1 94  ? 13.157 8.685   -7.593  1.00 14.25 ? 94  VAL F C   1 
ATOM   1907 O  O   . VAL B 1 94  ? 13.538 9.373   -8.548  1.00 15.78 ? 94  VAL F O   1 
ATOM   1908 C  CB  . VAL B 1 94  ? 11.858 6.818   -8.635  1.00 17.82 ? 94  VAL F CB  1 
ATOM   1909 C  CG1 . VAL B 1 94  ? 13.020 5.872   -8.335  1.00 18.39 ? 94  VAL F CG1 1 
ATOM   1910 C  CG2 . VAL B 1 94  ? 10.537 6.067   -8.625  1.00 19.08 ? 94  VAL F CG2 1 
ATOM   1911 N  N   . ALA B 1 95  ? 13.863 8.518   -6.481  1.00 14.56 ? 95  ALA F N   1 
ATOM   1912 C  CA  . ALA B 1 95  ? 15.244 8.938   -6.353  1.00 14.12 ? 95  ALA F CA  1 
ATOM   1913 C  C   . ALA B 1 95  ? 16.126 7.707   -6.423  1.00 15.41 ? 95  ALA F C   1 
ATOM   1914 O  O   . ALA B 1 95  ? 16.013 6.824   -5.580  1.00 17.21 ? 95  ALA F O   1 
ATOM   1915 C  CB  . ALA B 1 95  ? 15.452 9.656   -5.033  1.00 12.17 ? 95  ALA F CB  1 
ATOM   1916 N  N   . ASP B 1 96  ? 16.981 7.645   -7.442  1.00 16.19 ? 96  ASP F N   1 
ATOM   1917 C  CA  . ASP B 1 96  ? 18.013 6.618   -7.534  1.00 15.97 ? 96  ASP F CA  1 
ATOM   1918 C  C   . ASP B 1 96  ? 19.274 7.193   -6.912  1.00 15.34 ? 96  ASP F C   1 
ATOM   1919 O  O   . ASP B 1 96  ? 19.868 8.135   -7.432  1.00 20.78 ? 96  ASP F O   1 
ATOM   1920 C  CB  . ASP B 1 96  ? 18.215 6.190   -8.988  1.00 17.11 ? 96  ASP F CB  1 
ATOM   1921 C  CG  . ASP B 1 96  ? 17.032 5.394   -9.516  0.50 15.92 ? 96  ASP F CG  1 
ATOM   1922 O  OD1 . ASP B 1 96  ? 16.664 4.384   -8.871  0.50 15.76 ? 96  ASP F OD1 1 
ATOM   1923 O  OD2 . ASP B 1 96  ? 16.464 5.778   -10.557 0.50 18.26 ? 96  ASP F OD2 1 
ATOM   1924 N  N   . VAL B 1 97  ? 19.646 6.664   -5.758  1.00 14.89 ? 97  VAL F N   1 
ATOM   1925 C  CA  . VAL B 1 97  ? 20.720 7.221   -4.954  1.00 16.44 ? 97  VAL F CA  1 
ATOM   1926 C  C   . VAL B 1 97  ? 22.029 6.557   -5.345  1.00 16.32 ? 97  VAL F C   1 
ATOM   1927 O  O   . VAL B 1 97  ? 22.108 5.321   -5.413  1.00 16.31 ? 97  VAL F O   1 
ATOM   1928 C  CB  . VAL B 1 97  ? 20.430 7.034   -3.452  1.00 15.60 ? 97  VAL F CB  1 
ATOM   1929 C  CG1 . VAL B 1 97  ? 21.562 7.583   -2.602  1.00 16.06 ? 97  VAL F CG1 1 
ATOM   1930 C  CG2 . VAL B 1 97  ? 19.099 7.689   -3.099  1.00 15.28 ? 97  VAL F CG2 1 
ATOM   1931 N  N   . SER B 1 98  ? 23.042 7.382   -5.594  1.00 18.58 ? 98  SER F N   1 
ATOM   1932 C  CA  . SER B 1 98  ? 24.405 6.934   -5.847  1.00 20.95 ? 98  SER F CA  1 
ATOM   1933 C  C   . SER B 1 98  ? 25.375 8.014   -5.352  1.00 19.80 ? 98  SER F C   1 
ATOM   1934 O  O   . SER B 1 98  ? 25.590 9.025   -6.028  1.00 24.62 ? 98  SER F O   1 
ATOM   1935 C  CB  . SER B 1 98  ? 24.612 6.659   -7.335  1.00 23.21 ? 98  SER F CB  1 
ATOM   1936 O  OG  . SER B 1 98  ? 25.883 6.085   -7.547  1.00 27.89 ? 98  SER F OG  1 
ATOM   1937 N  N   . ILE B 1 99  ? 25.950 7.789   -4.178  1.00 18.82 ? 99  ILE F N   1 
ATOM   1938 C  CA  . ILE B 1 99  ? 26.806 8.747   -3.479  1.00 20.72 ? 99  ILE F CA  1 
ATOM   1939 C  C   . ILE B 1 99  ? 28.074 7.997   -3.097  1.00 16.83 ? 99  ILE F C   1 
ATOM   1940 O  O   . ILE B 1 99  ? 28.014 6.816   -2.734  1.00 19.91 ? 99  ILE F O   1 
ATOM   1941 C  CB  . ILE B 1 99  ? 26.109 9.283   -2.182  1.00 20.80 ? 99  ILE F CB  1 
ATOM   1942 C  CG1 . ILE B 1 99  ? 24.964 10.248  -2.521  1.00 19.29 ? 99  ILE F CG1 1 
ATOM   1943 C  CG2 . ILE B 1 99  ? 27.088 9.983   -1.237  1.00 23.23 ? 99  ILE F CG2 1 
ATOM   1944 C  CD1 . ILE B 1 99  ? 24.001 10.505  -1.372  1.00 20.93 ? 99  ILE F CD1 1 
ATOM   1945 N  N   . GLU B 1 100 ? 29.208 8.683   -3.141  1.00 17.26 ? 100 GLU F N   1 
ATOM   1946 C  CA  . GLU B 1 100 ? 30.420 8.235   -2.472  1.00 16.84 ? 100 GLU F CA  1 
ATOM   1947 C  C   . GLU B 1 100 ? 30.766 9.322   -1.474  1.00 16.16 ? 100 GLU F C   1 
ATOM   1948 O  O   . GLU B 1 100 ? 30.906 10.483  -1.852  1.00 18.99 ? 100 GLU F O   1 
ATOM   1949 C  CB  . GLU B 1 100 ? 31.562 8.038   -3.466  1.00 20.85 ? 100 GLU F CB  1 
ATOM   1950 C  CG  . GLU B 1 100 ? 32.828 7.471   -2.848  1.00 26.05 ? 100 GLU F CG  1 
ATOM   1951 C  CD  . GLU B 1 100 ? 33.945 7.302   -3.858  1.00 33.38 ? 100 GLU F CD  1 
ATOM   1952 O  OE1 . GLU B 1 100 ? 33.885 6.341   -4.648  1.00 39.40 ? 100 GLU F OE1 1 
ATOM   1953 O  OE2 . GLU B 1 100 ? 34.888 8.124   -3.852  1.00 37.35 ? 100 GLU F OE2 1 
ATOM   1954 N  N   . ASP B 1 101 ? 30.903 8.963   -0.207  1.00 16.64 ? 101 ASP F N   1 
ATOM   1955 C  CA  . ASP B 1 101 ? 31.208 9.958   0.812   1.00 16.11 ? 101 ASP F CA  1 
ATOM   1956 C  C   . ASP B 1 101 ? 32.414 9.532   1.615   1.00 15.44 ? 101 ASP F C   1 
ATOM   1957 O  O   . ASP B 1 101 ? 32.520 8.369   2.034   1.00 16.72 ? 101 ASP F O   1 
ATOM   1958 C  CB  . ASP B 1 101 ? 30.022 10.185  1.740   1.00 15.08 ? 101 ASP F CB  1 
ATOM   1959 C  CG  . ASP B 1 101 ? 30.171 11.449  2.563   1.00 15.99 ? 101 ASP F CG  1 
ATOM   1960 O  OD1 . ASP B 1 101 ? 29.977 12.541  1.980   1.00 19.20 ? 101 ASP F OD1 1 
ATOM   1961 O  OD2 . ASP B 1 101 ? 30.516 11.353  3.769   1.00 16.20 ? 101 ASP F OD2 1 
ATOM   1962 N  N   . SER B 1 102 ? 33.277 10.501  1.878   1.00 16.35 ? 102 SER F N   1 
ATOM   1963 C  CA  . SER B 1 102 ? 34.555 10.283  2.528   1.00 19.08 ? 102 SER F CA  1 
ATOM   1964 C  C   . SER B 1 102 ? 34.552 10.574  4.037   1.00 16.59 ? 102 SER F C   1 
ATOM   1965 O  O   . SER B 1 102 ? 35.547 10.308  4.712   1.00 20.64 ? 102 SER F O   1 
ATOM   1966 C  CB  . SER B 1 102 ? 35.608 11.150  1.804   1.00 20.33 ? 102 SER F CB  1 
ATOM   1967 O  OG  A SER B 1 102 ? 36.071 10.322  0.759   0.60 26.63 ? 102 SER F OG  1 
ATOM   1968 O  OG  B SER B 1 102 ? 35.505 12.431  2.406   0.40 21.43 ? 102 SER F OG  1 
ATOM   1969 N  N   . VAL B 1 103 ? 33.434 11.094  4.556   1.00 13.03 ? 103 VAL F N   1 
ATOM   1970 C  CA  . VAL B 1 103 ? 33.350 11.566  5.945   1.00 11.36 ? 103 VAL F CA  1 
ATOM   1971 C  C   . VAL B 1 103 ? 32.584 10.593  6.850   1.00 12.77 ? 103 VAL F C   1 
ATOM   1972 O  O   . VAL B 1 103 ? 33.046 10.270  7.948   1.00 14.28 ? 103 VAL F O   1 
ATOM   1973 C  CB  . VAL B 1 103 ? 32.747 12.992  5.986   1.00 12.13 ? 103 VAL F CB  1 
ATOM   1974 C  CG1 . VAL B 1 103 ? 32.543 13.466  7.414   1.00 13.58 ? 103 VAL F CG1 1 
ATOM   1975 C  CG2 . VAL B 1 103 ? 33.644 13.976  5.227   1.00 13.76 ? 103 VAL F CG2 1 
ATOM   1976 N  N   . ILE B 1 104 ? 31.439 10.106  6.387   1.00 11.73 ? 104 ILE F N   1 
ATOM   1977 C  CA  . ILE B 1 104 ? 30.772 8.995   7.081   1.00 12.41 ? 104 ILE F CA  1 
ATOM   1978 C  C   . ILE B 1 104 ? 31.689 7.777   7.057   1.00 11.53 ? 104 ILE F C   1 
ATOM   1979 O  O   . ILE B 1 104 ? 32.568 7.654   6.193   1.00 14.32 ? 104 ILE F O   1 
ATOM   1980 C  CB  . ILE B 1 104 ? 29.389 8.632   6.480   1.00 11.92 ? 104 ILE F CB  1 
ATOM   1981 C  CG1 . ILE B 1 104 ? 29.502 8.231   4.994   1.00 12.74 ? 104 ILE F CG1 1 
ATOM   1982 C  CG2 . ILE B 1 104 ? 28.412 9.782   6.694   1.00 11.45 ? 104 ILE F CG2 1 
ATOM   1983 C  CD1 . ILE B 1 104 ? 28.268 7.590   4.411   1.00 13.09 ? 104 ILE F CD1 1 
ATOM   1984 N  N   . SER B 1 105 ? 31.472 6.885   8.011   1.00 11.85 ? 105 SER F N   1 
ATOM   1985 C  CA  . SER B 1 105 ? 32.201 5.625   8.057   1.00 12.37 ? 105 SER F CA  1 
ATOM   1986 C  C   . SER B 1 105 ? 31.293 4.529   8.589   1.00 11.40 ? 105 SER F C   1 
ATOM   1987 O  O   . SER B 1 105 ? 30.237 4.803   9.139   1.00 11.53 ? 105 SER F O   1 
ATOM   1988 C  CB  . SER B 1 105 ? 33.426 5.749   8.951   1.00 12.84 ? 105 SER F CB  1 
ATOM   1989 O  OG  . SER B 1 105 ? 34.268 4.617   8.811   1.00 13.89 ? 105 SER F OG  1 
ATOM   1990 N  N   . LEU B 1 106 ? 31.710 3.283   8.385   1.00 11.46 ? 106 LEU F N   1 
ATOM   1991 C  CA  . LEU B 1 106 ? 31.055 2.133   8.991   1.00 12.30 ? 106 LEU F CA  1 
ATOM   1992 C  C   . LEU B 1 106 ? 31.883 1.562   10.149  1.00 14.29 ? 106 LEU F C   1 
ATOM   1993 O  O   . LEU B 1 106 ? 31.579 0.472   10.659  1.00 16.31 ? 106 LEU F O   1 
ATOM   1994 C  CB  . LEU B 1 106 ? 30.726 1.073   7.925   1.00 13.43 ? 106 LEU F CB  1 
ATOM   1995 C  CG  . LEU B 1 106 ? 29.870 1.553   6.742   1.00 12.57 ? 106 LEU F CG  1 
ATOM   1996 C  CD1 . LEU B 1 106 ? 29.590 0.401   5.786   1.00 12.91 ? 106 LEU F CD1 1 
ATOM   1997 C  CD2 . LEU B 1 106 ? 28.554 2.194   7.156   1.00 12.27 ? 106 LEU F CD2 1 
ATOM   1998 N  N   . SER B 1 107 ? 32.886 2.329   10.589  1.00 15.22 ? 107 SER F N   1 
ATOM   1999 C  CA  . SER B 1 107 ? 33.613 2.065   11.830  1.00 16.51 ? 107 SER F CA  1 
ATOM   2000 C  C   . SER B 1 107 ? 34.130 3.377   12.456  1.00 18.13 ? 107 SER F C   1 
ATOM   2001 O  O   . SER B 1 107 ? 34.123 4.429   11.806  1.00 18.82 ? 107 SER F O   1 
ATOM   2002 C  CB  . SER B 1 107 ? 34.750 1.068   11.578  1.00 20.98 ? 107 SER F CB  1 
ATOM   2003 O  OG  . SER B 1 107 ? 35.767 1.630   10.782  1.00 27.33 ? 107 SER F OG  1 
ATOM   2004 N  N   . GLY B 1 108 ? 34.541 3.318   13.722  1.00 20.20 ? 108 GLY F N   1 
ATOM   2005 C  CA  . GLY B 1 108 ? 35.107 4.490   14.411  1.00 21.17 ? 108 GLY F CA  1 
ATOM   2006 C  C   . GLY B 1 108 ? 34.075 5.504   14.878  1.00 20.01 ? 108 GLY F C   1 
ATOM   2007 O  O   . GLY B 1 108 ? 32.877 5.281   14.761  1.00 18.49 ? 108 GLY F O   1 
ATOM   2008 N  N   . ASP B 1 109 ? 34.521 6.652   15.389  1.00 19.88 ? 109 ASP F N   1 
ATOM   2009 C  CA  . ASP B 1 109 ? 33.556 7.623   15.921  1.00 20.43 ? 109 ASP F CA  1 
ATOM   2010 C  C   . ASP B 1 109 ? 32.802 8.432   14.859  1.00 16.99 ? 109 ASP F C   1 
ATOM   2011 O  O   . ASP B 1 109 ? 31.939 9.242   15.233  1.00 19.30 ? 109 ASP F O   1 
ATOM   2012 C  CB  . ASP B 1 109 ? 34.169 8.529   17.004  1.00 23.44 ? 109 ASP F CB  1 
ATOM   2013 C  CG  . ASP B 1 109 ? 35.094 9.608   16.461  1.00 24.99 ? 109 ASP F CG  1 
ATOM   2014 O  OD1 . ASP B 1 109 ? 35.420 9.636   15.256  1.00 24.44 ? 109 ASP F OD1 1 
ATOM   2015 O  OD2 . ASP B 1 109 ? 35.497 10.438  17.290  1.00 26.79 ? 109 ASP F OD2 1 
ATOM   2016 N  N   . HIS B 1 110 ? 33.113 8.197   13.575  1.00 14.40 ? 110 HIS F N   1 
ATOM   2017 C  CA  . HIS B 1 110 ? 32.305 8.688   12.470  1.00 12.93 ? 110 HIS F CA  1 
ATOM   2018 C  C   . HIS B 1 110 ? 31.364 7.589   11.971  1.00 12.09 ? 110 HIS F C   1 
ATOM   2019 O  O   . HIS B 1 110 ? 30.711 7.749   10.947  1.00 12.82 ? 110 HIS F O   1 
ATOM   2020 C  CB  . HIS B 1 110 ? 33.196 9.177   11.324  1.00 13.79 ? 110 HIS F CB  1 
ATOM   2021 C  CG  . HIS B 1 110 ? 33.989 10.402  11.651  1.00 16.93 ? 110 HIS F CG  1 
ATOM   2022 N  ND1 . HIS B 1 110 ? 34.346 10.747  12.938  1.00 21.05 ? 110 HIS F ND1 1 
ATOM   2023 C  CD2 . HIS B 1 110 ? 34.514 11.356  10.846  1.00 19.43 ? 110 HIS F CD2 1 
ATOM   2024 C  CE1 . HIS B 1 110 ? 35.039 11.870  12.913  1.00 23.48 ? 110 HIS F CE1 1 
ATOM   2025 N  NE2 . HIS B 1 110 ? 35.162 12.256  11.655  1.00 23.29 ? 110 HIS F NE2 1 
ATOM   2026 N  N   . CYS B 1 111 ? 31.261 6.494   12.727  1.00 11.07 ? 111 CYS F N   1 
ATOM   2027 C  CA  . CYS B 1 111 ? 30.426 5.379   12.327  1.00 11.37 ? 111 CYS F CA  1 
ATOM   2028 C  C   . CYS B 1 111 ? 28.963 5.749   12.386  1.00 10.22 ? 111 CYS F C   1 
ATOM   2029 O  O   . CYS B 1 111 ? 28.517 6.353   13.360  1.00 12.62 ? 111 CYS F O   1 
ATOM   2030 C  CB  . CYS B 1 111 ? 30.657 4.182   13.235  1.00 11.71 ? 111 CYS F CB  1 
ATOM   2031 S  SG  . CYS B 1 111 ? 29.800 2.700   12.691  1.00 15.08 ? 111 CYS F SG  1 
ATOM   2032 N  N   . ILE B 1 112 ? 28.229 5.364   11.346  1.00 9.83  ? 112 ILE F N   1 
ATOM   2033 C  CA  . ILE B 1 112 ? 26.812 5.653   11.224  1.00 10.27 ? 112 ILE F CA  1 
ATOM   2034 C  C   . ILE B 1 112 ? 25.902 4.452   11.495  1.00 9.72  ? 112 ILE F C   1 
ATOM   2035 O  O   . ILE B 1 112 ? 24.685 4.586   11.502  1.00 9.25  ? 112 ILE F O   1 
ATOM   2036 C  CB  . ILE B 1 112 ? 26.476 6.308   9.870   1.00 8.84  ? 112 ILE F CB  1 
ATOM   2037 C  CG1 . ILE B 1 112 ? 26.775 5.377   8.695   1.00 10.40 ? 112 ILE F CG1 1 
ATOM   2038 C  CG2 . ILE B 1 112 ? 27.226 7.629   9.728   1.00 9.37  ? 112 ILE F CG2 1 
ATOM   2039 C  CD1 . ILE B 1 112 ? 26.224 5.885   7.388   1.00 11.71 ? 112 ILE F CD1 1 
ATOM   2040 N  N   . ILE B 1 113 ? 26.492 3.279   11.715  1.00 9.21  ? 113 ILE F N   1 
ATOM   2041 C  CA  . ILE B 1 113 ? 25.699 2.114   12.104  1.00 9.07  ? 113 ILE F CA  1 
ATOM   2042 C  C   . ILE B 1 113 ? 25.002 2.386   13.438  1.00 9.83  ? 113 ILE F C   1 
ATOM   2043 O  O   . ILE B 1 113 ? 25.609 2.929   14.368  1.00 11.17 ? 113 ILE F O   1 
ATOM   2044 C  CB  . ILE B 1 113 ? 26.551 0.823   12.136  1.00 9.87  ? 113 ILE F CB  1 
ATOM   2045 C  CG1 . ILE B 1 113 ? 26.947 0.457   10.693  1.00 12.52 ? 113 ILE F CG1 1 
ATOM   2046 C  CG2 . ILE B 1 113 ? 25.795 -0.331  12.807  1.00 10.12 ? 113 ILE F CG2 1 
ATOM   2047 C  CD1 . ILE B 1 113 ? 28.114 -0.500  10.573  1.00 13.96 ? 113 ILE F CD1 1 
ATOM   2048 N  N   . GLY B 1 114 ? 23.722 2.029   13.498  1.00 8.68  ? 114 GLY F N   1 
ATOM   2049 C  CA  . GLY B 1 114 ? 22.919 2.262   14.668  1.00 8.46  ? 114 GLY F CA  1 
ATOM   2050 C  C   . GLY B 1 114 ? 22.344 3.653   14.771  1.00 8.13  ? 114 GLY F C   1 
ATOM   2051 O  O   . GLY B 1 114 ? 21.743 3.983   15.792  1.00 9.47  ? 114 GLY F O   1 
ATOM   2052 N  N   . ARG B 1 115 ? 22.543 4.467   13.732  1.00 8.46  ? 115 ARG F N   1 
ATOM   2053 C  CA  . ARG B 1 115 ? 21.987 5.820   13.682  1.00 8.69  ? 115 ARG F CA  1 
ATOM   2054 C  C   . ARG B 1 115 ? 20.843 5.822   12.682  1.00 8.83  ? 115 ARG F C   1 
ATOM   2055 O  O   . ARG B 1 115 ? 20.504 4.788   12.137  1.00 10.99 ? 115 ARG F O   1 
ATOM   2056 C  CB  . ARG B 1 115 ? 23.094 6.811   13.362  1.00 9.68  ? 115 ARG F CB  1 
ATOM   2057 C  CG  . ARG B 1 115 ? 24.224 6.676   14.358  1.00 9.72  ? 115 ARG F CG  1 
ATOM   2058 C  CD  . ARG B 1 115 ? 25.222 7.817   14.321  1.00 10.75 ? 115 ARG F CD  1 
ATOM   2059 N  NE  . ARG B 1 115 ? 26.337 7.582   15.240  1.00 11.37 ? 115 ARG F NE  1 
ATOM   2060 C  CZ  . ARG B 1 115 ? 26.354 7.878   16.547  1.00 12.38 ? 115 ARG F CZ  1 
ATOM   2061 N  NH1 . ARG B 1 115 ? 25.313 8.449   17.165  1.00 11.88 ? 115 ARG F NH1 1 
ATOM   2062 N  NH2 . ARG B 1 115 ? 27.446 7.611   17.248  1.00 12.85 ? 115 ARG F NH2 1 
ATOM   2063 N  N   . THR B 1 116 ? 20.207 6.966   12.460  1.00 8.91  ? 116 THR F N   1 
ATOM   2064 C  CA  . THR B 1 116 ? 19.022 7.020   11.608  1.00 9.23  ? 116 THR F CA  1 
ATOM   2065 C  C   . THR B 1 116 ? 19.301 7.791   10.338  1.00 8.36  ? 116 THR F C   1 
ATOM   2066 O  O   . THR B 1 116 ? 19.770 8.928   10.381  1.00 11.34 ? 116 THR F O   1 
ATOM   2067 C  CB  . THR B 1 116 ? 17.824 7.678   12.336  1.00 9.63  ? 116 THR F CB  1 
ATOM   2068 O  OG1 . THR B 1 116 ? 17.462 6.885   13.459  1.00 10.72 ? 116 THR F OG1 1 
ATOM   2069 C  CG2 . THR B 1 116 ? 16.615 7.814   11.466  1.00 12.16 ? 116 THR F CG2 1 
ATOM   2070 N  N   . LEU B 1 117 ? 18.967 7.195   9.201   1.00 9.00  ? 117 LEU F N   1 
ATOM   2071 C  CA  . LEU B 1 117 ? 18.972 7.888   7.921   1.00 8.64  ? 117 LEU F CA  1 
ATOM   2072 C  C   . LEU B 1 117 ? 17.603 8.490   7.696   1.00 8.43  ? 117 LEU F C   1 
ATOM   2073 O  O   . LEU B 1 117 ? 16.587 7.822   7.907   1.00 9.70  ? 117 LEU F O   1 
ATOM   2074 C  CB  . LEU B 1 117 ? 19.313 6.897   6.798   1.00 8.79  ? 117 LEU F CB  1 
ATOM   2075 C  CG  . LEU B 1 117 ? 19.498 7.468   5.394   1.00 9.68  ? 117 LEU F CG  1 
ATOM   2076 C  CD1 . LEU B 1 117 ? 20.731 8.357   5.331   1.00 11.33 ? 117 LEU F CD1 1 
ATOM   2077 C  CD2 . LEU B 1 117 ? 19.578 6.331   4.387   1.00 10.46 ? 117 LEU F CD2 1 
ATOM   2078 N  N   . VAL B 1 118 ? 17.584 9.762   7.269   1.00 9.62  ? 118 VAL F N   1 
ATOM   2079 C  CA  . VAL B 1 118 ? 16.333 10.504  7.082   1.00 8.90  ? 118 VAL F CA  1 
ATOM   2080 C  C   . VAL B 1 118 ? 16.316 11.159  5.713   1.00 8.88  ? 118 VAL F C   1 
ATOM   2081 O  O   . VAL B 1 118 ? 17.292 11.796  5.327   1.00 10.89 ? 118 VAL F O   1 
ATOM   2082 C  CB  . VAL B 1 118 ? 16.170 11.611  8.144   1.00 9.80  ? 118 VAL F CB  1 
ATOM   2083 C  CG1 . VAL B 1 118 ? 14.873 12.381  7.937   1.00 12.11 ? 118 VAL F CG1 1 
ATOM   2084 C  CG2 . VAL B 1 118 ? 16.209 11.014  9.538   1.00 10.15 ? 118 VAL F CG2 1 
ATOM   2085 N  N   . VAL B 1 119 ? 15.196 11.016  5.013   1.00 8.61  ? 119 VAL F N   1 
ATOM   2086 C  CA  . VAL B 1 119 ? 14.928 11.807  3.811   1.00 10.25 ? 119 VAL F CA  1 
ATOM   2087 C  C   . VAL B 1 119 ? 13.861 12.862  4.145   1.00 12.17 ? 119 VAL F C   1 
ATOM   2088 O  O   . VAL B 1 119 ? 12.851 12.563  4.778   1.00 11.74 ? 119 VAL F O   1 
ATOM   2089 C  CB  . VAL B 1 119 ? 14.540 10.927  2.599   1.00 10.63 ? 119 VAL F CB  1 
ATOM   2090 C  CG1 . VAL B 1 119 ? 13.254 10.136  2.814   1.00 12.37 ? 119 VAL F CG1 1 
ATOM   2091 C  CG2 . VAL B 1 119 ? 14.422 11.789  1.352   1.00 10.90 ? 119 VAL F CG2 1 
ATOM   2092 N  N   . HIS B 1 120 ? 14.104 14.085  3.676   1.00 11.92 ? 120 HIS F N   1 
ATOM   2093 C  CA  . HIS B 1 120 ? 13.340 15.263  4.059   1.00 12.74 ? 120 HIS F CA  1 
ATOM   2094 C  C   . HIS B 1 120 ? 12.393 15.762  2.977   1.00 13.65 ? 120 HIS F C   1 
ATOM   2095 O  O   . HIS B 1 120 ? 12.531 15.431  1.805   1.00 14.31 ? 120 HIS F O   1 
ATOM   2096 C  CB  . HIS B 1 120 ? 14.306 16.381  4.431   1.00 13.13 ? 120 HIS F CB  1 
ATOM   2097 C  CG  . HIS B 1 120 ? 14.817 16.281  5.824   1.00 13.92 ? 120 HIS F CG  1 
ATOM   2098 N  ND1 . HIS B 1 120 ? 14.136 16.826  6.888   1.00 15.73 ? 120 HIS F ND1 1 
ATOM   2099 C  CD2 . HIS B 1 120 ? 15.928 15.705  6.338   1.00 13.48 ? 120 HIS F CD2 1 
ATOM   2100 C  CE1 . HIS B 1 120 ? 14.810 16.601  7.993   1.00 17.32 ? 120 HIS F CE1 1 
ATOM   2101 N  NE2 . HIS B 1 120 ? 15.899 15.919  7.693   1.00 14.69 ? 120 HIS F NE2 1 
ATOM   2102 N  N   . GLU B 1 121 ? 11.452 16.589  3.420   1.00 15.09 ? 121 GLU F N   1 
ATOM   2103 C  CA  . GLU B 1 121 ? 10.407 17.190  2.593   1.00 16.95 ? 121 GLU F CA  1 
ATOM   2104 C  C   . GLU B 1 121 ? 10.957 18.148  1.545   1.00 16.66 ? 121 GLU F C   1 
ATOM   2105 O  O   . GLU B 1 121 ? 10.527 18.125  0.397   1.00 17.11 ? 121 GLU F O   1 
ATOM   2106 C  CB  . GLU B 1 121 ? 9.408  17.923  3.509   1.00 20.45 ? 121 GLU F CB  1 
ATOM   2107 C  CG  . GLU B 1 121 ? 8.404  18.858  2.839   1.00 25.52 ? 121 GLU F CG  1 
ATOM   2108 C  CD  . GLU B 1 121 ? 7.608  19.713  3.826   0.70 29.45 ? 121 GLU F CD  1 
ATOM   2109 O  OE1 . GLU B 1 121 ? 8.134  20.102  4.899   0.70 28.09 ? 121 GLU F OE1 1 
ATOM   2110 O  OE2 . GLU B 1 121 ? 6.449  20.023  3.501   0.70 37.06 ? 121 GLU F OE2 1 
ATOM   2111 N  N   . LYS B 1 122 ? 11.889 18.993  1.972   1.00 15.45 ? 122 LYS F N   1 
ATOM   2112 C  CA  . LYS B 1 122 ? 12.429 20.061  1.148   1.00 14.84 ? 122 LYS F CA  1 
ATOM   2113 C  C   . LYS B 1 122 ? 13.897 19.827  0.874   1.00 13.58 ? 122 LYS F C   1 
ATOM   2114 O  O   . LYS B 1 122 ? 14.522 18.903  1.408   1.00 14.04 ? 122 LYS F O   1 
ATOM   2115 C  CB  . LYS B 1 122 ? 12.251 21.420  1.842   1.00 16.76 ? 122 LYS F CB  1 
ATOM   2116 C  CG  . LYS B 1 122 ? 10.830 21.714  2.304   1.00 20.28 ? 122 LYS F CG  1 
ATOM   2117 C  CD  . LYS B 1 122 ? 10.645 23.179  2.690   1.00 24.17 ? 122 LYS F CD  1 
ATOM   2118 C  CE  . LYS B 1 122 ? 11.242 23.504  4.050   1.00 29.36 ? 122 LYS F CE  1 
ATOM   2119 N  NZ  . LYS B 1 122 ? 10.227 23.437  5.139   0.10 29.50 ? 122 LYS F NZ  1 
ATOM   2120 N  N   . ALA B 1 123 ? 14.448 20.664  0.014   1.00 13.65 ? 123 ALA F N   1 
ATOM   2121 C  CA  . ALA B 1 123 ? 15.868 20.629  -0.267  1.00 14.73 ? 123 ALA F CA  1 
ATOM   2122 C  C   . ALA B 1 123 ? 16.663 21.116  0.937   1.00 12.90 ? 123 ALA F C   1 
ATOM   2123 O  O   . ALA B 1 123 ? 16.247 22.031  1.649   1.00 14.53 ? 123 ALA F O   1 
ATOM   2124 C  CB  . ALA B 1 123 ? 16.189 21.476  -1.481  1.00 13.90 ? 123 ALA F CB  1 
ATOM   2125 N  N   . ASP B 1 124 ? 17.793 20.470  1.174   1.00 12.72 ? 124 ASP F N   1 
ATOM   2126 C  CA  . ASP B 1 124 ? 18.813 20.956  2.086   1.00 12.54 ? 124 ASP F CA  1 
ATOM   2127 C  C   . ASP B 1 124 ? 19.504 22.112  1.362   1.00 13.00 ? 124 ASP F C   1 
ATOM   2128 O  O   . ASP B 1 124 ? 20.011 21.926  0.256   1.00 13.85 ? 124 ASP F O   1 
ATOM   2129 C  CB  . ASP B 1 124 ? 19.773 19.800  2.409   1.00 12.43 ? 124 ASP F CB  1 
ATOM   2130 C  CG  . ASP B 1 124 ? 20.814 20.134  3.462   1.00 12.89 ? 124 ASP F CG  1 
ATOM   2131 O  OD1 . ASP B 1 124 ? 21.156 21.327  3.649   1.00 13.74 ? 124 ASP F OD1 1 
ATOM   2132 O  OD2 . ASP B 1 124 ? 21.315 19.171  4.101   1.00 16.00 ? 124 ASP F OD2 1 
ATOM   2133 N  N   . ASP B 1 125 ? 19.523 23.296  1.975   1.00 13.08 ? 125 ASP F N   1 
ATOM   2134 C  CA  . ASP B 1 125 ? 20.196 24.447  1.350   1.00 13.51 ? 125 ASP F CA  1 
ATOM   2135 C  C   . ASP B 1 125 ? 21.731 24.404  1.509   1.00 12.09 ? 125 ASP F C   1 
ATOM   2136 O  O   . ASP B 1 125 ? 22.419 25.328  1.069   1.00 14.54 ? 125 ASP F O   1 
ATOM   2137 C  CB  . ASP B 1 125 ? 19.590 25.783  1.820   1.00 13.23 ? 125 ASP F CB  1 
ATOM   2138 C  CG  . ASP B 1 125 ? 19.809 26.075  3.298   1.00 15.15 ? 125 ASP F CG  1 
ATOM   2139 O  OD1 . ASP B 1 125 ? 20.802 25.599  3.898   1.00 14.79 ? 125 ASP F OD1 1 
ATOM   2140 O  OD2 . ASP B 1 125 ? 18.977 26.830  3.856   1.00 16.34 ? 125 ASP F OD2 1 
ATOM   2141 N  N   . LEU B 1 126 ? 22.246 23.346  2.161   1.00 13.55 ? 126 LEU F N   1 
ATOM   2142 C  CA  . LEU B 1 126 ? 23.677 23.074  2.270   1.00 13.54 ? 126 LEU F CA  1 
ATOM   2143 C  C   . LEU B 1 126 ? 24.454 24.165  3.027   1.00 13.60 ? 126 LEU F C   1 
ATOM   2144 O  O   . LEU B 1 126 ? 25.652 24.365  2.797   1.00 16.00 ? 126 LEU F O   1 
ATOM   2145 C  CB  . LEU B 1 126 ? 24.279 22.820  0.872   1.00 14.41 ? 126 LEU F CB  1 
ATOM   2146 C  CG  . LEU B 1 126 ? 23.467 21.844  -0.005  1.00 14.23 ? 126 LEU F CG  1 
ATOM   2147 C  CD1 . LEU B 1 126 ? 24.121 21.628  -1.357  1.00 17.54 ? 126 LEU F CD1 1 
ATOM   2148 C  CD2 . LEU B 1 126 ? 23.267 20.495  0.682   1.00 13.46 ? 126 LEU F CD2 1 
ATOM   2149 N  N   . GLY B 1 127 ? 23.770 24.854  3.940   1.00 12.00 ? 127 GLY F N   1 
ATOM   2150 C  CA  . GLY B 1 127 ? 24.362 25.973  4.674   1.00 12.79 ? 127 GLY F CA  1 
ATOM   2151 C  C   . GLY B 1 127 ? 24.412 27.295  3.918   1.00 14.32 ? 127 GLY F C   1 
ATOM   2152 O  O   . GLY B 1 127 ? 25.013 28.255  4.405   1.00 17.07 ? 127 GLY F O   1 
ATOM   2153 N  N   . LYS B 1 128 ? 23.726 27.365  2.776   1.00 14.61 ? 128 LYS F N   1 
ATOM   2154 C  CA  . LYS B 1 128 ? 23.729 28.532  1.887   1.00 16.77 ? 128 LYS F CA  1 
ATOM   2155 C  C   . LYS B 1 128 ? 22.309 29.103  1.693   1.00 18.34 ? 128 LYS F C   1 
ATOM   2156 O  O   . LYS B 1 128 ? 21.938 29.531  0.594   1.00 21.37 ? 128 LYS F O   1 
ATOM   2157 C  CB  . LYS B 1 128 ? 24.309 28.159  0.516   1.00 18.55 ? 128 LYS F CB  1 
ATOM   2158 C  CG  . LYS B 1 128 ? 25.688 27.520  0.530   1.00 20.68 ? 128 LYS F CG  1 
ATOM   2159 C  CD  . LYS B 1 128 ? 26.780 28.465  1.003   1.00 24.29 ? 128 LYS F CD  1 
ATOM   2160 C  CE  . LYS B 1 128 ? 28.160 27.909  0.683   0.10 26.56 ? 128 LYS F CE  1 
ATOM   2161 N  NZ  . LYS B 1 128 ? 29.247 28.884  0.980   0.10 26.80 ? 128 LYS F NZ  1 
ATOM   2162 N  N   . GLY B 1 129 ? 21.533 29.137  2.769   1.00 17.98 ? 129 GLY F N   1 
ATOM   2163 C  CA  . GLY B 1 129 ? 20.160 29.653  2.746   1.00 17.81 ? 129 GLY F CA  1 
ATOM   2164 C  C   . GLY B 1 129 ? 19.990 31.089  3.233   1.00 17.76 ? 129 GLY F C   1 
ATOM   2165 O  O   . GLY B 1 129 ? 18.943 31.687  3.007   1.00 21.66 ? 129 GLY F O   1 
ATOM   2166 N  N   . GLY B 1 130 ? 20.994 31.629  3.922   1.00 16.97 ? 130 GLY F N   1 
ATOM   2167 C  CA  . GLY B 1 130 ? 20.969 33.020  4.383   1.00 18.17 ? 130 GLY F CA  1 
ATOM   2168 C  C   . GLY B 1 130 ? 20.194 33.295  5.659   1.00 19.27 ? 130 GLY F C   1 
ATOM   2169 O  O   . GLY B 1 130 ? 19.779 34.423  5.887   1.00 22.23 ? 130 GLY F O   1 
ATOM   2170 N  N   . ASN B 1 131 ? 19.989 32.282  6.499   1.00 19.95 ? 131 ASN F N   1 
ATOM   2171 C  CA  . ASN B 1 131 ? 19.424 32.473  7.840   1.00 20.96 ? 131 ASN F CA  1 
ATOM   2172 C  C   . ASN B 1 131 ? 20.168 31.607  8.844   1.00 17.99 ? 131 ASN F C   1 
ATOM   2173 O  O   . ASN B 1 131 ? 20.998 30.769  8.456   1.00 19.77 ? 131 ASN F O   1 
ATOM   2174 C  CB  . ASN B 1 131 ? 17.904 32.224  7.859   1.00 23.62 ? 131 ASN F CB  1 
ATOM   2175 C  CG  . ASN B 1 131 ? 17.516 30.783  7.569   1.00 21.68 ? 131 ASN F CG  1 
ATOM   2176 O  OD1 . ASN B 1 131 ? 18.361 29.914  7.413   1.00 20.77 ? 131 ASN F OD1 1 
ATOM   2177 N  ND2 . ASN B 1 131 ? 16.210 30.530  7.506   1.00 24.53 ? 131 ASN F ND2 1 
ATOM   2178 N  N   . GLU B 1 132 ? 19.850 31.787  10.128  1.00 18.28 ? 132 GLU F N   1 
ATOM   2179 C  CA  . GLU B 1 132 ? 20.560 31.035  11.166  1.00 18.66 ? 132 GLU F CA  1 
ATOM   2180 C  C   . GLU B 1 132 ? 20.332 29.536  11.033  1.00 17.21 ? 132 GLU F C   1 
ATOM   2181 O  O   . GLU B 1 132 ? 21.267 28.738  11.185  1.00 18.61 ? 132 GLU F O   1 
ATOM   2182 C  CB  . GLU B 1 132 ? 20.151 31.501  12.562  1.00 22.52 ? 132 GLU F CB  1 
ATOM   2183 C  CG  . GLU B 1 132 ? 21.006 30.740  13.607  0.00 29.95 ? 132 GLU F CG  1 
ATOM   2184 C  CD  . GLU B 1 132 ? 20.713 31.257  15.002  0.00 28.06 ? 132 GLU F CD  1 
ATOM   2185 O  OE1 . GLU B 1 132 ? 19.861 32.161  15.135  0.00 39.25 ? 132 GLU F OE1 1 
ATOM   2186 O  OE2 . GLU B 1 132 ? 21.334 30.760  15.964  0.00 16.55 ? 132 GLU F OE2 1 
ATOM   2187 N  N   . GLU B 1 133 ? 19.118 29.154  10.716  1.00 15.85 ? 133 GLU F N   1 
ATOM   2188 C  CA  . GLU B 1 133 ? 18.789 27.732  10.613  1.00 15.82 ? 133 GLU F CA  1 
ATOM   2189 C  C   . GLU B 1 133 ? 19.584 27.025  9.511   1.00 14.62 ? 133 GLU F C   1 
ATOM   2190 O  O   . GLU B 1 133 ? 19.878 25.836  9.623   1.00 15.02 ? 133 GLU F O   1 
ATOM   2191 C  CB  . GLU B 1 133 ? 17.288 27.555  10.411  1.00 19.72 ? 133 GLU F CB  1 
ATOM   2192 C  CG  . GLU B 1 133 ? 16.804 26.144  10.674  0.70 15.63 ? 133 GLU F CG  1 
ATOM   2193 C  CD  . GLU B 1 133 ? 15.331 25.951  10.372  0.70 19.70 ? 133 GLU F CD  1 
ATOM   2194 O  OE1 . GLU B 1 133 ? 14.566 26.937  10.386  0.70 25.51 ? 133 GLU F OE1 1 
ATOM   2195 O  OE2 . GLU B 1 133 ? 14.937 24.798  10.099  0.70 28.37 ? 133 GLU F OE2 1 
ATOM   2196 N  N   . SER B 1 134 ? 19.980 27.757  8.475   1.00 15.93 ? 134 SER F N   1 
ATOM   2197 C  CA  . SER B 1 134 ? 20.716 27.160  7.366   1.00 13.40 ? 134 SER F CA  1 
ATOM   2198 C  C   . SER B 1 134 ? 21.995 26.450  7.807   1.00 13.23 ? 134 SER F C   1 
ATOM   2199 O  O   . SER B 1 134 ? 22.290 25.365  7.316   1.00 15.48 ? 134 SER F O   1 
ATOM   2200 C  CB  . SER B 1 134 ? 21.045 28.210  6.303   1.00 13.38 ? 134 SER F CB  1 
ATOM   2201 O  OG  . SER B 1 134 ? 21.740 27.612  5.233   1.00 15.49 ? 134 SER F OG  1 
ATOM   2202 N  N   . THR B 1 135 ? 22.725 27.024  8.763   1.00 15.63 ? 135 THR F N   1 
ATOM   2203 C  CA  . THR B 1 135 ? 23.978 26.421  9.230   1.00 16.76 ? 135 THR F CA  1 
ATOM   2204 C  C   . THR B 1 135 ? 23.801 25.458  10.415  1.00 15.31 ? 135 THR F C   1 
ATOM   2205 O  O   . THR B 1 135 ? 24.791 25.023  11.008  1.00 16.67 ? 135 THR F O   1 
ATOM   2206 C  CB  . THR B 1 135 ? 25.038 27.489  9.542   1.00 18.60 ? 135 THR F CB  1 
ATOM   2207 O  OG1 . THR B 1 135 ? 24.496 28.442  10.456  1.00 26.30 ? 135 THR F OG1 1 
ATOM   2208 C  CG2 . THR B 1 135 ? 25.477 28.182  8.249   1.00 22.05 ? 135 THR F CG2 1 
ATOM   2209 N  N   . LYS B 1 136 ? 22.553 25.088  10.711  1.00 14.65 ? 136 LYS F N   1 
ATOM   2210 C  CA  . LYS B 1 136 ? 22.236 24.052  11.696  1.00 15.43 ? 136 LYS F CA  1 
ATOM   2211 C  C   . LYS B 1 136 ? 21.540 22.867  11.025  1.00 14.51 ? 136 LYS F C   1 
ATOM   2212 O  O   . LYS B 1 136 ? 22.005 21.744  11.154  1.00 16.25 ? 136 LYS F O   1 
ATOM   2213 C  CB  . LYS B 1 136 ? 21.386 24.624  12.832  1.00 17.52 ? 136 LYS F CB  1 
ATOM   2214 C  CG  . LYS B 1 136 ? 22.160 25.583  13.723  1.00 18.73 ? 136 LYS F CG  1 
ATOM   2215 C  CD  . LYS B 1 136 ? 21.385 25.964  14.969  1.00 23.06 ? 136 LYS F CD  1 
ATOM   2216 C  CE  . LYS B 1 136 ? 22.263 26.876  15.830  0.00 24.34 ? 136 LYS F CE  1 
ATOM   2217 N  NZ  . LYS B 1 136 ? 22.437 28.205  15.182  0.00 22.59 ? 136 LYS F NZ  1 
ATOM   2218 N  N   . THR B 1 137 ? 20.448 23.105  10.300  1.00 14.46 ? 137 THR F N   1 
ATOM   2219 C  CA  . THR B 1 137 ? 19.665 22.015  9.685   1.00 15.17 ? 137 THR F CA  1 
ATOM   2220 C  C   . THR B 1 137 ? 19.605 22.039  8.163   1.00 13.80 ? 137 THR F C   1 
ATOM   2221 O  O   . THR B 1 137 ? 19.196 21.070  7.537   1.00 14.68 ? 137 THR F O   1 
ATOM   2222 C  CB  . THR B 1 137 ? 18.204 22.047  10.151  1.00 17.20 ? 137 THR F CB  1 
ATOM   2223 O  OG1 . THR B 1 137 ? 17.567 23.190  9.568   1.00 16.53 ? 137 THR F OG1 1 
ATOM   2224 C  CG2 . THR B 1 137 ? 18.100 22.077  11.676  1.00 20.12 ? 137 THR F CG2 1 
ATOM   2225 N  N   . GLY B 1 138 ? 19.964 23.163  7.561   1.00 12.71 ? 138 GLY F N   1 
ATOM   2226 C  CA  . GLY B 1 138 ? 19.805 23.350  6.125   1.00 13.54 ? 138 GLY F CA  1 
ATOM   2227 C  C   . GLY B 1 138 ? 18.382 23.595  5.638   1.00 13.05 ? 138 GLY F C   1 
ATOM   2228 O  O   . GLY B 1 138 ? 18.141 23.591  4.429   1.00 13.57 ? 138 GLY F O   1 
ATOM   2229 N  N   . ASN B 1 139 ? 17.439 23.836  6.553   1.00 13.32 ? 139 ASN F N   1 
ATOM   2230 C  CA  . ASN B 1 139 ? 16.055 24.190  6.192   1.00 13.56 ? 139 ASN F CA  1 
ATOM   2231 C  C   . ASN B 1 139 ? 15.375 23.149  5.297   1.00 14.71 ? 139 ASN F C   1 
ATOM   2232 O  O   . ASN B 1 139 ? 14.668 23.495  4.361   1.00 14.95 ? 139 ASN F O   1 
ATOM   2233 C  CB  . ASN B 1 139 ? 16.007 25.577  5.517   1.00 12.66 ? 139 ASN F CB  1 
ATOM   2234 C  CG  . ASN B 1 139 ? 16.391 26.690  6.456   1.00 14.64 ? 139 ASN F CG  1 
ATOM   2235 O  OD1 . ASN B 1 139 ? 15.685 26.954  7.415   1.00 18.40 ? 139 ASN F OD1 1 
ATOM   2236 N  ND2 . ASN B 1 139 ? 17.512 27.344  6.189   1.00 16.13 ? 139 ASN F ND2 1 
ATOM   2237 N  N   . ALA B 1 140 ? 15.582 21.868  5.597   1.00 14.68 ? 140 ALA F N   1 
ATOM   2238 C  CA  . ALA B 1 140 ? 15.057 20.795  4.736   1.00 15.19 ? 140 ALA F CA  1 
ATOM   2239 C  C   . ALA B 1 140 ? 13.642 20.351  5.095   1.00 14.99 ? 140 ALA F C   1 
ATOM   2240 O  O   . ALA B 1 140 ? 13.107 19.448  4.469   1.00 16.40 ? 140 ALA F O   1 
ATOM   2241 C  CB  . ALA B 1 140 ? 16.007 19.606  4.701   1.00 15.58 ? 140 ALA F CB  1 
ATOM   2242 N  N   . GLY B 1 141 ? 13.021 20.993  6.075   1.00 19.79 ? 141 GLY F N   1 
ATOM   2243 C  CA  . GLY B 1 141 ? 11.620 20.753  6.347   1.00 21.65 ? 141 GLY F CA  1 
ATOM   2244 C  C   . GLY B 1 141 ? 11.403 19.426  7.036   1.00 18.35 ? 141 GLY F C   1 
ATOM   2245 O  O   . GLY B 1 141 ? 12.317 18.870  7.655   1.00 19.22 ? 141 GLY F O   1 
ATOM   2246 N  N   . SER B 1 142 ? 10.192 18.907  6.889   1.00 17.29 ? 142 SER F N   1 
ATOM   2247 C  CA  . SER B 1 142 ? 9.769  17.735  7.658   1.00 16.65 ? 142 SER F CA  1 
ATOM   2248 C  C   . SER B 1 142 ? 10.531 16.467  7.269   1.00 14.79 ? 142 SER F C   1 
ATOM   2249 O  O   . SER B 1 142 ? 11.122 16.374  6.188   1.00 16.07 ? 142 SER F O   1 
ATOM   2250 C  CB  . SER B 1 142 ? 8.255  17.511  7.542   1.00 24.06 ? 142 SER F CB  1 
ATOM   2251 O  OG  . SER B 1 142 ? 7.895  16.944  6.300   0.70 24.27 ? 142 SER F OG  1 
ATOM   2252 N  N   . ARG B 1 143 ? 10.529 15.513  8.193   1.00 14.17 ? 143 ARG F N   1 
ATOM   2253 C  CA  . ARG B 1 143 ? 11.141 14.197  7.992   1.00 13.72 ? 143 ARG F CA  1 
ATOM   2254 C  C   . ARG B 1 143 ? 10.114 13.282  7.345   1.00 13.35 ? 143 ARG F C   1 
ATOM   2255 O  O   . ARG B 1 143 ? 9.121  12.926  7.981   1.00 16.95 ? 143 ARG F O   1 
ATOM   2256 C  CB  . ARG B 1 143 ? 11.603 13.639  9.340   1.00 14.02 ? 143 ARG F CB  1 
ATOM   2257 C  CG  . ARG B 1 143 ? 12.601 14.559  10.017  1.00 13.69 ? 143 ARG F CG  1 
ATOM   2258 C  CD  . ARG B 1 143 ? 13.084 14.059  11.356  1.00 13.00 ? 143 ARG F CD  1 
ATOM   2259 N  NE  . ARG B 1 143 ? 13.927 15.083  11.965  1.00 12.66 ? 143 ARG F NE  1 
ATOM   2260 C  CZ  . ARG B 1 143 ? 14.600 14.977  13.101  1.00 13.57 ? 143 ARG F CZ  1 
ATOM   2261 N  NH1 . ARG B 1 143 ? 14.546 13.869  13.831  1.00 17.61 ? 143 ARG F NH1 1 
ATOM   2262 N  NH2 . ARG B 1 143 ? 15.326 16.004  13.532  1.00 14.43 ? 143 ARG F NH2 1 
ATOM   2263 N  N   . LEU B 1 144 ? 10.336 12.929  6.073   1.00 12.20 ? 144 LEU F N   1 
ATOM   2264 C  CA  . LEU B 1 144 ? 9.355  12.139  5.320   1.00 12.30 ? 144 LEU F CA  1 
ATOM   2265 C  C   . LEU B 1 144 ? 9.431  10.655  5.634   1.00 12.37 ? 144 LEU F C   1 
ATOM   2266 O  O   . LEU B 1 144 ? 8.406  9.979   5.702   1.00 14.64 ? 144 LEU F O   1 
ATOM   2267 C  CB  . LEU B 1 144 ? 9.511  12.342  3.807   1.00 14.14 ? 144 LEU F CB  1 
ATOM   2268 C  CG  . LEU B 1 144 ? 9.187  13.726  3.247   1.00 16.99 ? 144 LEU F CG  1 
ATOM   2269 C  CD1 . LEU B 1 144 ? 9.341  13.697  1.734   1.00 18.77 ? 144 LEU F CD1 1 
ATOM   2270 C  CD2 . LEU B 1 144 ? 7.793  14.193  3.638   1.00 20.07 ? 144 LEU F CD2 1 
ATOM   2271 N  N   . ALA B 1 145 ? 10.648 10.158  5.789   1.00 11.32 ? 145 ALA F N   1 
ATOM   2272 C  CA  . ALA B 1 145 ? 10.880 8.749   6.036   1.00 11.05 ? 145 ALA F CA  1 
ATOM   2273 C  C   . ALA B 1 145 ? 12.244 8.571   6.648   1.00 9.93  ? 145 ALA F C   1 
ATOM   2274 O  O   . ALA B 1 145 ? 13.157 9.366   6.430   1.00 11.70 ? 145 ALA F O   1 
ATOM   2275 C  CB  . ALA B 1 145 ? 10.770 7.961   4.735   1.00 12.11 ? 145 ALA F CB  1 
ATOM   2276 N  N   . CYS B 1 146 ? 12.377 7.505   7.420   1.00 9.88  ? 146 CYS F N   1 
ATOM   2277 C  CA  . CYS B 1 146 ? 13.609 7.212   8.085   1.00 10.57 ? 146 CYS F CA  1 
ATOM   2278 C  C   . CYS B 1 146 ? 13.703 5.740   8.402   1.00 9.72  ? 146 CYS F C   1 
ATOM   2279 O  O   . CYS B 1 146 ? 12.715 5.001   8.307   1.00 10.58 ? 146 CYS F O   1 
ATOM   2280 C  CB  . CYS B 1 146 ? 13.707 8.002   9.384   1.00 13.26 ? 146 CYS F CB  1 
ATOM   2281 S  SG  . CYS B 1 146 ? 12.371 7.662   10.560  1.00 17.20 ? 146 CYS F SG  1 
ATOM   2282 N  N   . GLY B 1 147 ? 14.902 5.345   8.782   1.00 9.24  ? 147 GLY F N   1 
ATOM   2283 C  CA  . GLY B 1 147 ? 15.134 4.013   9.313   1.00 9.48  ? 147 GLY F CA  1 
ATOM   2284 C  C   . GLY B 1 147 ? 16.473 3.941   10.003  1.00 8.58  ? 147 GLY F C   1 
ATOM   2285 O  O   . GLY B 1 147 ? 17.308 4.834   9.846   1.00 10.42 ? 147 GLY F O   1 
ATOM   2286 N  N   . VAL B 1 148 ? 16.665 2.896   10.793  1.00 9.29  ? 148 VAL F N   1 
ATOM   2287 C  CA  . VAL B 1 148 ? 17.898 2.697   11.532  1.00 9.26  ? 148 VAL F CA  1 
ATOM   2288 C  C   . VAL B 1 148 ? 18.898 1.975   10.617  1.00 9.23  ? 148 VAL F C   1 
ATOM   2289 O  O   . VAL B 1 148 ? 18.549 1.013   9.934   1.00 12.37 ? 148 VAL F O   1 
ATOM   2290 C  CB  . VAL B 1 148 ? 17.642 1.904   12.829  1.00 10.05 ? 148 VAL F CB  1 
ATOM   2291 C  CG1 . VAL B 1 148 ? 18.934 1.722   13.608  1.00 11.22 ? 148 VAL F CG1 1 
ATOM   2292 C  CG2 . VAL B 1 148 ? 16.581 2.581   13.690  1.00 11.35 ? 148 VAL F CG2 1 
ATOM   2293 N  N   . ILE B 1 149 ? 20.148 2.426   10.624  1.00 8.90  ? 149 ILE F N   1 
ATOM   2294 C  CA  . ILE B 1 149 ? 21.184 1.850   9.762   1.00 9.30  ? 149 ILE F CA  1 
ATOM   2295 C  C   . ILE B 1 149 ? 21.731 0.604   10.467  1.00 9.22  ? 149 ILE F C   1 
ATOM   2296 O  O   . ILE B 1 149 ? 22.266 0.686   11.573  1.00 10.33 ? 149 ILE F O   1 
ATOM   2297 C  CB  . ILE B 1 149 ? 22.299 2.884   9.494   1.00 9.66  ? 149 ILE F CB  1 
ATOM   2298 C  CG1 . ILE B 1 149 ? 21.717 4.106   8.764   1.00 10.49 ? 149 ILE F CG1 1 
ATOM   2299 C  CG2 . ILE B 1 149 ? 23.433 2.271   8.681   1.00 10.38 ? 149 ILE F CG2 1 
ATOM   2300 C  CD1 . ILE B 1 149 ? 22.640 5.309   8.711   1.00 11.14 ? 149 ILE F CD1 1 
ATOM   2301 N  N   . GLY B 1 150 ? 21.618 -0.538  9.801   1.00 8.45  ? 150 GLY F N   1 
ATOM   2302 C  CA  . GLY B 1 150 ? 22.022 -1.813  10.395  1.00 8.79  ? 150 GLY F CA  1 
ATOM   2303 C  C   . GLY B 1 150 ? 23.147 -2.497  9.658   1.00 9.97  ? 150 GLY F C   1 
ATOM   2304 O  O   . GLY B 1 150 ? 23.415 -2.208  8.497   1.00 10.92 ? 150 GLY F O   1 
ATOM   2305 N  N   . ILE B 1 151 ? 23.821 -3.398  10.359  1.00 9.97  ? 151 ILE F N   1 
ATOM   2306 C  CA  . ILE B 1 151 ? 24.885 -4.196  9.766   1.00 10.98 ? 151 ILE F CA  1 
ATOM   2307 C  C   . ILE B 1 151 ? 24.285 -5.177  8.758   1.00 10.51 ? 151 ILE F C   1 
ATOM   2308 O  O   . ILE B 1 151 ? 23.310 -5.869  9.052   1.00 11.83 ? 151 ILE F O   1 
ATOM   2309 C  CB  . ILE B 1 151 ? 25.638 -4.985  10.851  1.00 12.64 ? 151 ILE F CB  1 
ATOM   2310 C  CG1 . ILE B 1 151 ? 26.402 -4.029  11.769  1.00 13.84 ? 151 ILE F CG1 1 
ATOM   2311 C  CG2 . ILE B 1 151 ? 26.567 -6.024  10.224  1.00 13.61 ? 151 ILE F CG2 1 
ATOM   2312 C  CD1 . ILE B 1 151 ? 26.806 -4.670  13.075  1.00 16.06 ? 151 ILE F CD1 1 
ATOM   2313 N  N   . ALA B 1 152 ? 24.895 -5.235  7.576   1.00 10.88 ? 152 ALA F N   1 
ATOM   2314 C  CA  . ALA B 1 152 ? 24.493 -6.161  6.530   1.00 12.01 ? 152 ALA F CA  1 
ATOM   2315 C  C   . ALA B 1 152 ? 25.560 -7.237  6.319   1.00 14.05 ? 152 ALA F C   1 
ATOM   2316 O  O   . ALA B 1 152 ? 26.717 -7.103  6.720   1.00 15.00 ? 152 ALA F O   1 
ATOM   2317 C  CB  . ALA B 1 152 ? 24.224 -5.406  5.235   1.00 12.08 ? 152 ALA F CB  1 
ATOM   2318 N  N   . GLN B 1 153 ? 25.155 -8.317  5.674   1.00 14.42 ? 153 GLN F N   1 
ATOM   2319 C  CA  . GLN B 1 153 ? 26.094 -9.385  5.371   1.00 16.57 ? 153 GLN F CA  1 
ATOM   2320 C  C   . GLN B 1 153 ? 27.118 -8.942  4.340   1.00 21.01 ? 153 GLN F C   1 
ATOM   2321 O  O   . GLN B 1 153 ? 26.807 -8.192  3.411   1.00 26.24 ? 153 GLN F O   1 
ATOM   2322 C  CB  . GLN B 1 153 ? 25.353 -10.587 4.834   1.00 16.19 ? 153 GLN F CB  1 
ATOM   2323 C  CG  . GLN B 1 153 ? 26.231 -11.796 4.587   1.00 16.13 ? 153 GLN F CG  1 
ATOM   2324 C  CD  . GLN B 1 153 ? 25.399 -12.976 4.216   1.00 17.85 ? 153 GLN F CD  1 
ATOM   2325 O  OE1 . GLN B 1 153 ? 25.293 -13.340 3.051   1.00 28.94 ? 153 GLN F OE1 1 
ATOM   2326 N  NE2 . GLN B 1 153 ? 24.806 -13.551 5.174   1.00 18.09 ? 153 GLN F NE2 1 
ATOM   2327 O  OXT . GLN B 1 153 ? 28.274 -9.356  4.429   1.00 26.53 ? 153 GLN F OXT 1 
HETATM 2328 ZN ZN  . ZN  C 2 .   ? 20.927 -18.985 19.561  1.00 9.39  ? 501 ZN  A ZN  1 
HETATM 2329 C  C11 . 9JK D 3 .   ? 34.219 -1.546  18.202  0.80 35.00 ? 502 9JK A C11 1 
HETATM 2330 C  C12 . 9JK D 3 .   ? 35.236 -2.498  17.966  0.80 39.82 ? 502 9JK A C12 1 
HETATM 2331 C  C13 . 9JK D 3 .   ? 36.530 -2.307  18.463  0.80 44.26 ? 502 9JK A C13 1 
HETATM 2332 C  C14 . 9JK D 3 .   ? 36.846 -1.150  19.182  0.80 47.39 ? 502 9JK A C14 1 
HETATM 2333 C  C15 . 9JK D 3 .   ? 35.863 -0.194  19.405  0.80 44.01 ? 502 9JK A C15 1 
HETATM 2334 S  S01 . 9JK D 3 .   ? 28.834 -1.263  19.462  0.80 21.67 ? 502 9JK A S01 1 
HETATM 2335 C  C02 . 9JK D 3 .   ? 29.113 -1.561  17.743  0.80 22.89 ? 502 9JK A C02 1 
HETATM 2336 C  C03 . 9JK D 3 .   ? 28.020 -1.815  16.917  0.80 22.46 ? 502 9JK A C03 1 
HETATM 2337 C  C04 . 9JK D 3 .   ? 28.154 -2.059  15.540  0.80 20.85 ? 502 9JK A C04 1 
HETATM 2338 C  C05 . 9JK D 3 .   ? 29.424 -2.050  14.980  0.80 22.51 ? 502 9JK A C05 1 
HETATM 2339 C  C06 . 9JK D 3 .   ? 30.521 -1.800  15.821  0.80 25.39 ? 502 9JK A C06 1 
HETATM 2340 C  C07 . 9JK D 3 .   ? 30.410 -1.568  17.213  0.80 24.47 ? 502 9JK A C07 1 
HETATM 2341 C  C08 . 9JK D 3 .   ? 31.664 -1.292  17.986  0.80 27.63 ? 502 9JK A C08 1 
HETATM 2342 O  O09 . 9JK D 3 .   ? 31.591 -0.572  19.010  0.80 25.88 ? 502 9JK A O09 1 
HETATM 2343 N  N10 . 9JK D 3 .   ? 32.937 -1.761  17.639  0.80 29.23 ? 502 9JK A N10 1 
HETATM 2344 C  C16 . 9JK D 3 .   ? 34.579 -0.388  18.909  0.80 39.64 ? 502 9JK A C16 1 
HETATM 2345 ZN ZN  . ZN  E 2 .   ? 15.383 -16.129 16.334  0.60 9.14  ? 503 ZN  A ZN  1 
HETATM 2346 S  S   . SO4 F 4 .   ? 15.374 -18.456 14.180  0.70 13.77 ? 504 SO4 A S   1 
HETATM 2347 O  O1  . SO4 F 4 .   ? 16.673 -18.749 13.564  0.70 19.59 ? 504 SO4 A O1  1 
HETATM 2348 O  O2  . SO4 F 4 .   ? 14.597 -17.594 13.279  0.70 14.17 ? 504 SO4 A O2  1 
HETATM 2349 O  O3  . SO4 F 4 .   ? 14.601 -19.705 14.367  0.70 18.06 ? 504 SO4 A O3  1 
HETATM 2350 O  O4  . SO4 F 4 .   ? 15.646 -17.910 15.506  0.70 10.98 ? 504 SO4 A O4  1 
HETATM 2351 ZN ZN  . ZN  G 2 .   ? 23.874 18.959  9.127   1.00 10.26 ? 501 ZN  F ZN  1 
HETATM 2352 ZN ZN  . ZN  H 2 .   ? 17.405 16.039  8.780   0.50 10.94 ? 502 ZN  F ZN  1 
HETATM 2353 C  C11 . 9JK I 3 .   ? 33.527 3.857   17.929  0.80 27.35 ? 503 9JK F C11 1 
HETATM 2354 C  C12 . 9JK I 3 .   ? 34.632 2.977   17.753  0.80 27.39 ? 503 9JK F C12 1 
HETATM 2355 C  C13 . 9JK I 3 .   ? 35.942 3.365   18.068  0.80 26.99 ? 503 9JK F C13 1 
HETATM 2356 C  C14 . 9JK I 3 .   ? 36.205 4.630   18.585  0.80 28.23 ? 503 9JK F C14 1 
HETATM 2357 C  C15 . 9JK I 3 .   ? 35.138 5.507   18.776  0.80 29.82 ? 503 9JK F C15 1 
HETATM 2358 S  S01 . 9JK I 3 .   ? 30.542 1.389   14.076  0.80 20.85 ? 503 9JK F S01 1 
HETATM 2359 C  C02 . 9JK I 3 .   ? 29.591 1.637   15.573  0.80 24.78 ? 503 9JK F C02 1 
HETATM 2360 C  C03 . 9JK I 3 .   ? 28.220 1.418   15.538  0.80 25.55 ? 503 9JK F C03 1 
HETATM 2361 C  C04 . 9JK I 3 .   ? 27.404 1.595   16.662  0.80 27.55 ? 503 9JK F C04 1 
HETATM 2362 C  C05 . 9JK I 3 .   ? 27.974 2.004   17.861  0.80 27.60 ? 503 9JK F C05 1 
HETATM 2363 C  C06 . 9JK I 3 .   ? 29.356 2.232   17.897  0.80 26.69 ? 503 9JK F C06 1 
HETATM 2364 C  C07 . 9JK I 3 .   ? 30.193 2.066   16.780  0.80 25.66 ? 503 9JK F C07 1 
HETATM 2365 C  C08 . 9JK I 3 .   ? 31.621 2.329   16.978  0.80 25.58 ? 503 9JK F C08 1 
HETATM 2366 O  O09 . 9JK I 3 .   ? 32.410 1.448   16.582  0.80 25.61 ? 503 9JK F O09 1 
HETATM 2367 N  N10 . 9JK I 3 .   ? 32.169 3.468   17.625  0.80 25.26 ? 503 9JK F N10 1 
HETATM 2368 C  C16 . 9JK I 3 .   ? 33.827 5.123   18.459  0.80 28.06 ? 503 9JK F C16 1 
HETATM 2369 S  S   . SO4 J 4 .   ? 16.197 18.369  10.611  0.70 17.67 ? 504 SO4 F S   1 
HETATM 2370 O  O1  . SO4 J 4 .   ? 17.176 17.880  9.636   0.70 14.57 ? 504 SO4 F O1  1 
HETATM 2371 O  O2  . SO4 J 4 .   ? 15.552 19.565  10.009  0.70 21.18 ? 504 SO4 F O2  1 
HETATM 2372 O  O3  . SO4 J 4 .   ? 16.951 18.759  11.817  0.70 22.82 ? 504 SO4 F O3  1 
HETATM 2373 O  O4  . SO4 J 4 .   ? 15.115 17.437  10.957  0.70 19.98 ? 504 SO4 F O4  1 
HETATM 2374 O  O   . HOH K 5 .   ? 5.630  -0.615  16.295  1.00 39.75 ? 601 HOH A O   1 
HETATM 2375 O  O   . HOH K 5 .   ? 18.880 15.297  26.849  1.00 37.73 ? 602 HOH A O   1 
HETATM 2376 O  O   . HOH K 5 .   ? 17.194 -14.691 8.072   1.00 22.11 ? 603 HOH A O   1 
HETATM 2377 O  O   . HOH K 5 .   ? 18.407 -18.659 11.870  1.00 33.04 ? 604 HOH A O   1 
HETATM 2378 O  O   . HOH K 5 .   ? 30.922 -25.246 31.691  1.00 36.41 ? 605 HOH A O   1 
HETATM 2379 O  O   . HOH K 5 .   ? 35.293 -11.203 22.383  1.00 29.57 ? 606 HOH A O   1 
HETATM 2380 O  O   . HOH K 5 .   ? 28.842 -25.580 28.646  1.00 30.24 ? 607 HOH A O   1 
HETATM 2381 O  O   . HOH K 5 .   ? 30.825 -24.620 20.803  1.00 42.35 ? 608 HOH A O   1 
HETATM 2382 O  O   . HOH K 5 .   ? 14.148 -20.341 17.079  1.00 19.89 ? 609 HOH A O   1 
HETATM 2383 O  O   . HOH K 5 .   ? 28.794 1.843   21.593  1.00 37.14 ? 610 HOH A O   1 
HETATM 2384 O  O   . HOH K 5 .   ? 10.335 -14.562 30.579  1.00 32.20 ? 611 HOH A O   1 
HETATM 2385 O  O   . HOH K 5 .   ? 1.892  -18.932 23.255  1.00 37.37 ? 612 HOH A O   1 
HETATM 2386 O  O   . HOH K 5 .   ? 33.563 -20.475 29.787  1.00 43.50 ? 613 HOH A O   1 
HETATM 2387 O  O   . HOH K 5 .   ? 31.999 -4.679  25.919  1.00 36.21 ? 614 HOH A O   1 
HETATM 2388 O  O   . HOH K 5 .   ? 10.969 -3.649  6.605   1.00 44.21 ? 615 HOH A O   1 
HETATM 2389 O  O   . HOH K 5 .   ? 36.040 -8.135  23.277  0.50 10.14 ? 616 HOH A O   1 
HETATM 2390 O  O   . HOH K 5 .   ? 5.683  -10.374 31.221  1.00 27.42 ? 617 HOH A O   1 
HETATM 2391 O  O   . HOH K 5 .   ? 29.890 -26.557 25.543  1.00 39.27 ? 618 HOH A O   1 
HETATM 2392 O  O   . HOH K 5 .   ? 3.661  -5.200  13.897  1.00 28.34 ? 619 HOH A O   1 
HETATM 2393 O  O   . HOH K 5 .   ? -5.203 -8.016  33.224  1.00 39.46 ? 620 HOH A O   1 
HETATM 2394 O  O   . HOH K 5 .   ? 12.377 -19.814 12.881  1.00 44.18 ? 621 HOH A O   1 
HETATM 2395 O  O   . HOH K 5 .   ? 34.618 -18.993 26.966  1.00 52.93 ? 622 HOH A O   1 
HETATM 2396 O  O   . HOH K 5 .   ? 19.309 -24.457 28.614  1.00 29.69 ? 623 HOH A O   1 
HETATM 2397 O  O   . HOH K 5 .   ? 27.089 -4.938  16.433  1.00 24.71 ? 624 HOH A O   1 
HETATM 2398 O  O   . HOH K 5 .   ? 28.460 -7.081  28.713  1.00 36.98 ? 625 HOH A O   1 
HETATM 2399 O  O   . HOH K 5 .   ? 34.087 -20.257 13.668  1.00 47.57 ? 626 HOH A O   1 
HETATM 2400 O  O   . HOH K 5 .   ? 14.360 0.058   15.974  1.00 9.32  ? 627 HOH A O   1 
HETATM 2401 O  O   . HOH K 5 .   ? 21.839 -28.421 25.072  1.00 37.03 ? 628 HOH A O   1 
HETATM 2402 O  O   . HOH K 5 .   ? -0.596 -16.219 32.734  1.00 15.37 ? 629 HOH A O   1 
HETATM 2403 O  O   . HOH K 5 .   ? -1.664 -7.053  30.964  1.00 28.84 ? 630 HOH A O   1 
HETATM 2404 O  O   . HOH K 5 .   ? 12.700 -2.779  10.719  1.00 37.97 ? 631 HOH A O   1 
HETATM 2405 O  O   . HOH K 5 .   ? 34.714 -16.379 24.383  1.00 27.95 ? 632 HOH A O   1 
HETATM 2406 O  O   . HOH K 5 .   ? -7.424 -12.278 28.186  1.00 51.22 ? 633 HOH A O   1 
HETATM 2407 O  O   . HOH K 5 .   ? 23.412 -25.396 31.245  1.00 65.92 ? 634 HOH A O   1 
HETATM 2408 O  O   . HOH K 5 .   ? 33.081 -3.813  33.434  1.00 50.84 ? 635 HOH A O   1 
HETATM 2409 O  O   . HOH K 5 .   ? 23.460 -22.617 33.847  1.00 94.40 ? 636 HOH A O   1 
HETATM 2410 O  O   . HOH K 5 .   ? 13.756 -22.285 14.201  1.00 45.43 ? 637 HOH A O   1 
HETATM 2411 O  O   . HOH K 5 .   ? 11.085 -1.567  13.490  1.00 19.65 ? 638 HOH A O   1 
HETATM 2412 O  O   . HOH K 5 .   ? 15.565 -14.092 29.370  1.00 17.95 ? 639 HOH A O   1 
HETATM 2413 O  O   . HOH K 5 .   ? 16.160 -8.546  1.641   1.00 26.14 ? 640 HOH A O   1 
HETATM 2414 O  O   . HOH K 5 .   ? 28.700 -16.832 22.766  1.00 14.23 ? 641 HOH A O   1 
HETATM 2415 O  O   . HOH K 5 .   ? 0.537  -13.084 17.957  1.00 22.53 ? 642 HOH A O   1 
HETATM 2416 O  O   . HOH K 5 .   ? 9.720  -24.696 21.003  1.00 21.59 ? 643 HOH A O   1 
HETATM 2417 O  O   . HOH K 5 .   ? 9.059  -8.625  33.760  1.00 45.94 ? 644 HOH A O   1 
HETATM 2418 O  O   . HOH K 5 .   ? 28.501 -16.177 20.166  1.00 10.62 ? 645 HOH A O   1 
HETATM 2419 O  O   . HOH K 5 .   ? 23.988 5.984   24.398  1.00 17.62 ? 646 HOH A O   1 
HETATM 2420 O  O   . HOH K 5 .   ? 10.568 -3.741  11.804  1.00 44.63 ? 647 HOH A O   1 
HETATM 2421 O  O   . HOH K 5 .   ? 16.416 3.276   25.357  1.00 19.91 ? 648 HOH A O   1 
HETATM 2422 O  O   . HOH K 5 .   ? 5.435  -10.618 11.290  1.00 39.46 ? 649 HOH A O   1 
HETATM 2423 O  O   . HOH K 5 .   ? 12.929 4.901   25.530  1.00 31.79 ? 650 HOH A O   1 
HETATM 2424 O  O   . HOH K 5 .   ? 34.479 -19.178 21.500  1.00 38.24 ? 651 HOH A O   1 
HETATM 2425 O  O   . HOH K 5 .   ? 31.247 -8.931  16.362  1.00 31.80 ? 652 HOH A O   1 
HETATM 2426 O  O   . HOH K 5 .   ? 7.380  -16.933 32.668  1.00 17.23 ? 653 HOH A O   1 
HETATM 2427 O  O   . HOH K 5 .   ? 2.938  -8.850  31.255  1.00 26.91 ? 654 HOH A O   1 
HETATM 2428 O  O   . HOH K 5 .   ? 9.481  -3.971  32.118  1.00 23.79 ? 655 HOH A O   1 
HETATM 2429 O  O   . HOH K 5 .   ? 23.867 7.746   26.584  1.00 39.97 ? 656 HOH A O   1 
HETATM 2430 O  O   . HOH K 5 .   ? 19.803 -12.097 35.274  1.00 40.81 ? 657 HOH A O   1 
HETATM 2431 O  O   . HOH K 5 .   ? 32.003 -6.587  23.339  1.00 19.69 ? 658 HOH A O   1 
HETATM 2432 O  O   . HOH K 5 .   ? 29.313 -17.861 27.464  1.00 16.26 ? 659 HOH A O   1 
HETATM 2433 O  O   . HOH K 5 .   ? 20.221 -12.828 30.891  1.00 17.80 ? 660 HOH A O   1 
HETATM 2434 O  O   . HOH K 5 .   ? 2.427  -17.347 18.876  1.00 25.63 ? 661 HOH A O   1 
HETATM 2435 O  O   . HOH K 5 .   ? 26.748 -2.044  33.065  1.00 20.51 ? 662 HOH A O   1 
HETATM 2436 O  O   . HOH K 5 .   ? 21.059 -19.685 15.194  1.00 32.10 ? 663 HOH A O   1 
HETATM 2437 O  O   . HOH K 5 .   ? 29.507 -16.250 25.259  1.00 22.08 ? 664 HOH A O   1 
HETATM 2438 O  O   . HOH K 5 .   ? 23.702 -24.954 24.799  1.00 25.10 ? 665 HOH A O   1 
HETATM 2439 O  O   . HOH K 5 .   ? 18.054 2.778   27.315  1.00 32.10 ? 666 HOH A O   1 
HETATM 2440 O  O   . HOH K 5 .   ? 11.164 -27.385 21.244  1.00 22.86 ? 667 HOH A O   1 
HETATM 2441 O  O   . HOH K 5 .   ? 26.781 -14.262 13.959  1.00 17.27 ? 668 HOH A O   1 
HETATM 2442 O  O   . HOH K 5 .   ? 20.443 -10.479 4.802   1.00 35.95 ? 669 HOH A O   1 
HETATM 2443 O  O   . HOH K 5 .   ? 17.997 -18.199 24.014  1.00 11.69 ? 670 HOH A O   1 
HETATM 2444 O  O   . HOH K 5 .   ? 22.360 -8.466  4.905   1.00 23.44 ? 671 HOH A O   1 
HETATM 2445 O  O   . HOH K 5 .   ? 17.587 -2.706  7.736   1.00 13.11 ? 672 HOH A O   1 
HETATM 2446 O  O   . HOH K 5 .   ? 2.940  -2.768  29.510  1.00 44.52 ? 673 HOH A O   1 
HETATM 2447 O  O   . HOH K 5 .   ? 5.817  -20.685 14.489  1.00 20.43 ? 674 HOH A O   1 
HETATM 2448 O  O   . HOH K 5 .   ? 19.943 -22.344 31.875  1.00 35.32 ? 675 HOH A O   1 
HETATM 2449 O  O   . HOH K 5 .   ? 25.709 -17.069 30.192  1.00 16.94 ? 676 HOH A O   1 
HETATM 2450 O  O   . HOH K 5 .   ? 14.272 -11.968 33.257  1.00 31.18 ? 677 HOH A O   1 
HETATM 2451 O  O   . HOH K 5 .   ? 3.191  -9.678  14.208  1.00 47.08 ? 678 HOH A O   1 
HETATM 2452 O  O   . HOH K 5 .   ? 4.018  1.514   12.375  1.00 41.09 ? 679 HOH A O   1 
HETATM 2453 O  O   . HOH K 5 .   ? 26.021 -20.284 14.253  1.00 19.47 ? 680 HOH A O   1 
HETATM 2454 O  O   . HOH K 5 .   ? 18.219 -30.890 22.950  1.00 29.77 ? 681 HOH A O   1 
HETATM 2455 O  O   . HOH K 5 .   ? 29.855 -8.015  12.203  1.00 53.86 ? 682 HOH A O   1 
HETATM 2456 O  O   . HOH K 5 .   ? 31.435 1.621   20.861  1.00 36.43 ? 683 HOH A O   1 
HETATM 2457 O  O   . HOH K 5 .   ? 12.027 -23.242 27.366  1.00 27.14 ? 684 HOH A O   1 
HETATM 2458 O  O   . HOH K 5 .   ? 12.669 -19.236 29.317  1.00 23.57 ? 685 HOH A O   1 
HETATM 2459 O  O   . HOH K 5 .   ? 21.514 -25.710 26.484  1.00 35.87 ? 686 HOH A O   1 
HETATM 2460 O  O   . HOH K 5 .   ? 23.799 -1.690  33.284  1.00 31.24 ? 687 HOH A O   1 
HETATM 2461 O  O   . HOH K 5 .   ? 16.261 -36.627 18.156  1.00 22.78 ? 688 HOH A O   1 
HETATM 2462 O  O   . HOH K 5 .   ? 28.140 -9.837  11.352  1.00 33.00 ? 689 HOH A O   1 
HETATM 2463 O  O   . HOH K 5 .   ? 0.400  1.692   20.702  1.00 40.37 ? 690 HOH A O   1 
HETATM 2464 O  O   . HOH K 5 .   ? -5.717 -7.782  25.677  1.00 26.43 ? 691 HOH A O   1 
HETATM 2465 O  O   . HOH K 5 .   ? 9.798  -5.944  10.595  1.00 49.56 ? 692 HOH A O   1 
HETATM 2466 O  O   . HOH K 5 .   ? 34.517 -17.302 16.720  1.00 40.83 ? 693 HOH A O   1 
HETATM 2467 O  O   . HOH K 5 .   ? 9.496  -16.155 10.135  1.00 22.56 ? 694 HOH A O   1 
HETATM 2468 O  O   . HOH K 5 .   ? 13.260 -13.178 30.441  1.00 24.61 ? 695 HOH A O   1 
HETATM 2469 O  O   . HOH K 5 .   ? 35.528 -5.972  21.904  1.00 30.73 ? 696 HOH A O   1 
HETATM 2470 O  O   . HOH K 5 .   ? 8.917  -11.072 29.733  1.00 16.72 ? 697 HOH A O   1 
HETATM 2471 O  O   . HOH K 5 .   ? 23.665 -13.154 31.461  1.00 17.66 ? 698 HOH A O   1 
HETATM 2472 O  O   . HOH K 5 .   ? 29.580 -6.670  17.365  1.00 27.81 ? 699 HOH A O   1 
HETATM 2473 O  O   . HOH K 5 .   ? 4.170  -2.446  23.714  1.00 33.31 ? 700 HOH A O   1 
HETATM 2474 O  O   . HOH K 5 .   ? 33.062 2.389   31.457  1.00 51.01 ? 701 HOH A O   1 
HETATM 2475 O  O   . HOH K 5 .   ? 17.051 4.644   32.280  1.00 46.58 ? 702 HOH A O   1 
HETATM 2476 O  O   . HOH K 5 .   ? 6.108  -0.510  18.722  1.00 28.29 ? 703 HOH A O   1 
HETATM 2477 O  O   . HOH K 5 .   ? 24.012 8.641   22.144  1.00 30.60 ? 704 HOH A O   1 
HETATM 2478 O  O   . HOH K 5 .   ? -1.635 -5.393  19.202  1.00 66.67 ? 705 HOH A O   1 
HETATM 2479 O  O   . HOH K 5 .   ? 37.670 -4.699  30.648  1.00 50.17 ? 706 HOH A O   1 
HETATM 2480 O  O   . HOH K 5 .   ? 28.960 1.700   28.963  1.00 35.51 ? 707 HOH A O   1 
HETATM 2481 O  O   . HOH K 5 .   ? -7.105 -14.195 26.431  1.00 35.35 ? 708 HOH A O   1 
HETATM 2482 O  O   . HOH K 5 .   ? 16.063 -31.156 14.097  1.00 26.81 ? 709 HOH A O   1 
HETATM 2483 O  O   . HOH K 5 .   ? 23.628 10.946  23.985  1.00 35.01 ? 710 HOH A O   1 
HETATM 2484 O  O   . HOH K 5 .   ? 6.422  -23.407 22.072  1.00 25.24 ? 711 HOH A O   1 
HETATM 2485 O  O   . HOH K 5 .   ? 2.012  -15.081 19.357  1.00 16.90 ? 712 HOH A O   1 
HETATM 2486 O  O   . HOH K 5 .   ? 11.332 -23.392 14.476  1.00 29.83 ? 713 HOH A O   1 
HETATM 2487 O  O   . HOH K 5 .   ? 13.888 -0.791  13.114  1.00 12.93 ? 714 HOH A O   1 
HETATM 2488 O  O   . HOH K 5 .   ? 8.514  -9.456  8.897   1.00 31.84 ? 715 HOH A O   1 
HETATM 2489 O  O   . HOH K 5 .   ? 23.491 -10.358 34.218  1.00 36.51 ? 716 HOH A O   1 
HETATM 2490 O  O   . HOH K 5 .   ? 24.734 -22.716 15.951  1.00 11.84 ? 717 HOH A O   1 
HETATM 2491 O  O   . HOH K 5 .   ? 11.032 -14.040 8.803   1.00 56.52 ? 718 HOH A O   1 
HETATM 2492 O  O   . HOH K 5 .   ? 16.901 8.194   25.147  1.00 35.01 ? 719 HOH A O   1 
HETATM 2493 O  O   . HOH K 5 .   ? 35.130 -4.376  24.635  1.00 36.78 ? 720 HOH A O   1 
HETATM 2494 O  O   . HOH K 5 .   ? -4.842 -15.450 25.943  1.00 29.90 ? 721 HOH A O   1 
HETATM 2495 O  O   . HOH K 5 .   ? 4.640  -6.073  34.881  1.00 32.26 ? 722 HOH A O   1 
HETATM 2496 O  O   . HOH K 5 .   ? 16.391 10.906  21.551  1.00 32.47 ? 723 HOH A O   1 
HETATM 2497 O  O   . HOH K 5 .   ? 17.362 -11.677 33.485  1.00 18.50 ? 724 HOH A O   1 
HETATM 2498 O  O   . HOH K 5 .   ? 20.560 -19.316 13.219  1.00 32.78 ? 725 HOH A O   1 
HETATM 2499 O  O   . HOH K 5 .   ? 18.833 -20.002 30.609  1.00 15.00 ? 726 HOH A O   1 
HETATM 2500 O  O   . HOH K 5 .   ? -3.332 -13.419 24.454  1.00 35.59 ? 727 HOH A O   1 
HETATM 2501 O  O   . HOH K 5 .   ? 15.790 -4.587  33.545  1.00 38.16 ? 728 HOH A O   1 
HETATM 2502 O  O   . HOH K 5 .   ? 2.430  -22.012 17.495  1.00 42.26 ? 729 HOH A O   1 
HETATM 2503 O  O   . HOH K 5 .   ? -3.126 -10.901 32.017  1.00 33.74 ? 730 HOH A O   1 
HETATM 2504 O  O   . HOH K 5 .   ? 30.608 -9.631  27.602  1.00 73.63 ? 731 HOH A O   1 
HETATM 2505 O  O   . HOH K 5 .   ? 4.407  -0.937  21.249  1.00 20.53 ? 732 HOH A O   1 
HETATM 2506 O  O   . HOH K 5 .   ? 11.595 -15.594 3.073   1.00 37.36 ? 733 HOH A O   1 
HETATM 2507 O  O   . HOH K 5 .   ? 8.736  -20.899 11.290  1.00 49.06 ? 734 HOH A O   1 
HETATM 2508 O  O   . HOH K 5 .   ? 16.415 -6.766  35.213  1.00 51.81 ? 735 HOH A O   1 
HETATM 2509 O  O   . HOH K 5 .   ? 11.545 -10.714 30.611  1.00 9.67  ? 736 HOH A O   1 
HETATM 2510 O  O   . HOH K 5 .   ? 14.793 -17.249 29.512  1.00 16.05 ? 737 HOH A O   1 
HETATM 2511 O  O   . HOH K 5 .   ? 23.603 -20.946 35.877  1.00 58.87 ? 738 HOH A O   1 
HETATM 2512 O  O   . HOH K 5 .   ? 19.034 -34.332 19.843  1.00 43.34 ? 739 HOH A O   1 
HETATM 2513 O  O   . HOH K 5 .   ? 12.670 -16.209 8.703   1.00 39.32 ? 740 HOH A O   1 
HETATM 2514 O  O   . HOH K 5 .   ? 17.688 -30.116 11.720  1.00 31.38 ? 741 HOH A O   1 
HETATM 2515 O  O   . HOH K 5 .   ? 33.766 -1.863  14.067  1.00 36.42 ? 742 HOH A O   1 
HETATM 2516 O  O   . HOH K 5 .   ? 11.211 -28.076 25.794  1.00 81.58 ? 743 HOH A O   1 
HETATM 2517 O  O   . HOH K 5 .   ? 33.543 -11.580 15.690  1.00 40.27 ? 744 HOH A O   1 
HETATM 2518 O  O   . HOH K 5 .   ? 30.380 -10.800 14.120  1.00 38.32 ? 745 HOH A O   1 
HETATM 2519 O  O   . HOH K 5 .   ? 2.132  -12.108 13.517  1.00 43.12 ? 746 HOH A O   1 
HETATM 2520 O  O   . HOH K 5 .   ? 10.115 -28.257 18.840  1.00 33.64 ? 747 HOH A O   1 
HETATM 2521 O  O   . HOH K 5 .   ? 3.375  -12.412 11.315  1.00 40.94 ? 748 HOH A O   1 
HETATM 2522 O  O   . HOH K 5 .   ? 9.882  -25.419 24.024  1.00 27.78 ? 749 HOH A O   1 
HETATM 2523 O  O   . HOH K 5 .   ? 0.698  -19.562 18.261  1.00 40.85 ? 750 HOH A O   1 
HETATM 2524 O  O   . HOH K 5 .   ? 26.860 -2.087  35.993  1.00 34.84 ? 751 HOH A O   1 
HETATM 2525 O  O   . HOH K 5 .   ? 14.572 -22.838 11.612  1.00 39.79 ? 752 HOH A O   1 
HETATM 2526 O  O   . HOH K 5 .   ? 24.276 -26.224 28.154  1.00 30.30 ? 753 HOH A O   1 
HETATM 2527 O  O   . HOH K 5 .   ? 8.883  -5.232  34.540  1.00 32.22 ? 754 HOH A O   1 
HETATM 2528 O  O   . HOH K 5 .   ? 17.621 -13.677 31.170  1.00 18.19 ? 755 HOH A O   1 
HETATM 2529 O  O   . HOH K 5 .   ? 27.047 3.826   20.921  1.00 40.82 ? 756 HOH A O   1 
HETATM 2530 O  O   . HOH K 5 .   ? 5.662  -8.642  35.067  1.00 28.40 ? 757 HOH A O   1 
HETATM 2531 O  O   . HOH K 5 .   ? 4.124  -10.541 33.356  1.00 37.92 ? 758 HOH A O   1 
HETATM 2532 O  O   . HOH K 5 .   ? 18.218 -25.468 12.154  1.00 32.13 ? 759 HOH A O   1 
HETATM 2533 O  O   . HOH K 5 .   ? 10.138 1.026   13.053  1.00 36.23 ? 760 HOH A O   1 
HETATM 2534 O  O   . HOH K 5 .   ? 26.464 6.088   22.837  1.00 33.85 ? 761 HOH A O   1 
HETATM 2535 O  O   . HOH K 5 .   ? 20.160 -21.326 11.806  1.00 46.89 ? 762 HOH A O   1 
HETATM 2536 O  O   . HOH K 5 .   ? -1.658 -12.246 11.931  1.00 46.82 ? 763 HOH A O   1 
HETATM 2537 O  O   . HOH K 5 .   ? 16.481 -18.627 31.146  1.00 34.11 ? 764 HOH A O   1 
HETATM 2538 O  O   . HOH K 5 .   ? 36.260 -13.358 14.391  1.00 33.04 ? 765 HOH A O   1 
HETATM 2539 O  O   . HOH K 5 .   ? 0.841  -13.426 15.291  1.00 38.72 ? 766 HOH A O   1 
HETATM 2540 O  O   . HOH K 5 .   ? 16.995 -15.935 32.558  1.00 33.79 ? 767 HOH A O   1 
HETATM 2541 O  O   . HOH L 5 .   ? 23.865 -5.888  0.814   1.00 42.96 ? 601 HOH F O   1 
HETATM 2542 O  O   . HOH L 5 .   ? 43.083 5.983   7.666   1.00 38.06 ? 602 HOH F O   1 
HETATM 2543 O  O   . HOH L 5 .   ? 14.458 14.608  16.707  0.50 15.87 ? 603 HOH F O   1 
HETATM 2544 O  O   . HOH L 5 .   ? 40.717 3.768   9.668   1.00 40.44 ? 604 HOH F O   1 
HETATM 2545 O  O   . HOH L 5 .   ? 38.147 2.258   -0.931  1.00 30.37 ? 605 HOH F O   1 
HETATM 2546 O  O   . HOH L 5 .   ? 23.815 -8.279  2.428   1.00 33.49 ? 606 HOH F O   1 
HETATM 2547 O  O   . HOH L 5 .   ? 37.843 8.674   1.283   1.00 48.73 ? 607 HOH F O   1 
HETATM 2548 O  O   . HOH L 5 .   ? 35.005 0.714   8.414   1.00 64.23 ? 608 HOH F O   1 
HETATM 2549 O  O   . HOH L 5 .   ? 17.400 18.557  14.289  1.00 40.78 ? 609 HOH F O   1 
HETATM 2550 O  O   . HOH L 5 .   ? 6.523  4.124   4.320   1.00 37.84 ? 610 HOH F O   1 
HETATM 2551 O  O   . HOH L 5 .   ? 30.008 -7.563  4.997   1.00 72.99 ? 611 HOH F O   1 
HETATM 2552 O  O   . HOH L 5 .   ? 34.333 0.604   15.063  1.00 32.15 ? 612 HOH F O   1 
HETATM 2553 O  O   . HOH L 5 .   ? 34.804 9.999   -1.486  1.00 44.75 ? 613 HOH F O   1 
HETATM 2554 O  O   . HOH L 5 .   ? 14.992 22.331  9.266   1.00 41.80 ? 614 HOH F O   1 
HETATM 2555 O  O   . HOH L 5 .   ? 6.333  11.280  4.749   1.00 28.12 ? 615 HOH F O   1 
HETATM 2556 O  O   . HOH L 5 .   ? 17.364 32.899  15.505  1.00 36.02 ? 616 HOH F O   1 
HETATM 2557 O  O   . HOH L 5 .   ? 16.657 20.377  7.578   1.00 26.15 ? 617 HOH F O   1 
HETATM 2558 O  O   . HOH L 5 .   ? 34.287 17.290  3.837   1.00 42.56 ? 618 HOH F O   1 
HETATM 2559 O  O   . HOH L 5 .   ? 21.095 14.477  -5.883  1.00 33.12 ? 619 HOH F O   1 
HETATM 2560 O  O   . HOH L 5 .   ? 9.037  3.489   14.155  1.00 46.21 ? 620 HOH F O   1 
HETATM 2561 O  O   . HOH L 5 .   ? 4.251  9.214   -1.612  1.00 36.95 ? 621 HOH F O   1 
HETATM 2562 O  O   . HOH L 5 .   ? 5.987  12.449  -0.746  1.00 26.58 ? 622 HOH F O   1 
HETATM 2563 O  O   . HOH L 5 .   ? 27.652 24.521  0.679   1.00 33.06 ? 623 HOH F O   1 
HETATM 2564 O  O   . HOH L 5 .   ? 20.800 -4.958  -0.205  1.00 32.39 ? 624 HOH F O   1 
HETATM 2565 O  O   . HOH L 5 .   ? 31.968 -1.766  12.081  1.00 35.84 ? 625 HOH F O   1 
HETATM 2566 O  O   . HOH L 5 .   ? 7.855  18.781  -7.288  0.50 27.93 ? 626 HOH F O   1 
HETATM 2567 O  O   . HOH L 5 .   ? 24.664 13.969  -2.004  1.00 26.27 ? 627 HOH F O   1 
HETATM 2568 O  O   . HOH L 5 .   ? 9.858  18.581  -4.326  1.00 36.43 ? 628 HOH F O   1 
HETATM 2569 O  O   A HOH L 5 .   ? 35.012 1.680   0.083   0.50 31.29 ? 629 HOH F O   1 
HETATM 2570 O  O   B HOH L 5 .   ? 36.058 1.998   1.057   0.50 26.76 ? 629 HOH F O   1 
HETATM 2571 O  O   . HOH L 5 .   ? 33.033 17.208  19.246  1.00 13.45 ? 630 HOH F O   1 
HETATM 2572 O  O   . HOH L 5 .   ? 17.662 10.143  -8.938  1.00 34.41 ? 631 HOH F O   1 
HETATM 2573 O  O   . HOH L 5 .   ? 33.669 15.585  1.454   1.00 36.27 ? 632 HOH F O   1 
HETATM 2574 O  O   . HOH L 5 .   ? 37.160 13.087  4.420   1.00 41.35 ? 633 HOH F O   1 
HETATM 2575 O  O   . HOH L 5 .   ? 11.547 18.601  -2.050  1.00 35.51 ? 634 HOH F O   1 
HETATM 2576 O  O   . HOH L 5 .   ? 29.790 24.799  5.205   1.00 93.53 ? 635 HOH F O   1 
HETATM 2577 O  O   . HOH L 5 .   ? 12.401 1.542   8.800   1.00 23.77 ? 636 HOH F O   1 
HETATM 2578 O  O   . HOH L 5 .   ? 5.748  9.378   8.027   1.00 38.18 ? 637 HOH F O   1 
HETATM 2579 O  O   . HOH L 5 .   ? 16.563 -0.211  8.587   1.00 11.55 ? 638 HOH F O   1 
HETATM 2580 O  O   . HOH L 5 .   ? 23.892 13.342  22.353  1.00 32.81 ? 639 HOH F O   1 
HETATM 2581 O  O   . HOH L 5 .   ? 10.020 8.390   21.644  1.00 24.29 ? 640 HOH F O   1 
HETATM 2582 O  O   . HOH L 5 .   ? 35.088 7.193   5.343   1.00 33.86 ? 641 HOH F O   1 
HETATM 2583 O  O   . HOH L 5 .   ? 17.080 8.360   22.180  1.00 17.24 ? 642 HOH F O   1 
HETATM 2584 O  O   . HOH L 5 .   ? 23.660 -3.382  1.871   1.00 25.98 ? 643 HOH F O   1 
HETATM 2585 O  O   . HOH L 5 .   ? 30.569 16.263  12.773  1.00 10.29 ? 644 HOH F O   1 
HETATM 2586 O  O   . HOH L 5 .   ? 32.198 16.921  10.712  1.00 16.34 ? 645 HOH F O   1 
HETATM 2587 O  O   . HOH L 5 .   ? 36.691 5.147   9.966   1.00 30.10 ? 646 HOH F O   1 
HETATM 2588 O  O   . HOH L 5 .   ? 31.860 12.061  -3.876  1.00 40.24 ? 647 HOH F O   1 
HETATM 2589 O  O   . HOH L 5 .   ? 19.727 16.823  -9.166  1.00 18.65 ? 648 HOH F O   1 
HETATM 2590 O  O   . HOH L 5 .   ? 25.397 14.290  16.766  0.40 9.08  ? 649 HOH F O   1 
HETATM 2591 O  O   . HOH L 5 .   ? 23.860 18.184  3.786   1.00 14.96 ? 650 HOH F O   1 
HETATM 2592 O  O   . HOH L 5 .   ? 19.578 28.696  -0.558  1.00 41.70 ? 651 HOH F O   1 
HETATM 2593 O  O   . HOH L 5 .   ? 7.266  6.992   -6.645  1.00 26.55 ? 652 HOH F O   1 
HETATM 2594 O  O   . HOH L 5 .   ? 15.355 24.643  1.805   1.00 24.12 ? 653 HOH F O   1 
HETATM 2595 O  O   . HOH L 5 .   ? 14.738 2.549   17.232  1.00 12.96 ? 654 HOH F O   1 
HETATM 2596 O  O   . HOH L 5 .   ? 21.289 3.849   -7.617  1.00 33.16 ? 655 HOH F O   1 
HETATM 2597 O  O   . HOH L 5 .   ? 29.263 -6.000  7.041   1.00 21.22 ? 656 HOH F O   1 
HETATM 2598 O  O   . HOH L 5 .   ? 27.986 25.753  3.458   1.00 50.73 ? 657 HOH F O   1 
HETATM 2599 O  O   . HOH L 5 .   ? 13.177 16.105  -13.699 1.00 21.92 ? 658 HOH F O   1 
HETATM 2600 O  O   . HOH L 5 .   ? 27.832 8.142   19.976  1.00 45.10 ? 659 HOH F O   1 
HETATM 2601 O  O   . HOH L 5 .   ? 29.546 12.887  -0.772  1.00 25.83 ? 660 HOH F O   1 
HETATM 2602 O  O   . HOH L 5 .   ? 35.249 6.986   12.111  1.00 17.66 ? 661 HOH F O   1 
HETATM 2603 O  O   . HOH L 5 .   ? 36.158 18.719  16.658  1.00 20.91 ? 662 HOH F O   1 
HETATM 2604 O  O   . HOH L 5 .   ? 29.909 6.835   15.769  1.00 22.66 ? 663 HOH F O   1 
HETATM 2605 O  O   . HOH L 5 .   ? 4.888  12.043  1.795   1.00 38.55 ? 664 HOH F O   1 
HETATM 2606 O  O   . HOH L 5 .   ? 23.328 13.018  -4.054  1.00 30.11 ? 665 HOH F O   1 
HETATM 2607 O  O   . HOH L 5 .   ? 25.302 9.627   19.814  1.00 27.39 ? 666 HOH F O   1 
HETATM 2608 O  O   . HOH L 5 .   ? 16.534 27.334  2.509   1.00 26.33 ? 667 HOH F O   1 
HETATM 2609 O  O   . HOH L 5 .   ? 27.764 4.584   15.469  1.00 40.87 ? 668 HOH F O   1 
HETATM 2610 O  O   . HOH L 5 .   ? 21.593 19.578  12.969  1.00 29.58 ? 669 HOH F O   1 
HETATM 2611 O  O   . HOH L 5 .   ? 37.326 6.862   15.883  1.00 29.36 ? 670 HOH F O   1 
HETATM 2612 O  O   . HOH L 5 .   ? 25.185 20.156  16.309  1.00 13.12 ? 671 HOH F O   1 
HETATM 2613 O  O   . HOH L 5 .   ? 13.433 15.930  16.377  0.50 14.89 ? 672 HOH F O   1 
HETATM 2614 O  O   . HOH L 5 .   ? 23.577 30.688  4.957   1.00 26.85 ? 673 HOH F O   1 
HETATM 2615 O  O   . HOH L 5 .   ? 19.173 36.395  7.900   1.00 27.65 ? 674 HOH F O   1 
HETATM 2616 O  O   . HOH L 5 .   ? 16.854 30.907  11.100  1.00 28.44 ? 675 HOH F O   1 
HETATM 2617 O  O   . HOH L 5 .   ? 20.269 23.441  -2.199  1.00 32.86 ? 676 HOH F O   1 
HETATM 2618 O  O   . HOH L 5 .   ? 25.887 14.170  17.125  0.60 11.70 ? 677 HOH F O   1 
HETATM 2619 O  O   . HOH L 5 .   ? 32.770 24.626  13.842  1.00 77.89 ? 678 HOH F O   1 
HETATM 2620 O  O   . HOH L 5 .   ? 34.601 17.457  6.595   1.00 31.62 ? 679 HOH F O   1 
HETATM 2621 O  O   . HOH L 5 .   ? 22.155 19.191  -3.682  1.00 25.05 ? 680 HOH F O   1 
HETATM 2622 O  O   . HOH L 5 .   ? 7.784  9.899   11.721  1.00 43.29 ? 681 HOH F O   1 
HETATM 2623 O  O   . HOH L 5 .   ? 33.652 24.507  4.278   1.00 28.02 ? 682 HOH F O   1 
HETATM 2624 O  O   . HOH L 5 .   ? 9.285  16.040  10.783  1.00 29.02 ? 683 HOH F O   1 
HETATM 2625 O  O   . HOH L 5 .   ? 15.447 8.630   -10.638 1.00 31.55 ? 684 HOH F O   1 
HETATM 2626 O  O   . HOH L 5 .   ? 7.908  14.350  -1.112  1.00 24.72 ? 685 HOH F O   1 
HETATM 2627 O  O   . HOH L 5 .   ? 37.362 -5.373  1.488   1.00 46.46 ? 686 HOH F O   1 
HETATM 2628 O  O   . HOH L 5 .   ? 7.936  16.820  -0.261  1.00 34.26 ? 687 HOH F O   1 
HETATM 2629 O  O   . HOH L 5 .   ? 19.487 10.886  -5.836  1.00 17.74 ? 688 HOH F O   1 
HETATM 2630 O  O   . HOH L 5 .   ? 26.085 11.949  -5.672  1.00 38.27 ? 689 HOH F O   1 
HETATM 2631 O  O   . HOH L 5 .   ? 35.131 9.373   20.060  1.00 18.75 ? 690 HOH F O   1 
HETATM 2632 O  O   . HOH L 5 .   ? 32.593 13.215  0.698   1.00 29.98 ? 691 HOH F O   1 
HETATM 2633 O  O   . HOH L 5 .   ? 12.988 23.349  7.923   1.00 30.67 ? 692 HOH F O   1 
HETATM 2634 O  O   . HOH L 5 .   ? 9.982  20.528  -8.140  1.00 33.37 ? 693 HOH F O   1 
HETATM 2635 O  O   . HOH L 5 .   ? 19.942 19.027  13.980  1.00 28.23 ? 694 HOH F O   1 
HETATM 2636 O  O   . HOH L 5 .   ? 34.832 23.711  2.043   1.00 41.59 ? 695 HOH F O   1 
HETATM 2637 O  O   . HOH L 5 .   ? 27.139 4.667   -5.211  1.00 39.38 ? 696 HOH F O   1 
HETATM 2638 O  O   . HOH L 5 .   ? 7.947  10.335  8.983   1.00 37.63 ? 697 HOH F O   1 
HETATM 2639 O  O   . HOH L 5 .   ? 37.641 8.262   3.871   1.00 28.60 ? 698 HOH F O   1 
HETATM 2640 O  O   . HOH L 5 .   ? 28.670 22.525  16.553  1.00 34.95 ? 699 HOH F O   1 
HETATM 2641 O  O   . HOH L 5 .   ? 5.999  15.583  -8.054  1.00 31.41 ? 700 HOH F O   1 
HETATM 2642 O  O   . HOH L 5 .   ? 28.228 -8.776  8.809   1.00 29.42 ? 701 HOH F O   1 
HETATM 2643 O  O   . HOH L 5 .   ? 14.559 0.661   10.666  1.00 14.09 ? 702 HOH F O   1 
HETATM 2644 O  O   . HOH L 5 .   ? 11.827 3.301   10.711  1.00 47.35 ? 703 HOH F O   1 
HETATM 2645 O  O   . HOH L 5 .   ? 8.349  20.784  -13.675 1.00 67.45 ? 704 HOH F O   1 
HETATM 2646 O  O   . HOH L 5 .   ? 24.983 22.625  14.331  1.00 11.41 ? 705 HOH F O   1 
HETATM 2647 O  O   . HOH L 5 .   ? 35.596 -1.635  6.183   1.00 32.60 ? 706 HOH F O   1 
HETATM 2648 O  O   . HOH L 5 .   ? 18.915 6.043   -12.473 1.00 34.51 ? 707 HOH F O   1 
HETATM 2649 O  O   . HOH L 5 .   ? 15.405 5.765   24.155  1.00 35.83 ? 708 HOH F O   1 
HETATM 2650 O  O   . HOH L 5 .   ? 11.702 16.852  18.151  1.00 32.79 ? 709 HOH F O   1 
HETATM 2651 O  O   . HOH L 5 .   ? 13.094 23.343  -0.946  1.00 22.61 ? 710 HOH F O   1 
HETATM 2652 O  O   . HOH L 5 .   ? 14.021 9.926   22.153  1.00 61.11 ? 711 HOH F O   1 
HETATM 2653 O  O   . HOH L 5 .   ? 29.000 -11.017 7.032   1.00 43.18 ? 712 HOH F O   1 
HETATM 2654 O  O   . HOH L 5 .   ? 24.074 17.122  -2.664  1.00 17.70 ? 713 HOH F O   1 
HETATM 2655 O  O   . HOH L 5 .   ? 28.770 11.694  -4.391  1.00 31.58 ? 714 HOH F O   1 
HETATM 2656 O  O   . HOH L 5 .   ? 28.056 19.887  -1.425  1.00 17.50 ? 715 HOH F O   1 
HETATM 2657 O  O   . HOH L 5 .   ? 22.198 10.553  -5.182  1.00 16.00 ? 716 HOH F O   1 
HETATM 2658 O  O   . HOH L 5 .   ? 25.302 -0.870  -7.073  1.00 41.72 ? 717 HOH F O   1 
HETATM 2659 O  O   . HOH L 5 .   ? 18.682 34.891  10.554  1.00 41.74 ? 718 HOH F O   1 
HETATM 2660 O  O   . HOH L 5 .   ? 36.299 14.018  9.031   1.00 32.88 ? 719 HOH F O   1 
HETATM 2661 O  O   . HOH L 5 .   ? 33.276 10.368  -5.941  1.00 43.62 ? 720 HOH F O   1 
HETATM 2662 O  O   . HOH L 5 .   ? 9.775  17.951  16.607  1.00 41.03 ? 721 HOH F O   1 
HETATM 2663 O  O   . HOH L 5 .   ? 37.996 4.016   12.079  1.00 47.16 ? 722 HOH F O   1 
HETATM 2664 O  O   . HOH L 5 .   ? 32.372 -0.690  -2.017  1.00 54.39 ? 723 HOH F O   1 
HETATM 2665 O  O   . HOH L 5 .   ? 22.063 16.978  -5.308  1.00 54.83 ? 724 HOH F O   1 
HETATM 2666 O  O   . HOH L 5 .   ? 10.279 14.921  13.088  1.00 73.87 ? 725 HOH F O   1 
HETATM 2667 O  O   . HOH L 5 .   ? 28.777 5.591   19.941  1.00 52.89 ? 726 HOH F O   1 
HETATM 2668 O  O   . HOH L 5 .   ? 22.105 21.187  14.753  1.00 35.45 ? 727 HOH F O   1 
HETATM 2669 O  O   . HOH L 5 .   ? 31.137 25.684  15.390  1.00 56.38 ? 728 HOH F O   1 
HETATM 2670 O  O   . HOH L 5 .   ? 16.878 29.885  13.820  1.00 31.01 ? 729 HOH F O   1 
HETATM 2671 O  O   . HOH L 5 .   ? 17.273 25.128  -0.654  1.00 28.81 ? 730 HOH F O   1 
HETATM 2672 O  O   . HOH L 5 .   ? 34.305 16.313  9.089   1.00 27.36 ? 731 HOH F O   1 
HETATM 2673 O  O   . HOH L 5 .   ? 37.274 18.523  3.021   1.00 37.51 ? 732 HOH F O   1 
HETATM 2674 O  O   . HOH L 5 .   ? 14.290 28.109  3.679   1.00 34.14 ? 733 HOH F O   1 
HETATM 2675 O  O   . HOH L 5 .   ? 36.488 7.982   9.841   1.00 32.69 ? 734 HOH F O   1 
HETATM 2676 O  O   . HOH L 5 .   ? 7.375  4.460   -7.610  1.00 44.36 ? 735 HOH F O   1 
HETATM 2677 O  O   . HOH L 5 .   ? 31.528 26.136  3.998   1.00 43.71 ? 736 HOH F O   1 
HETATM 2678 O  O   . HOH L 5 .   ? 8.048  20.687  -4.518  1.00 41.77 ? 737 HOH F O   1 
HETATM 2679 O  O   . HOH L 5 .   ? 15.497 34.748  8.045   1.00 41.67 ? 738 HOH F O   1 
HETATM 2680 O  O   . HOH L 5 .   ? 5.291  19.640  -3.744  1.00 45.87 ? 739 HOH F O   1 
HETATM 2681 O  O   . HOH L 5 .   ? 22.011 5.220   -9.862  1.00 37.86 ? 740 HOH F O   1 
HETATM 2682 O  O   . HOH L 5 .   ? 36.039 2.346   -2.367  1.00 43.67 ? 741 HOH F O   1 
HETATM 2683 O  O   . HOH L 5 .   ? 30.284 -3.797  11.696  1.00 38.88 ? 742 HOH F O   1 
HETATM 2684 O  O   . HOH L 5 .   ? 30.223 -6.158  9.574   1.00 33.58 ? 743 HOH F O   1 
HETATM 2685 O  O   . HOH L 5 .   ? 27.505 13.630  -2.384  1.00 27.72 ? 744 HOH F O   1 
HETATM 2686 O  O   . HOH L 5 .   ? 11.412 -1.166  8.933   1.00 32.34 ? 745 HOH F O   1 
HETATM 2687 O  O   . HOH L 5 .   ? 19.531 21.019  15.231  1.00 38.18 ? 746 HOH F O   1 
# 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   ALA 1   1   1   ALA ALA A . n 
A 1 2   THR 2   2   2   THR THR A . n 
A 1 3   LYS 3   3   3   LYS LYS A . n 
A 1 4   ALA 4   4   4   ALA ALA A . n 
A 1 5   VAL 5   5   5   VAL VAL A . n 
A 1 6   CYS 6   6   6   CYS CYS A . n 
A 1 7   VAL 7   7   7   VAL VAL A . n 
A 1 8   LEU 8   8   8   LEU LEU A . n 
A 1 9   LYS 9   9   9   LYS LYS A . n 
A 1 10  GLY 10  10  10  GLY GLY A . n 
A 1 11  ASP 11  11  11  ASP ASP A . n 
A 1 12  GLY 12  12  12  GLY GLY A . n 
A 1 13  PRO 13  13  13  PRO PRO A . n 
A 1 14  VAL 14  14  14  VAL VAL A . n 
A 1 15  GLN 15  15  15  GLN GLN A . n 
A 1 16  GLY 16  16  16  GLY GLY A . n 
A 1 17  ILE 17  17  17  ILE ILE A . n 
A 1 18  ILE 18  18  18  ILE ILE A . n 
A 1 19  ASN 19  19  19  ASN ASN A . n 
A 1 20  PHE 20  20  20  PHE PHE A . n 
A 1 21  GLU 21  21  21  GLU GLU A . n 
A 1 22  GLN 22  22  22  GLN GLN A . n 
A 1 23  LYS 23  23  23  LYS LYS A . n 
A 1 24  GLU 24  24  24  GLU GLU A . n 
A 1 25  SER 25  25  25  SER SER A . n 
A 1 26  ASN 26  26  26  ASN ASN A . n 
A 1 27  GLY 27  27  27  GLY GLY A . n 
A 1 28  PRO 28  28  28  PRO PRO A . n 
A 1 29  VAL 29  29  29  VAL VAL A . n 
A 1 30  LYS 30  30  30  LYS LYS A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  TRP 32  32  32  TRP TRP A . n 
A 1 33  GLY 33  33  33  GLY GLY A . n 
A 1 34  SER 34  34  34  SER SER A . n 
A 1 35  ILE 35  35  35  ILE ILE A . n 
A 1 36  LYS 36  36  36  LYS LYS A . n 
A 1 37  GLY 37  37  37  GLY GLY A . n 
A 1 38  LEU 38  38  38  LEU LEU A . n 
A 1 39  THR 39  39  39  THR THR A . n 
A 1 40  GLU 40  40  40  GLU GLU A . n 
A 1 41  GLY 41  41  41  GLY GLY A . n 
A 1 42  LEU 42  42  42  LEU LEU A . n 
A 1 43  HIS 43  43  43  HIS HIS A . n 
A 1 44  GLY 44  44  44  GLY GLY A . n 
A 1 45  PHE 45  45  45  PHE PHE A . n 
A 1 46  HIS 46  46  46  HIS HIS A . n 
A 1 47  VAL 47  47  47  VAL VAL A . n 
A 1 48  HIS 48  48  48  HIS HIS A . n 
A 1 49  GLU 49  49  49  GLU GLU A . n 
A 1 50  PHE 50  50  50  PHE PHE A . n 
A 1 51  GLY 51  51  51  GLY GLY A . n 
A 1 52  ASP 52  52  52  ASP ASP A . n 
A 1 53  ASN 53  53  53  ASN ASN A . n 
A 1 54  THR 54  54  54  THR THR A . n 
A 1 55  ALA 55  55  55  ALA ALA A . n 
A 1 56  GLY 56  56  56  GLY GLY A . n 
A 1 57  CYS 57  57  57  CYS CYS A . n 
A 1 58  THR 58  58  58  THR THR A . n 
A 1 59  SER 59  59  59  SER SER A . n 
A 1 60  ALA 60  60  60  ALA ALA A . n 
A 1 61  GLY 61  61  61  GLY GLY A . n 
A 1 62  PRO 62  62  62  PRO PRO A . n 
A 1 63  HIS 63  63  63  HIS HIS A . n 
A 1 64  PHE 64  64  64  PHE PHE A . n 
A 1 65  ASN 65  65  65  ASN ASN A . n 
A 1 66  PRO 66  66  66  PRO PRO A . n 
A 1 67  LEU 67  67  67  LEU LEU A . n 
A 1 68  SER 68  68  68  SER SER A . n 
A 1 69  ARG 69  69  69  ARG ARG A . n 
A 1 70  LYS 70  70  70  LYS LYS A . n 
A 1 71  HIS 71  71  71  HIS HIS A . n 
A 1 72  GLY 72  72  72  GLY GLY A . n 
A 1 73  GLY 73  73  73  GLY GLY A . n 
A 1 74  PRO 74  74  74  PRO PRO A . n 
A 1 75  LYS 75  75  75  LYS LYS A . n 
A 1 76  ASP 76  76  76  ASP ASP A . n 
A 1 77  GLU 77  77  77  GLU GLU A . n 
A 1 78  GLU 78  78  78  GLU GLU A . n 
A 1 79  ARG 79  79  79  ARG ARG A . n 
A 1 80  HIS 80  80  80  HIS HIS A . n 
A 1 81  VAL 81  81  81  VAL VAL A . n 
A 1 82  GLY 82  82  82  GLY GLY A . n 
A 1 83  ASP 83  83  83  ASP ASP A . n 
A 1 84  LEU 84  84  84  LEU LEU A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  ASN 86  86  86  ASN ASN A . n 
A 1 87  VAL 87  87  87  VAL VAL A . n 
A 1 88  THR 88  88  88  THR THR A . n 
A 1 89  ALA 89  89  89  ALA ALA A . n 
A 1 90  ASP 90  90  90  ASP ASP A . n 
A 1 91  LYS 91  91  91  LYS LYS A . n 
A 1 92  ASP 92  92  92  ASP ASP A . n 
A 1 93  GLY 93  93  93  GLY GLY A . n 
A 1 94  VAL 94  94  94  VAL VAL A . n 
A 1 95  ALA 95  95  95  ALA ALA A . n 
A 1 96  ASP 96  96  96  ASP ASP A . n 
A 1 97  VAL 97  97  97  VAL VAL A . n 
A 1 98  SER 98  98  98  SER SER A . n 
A 1 99  ILE 99  99  99  ILE ILE A . n 
A 1 100 GLU 100 100 100 GLU GLU A . n 
A 1 101 ASP 101 101 101 ASP ASP A . n 
A 1 102 SER 102 102 102 SER SER A . n 
A 1 103 VAL 103 103 103 VAL VAL A . n 
A 1 104 ILE 104 104 104 ILE ILE A . n 
A 1 105 SER 105 105 105 SER SER A . n 
A 1 106 LEU 106 106 106 LEU LEU A . n 
A 1 107 SER 107 107 107 SER SER A . n 
A 1 108 GLY 108 108 108 GLY GLY A . n 
A 1 109 ASP 109 109 109 ASP ASP A . n 
A 1 110 HIS 110 110 110 HIS HIS A . n 
A 1 111 CYS 111 111 111 CYS CYS A . n 
A 1 112 ILE 112 112 112 ILE ILE A . n 
A 1 113 ILE 113 113 113 ILE ILE A . n 
A 1 114 GLY 114 114 114 GLY GLY A . n 
A 1 115 ARG 115 115 115 ARG ARG A . n 
A 1 116 THR 116 116 116 THR THR A . n 
A 1 117 LEU 117 117 117 LEU LEU A . n 
A 1 118 VAL 118 118 118 VAL VAL A . n 
A 1 119 VAL 119 119 119 VAL VAL A . n 
A 1 120 HIS 120 120 120 HIS HIS A . n 
A 1 121 GLU 121 121 121 GLU GLU A . n 
A 1 122 LYS 122 122 122 LYS LYS A . n 
A 1 123 ALA 123 123 123 ALA ALA A . n 
A 1 124 ASP 124 124 124 ASP ASP A . n 
A 1 125 ASP 125 125 125 ASP ASP A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 GLY 127 127 127 GLY GLY A . n 
A 1 128 LYS 128 128 128 LYS LYS A . n 
A 1 129 GLY 129 129 129 GLY GLY A . n 
A 1 130 GLY 130 130 130 GLY GLY A . n 
A 1 131 ASN 131 131 131 ASN ASN A . n 
A 1 132 GLU 132 132 132 GLU GLU A . n 
A 1 133 GLU 133 133 133 GLU GLU A . n 
A 1 134 SER 134 134 134 SER SER A . n 
A 1 135 THR 135 135 135 THR THR A . n 
A 1 136 LYS 136 136 136 LYS LYS A . n 
A 1 137 THR 137 137 137 THR THR A . n 
A 1 138 GLY 138 138 138 GLY GLY A . n 
A 1 139 ASN 139 139 139 ASN ASN A . n 
A 1 140 ALA 140 140 140 ALA ALA A . n 
A 1 141 GLY 141 141 141 GLY GLY A . n 
A 1 142 SER 142 142 142 SER SER A . n 
A 1 143 ARG 143 143 143 ARG ARG A . n 
A 1 144 LEU 144 144 144 LEU LEU A . n 
A 1 145 ALA 145 145 145 ALA ALA A . n 
A 1 146 CYS 146 146 146 CYS CYS A . n 
A 1 147 GLY 147 147 147 GLY GLY A . n 
A 1 148 VAL 148 148 148 VAL VAL A . n 
A 1 149 ILE 149 149 149 ILE ILE A . n 
A 1 150 GLY 150 150 150 GLY GLY A . n 
A 1 151 ILE 151 151 151 ILE ILE A . n 
A 1 152 ALA 152 152 152 ALA ALA A . n 
A 1 153 GLN 153 153 153 GLN GLN A . n 
B 1 1   ALA 1   1   1   ALA ALA F . n 
B 1 2   THR 2   2   2   THR THR F . n 
B 1 3   LYS 3   3   3   LYS LYS F . n 
B 1 4   ALA 4   4   4   ALA ALA F . n 
B 1 5   VAL 5   5   5   VAL VAL F . n 
B 1 6   CYS 6   6   6   CYS CYS F . n 
B 1 7   VAL 7   7   7   VAL VAL F . n 
B 1 8   LEU 8   8   8   LEU LEU F . n 
B 1 9   LYS 9   9   9   LYS LYS F . n 
B 1 10  GLY 10  10  10  GLY GLY F . n 
B 1 11  ASP 11  11  11  ASP ASP F . n 
B 1 12  GLY 12  12  12  GLY GLY F . n 
B 1 13  PRO 13  13  13  PRO PRO F . n 
B 1 14  VAL 14  14  14  VAL VAL F . n 
B 1 15  GLN 15  15  15  GLN GLN F . n 
B 1 16  GLY 16  16  16  GLY GLY F . n 
B 1 17  ILE 17  17  17  ILE ILE F . n 
B 1 18  ILE 18  18  18  ILE ILE F . n 
B 1 19  ASN 19  19  19  ASN ASN F . n 
B 1 20  PHE 20  20  20  PHE PHE F . n 
B 1 21  GLU 21  21  21  GLU GLU F . n 
B 1 22  GLN 22  22  22  GLN GLN F . n 
B 1 23  LYS 23  23  23  LYS LYS F . n 
B 1 24  GLU 24  24  24  GLU GLU F . n 
B 1 25  SER 25  25  25  SER SER F . n 
B 1 26  ASN 26  26  26  ASN ASN F . n 
B 1 27  GLY 27  27  27  GLY GLY F . n 
B 1 28  PRO 28  28  28  PRO PRO F . n 
B 1 29  VAL 29  29  29  VAL VAL F . n 
B 1 30  LYS 30  30  30  LYS LYS F . n 
B 1 31  VAL 31  31  31  VAL VAL F . n 
B 1 32  TRP 32  32  32  TRP TRP F . n 
B 1 33  GLY 33  33  33  GLY GLY F . n 
B 1 34  SER 34  34  34  SER SER F . n 
B 1 35  ILE 35  35  35  ILE ILE F . n 
B 1 36  LYS 36  36  36  LYS LYS F . n 
B 1 37  GLY 37  37  37  GLY GLY F . n 
B 1 38  LEU 38  38  38  LEU LEU F . n 
B 1 39  THR 39  39  39  THR THR F . n 
B 1 40  GLU 40  40  40  GLU GLU F . n 
B 1 41  GLY 41  41  41  GLY GLY F . n 
B 1 42  LEU 42  42  42  LEU LEU F . n 
B 1 43  HIS 43  43  43  HIS HIS F . n 
B 1 44  GLY 44  44  44  GLY GLY F . n 
B 1 45  PHE 45  45  45  PHE PHE F . n 
B 1 46  HIS 46  46  46  HIS HIS F . n 
B 1 47  VAL 47  47  47  VAL VAL F . n 
B 1 48  HIS 48  48  48  HIS HIS F . n 
B 1 49  GLU 49  49  49  GLU GLU F . n 
B 1 50  PHE 50  50  50  PHE PHE F . n 
B 1 51  GLY 51  51  51  GLY GLY F . n 
B 1 52  ASP 52  52  52  ASP ASP F . n 
B 1 53  ASN 53  53  53  ASN ASN F . n 
B 1 54  THR 54  54  54  THR THR F . n 
B 1 55  ALA 55  55  55  ALA ALA F . n 
B 1 56  GLY 56  56  56  GLY GLY F . n 
B 1 57  CYS 57  57  57  CYS CYS F . n 
B 1 58  THR 58  58  58  THR THR F . n 
B 1 59  SER 59  59  59  SER SER F . n 
B 1 60  ALA 60  60  60  ALA ALA F . n 
B 1 61  GLY 61  61  61  GLY GLY F . n 
B 1 62  PRO 62  62  62  PRO PRO F . n 
B 1 63  HIS 63  63  63  HIS HIS F . n 
B 1 64  PHE 64  64  64  PHE PHE F . n 
B 1 65  ASN 65  65  65  ASN ASN F . n 
B 1 66  PRO 66  66  66  PRO PRO F . n 
B 1 67  LEU 67  67  67  LEU LEU F . n 
B 1 68  SER 68  68  68  SER SER F . n 
B 1 69  ARG 69  69  69  ARG ARG F . n 
B 1 70  LYS 70  70  70  LYS LYS F . n 
B 1 71  HIS 71  71  71  HIS HIS F . n 
B 1 72  GLY 72  72  72  GLY GLY F . n 
B 1 73  GLY 73  73  73  GLY GLY F . n 
B 1 74  PRO 74  74  74  PRO PRO F . n 
B 1 75  LYS 75  75  75  LYS LYS F . n 
B 1 76  ASP 76  76  76  ASP ASP F . n 
B 1 77  GLU 77  77  77  GLU GLU F . n 
B 1 78  GLU 78  78  78  GLU GLU F . n 
B 1 79  ARG 79  79  79  ARG ARG F . n 
B 1 80  HIS 80  80  80  HIS HIS F . n 
B 1 81  VAL 81  81  81  VAL VAL F . n 
B 1 82  GLY 82  82  82  GLY GLY F . n 
B 1 83  ASP 83  83  83  ASP ASP F . n 
B 1 84  LEU 84  84  84  LEU LEU F . n 
B 1 85  GLY 85  85  85  GLY GLY F . n 
B 1 86  ASN 86  86  86  ASN ASN F . n 
B 1 87  VAL 87  87  87  VAL VAL F . n 
B 1 88  THR 88  88  88  THR THR F . n 
B 1 89  ALA 89  89  89  ALA ALA F . n 
B 1 90  ASP 90  90  90  ASP ASP F . n 
B 1 91  LYS 91  91  91  LYS LYS F . n 
B 1 92  ASP 92  92  92  ASP ASP F . n 
B 1 93  GLY 93  93  93  GLY GLY F . n 
B 1 94  VAL 94  94  94  VAL VAL F . n 
B 1 95  ALA 95  95  95  ALA ALA F . n 
B 1 96  ASP 96  96  96  ASP ASP F . n 
B 1 97  VAL 97  97  97  VAL VAL F . n 
B 1 98  SER 98  98  98  SER SER F . n 
B 1 99  ILE 99  99  99  ILE ILE F . n 
B 1 100 GLU 100 100 100 GLU GLU F . n 
B 1 101 ASP 101 101 101 ASP ASP F . n 
B 1 102 SER 102 102 102 SER SER F . n 
B 1 103 VAL 103 103 103 VAL VAL F . n 
B 1 104 ILE 104 104 104 ILE ILE F . n 
B 1 105 SER 105 105 105 SER SER F . n 
B 1 106 LEU 106 106 106 LEU LEU F . n 
B 1 107 SER 107 107 107 SER SER F . n 
B 1 108 GLY 108 108 108 GLY GLY F . n 
B 1 109 ASP 109 109 109 ASP ASP F . n 
B 1 110 HIS 110 110 110 HIS HIS F . n 
B 1 111 CYS 111 111 111 CYS CYS F . n 
B 1 112 ILE 112 112 112 ILE ILE F . n 
B 1 113 ILE 113 113 113 ILE ILE F . n 
B 1 114 GLY 114 114 114 GLY GLY F . n 
B 1 115 ARG 115 115 115 ARG ARG F . n 
B 1 116 THR 116 116 116 THR THR F . n 
B 1 117 LEU 117 117 117 LEU LEU F . n 
B 1 118 VAL 118 118 118 VAL VAL F . n 
B 1 119 VAL 119 119 119 VAL VAL F . n 
B 1 120 HIS 120 120 120 HIS HIS F . n 
B 1 121 GLU 121 121 121 GLU GLU F . n 
B 1 122 LYS 122 122 122 LYS LYS F . n 
B 1 123 ALA 123 123 123 ALA ALA F . n 
B 1 124 ASP 124 124 124 ASP ASP F . n 
B 1 125 ASP 125 125 125 ASP ASP F . n 
B 1 126 LEU 126 126 126 LEU LEU F . n 
B 1 127 GLY 127 127 127 GLY GLY F . n 
B 1 128 LYS 128 128 128 LYS LYS F . n 
B 1 129 GLY 129 129 129 GLY GLY F . n 
B 1 130 GLY 130 130 130 GLY GLY F . n 
B 1 131 ASN 131 131 131 ASN ASN F . n 
B 1 132 GLU 132 132 132 GLU GLU F . n 
B 1 133 GLU 133 133 133 GLU GLU F . n 
B 1 134 SER 134 134 134 SER SER F . n 
B 1 135 THR 135 135 135 THR THR F . n 
B 1 136 LYS 136 136 136 LYS LYS F . n 
B 1 137 THR 137 137 137 THR THR F . n 
B 1 138 GLY 138 138 138 GLY GLY F . n 
B 1 139 ASN 139 139 139 ASN ASN F . n 
B 1 140 ALA 140 140 140 ALA ALA F . n 
B 1 141 GLY 141 141 141 GLY GLY F . n 
B 1 142 SER 142 142 142 SER SER F . n 
B 1 143 ARG 143 143 143 ARG ARG F . n 
B 1 144 LEU 144 144 144 LEU LEU F . n 
B 1 145 ALA 145 145 145 ALA ALA F . n 
B 1 146 CYS 146 146 146 CYS CYS F . n 
B 1 147 GLY 147 147 147 GLY GLY F . n 
B 1 148 VAL 148 148 148 VAL VAL F . n 
B 1 149 ILE 149 149 149 ILE ILE F . n 
B 1 150 GLY 150 150 150 GLY GLY F . n 
B 1 151 ILE 151 151 151 ILE ILE F . n 
B 1 152 ALA 152 152 152 ALA ALA F . n 
B 1 153 GLN 153 153 153 GLN GLN F . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 ZN  1   501 501 ZN  ZN  A . 
D 3 9JK 1   502 503 9JK DR1 A . 
E 2 ZN  1   503 502 ZN  ZN  A . 
F 4 SO4 1   504 504 SO4 SO4 A . 
G 2 ZN  1   501 501 ZN  ZN  F . 
H 2 ZN  1   502 502 ZN  ZN  F . 
I 3 9JK 1   503 503 9JK DR1 F . 
J 4 SO4 1   504 504 SO4 SO4 F . 
K 5 HOH 1   601 33  HOH HOH A . 
K 5 HOH 2   602 52  HOH HOH A . 
K 5 HOH 3   603 14  HOH HOH A . 
K 5 HOH 4   604 25  HOH HOH A . 
K 5 HOH 5   605 27  HOH HOH A . 
K 5 HOH 6   606 3   HOH HOH A . 
K 5 HOH 7   607 289 HOH HOH A . 
K 5 HOH 8   608 164 HOH HOH A . 
K 5 HOH 9   609 7   HOH HOH A . 
K 5 HOH 10  610 187 HOH HOH A . 
K 5 HOH 11  611 172 HOH HOH A . 
K 5 HOH 12  612 135 HOH HOH A . 
K 5 HOH 13  613 54  HOH HOH A . 
K 5 HOH 14  614 186 HOH HOH A . 
K 5 HOH 15  615 84  HOH HOH A . 
K 5 HOH 16  616 175 HOH HOH A . 
K 5 HOH 17  617 171 HOH HOH A . 
K 5 HOH 18  618 78  HOH HOH A . 
K 5 HOH 19  619 112 HOH HOH A . 
K 5 HOH 20  620 176 HOH HOH A . 
K 5 HOH 21  621 97  HOH HOH A . 
K 5 HOH 22  622 88  HOH HOH A . 
K 5 HOH 23  623 158 HOH HOH A . 
K 5 HOH 24  624 193 HOH HOH A . 
K 5 HOH 25  625 185 HOH HOH A . 
K 5 HOH 26  626 154 HOH HOH A . 
K 5 HOH 27  627 206 HOH HOH A . 
K 5 HOH 28  628 201 HOH HOH A . 
K 5 HOH 29  629 19  HOH HOH A . 
K 5 HOH 30  630 2   HOH HOH A . 
K 5 HOH 31  631 98  HOH HOH A . 
K 5 HOH 32  632 10  HOH HOH A . 
K 5 HOH 33  633 256 HOH HOH A . 
K 5 HOH 34  634 159 HOH HOH A . 
K 5 HOH 35  635 258 HOH HOH A . 
K 5 HOH 36  636 79  HOH HOH A . 
K 5 HOH 37  637 96  HOH HOH A . 
K 5 HOH 38  638 107 HOH HOH A . 
K 5 HOH 39  639 166 HOH HOH A . 
K 5 HOH 40  640 8   HOH HOH A . 
K 5 HOH 41  641 165 HOH HOH A . 
K 5 HOH 42  642 132 HOH HOH A . 
K 5 HOH 43  643 196 HOH HOH A . 
K 5 HOH 44  644 74  HOH HOH A . 
K 5 HOH 45  645 153 HOH HOH A . 
K 5 HOH 46  646 208 HOH HOH A . 
K 5 HOH 47  647 205 HOH HOH A . 
K 5 HOH 48  648 118 HOH HOH A . 
K 5 HOH 49  649 73  HOH HOH A . 
K 5 HOH 50  650 89  HOH HOH A . 
K 5 HOH 51  651 123 HOH HOH A . 
K 5 HOH 52  652 190 HOH HOH A . 
K 5 HOH 53  653 69  HOH HOH A . 
K 5 HOH 54  654 173 HOH HOH A . 
K 5 HOH 55  655 177 HOH HOH A . 
K 5 HOH 56  656 209 HOH HOH A . 
K 5 HOH 57  657 156 HOH HOH A . 
K 5 HOH 58  658 188 HOH HOH A . 
K 5 HOH 59  659 161 HOH HOH A . 
K 5 HOH 60  660 184 HOH HOH A . 
K 5 HOH 61  661 194 HOH HOH A . 
K 5 HOH 62  662 128 HOH HOH A . 
K 5 HOH 63  663 61  HOH HOH A . 
K 5 HOH 64  664 126 HOH HOH A . 
K 5 HOH 65  665 163 HOH HOH A . 
K 5 HOH 66  666 120 HOH HOH A . 
K 5 HOH 67  667 198 HOH HOH A . 
K 5 HOH 68  668 236 HOH HOH A . 
K 5 HOH 69  669 37  HOH HOH A . 
K 5 HOH 70  670 197 HOH HOH A . 
K 5 HOH 71  671 145 HOH HOH A . 
K 5 HOH 72  672 143 HOH HOH A . 
K 5 HOH 73  673 130 HOH HOH A . 
K 5 HOH 74  674 56  HOH HOH A . 
K 5 HOH 75  675 160 HOH HOH A . 
K 5 HOH 76  676 155 HOH HOH A . 
K 5 HOH 77  677 178 HOH HOH A . 
K 5 HOH 78  678 204 HOH HOH A . 
K 5 HOH 79  679 75  HOH HOH A . 
K 5 HOH 80  680 272 HOH HOH A . 
K 5 HOH 81  681 200 HOH HOH A . 
K 5 HOH 82  682 103 HOH HOH A . 
K 5 HOH 83  683 36  HOH HOH A . 
K 5 HOH 84  684 249 HOH HOH A . 
K 5 HOH 85  685 248 HOH HOH A . 
K 5 HOH 86  686 199 HOH HOH A . 
K 5 HOH 87  687 127 HOH HOH A . 
K 5 HOH 88  688 23  HOH HOH A . 
K 5 HOH 89  689 142 HOH HOH A . 
K 5 HOH 90  690 48  HOH HOH A . 
K 5 HOH 91  691 6   HOH HOH A . 
K 5 HOH 92  692 146 HOH HOH A . 
K 5 HOH 93  693 124 HOH HOH A . 
K 5 HOH 94  694 18  HOH HOH A . 
K 5 HOH 95  695 167 HOH HOH A . 
K 5 HOH 96  696 191 HOH HOH A . 
K 5 HOH 97  697 170 HOH HOH A . 
K 5 HOH 98  698 183 HOH HOH A . 
K 5 HOH 99  699 192 HOH HOH A . 
K 5 HOH 100 700 115 HOH HOH A . 
K 5 HOH 101 701 47  HOH HOH A . 
K 5 HOH 102 702 105 HOH HOH A . 
K 5 HOH 103 703 116 HOH HOH A . 
K 5 HOH 104 704 207 HOH HOH A . 
K 5 HOH 105 705 111 HOH HOH A . 
K 5 HOH 106 706 81  HOH HOH A . 
K 5 HOH 107 707 121 HOH HOH A . 
K 5 HOH 108 708 224 HOH HOH A . 
K 5 HOH 109 709 203 HOH HOH A . 
K 5 HOH 110 710 211 HOH HOH A . 
K 5 HOH 111 711 13  HOH HOH A . 
K 5 HOH 112 712 134 HOH HOH A . 
K 5 HOH 113 713 16  HOH HOH A . 
K 5 HOH 114 714 21  HOH HOH A . 
K 5 HOH 115 715 150 HOH HOH A . 
K 5 HOH 116 716 182 HOH HOH A . 
K 5 HOH 117 717 22  HOH HOH A . 
K 5 HOH 118 718 29  HOH HOH A . 
K 5 HOH 119 719 210 HOH HOH A . 
K 5 HOH 120 720 108 HOH HOH A . 
K 5 HOH 121 721 68  HOH HOH A . 
K 5 HOH 122 722 38  HOH HOH A . 
K 5 HOH 123 723 11  HOH HOH A . 
K 5 HOH 124 724 181 HOH HOH A . 
K 5 HOH 125 725 62  HOH HOH A . 
K 5 HOH 126 726 312 HOH HOH A . 
K 5 HOH 127 727 133 HOH HOH A . 
K 5 HOH 128 728 180 HOH HOH A . 
K 5 HOH 129 729 195 HOH HOH A . 
K 5 HOH 130 730 174 HOH HOH A . 
K 5 HOH 131 731 86  HOH HOH A . 
K 5 HOH 132 732 114 HOH HOH A . 
K 5 HOH 133 733 226 HOH HOH A . 
K 5 HOH 134 734 50  HOH HOH A . 
K 5 HOH 135 735 179 HOH HOH A . 
K 5 HOH 136 736 104 HOH HOH A . 
K 5 HOH 137 737 168 HOH HOH A . 
K 5 HOH 138 738 157 HOH HOH A . 
K 5 HOH 139 739 101 HOH HOH A . 
K 5 HOH 140 740 53  HOH HOH A . 
K 5 HOH 141 741 202 HOH HOH A . 
K 5 HOH 142 742 95  HOH HOH A . 
K 5 HOH 143 743 117 HOH HOH A . 
K 5 HOH 144 744 189 HOH HOH A . 
K 5 HOH 145 745 119 HOH HOH A . 
K 5 HOH 146 746 144 HOH HOH A . 
K 5 HOH 147 747 139 HOH HOH A . 
K 5 HOH 148 748 106 HOH HOH A . 
K 5 HOH 149 749 140 HOH HOH A . 
K 5 HOH 150 750 138 HOH HOH A . 
K 5 HOH 151 751 110 HOH HOH A . 
K 5 HOH 152 752 87  HOH HOH A . 
K 5 HOH 153 753 102 HOH HOH A . 
K 5 HOH 154 754 131 HOH HOH A . 
K 5 HOH 155 755 129 HOH HOH A . 
K 5 HOH 156 756 93  HOH HOH A . 
K 5 HOH 157 757 72  HOH HOH A . 
K 5 HOH 158 758 66  HOH HOH A . 
K 5 HOH 159 759 39  HOH HOH A . 
K 5 HOH 160 760 40  HOH HOH A . 
K 5 HOH 161 761 148 HOH HOH A . 
K 5 HOH 162 762 51  HOH HOH A . 
K 5 HOH 163 763 35  HOH HOH A . 
K 5 HOH 164 764 125 HOH HOH A . 
K 5 HOH 165 765 122 HOH HOH A . 
K 5 HOH 166 766 113 HOH HOH A . 
K 5 HOH 167 767 109 HOH HOH A . 
L 5 HOH 1   601 45  HOH HOH F . 
L 5 HOH 2   602 60  HOH HOH F . 
L 5 HOH 3   603 169 HOH HOH F . 
L 5 HOH 4   604 31  HOH HOH F . 
L 5 HOH 5   605 223 HOH HOH F . 
L 5 HOH 6   606 311 HOH HOH F . 
L 5 HOH 7   607 57  HOH HOH F . 
L 5 HOH 8   608 222 HOH HOH F . 
L 5 HOH 9   609 30  HOH HOH F . 
L 5 HOH 10  610 215 HOH HOH F . 
L 5 HOH 11  611 83  HOH HOH F . 
L 5 HOH 12  612 80  HOH HOH F . 
L 5 HOH 13  613 284 HOH HOH F . 
L 5 HOH 14  614 28  HOH HOH F . 
L 5 HOH 15  615 216 HOH HOH F . 
L 5 HOH 16  616 26  HOH HOH F . 
L 5 HOH 17  617 305 HOH HOH F . 
L 5 HOH 18  618 90  HOH HOH F . 
L 5 HOH 19  619 269 HOH HOH F . 
L 5 HOH 20  620 91  HOH HOH F . 
L 5 HOH 21  621 94  HOH HOH F . 
L 5 HOH 22  622 231 HOH HOH F . 
L 5 HOH 23  623 262 HOH HOH F . 
L 5 HOH 24  624 149 HOH HOH F . 
L 5 HOH 25  625 92  HOH HOH F . 
L 5 HOH 26  626 237 HOH HOH F . 
L 5 HOH 27  627 266 HOH HOH F . 
L 5 HOH 28  628 233 HOH HOH F . 
L 5 HOH 29  629 32  HOH HOH F . 
L 5 HOH 30  630 253 HOH HOH F . 
L 5 HOH 31  631 271 HOH HOH F . 
L 5 HOH 32  632 260 HOH HOH F . 
L 5 HOH 33  633 283 HOH HOH F . 
L 5 HOH 34  634 9   HOH HOH F . 
L 5 HOH 35  635 259 HOH HOH F . 
L 5 HOH 36  636 213 HOH HOH F . 
L 5 HOH 37  637 5   HOH HOH F . 
L 5 HOH 38  638 307 HOH HOH F . 
L 5 HOH 39  639 136 HOH HOH F . 
L 5 HOH 40  640 17  HOH HOH F . 
L 5 HOH 41  641 285 HOH HOH F . 
L 5 HOH 42  642 212 HOH HOH F . 
L 5 HOH 43  643 219 HOH HOH F . 
L 5 HOH 44  644 250 HOH HOH F . 
L 5 HOH 45  645 264 HOH HOH F . 
L 5 HOH 46  646 286 HOH HOH F . 
L 5 HOH 47  647 279 HOH HOH F . 
L 5 HOH 48  648 270 HOH HOH F . 
L 5 HOH 49  649 251 HOH HOH F . 
L 5 HOH 50  650 296 HOH HOH F . 
L 5 HOH 51  651 42  HOH HOH F . 
L 5 HOH 52  652 273 HOH HOH F . 
L 5 HOH 53  653 295 HOH HOH F . 
L 5 HOH 54  654 244 HOH HOH F . 
L 5 HOH 55  655 276 HOH HOH F . 
L 5 HOH 56  656 308 HOH HOH F . 
L 5 HOH 57  657 298 HOH HOH F . 
L 5 HOH 58  658 235 HOH HOH F . 
L 5 HOH 59  659 162 HOH HOH F . 
L 5 HOH 60  660 281 HOH HOH F . 
L 5 HOH 61  661 287 HOH HOH F . 
L 5 HOH 62  662 254 HOH HOH F . 
L 5 HOH 63  663 291 HOH HOH F . 
L 5 HOH 64  664 217 HOH HOH F . 
L 5 HOH 65  665 267 HOH HOH F . 
L 5 HOH 66  666 243 HOH HOH F . 
L 5 HOH 67  667 297 HOH HOH F . 
L 5 HOH 68  668 292 HOH HOH F . 
L 5 HOH 69  669 67  HOH HOH F . 
L 5 HOH 70  670 288 HOH HOH F . 
L 5 HOH 71  671 252 HOH HOH F . 
L 5 HOH 72  672 247 HOH HOH F . 
L 5 HOH 73  673 77  HOH HOH F . 
L 5 HOH 74  674 300 HOH HOH F . 
L 5 HOH 75  675 304 HOH HOH F . 
L 5 HOH 76  676 71  HOH HOH F . 
L 5 HOH 77  677 137 HOH HOH F . 
L 5 HOH 78  678 1   HOH HOH F . 
L 5 HOH 79  679 263 HOH HOH F . 
L 5 HOH 80  680 151 HOH HOH F . 
L 5 HOH 81  681 70  HOH HOH F . 
L 5 HOH 82  682 59  HOH HOH F . 
L 5 HOH 83  683 12  HOH HOH F . 
L 5 HOH 84  684 99  HOH HOH F . 
L 5 HOH 85  685 232 HOH HOH F . 
L 5 HOH 86  686 82  HOH HOH F . 
L 5 HOH 87  687 294 HOH HOH F . 
L 5 HOH 88  688 274 HOH HOH F . 
L 5 HOH 89  689 228 HOH HOH F . 
L 5 HOH 90  690 290 HOH HOH F . 
L 5 HOH 91  691 282 HOH HOH F . 
L 5 HOH 92  692 24  HOH HOH F . 
L 5 HOH 93  693 238 HOH HOH F . 
L 5 HOH 94  694 63  HOH HOH F . 
L 5 HOH 95  695 58  HOH HOH F . 
L 5 HOH 96  696 278 HOH HOH F . 
L 5 HOH 97  697 85  HOH HOH F . 
L 5 HOH 98  698 225 HOH HOH F . 
L 5 HOH 99  699 255 HOH HOH F . 
L 5 HOH 100 700 234 HOH HOH F . 
L 5 HOH 101 701 309 HOH HOH F . 
L 5 HOH 102 702 20  HOH HOH F . 
L 5 HOH 103 703 306 HOH HOH F . 
L 5 HOH 104 704 141 HOH HOH F . 
L 5 HOH 105 705 265 HOH HOH F . 
L 5 HOH 106 706 221 HOH HOH F . 
L 5 HOH 107 707 275 HOH HOH F . 
L 5 HOH 108 708 245 HOH HOH F . 
L 5 HOH 109 709 246 HOH HOH F . 
L 5 HOH 110 710 15  HOH HOH F . 
L 5 HOH 111 711 76  HOH HOH F . 
L 5 HOH 112 712 310 HOH HOH F . 
L 5 HOH 113 713 268 HOH HOH F . 
L 5 HOH 114 714 280 HOH HOH F . 
L 5 HOH 115 715 261 HOH HOH F . 
L 5 HOH 116 716 277 HOH HOH F . 
L 5 HOH 117 717 301 HOH HOH F . 
L 5 HOH 118 718 303 HOH HOH F . 
L 5 HOH 119 719 4   HOH HOH F . 
L 5 HOH 120 720 230 HOH HOH F . 
L 5 HOH 121 721 220 HOH HOH F . 
L 5 HOH 122 722 239 HOH HOH F . 
L 5 HOH 123 723 100 HOH HOH F . 
L 5 HOH 124 724 152 HOH HOH F . 
L 5 HOH 125 725 34  HOH HOH F . 
L 5 HOH 126 726 293 HOH HOH F . 
L 5 HOH 127 727 64  HOH HOH F . 
L 5 HOH 128 728 55  HOH HOH F . 
L 5 HOH 129 729 302 HOH HOH F . 
L 5 HOH 130 730 240 HOH HOH F . 
L 5 HOH 131 731 257 HOH HOH F . 
L 5 HOH 132 732 313 HOH HOH F . 
L 5 HOH 133 733 241 HOH HOH F . 
L 5 HOH 134 734 218 HOH HOH F . 
L 5 HOH 135 735 229 HOH HOH F . 
L 5 HOH 136 736 299 HOH HOH F . 
L 5 HOH 137 737 41  HOH HOH F . 
L 5 HOH 138 738 242 HOH HOH F . 
L 5 HOH 139 739 49  HOH HOH F . 
L 5 HOH 140 740 46  HOH HOH F . 
L 5 HOH 141 741 214 HOH HOH F . 
L 5 HOH 142 742 43  HOH HOH F . 
L 5 HOH 143 743 44  HOH HOH F . 
L 5 HOH 144 744 227 HOH HOH F . 
L 5 HOH 145 745 147 HOH HOH F . 
L 5 HOH 146 746 65  HOH HOH F . 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L 
# 
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)' 2270  ? 
1 MORE         -135  ? 
1 'SSA (A^2)'  13740 ? 
# 
_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 46  ? A HIS 46  ? 1_555 ZN ? E ZN . ? A ZN 503 ? 1_555 NE2 ? A HIS 48  ? A HIS 48  ? 1_555 118.8 ? 
2  ND1 ? A HIS 46  ? A HIS 46  ? 1_555 ZN ? E ZN . ? A ZN 503 ? 1_555 NE2 ? A HIS 120 ? A HIS 120 ? 1_555 98.4  ? 
3  NE2 ? A HIS 48  ? A HIS 48  ? 1_555 ZN ? E ZN . ? A ZN 503 ? 1_555 NE2 ? A HIS 120 ? A HIS 120 ? 1_555 121.6 ? 
4  ND1 ? A HIS 46  ? A HIS 46  ? 1_555 ZN ? E ZN . ? A ZN 503 ? 1_555 O4  ? F SO4 .   ? A SO4 504 ? 1_555 104.6 ? 
5  NE2 ? A HIS 48  ? A HIS 48  ? 1_555 ZN ? E ZN . ? A ZN 503 ? 1_555 O4  ? F SO4 .   ? A SO4 504 ? 1_555 108.2 ? 
6  NE2 ? A HIS 120 ? A HIS 120 ? 1_555 ZN ? E ZN . ? A ZN 503 ? 1_555 O4  ? F SO4 .   ? A SO4 504 ? 1_555 103.1 ? 
7  ND1 ? A HIS 63  ? A HIS 63  ? 1_555 ZN ? C ZN . ? A ZN 501 ? 1_555 ND1 ? A HIS 71  ? A HIS 71  ? 1_555 102.9 ? 
8  ND1 ? A HIS 63  ? A HIS 63  ? 1_555 ZN ? C ZN . ? A ZN 501 ? 1_555 ND1 ? A HIS 80  ? A HIS 80  ? 1_555 108.9 ? 
9  ND1 ? A HIS 71  ? A HIS 71  ? 1_555 ZN ? C ZN . ? A ZN 501 ? 1_555 ND1 ? A HIS 80  ? A HIS 80  ? 1_555 123.6 ? 
10 ND1 ? A HIS 63  ? A HIS 63  ? 1_555 ZN ? C ZN . ? A ZN 501 ? 1_555 OD1 ? A ASP 83  ? A ASP 83  ? 1_555 105.5 ? 
11 ND1 ? A HIS 71  ? A HIS 71  ? 1_555 ZN ? C ZN . ? A ZN 501 ? 1_555 OD1 ? A ASP 83  ? A ASP 83  ? 1_555 98.0  ? 
12 ND1 ? A HIS 80  ? A HIS 80  ? 1_555 ZN ? C ZN . ? A ZN 501 ? 1_555 OD1 ? A ASP 83  ? A ASP 83  ? 1_555 115.9 ? 
13 ND1 ? B HIS 46  ? F HIS 46  ? 1_555 ZN ? H ZN . ? F ZN 502 ? 1_555 NE2 ? B HIS 48  ? F HIS 48  ? 1_555 116.7 ? 
14 ND1 ? B HIS 46  ? F HIS 46  ? 1_555 ZN ? H ZN . ? F ZN 502 ? 1_555 NE2 ? B HIS 120 ? F HIS 120 ? 1_555 98.3  ? 
15 NE2 ? B HIS 48  ? F HIS 48  ? 1_555 ZN ? H ZN . ? F ZN 502 ? 1_555 NE2 ? B HIS 120 ? F HIS 120 ? 1_555 124.2 ? 
16 ND1 ? B HIS 46  ? F HIS 46  ? 1_555 ZN ? H ZN . ? F ZN 502 ? 1_555 O1  ? J SO4 .   ? F SO4 504 ? 1_555 104.8 ? 
17 NE2 ? B HIS 48  ? F HIS 48  ? 1_555 ZN ? H ZN . ? F ZN 502 ? 1_555 O1  ? J SO4 .   ? F SO4 504 ? 1_555 108.3 ? 
18 NE2 ? B HIS 120 ? F HIS 120 ? 1_555 ZN ? H ZN . ? F ZN 502 ? 1_555 O1  ? J SO4 .   ? F SO4 504 ? 1_555 102.2 ? 
19 ND1 ? B HIS 63  ? F HIS 63  ? 1_555 ZN ? G ZN . ? F ZN 501 ? 1_555 ND1 ? B HIS 71  ? F HIS 71  ? 1_555 102.5 ? 
20 ND1 ? B HIS 63  ? F HIS 63  ? 1_555 ZN ? G ZN . ? F ZN 501 ? 1_555 ND1 ? B HIS 80  ? F HIS 80  ? 1_555 110.4 ? 
21 ND1 ? B HIS 71  ? F HIS 71  ? 1_555 ZN ? G ZN . ? F ZN 501 ? 1_555 ND1 ? B HIS 80  ? F HIS 80  ? 1_555 121.8 ? 
22 ND1 ? B HIS 63  ? F HIS 63  ? 1_555 ZN ? G ZN . ? F ZN 501 ? 1_555 OD1 ? B ASP 83  ? F ASP 83  ? 1_555 106.8 ? 
23 ND1 ? B HIS 71  ? F HIS 71  ? 1_555 ZN ? G ZN . ? F ZN 501 ? 1_555 OD1 ? B ASP 83  ? F ASP 83  ? 1_555 96.9  ? 
24 ND1 ? B HIS 80  ? F HIS 80  ? 1_555 ZN ? G ZN . ? F ZN 501 ? 1_555 OD1 ? B ASP 83  ? F ASP 83  ? 1_555 116.6 ? 
# 
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 2018-06-13 
2 'Structure model' 1 1 2018-06-27 
3 'Structure model' 1 2 2019-02-20 
# 
_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         ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Data collection'      
2 2 'Structure model' 'Database references'  
3 3 'Structure model' 'Data collection'      
4 3 'Structure model' 'Derived calculations' 
# 
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             
3 3 'Structure model' pdbx_data_processing_status 
4 3 'Structure model' struct_conn                 
# 
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'                    
12 2 'Structure model' '_citation_author.name'             
# 
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       ? ? ? ? ? ? ? ? ? ? ? REFMAC  ? ? ? 5.8.0158 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? iMOSFLM ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP  ? ? ? .        4 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 NZ  F LYS 3   ? ? O   F HOH 601 ? ? 1.26 
2 1 CE  F LYS 3   ? ? O   F HOH 601 ? ? 1.41 
3 1 OD1 F ASN 26  ? ? O   F HOH 602 ? ? 1.95 
4 1 O   F HOH 669 ? ? O   F HOH 694 ? ? 2.01 
5 1 O   A HOH 663 ? ? O   A HOH 725 ? ? 2.07 
6 1 NH2 A ARG 69  ? B OE1 A GLU 78  ? ? 2.12 
7 1 CG  F ASN 26  ? ? O   F HOH 602 ? ? 2.12 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
MNDA                                        'United Kingdom' Hasnain/Apr15/833-791 1 
'Medical Research Council (United Kingdom)' 'United Kingdom' MRF-060-0002-RG-HASNA 2 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'                         ZN  
3 '~{N}-phenyl-2-sulfanyl-benzamide' 9JK 
4 'SULFATE ION'                      SO4 
5 water                              HOH 
# 
loop_
_pdbx_struct_assembly_auth_evidence.id 
_pdbx_struct_assembly_auth_evidence.assembly_id 
_pdbx_struct_assembly_auth_evidence.experimental_support 
_pdbx_struct_assembly_auth_evidence.details 
1 1 'mass spectrometry' ? 
2 1 SAXS                ? 
3 1 'gel filtration'    ? 
# 
