data_5O40
# 
_entry.id   5O40 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.295 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   5O40         
WWPDB D_1200005144 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        5O40 
_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 
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                   106.35 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     5O40 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     38.100 
_cell.length_a_esd                 ? 
_cell.length_b                     67.840 
_cell.length_b_esd                 ? 
_cell.length_c                     51.040 
_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                         5O40 
_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-selanyl-benzamide' 276.193   2   ?        ? ? ? 
4 non-polymer syn 'SULFATE ION'                     96.063    2   ?        ? ? ? 
5 water       nat water                             18.015    309 ?        ? ? ? 
# 
_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                       ? 
_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 5O40 A 1 ? 153 ? P00441 2 ? 154 ? 1 153 
2 1 5O40 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 
9JT non-polymer         . '~{N}-phenyl-2-selanyl-benzamide' ? 'C13 H11 N O Se' 276.193 
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                   5O40 
_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         38.48 
_exptl_crystal.description                 ? 
_exptl_crystal.F_000                       ? 
_exptl_crystal.id                          1 
_exptl_crystal.preparation                 ? 
_exptl_crystal.size_max                    ? 
_exptl_crystal.size_mid                    ? 
_exptl_crystal.size_min                    ? 
_exptl_crystal.size_rad                    ? 
_exptl_crystal.colour_lustre               ? 
_exptl_crystal.colour_modifier             ? 
_exptl_crystal.colour_primary              ? 
_exptl_crystal.density_meas                ? 
_exptl_crystal.density_meas_esd            ? 
_exptl_crystal.density_meas_gt             ? 
_exptl_crystal.density_meas_lt             ? 
_exptl_crystal.density_meas_temp           ? 
_exptl_crystal.density_meas_temp_esd       ? 
_exptl_crystal.density_meas_temp_gt        ? 
_exptl_crystal.density_meas_temp_lt        ? 
_exptl_crystal.pdbx_crystal_image_url      ? 
_exptl_crystal.pdbx_crystal_image_format   ? 
_exptl_crystal.pdbx_mosaicity              ? 
_exptl_crystal.pdbx_mosaicity_esd          ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              4 
_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 4, 2.4 M AMSO4, 150 mM NaCl' 
_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' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2016-07-14 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    'Cryogenically cooled 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                        'SOLEIL BEAMLINE PROXIMA 1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.987 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   'PROXIMA 1' 
_diffrn_source.pdbx_synchrotron_site       SOLEIL 
# 
_reflns.B_iso_Wilson_estimate            ? 
_reflns.entry_id                         5O40 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                1.5 
_reflns.d_resolution_low                 49.01 
_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                       39891 
_reflns.observed_criterion               ? 
_reflns.observed_criterion_F_max         ? 
_reflns.observed_criterion_F_min         ? 
_reflns.observed_criterion_I_max         ? 
_reflns.observed_criterion_I_min         ? 
_reflns.observed_criterion_sigma_F       ? 
_reflns.observed_criterion_sigma_I       ? 
_reflns.percent_possible_obs             99.9 
_reflns.R_free_details                   ? 
_reflns.Rmerge_F_all                     ? 
_reflns.Rmerge_F_obs                     ? 
_reflns.Friedel_coverage                 ? 
_reflns.number_gt                        ? 
_reflns.threshold_expression             ? 
_reflns.pdbx_redundancy                  3.1 
_reflns.pdbx_Rmerge_I_obs                0.11 
_reflns.pdbx_Rmerge_I_all                ? 
_reflns.pdbx_Rsym_value                  ? 
_reflns.pdbx_netI_over_av_sigmaI         ? 
_reflns.pdbx_netI_over_sigmaI            5.9 
_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                  1.5 
_reflns_shell.d_res_low                   1.52 
_reflns_shell.meanI_over_sigI_all         ? 
_reflns_shell.meanI_over_sigI_obs         1.5 
_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        99.5 
_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                0.59 
_reflns_shell.meanI_over_sigI_gt          ? 
_reflns_shell.meanI_over_uI_all           ? 
_reflns_shell.meanI_over_uI_gt            ? 
_reflns_shell.number_measured_gt          ? 
_reflns_shell.number_unique_gt            ? 
_reflns_shell.percent_possible_gt         ? 
_reflns_shell.Rmerge_F_gt                 ? 
_reflns_shell.Rmerge_I_gt                 ? 
_reflns_shell.pdbx_redundancy             3.1 
_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]                            -0.52 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            -0.56 
_refine.aniso_B[2][2]                            0.63 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            0.19 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               12.371 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.964 
_refine.correlation_coeff_Fo_to_Fc_free          0.945 
_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                                 5O40 
_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                            1.50 
_refine.ls_d_res_low                             48.98 
_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                     37783 
_refine.ls_number_reflns_R_free                  2081 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.85 
_refine.ls_percent_reflns_R_free                 5.2 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.17079 
_refine.ls_R_factor_R_free                       0.21526 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.16836 
_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                       0.109 
_refine.pdbx_overall_ESU_R_Free                  0.086 
_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                             4.995 
_refine.overall_SU_ML                            0.077 
_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             309 
_refine_hist.number_atoms_total               2575 
_refine_hist.d_res_high                       1.50 
_refine_hist.d_res_low                        48.98 
# 
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' ? 0.008  0.019  2338 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.002  0.020  2059 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.363  1.962  3179 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 1.220  3.001  4784 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.627  5.000  318  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 39.102 25.474 95   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 9.902  15.000 349  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? 9.304  15.000 8    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.075  0.200  346  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.004  0.020  2732 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.002  0.020  452  ? 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' ? 1.275  1.073  1251 ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 1.276  1.073  1250 ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 1.738  1.618  1570 ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 1.739  1.618  1571 ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 1.673  1.246  1087 ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 1.674  1.247  1084 ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 2.207  1.790  1602 ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 4.279  15.289 2561 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 3.486  14.227 2468 ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? 4.575  3.000  4385 ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? 32.449 5.000  152  ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? 11.472 5.000  4483 ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.500 
_refine_ls_shell.d_res_low                        1.539 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             181 
_refine_ls_shell.number_reflns_R_work             2748 
_refine_ls_shell.percent_reflns_obs               99.63 
_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                  0.302 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.285 
_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                     5O40 
_struct.title                        'SOD1 bound to Ebselen' 
_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        5O40 
_struct_keywords.text            'OXIDOREDUCTASE, Complex, Inhibitor' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 3 ? 
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 GLU A 132 ? LYS A 136 ? GLU A 132 LYS A 136 5 ? 5 
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 GLU B 132 ? LYS B 136 ? GLU F 132 LYS F 136 5 ? 5 
# 
_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 ? ? ? ? ? ? ? 2.050 ? 
disulf2  disulf ? ? B CYS 57  SG  ? ? ? 1_555 B CYS 146 SG ? ? F CYS 57  F CYS 146 1_555 ? ? ? ? ? ? ? 2.053 ? 
metalc1  metalc ? ? A HIS 46  ND1 ? ? ? 1_555 D ZN  .   ZN ? ? A HIS 46  A ZN  502 1_555 ? ? ? ? ? ? ? 2.079 ? 
metalc2  metalc ? ? A HIS 48  NE2 ? ? ? 1_555 D ZN  .   ZN ? ? A HIS 48  A ZN  502 1_555 ? ? ? ? ? ? ? 2.073 ? 
metalc3  metalc ? ? A HIS 63  ND1 ? ? ? 1_555 C ZN  .   ZN ? ? A HIS 63  A ZN  501 1_555 ? ? ? ? ? ? ? 2.052 ? 
metalc4  metalc ? ? A HIS 71  ND1 ? ? ? 1_555 C ZN  .   ZN ? ? A HIS 71  A ZN  501 1_555 ? ? ? ? ? ? ? 2.057 ? 
metalc5  metalc ? ? A HIS 80  ND1 ? ? ? 1_555 C ZN  .   ZN ? ? A HIS 80  A ZN  501 1_555 ? ? ? ? ? ? ? 2.020 ? 
metalc6  metalc ? ? A ASP 83  OD1 ? ? ? 1_555 C ZN  .   ZN ? ? A ASP 83  A ZN  501 1_555 ? ? ? ? ? ? ? 1.973 ? 
metalc7  metalc ? ? A HIS 120 NE2 ? ? ? 1_555 D ZN  .   ZN ? ? A HIS 120 A ZN  502 1_555 ? ? ? ? ? ? ? 1.981 ? 
metalc8  metalc ? ? B HIS 46  ND1 ? ? ? 1_555 H ZN  .   ZN ? ? F HIS 46  F ZN  502 1_555 ? ? ? ? ? ? ? 2.079 ? 
metalc9  metalc ? ? B HIS 48  NE2 ? ? ? 1_555 H ZN  .   ZN ? ? F HIS 48  F ZN  502 1_555 ? ? ? ? ? ? ? 2.105 ? 
metalc10 metalc ? ? B HIS 63  ND1 ? ? ? 1_555 G ZN  .   ZN ? ? F HIS 63  F ZN  501 1_555 ? ? ? ? ? ? ? 2.038 ? 
metalc11 metalc ? ? B HIS 71  ND1 ? ? ? 1_555 G ZN  .   ZN ? ? F HIS 71  F ZN  501 1_555 ? ? ? ? ? ? ? 2.093 ? 
metalc12 metalc ? ? B HIS 80  ND1 ? ? ? 1_555 G ZN  .   ZN ? ? F HIS 80  F ZN  501 1_555 ? ? ? ? ? ? ? 2.037 ? 
metalc13 metalc ? ? B ASP 83  OD1 ? ? ? 1_555 G ZN  .   ZN ? ? F ASP 83  F ZN  501 1_555 ? ? ? ? ? ? ? 1.981 ? 
metalc14 metalc ? ? B HIS 120 NE2 ? ? ? 1_555 H ZN  .   ZN ? ? F HIS 120 F ZN  502 1_555 ? ? ? ? ? ? ? 1.972 ? 
metalc15 metalc ? ? D ZN  .   ZN  ? ? ? 1_555 F SO4 .   O4 ? ? A ZN  502 A SO4 504 1_555 ? ? ? ? ? ? ? 2.010 ? 
metalc16 metalc ? ? H ZN  .   ZN  ? ? ? 1_555 J SO4 .   O1 ? ? F ZN  502 F SO4 504 1_555 ? ? ? ? ? ? ? 1.969 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
# 
_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       -1.48 
# 
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 PHE A 20  ? O PHE A 20  N ALA A 4   ? N ALA A 4   
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 ALA B 95  ? O ALA F 95  N ILE B 35  ? N ILE F 35  
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 ZN  502 ? 5  'binding site for residue ZN A 502'  
AC3 Software A 9JT 503 ? 9  'binding site for residue 9JT A 503' 
AC4 Software A SO4 504 ? 10 '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 9JT 503 ? 8  'binding site for residue 9JT F 503' 
AC8 Software F SO4 504 ? 10 'binding site for residue SO4 F 504' 
# 
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 5  HIS A 46  ? HIS A 46  . ? 1_555 ? 
6  AC2 5  HIS A 48  ? HIS A 48  . ? 1_555 ? 
7  AC2 5  HIS A 63  ? HIS A 63  . ? 1_555 ? 
8  AC2 5  HIS A 120 ? HIS A 120 . ? 1_555 ? 
9  AC2 5  SO4 F .   ? SO4 A 504 . ? 1_555 ? 
10 AC3 9  GLN A 15  ? GLN A 15  . ? 1_655 ? 
11 AC3 9  LYS A 36  ? LYS A 36  . ? 1_655 ? 
12 AC3 9  LEU A 106 ? LEU A 106 . ? 1_555 ? 
13 AC3 9  SER A 107 ? SER A 107 . ? 1_555 ? 
14 AC3 9  GLY A 108 ? GLY A 108 . ? 1_555 ? 
15 AC3 9  CYS A 111 ? CYS A 111 . ? 1_555 ? 
16 AC3 9  ILE A 113 ? ILE A 113 . ? 1_555 ? 
17 AC3 9  HOH K .   ? HOH A 613 . ? 1_555 ? 
18 AC3 9  9JT I .   ? 9JT F 503 . ? 1_555 ? 
19 AC4 10 HIS A 46  ? HIS A 46  . ? 1_555 ? 
20 AC4 10 HIS A 48  ? HIS A 48  . ? 1_555 ? 
21 AC4 10 HIS A 63  ? HIS A 63  . ? 1_555 ? 
22 AC4 10 HIS A 120 ? HIS A 120 . ? 1_555 ? 
23 AC4 10 THR A 137 ? THR A 137 . ? 1_555 ? 
24 AC4 10 ARG A 143 ? ARG A 143 . ? 1_555 ? 
25 AC4 10 ZN  D .   ? ZN  A 502 . ? 1_555 ? 
26 AC4 10 HOH K .   ? HOH A 602 . ? 1_555 ? 
27 AC4 10 HOH K .   ? HOH A 629 . ? 1_555 ? 
28 AC4 10 HOH K .   ? HOH A 646 . ? 1_555 ? 
29 AC5 4  HIS B 63  ? HIS F 63  . ? 1_555 ? 
30 AC5 4  HIS B 71  ? HIS F 71  . ? 1_555 ? 
31 AC5 4  HIS B 80  ? HIS F 80  . ? 1_555 ? 
32 AC5 4  ASP B 83  ? ASP F 83  . ? 1_555 ? 
33 AC6 5  HIS B 46  ? HIS F 46  . ? 1_555 ? 
34 AC6 5  HIS B 48  ? HIS F 48  . ? 1_555 ? 
35 AC6 5  HIS B 63  ? HIS F 63  . ? 1_555 ? 
36 AC6 5  HIS B 120 ? HIS F 120 . ? 1_555 ? 
37 AC6 5  SO4 J .   ? SO4 F 504 . ? 1_555 ? 
38 AC7 8  9JT E .   ? 9JT A 503 . ? 1_555 ? 
39 AC7 8  LEU B 106 ? LEU F 106 . ? 1_555 ? 
40 AC7 8  GLY B 108 ? GLY F 108 . ? 1_555 ? 
41 AC7 8  ASP B 109 ? ASP F 109 . ? 1_555 ? 
42 AC7 8  CYS B 111 ? CYS F 111 . ? 1_555 ? 
43 AC7 8  ILE B 113 ? ILE F 113 . ? 1_555 ? 
44 AC7 8  HOH L .   ? HOH F 609 . ? 1_555 ? 
45 AC7 8  HOH L .   ? HOH F 685 . ? 1_555 ? 
46 AC8 10 HIS B 46  ? HIS F 46  . ? 1_555 ? 
47 AC8 10 HIS B 48  ? HIS F 48  . ? 1_555 ? 
48 AC8 10 HIS B 63  ? HIS F 63  . ? 1_555 ? 
49 AC8 10 HIS B 120 ? HIS F 120 . ? 1_555 ? 
50 AC8 10 THR B 137 ? THR F 137 . ? 1_555 ? 
51 AC8 10 ARG B 143 ? ARG F 143 . ? 1_555 ? 
52 AC8 10 ZN  H .   ? ZN  F 502 . ? 1_555 ? 
53 AC8 10 HOH L .   ? HOH F 618 . ? 1_555 ? 
54 AC8 10 HOH L .   ? HOH F 626 . ? 1_555 ? 
55 AC8 10 HOH L .   ? HOH F 646 . ? 1_555 ? 
# 
_atom_sites.entry_id                    5O40 
_atom_sites.fract_transf_matrix[1][1]   0.026247 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.007700 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.014741 
_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]   0.020418 
_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  
SE 
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   ? 27.927 5.903   30.565  0.60 20.16 ? 1   ALA A N   1 
ATOM   2    C  CA  . ALA A 1 1   ? 26.922 4.861   30.191  0.60 18.41 ? 1   ALA A CA  1 
ATOM   3    C  C   . ALA A 1 1   ? 26.578 4.914   28.707  0.60 14.82 ? 1   ALA A C   1 
ATOM   4    O  O   . ALA A 1 1   ? 26.537 5.982   28.108  0.60 14.67 ? 1   ALA A O   1 
ATOM   5    C  CB  . ALA A 1 1   ? 25.654 5.014   31.015  0.60 18.67 ? 1   ALA A CB  1 
ATOM   6    N  N   . THR A 1 2   ? 26.317 3.747   28.135  0.70 14.49 ? 2   THR A N   1 
ATOM   7    C  CA  . THR A 1 2   ? 25.889 3.622   26.754  0.70 13.63 ? 2   THR A CA  1 
ATOM   8    C  C   . THR A 1 2   ? 24.458 3.100   26.773  0.90 8.60  ? 2   THR A C   1 
ATOM   9    O  O   . THR A 1 2   ? 24.091 2.273   27.622  0.80 7.84  ? 2   THR A O   1 
ATOM   10   C  CB  . THR A 1 2   ? 26.806 2.666   25.975  0.70 15.15 ? 2   THR A CB  1 
ATOM   11   O  OG1 . THR A 1 2   ? 28.167 3.077   26.141  0.70 16.65 ? 2   THR A OG1 1 
ATOM   12   C  CG2 . THR A 1 2   ? 26.477 2.665   24.486  0.70 16.69 ? 2   THR A CG2 1 
ATOM   13   N  N   . LYS A 1 3   ? 23.653 3.588   25.835  1.00 9.63  ? 3   LYS A N   1 
ATOM   14   C  CA  . LYS A 1 3   ? 22.253 3.199   25.744  1.00 9.90  ? 3   LYS A CA  1 
ATOM   15   C  C   . LYS A 1 3   ? 21.916 2.866   24.313  1.00 8.05  ? 3   LYS A C   1 
ATOM   16   O  O   . LYS A 1 3   ? 22.484 3.447   23.386  1.00 9.10  ? 3   LYS A O   1 
ATOM   17   C  CB  . LYS A 1 3   ? 21.345 4.321   26.250  1.00 10.21 ? 3   LYS A CB  1 
ATOM   18   C  CG  . LYS A 1 3   ? 21.504 4.624   27.734  1.00 13.08 ? 3   LYS A CG  1 
ATOM   19   C  CD  . LYS A 1 3   ? 20.586 5.757   28.162  1.00 16.63 ? 3   LYS A CD  1 
ATOM   20   C  CE  . LYS A 1 3   ? 20.426 5.827   29.671  1.00 20.72 ? 3   LYS A CE  1 
ATOM   21   N  NZ  . LYS A 1 3   ? 19.583 6.987   30.074  0.10 22.01 ? 3   LYS A NZ  1 
ATOM   22   N  N   . ALA A 1 4   ? 20.990 1.928   24.141  1.00 6.81  ? 4   ALA A N   1 
ATOM   23   C  CA  . ALA A 1 4   ? 20.481 1.565   22.827  1.00 7.49  ? 4   ALA A CA  1 
ATOM   24   C  C   . ALA A 1 4   ? 18.997 1.324   22.917  1.00 7.30  ? 4   ALA A C   1 
ATOM   25   O  O   . ALA A 1 4   ? 18.445 1.184   24.014  1.00 8.12  ? 4   ALA A O   1 
ATOM   26   C  CB  . ALA A 1 4   ? 21.205 0.340   22.273  1.00 6.99  ? 4   ALA A CB  1 
ATOM   27   N  N   . VAL A 1 5   ? 18.348 1.277   21.765  1.00 7.44  ? 5   VAL A N   1 
ATOM   28   C  CA  . VAL A 1 5   ? 16.902 1.115   21.717  1.00 8.13  ? 5   VAL A CA  1 
ATOM   29   C  C   . VAL A 1 5   ? 16.494 0.371   20.452  1.00 8.16  ? 5   VAL A C   1 
ATOM   30   O  O   . VAL A 1 5   ? 17.224 0.389   19.453  1.00 8.81  ? 5   VAL A O   1 
ATOM   31   C  CB  . VAL A 1 5   ? 16.200 2.491   21.854  1.00 8.46  ? 5   VAL A CB  1 
ATOM   32   C  CG1 . VAL A 1 5   ? 16.422 3.358   20.621  1.00 8.27  ? 5   VAL A CG1 1 
ATOM   33   C  CG2 . VAL A 1 5   ? 14.717 2.340   22.169  1.00 9.78  ? 5   VAL A CG2 1 
ATOM   34   N  N   . CYS A 1 6   ? 15.344 -0.301  20.515  1.00 7.48  ? 6   CYS A N   1 
ATOM   35   C  CA  . CYS A 1 6   ? 14.829 -1.067  19.394  1.00 7.54  ? 6   CYS A CA  1 
ATOM   36   C  C   . CYS A 1 6   ? 13.313 -1.047  19.363  1.00 7.15  ? 6   CYS A C   1 
ATOM   37   O  O   . CYS A 1 6   ? 12.676 -1.307  20.376  1.00 8.16  ? 6   CYS A O   1 
ATOM   38   C  CB  . CYS A 1 6   ? 15.302 -2.513  19.523  1.00 7.24  ? 6   CYS A CB  1 
ATOM   39   S  SG  . CYS A 1 6   ? 14.906 -3.551  18.095  1.00 8.38  ? 6   CYS A SG  1 
ATOM   40   N  N   . VAL A 1 7   ? 12.749 -0.744  18.201  1.00 8.47  ? 7   VAL A N   1 
ATOM   41   C  CA  . VAL A 1 7   ? 11.319 -0.852  17.965  1.00 9.41  ? 7   VAL A CA  1 
ATOM   42   C  C   . VAL A 1 7   ? 11.046 -2.155  17.224  1.00 8.41  ? 7   VAL A C   1 
ATOM   43   O  O   . VAL A 1 7   ? 11.558 -2.361  16.119  1.00 8.77  ? 7   VAL A O   1 
ATOM   44   C  CB  . VAL A 1 7   ? 10.803 0.315   17.124  1.00 14.22 ? 7   VAL A CB  1 
ATOM   45   C  CG1 . VAL A 1 7   ? 9.306  0.172   16.862  1.00 17.16 ? 7   VAL A CG1 1 
ATOM   46   C  CG2 . VAL A 1 7   ? 11.099 1.630   17.824  1.00 14.81 ? 7   VAL A CG2 1 
ATOM   47   N  N   . LEU A 1 8   ? 10.229 -3.014  17.826  1.00 8.55  ? 8   LEU A N   1 
ATOM   48   C  CA  . LEU A 1 8   ? 9.862  -4.304  17.244  1.00 8.53  ? 8   LEU A CA  1 
ATOM   49   C  C   . LEU A 1 8   ? 8.551  -4.170  16.499  1.00 9.15  ? 8   LEU A C   1 
ATOM   50   O  O   . LEU A 1 8   ? 7.540  -3.793  17.091  1.00 10.25 ? 8   LEU A O   1 
ATOM   51   C  CB  . LEU A 1 8   ? 9.717  -5.347  18.348  1.00 8.89  ? 8   LEU A CB  1 
ATOM   52   C  CG  . LEU A 1 8   ? 10.981 -5.648  19.146  1.00 10.08 ? 8   LEU A CG  1 
ATOM   53   C  CD1 . LEU A 1 8   ? 10.613 -6.485  20.362  1.00 10.21 ? 8   LEU A CD1 1 
ATOM   54   C  CD2 . LEU A 1 8   ? 12.008 -6.376  18.301  1.00 11.24 ? 8   LEU A CD2 1 
ATOM   55   N  N   . LYS A 1 9   ? 8.581  -4.447  15.198  1.00 9.52  ? 9   LYS A N   1 
ATOM   56   C  CA  . LYS A 1 9   ? 7.385  -4.493  14.364  1.00 10.53 ? 9   LYS A CA  1 
ATOM   57   C  C   . LYS A 1 9   ? 7.463  -5.704  13.445  1.00 10.74 ? 9   LYS A C   1 
ATOM   58   O  O   . LYS A 1 9   ? 8.547  -6.208  13.168  1.00 9.76  ? 9   LYS A O   1 
ATOM   59   C  CB  . LYS A 1 9   ? 7.261  -3.214  13.526  1.00 11.33 ? 9   LYS A CB  1 
ATOM   60   C  CG  . LYS A 1 9   ? 6.976  -1.960  14.336  0.50 11.84 ? 9   LYS A CG  1 
ATOM   61   C  CD  . LYS A 1 9   ? 7.041  -0.825  13.153  0.00 21.93 ? 9   LYS A CD  1 
ATOM   62   C  CE  . LYS A 1 9   ? 6.785  0.522   13.810  0.00 21.64 ? 9   LYS A CE  1 
ATOM   63   N  NZ  . LYS A 1 9   ? 6.775  1.632   12.817  0.00 25.50 ? 9   LYS A NZ  1 
ATOM   64   N  N   . GLY A 1 10  ? 6.306  -6.159  12.982  1.00 12.16 ? 10  GLY A N   1 
ATOM   65   C  CA  . GLY A 1 10  ? 6.217  -7.248  12.018  1.00 14.00 ? 10  GLY A CA  1 
ATOM   66   C  C   . GLY A 1 10  ? 4.982  -7.126  11.150  1.00 14.77 ? 10  GLY A C   1 
ATOM   67   O  O   . GLY A 1 10  ? 4.370  -6.056  11.059  1.00 16.20 ? 10  GLY A O   1 
ATOM   68   N  N   . ASP A 1 11  ? 4.620  -8.233  10.511  1.00 16.78 ? 11  ASP A N   1 
ATOM   69   C  CA  . ASP A 1 11  ? 3.468  -8.285  9.609   1.00 19.96 ? 11  ASP A CA  1 
ATOM   70   C  C   . ASP A 1 11  ? 2.122  -8.472  10.324  1.00 20.00 ? 11  ASP A C   1 
ATOM   71   O  O   . ASP A 1 11  ? 1.070  -8.296  9.708   1.00 20.61 ? 11  ASP A O   1 
ATOM   72   C  CB  . ASP A 1 11  ? 3.661  -9.413  8.589   1.00 22.15 ? 11  ASP A CB  1 
ATOM   73   C  CG  . ASP A 1 11  ? 4.853  -9.182  7.673   0.50 23.88 ? 11  ASP A CG  1 
ATOM   74   O  OD1 . ASP A 1 11  ? 5.067  -8.034  7.231   0.50 22.32 ? 11  ASP A OD1 1 
ATOM   75   O  OD2 . ASP A 1 11  ? 5.574  -10.159 7.387   0.50 24.84 ? 11  ASP A OD2 1 
ATOM   76   N  N   . GLY A 1 12  ? 2.154  -8.837  11.607  1.00 19.28 ? 12  GLY A N   1 
ATOM   77   C  CA  . GLY A 1 12  ? 0.942  -9.140  12.372  1.00 18.43 ? 12  GLY A CA  1 
ATOM   78   C  C   . GLY A 1 12  ? 0.742  -8.162  13.514  1.00 17.43 ? 12  GLY A C   1 
ATOM   79   O  O   . GLY A 1 12  ? 1.123  -6.999  13.397  1.00 16.69 ? 12  GLY A O   1 
ATOM   80   N  N   . PRO A 1 13  ? 0.162  -8.629  14.638  1.00 17.40 ? 13  PRO A N   1 
ATOM   81   C  CA  . PRO A 1 13  ? -0.167 -7.729  15.746  1.00 16.96 ? 13  PRO A CA  1 
ATOM   82   C  C   . PRO A 1 13  ? 0.974  -7.444  16.731  1.00 14.11 ? 13  PRO A C   1 
ATOM   83   O  O   . PRO A 1 13  ? 0.812  -6.593  17.603  1.00 14.91 ? 13  PRO A O   1 
ATOM   84   C  CB  . PRO A 1 13  ? -1.287 -8.483  16.463  1.00 18.18 ? 13  PRO A CB  1 
ATOM   85   C  CG  . PRO A 1 13  ? -0.914 -9.916  16.281  1.00 17.69 ? 13  PRO A CG  1 
ATOM   86   C  CD  . PRO A 1 13  ? -0.289 -10.010 14.914  1.00 18.07 ? 13  PRO A CD  1 
ATOM   87   N  N   . VAL A 1 14  ? 2.109  -8.134  16.600  1.00 12.31 ? 14  VAL A N   1 
ATOM   88   C  CA  . VAL A 1 14  ? 3.163  -8.043  17.600  1.00 11.27 ? 14  VAL A CA  1 
ATOM   89   C  C   . VAL A 1 14  ? 3.968  -6.761  17.407  1.00 11.15 ? 14  VAL A C   1 
ATOM   90   O  O   . VAL A 1 14  ? 4.477  -6.491  16.321  1.00 12.42 ? 14  VAL A O   1 
ATOM   91   C  CB  . VAL A 1 14  ? 4.113  -9.260  17.585  1.00 11.08 ? 14  VAL A CB  1 
ATOM   92   C  CG1 . VAL A 1 14  ? 5.141  -9.141  18.699  1.00 11.33 ? 14  VAL A CG1 1 
ATOM   93   C  CG2 . VAL A 1 14  ? 3.338  -10.553 17.760  1.00 10.67 ? 14  VAL A CG2 1 
ATOM   94   N  N   . GLN A 1 15  ? 4.072  -5.972  18.468  1.00 10.29 ? 15  GLN A N   1 
ATOM   95   C  CA  . GLN A 1 15  ? 4.893  -4.770  18.451  1.00 11.17 ? 15  GLN A CA  1 
ATOM   96   C  C   . GLN A 1 15  ? 5.414  -4.483  19.845  1.00 9.93  ? 15  GLN A C   1 
ATOM   97   O  O   . GLN A 1 15  ? 4.795  -4.870  20.843  1.00 10.26 ? 15  GLN A O   1 
ATOM   98   C  CB  . GLN A 1 15  ? 4.123  -3.570  17.901  1.00 13.64 ? 15  GLN A CB  1 
ATOM   99   C  CG  . GLN A 1 15  ? 2.879  -3.185  18.677  1.00 15.08 ? 15  GLN A CG  1 
ATOM   100  C  CD  . GLN A 1 15  ? 2.171  -1.989  18.071  0.50 15.81 ? 15  GLN A CD  1 
ATOM   101  O  OE1 . GLN A 1 15  ? 1.486  -2.105  17.057  0.50 16.26 ? 15  GLN A OE1 1 
ATOM   102  N  NE2 . GLN A 1 15  ? 2.324  -0.835  18.697  0.50 15.93 ? 15  GLN A NE2 1 
ATOM   103  N  N   . GLY A 1 16  ? 6.567  -3.831  19.903  1.00 9.09  ? 16  GLY A N   1 
ATOM   104  C  CA  . GLY A 1 16  ? 7.231  -3.585  21.171  1.00 8.86  ? 16  GLY A CA  1 
ATOM   105  C  C   . GLY A 1 16  ? 8.299  -2.520  21.095  1.00 8.11  ? 16  GLY A C   1 
ATOM   106  O  O   . GLY A 1 16  ? 8.673  -2.076  20.009  1.00 8.62  ? 16  GLY A O   1 
ATOM   107  N  N   . ILE A 1 17  ? 8.766  -2.125  22.272  1.00 8.09  ? 17  ILE A N   1 
ATOM   108  C  CA  . ILE A 1 17  ? 9.850  -1.181  22.450  1.00 9.59  ? 17  ILE A CA  1 
ATOM   109  C  C   . ILE A 1 17  ? 10.768 -1.800  23.480  1.00 8.05  ? 17  ILE A C   1 
ATOM   110  O  O   . ILE A 1 17  ? 10.301 -2.148  24.568  1.00 7.89  ? 17  ILE A O   1 
ATOM   111  C  CB  . ILE A 1 17  ? 9.350  0.170   23.022  1.00 11.69 ? 17  ILE A CB  1 
ATOM   112  C  CG1 . ILE A 1 17  ? 8.282  0.812   22.128  1.00 15.65 ? 17  ILE A CG1 1 
ATOM   113  C  CG2 . ILE A 1 17  ? 10.519 1.124   23.254  1.00 12.36 ? 17  ILE A CG2 1 
ATOM   114  C  CD1 . ILE A 1 17  ? 8.791  1.372   20.817  1.00 18.59 ? 17  ILE A CD1 1 
ATOM   115  N  N   . ILE A 1 18  ? 12.052 -1.931  23.148  1.00 8.25  ? 18  ILE A N   1 
ATOM   116  C  CA  . ILE A 1 18  ? 13.048 -2.492  24.050  1.00 8.52  ? 18  ILE A CA  1 
ATOM   117  C  C   . ILE A 1 18  ? 14.235 -1.546  24.183  1.00 7.50  ? 18  ILE A C   1 
ATOM   118  O  O   . ILE A 1 18  ? 14.753 -1.031  23.184  1.00 8.48  ? 18  ILE A O   1 
ATOM   119  C  CB  . ILE A 1 18  ? 13.521 -3.887  23.577  1.00 8.52  ? 18  ILE A CB  1 
ATOM   120  C  CG1 . ILE A 1 18  ? 12.334 -4.865  23.482  1.00 8.85  ? 18  ILE A CG1 1 
ATOM   121  C  CG2 . ILE A 1 18  ? 14.606 -4.426  24.497  1.00 9.32  ? 18  ILE A CG2 1 
ATOM   122  C  CD1 . ILE A 1 18  ? 11.701 -5.271  24.806  1.00 8.97  ? 18  ILE A CD1 1 
ATOM   123  N  N   . ASN A 1 19  ? 14.643 -1.330  25.431  1.00 7.77  ? 19  ASN A N   1 
ATOM   124  C  CA  . ASN A 1 19  ? 15.722 -0.426  25.800  1.00 8.16  ? 19  ASN A CA  1 
ATOM   125  C  C   . ASN A 1 19  ? 16.903 -1.214  26.331  1.00 7.01  ? 19  ASN A C   1 
ATOM   126  O  O   . ASN A 1 19  ? 16.717 -2.231  26.991  1.00 7.11  ? 19  ASN A O   1 
ATOM   127  C  CB  . ASN A 1 19  ? 15.244 0.514   26.905  1.00 8.57  ? 19  ASN A CB  1 
ATOM   128  C  CG  . ASN A 1 19  ? 14.002 1.288   26.515  1.00 8.99  ? 19  ASN A CG  1 
ATOM   129  O  OD1 . ASN A 1 19  ? 12.882 0.939   26.905  1.00 11.73 ? 19  ASN A OD1 1 
ATOM   130  N  ND2 . ASN A 1 19  ? 14.189 2.332   25.746  1.00 8.55  ? 19  ASN A ND2 1 
ATOM   131  N  N   . PHE A 1 20  ? 18.114 -0.743  26.038  1.00 6.90  ? 20  PHE A N   1 
ATOM   132  C  CA  . PHE A 1 20  ? 19.348 -1.346  26.527  1.00 8.24  ? 20  PHE A CA  1 
ATOM   133  C  C   . PHE A 1 20  ? 20.176 -0.286  27.240  1.00 7.98  ? 20  PHE A C   1 
ATOM   134  O  O   . PHE A 1 20  ? 20.290 0.842   26.747  1.00 7.43  ? 20  PHE A O   1 
ATOM   135  C  CB  . PHE A 1 20  ? 20.178 -1.941  25.379  1.00 7.81  ? 20  PHE A CB  1 
ATOM   136  C  CG  . PHE A 1 20  ? 19.449 -2.963  24.543  1.00 7.60  ? 20  PHE A CG  1 
ATOM   137  C  CD1 . PHE A 1 20  ? 18.611 -2.574  23.500  1.00 7.99  ? 20  PHE A CD1 1 
ATOM   138  C  CD2 . PHE A 1 20  ? 19.615 -4.327  24.786  1.00 7.72  ? 20  PHE A CD2 1 
ATOM   139  C  CE1 . PHE A 1 20  ? 17.938 -3.518  22.734  1.00 7.69  ? 20  PHE A CE1 1 
ATOM   140  C  CE2 . PHE A 1 20  ? 18.955 -5.268  24.011  1.00 8.92  ? 20  PHE A CE2 1 
ATOM   141  C  CZ  . PHE A 1 20  ? 18.120 -4.866  22.989  1.00 8.36  ? 20  PHE A CZ  1 
ATOM   142  N  N   . GLU A 1 21  ? 20.750 -0.633  28.392  1.00 9.08  ? 21  GLU A N   1 
ATOM   143  C  CA  . GLU A 1 21  ? 21.650 0.276   29.113  1.00 9.13  ? 21  GLU A CA  1 
ATOM   144  C  C   . GLU A 1 21  ? 22.840 -0.477  29.677  1.00 8.95  ? 21  GLU A C   1 
ATOM   145  O  O   . GLU A 1 21  ? 22.670 -1.506  30.331  1.00 9.63  ? 21  GLU A O   1 
ATOM   146  C  CB  . GLU A 1 21  ? 20.919 1.014   30.246  1.00 10.43 ? 21  GLU A CB  1 
ATOM   147  C  CG  . GLU A 1 21  ? 21.771 2.081   30.941  1.00 12.96 ? 21  GLU A CG  1 
ATOM   148  C  CD  . GLU A 1 21  ? 20.981 2.991   31.873  0.50 17.59 ? 21  GLU A CD  1 
ATOM   149  O  OE1 . GLU A 1 21  ? 19.752 2.808   32.031  0.50 16.91 ? 21  GLU A OE1 1 
ATOM   150  O  OE2 . GLU A 1 21  ? 21.601 3.906   32.455  0.50 17.72 ? 21  GLU A OE2 1 
ATOM   151  N  N   . GLN A 1 22  ? 24.035 0.055   29.429  1.00 9.04  ? 22  GLN A N   1 
ATOM   152  C  CA  . GLN A 1 22  ? 25.285 -0.511  29.925  1.00 9.93  ? 22  GLN A CA  1 
ATOM   153  C  C   . GLN A 1 22  ? 26.053 0.597   30.647  1.00 12.15 ? 22  GLN A C   1 
ATOM   154  O  O   . GLN A 1 22  ? 26.605 1.488   30.014  1.00 12.99 ? 22  GLN A O   1 
ATOM   155  C  CB  . GLN A 1 22  ? 26.092 -1.085  28.762  1.00 9.34  ? 22  GLN A CB  1 
ATOM   156  C  CG  . GLN A 1 22  ? 27.328 -1.862  29.186  1.00 8.69  ? 22  GLN A CG  1 
ATOM   157  C  CD  . GLN A 1 22  ? 28.037 -2.517  28.015  1.00 9.07  ? 22  GLN A CD  1 
ATOM   158  O  OE1 . GLN A 1 22  ? 28.014 -2.001  26.896  1.00 10.22 ? 22  GLN A OE1 1 
ATOM   159  N  NE2 . GLN A 1 22  ? 28.685 -3.652  28.266  1.00 9.59  ? 22  GLN A NE2 1 
ATOM   160  N  N   . LYS A 1 23  ? 26.078 0.538   31.975  1.00 14.31 ? 23  LYS A N   1 
ATOM   161  C  CA  . LYS A 1 23  ? 26.617 1.642   32.788  1.00 18.19 ? 23  LYS A CA  1 
ATOM   162  C  C   . LYS A 1 23  ? 28.130 1.768   32.662  1.00 20.47 ? 23  LYS A C   1 
ATOM   163  O  O   . LYS A 1 23  ? 28.662 2.881   32.599  1.00 20.26 ? 23  LYS A O   1 
ATOM   164  C  CB  . LYS A 1 23  ? 26.240 1.470   34.263  1.00 21.98 ? 23  LYS A CB  1 
ATOM   165  C  CG  . LYS A 1 23  ? 24.744 1.527   34.538  1.00 26.28 ? 23  LYS A CG  1 
ATOM   166  C  CD  . LYS A 1 23  ? 24.397 1.448   35.965  0.00 29.12 ? 23  LYS A CD  1 
ATOM   167  C  CE  . LYS A 1 23  ? 24.589 0.042   36.508  0.00 26.18 ? 23  LYS A CE  1 
ATOM   168  N  NZ  . LYS A 1 23  ? 24.143 -0.072  37.925  0.00 31.27 ? 23  LYS A NZ  1 
ATOM   169  N  N   . GLU A 1 24  ? 28.814 0.626   32.642  1.00 23.97 ? 24  GLU A N   1 
ATOM   170  C  CA  . GLU A 1 24  ? 30.265 0.596   32.582  1.00 27.12 ? 24  GLU A CA  1 
ATOM   171  C  C   . GLU A 1 24  ? 30.721 -0.221  31.383  1.00 23.25 ? 24  GLU A C   1 
ATOM   172  O  O   . GLU A 1 24  ? 30.084 -1.209  30.999  1.00 23.65 ? 24  GLU A O   1 
ATOM   173  C  CB  . GLU A 1 24  ? 30.838 0.035   33.893  1.00 30.71 ? 24  GLU A CB  1 
ATOM   174  C  CG  . GLU A 1 24  ? 32.354 0.132   34.011  1.00 35.24 ? 24  GLU A CG  1 
ATOM   175  C  CD  . GLU A 1 24  ? 32.943 -0.162  35.346  0.00 32.08 ? 24  GLU A CD  1 
ATOM   176  O  OE1 . GLU A 1 24  ? 32.140 -0.469  36.252  0.00 25.10 ? 24  GLU A OE1 1 
ATOM   177  O  OE2 . GLU A 1 24  ? 34.180 -0.138  35.513  0.00 34.11 ? 24  GLU A OE2 1 
ATOM   178  N  N   . SER A 1 25  ? 31.816 0.223   30.774  1.00 25.29 ? 25  SER A N   1 
ATOM   179  C  CA  . SER A 1 25  ? 32.459 -0.524  29.707  1.00 26.48 ? 25  SER A CA  1 
ATOM   180  C  C   . SER A 1 25  ? 32.694 -1.945  30.211  1.00 28.24 ? 25  SER A C   1 
ATOM   181  O  O   . SER A 1 25  ? 33.233 -2.130  31.307  1.00 32.14 ? 25  SER A O   1 
ATOM   182  C  CB  . SER A 1 25  ? 33.788 0.128   29.325  1.00 30.64 ? 25  SER A CB  1 
ATOM   183  O  OG  . SER A 1 25  ? 34.481 -0.643  28.357  1.00 35.27 ? 25  SER A OG  1 
ATOM   184  N  N   . ASN A 1 26  ? 32.239 -2.928  29.435  1.00 26.65 ? 26  ASN A N   1 
ATOM   185  C  CA  . ASN A 1 26  ? 32.341 -4.354  29.782  1.00 25.00 ? 26  ASN A CA  1 
ATOM   186  C  C   . ASN A 1 26  ? 31.530 -4.792  31.023  1.00 25.46 ? 26  ASN A C   1 
ATOM   187  O  O   . ASN A 1 26  ? 31.781 -5.862  31.589  1.00 27.06 ? 26  ASN A O   1 
ATOM   188  C  CB  . ASN A 1 26  ? 33.817 -4.776  29.903  1.00 25.85 ? 26  ASN A CB  1 
ATOM   189  C  CG  . ASN A 1 26  ? 34.586 -4.582  28.607  0.50 22.78 ? 26  ASN A CG  1 
ATOM   190  O  OD1 . ASN A 1 26  ? 34.130 -4.979  27.537  0.50 21.31 ? 26  ASN A OD1 1 
ATOM   191  N  ND2 . ASN A 1 26  ? 35.763 -3.984  28.701  0.50 20.48 ? 26  ASN A ND2 1 
ATOM   192  N  N   . GLY A 1 27  ? 30.543 -3.987  31.415  1.00 17.80 ? 27  GLY A N   1 
ATOM   193  C  CA  . GLY A 1 27  ? 29.637 -4.333  32.503  1.00 16.70 ? 27  GLY A CA  1 
ATOM   194  C  C   . GLY A 1 27  ? 28.406 -5.003  31.914  1.00 14.73 ? 27  GLY A C   1 
ATOM   195  O  O   . GLY A 1 27  ? 28.266 -5.084  30.685  1.00 13.52 ? 27  GLY A O   1 
ATOM   196  N  N   . PRO A 1 28  ? 27.497 -5.484  32.779  1.00 12.46 ? 28  PRO A N   1 
ATOM   197  C  CA  . PRO A 1 28  ? 26.274 -6.085  32.268  1.00 12.56 ? 28  PRO A CA  1 
ATOM   198  C  C   . PRO A 1 28  ? 25.360 -5.072  31.599  1.00 10.78 ? 28  PRO A C   1 
ATOM   199  O  O   . PRO A 1 28  ? 25.408 -3.867  31.903  1.00 10.97 ? 28  PRO A O   1 
ATOM   200  C  CB  . PRO A 1 28  ? 25.608 -6.664  33.520  1.00 12.64 ? 28  PRO A CB  1 
ATOM   201  C  CG  . PRO A 1 28  ? 26.156 -5.872  34.648  1.00 14.95 ? 28  PRO A CG  1 
ATOM   202  C  CD  . PRO A 1 28  ? 27.555 -5.513  34.254  1.00 13.28 ? 28  PRO A CD  1 
ATOM   203  N  N   . VAL A 1 29  ? 24.543 -5.577  30.686  1.00 10.71 ? 29  VAL A N   1 
ATOM   204  C  CA  . VAL A 1 29  ? 23.582 -4.768  29.967  1.00 10.04 ? 29  VAL A CA  1 
ATOM   205  C  C   . VAL A 1 29  ? 22.206 -5.046  30.540  1.00 9.08  ? 29  VAL A C   1 
ATOM   206  O  O   . VAL A 1 29  ? 21.777 -6.198  30.615  1.00 9.26  ? 29  VAL A O   1 
ATOM   207  C  CB  . VAL A 1 29  ? 23.583 -5.069  28.457  1.00 9.42  ? 29  VAL A CB  1 
ATOM   208  C  CG1 . VAL A 1 29  ? 22.596 -4.153  27.741  1.00 10.16 ? 29  VAL A CG1 1 
ATOM   209  C  CG2 . VAL A 1 29  ? 24.985 -4.894  27.879  1.00 9.85  ? 29  VAL A CG2 1 
ATOM   210  N  N   . LYS A 1 30  ? 21.524 -3.986  30.960  1.00 9.47  ? 30  LYS A N   1 
ATOM   211  C  CA  . LYS A 1 30  ? 20.122 -4.072  31.352  1.00 9.85  ? 30  LYS A CA  1 
ATOM   212  C  C   . LYS A 1 30  ? 19.239 -3.943  30.116  1.00 8.50  ? 30  LYS A C   1 
ATOM   213  O  O   . LYS A 1 30  ? 19.448 -3.048  29.305  1.00 8.32  ? 30  LYS A O   1 
ATOM   214  C  CB  . LYS A 1 30  ? 19.783 -2.972  32.356  1.00 10.92 ? 30  LYS A CB  1 
ATOM   215  C  CG  . LYS A 1 30  ? 20.542 -3.106  33.671  1.00 15.34 ? 30  LYS A CG  1 
ATOM   216  C  CD  . LYS A 1 30  ? 20.081 -2.138  34.670  0.00 14.93 ? 30  LYS A CD  1 
ATOM   217  C  CE  . LYS A 1 30  ? 20.781 -2.308  36.008  0.00 13.81 ? 30  LYS A CE  1 
ATOM   218  N  NZ  . LYS A 1 30  ? 20.429 -1.220  36.962  0.00 13.26 ? 30  LYS A NZ  1 
ATOM   219  N  N   . VAL A 1 31  ? 18.252 -4.826  29.996  1.00 9.54  ? 31  VAL A N   1 
ATOM   220  C  CA  . VAL A 1 31  ? 17.324 -4.843  28.869  1.00 13.44 ? 31  VAL A CA  1 
ATOM   221  C  C   . VAL A 1 31  ? 15.937 -4.724  29.477  1.00 10.93 ? 31  VAL A C   1 
ATOM   222  O  O   . VAL A 1 31  ? 15.565 -5.546  30.308  1.00 10.63 ? 31  VAL A O   1 
ATOM   223  C  CB  . VAL A 1 31  ? 17.428 -6.165  28.064  1.00 16.89 ? 31  VAL A CB  1 
ATOM   224  C  CG1 . VAL A 1 31  ? 16.545 -6.129  26.820  1.00 10.99 ? 31  VAL A CG1 1 
ATOM   225  C  CG2 . VAL A 1 31  ? 18.875 -6.464  27.694  1.00 17.82 ? 31  VAL A CG2 1 
ATOM   226  N  N   A TRP A 1 32  ? 15.175 -3.710  29.082  0.50 10.57 ? 32  TRP A N   1 
ATOM   227  N  N   B TRP A 1 32  ? 15.191 -3.687  29.090  0.50 10.66 ? 32  TRP A N   1 
ATOM   228  C  CA  A TRP A 1 32  ? 13.811 -3.576  29.581  0.50 10.45 ? 32  TRP A CA  1 
ATOM   229  C  CA  B TRP A 1 32  ? 13.838 -3.471  29.613  0.50 10.62 ? 32  TRP A CA  1 
ATOM   230  C  C   A TRP A 1 32  ? 12.896 -2.918  28.573  0.50 7.82  ? 32  TRP A C   1 
ATOM   231  C  C   B TRP A 1 32  ? 12.896 -2.903  28.565  0.50 8.15  ? 32  TRP A C   1 
ATOM   232  O  O   A TRP A 1 32  ? 13.329 -2.131  27.727  0.50 5.61  ? 32  TRP A O   1 
ATOM   233  O  O   B TRP A 1 32  ? 13.316 -2.166  27.671  0.50 6.05  ? 32  TRP A O   1 
ATOM   234  C  CB  A TRP A 1 32  ? 13.781 -2.793  30.898  0.50 7.92  ? 32  TRP A CB  1 
ATOM   235  C  CB  B TRP A 1 32  ? 13.859 -2.558  30.851  0.50 8.74  ? 32  TRP A CB  1 
ATOM   236  C  CG  A TRP A 1 32  ? 13.950 -1.333  30.705  0.50 8.67  ? 32  TRP A CG  1 
ATOM   237  C  CG  B TRP A 1 32  ? 14.331 -1.140  30.607  0.50 9.04  ? 32  TRP A CG  1 
ATOM   238  C  CD1 A TRP A 1 32  ? 12.965 -0.387  30.675  0.50 9.13  ? 32  TRP A CD1 1 
ATOM   239  C  CD1 B TRP A 1 32  ? 15.615 -0.687  30.657  0.50 8.95  ? 32  TRP A CD1 1 
ATOM   240  C  CD2 A TRP A 1 32  ? 15.180 -0.640  30.505  0.50 8.62  ? 32  TRP A CD2 1 
ATOM   241  C  CD2 B TRP A 1 32  ? 13.514 0.005   30.316  0.50 9.51  ? 32  TRP A CD2 1 
ATOM   242  N  NE1 A TRP A 1 32  ? 13.512 0.854   30.464  0.50 10.06 ? 32  TRP A NE1 1 
ATOM   243  N  NE1 B TRP A 1 32  ? 15.656 0.663   30.396  0.50 9.26  ? 32  TRP A NE1 1 
ATOM   244  C  CE2 A TRP A 1 32  ? 14.871 0.726   30.361  0.50 8.98  ? 32  TRP A CE2 1 
ATOM   245  C  CE2 B TRP A 1 32  ? 14.379 1.114   30.189  0.50 9.64  ? 32  TRP A CE2 1 
ATOM   246  C  CE3 A TRP A 1 32  ? 16.518 -1.041  30.433  0.50 9.46  ? 32  TRP A CE3 1 
ATOM   247  C  CE3 B TRP A 1 32  ? 12.139 0.200   30.144  0.50 9.97  ? 32  TRP A CE3 1 
ATOM   248  C  CZ2 A TRP A 1 32  ? 15.847 1.688   30.141  0.50 9.52  ? 32  TRP A CZ2 1 
ATOM   249  C  CZ2 B TRP A 1 32  ? 13.915 2.395   29.890  0.50 9.86  ? 32  TRP A CZ2 1 
ATOM   250  C  CZ3 A TRP A 1 32  ? 17.482 -0.088  30.220  0.50 9.07  ? 32  TRP A CZ3 1 
ATOM   251  C  CZ3 B TRP A 1 32  ? 11.679 1.482   29.853  0.50 9.86  ? 32  TRP A CZ3 1 
ATOM   252  C  CH2 A TRP A 1 32  ? 17.144 1.266   30.083  0.50 9.51  ? 32  TRP A CH2 1 
ATOM   253  C  CH2 B TRP A 1 32  ? 12.565 2.556   29.729  0.50 10.34 ? 32  TRP A CH2 1 
ATOM   254  N  N   . GLY A 1 33  ? 11.618 -3.244  28.681  1.00 7.99  ? 33  GLY A N   1 
ATOM   255  C  CA  . GLY A 1 33  ? 10.608 -2.681  27.805  1.00 9.68  ? 33  GLY A CA  1 
ATOM   256  C  C   . GLY A 1 33  ? 9.381  -3.540  27.818  1.00 8.56  ? 33  GLY A C   1 
ATOM   257  O  O   . GLY A 1 33  ? 9.133  -4.258  28.787  1.00 9.43  ? 33  GLY A O   1 
ATOM   258  N  N   . SER A 1 34  ? 8.616  -3.455  26.743  1.00 8.78  ? 34  SER A N   1 
ATOM   259  C  CA  . SER A 1 34  ? 7.333  -4.122  26.657  1.00 9.51  ? 34  SER A CA  1 
ATOM   260  C  C   . SER A 1 34  ? 7.038  -4.562  25.234  1.00 8.47  ? 34  SER A C   1 
ATOM   261  O  O   . SER A 1 34  ? 7.390  -3.868  24.275  1.00 9.81  ? 34  SER A O   1 
ATOM   262  C  CB  . SER A 1 34  ? 6.230  -3.187  27.152  1.00 9.67  ? 34  SER A CB  1 
ATOM   263  O  OG  . SER A 1 34  ? 5.048  -3.924  27.386  1.00 13.23 ? 34  SER A OG  1 
ATOM   264  N  N   . ILE A 1 35  ? 6.408  -5.729  25.105  1.00 8.53  ? 35  ILE A N   1 
ATOM   265  C  CA  . ILE A 1 35  ? 5.949  -6.246  23.817  1.00 8.95  ? 35  ILE A CA  1 
ATOM   266  C  C   . ILE A 1 35  ? 4.494  -6.683  23.987  1.00 8.77  ? 35  ILE A C   1 
ATOM   267  O  O   . ILE A 1 35  ? 4.142  -7.296  24.989  1.00 9.99  ? 35  ILE A O   1 
ATOM   268  C  CB  . ILE A 1 35  ? 6.795  -7.445  23.325  1.00 8.84  ? 35  ILE A CB  1 
ATOM   269  C  CG1 . ILE A 1 35  ? 8.301  -7.139  23.402  1.00 9.58  ? 35  ILE A CG1 1 
ATOM   270  C  CG2 . ILE A 1 35  ? 6.400  -7.829  21.898  1.00 9.16  ? 35  ILE A CG2 1 
ATOM   271  C  CD1 . ILE A 1 35  ? 9.217  -8.315  23.107  1.00 9.83  ? 35  ILE A CD1 1 
ATOM   272  N  N   . LYS A 1 36  ? 3.650  -6.342  23.021  1.00 8.94  ? 36  LYS A N   1 
ATOM   273  C  CA  . LYS A 1 36  ? 2.229  -6.691  23.074  1.00 9.98  ? 36  LYS A CA  1 
ATOM   274  C  C   . LYS A 1 36  ? 1.818  -7.378  21.775  1.00 9.24  ? 36  LYS A C   1 
ATOM   275  O  O   . LYS A 1 36  ? 2.584  -7.410  20.811  1.00 9.88  ? 36  LYS A O   1 
ATOM   276  C  CB  . LYS A 1 36  ? 1.374  -5.453  23.356  1.00 9.78  ? 36  LYS A CB  1 
ATOM   277  C  CG  . LYS A 1 36  ? 1.408  -4.377  22.284  1.00 10.02 ? 36  LYS A CG  1 
ATOM   278  C  CD  . LYS A 1 36  ? 0.534  -3.187  22.677  0.50 10.09 ? 36  LYS A CD  1 
ATOM   279  C  CE  . LYS A 1 36  ? 0.798  -2.001  21.765  0.50 10.90 ? 36  LYS A CE  1 
ATOM   280  N  NZ  . LYS A 1 36  ? -0.120 -0.855  22.021  0.50 12.04 ? 36  LYS A NZ  1 
ATOM   281  N  N   . GLY A 1 37  ? 0.611  -7.934  21.768  1.00 9.45  ? 37  GLY A N   1 
ATOM   282  C  CA  . GLY A 1 37  ? 0.087  -8.672  20.618  1.00 8.61  ? 37  GLY A CA  1 
ATOM   283  C  C   . GLY A 1 37  ? 0.525  -10.128 20.536  1.00 8.65  ? 37  GLY A C   1 
ATOM   284  O  O   . GLY A 1 37  ? 0.390  -10.745 19.487  1.00 9.04  ? 37  GLY A O   1 
ATOM   285  N  N   . LEU A 1 38  ? 1.042  -10.669 21.638  1.00 8.83  ? 38  LEU A N   1 
ATOM   286  C  CA  . LEU A 1 38  ? 1.576  -12.033 21.687  1.00 9.00  ? 38  LEU A CA  1 
ATOM   287  C  C   . LEU A 1 38  ? 0.557  -13.025 22.219  1.00 9.18  ? 38  LEU A C   1 
ATOM   288  O  O   . LEU A 1 38  ? -0.365 -12.656 22.953  1.00 10.19 ? 38  LEU A O   1 
ATOM   289  C  CB  . LEU A 1 38  ? 2.804  -12.076 22.589  1.00 10.17 ? 38  LEU A CB  1 
ATOM   290  C  CG  . LEU A 1 38  ? 4.007  -11.278 22.091  1.00 12.89 ? 38  LEU A CG  1 
ATOM   291  C  CD1 . LEU A 1 38  ? 4.948  -10.967 23.244  1.00 15.98 ? 38  LEU A CD1 1 
ATOM   292  C  CD2 . LEU A 1 38  ? 4.733  -12.031 20.977  1.00 11.57 ? 38  LEU A CD2 1 
ATOM   293  N  N   . THR A 1 39  ? 0.730  -14.293 21.860  1.00 7.89  ? 39  THR A N   1 
ATOM   294  C  CA  . THR A 1 39  ? 0.004  -15.358 22.533  1.00 9.14  ? 39  THR A CA  1 
ATOM   295  C  C   . THR A 1 39  ? 0.599  -15.515 23.926  1.00 9.13  ? 39  THR A C   1 
ATOM   296  O  O   . THR A 1 39  ? 1.790  -15.283 24.137  1.00 9.30  ? 39  THR A O   1 
ATOM   297  C  CB  . THR A 1 39  ? 0.088  -16.690 21.781  1.00 13.71 ? 39  THR A CB  1 
ATOM   298  O  OG1 . THR A 1 39  ? 1.464  -17.020 21.563  1.00 13.46 ? 39  THR A OG1 1 
ATOM   299  C  CG2 . THR A 1 39  ? -0.635 -16.589 20.447  1.00 15.42 ? 39  THR A CG2 1 
ATOM   300  N  N   . GLU A 1 40  ? -0.239 -15.892 24.877  1.00 8.57  ? 40  GLU A N   1 
ATOM   301  C  CA  . GLU A 1 40  ? 0.214  -16.099 26.243  1.00 9.12  ? 40  GLU A CA  1 
ATOM   302  C  C   . GLU A 1 40  ? 1.239  -17.233 26.295  1.00 8.41  ? 40  GLU A C   1 
ATOM   303  O  O   . GLU A 1 40  ? 1.061  -18.274 25.646  1.00 8.92  ? 40  GLU A O   1 
ATOM   304  C  CB  . GLU A 1 40  ? -0.988 -16.400 27.147  1.00 9.30  ? 40  GLU A CB  1 
ATOM   305  C  CG  . GLU A 1 40  ? -0.693 -16.320 28.640  1.00 9.92  ? 40  GLU A CG  1 
ATOM   306  C  CD  . GLU A 1 40  ? -0.584 -17.670 29.313  1.00 10.46 ? 40  GLU A CD  1 
ATOM   307  O  OE1 . GLU A 1 40  ? -0.031 -18.587 28.679  1.00 13.08 ? 40  GLU A OE1 1 
ATOM   308  O  OE2 . GLU A 1 40  ? -1.030 -17.803 30.482  1.00 11.41 ? 40  GLU A OE2 1 
ATOM   309  N  N   . GLY A 1 41  ? 2.319  -17.007 27.041  1.00 8.35  ? 41  GLY A N   1 
ATOM   310  C  CA  . GLY A 1 41  ? 3.422  -17.974 27.164  1.00 8.44  ? 41  GLY A CA  1 
ATOM   311  C  C   . GLY A 1 41  ? 4.794  -17.454 26.774  1.00 7.59  ? 41  GLY A C   1 
ATOM   312  O  O   . GLY A 1 41  ? 5.030  -16.239 26.714  1.00 8.38  ? 41  GLY A O   1 
ATOM   313  N  N   . LEU A 1 42  ? 5.701  -18.383 26.486  1.00 7.99  ? 42  LEU A N   1 
ATOM   314  C  CA  . LEU A 1 42  ? 7.092  -18.045 26.213  1.00 7.57  ? 42  LEU A CA  1 
ATOM   315  C  C   . LEU A 1 42  ? 7.343  -17.760 24.735  1.00 7.30  ? 42  LEU A C   1 
ATOM   316  O  O   . LEU A 1 42  ? 6.814  -18.456 23.855  1.00 7.47  ? 42  LEU A O   1 
ATOM   317  C  CB  . LEU A 1 42  ? 8.015  -19.155 26.693  1.00 8.45  ? 42  LEU A CB  1 
ATOM   318  C  CG  . LEU A 1 42  ? 7.941  -19.491 28.185  1.00 10.32 ? 42  LEU A CG  1 
ATOM   319  C  CD1 . LEU A 1 42  ? 8.878  -20.647 28.486  1.00 12.57 ? 42  LEU A CD1 1 
ATOM   320  C  CD2 . LEU A 1 42  ? 8.279  -18.282 29.046  1.00 12.29 ? 42  LEU A CD2 1 
ATOM   321  N  N   . HIS A 1 43  ? 8.173  -16.750 24.477  1.00 6.36  ? 43  HIS A N   1 
ATOM   322  C  CA  . HIS A 1 43  ? 8.506  -16.344 23.111  1.00 6.48  ? 43  HIS A CA  1 
ATOM   323  C  C   . HIS A 1 43  ? 9.999  -16.114 22.991  1.00 6.42  ? 43  HIS A C   1 
ATOM   324  O  O   . HIS A 1 43  ? 10.565 -15.301 23.723  1.00 6.99  ? 43  HIS A O   1 
ATOM   325  C  CB  . HIS A 1 43  ? 7.730  -15.080 22.743  1.00 6.86  ? 43  HIS A CB  1 
ATOM   326  C  CG  . HIS A 1 43  ? 6.260  -15.315 22.625  1.00 6.79  ? 43  HIS A CG  1 
ATOM   327  N  ND1 . HIS A 1 43  ? 5.670  -15.766 21.465  1.00 7.22  ? 43  HIS A ND1 1 
ATOM   328  C  CD2 . HIS A 1 43  ? 5.267  -15.222 23.540  1.00 7.20  ? 43  HIS A CD2 1 
ATOM   329  C  CE1 . HIS A 1 43  ? 4.375  -15.923 21.663  1.00 7.26  ? 43  HIS A CE1 1 
ATOM   330  N  NE2 . HIS A 1 43  ? 4.103  -15.597 22.914  1.00 7.35  ? 43  HIS A NE2 1 
ATOM   331  N  N   . GLY A 1 44  ? 10.636 -16.841 22.073  1.00 5.79  ? 44  GLY A N   1 
ATOM   332  C  CA  . GLY A 1 44  ? 12.078 -16.741 21.860  1.00 5.99  ? 44  GLY A CA  1 
ATOM   333  C  C   . GLY A 1 44  ? 12.506 -15.310 21.584  1.00 5.63  ? 44  GLY A C   1 
ATOM   334  O  O   . GLY A 1 44  ? 11.808 -14.587 20.871  1.00 5.45  ? 44  GLY A O   1 
ATOM   335  N  N   . PHE A 1 45  ? 13.632 -14.919 22.171  1.00 5.29  ? 45  PHE A N   1 
ATOM   336  C  CA  . PHE A 1 45  ? 14.101 -13.521 22.178  1.00 5.24  ? 45  PHE A CA  1 
ATOM   337  C  C   . PHE A 1 45  ? 15.568 -13.529 21.802  1.00 5.50  ? 45  PHE A C   1 
ATOM   338  O  O   . PHE A 1 45  ? 16.410 -13.952 22.599  1.00 5.72  ? 45  PHE A O   1 
ATOM   339  C  CB  . PHE A 1 45  ? 13.881 -12.947 23.583  1.00 4.91  ? 45  PHE A CB  1 
ATOM   340  C  CG  . PHE A 1 45  ? 13.948 -11.438 23.688  1.00 5.51  ? 45  PHE A CG  1 
ATOM   341  C  CD1 . PHE A 1 45  ? 13.180 -10.609 22.867  1.00 5.57  ? 45  PHE A CD1 1 
ATOM   342  C  CD2 . PHE A 1 45  ? 14.703 -10.852 24.703  1.00 5.39  ? 45  PHE A CD2 1 
ATOM   343  C  CE1 . PHE A 1 45  ? 13.230 -9.221  23.022  1.00 6.02  ? 45  PHE A CE1 1 
ATOM   344  C  CE2 . PHE A 1 45  ? 14.752 -9.472  24.856  1.00 5.69  ? 45  PHE A CE2 1 
ATOM   345  C  CZ  . PHE A 1 45  ? 14.020 -8.665  24.015  1.00 7.21  ? 45  PHE A CZ  1 
ATOM   346  N  N   . HIS A 1 46  ? 15.864 -13.085 20.575  1.00 5.25  ? 46  HIS A N   1 
ATOM   347  C  CA  . HIS A 1 46  ? 17.191 -13.269 19.986  1.00 5.25  ? 46  HIS A CA  1 
ATOM   348  C  C   . HIS A 1 46  ? 17.722 -11.983 19.382  1.00 4.81  ? 46  HIS A C   1 
ATOM   349  O  O   . HIS A 1 46  ? 16.963 -11.228 18.789  1.00 4.79  ? 46  HIS A O   1 
ATOM   350  C  CB  . HIS A 1 46  ? 17.141 -14.274 18.830  1.00 5.61  ? 46  HIS A CB  1 
ATOM   351  C  CG  . HIS A 1 46  ? 16.645 -15.634 19.210  1.00 7.21  ? 46  HIS A CG  1 
ATOM   352  N  ND1 . HIS A 1 46  ? 15.954 -16.439 18.328  1.00 7.94  ? 46  HIS A ND1 1 
ATOM   353  C  CD2 . HIS A 1 46  ? 16.725 -16.325 20.374  1.00 6.83  ? 46  HIS A CD2 1 
ATOM   354  C  CE1 . HIS A 1 46  ? 15.626 -17.567 18.937  1.00 8.60  ? 46  HIS A CE1 1 
ATOM   355  N  NE2 . HIS A 1 46  ? 16.086 -17.526 20.175  1.00 7.44  ? 46  HIS A NE2 1 
ATOM   356  N  N   . VAL A 1 47  ? 19.024 -11.773 19.504  1.00 4.46  ? 47  VAL A N   1 
ATOM   357  C  CA  . VAL A 1 47  ? 19.732 -10.874 18.586  1.00 5.25  ? 47  VAL A CA  1 
ATOM   358  C  C   . VAL A 1 47  ? 20.238 -11.730 17.422  1.00 6.11  ? 47  VAL A C   1 
ATOM   359  O  O   . VAL A 1 47  ? 21.012 -12.687 17.619  1.00 6.62  ? 47  VAL A O   1 
ATOM   360  C  CB  . VAL A 1 47  ? 20.886 -10.120 19.255  1.00 5.55  ? 47  VAL A CB  1 
ATOM   361  C  CG1 . VAL A 1 47  ? 21.551 -9.159  18.270  1.00 5.23  ? 47  VAL A CG1 1 
ATOM   362  C  CG2 . VAL A 1 47  ? 20.365 -9.367  20.469  1.00 5.21  ? 47  VAL A CG2 1 
ATOM   363  N  N   . HIS A 1 48  ? 19.777 -11.380 16.222  1.00 6.32  ? 48  HIS A N   1 
ATOM   364  C  CA  . HIS A 1 48  ? 20.232 -11.988 14.975  1.00 6.54  ? 48  HIS A CA  1 
ATOM   365  C  C   . HIS A 1 48  ? 21.323 -11.127 14.360  1.00 6.84  ? 48  HIS A C   1 
ATOM   366  O  O   . HIS A 1 48  ? 21.391 -9.925  14.613  1.00 7.25  ? 48  HIS A O   1 
ATOM   367  C  CB  . HIS A 1 48  ? 19.056 -12.149 14.018  1.00 6.80  ? 48  HIS A CB  1 
ATOM   368  C  CG  . HIS A 1 48  ? 18.175 -13.313 14.343  1.00 6.95  ? 48  HIS A CG  1 
ATOM   369  N  ND1 . HIS A 1 48  ? 18.089 -14.405 13.511  1.00 7.60  ? 48  HIS A ND1 1 
ATOM   370  C  CD2 . HIS A 1 48  ? 17.370 -13.581 15.402  1.00 7.91  ? 48  HIS A CD2 1 
ATOM   371  C  CE1 . HIS A 1 48  ? 17.264 -15.291 14.027  1.00 8.51  ? 48  HIS A CE1 1 
ATOM   372  N  NE2 . HIS A 1 48  ? 16.810 -14.823 15.174  1.00 8.39  ? 48  HIS A NE2 1 
ATOM   373  N  N   . GLU A 1 49  ? 22.148 -11.748 13.526  1.00 7.19  ? 49  GLU A N   1 
ATOM   374  C  CA  . GLU A 1 49  ? 23.434 -11.182 13.123  1.00 6.83  ? 49  GLU A CA  1 
ATOM   375  C  C   . GLU A 1 49  ? 23.330 -9.871  12.357  1.00 6.85  ? 49  GLU A C   1 
ATOM   376  O  O   . GLU A 1 49  ? 24.127 -8.964  12.606  1.00 7.15  ? 49  GLU A O   1 
ATOM   377  C  CB  . GLU A 1 49  ? 24.209 -12.190 12.285  1.00 7.89  ? 49  GLU A CB  1 
ATOM   378  C  CG  A GLU A 1 49  ? 25.624 -11.750 11.943  0.70 7.66  ? 49  GLU A CG  1 
ATOM   379  C  CG  B GLU A 1 49  ? 25.632 -11.767 11.942  0.30 8.57  ? 49  GLU A CG  1 
ATOM   380  C  CD  A GLU A 1 49  ? 26.365 -12.748 11.086  0.70 7.99  ? 49  GLU A CD  1 
ATOM   381  C  CD  B GLU A 1 49  ? 26.357 -12.772 11.072  0.30 9.27  ? 49  GLU A CD  1 
ATOM   382  O  OE1 A GLU A 1 49  ? 25.777 -13.792 10.737  0.70 9.75  ? 49  GLU A OE1 1 
ATOM   383  O  OE1 B GLU A 1 49  ? 25.729 -13.765 10.649  0.30 9.44  ? 49  GLU A OE1 1 
ATOM   384  O  OE2 A GLU A 1 49  ? 27.539 -12.475 10.756  0.70 10.34 ? 49  GLU A OE2 1 
ATOM   385  O  OE2 B GLU A 1 49  ? 27.559 -12.560 10.805  0.30 9.88  ? 49  GLU A OE2 1 
ATOM   386  N  N   . PHE A 1 50  ? 22.388 -9.780  11.419  1.00 6.15  ? 50  PHE A N   1 
ATOM   387  C  CA  . PHE A 1 50  ? 22.327 -8.614  10.513  1.00 6.37  ? 50  PHE A CA  1 
ATOM   388  C  C   . PHE A 1 50  ? 21.220 -7.657  10.899  1.00 6.93  ? 50  PHE A C   1 
ATOM   389  O  O   . PHE A 1 50  ? 20.088 -8.067  11.165  1.00 7.07  ? 50  PHE A O   1 
ATOM   390  C  CB  . PHE A 1 50  ? 22.159 -9.057  9.055   1.00 7.27  ? 50  PHE A CB  1 
ATOM   391  C  CG  . PHE A 1 50  ? 23.147 -10.102 8.643   1.00 8.00  ? 50  PHE A CG  1 
ATOM   392  C  CD1 . PHE A 1 50  ? 24.510 -9.866  8.768   1.00 8.46  ? 50  PHE A CD1 1 
ATOM   393  C  CD2 . PHE A 1 50  ? 22.717 -11.331 8.156   1.00 7.36  ? 50  PHE A CD2 1 
ATOM   394  C  CE1 . PHE A 1 50  ? 25.434 -10.846 8.429   1.00 8.96  ? 50  PHE A CE1 1 
ATOM   395  C  CE2 . PHE A 1 50  ? 23.635 -12.308 7.807   1.00 9.35  ? 50  PHE A CE2 1 
ATOM   396  C  CZ  . PHE A 1 50  ? 24.991 -12.066 7.941   1.00 11.97 ? 50  PHE A CZ  1 
ATOM   397  N  N   . GLY A 1 51  ? 21.550 -6.369  10.897  1.00 6.64  ? 51  GLY A N   1 
ATOM   398  C  CA  . GLY A 1 51  ? 20.551 -5.312  11.021  1.00 7.20  ? 51  GLY A CA  1 
ATOM   399  C  C   . GLY A 1 51  ? 19.923 -5.014  9.676   1.00 7.13  ? 51  GLY A C   1 
ATOM   400  O  O   . GLY A 1 51  ? 19.786 -3.859  9.297   1.00 7.74  ? 51  GLY A O   1 
ATOM   401  N  N   . ASP A 1 52  ? 19.530 -6.062  8.963   1.00 8.98  ? 52  ASP A N   1 
ATOM   402  C  CA  . ASP A 1 52  ? 19.037 -5.959  7.607   1.00 9.41  ? 52  ASP A CA  1 
ATOM   403  C  C   . ASP A 1 52  ? 17.584 -6.337  7.719   1.00 8.86  ? 52  ASP A C   1 
ATOM   404  O  O   . ASP A 1 52  ? 17.256 -7.518  7.923   1.00 9.62  ? 52  ASP A O   1 
ATOM   405  C  CB  . ASP A 1 52  ? 19.805 -6.911  6.670   1.00 9.86  ? 52  ASP A CB  1 
ATOM   406  C  CG  . ASP A 1 52  ? 19.350 -6.815  5.218   1.00 10.89 ? 52  ASP A CG  1 
ATOM   407  O  OD1 . ASP A 1 52  ? 18.200 -6.396  4.959   1.00 10.63 ? 52  ASP A OD1 1 
ATOM   408  O  OD2 . ASP A 1 52  ? 20.154 -7.163  4.326   1.00 13.74 ? 52  ASP A OD2 1 
ATOM   409  N  N   . ASN A 1 53  ? 16.710 -5.336  7.627   1.00 10.30 ? 53  ASN A N   1 
ATOM   410  C  CA  . ASN A 1 53  ? 15.271 -5.590  7.640   1.00 12.87 ? 53  ASN A CA  1 
ATOM   411  C  C   . ASN A 1 53  ? 14.615 -5.247  6.298   1.00 11.24 ? 53  ASN A C   1 
ATOM   412  O  O   . ASN A 1 53  ? 13.417 -4.960  6.232   1.00 12.19 ? 53  ASN A O   1 
ATOM   413  C  CB  . ASN A 1 53  ? 14.609 -4.896  8.838   1.00 13.99 ? 53  ASN A CB  1 
ATOM   414  C  CG  . ASN A 1 53  ? 14.965 -5.556  10.186  1.00 15.86 ? 53  ASN A CG  1 
ATOM   415  O  OD1 . ASN A 1 53  ? 15.614 -6.626  10.260  1.00 16.66 ? 53  ASN A OD1 1 
ATOM   416  N  ND2 . ASN A 1 53  ? 14.537 -4.919  11.261  1.00 18.21 ? 53  ASN A ND2 1 
ATOM   417  N  N   . THR A 1 54  ? 15.390 -5.367  5.219   1.00 10.20 ? 54  THR A N   1 
ATOM   418  C  CA  . THR A 1 54  ? 14.906 -5.035  3.880   1.00 12.38 ? 54  THR A CA  1 
ATOM   419  C  C   . THR A 1 54  ? 13.776 -5.946  3.410   1.00 11.69 ? 54  THR A C   1 
ATOM   420  O  O   . THR A 1 54  ? 12.894 -5.481  2.696   1.00 11.48 ? 54  THR A O   1 
ATOM   421  C  CB  . THR A 1 54  ? 16.040 -5.023  2.842   1.00 12.07 ? 54  THR A CB  1 
ATOM   422  O  OG1 . THR A 1 54  ? 16.720 -6.275  2.854   1.00 11.94 ? 54  THR A OG1 1 
ATOM   423  C  CG2 . THR A 1 54  ? 17.034 -3.904  3.142   1.00 13.26 ? 54  THR A CG2 1 
ATOM   424  N  N   . ALA A 1 55  ? 13.794 -7.221  3.822   1.00 12.36 ? 55  ALA A N   1 
ATOM   425  C  CA  . ALA A 1 55  ? 12.648 -8.119  3.610   1.00 15.14 ? 55  ALA A CA  1 
ATOM   426  C  C   . ALA A 1 55  ? 11.933 -8.436  4.922   1.00 16.39 ? 55  ALA A C   1 
ATOM   427  O  O   . ALA A 1 55  ? 11.430 -9.546  5.117   1.00 19.58 ? 55  ALA A O   1 
ATOM   428  C  CB  . ALA A 1 55  ? 13.087 -9.400  2.917   1.00 17.80 ? 55  ALA A CB  1 
ATOM   429  N  N   . GLY A 1 56  ? 11.855 -7.453  5.814   1.00 14.59 ? 56  GLY A N   1 
ATOM   430  C  CA  . GLY A 1 56  ? 11.336 -7.680  7.152   1.00 14.71 ? 56  GLY A CA  1 
ATOM   431  C  C   . GLY A 1 56  ? 12.316 -8.508  7.960   1.00 9.28  ? 56  GLY A C   1 
ATOM   432  O  O   . GLY A 1 56  ? 13.526 -8.394  7.788   1.00 12.70 ? 56  GLY A O   1 
ATOM   433  N  N   . CYS A 1 57  ? 11.793 -9.364  8.831   1.00 8.95  ? 57  CYS A N   1 
ATOM   434  C  CA  . CYS A 1 57  ? 12.649 -10.116 9.750   1.00 9.86  ? 57  CYS A CA  1 
ATOM   435  C  C   . CYS A 1 57  ? 13.437 -11.236 9.097   1.00 10.77 ? 57  CYS A C   1 
ATOM   436  O  O   . CYS A 1 57  ? 14.455 -11.670 9.639   1.00 11.03 ? 57  CYS A O   1 
ATOM   437  C  CB  . CYS A 1 57  ? 11.815 -10.677 10.876  1.00 9.86  ? 57  CYS A CB  1 
ATOM   438  S  SG  . CYS A 1 57  ? 10.857 -9.413  11.727  1.00 11.12 ? 57  CYS A SG  1 
ATOM   439  N  N   . THR A 1 58  ? 12.985 -11.685 7.934   1.00 11.59 ? 58  THR A N   1 
ATOM   440  C  CA  . THR A 1 58  ? 13.647 -12.791 7.243   1.00 13.80 ? 58  THR A CA  1 
ATOM   441  C  C   . THR A 1 58  ? 15.089 -12.512 6.767   1.00 14.16 ? 58  THR A C   1 
ATOM   442  O  O   . THR A 1 58  ? 15.854 -13.457 6.590   1.00 21.55 ? 58  THR A O   1 
ATOM   443  C  CB  . THR A 1 58  ? 12.785 -13.329 6.080   1.00 17.41 ? 58  THR A CB  1 
ATOM   444  O  OG1 . THR A 1 58  ? 13.325 -14.574 5.619   1.00 21.76 ? 58  THR A OG1 1 
ATOM   445  C  CG2 . THR A 1 58  ? 12.738 -12.372 4.924   1.00 19.08 ? 58  THR A CG2 1 
ATOM   446  N  N   A SER A 1 59  ? 15.437 -11.239 6.556   0.50 15.00 ? 59  SER A N   1 
ATOM   447  N  N   B SER A 1 59  ? 15.432 -11.240 6.558   0.50 13.66 ? 59  SER A N   1 
ATOM   448  C  CA  A SER A 1 59  ? 16.790 -10.837 6.140   0.50 14.09 ? 59  SER A CA  1 
ATOM   449  C  CA  B SER A 1 59  ? 16.778 -10.839 6.139   0.50 12.03 ? 59  SER A CA  1 
ATOM   450  C  C   A SER A 1 59  ? 17.809 -10.707 7.276   0.50 10.48 ? 59  SER A C   1 
ATOM   451  C  C   B SER A 1 59  ? 17.799 -10.686 7.274   0.50 9.48  ? 59  SER A C   1 
ATOM   452  O  O   A SER A 1 59  ? 18.983 -10.435 7.010   0.50 10.01 ? 59  SER A O   1 
ATOM   453  O  O   B SER A 1 59  ? 18.967 -10.394 7.005   0.50 9.20  ? 59  SER A O   1 
ATOM   454  C  CB  A SER A 1 59  ? 16.740 -9.494  5.402   0.50 10.30 ? 59  SER A CB  1 
ATOM   455  C  CB  B SER A 1 59  ? 16.701 -9.527  5.345   0.50 7.34  ? 59  SER A CB  1 
ATOM   456  O  OG  A SER A 1 59  ? 15.904 -9.544  4.265   0.50 12.16 ? 59  SER A OG  1 
ATOM   457  O  OG  B SER A 1 59  ? 15.729 -8.643  5.889   0.50 8.55  ? 59  SER A OG  1 
ATOM   458  N  N   . ALA A 1 60  ? 17.375 -10.897 8.523   1.00 8.42  ? 60  ALA A N   1 
ATOM   459  C  CA  . ALA A 1 60  ? 18.239 -10.693 9.691   1.00 9.55  ? 60  ALA A CA  1 
ATOM   460  C  C   . ALA A 1 60  ? 19.303 -11.778 9.891   1.00 8.61  ? 60  ALA A C   1 
ATOM   461  O  O   . ALA A 1 60  ? 20.231 -11.586 10.677  1.00 8.49  ? 60  ALA A O   1 
ATOM   462  C  CB  . ALA A 1 60  ? 17.397 -10.557 10.953  1.00 10.04 ? 60  ALA A CB  1 
ATOM   463  N  N   . GLY A 1 61  ? 19.172 -12.910 9.195   1.00 7.51  ? 61  GLY A N   1 
ATOM   464  C  CA  . GLY A 1 61  ? 20.205 -13.931 9.228   1.00 7.42  ? 61  GLY A CA  1 
ATOM   465  C  C   . GLY A 1 61  ? 20.173 -14.801 10.475  1.00 7.76  ? 61  GLY A C   1 
ATOM   466  O  O   . GLY A 1 61  ? 19.154 -14.851 11.175  1.00 8.06  ? 61  GLY A O   1 
ATOM   467  N  N   . PRO A 1 62  ? 21.292 -15.489 10.762  1.00 8.23  ? 62  PRO A N   1 
ATOM   468  C  CA  . PRO A 1 62  ? 21.350 -16.415 11.889  1.00 8.51  ? 62  PRO A CA  1 
ATOM   469  C  C   . PRO A 1 62  ? 21.487 -15.703 13.226  1.00 7.38  ? 62  PRO A C   1 
ATOM   470  O  O   . PRO A 1 62  ? 21.556 -14.466 13.283  1.00 7.57  ? 62  PRO A O   1 
ATOM   471  C  CB  . PRO A 1 62  ? 22.600 -17.242 11.584  1.00 9.53  ? 62  PRO A CB  1 
ATOM   472  C  CG  . PRO A 1 62  ? 23.496 -16.293 10.874  1.00 9.98  ? 62  PRO A CG  1 
ATOM   473  C  CD  . PRO A 1 62  ? 22.586 -15.413 10.057  1.00 9.46  ? 62  PRO A CD  1 
ATOM   474  N  N   . HIS A 1 63  ? 21.571 -16.475 14.301  1.00 8.27  ? 63  HIS A N   1 
ATOM   475  C  CA  . HIS A 1 63  ? 21.784 -15.896 15.626  1.00 7.70  ? 63  HIS A CA  1 
ATOM   476  C  C   . HIS A 1 63  ? 23.138 -15.204 15.665  1.00 6.63  ? 63  HIS A C   1 
ATOM   477  O  O   . HIS A 1 63  ? 24.099 -15.711 15.109  1.00 7.54  ? 63  HIS A O   1 
ATOM   478  C  CB  . HIS A 1 63  ? 21.744 -16.985 16.702  1.00 8.46  ? 63  HIS A CB  1 
ATOM   479  C  CG  . HIS A 1 63  ? 20.404 -17.629 16.858  1.00 9.13  ? 63  HIS A CG  1 
ATOM   480  N  ND1 . HIS A 1 63  ? 20.051 -18.365 17.970  1.00 8.89  ? 63  HIS A ND1 1 
ATOM   481  C  CD2 . HIS A 1 63  ? 19.317 -17.623 16.049  1.00 10.12 ? 63  HIS A CD2 1 
ATOM   482  C  CE1 . HIS A 1 63  ? 18.812 -18.793 17.829  1.00 8.43  ? 63  HIS A CE1 1 
ATOM   483  N  NE2 . HIS A 1 63  ? 18.345 -18.365 16.671  1.00 8.99  ? 63  HIS A NE2 1 
ATOM   484  N  N   . PHE A 1 64  ? 23.212 -14.043 16.317  1.00 6.63  ? 64  PHE A N   1 
ATOM   485  C  CA  . PHE A 1 64  ? 24.479 -13.344 16.445  1.00 7.30  ? 64  PHE A CA  1 
ATOM   486  C  C   . PHE A 1 64  ? 25.425 -14.206 17.268  1.00 7.35  ? 64  PHE A C   1 
ATOM   487  O  O   . PHE A 1 64  ? 25.143 -14.505 18.429  1.00 7.27  ? 64  PHE A O   1 
ATOM   488  C  CB  . PHE A 1 64  ? 24.282 -11.959 17.063  1.00 6.82  ? 64  PHE A CB  1 
ATOM   489  C  CG  . PHE A 1 64  ? 25.564 -11.198 17.281  1.00 7.44  ? 64  PHE A CG  1 
ATOM   490  C  CD1 . PHE A 1 64  ? 26.510 -11.096 16.268  1.00 7.86  ? 64  PHE A CD1 1 
ATOM   491  C  CD2 . PHE A 1 64  ? 25.821 -10.570 18.492  1.00 7.87  ? 64  PHE A CD2 1 
ATOM   492  C  CE1 . PHE A 1 64  ? 27.693 -10.402 16.466  1.00 9.26  ? 64  PHE A CE1 1 
ATOM   493  C  CE2 . PHE A 1 64  ? 27.001 -9.865  18.692  1.00 9.01  ? 64  PHE A CE2 1 
ATOM   494  C  CZ  . PHE A 1 64  ? 27.935 -9.779  17.674  1.00 9.20  ? 64  PHE A CZ  1 
ATOM   495  N  N   . ASN A 1 65  ? 26.517 -14.641 16.638  1.00 8.70  ? 65  ASN A N   1 
ATOM   496  C  CA  . ASN A 1 65  ? 27.381 -15.692 17.194  1.00 9.98  ? 65  ASN A CA  1 
ATOM   497  C  C   . ASN A 1 65  ? 28.850 -15.422 16.849  1.00 10.20 ? 65  ASN A C   1 
ATOM   498  O  O   . ASN A 1 65  ? 29.503 -16.227 16.171  1.00 11.34 ? 65  ASN A O   1 
ATOM   499  C  CB  . ASN A 1 65  ? 26.924 -17.066 16.677  1.00 9.81  ? 65  ASN A CB  1 
ATOM   500  C  CG  . ASN A 1 65  ? 27.691 -18.231 17.300  1.00 9.96  ? 65  ASN A CG  1 
ATOM   501  O  OD1 . ASN A 1 65  ? 28.182 -18.150 18.435  1.00 9.48  ? 65  ASN A OD1 1 
ATOM   502  N  ND2 . ASN A 1 65  ? 27.773 -19.342 16.562  1.00 10.76 ? 65  ASN A ND2 1 
ATOM   503  N  N   . PRO A 1 66  ? 29.388 -14.290 17.336  1.00 9.77  ? 66  PRO A N   1 
ATOM   504  C  CA  . PRO A 1 66  ? 30.768 -13.937 16.990  1.00 11.25 ? 66  PRO A CA  1 
ATOM   505  C  C   . PRO A 1 66  ? 31.805 -14.892 17.570  1.00 11.67 ? 66  PRO A C   1 
ATOM   506  O  O   . PRO A 1 66  ? 32.907 -14.949 17.045  1.00 14.16 ? 66  PRO A O   1 
ATOM   507  C  CB  . PRO A 1 66  ? 30.929 -12.534 17.582  1.00 9.75  ? 66  PRO A CB  1 
ATOM   508  C  CG  . PRO A 1 66  ? 29.995 -12.527 18.748  1.00 9.52  ? 66  PRO A CG  1 
ATOM   509  C  CD  . PRO A 1 66  ? 28.812 -13.346 18.316  1.00 9.53  ? 66  PRO A CD  1 
ATOM   510  N  N   . LEU A 1 67  ? 31.448 -15.661 18.606  1.00 12.19 ? 67  LEU A N   1 
ATOM   511  C  CA  . LEU A 1 67  ? 32.396 -16.559 19.272  1.00 13.49 ? 67  LEU A CA  1 
ATOM   512  C  C   . LEU A 1 67  ? 32.261 -18.031 18.840  1.00 13.66 ? 67  LEU A C   1 
ATOM   513  O  O   . LEU A 1 67  ? 32.930 -18.902 19.402  1.00 14.20 ? 67  LEU A O   1 
ATOM   514  C  CB  . LEU A 1 67  ? 32.265 -16.407 20.792  1.00 14.12 ? 67  LEU A CB  1 
ATOM   515  C  CG  . LEU A 1 67  ? 32.473 -14.979 21.322  1.00 16.54 ? 67  LEU A CG  1 
ATOM   516  C  CD1 . LEU A 1 67  ? 31.990 -14.862 22.762  1.00 17.66 ? 67  LEU A CD1 1 
ATOM   517  C  CD2 . LEU A 1 67  ? 33.929 -14.545 21.206  1.00 17.88 ? 67  LEU A CD2 1 
ATOM   518  N  N   . SER A 1 68  ? 31.426 -18.295 17.829  1.00 13.63 ? 68  SER A N   1 
ATOM   519  C  CA  . SER A 1 68  ? 31.291 -19.632 17.223  1.00 13.86 ? 68  SER A CA  1 
ATOM   520  C  C   . SER A 1 68  ? 30.976 -20.719 18.242  1.00 13.63 ? 68  SER A C   1 
ATOM   521  O  O   . SER A 1 68  ? 31.676 -21.736 18.330  1.00 16.49 ? 68  SER A O   1 
ATOM   522  C  CB  . SER A 1 68  ? 32.556 -19.998 16.436  1.00 15.04 ? 68  SER A CB  1 
ATOM   523  O  OG  . SER A 1 68  ? 32.821 -19.027 15.445  1.00 16.52 ? 68  SER A OG  1 
ATOM   524  N  N   . ARG A 1 69  ? 29.917 -20.467 19.006  1.00 13.84 ? 69  ARG A N   1 
ATOM   525  C  CA  . ARG A 1 69  ? 29.445 -21.417 19.989  1.00 12.18 ? 69  ARG A CA  1 
ATOM   526  C  C   . ARG A 1 69  ? 28.133 -22.009 19.494  1.00 10.26 ? 69  ARG A C   1 
ATOM   527  O  O   . ARG A 1 69  ? 27.606 -21.597 18.460  1.00 9.66  ? 69  ARG A O   1 
ATOM   528  C  CB  . ARG A 1 69  ? 29.256 -20.731 21.347  1.00 13.86 ? 69  ARG A CB  1 
ATOM   529  C  CG  . ARG A 1 69  ? 30.493 -20.014 21.889  1.00 17.31 ? 69  ARG A CG  1 
ATOM   530  C  CD  . ARG A 1 69  ? 31.682 -20.941 22.120  1.00 20.21 ? 69  ARG A CD  1 
ATOM   531  N  NE  . ARG A 1 69  ? 31.406 -21.990 23.107  1.00 24.44 ? 69  ARG A NE  1 
ATOM   532  C  CZ  . ARG A 1 69  ? 31.400 -21.830 24.436  1.00 24.68 ? 69  ARG A CZ  1 
ATOM   533  N  NH1 . ARG A 1 69  ? 31.630 -20.642 25.006  1.00 25.85 ? 69  ARG A NH1 1 
ATOM   534  N  NH2 . ARG A 1 69  ? 31.147 -22.884 25.209  1.00 28.21 ? 69  ARG A NH2 1 
ATOM   535  N  N   . LYS A 1 70  ? 27.604 -22.984 20.222  1.00 9.85  ? 70  LYS A N   1 
ATOM   536  C  CA  . LYS A 1 70  ? 26.280 -23.540 19.938  1.00 10.35 ? 70  LYS A CA  1 
ATOM   537  C  C   . LYS A 1 70  ? 25.195 -22.742 20.658  1.00 8.91  ? 70  LYS A C   1 
ATOM   538  O  O   . LYS A 1 70  ? 25.475 -21.945 21.554  1.00 9.08  ? 70  LYS A O   1 
ATOM   539  C  CB  . LYS A 1 70  ? 26.206 -25.009 20.352  1.00 10.93 ? 70  LYS A CB  1 
ATOM   540  C  CG  . LYS A 1 70  ? 27.185 -25.897 19.602  1.00 13.27 ? 70  LYS A CG  1 
ATOM   541  C  CD  . LYS A 1 70  ? 27.078 -27.350 20.035  1.00 16.24 ? 70  LYS A CD  1 
ATOM   542  C  CE  . LYS A 1 70  ? 28.010 -28.214 19.325  0.00 32.47 ? 70  LYS A CE  1 
ATOM   543  N  NZ  . LYS A 1 70  ? 27.505 -28.274 17.922  0.00 33.71 ? 70  LYS A NZ  1 
ATOM   544  N  N   . HIS A 1 71  ? 23.958 -22.967 20.242  1.00 8.87  ? 71  HIS A N   1 
ATOM   545  C  CA  . HIS A 1 71  ? 22.802 -22.281 20.803  1.00 9.03  ? 71  HIS A CA  1 
ATOM   546  C  C   . HIS A 1 71  ? 22.509 -22.737 22.234  1.00 8.32  ? 71  HIS A C   1 
ATOM   547  O  O   . HIS A 1 71  ? 22.610 -23.920 22.556  1.00 9.64  ? 71  HIS A O   1 
ATOM   548  C  CB  . HIS A 1 71  ? 21.570 -22.510 19.939  1.00 9.65  ? 71  HIS A CB  1 
ATOM   549  C  CG  . HIS A 1 71  ? 20.345 -21.828 20.454  1.00 8.16  ? 71  HIS A CG  1 
ATOM   550  N  ND1 . HIS A 1 71  ? 20.143 -20.464 20.370  1.00 8.08  ? 71  HIS A ND1 1 
ATOM   551  C  CD2 . HIS A 1 71  ? 19.282 -22.324 21.132  1.00 8.79  ? 71  HIS A CD2 1 
ATOM   552  C  CE1 . HIS A 1 71  ? 18.994 -20.161 20.944  1.00 8.58  ? 71  HIS A CE1 1 
ATOM   553  N  NE2 . HIS A 1 71  ? 18.450 -21.270 21.412  1.00 8.10  ? 71  HIS A NE2 1 
ATOM   554  N  N   . GLY A 1 72  ? 22.147 -21.785 23.083  1.00 9.12  ? 72  GLY A N   1 
ATOM   555  C  CA  . GLY A 1 72  ? 21.751 -22.081 24.441  1.00 9.13  ? 72  GLY A CA  1 
ATOM   556  C  C   . GLY A 1 72  ? 20.851 -21.013 24.994  1.00 9.01  ? 72  GLY A C   1 
ATOM   557  O  O   . GLY A 1 72  ? 20.278 -20.205 24.256  1.00 9.53  ? 72  GLY A O   1 
ATOM   558  N  N   . GLY A 1 73  ? 20.717 -21.034 26.309  1.00 10.08 ? 73  GLY A N   1 
ATOM   559  C  CA  . GLY A 1 73  ? 19.977 -20.018 27.019  1.00 9.32  ? 73  GLY A CA  1 
ATOM   560  C  C   . GLY A 1 73  ? 20.933 -18.984 27.578  1.00 8.99  ? 73  GLY A C   1 
ATOM   561  O  O   . GLY A 1 73  ? 22.153 -19.209 27.626  1.00 9.22  ? 73  GLY A O   1 
ATOM   562  N  N   . PRO A 1 74  ? 20.381 -17.843 28.025  1.00 8.83  ? 74  PRO A N   1 
ATOM   563  C  CA  . PRO A 1 74  ? 21.212 -16.745 28.497  1.00 9.47  ? 74  PRO A CA  1 
ATOM   564  C  C   . PRO A 1 74  ? 22.051 -17.078 29.731  1.00 9.61  ? 74  PRO A C   1 
ATOM   565  O  O   . PRO A 1 74  ? 23.113 -16.500 29.901  1.00 11.26 ? 74  PRO A O   1 
ATOM   566  C  CB  . PRO A 1 74  ? 20.197 -15.626 28.786  1.00 9.20  ? 74  PRO A CB  1 
ATOM   567  C  CG  . PRO A 1 74  ? 18.883 -16.296 28.909  1.00 9.31  ? 74  PRO A CG  1 
ATOM   568  C  CD  . PRO A 1 74  ? 18.953 -17.490 28.013  1.00 8.73  ? 74  PRO A CD  1 
ATOM   569  N  N   . LYS A 1 75  ? 21.603 -18.030 30.552  1.00 10.05 ? 75  LYS A N   1 
ATOM   570  C  CA  . LYS A 1 75  ? 22.350 -18.426 31.749  1.00 11.27 ? 75  LYS A CA  1 
ATOM   571  C  C   . LYS A 1 75  ? 23.302 -19.603 31.515  1.00 11.22 ? 75  LYS A C   1 
ATOM   572  O  O   . LYS A 1 75  ? 23.892 -20.113 32.460  1.00 12.64 ? 75  LYS A O   1 
ATOM   573  C  CB  . LYS A 1 75  ? 21.372 -18.718 32.891  1.00 14.36 ? 75  LYS A CB  1 
ATOM   574  C  CG  . LYS A 1 75  ? 20.507 -17.519 33.259  1.00 18.74 ? 75  LYS A CG  1 
ATOM   575  C  CD  . LYS A 1 75  ? 21.303 -16.310 33.643  0.00 27.24 ? 75  LYS A CD  1 
ATOM   576  C  CE  . LYS A 1 75  ? 20.592 -14.990 33.416  0.00 35.87 ? 75  LYS A CE  1 
ATOM   577  N  NZ  . LYS A 1 75  ? 21.538 -13.865 33.667  0.00 40.54 ? 75  LYS A NZ  1 
ATOM   578  N  N   . ASP A 1 76  ? 23.461 -20.020 30.263  1.00 11.43 ? 76  ASP A N   1 
ATOM   579  C  CA  . ASP A 1 76  ? 24.398 -21.078 29.908  1.00 11.39 ? 76  ASP A CA  1 
ATOM   580  C  C   . ASP A 1 76  ? 25.736 -20.532 29.458  1.00 11.26 ? 76  ASP A C   1 
ATOM   581  O  O   . ASP A 1 76  ? 25.812 -19.447 28.864  1.00 10.90 ? 76  ASP A O   1 
ATOM   582  C  CB  . ASP A 1 76  ? 23.849 -21.927 28.763  1.00 11.43 ? 76  ASP A CB  1 
ATOM   583  C  CG  . ASP A 1 76  ? 22.534 -22.589 29.094  1.00 13.29 ? 76  ASP A CG  1 
ATOM   584  O  OD1 . ASP A 1 76  ? 22.238 -22.800 30.283  1.00 17.13 ? 76  ASP A OD1 1 
ATOM   585  O  OD2 . ASP A 1 76  ? 21.795 -22.906 28.143  1.00 12.97 ? 76  ASP A OD2 1 
ATOM   586  N  N   A GLU A 1 77  ? 26.787 -21.298 29.736  0.50 11.33 ? 77  GLU A N   1 
ATOM   587  N  N   B GLU A 1 77  ? 26.792 -21.292 29.738  0.50 12.25 ? 77  GLU A N   1 
ATOM   588  C  CA  A GLU A 1 77  ? 28.116 -21.027 29.211  0.50 11.83 ? 77  GLU A CA  1 
ATOM   589  C  CA  B GLU A 1 77  ? 28.122 -21.023 29.199  0.50 13.80 ? 77  GLU A CA  1 
ATOM   590  C  C   A GLU A 1 77  ? 28.145 -21.216 27.689  0.50 10.82 ? 77  GLU A C   1 
ATOM   591  C  C   B GLU A 1 77  ? 28.133 -21.207 27.681  0.50 11.60 ? 77  GLU A C   1 
ATOM   592  O  O   A GLU A 1 77  ? 28.674 -20.369 26.961  0.50 10.49 ? 77  GLU A O   1 
ATOM   593  O  O   B GLU A 1 77  ? 28.642 -20.353 26.948  0.50 11.14 ? 77  GLU A O   1 
ATOM   594  C  CB  A GLU A 1 77  ? 29.120 -21.957 29.884  0.50 12.93 ? 77  GLU A CB  1 
ATOM   595  C  CB  B GLU A 1 77  ? 29.129 -21.972 29.835  0.50 18.00 ? 77  GLU A CB  1 
ATOM   596  C  CG  A GLU A 1 77  ? 30.565 -21.586 29.639  0.50 12.97 ? 77  GLU A CG  1 
ATOM   597  C  CG  B GLU A 1 77  ? 30.571 -21.740 29.425  0.50 22.67 ? 77  GLU A CG  1 
ATOM   598  C  CD  A GLU A 1 77  ? 31.048 -22.057 28.294  0.50 13.01 ? 77  GLU A CD  1 
ATOM   599  C  CD  B GLU A 1 77  ? 31.450 -22.921 29.776  0.50 19.21 ? 77  GLU A CD  1 
ATOM   600  O  OE1 A GLU A 1 77  ? 30.549 -23.104 27.823  0.50 12.78 ? 77  GLU A OE1 1 
ATOM   601  O  OE1 B GLU A 1 77  ? 30.953 -24.056 29.695  0.50 19.39 ? 77  GLU A OE1 1 
ATOM   602  O  OE2 A GLU A 1 77  ? 31.918 -21.387 27.697  0.50 12.89 ? 77  GLU A OE2 1 
ATOM   603  O  OE2 B GLU A 1 77  ? 32.629 -22.730 30.127  0.50 19.14 ? 77  GLU A OE2 1 
ATOM   604  N  N   . GLU A 1 78  ? 27.562 -22.320 27.222  1.00 10.77 ? 78  GLU A N   1 
ATOM   605  C  CA  . GLU A 1 78  ? 27.464 -22.616 25.790  1.00 9.55  ? 78  GLU A CA  1 
ATOM   606  C  C   . GLU A 1 78  ? 26.248 -21.905 25.220  1.00 8.56  ? 78  GLU A C   1 
ATOM   607  O  O   . GLU A 1 78  ? 25.118 -22.389 25.312  1.00 9.21  ? 78  GLU A O   1 
ATOM   608  C  CB  . GLU A 1 78  ? 27.388 -24.130 25.535  1.00 9.92  ? 78  GLU A CB  1 
ATOM   609  C  CG  . GLU A 1 78  ? 27.465 -24.514 24.057  1.00 11.17 ? 78  GLU A CG  1 
ATOM   610  C  CD  . GLU A 1 78  ? 28.868 -24.396 23.475  1.00 11.85 ? 78  GLU A CD  1 
ATOM   611  O  OE1 . GLU A 1 78  ? 29.848 -24.655 24.207  1.00 19.16 ? 78  GLU A OE1 1 
ATOM   612  O  OE2 . GLU A 1 78  ? 29.005 -24.067 22.277  1.00 16.39 ? 78  GLU A OE2 1 
ATOM   613  N  N   . ARG A 1 79  ? 26.486 -20.727 24.654  1.00 7.75  ? 79  ARG A N   1 
ATOM   614  C  CA  . ARG A 1 79  ? 25.423 -19.938 24.044  1.00 7.25  ? 79  ARG A CA  1 
ATOM   615  C  C   . ARG A 1 79  ? 25.997 -19.049 22.958  1.00 7.20  ? 79  ARG A C   1 
ATOM   616  O  O   . ARG A 1 79  ? 27.201 -18.753 22.940  1.00 7.43  ? 79  ARG A O   1 
ATOM   617  C  CB  . ARG A 1 79  ? 24.717 -19.063 25.088  1.00 7.19  ? 79  ARG A CB  1 
ATOM   618  C  CG  . ARG A 1 79  ? 25.657 -18.130 25.833  1.00 6.95  ? 79  ARG A CG  1 
ATOM   619  C  CD  . ARG A 1 79  ? 24.915 -17.117 26.687  1.00 6.65  ? 79  ARG A CD  1 
ATOM   620  N  NE  . ARG A 1 79  ? 24.522 -15.932 25.936  1.00 7.22  ? 79  ARG A NE  1 
ATOM   621  C  CZ  . ARG A 1 79  ? 24.040 -14.823 26.494  1.00 7.35  ? 79  ARG A CZ  1 
ATOM   622  N  NH1 . ARG A 1 79  ? 23.875 -14.756 27.813  1.00 9.81  ? 79  ARG A NH1 1 
ATOM   623  N  NH2 . ARG A 1 79  ? 23.717 -13.776 25.734  1.00 8.79  ? 79  ARG A NH2 1 
ATOM   624  N  N   . HIS A 1 80  ? 25.114 -18.623 22.063  1.00 6.16  ? 80  HIS A N   1 
ATOM   625  C  CA  . HIS A 1 80  ? 25.393 -17.497 21.169  1.00 5.90  ? 80  HIS A CA  1 
ATOM   626  C  C   . HIS A 1 80  ? 25.345 -16.191 21.962  1.00 5.96  ? 80  HIS A C   1 
ATOM   627  O  O   . HIS A 1 80  ? 24.592 -16.079 22.934  1.00 7.02  ? 80  HIS A O   1 
ATOM   628  C  CB  . HIS A 1 80  ? 24.367 -17.453 20.034  1.00 5.75  ? 80  HIS A CB  1 
ATOM   629  C  CG  . HIS A 1 80  ? 24.300 -18.719 19.242  1.00 5.91  ? 80  HIS A CG  1 
ATOM   630  N  ND1 . HIS A 1 80  ? 23.127 -19.248 18.747  1.00 6.67  ? 80  HIS A ND1 1 
ATOM   631  C  CD2 . HIS A 1 80  ? 25.286 -19.559 18.854  1.00 5.98  ? 80  HIS A CD2 1 
ATOM   632  C  CE1 . HIS A 1 80  ? 23.407 -20.347 18.065  1.00 6.24  ? 80  HIS A CE1 1 
ATOM   633  N  NE2 . HIS A 1 80  ? 24.705 -20.562 18.125  1.00 6.73  ? 80  HIS A NE2 1 
ATOM   634  N  N   . VAL A 1 81  ? 26.135 -15.198 21.559  1.00 5.28  ? 81  VAL A N   1 
ATOM   635  C  CA  . VAL A 1 81  ? 25.987 -13.872 22.176  1.00 6.06  ? 81  VAL A CA  1 
ATOM   636  C  C   . VAL A 1 81  ? 24.527 -13.423 22.105  1.00 5.83  ? 81  VAL A C   1 
ATOM   637  O  O   . VAL A 1 81  ? 23.990 -12.922 23.088  1.00 6.67  ? 81  VAL A O   1 
ATOM   638  C  CB  . VAL A 1 81  ? 26.924 -12.808 21.571  1.00 7.67  ? 81  VAL A CB  1 
ATOM   639  C  CG1 . VAL A 1 81  ? 26.505 -11.396 22.002  1.00 6.84  ? 81  VAL A CG1 1 
ATOM   640  C  CG2 . VAL A 1 81  ? 28.363 -13.080 21.986  1.00 9.63  ? 81  VAL A CG2 1 
ATOM   641  N  N   . GLY A 1 82  ? 23.875 -13.629 20.963  1.00 6.37  ? 82  GLY A N   1 
ATOM   642  C  CA  . GLY A 1 82  ? 22.484 -13.229 20.790  1.00 6.92  ? 82  GLY A CA  1 
ATOM   643  C  C   . GLY A 1 82  ? 21.386 -14.028 21.498  1.00 6.54  ? 82  GLY A C   1 
ATOM   644  O  O   . GLY A 1 82  ? 20.201 -13.752 21.294  1.00 6.85  ? 82  GLY A O   1 
ATOM   645  N  N   . ASP A 1 83  ? 21.750 -15.001 22.334  1.00 5.73  ? 83  ASP A N   1 
ATOM   646  C  CA  . ASP A 1 83  ? 20.756 -15.867 22.971  1.00 5.51  ? 83  ASP A CA  1 
ATOM   647  C  C   . ASP A 1 83  ? 20.241 -15.240 24.250  1.00 5.88  ? 83  ASP A C   1 
ATOM   648  O  O   . ASP A 1 83  ? 20.816 -15.431 25.324  1.00 6.14  ? 83  ASP A O   1 
ATOM   649  C  CB  . ASP A 1 83  ? 21.362 -17.243 23.251  1.00 6.13  ? 83  ASP A CB  1 
ATOM   650  C  CG  . ASP A 1 83  ? 21.573 -18.047 21.997  1.00 6.68  ? 83  ASP A CG  1 
ATOM   651  O  OD1 . ASP A 1 83  ? 21.020 -17.663 20.946  1.00 6.91  ? 83  ASP A OD1 1 
ATOM   652  O  OD2 . ASP A 1 83  ? 22.314 -19.051 22.056  1.00 6.71  ? 83  ASP A OD2 1 
ATOM   653  N  N   . LEU A 1 84  ? 19.144 -14.502 24.129  1.00 5.44  ? 84  LEU A N   1 
ATOM   654  C  CA  . LEU A 1 84  ? 18.532 -13.835 25.280  1.00 5.80  ? 84  LEU A CA  1 
ATOM   655  C  C   . LEU A 1 84  ? 17.319 -14.622 25.787  1.00 6.51  ? 84  LEU A C   1 
ATOM   656  O  O   . LEU A 1 84  ? 16.543 -14.128 26.604  1.00 9.57  ? 84  LEU A O   1 
ATOM   657  C  CB  . LEU A 1 84  ? 18.191 -12.369 24.950  1.00 6.37  ? 84  LEU A CB  1 
ATOM   658  C  CG  . LEU A 1 84  ? 19.405 -11.480 24.661  1.00 7.60  ? 84  LEU A CG  1 
ATOM   659  C  CD1 . LEU A 1 84  ? 18.941 -10.065 24.328  1.00 6.56  ? 84  LEU A CD1 1 
ATOM   660  C  CD2 . LEU A 1 84  ? 20.410 -11.441 25.805  1.00 7.66  ? 84  LEU A CD2 1 
ATOM   661  N  N   . GLY A 1 85  ? 17.174 -15.868 25.342  1.00 6.52  ? 85  GLY A N   1 
ATOM   662  C  CA  . GLY A 1 85  ? 16.200 -16.760 25.961  1.00 7.86  ? 85  GLY A CA  1 
ATOM   663  C  C   . GLY A 1 85  ? 14.786 -16.504 25.502  1.00 7.19  ? 85  GLY A C   1 
ATOM   664  O  O   . GLY A 1 85  ? 14.511 -16.490 24.306  1.00 7.46  ? 85  GLY A O   1 
ATOM   665  N  N   . ASN A 1 86  ? 13.887 -16.322 26.462  1.00 6.51  ? 86  ASN A N   1 
ATOM   666  C  CA  . ASN A 1 86  ? 12.487 -16.096 26.187  1.00 6.35  ? 86  ASN A CA  1 
ATOM   667  C  C   . ASN A 1 86  ? 11.990 -14.898 26.955  1.00 7.02  ? 86  ASN A C   1 
ATOM   668  O  O   . ASN A 1 86  ? 12.471 -14.623 28.058  1.00 8.28  ? 86  ASN A O   1 
ATOM   669  C  CB  . ASN A 1 86  ? 11.649 -17.300 26.628  1.00 5.18  ? 86  ASN A CB  1 
ATOM   670  C  CG  . ASN A 1 86  ? 11.886 -18.517 25.779  1.00 6.30  ? 86  ASN A CG  1 
ATOM   671  O  OD1 . ASN A 1 86  ? 11.528 -18.538 24.606  1.00 6.89  ? 86  ASN A OD1 1 
ATOM   672  N  ND2 . ASN A 1 86  ? 12.470 -19.548 26.372  1.00 6.99  ? 86  ASN A ND2 1 
ATOM   673  N  N   . VAL A 1 87  ? 11.014 -14.211 26.373  1.00 7.44  ? 87  VAL A N   1 
ATOM   674  C  CA  . VAL A 1 87  ? 10.164 -13.288 27.123  1.00 8.11  ? 87  VAL A CA  1 
ATOM   675  C  C   . VAL A 1 87  ? 8.834  -13.993 27.381  1.00 7.99  ? 87  VAL A C   1 
ATOM   676  O  O   . VAL A 1 87  ? 8.498  -14.957 26.696  1.00 8.11  ? 87  VAL A O   1 
ATOM   677  C  CB  . VAL A 1 87  ? 9.969  -11.936 26.409  1.00 10.32 ? 87  VAL A CB  1 
ATOM   678  C  CG1 . VAL A 1 87  ? 11.322 -11.274 26.220  1.00 10.07 ? 87  VAL A CG1 1 
ATOM   679  C  CG2 . VAL A 1 87  ? 9.249  -12.087 25.079  1.00 9.46  ? 87  VAL A CG2 1 
ATOM   680  N  N   . THR A 1 88  ? 8.099  -13.516 28.380  1.00 8.63  ? 88  THR A N   1 
ATOM   681  C  CA  . THR A 1 88  ? 6.874  -14.166 28.839  1.00 9.07  ? 88  THR A CA  1 
ATOM   682  C  C   . THR A 1 88  ? 5.720  -13.215 28.651  1.00 8.22  ? 88  THR A C   1 
ATOM   683  O  O   . THR A 1 88  ? 5.725  -12.130 29.227  1.00 9.61  ? 88  THR A O   1 
ATOM   684  C  CB  . THR A 1 88  ? 6.983  -14.544 30.330  1.00 10.03 ? 88  THR A CB  1 
ATOM   685  O  OG1 . THR A 1 88  ? 8.059  -15.465 30.492  1.00 11.45 ? 88  THR A OG1 1 
ATOM   686  C  CG2 . THR A 1 88  ? 5.693  -15.180 30.861  1.00 11.81 ? 88  THR A CG2 1 
ATOM   687  N  N   . ALA A 1 89  ? 4.756  -13.613 27.828  1.00 8.34  ? 89  ALA A N   1 
ATOM   688  C  CA  . ALA A 1 89  ? 3.532  -12.865 27.638  1.00 9.19  ? 89  ALA A CA  1 
ATOM   689  C  C   . ALA A 1 89  ? 2.450  -13.406 28.559  1.00 9.56  ? 89  ALA A C   1 
ATOM   690  O  O   . ALA A 1 89  ? 2.310  -14.629 28.723  1.00 9.24  ? 89  ALA A O   1 
ATOM   691  C  CB  . ALA A 1 89  ? 3.063  -12.932 26.195  1.00 9.95  ? 89  ALA A CB  1 
ATOM   692  N  N   . ASP A 1 90  ? 1.690  -12.474 29.136  1.00 9.51  ? 90  ASP A N   1 
ATOM   693  C  CA  . ASP A 1 90  ? 0.546  -12.782 29.993  1.00 10.60 ? 90  ASP A CA  1 
ATOM   694  C  C   . ASP A 1 90  ? -0.716 -13.032 29.152  1.00 10.89 ? 90  ASP A C   1 
ATOM   695  O  O   . ASP A 1 90  ? -0.648 -13.035 27.915  1.00 10.77 ? 90  ASP A O   1 
ATOM   696  C  CB  . ASP A 1 90  ? 0.360  -11.665 31.047  1.00 10.52 ? 90  ASP A CB  1 
ATOM   697  C  CG  . ASP A 1 90  ? -0.056 -10.310 30.455  1.00 11.13 ? 90  ASP A CG  1 
ATOM   698  O  OD1 . ASP A 1 90  ? -0.582 -10.243 29.320  1.00 11.93 ? 90  ASP A OD1 1 
ATOM   699  O  OD2 . ASP A 1 90  ? 0.138  -9.294  31.165  1.00 13.14 ? 90  ASP A OD2 1 
ATOM   700  N  N   . LYS A 1 91  ? -1.857 -13.239 29.811  1.00 11.25 ? 91  LYS A N   1 
ATOM   701  C  CA  . LYS A 1 91  ? -3.129 -13.489 29.110  1.00 10.41 ? 91  LYS A CA  1 
ATOM   702  C  C   . LYS A 1 91  ? -3.698 -12.287 28.349  1.00 10.82 ? 91  LYS A C   1 
ATOM   703  O  O   . LYS A 1 91  ? -4.624 -12.449 27.555  1.00 11.79 ? 91  LYS A O   1 
ATOM   704  C  CB  . LYS A 1 91  ? -4.204 -14.050 30.069  1.00 10.61 ? 91  LYS A CB  1 
ATOM   705  C  CG  . LYS A 1 91  ? -3.996 -15.507 30.465  1.00 11.28 ? 91  LYS A CG  1 
ATOM   706  C  CD  . LYS A 1 91  ? -4.162 -16.492 29.313  1.00 12.76 ? 91  LYS A CD  1 
ATOM   707  C  CE  . LYS A 1 91  ? -5.602 -16.741 28.925  1.00 14.82 ? 91  LYS A CE  1 
ATOM   708  N  NZ  . LYS A 1 91  ? -5.684 -17.935 28.033  1.00 18.07 ? 91  LYS A NZ  1 
ATOM   709  N  N   . ASP A 1 92  ? -3.171 -11.089 28.597  1.00 10.14 ? 92  ASP A N   1 
ATOM   710  C  CA  . ASP A 1 92  ? -3.514 -9.924  27.776  1.00 10.74 ? 92  ASP A CA  1 
ATOM   711  C  C   . ASP A 1 92  ? -2.624 -9.818  26.544  1.00 10.62 ? 92  ASP A C   1 
ATOM   712  O  O   . ASP A 1 92  ? -2.813 -8.914  25.719  1.00 12.19 ? 92  ASP A O   1 
ATOM   713  C  CB  . ASP A 1 92  ? -3.423 -8.645  28.595  1.00 12.58 ? 92  ASP A CB  1 
ATOM   714  C  CG  . ASP A 1 92  ? -4.331 -8.666  29.808  1.00 15.07 ? 92  ASP A CG  1 
ATOM   715  O  OD1 . ASP A 1 92  ? -5.415 -9.300  29.758  1.00 15.93 ? 92  ASP A OD1 1 
ATOM   716  O  OD2 . ASP A 1 92  ? -3.948 -8.048  30.818  1.00 15.46 ? 92  ASP A OD2 1 
ATOM   717  N  N   . GLY A 1 93  ? -1.656 -10.729 26.437  1.00 9.86  ? 93  GLY A N   1 
ATOM   718  C  CA  . GLY A 1 93  ? -0.721 -10.784 25.320  1.00 9.48  ? 93  GLY A CA  1 
ATOM   719  C  C   . GLY A 1 93  ? 0.461  -9.849  25.461  1.00 9.76  ? 93  GLY A C   1 
ATOM   720  O  O   . GLY A 1 93  ? 1.133  -9.553  24.478  1.00 9.48  ? 93  GLY A O   1 
ATOM   721  N  N   . VAL A 1 94  ? 0.710  -9.403  26.690  1.00 10.21 ? 94  VAL A N   1 
ATOM   722  C  CA  . VAL A 1 94  ? 1.756  -8.447  26.991  1.00 10.20 ? 94  VAL A CA  1 
ATOM   723  C  C   . VAL A 1 94  ? 2.923  -9.120  27.696  1.00 9.68  ? 94  VAL A C   1 
ATOM   724  O  O   . VAL A 1 94  ? 2.735  -9.810  28.706  1.00 9.73  ? 94  VAL A O   1 
ATOM   725  C  CB  . VAL A 1 94  ? 1.235  -7.328  27.906  1.00 14.27 ? 94  VAL A CB  1 
ATOM   726  C  CG1 . VAL A 1 94  ? 2.343  -6.324  28.218  1.00 13.23 ? 94  VAL A CG1 1 
ATOM   727  C  CG2 . VAL A 1 94  ? 0.045  -6.638  27.255  1.00 13.11 ? 94  VAL A CG2 1 
ATOM   728  N  N   . ALA A 1 95  ? 4.122  -8.880  27.173  1.00 9.77  ? 95  ALA A N   1 
ATOM   729  C  CA  . ALA A 1 95  ? 5.370  -9.302  27.801  1.00 10.12 ? 95  ALA A CA  1 
ATOM   730  C  C   . ALA A 1 95  ? 6.120  -8.085  28.334  1.00 8.65  ? 95  ALA A C   1 
ATOM   731  O  O   . ALA A 1 95  ? 6.552  -7.233  27.558  1.00 11.71 ? 95  ALA A O   1 
ATOM   732  C  CB  . ALA A 1 95  ? 6.235  -10.042 26.789  1.00 10.78 ? 95  ALA A CB  1 
ATOM   733  N  N   . ASP A 1 96  ? 6.256  -8.003  29.654  1.00 12.41 ? 96  ASP A N   1 
ATOM   734  C  CA  . ASP A 1 96  ? 7.096  -6.989  30.278  1.00 11.21 ? 96  ASP A CA  1 
ATOM   735  C  C   . ASP A 1 96  ? 8.494  -7.569  30.405  1.00 11.37 ? 96  ASP A C   1 
ATOM   736  O  O   . ASP A 1 96  ? 8.708  -8.580  31.074  1.00 12.27 ? 96  ASP A O   1 
ATOM   737  C  CB  . ASP A 1 96  ? 6.521  -6.558  31.621  1.00 13.43 ? 96  ASP A CB  1 
ATOM   738  C  CG  . ASP A 1 96  ? 5.244  -5.744  31.463  1.00 16.00 ? 96  ASP A CG  1 
ATOM   739  O  OD1 . ASP A 1 96  ? 5.183  -4.849  30.580  1.00 18.61 ? 96  ASP A OD1 1 
ATOM   740  O  OD2 . ASP A 1 96  ? 4.295  -5.994  32.226  1.00 21.97 ? 96  ASP A OD2 1 
ATOM   741  N  N   . VAL A 1 97  ? 9.432  -6.943  29.705  1.00 10.51 ? 97  VAL A N   1 
ATOM   742  C  CA  . VAL A 1 97  ? 10.783 -7.453  29.585  1.00 12.20 ? 97  VAL A CA  1 
ATOM   743  C  C   . VAL A 1 97  ? 11.650 -6.776  30.619  1.00 10.78 ? 97  VAL A C   1 
ATOM   744  O  O   . VAL A 1 97  ? 11.655 -5.551  30.729  1.00 11.65 ? 97  VAL A O   1 
ATOM   745  C  CB  . VAL A 1 97  ? 11.353 -7.199  28.177  1.00 12.31 ? 97  VAL A CB  1 
ATOM   746  C  CG1 . VAL A 1 97  ? 12.797 -7.670  28.071  1.00 12.11 ? 97  VAL A CG1 1 
ATOM   747  C  CG2 . VAL A 1 97  ? 10.489 -7.882  27.128  1.00 13.86 ? 97  VAL A CG2 1 
ATOM   748  N  N   . SER A 1 98  ? 12.376 -7.588  31.371  0.90 12.34 ? 98  SER A N   1 
ATOM   749  C  CA  . SER A 1 98  ? 13.353 -7.114  32.329  0.90 12.64 ? 98  SER A CA  1 
ATOM   750  C  C   . SER A 1 98  ? 14.421 -8.200  32.420  0.90 10.87 ? 98  SER A C   1 
ATOM   751  O  O   . SER A 1 98  ? 14.185 -9.273  32.990  0.90 15.10 ? 98  SER A O   1 
ATOM   752  C  CB  . SER A 1 98  ? 12.699 -6.853  33.684  0.90 15.77 ? 98  SER A CB  1 
ATOM   753  O  OG  . SER A 1 98  ? 13.630 -6.274  34.574  0.90 18.96 ? 98  SER A OG  1 
ATOM   754  N  N   . ILE A 1 99  ? 15.574 -7.925  31.821  1.00 11.68 ? 99  ILE A N   1 
ATOM   755  C  CA  . ILE A 1 99  ? 16.678 -8.887  31.681  1.00 12.45 ? 99  ILE A CA  1 
ATOM   756  C  C   . ILE A 1 99  ? 17.947 -8.120  32.061  1.00 10.63 ? 99  ILE A C   1 
ATOM   757  O  O   . ILE A 1 99  ? 18.057 -6.919  31.788  1.00 10.57 ? 99  ILE A O   1 
ATOM   758  C  CB  . ILE A 1 99  ? 16.782 -9.407  30.210  1.00 13.90 ? 99  ILE A CB  1 
ATOM   759  C  CG1 . ILE A 1 99  ? 15.599 -10.315 29.845  1.00 16.04 ? 99  ILE A CG1 1 
ATOM   760  C  CG2 . ILE A 1 99  ? 18.071 -10.181 29.952  1.00 14.52 ? 99  ILE A CG2 1 
ATOM   761  C  CD1 . ILE A 1 99  ? 15.398 -10.494 28.348  1.00 17.85 ? 99  ILE A CD1 1 
ATOM   762  N  N   . GLU A 1 100 ? 18.889 -8.798  32.704  1.00 10.93 ? 100 GLU A N   1 
ATOM   763  C  CA  . GLU A 1 100 ? 20.261 -8.330  32.779  1.00 13.15 ? 100 GLU A CA  1 
ATOM   764  C  C   . GLU A 1 100 ? 21.111 -9.412  32.150  1.00 9.88  ? 100 GLU A C   1 
ATOM   765  O  O   . GLU A 1 100 ? 20.953 -10.586 32.481  1.00 10.34 ? 100 GLU A O   1 
ATOM   766  C  CB  . GLU A 1 100 ? 20.700 -8.084  34.217  1.00 14.31 ? 100 GLU A CB  1 
ATOM   767  C  CG  . GLU A 1 100 ? 22.085 -7.466  34.343  1.00 20.97 ? 100 GLU A CG  1 
ATOM   768  C  CD  . GLU A 1 100 ? 22.423 -7.086  35.772  1.00 23.65 ? 100 GLU A CD  1 
ATOM   769  O  OE1 . GLU A 1 100 ? 21.740 -6.191  36.313  1.00 27.50 ? 100 GLU A OE1 1 
ATOM   770  O  OE2 . GLU A 1 100 ? 23.365 -7.684  36.347  1.00 27.86 ? 100 GLU A OE2 1 
ATOM   771  N  N   . ASP A 1 101 ? 22.000 -9.026  31.240  1.00 9.42  ? 101 ASP A N   1 
ATOM   772  C  CA  . ASP A 1 101 ? 22.862 -9.992  30.572  1.00 9.25  ? 101 ASP A CA  1 
ATOM   773  C  C   . ASP A 1 101 ? 24.301 -9.506  30.549  1.00 9.09  ? 101 ASP A C   1 
ATOM   774  O  O   . ASP A 1 101 ? 24.564 -8.344  30.255  1.00 9.69  ? 101 ASP A O   1 
ATOM   775  C  CB  . ASP A 1 101 ? 22.365 -10.251 29.154  1.00 8.22  ? 101 ASP A CB  1 
ATOM   776  C  CG  . ASP A 1 101 ? 22.997 -11.473 28.536  1.00 8.90  ? 101 ASP A CG  1 
ATOM   777  O  OD1 . ASP A 1 101 ? 22.593 -12.598 28.921  1.00 9.75  ? 101 ASP A OD1 1 
ATOM   778  O  OD2 . ASP A 1 101 ? 23.912 -11.316 27.693  1.00 8.76  ? 101 ASP A OD2 1 
ATOM   779  N  N   . SER A 1 102 ? 25.236 -10.403 30.844  1.00 10.00 ? 102 SER A N   1 
ATOM   780  C  CA  . SER A 1 102 ? 26.648 -10.040 30.899  1.00 10.44 ? 102 SER A CA  1 
ATOM   781  C  C   . SER A 1 102 ? 27.457 -10.519 29.687  1.00 8.52  ? 102 SER A C   1 
ATOM   782  O  O   . SER A 1 102 ? 28.671 -10.329 29.657  1.00 8.63  ? 102 SER A O   1 
ATOM   783  C  CB  . SER A 1 102 ? 27.253 -10.548 32.203  1.00 10.76 ? 102 SER A CB  1 
ATOM   784  O  OG  . SER A 1 102 ? 27.153 -11.947 32.267  1.00 14.54 ? 102 SER A OG  1 
ATOM   785  N  N   . VAL A 1 103 ? 26.788 -11.078 28.680  1.00 6.86  ? 103 VAL A N   1 
ATOM   786  C  CA  . VAL A 1 103 ? 27.463 -11.580 27.473  1.00 6.24  ? 103 VAL A CA  1 
ATOM   787  C  C   . VAL A 1 103 ? 27.303 -10.588 26.316  1.00 7.06  ? 103 VAL A C   1 
ATOM   788  O  O   . VAL A 1 103 ? 28.286 -10.265 25.649  1.00 7.75  ? 103 VAL A O   1 
ATOM   789  C  CB  . VAL A 1 103 ? 26.953 -12.982 27.074  1.00 6.53  ? 103 VAL A CB  1 
ATOM   790  C  CG1 . VAL A 1 103 ? 27.558 -13.450 25.750  1.00 6.89  ? 103 VAL A CG1 1 
ATOM   791  C  CG2 . VAL A 1 103 ? 27.276 -13.975 28.174  1.00 7.58  ? 103 VAL A CG2 1 
ATOM   792  N  N   . ILE A 1 104 ? 26.085 -10.107 26.077  1.00 6.71  ? 104 ILE A N   1 
ATOM   793  C  CA  . ILE A 1 104 ? 25.895 -9.004  25.112  1.00 6.85  ? 104 ILE A CA  1 
ATOM   794  C  C   . ILE A 1 104 ? 26.620 -7.764  25.616  1.00 6.90  ? 104 ILE A C   1 
ATOM   795  O  O   . ILE A 1 104 ? 26.888 -7.623  26.814  1.00 7.37  ? 104 ILE A O   1 
ATOM   796  C  CB  . ILE A 1 104 ? 24.415 -8.627  24.847  1.00 7.43  ? 104 ILE A CB  1 
ATOM   797  C  CG1 . ILE A 1 104 ? 23.719 -8.126  26.129  1.00 7.30  ? 104 ILE A CG1 1 
ATOM   798  C  CG2 . ILE A 1 104 ? 23.673 -9.788  24.198  1.00 7.68  ? 104 ILE A CG2 1 
ATOM   799  C  CD1 . ILE A 1 104 ? 22.297 -7.672  25.931  1.00 7.28  ? 104 ILE A CD1 1 
ATOM   800  N  N   . SER A 1 105 ? 26.911 -6.861  24.692  1.00 6.33  ? 105 SER A N   1 
ATOM   801  C  CA  . SER A 1 105 ? 27.535 -5.583  25.026  1.00 7.68  ? 105 SER A CA  1 
ATOM   802  C  C   . SER A 1 105 ? 26.993 -4.520  24.102  1.00 7.67  ? 105 SER A C   1 
ATOM   803  O  O   . SER A 1 105 ? 26.346 -4.828  23.103  1.00 7.87  ? 105 SER A O   1 
ATOM   804  C  CB  . SER A 1 105 ? 29.058 -5.659  24.910  1.00 8.81  ? 105 SER A CB  1 
ATOM   805  O  OG  . SER A 1 105 ? 29.660 -4.491  25.439  1.00 9.44  ? 105 SER A OG  1 
ATOM   806  N  N   . LEU A 1 106 ? 27.227 -3.265  24.474  1.00 7.72  ? 106 LEU A N   1 
ATOM   807  C  CA  . LEU A 1 106 ? 26.909 -2.130  23.615  1.00 8.27  ? 106 LEU A CA  1 
ATOM   808  C  C   . LEU A 1 106 ? 28.175 -1.492  23.038  1.00 9.67  ? 106 LEU A C   1 
ATOM   809  O  O   . LEU A 1 106 ? 28.100 -0.425  22.440  1.00 10.59 ? 106 LEU A O   1 
ATOM   810  C  CB  . LEU A 1 106 ? 26.031 -1.121  24.358  1.00 8.73  ? 106 LEU A CB  1 
ATOM   811  C  CG  . LEU A 1 106 ? 24.697 -1.665  24.884  1.00 8.54  ? 106 LEU A CG  1 
ATOM   812  C  CD1 . LEU A 1 106 ? 23.912 -0.549  25.568  1.00 7.90  ? 106 LEU A CD1 1 
ATOM   813  C  CD2 . LEU A 1 106 ? 23.843 -2.307  23.787  1.00 8.21  ? 106 LEU A CD2 1 
ATOM   814  N  N   . SER A 1 107 ? 29.320 -2.162  23.187  1.00 9.04  ? 107 SER A N   1 
ATOM   815  C  CA  . SER A 1 107 ? 30.531 -1.818  22.440  1.00 11.16 ? 107 SER A CA  1 
ATOM   816  C  C   . SER A 1 107 ? 31.359 -3.073  22.143  1.00 13.68 ? 107 SER A C   1 
ATOM   817  O  O   . SER A 1 107 ? 31.170 -4.113  22.770  1.00 14.63 ? 107 SER A O   1 
ATOM   818  C  CB  . SER A 1 107 ? 31.360 -0.783  23.198  1.00 15.54 ? 107 SER A CB  1 
ATOM   819  O  OG  . SER A 1 107 ? 31.994 -1.340  24.334  1.00 16.30 ? 107 SER A OG  1 
ATOM   820  N  N   . GLY A 1 108 ? 32.247 -2.971  21.160  1.00 15.65 ? 108 GLY A N   1 
ATOM   821  C  CA  . GLY A 1 108 ? 33.199 -4.035  20.858  1.00 16.13 ? 108 GLY A CA  1 
ATOM   822  C  C   . GLY A 1 108 ? 32.656 -5.229  20.089  1.00 13.64 ? 108 GLY A C   1 
ATOM   823  O  O   . GLY A 1 108 ? 31.590 -5.164  19.477  1.00 12.55 ? 108 GLY A O   1 
ATOM   824  N  N   . ASP A 1 109 ? 33.408 -6.328  20.137  1.00 12.51 ? 109 ASP A N   1 
ATOM   825  C  CA  A ASP A 1 109 ? 33.111 -7.582  19.424  0.50 13.25 ? 109 ASP A CA  1 
ATOM   826  C  CA  B ASP A 1 109 ? 33.041 -7.500  19.329  0.50 13.29 ? 109 ASP A CA  1 
ATOM   827  C  C   . ASP A 1 109 ? 31.752 -8.199  19.792  1.00 11.21 ? 109 ASP A C   1 
ATOM   828  O  O   . ASP A 1 109 ? 31.103 -8.850  18.974  1.00 10.36 ? 109 ASP A O   1 
ATOM   829  C  CB  A ASP A 1 109 ? 34.235 -8.593  19.719  0.50 15.18 ? 109 ASP A CB  1 
ATOM   830  C  CB  B ASP A 1 109 ? 34.204 -8.482  19.168  0.50 16.05 ? 109 ASP A CB  1 
ATOM   831  C  CG  A ASP A 1 109 ? 34.174 -9.822  18.838  0.50 16.36 ? 109 ASP A CG  1 
ATOM   832  C  CG  B ASP A 1 109 ? 34.630 -9.096  20.461  0.50 17.82 ? 109 ASP A CG  1 
ATOM   833  O  OD1 A ASP A 1 109 ? 33.867 -9.681  17.639  0.50 17.03 ? 109 ASP A OD1 1 
ATOM   834  O  OD1 B ASP A 1 109 ? 34.504 -8.428  21.504  0.50 17.98 ? 109 ASP A OD1 1 
ATOM   835  O  OD2 A ASP A 1 109 ? 34.446 -10.926 19.345  0.50 16.10 ? 109 ASP A OD2 1 
ATOM   836  O  OD2 B ASP A 1 109 ? 35.102 -10.248 20.425  0.50 19.99 ? 109 ASP A OD2 1 
ATOM   837  N  N   . HIS A 1 110 ? 31.352 -8.030  21.057  1.00 8.83  ? 110 HIS A N   1 
ATOM   838  C  CA  . HIS A 1 110 ? 30.045 -8.540  21.534  1.00 8.38  ? 110 HIS A CA  1 
ATOM   839  C  C   . HIS A 1 110 ? 28.895 -7.534  21.297  1.00 8.48  ? 110 HIS A C   1 
ATOM   840  O  O   . HIS A 1 110 ? 27.766 -7.761  21.752  1.00 7.84  ? 110 HIS A O   1 
ATOM   841  C  CB  . HIS A 1 110 ? 30.066 -8.882  23.039  1.00 8.97  ? 110 HIS A CB  1 
ATOM   842  C  CG  . HIS A 1 110 ? 31.084 -9.907  23.446  1.00 10.76 ? 110 HIS A CG  1 
ATOM   843  N  ND1 . HIS A 1 110 ? 30.907 -10.716 24.548  1.00 12.41 ? 110 HIS A ND1 1 
ATOM   844  C  CD2 . HIS A 1 110 ? 32.307 -10.214 22.951  1.00 11.78 ? 110 HIS A CD2 1 
ATOM   845  C  CE1 . HIS A 1 110 ? 31.965 -11.496 24.693  1.00 11.33 ? 110 HIS A CE1 1 
ATOM   846  N  NE2 . HIS A 1 110 ? 32.830 -11.209 23.738  1.00 12.97 ? 110 HIS A NE2 1 
ATOM   847  N  N   . CYS A 1 111 ? 29.164 -6.436  20.588  1.00 8.68  ? 111 CYS A N   1 
ATOM   848  C  CA  . CYS A 1 111 ? 28.188 -5.355  20.443  1.00 9.36  ? 111 CYS A CA  1 
ATOM   849  C  C   . CYS A 1 111 ? 26.973 -5.780  19.630  1.00 8.23  ? 111 CYS A C   1 
ATOM   850  O  O   . CYS A 1 111 ? 27.110 -6.389  18.569  1.00 9.01  ? 111 CYS A O   1 
ATOM   851  C  CB  . CYS A 1 111 ? 28.817 -4.127  19.795  1.00 9.88  ? 111 CYS A CB  1 
ATOM   852  S  SG  . CYS A 1 111 ? 27.745 -2.688  19.805  1.00 11.88 ? 111 CYS A SG  1 
ATOM   853  N  N   . ILE A 1 112 ? 25.790 -5.460  20.142  1.00 7.56  ? 112 ILE A N   1 
ATOM   854  C  CA  . ILE A 1 112 ? 24.537 -5.773  19.467  1.00 6.58  ? 112 ILE A CA  1 
ATOM   855  C  C   . ILE A 1 112 ? 23.905 -4.585  18.726  1.00 6.55  ? 112 ILE A C   1 
ATOM   856  O  O   . ILE A 1 112 ? 22.907 -4.743  18.050  1.00 5.82  ? 112 ILE A O   1 
ATOM   857  C  CB  . ILE A 1 112 ? 23.521 -6.430  20.430  1.00 7.74  ? 112 ILE A CB  1 
ATOM   858  C  CG1 . ILE A 1 112 ? 23.108 -5.496  21.589  1.00 8.20  ? 112 ILE A CG1 1 
ATOM   859  C  CG2 . ILE A 1 112 ? 24.108 -7.743  20.950  1.00 7.47  ? 112 ILE A CG2 1 
ATOM   860  C  CD1 . ILE A 1 112 ? 21.936 -6.028  22.387  1.00 9.04  ? 112 ILE A CD1 1 
ATOM   861  N  N   . ILE A 1 113 ? 24.478 -3.392  18.862  1.00 6.36  ? 113 ILE A N   1 
ATOM   862  C  CA  . ILE A 1 113 ? 23.982 -2.237  18.117  1.00 6.54  ? 113 ILE A CA  1 
ATOM   863  C  C   . ILE A 1 113 ? 24.210 -2.489  16.616  1.00 6.67  ? 113 ILE A C   1 
ATOM   864  O  O   . ILE A 1 113 ? 25.261 -2.997  16.211  1.00 7.85  ? 113 ILE A O   1 
ATOM   865  C  CB  . ILE A 1 113 ? 24.633 -0.923  18.603  1.00 6.52  ? 113 ILE A CB  1 
ATOM   866  C  CG1 . ILE A 1 113 ? 24.217 -0.637  20.063  1.00 7.77  ? 113 ILE A CG1 1 
ATOM   867  C  CG2 . ILE A 1 113 ? 24.257 0.235   17.678  1.00 6.69  ? 113 ILE A CG2 1 
ATOM   868  C  CD1 . ILE A 1 113 ? 25.049 0.431   20.746  1.00 8.78  ? 113 ILE A CD1 1 
ATOM   869  N  N   . GLY A 1 114 ? 23.196 -2.159  15.822  1.00 6.00  ? 114 GLY A N   1 
ATOM   870  C  CA  . GLY A 1 114 ? 23.197 -2.366  14.386  1.00 5.86  ? 114 GLY A CA  1 
ATOM   871  C  C   . GLY A 1 114 ? 22.798 -3.760  13.937  1.00 6.30  ? 114 GLY A C   1 
ATOM   872  O  O   . GLY A 1 114 ? 22.863 -4.060  12.749  1.00 7.08  ? 114 GLY A O   1 
ATOM   873  N  N   . ARG A 1 115 ? 22.368 -4.593  14.882  1.00 6.75  ? 115 ARG A N   1 
ATOM   874  C  CA  . ARG A 1 115 ? 21.904 -5.948  14.619  1.00 7.15  ? 115 ARG A CA  1 
ATOM   875  C  C   . ARG A 1 115 ? 20.402 -5.966  14.878  1.00 7.08  ? 115 ARG A C   1 
ATOM   876  O  O   . ARG A 1 115 ? 19.837 -4.940  15.233  1.00 7.81  ? 115 ARG A O   1 
ATOM   877  C  CB  . ARG A 1 115 ? 22.700 -6.916  15.493  1.00 8.33  ? 115 ARG A CB  1 
ATOM   878  C  CG  . ARG A 1 115 ? 24.199 -6.768  15.210  1.00 9.44  ? 115 ARG A CG  1 
ATOM   879  C  CD  . ARG A 1 115 ? 25.066 -7.838  15.833  1.00 10.66 ? 115 ARG A CD  1 
ATOM   880  N  NE  . ARG A 1 115 ? 26.489 -7.549  15.618  1.00 10.83 ? 115 ARG A NE  1 
ATOM   881  C  CZ  . ARG A 1 115 ? 27.198 -7.848  14.524  1.00 11.79 ? 115 ARG A CZ  1 
ATOM   882  N  NH1 . ARG A 1 115 ? 26.655 -8.465  13.476  1.00 14.38 ? 115 ARG A NH1 1 
ATOM   883  N  NH2 . ARG A 1 115 ? 28.492 -7.537  14.485  1.00 11.78 ? 115 ARG A NH2 1 
ATOM   884  N  N   . THR A 1 116 ? 19.747 -7.094  14.631  1.00 6.99  ? 116 THR A N   1 
ATOM   885  C  CA  . THR A 1 116 ? 18.292 -7.194  14.712  1.00 7.18  ? 116 THR A CA  1 
ATOM   886  C  C   . THR A 1 116 ? 17.853 -7.961  15.948  1.00 6.87  ? 116 THR A C   1 
ATOM   887  O  O   . THR A 1 116 ? 18.277 -9.094  16.157  1.00 7.65  ? 116 THR A O   1 
ATOM   888  C  CB  . THR A 1 116 ? 17.698 -7.875  13.463  1.00 7.86  ? 116 THR A CB  1 
ATOM   889  O  OG1 . THR A 1 116 ? 17.990 -7.086  12.307  1.00 7.72  ? 116 THR A OG1 1 
ATOM   890  C  CG2 . THR A 1 116 ? 16.191 -8.020  13.555  1.00 8.75  ? 116 THR A CG2 1 
ATOM   891  N  N   . LEU A 1 117 ? 16.987 -7.342  16.741  1.00 7.06  ? 117 LEU A N   1 
ATOM   892  C  CA  . LEU A 1 117 ? 16.329 -8.011  17.862  1.00 5.91  ? 117 LEU A CA  1 
ATOM   893  C  C   . LEU A 1 117 ? 15.065 -8.644  17.321  1.00 5.92  ? 117 LEU A C   1 
ATOM   894  O  O   . LEU A 1 117 ? 14.325 -8.003  16.587  1.00 5.98  ? 117 LEU A O   1 
ATOM   895  C  CB  . LEU A 1 117 ? 15.975 -6.996  18.953  1.00 5.90  ? 117 LEU A CB  1 
ATOM   896  C  CG  . LEU A 1 117 ? 15.388 -7.543  20.255  1.00 6.17  ? 117 LEU A CG  1 
ATOM   897  C  CD1 . LEU A 1 117 ? 16.438 -8.356  20.987  1.00 7.32  ? 117 LEU A CD1 1 
ATOM   898  C  CD2 . LEU A 1 117 ? 14.903 -6.397  21.135  1.00 6.37  ? 117 LEU A CD2 1 
ATOM   899  N  N   . VAL A 1 118 ? 14.828 -9.908  17.663  1.00 5.45  ? 118 VAL A N   1 
ATOM   900  C  CA  . VAL A 1 118 ? 13.678 -10.649 17.132  1.00 5.91  ? 118 VAL A CA  1 
ATOM   901  C  C   . VAL A 1 118 ? 12.908 -11.316 18.269  1.00 5.46  ? 118 VAL A C   1 
ATOM   902  O  O   . VAL A 1 118 ? 13.508 -11.942 19.145  1.00 5.72  ? 118 VAL A O   1 
ATOM   903  C  CB  . VAL A 1 118 ? 14.124 -11.748 16.145  1.00 6.67  ? 118 VAL A CB  1 
ATOM   904  C  CG1 . VAL A 1 118 ? 12.933 -12.517 15.589  1.00 5.80  ? 118 VAL A CG1 1 
ATOM   905  C  CG2 . VAL A 1 118 ? 14.917 -11.147 14.999  1.00 7.06  ? 118 VAL A CG2 1 
ATOM   906  N  N   . VAL A 1 119 ? 11.584 -11.186 18.219  1.00 4.93  ? 119 VAL A N   1 
ATOM   907  C  CA  . VAL A 1 119 ? 10.696 -11.949 19.083  1.00 5.54  ? 119 VAL A CA  1 
ATOM   908  C  C   . VAL A 1 119 ? 9.958  -13.000 18.253  1.00 6.15  ? 119 VAL A C   1 
ATOM   909  O  O   . VAL A 1 119 ? 9.443  -12.730 17.159  1.00 6.02  ? 119 VAL A O   1 
ATOM   910  C  CB  . VAL A 1 119 ? 9.729  -11.073 19.919  1.00 5.68  ? 119 VAL A CB  1 
ATOM   911  C  CG1 . VAL A 1 119 ? 8.748  -10.286 19.062  1.00 4.53  ? 119 VAL A CG1 1 
ATOM   912  C  CG2 . VAL A 1 119 ? 8.992  -11.943 20.934  1.00 5.09  ? 119 VAL A CG2 1 
ATOM   913  N  N   . HIS A 1 120 ? 9.918  -14.207 18.815  1.00 6.72  ? 120 HIS A N   1 
ATOM   914  C  CA  . HIS A 1 120 ? 9.498  -15.398 18.098  1.00 7.70  ? 120 HIS A CA  1 
ATOM   915  C  C   . HIS A 1 120 ? 8.111  -15.910 18.459  1.00 8.01  ? 120 HIS A C   1 
ATOM   916  O  O   . HIS A 1 120 ? 7.562  -15.616 19.515  1.00 8.21  ? 120 HIS A O   1 
ATOM   917  C  CB  . HIS A 1 120 ? 10.525 -16.499 18.308  1.00 7.87  ? 120 HIS A CB  1 
ATOM   918  C  CG  . HIS A 1 120 ? 11.704 -16.397 17.403  1.00 7.09  ? 120 HIS A CG  1 
ATOM   919  N  ND1 . HIS A 1 120 ? 11.701 -16.925 16.129  1.00 8.07  ? 120 HIS A ND1 1 
ATOM   920  C  CD2 . HIS A 1 120 ? 12.920 -15.831 17.578  1.00 7.00  ? 120 HIS A CD2 1 
ATOM   921  C  CE1 . HIS A 1 120 ? 12.868 -16.685 15.561  1.00 8.61  ? 120 HIS A CE1 1 
ATOM   922  N  NE2 . HIS A 1 120 ? 13.629 -16.026 16.416  1.00 7.69  ? 120 HIS A NE2 1 
ATOM   923  N  N   . GLU A 1 121 ? 7.591  -16.709 17.539  1.00 9.99  ? 121 GLU A N   1 
ATOM   924  C  CA  . GLU A 1 121 ? 6.293  -17.364 17.621  1.00 10.42 ? 121 GLU A CA  1 
ATOM   925  C  C   . GLU A 1 121 ? 6.142  -18.290 18.824  1.00 10.97 ? 121 GLU A C   1 
ATOM   926  O  O   . GLU A 1 121 ? 5.114  -18.266 19.506  1.00 9.68  ? 121 GLU A O   1 
ATOM   927  C  CB  . GLU A 1 121 ? 6.097  -18.183 16.339  1.00 11.51 ? 121 GLU A CB  1 
ATOM   928  C  CG  . GLU A 1 121 ? 4.792  -18.958 16.233  1.00 14.16 ? 121 GLU A CG  1 
ATOM   929  C  CD  . GLU A 1 121 ? 4.824  -20.055 15.181  1.00 18.25 ? 121 GLU A CD  1 
ATOM   930  O  OE1 . GLU A 1 121 ? 5.871  -20.268 14.518  1.00 18.05 ? 121 GLU A OE1 1 
ATOM   931  O  OE2 . GLU A 1 121 ? 3.780  -20.727 15.027  1.00 21.05 ? 121 GLU A OE2 1 
ATOM   932  N  N   . LYS A 1 122 ? 7.164  -19.121 19.024  1.00 11.13 ? 122 LYS A N   1 
ATOM   933  C  CA  . LYS A 1 122 ? 7.172  -20.199 20.005  1.00 10.67 ? 122 LYS A CA  1 
ATOM   934  C  C   . LYS A 1 122 ? 8.290  -19.979 21.004  1.00 9.77  ? 122 LYS A C   1 
ATOM   935  O  O   . LYS A 1 122 ? 9.078  -19.039 20.878  1.00 10.23 ? 122 LYS A O   1 
ATOM   936  C  CB  . LYS A 1 122 ? 7.374  -21.551 19.296  1.00 12.08 ? 122 LYS A CB  1 
ATOM   937  C  CG  . LYS A 1 122 ? 6.365  -21.811 18.189  1.00 16.61 ? 122 LYS A CG  1 
ATOM   938  C  CD  . LYS A 1 122 ? 6.359  -23.262 17.729  1.00 20.81 ? 122 LYS A CD  1 
ATOM   939  C  CE  . LYS A 1 122 ? 7.540  -23.596 16.836  1.00 19.16 ? 122 LYS A CE  1 
ATOM   940  N  NZ  . LYS A 1 122 ? 7.334  -24.898 16.143  1.00 25.47 ? 122 LYS A NZ  1 
ATOM   941  N  N   . ALA A 1 123 ? 8.341  -20.850 22.004  1.00 10.12 ? 123 ALA A N   1 
ATOM   942  C  CA  . ALA A 1 123 ? 9.402  -20.827 22.998  1.00 11.10 ? 123 ALA A CA  1 
ATOM   943  C  C   . ALA A 1 123 ? 10.735 -21.292 22.398  1.00 9.86  ? 123 ALA A C   1 
ATOM   944  O  O   . ALA A 1 123 ? 10.785 -22.222 21.594  1.00 11.01 ? 123 ALA A O   1 
ATOM   945  C  CB  . ALA A 1 123 ? 9.026  -21.698 24.183  1.00 11.11 ? 123 ALA A CB  1 
ATOM   946  N  N   . ASP A 1 124 ? 11.803 -20.599 22.766  1.00 9.67  ? 124 ASP A N   1 
ATOM   947  C  CA  . ASP A 1 124 ? 13.163 -21.072 22.586  1.00 9.12  ? 124 ASP A CA  1 
ATOM   948  C  C   . ASP A 1 124 ? 13.375 -22.197 23.599  1.00 8.77  ? 124 ASP A C   1 
ATOM   949  O  O   . ASP A 1 124 ? 13.204 -21.989 24.793  1.00 9.11  ? 124 ASP A O   1 
ATOM   950  C  CB  . ASP A 1 124 ? 14.132 -19.902 22.829  1.00 8.78  ? 124 ASP A CB  1 
ATOM   951  C  CG  . ASP A 1 124 ? 15.580 -20.222 22.491  1.00 8.09  ? 124 ASP A CG  1 
ATOM   952  O  OD1 . ASP A 1 124 ? 15.998 -21.394 22.565  1.00 8.08  ? 124 ASP A OD1 1 
ATOM   953  O  OD2 . ASP A 1 124 ? 16.325 -19.274 22.184  1.00 9.09  ? 124 ASP A OD2 1 
ATOM   954  N  N   . ASP A 1 125 ? 13.727 -23.391 23.118  1.00 8.67  ? 125 ASP A N   1 
ATOM   955  C  CA  . ASP A 1 125 ? 13.961 -24.542 24.012  1.00 9.04  ? 125 ASP A CA  1 
ATOM   956  C  C   . ASP A 1 125 ? 15.338 -24.498 24.689  1.00 9.29  ? 125 ASP A C   1 
ATOM   957  O  O   . ASP A 1 125 ? 15.690 -25.418 25.426  1.00 10.47 ? 125 ASP A O   1 
ATOM   958  C  CB  . ASP A 1 125 ? 13.706 -25.897 23.297  1.00 9.42  ? 125 ASP A CB  1 
ATOM   959  C  CG  . ASP A 1 125 ? 14.668 -26.186 22.146  1.00 10.86 ? 125 ASP A CG  1 
ATOM   960  O  OD1 . ASP A 1 125 ? 15.824 -25.715 22.153  1.00 10.28 ? 125 ASP A OD1 1 
ATOM   961  O  OD2 . ASP A 1 125 ? 14.259 -26.935 21.223  1.00 11.38 ? 125 ASP A OD2 1 
ATOM   962  N  N   . LEU A 1 126 ? 16.130 -23.462 24.395  1.00 9.57  ? 126 LEU A N   1 
ATOM   963  C  CA  . LEU A 1 126 ? 17.388 -23.166 25.089  1.00 10.19 ? 126 LEU A CA  1 
ATOM   964  C  C   . LEU A 1 126 ? 18.450 -24.251 24.906  1.00 11.07 ? 126 LEU A C   1 
ATOM   965  O  O   . LEU A 1 126 ? 19.332 -24.413 25.752  1.00 11.91 ? 126 LEU A O   1 
ATOM   966  C  CB  . LEU A 1 126 ? 17.144 -22.883 26.583  1.00 10.38 ? 126 LEU A CB  1 
ATOM   967  C  CG  . LEU A 1 126 ? 16.044 -21.876 26.940  1.00 9.79  ? 126 LEU A CG  1 
ATOM   968  C  CD1 . LEU A 1 126 ? 16.092 -21.571 28.428  1.00 11.38 ? 126 LEU A CD1 1 
ATOM   969  C  CD2 . LEU A 1 126 ? 16.155 -20.577 26.155  1.00 8.57  ? 126 LEU A CD2 1 
ATOM   970  N  N   . GLY A 1 127 ? 18.375 -24.966 23.783  1.00 11.10 ? 127 GLY A N   1 
ATOM   971  C  CA  . GLY A 1 127 ? 19.278 -26.081 23.496  1.00 11.82 ? 127 GLY A CA  1 
ATOM   972  C  C   . GLY A 1 127 ? 18.903 -27.415 24.136  1.00 12.99 ? 127 GLY A C   1 
ATOM   973  O  O   . GLY A 1 127 ? 19.692 -28.357 24.067  1.00 15.91 ? 127 GLY A O   1 
ATOM   974  N  N   . LYS A 1 128 ? 17.689 -27.510 24.696  1.00 12.48 ? 128 LYS A N   1 
ATOM   975  C  CA  . LYS A 1 128 ? 17.216 -28.686 25.455  1.00 15.79 ? 128 LYS A CA  1 
ATOM   976  C  C   . LYS A 1 128 ? 15.918 -29.272 24.869  1.00 14.23 ? 128 LYS A C   1 
ATOM   977  O  O   . LYS A 1 128 ? 15.014 -29.685 25.616  1.00 20.32 ? 128 LYS A O   1 
ATOM   978  C  CB  . LYS A 1 128 ? 16.956 -28.289 26.917  1.00 22.52 ? 128 LYS A CB  1 
ATOM   979  C  CG  . LYS A 1 128 ? 18.080 -27.549 27.616  1.00 25.89 ? 128 LYS A CG  1 
ATOM   980  C  CD  . LYS A 1 128 ? 19.275 -28.445 27.880  1.00 26.95 ? 128 LYS A CD  1 
ATOM   981  C  CE  . LYS A 1 128 ? 20.420 -27.649 28.486  1.00 29.05 ? 128 LYS A CE  1 
ATOM   982  N  NZ  . LYS A 1 128 ? 20.121 -27.165 29.861  1.00 31.66 ? 128 LYS A NZ  1 
ATOM   983  N  N   . GLY A 1 129 ? 15.824 -29.319 23.544  0.70 9.37  ? 129 GLY A N   1 
ATOM   984  C  CA  . GLY A 1 129 ? 14.603 -29.760 22.855  0.70 8.52  ? 129 GLY A CA  1 
ATOM   985  C  C   . GLY A 1 129 ? 14.607 -31.203 22.370  0.70 8.12  ? 129 GLY A C   1 
ATOM   986  O  O   . GLY A 1 129 ? 13.550 -31.745 22.040  0.70 9.46  ? 129 GLY A O   1 
ATOM   987  N  N   . GLY A 1 130 ? 15.785 -31.808 22.282  0.70 7.60  ? 130 GLY A N   1 
ATOM   988  C  CA  . GLY A 1 130 ? 15.910 -33.216 21.866  0.70 7.79  ? 130 GLY A CA  1 
ATOM   989  C  C   . GLY A 1 130 ? 15.956 -33.457 20.364  0.70 9.25  ? 130 GLY A C   1 
ATOM   990  O  O   . GLY A 1 130 ? 15.614 -34.545 19.904  0.70 9.51  ? 130 GLY A O   1 
ATOM   991  N  N   . ASN A 1 131 ? 16.378 -32.443 19.604  1.00 11.74 ? 131 ASN A N   1 
ATOM   992  C  CA  . ASN A 1 131 ? 16.662 -32.575 18.165  1.00 14.85 ? 131 ASN A CA  1 
ATOM   993  C  C   . ASN A 1 131 ? 17.899 -31.753 17.784  1.00 16.21 ? 131 ASN A C   1 
ATOM   994  O  O   . ASN A 1 131 ? 18.412 -30.987 18.604  1.00 18.31 ? 131 ASN A O   1 
ATOM   995  C  CB  . ASN A 1 131 ? 15.423 -32.250 17.296  1.00 16.03 ? 131 ASN A CB  1 
ATOM   996  C  CG  . ASN A 1 131 ? 14.992 -30.788 17.348  1.00 16.53 ? 131 ASN A CG  1 
ATOM   997  O  OD1 . ASN A 1 131 ? 15.689 -29.923 17.871  1.00 18.14 ? 131 ASN A OD1 1 
ATOM   998  N  ND2 . ASN A 1 131 ? 13.832 -30.508 16.766  1.00 18.33 ? 131 ASN A ND2 1 
ATOM   999  N  N   . GLU A 1 132 ? 18.380 -31.910 16.553  1.00 15.87 ? 132 GLU A N   1 
ATOM   1000 C  CA  . GLU A 1 132 ? 19.599 -31.208 16.117  1.00 16.76 ? 132 GLU A CA  1 
ATOM   1001 C  C   . GLU A 1 132 ? 19.380 -29.694 16.073  1.00 15.23 ? 132 GLU A C   1 
ATOM   1002 O  O   . GLU A 1 132 ? 20.256 -28.917 16.476  1.00 16.24 ? 132 GLU A O   1 
ATOM   1003 C  CB  . GLU A 1 132 ? 20.068 -31.704 14.747  1.00 21.08 ? 132 GLU A CB  1 
ATOM   1004 C  CG  . GLU A 1 132 ? 21.429 -31.160 14.324  1.00 23.67 ? 132 GLU A CG  1 
ATOM   1005 C  CD  . GLU A 1 132 ? 21.840 -31.568 13.036  0.00 37.20 ? 132 GLU A CD  1 
ATOM   1006 O  OE1 . GLU A 1 132 ? 21.160 -32.434 12.447  0.00 39.51 ? 132 GLU A OE1 1 
ATOM   1007 O  OE2 . GLU A 1 132 ? 22.925 -31.136 12.592  0.00 42.83 ? 132 GLU A OE2 1 
ATOM   1008 N  N   . GLU A 1 133 ? 18.205 -29.294 15.593  1.00 15.62 ? 133 GLU A N   1 
ATOM   1009 C  CA  . GLU A 1 133 ? 17.832 -27.882 15.511  1.00 10.62 ? 133 GLU A CA  1 
ATOM   1010 C  C   . GLU A 1 133 ? 17.902 -27.168 16.866  1.00 9.67  ? 133 GLU A C   1 
ATOM   1011 O  O   . GLU A 1 133 ? 18.251 -25.982 16.926  1.00 11.51 ? 133 GLU A O   1 
ATOM   1012 C  CB  . GLU A 1 133 ? 16.434 -27.728 14.904  1.00 11.09 ? 133 GLU A CB  1 
ATOM   1013 C  CG  . GLU A 1 133 ? 16.095 -26.299 14.503  1.00 15.22 ? 133 GLU A CG  1 
ATOM   1014 C  CD  . GLU A 1 133 ? 14.770 -26.158 13.771  1.00 19.45 ? 133 GLU A CD  1 
ATOM   1015 O  OE1 . GLU A 1 133 ? 14.240 -27.161 13.241  1.00 25.66 ? 133 GLU A OE1 1 
ATOM   1016 O  OE2 . GLU A 1 133 ? 14.252 -25.023 13.731  1.00 26.12 ? 133 GLU A OE2 1 
ATOM   1017 N  N   . SER A 1 134 ? 17.592 -27.883 17.950  1.00 11.89 ? 134 SER A N   1 
ATOM   1018 C  CA  . SER A 1 134 ? 17.639 -27.303 19.288  1.00 11.34 ? 134 SER A CA  1 
ATOM   1019 C  C   . SER A 1 134 ? 18.948 -26.559 19.606  1.00 10.72 ? 134 SER A C   1 
ATOM   1020 O  O   . SER A 1 134 ? 18.904 -25.448 20.145  1.00 12.41 ? 134 SER A O   1 
ATOM   1021 C  CB  . SER A 1 134 ? 17.355 -28.370 20.342  1.00 10.46 ? 134 SER A CB  1 
ATOM   1022 O  OG  . SER A 1 134 ? 17.388 -27.807 21.629  1.00 11.11 ? 134 SER A OG  1 
ATOM   1023 N  N   . THR A 1 135 ? 20.099 -27.129 19.244  1.00 13.73 ? 135 THR A N   1 
ATOM   1024 C  CA  . THR A 1 135 ? 21.382 -26.483 19.540  1.00 14.66 ? 135 THR A CA  1 
ATOM   1025 C  C   . THR A 1 135 ? 21.902 -25.594 18.405  1.00 13.50 ? 135 THR A C   1 
ATOM   1026 O  O   . THR A 1 135 ? 23.043 -25.150 18.449  1.00 14.37 ? 135 THR A O   1 
ATOM   1027 C  CB  . THR A 1 135 ? 22.436 -27.512 19.966  1.00 17.02 ? 135 THR A CB  1 
ATOM   1028 O  OG1 . THR A 1 135 ? 22.531 -28.512 18.957  1.00 19.06 ? 135 THR A OG1 1 
ATOM   1029 C  CG2 . THR A 1 135 ? 22.037 -28.152 21.308  1.00 20.69 ? 135 THR A CG2 1 
ATOM   1030 N  N   . LYS A 1 136 ? 21.057 -25.304 17.416  1.00 13.71 ? 136 LYS A N   1 
ATOM   1031 C  CA  . LYS A 1 136 ? 21.347 -24.277 16.409  1.00 12.96 ? 136 LYS A CA  1 
ATOM   1032 C  C   . LYS A 1 136 ? 20.444 -23.059 16.575  1.00 12.40 ? 136 LYS A C   1 
ATOM   1033 O  O   . LYS A 1 136 ? 20.938 -21.936 16.632  1.00 13.84 ? 136 LYS A O   1 
ATOM   1034 C  CB  . LYS A 1 136 ? 21.185 -24.841 14.997  1.00 15.32 ? 136 LYS A CB  1 
ATOM   1035 C  CG  . LYS A 1 136 ? 22.241 -25.856 14.597  1.00 17.63 ? 136 LYS A CG  1 
ATOM   1036 C  CD  . LYS A 1 136 ? 22.347 -26.158 13.222  0.00 22.70 ? 136 LYS A CD  1 
ATOM   1037 C  CE  . LYS A 1 136 ? 22.549 -25.031 12.222  0.00 18.91 ? 136 LYS A CE  1 
ATOM   1038 N  NZ  . LYS A 1 136 ? 22.552 -25.528 10.819  0.00 16.20 ? 136 LYS A NZ  1 
ATOM   1039 N  N   . THR A 1 137 ? 19.129 -23.276 16.613  1.00 12.03 ? 137 THR A N   1 
ATOM   1040 C  CA  . THR A 1 137 ? 18.152 -22.170 16.723  1.00 12.56 ? 137 THR A CA  1 
ATOM   1041 C  C   . THR A 1 137 ? 17.264 -22.169 17.969  1.00 10.68 ? 137 THR A C   1 
ATOM   1042 O  O   . THR A 1 137 ? 16.673 -21.138 18.299  1.00 10.55 ? 137 THR A O   1 
ATOM   1043 C  CB  . THR A 1 137 ? 17.194 -22.129 15.516  1.00 14.20 ? 137 THR A CB  1 
ATOM   1044 O  OG1 . THR A 1 137 ? 16.254 -23.205 15.611  1.00 13.40 ? 137 THR A OG1 1 
ATOM   1045 C  CG2 . THR A 1 137 ? 17.959 -22.185 14.190  1.00 14.69 ? 137 THR A CG2 1 
ATOM   1046 N  N   . GLY A 1 138 ? 17.130 -23.313 18.632  1.00 9.92  ? 138 GLY A N   1 
ATOM   1047 C  CA  . GLY A 1 138 ? 16.200 -23.452 19.746  1.00 11.01 ? 138 GLY A CA  1 
ATOM   1048 C  C   . GLY A 1 138 ? 14.735 -23.630 19.383  1.00 9.91  ? 138 GLY A C   1 
ATOM   1049 O  O   . GLY A 1 138 ? 13.884 -23.576 20.265  1.00 10.21 ? 138 GLY A O   1 
ATOM   1050 N  N   . ASN A 1 139 ? 14.429 -23.840 18.099  1.00 10.00 ? 139 ASN A N   1 
ATOM   1051 C  CA  . ASN A 1 139 ? 13.077 -24.211 17.651  1.00 10.26 ? 139 ASN A CA  1 
ATOM   1052 C  C   . ASN A 1 139 ? 11.973 -23.221 18.022  1.00 9.98  ? 139 ASN A C   1 
ATOM   1053 O  O   . ASN A 1 139 ? 10.869 -23.636 18.370  1.00 10.48 ? 139 ASN A O   1 
ATOM   1054 C  CB  . ASN A 1 139 ? 12.691 -25.606 18.192  1.00 9.34  ? 139 ASN A CB  1 
ATOM   1055 C  CG  . ASN A 1 139 ? 13.556 -26.700 17.634  1.00 12.26 ? 139 ASN A CG  1 
ATOM   1056 O  OD1 . ASN A 1 139 ? 13.511 -26.977 16.435  1.00 14.04 ? 139 ASN A OD1 1 
ATOM   1057 N  ND2 . ASN A 1 139 ? 14.347 -27.336 18.492  1.00 13.22 ? 139 ASN A ND2 1 
ATOM   1058 N  N   . ALA A 1 140 ? 12.269 -21.924 17.946  1.00 9.54  ? 140 ALA A N   1 
ATOM   1059 C  CA  . ALA A 1 140 ? 11.307 -20.890 18.370  1.00 9.74  ? 140 ALA A CA  1 
ATOM   1060 C  C   . ALA A 1 140 ? 10.327 -20.441 17.270  1.00 8.97  ? 140 ALA A C   1 
ATOM   1061 O  O   . ALA A 1 140 ? 9.540  -19.517 17.482  1.00 9.62  ? 140 ALA A O   1 
ATOM   1062 C  CB  . ALA A 1 140 ? 12.029 -19.691 18.983  1.00 9.23  ? 140 ALA A CB  1 
ATOM   1063 N  N   . GLY A 1 141 ? 10.352 -21.091 16.106  1.00 9.52  ? 141 GLY A N   1 
ATOM   1064 C  CA  . GLY A 1 141 ? 9.340  -20.842 15.100  1.00 9.79  ? 141 GLY A CA  1 
ATOM   1065 C  C   . GLY A 1 141 ? 9.544  -19.504 14.415  1.00 9.52  ? 141 GLY A C   1 
ATOM   1066 O  O   . GLY A 1 141 ? 10.655 -18.951 14.422  1.00 9.44  ? 141 GLY A O   1 
ATOM   1067 N  N   A SER A 1 142 ? 8.455  -18.974 13.857  0.50 9.38  ? 142 SER A N   1 
ATOM   1068 N  N   B SER A 1 142 ? 8.467  -18.971 13.846  0.50 9.34  ? 142 SER A N   1 
ATOM   1069 C  CA  A SER A 1 142 ? 8.490  -17.789 12.995  0.50 9.65  ? 142 SER A CA  1 
ATOM   1070 C  CA  B SER A 1 142 ? 8.554  -17.803 12.972  0.50 9.48  ? 142 SER A CA  1 
ATOM   1071 C  C   A SER A 1 142 ? 8.941  -16.530 13.734  0.50 8.69  ? 142 SER A C   1 
ATOM   1072 C  C   B SER A 1 142 ? 8.929  -16.530 13.724  0.50 8.78  ? 142 SER A C   1 
ATOM   1073 O  O   A SER A 1 142 ? 8.862  -16.454 14.964  0.50 8.63  ? 142 SER A O   1 
ATOM   1074 O  O   B SER A 1 142 ? 8.791  -16.445 14.948  0.50 8.75  ? 142 SER A O   1 
ATOM   1075 C  CB  A SER A 1 142 ? 7.109  -17.530 12.393  0.50 11.35 ? 142 SER A CB  1 
ATOM   1076 C  CB  B SER A 1 142 ? 7.236  -17.588 12.235  0.50 10.89 ? 142 SER A CB  1 
ATOM   1077 O  OG  A SER A 1 142 ? 6.554  -18.695 11.804  0.50 13.06 ? 142 SER A OG  1 
ATOM   1078 O  OG  B SER A 1 142 ? 6.223  -17.130 13.112  0.50 10.95 ? 142 SER A OG  1 
ATOM   1079 N  N   . ARG A 1 143 ? 9.408  -15.551 12.961  1.00 8.70  ? 143 ARG A N   1 
ATOM   1080 C  CA  . ARG A 1 143 ? 9.836  -14.257 13.483  1.00 8.48  ? 143 ARG A CA  1 
ATOM   1081 C  C   . ARG A 1 143 ? 8.613  -13.350 13.446  1.00 8.64  ? 143 ARG A C   1 
ATOM   1082 O  O   . ARG A 1 143 ? 8.162  -12.951 12.374  1.00 10.64 ? 143 ARG A O   1 
ATOM   1083 C  CB  . ARG A 1 143 ? 10.988 -13.712 12.628  1.00 8.92  ? 143 ARG A CB  1 
ATOM   1084 C  CG  . ARG A 1 143 ? 12.173 -14.669 12.592  1.00 9.08  ? 143 ARG A CG  1 
ATOM   1085 C  CD  . ARG A 1 143 ? 13.337 -14.198 11.747  1.00 9.38  ? 143 ARG A CD  1 
ATOM   1086 N  NE  . ARG A 1 143 ? 14.367 -15.235 11.671  1.00 9.76  ? 143 ARG A NE  1 
ATOM   1087 C  CZ  . ARG A 1 143 ? 15.514 -15.127 11.011  1.00 10.17 ? 143 ARG A CZ  1 
ATOM   1088 N  NH1 . ARG A 1 143 ? 15.809 -14.012 10.347  1.00 12.05 ? 143 ARG A NH1 1 
ATOM   1089 N  NH2 . ARG A 1 143 ? 16.375 -16.138 11.018  1.00 9.77  ? 143 ARG A NH2 1 
ATOM   1090 N  N   . LEU A 1 144 ? 8.050  -13.049 14.613  1.00 7.78  ? 144 LEU A N   1 
ATOM   1091 C  CA  . LEU A 1 144 ? 6.797  -12.305 14.672  1.00 7.97  ? 144 LEU A CA  1 
ATOM   1092 C  C   . LEU A 1 144 ? 7.018  -10.807 14.536  1.00 7.49  ? 144 LEU A C   1 
ATOM   1093 O  O   . LEU A 1 144 ? 6.220  -10.107 13.911  1.00 8.27  ? 144 LEU A O   1 
ATOM   1094 C  CB  . LEU A 1 144 ? 6.038  -12.595 15.970  1.00 8.69  ? 144 LEU A CB  1 
ATOM   1095 C  CG  . LEU A 1 144 ? 5.561  -14.032 16.234  1.00 10.87 ? 144 LEU A CG  1 
ATOM   1096 C  CD1 . LEU A 1 144 ? 4.694  -14.056 17.487  1.00 13.52 ? 144 LEU A CD1 1 
ATOM   1097 C  CD2 . LEU A 1 144 ? 4.794  -14.586 15.047  1.00 13.14 ? 144 LEU A CD2 1 
ATOM   1098 N  N   . ALA A 1 145 ? 8.085  -10.322 15.153  1.00 6.87  ? 145 ALA A N   1 
ATOM   1099 C  CA  . ALA A 1 145 ? 8.425  -8.911  15.081  1.00 6.23  ? 145 ALA A CA  1 
ATOM   1100 C  C   . ALA A 1 145 ? 9.905  -8.741  15.297  1.00 5.99  ? 145 ALA A C   1 
ATOM   1101 O  O   . ALA A 1 145 ? 10.560 -9.581  15.933  1.00 6.40  ? 145 ALA A O   1 
ATOM   1102 C  CB  . ALA A 1 145 ? 7.630  -8.112  16.104  1.00 5.87  ? 145 ALA A CB  1 
ATOM   1103 N  N   . CYS A 1 146 ? 10.432 -7.662  14.728  1.00 5.63  ? 146 CYS A N   1 
ATOM   1104 C  CA  . CYS A 1 146 ? 11.844 -7.360  14.836  1.00 6.09  ? 146 CYS A CA  1 
ATOM   1105 C  C   . CYS A 1 146 ? 12.114 -5.890  14.587  1.00 6.51  ? 146 CYS A C   1 
ATOM   1106 O  O   . CYS A 1 146 ? 11.250 -5.148  14.129  1.00 6.52  ? 146 CYS A O   1 
ATOM   1107 C  CB  . CYS A 1 146 ? 12.634 -8.197  13.832  1.00 7.79  ? 146 CYS A CB  1 
ATOM   1108 S  SG  . CYS A 1 146 ? 12.189 -7.903  12.113  1.00 9.40  ? 146 CYS A SG  1 
ATOM   1109 N  N   . GLY A 1 147 ? 13.336 -5.495  14.903  1.00 6.72  ? 147 GLY A N   1 
ATOM   1110 C  CA  . GLY A 1 147 ? 13.835 -4.186  14.538  1.00 6.26  ? 147 GLY A CA  1 
ATOM   1111 C  C   . GLY A 1 147 ? 15.332 -4.107  14.695  1.00 6.70  ? 147 GLY A C   1 
ATOM   1112 O  O   . GLY A 1 147 ? 15.960 -4.980  15.308  1.00 7.03  ? 147 GLY A O   1 
ATOM   1113 N  N   . VAL A 1 148 ? 15.899 -3.033  14.164  1.00 6.51  ? 148 VAL A N   1 
ATOM   1114 C  CA  . VAL A 1 148 ? 17.331 -2.819  14.234  1.00 7.14  ? 148 VAL A CA  1 
ATOM   1115 C  C   . VAL A 1 148 ? 17.634 -2.091  15.539  1.00 6.61  ? 148 VAL A C   1 
ATOM   1116 O  O   . VAL A 1 148 ? 16.965 -1.095  15.886  1.00 7.41  ? 148 VAL A O   1 
ATOM   1117 C  CB  . VAL A 1 148 ? 17.836 -2.012  13.027  1.00 7.76  ? 148 VAL A CB  1 
ATOM   1118 C  CG1 . VAL A 1 148 ? 19.345 -1.838  13.091  1.00 8.28  ? 148 VAL A CG1 1 
ATOM   1119 C  CG2 . VAL A 1 148 ? 17.421 -2.698  11.727  1.00 7.80  ? 148 VAL A CG2 1 
ATOM   1120 N  N   . ILE A 1 149 ? 18.651 -2.571  16.243  1.00 7.64  ? 149 ILE A N   1 
ATOM   1121 C  CA  . ILE A 1 149 ? 19.054 -2.000  17.529  1.00 6.72  ? 149 ILE A CA  1 
ATOM   1122 C  C   . ILE A 1 149 ? 19.864 -0.726  17.252  1.00 6.04  ? 149 ILE A C   1 
ATOM   1123 O  O   . ILE A 1 149 ? 20.908 -0.791  16.614  1.00 7.20  ? 149 ILE A O   1 
ATOM   1124 C  CB  . ILE A 1 149 ? 19.879 -3.005  18.357  1.00 7.13  ? 149 ILE A CB  1 
ATOM   1125 C  CG1 . ILE A 1 149 ? 19.017 -4.247  18.674  1.00 7.34  ? 149 ILE A CG1 1 
ATOM   1126 C  CG2 . ILE A 1 149 ? 20.397 -2.373  19.653  1.00 7.13  ? 149 ILE A CG2 1 
ATOM   1127 C  CD1 . ILE A 1 149 ? 19.756 -5.425  19.261  1.00 8.22  ? 149 ILE A CD1 1 
ATOM   1128 N  N   . GLY A 1 150 ? 19.382 0.418   17.738  1.00 5.63  ? 150 GLY A N   1 
ATOM   1129 C  CA  . GLY A 1 150 ? 20.009 1.711   17.461  1.00 6.07  ? 150 GLY A CA  1 
ATOM   1130 C  C   . GLY A 1 150 ? 20.616 2.353   18.685  1.00 6.40  ? 150 GLY A C   1 
ATOM   1131 O  O   . GLY A 1 150 ? 20.229 2.045   19.805  1.00 7.03  ? 150 GLY A O   1 
ATOM   1132 N  N   . ILE A 1 151 ? 21.557 3.265   18.452  1.00 7.71  ? 151 ILE A N   1 
ATOM   1133 C  CA  . ILE A 1 151 ? 22.174 4.058   19.507  1.00 7.59  ? 151 ILE A CA  1 
ATOM   1134 C  C   . ILE A 1 151 ? 21.118 5.010   20.054  1.00 7.67  ? 151 ILE A C   1 
ATOM   1135 O  O   . ILE A 1 151 ? 20.384 5.633   19.294  1.00 7.33  ? 151 ILE A O   1 
ATOM   1136 C  CB  . ILE A 1 151 ? 23.374 4.874   18.967  1.00 8.56  ? 151 ILE A CB  1 
ATOM   1137 C  CG1 . ILE A 1 151 ? 24.469 3.939   18.456  1.00 8.65  ? 151 ILE A CG1 1 
ATOM   1138 C  CG2 . ILE A 1 151 ? 23.942 5.812   20.037  1.00 9.43  ? 151 ILE A CG2 1 
ATOM   1139 C  CD1 . ILE A 1 151 ? 25.560 4.626   17.659  1.00 8.63  ? 151 ILE A CD1 1 
ATOM   1140 N  N   . ALA A 1 152 ? 21.062 5.112   21.376  1.00 7.18  ? 152 ALA A N   1 
ATOM   1141 C  CA  . ALA A 1 152 ? 20.144 6.012   22.056  1.00 7.35  ? 152 ALA A CA  1 
ATOM   1142 C  C   . ALA A 1 152 ? 20.923 7.076   22.819  1.00 8.63  ? 152 ALA A C   1 
ATOM   1143 O  O   . ALA A 1 152 ? 22.123 6.932   23.101  1.00 9.20  ? 152 ALA A O   1 
ATOM   1144 C  CB  . ALA A 1 152 ? 19.241 5.234   22.998  1.00 5.76  ? 152 ALA A CB  1 
ATOM   1145 N  N   . GLN A 1 153 ? 20.210 8.144   23.150  1.00 9.47  ? 153 GLN A N   1 
ATOM   1146 C  CA  . GLN A 1 153 ? 20.776 9.285   23.845  1.00 12.11 ? 153 GLN A CA  1 
ATOM   1147 C  C   . GLN A 1 153 ? 21.169 8.949   25.271  1.00 13.57 ? 153 GLN A C   1 
ATOM   1148 O  O   . GLN A 1 153 ? 20.433 8.273   25.980  1.00 15.96 ? 153 GLN A O   1 
ATOM   1149 C  CB  . GLN A 1 153 ? 19.750 10.405  23.860  1.00 13.11 ? 153 GLN A CB  1 
ATOM   1150 C  CG  . GLN A 1 153 ? 20.206 11.690  24.520  1.00 13.38 ? 153 GLN A CG  1 
ATOM   1151 C  CD  . GLN A 1 153 ? 19.180 12.782  24.338  1.00 15.63 ? 153 GLN A CD  1 
ATOM   1152 O  OE1 . GLN A 1 153 ? 18.547 12.874  23.285  1.00 15.69 ? 153 GLN A OE1 1 
ATOM   1153 N  NE2 . GLN A 1 153 ? 18.998 13.610  25.364  1.00 16.63 ? 153 GLN A NE2 1 
ATOM   1154 O  OXT . GLN A 1 153 ? 22.224 9.374   25.737  1.00 16.49 ? 153 GLN A OXT 1 
ATOM   1155 N  N   . ALA B 1 1   ? 35.885 -5.756  3.662   1.00 28.11 ? 1   ALA F N   1 
ATOM   1156 C  CA  . ALA B 1 1   ? 34.776 -4.785  3.430   1.00 26.17 ? 1   ALA F CA  1 
ATOM   1157 C  C   . ALA B 1 1   ? 33.753 -4.849  4.549   1.00 23.35 ? 1   ALA F C   1 
ATOM   1158 O  O   . ALA B 1 1   ? 33.532 -5.898  5.145   1.00 26.58 ? 1   ALA F O   1 
ATOM   1159 C  CB  . ALA B 1 1   ? 34.094 -5.037  2.091   1.00 25.57 ? 1   ALA F CB  1 
ATOM   1160 N  N   . THR B 1 2   ? 33.142 -3.704  4.821   1.00 22.90 ? 2   THR F N   1 
ATOM   1161 C  CA  . THR B 1 2   ? 32.024 -3.597  5.733   1.00 17.51 ? 2   THR F CA  1 
ATOM   1162 C  C   . THR B 1 2   ? 30.844 -3.082  4.928   1.00 12.01 ? 2   THR F C   1 
ATOM   1163 O  O   . THR B 1 2   ? 31.003 -2.255  4.022   1.00 13.08 ? 2   THR F O   1 
ATOM   1164 C  CB  . THR B 1 2   ? 32.350 -2.646  6.895   1.00 19.98 ? 2   THR F CB  1 
ATOM   1165 O  OG1 . THR B 1 2   ? 33.541 -3.103  7.543   1.00 21.43 ? 2   THR F OG1 1 
ATOM   1166 C  CG2 . THR B 1 2   ? 31.218 -2.607  7.919   1.00 19.38 ? 2   THR F CG2 1 
ATOM   1167 N  N   . LYS B 1 3   ? 29.660 -3.570  5.276   1.00 10.29 ? 3   LYS F N   1 
ATOM   1168 C  CA  . LYS B 1 3   ? 28.439 -3.236  4.570   1.00 10.73 ? 3   LYS F CA  1 
ATOM   1169 C  C   . LYS B 1 3   ? 27.347 -2.929  5.566   1.00 9.68  ? 3   LYS F C   1 
ATOM   1170 O  O   . LYS B 1 3   ? 27.282 -3.540  6.639   1.00 10.26 ? 3   LYS F O   1 
ATOM   1171 C  CB  . LYS B 1 3   ? 28.019 -4.385  3.655   1.00 13.75 ? 3   LYS F CB  1 
ATOM   1172 C  CG  . LYS B 1 3   ? 28.986 -4.626  2.499   1.00 16.37 ? 3   LYS F CG  1 
ATOM   1173 C  CD  . LYS B 1 3   ? 28.606 -5.850  1.679   1.00 19.90 ? 3   LYS F CD  1 
ATOM   1174 C  CE  . LYS B 1 3   ? 29.571 -6.068  0.529   1.00 24.37 ? 3   LYS F CE  1 
ATOM   1175 N  NZ  . LYS B 1 3   ? 28.992 -7.000  -0.475  1.00 30.07 ? 3   LYS F NZ  1 
ATOM   1176 N  N   . ALA B 1 4   ? 26.505 -1.963  5.226   1.00 9.52  ? 4   ALA F N   1 
ATOM   1177 C  CA  . ALA B 1 4   ? 25.362 -1.621  6.053   1.00 9.07  ? 4   ALA F CA  1 
ATOM   1178 C  C   . ALA B 1 4   ? 24.171 -1.398  5.161   1.00 9.25  ? 4   ALA F C   1 
ATOM   1179 O  O   . ALA B 1 4   ? 24.313 -1.257  3.941   1.00 9.96  ? 4   ALA F O   1 
ATOM   1180 C  CB  . ALA B 1 4   ? 25.655 -0.387  6.897   1.00 8.13  ? 4   ALA F CB  1 
ATOM   1181 N  N   . VAL B 1 5   ? 22.995 -1.374  5.768   1.00 9.13  ? 5   VAL F N   1 
ATOM   1182 C  CA  . VAL B 1 5   ? 21.764 -1.224  5.023   1.00 9.44  ? 5   VAL F CA  1 
ATOM   1183 C  C   . VAL B 1 5   ? 20.743 -0.474  5.868   1.00 9.16  ? 5   VAL F C   1 
ATOM   1184 O  O   . VAL B 1 5   ? 20.827 -0.473  7.104   1.00 8.93  ? 5   VAL F O   1 
ATOM   1185 C  CB  . VAL B 1 5   ? 21.256 -2.607  4.535   1.00 9.75  ? 5   VAL F CB  1 
ATOM   1186 C  CG1 . VAL B 1 5   ? 20.765 -3.462  5.692   1.00 9.72  ? 5   VAL F CG1 1 
ATOM   1187 C  CG2 . VAL B 1 5   ? 20.185 -2.468  3.467   1.00 11.27 ? 5   VAL F CG2 1 
ATOM   1188 N  N   . CYS B 1 6   ? 19.798 0.175   5.200   1.00 9.54  ? 6   CYS F N   1 
ATOM   1189 C  CA  . CYS B 1 6   ? 18.752 0.924   5.878   1.00 8.94  ? 6   CYS F CA  1 
ATOM   1190 C  C   . CYS B 1 6   ? 17.468 0.895   5.082   1.00 8.85  ? 6   CYS F C   1 
ATOM   1191 O  O   . CYS B 1 6   ? 17.488 1.157   3.877   1.00 8.71  ? 6   CYS F O   1 
ATOM   1192 C  CB  . CYS B 1 6   ? 19.206 2.372   6.053   1.00 8.43  ? 6   CYS F CB  1 
ATOM   1193 S  SG  . CYS B 1 6   ? 18.089 3.392   7.028   1.00 10.06 ? 6   CYS F SG  1 
ATOM   1194 N  N   . VAL B 1 7   ? 16.360 0.590   5.758   1.00 9.37  ? 7   VAL F N   1 
ATOM   1195 C  CA  . VAL B 1 7   ? 15.024 0.669   5.170   1.00 10.19 ? 7   VAL F CA  1 
ATOM   1196 C  C   . VAL B 1 7   ? 14.414 1.981   5.616   1.00 10.24 ? 7   VAL F C   1 
ATOM   1197 O  O   . VAL B 1 7   ? 14.283 2.204   6.811   1.00 10.87 ? 7   VAL F O   1 
ATOM   1198 C  CB  . VAL B 1 7   ? 14.116 -0.479  5.645   1.00 12.51 ? 7   VAL F CB  1 
ATOM   1199 C  CG1 . VAL B 1 7   ? 12.720 -0.371  5.036   1.00 16.34 ? 7   VAL F CG1 1 
ATOM   1200 C  CG2 . VAL B 1 7   ? 14.734 -1.808  5.278   1.00 11.96 ? 7   VAL F CG2 1 
ATOM   1201 N  N   . LEU B 1 8   ? 14.078 2.842   4.658   1.00 10.67 ? 8   LEU F N   1 
ATOM   1202 C  CA  A LEU B 1 8   ? 13.427 4.125   4.943   0.70 10.66 ? 8   LEU F CA  1 
ATOM   1203 C  CA  B LEU B 1 8   ? 13.432 4.128   4.937   0.30 10.71 ? 8   LEU F CA  1 
ATOM   1204 C  C   . LEU B 1 8   ? 11.925 3.946   4.855   1.00 11.32 ? 8   LEU F C   1 
ATOM   1205 O  O   . LEU B 1 8   ? 11.419 3.498   3.829   1.00 11.95 ? 8   LEU F O   1 
ATOM   1206 C  CB  A LEU B 1 8   ? 13.866 5.194   3.946   0.70 11.49 ? 8   LEU F CB  1 
ATOM   1207 C  CB  B LEU B 1 8   ? 13.868 5.194   3.928   0.30 11.68 ? 8   LEU F CB  1 
ATOM   1208 C  CG  A LEU B 1 8   ? 15.344 5.594   3.938   0.70 12.76 ? 8   LEU F CG  1 
ATOM   1209 C  CG  B LEU B 1 8   ? 15.303 5.726   3.995   0.30 13.20 ? 8   LEU F CG  1 
ATOM   1210 C  CD1 A LEU B 1 8   ? 15.624 6.547   2.780   0.70 11.78 ? 8   LEU F CD1 1 
ATOM   1211 C  CD1 B LEU B 1 8   ? 16.325 4.638   3.701   0.30 12.66 ? 8   LEU F CD1 1 
ATOM   1212 C  CD2 A LEU B 1 8   ? 15.760 6.234   5.252   0.70 12.85 ? 8   LEU F CD2 1 
ATOM   1213 C  CD2 B LEU B 1 8   ? 15.469 6.873   3.007   0.30 13.30 ? 8   LEU F CD2 1 
ATOM   1214 N  N   . LYS B 1 9   ? 11.221 4.289   5.932   1.00 10.63 ? 9   LYS F N   1 
ATOM   1215 C  CA  . LYS B 1 9   ? 9.761  4.231   5.956   1.00 11.94 ? 9   LYS F CA  1 
ATOM   1216 C  C   . LYS B 1 9   ? 9.188  5.502   6.556   1.00 14.19 ? 9   LYS F C   1 
ATOM   1217 O  O   . LYS B 1 9   ? 9.716  6.036   7.533   1.00 14.42 ? 9   LYS F O   1 
ATOM   1218 C  CB  . LYS B 1 9   ? 9.255  3.010   6.727   1.00 13.40 ? 9   LYS F CB  1 
ATOM   1219 C  CG  . LYS B 1 9   ? 9.409  1.707   5.966   1.00 16.57 ? 9   LYS F CG  1 
ATOM   1220 C  CD  . LYS B 1 9   ? 8.536  0.589   6.529   1.00 19.63 ? 9   LYS F CD  1 
ATOM   1221 C  CE  . LYS B 1 9   ? 8.624  -0.673  5.673   1.00 22.88 ? 9   LYS F CE  1 
ATOM   1222 N  NZ  . LYS B 1 9   ? 7.973  -0.529  4.340   0.10 25.25 ? 9   LYS F NZ  1 
ATOM   1223 N  N   . GLY B 1 10  ? 8.095  5.948   5.941   0.80 16.94 ? 10  GLY F N   1 
ATOM   1224 C  CA  . GLY B 1 10  ? 7.363  7.141   6.327   0.80 18.45 ? 10  GLY F CA  1 
ATOM   1225 C  C   . GLY B 1 10  ? 6.160  7.305   5.397   0.80 20.99 ? 10  GLY F C   1 
ATOM   1226 O  O   . GLY B 1 10  ? 6.045  6.591   4.388   0.80 20.04 ? 10  GLY F O   1 
ATOM   1227 N  N   . ASP B 1 11  ? 5.268  8.235   5.727   1.00 22.72 ? 11  ASP F N   1 
ATOM   1228 C  CA  . ASP B 1 11  ? 3.971  8.358   5.036   1.00 26.35 ? 11  ASP F CA  1 
ATOM   1229 C  C   . ASP B 1 11  ? 4.113  8.804   3.583   1.00 25.65 ? 11  ASP F C   1 
ATOM   1230 O  O   . ASP B 1 11  ? 4.991  9.610   3.254   1.00 27.15 ? 11  ASP F O   1 
ATOM   1231 C  CB  . ASP B 1 11  ? 3.052  9.341   5.761   1.00 27.67 ? 11  ASP F CB  1 
ATOM   1232 C  CG  . ASP B 1 11  ? 2.644  8.866   7.139   1.00 31.39 ? 11  ASP F CG  1 
ATOM   1233 O  OD1 . ASP B 1 11  ? 3.009  7.740   7.534   1.00 34.56 ? 11  ASP F OD1 1 
ATOM   1234 O  OD2 . ASP B 1 11  ? 1.948  9.636   7.833   1.00 37.51 ? 11  ASP F OD2 1 
ATOM   1235 N  N   . GLY B 1 12  ? 3.280  8.232   2.719   1.00 24.58 ? 12  GLY F N   1 
ATOM   1236 C  CA  . GLY B 1 12  ? 3.304  8.537   1.301   1.00 27.15 ? 12  GLY F CA  1 
ATOM   1237 C  C   . GLY B 1 12  ? 2.640  7.453   0.469   1.00 26.75 ? 12  GLY F C   1 
ATOM   1238 O  O   . GLY B 1 12  ? 1.657  7.719   -0.223  1.00 30.37 ? 12  GLY F O   1 
ATOM   1239 N  N   . PRO B 1 13  ? 3.172  6.221   0.531   1.00 26.36 ? 13  PRO F N   1 
ATOM   1240 C  CA  . PRO B 1 13  ? 4.354  5.870   1.315   1.00 24.53 ? 13  PRO F CA  1 
ATOM   1241 C  C   . PRO B 1 13  ? 5.634  6.385   0.679   1.00 21.39 ? 13  PRO F C   1 
ATOM   1242 O  O   . PRO B 1 13  ? 5.874  6.137   -0.502  1.00 21.66 ? 13  PRO F O   1 
ATOM   1243 C  CB  . PRO B 1 13  ? 4.338  4.336   1.297   1.00 27.60 ? 13  PRO F CB  1 
ATOM   1244 C  CG  . PRO B 1 13  ? 3.667  3.985   0.013   1.00 28.88 ? 13  PRO F CG  1 
ATOM   1245 C  CD  . PRO B 1 13  ? 2.644  5.063   -0.220  1.00 28.32 ? 13  PRO F CD  1 
ATOM   1246 N  N   . VAL B 1 14  ? 6.431  7.121   1.446   1.00 20.96 ? 14  VAL F N   1 
ATOM   1247 C  CA  . VAL B 1 14  ? 7.821  7.319   1.089   1.00 19.16 ? 14  VAL F CA  1 
ATOM   1248 C  C   . VAL B 1 14  ? 8.528  6.092   1.613   1.00 19.00 ? 14  VAL F C   1 
ATOM   1249 O  O   . VAL B 1 14  ? 8.492  5.806   2.813   1.00 21.58 ? 14  VAL F O   1 
ATOM   1250 C  CB  . VAL B 1 14  ? 8.440  8.589   1.686   1.00 17.41 ? 14  VAL F CB  1 
ATOM   1251 C  CG1 . VAL B 1 14  ? 9.943  8.633   1.409   1.00 17.07 ? 14  VAL F CG1 1 
ATOM   1252 C  CG2 . VAL B 1 14  ? 7.774  9.809   1.081   1.00 17.51 ? 14  VAL F CG2 1 
ATOM   1253 N  N   . GLN B 1 15  ? 9.149  5.347   0.712   1.00 19.34 ? 15  GLN F N   1 
ATOM   1254 C  CA  . GLN B 1 15  ? 9.882  4.179   1.126   1.00 20.37 ? 15  GLN F CA  1 
ATOM   1255 C  C   . GLN B 1 15  ? 11.077 3.937   0.247   1.00 16.96 ? 15  GLN F C   1 
ATOM   1256 O  O   . GLN B 1 15  ? 11.072 4.212   -0.960  1.00 18.25 ? 15  GLN F O   1 
ATOM   1257 C  CB  . GLN B 1 15  ? 8.974  2.955   1.226   1.00 25.04 ? 15  GLN F CB  1 
ATOM   1258 C  CG  . GLN B 1 15  ? 8.127  2.656   0.006   1.00 29.75 ? 15  GLN F CG  1 
ATOM   1259 C  CD  . GLN B 1 15  ? 7.263  1.429   0.218   1.00 37.28 ? 15  GLN F CD  1 
ATOM   1260 O  OE1 . GLN B 1 15  ? 6.200  1.500   0.840   1.00 43.62 ? 15  GLN F OE1 1 
ATOM   1261 N  NE2 . GLN B 1 15  ? 7.720  0.290   -0.292  1.00 39.55 ? 15  GLN F NE2 1 
ATOM   1262 N  N   . GLY B 1 16  ? 12.128 3.459   0.889   1.00 15.04 ? 16  GLY F N   1 
ATOM   1263 C  CA  . GLY B 1 16  ? 13.406 3.338   0.248   1.00 15.92 ? 16  GLY F CA  1 
ATOM   1264 C  C   . GLY B 1 16  ? 14.258 2.274   0.875   1.00 12.52 ? 16  GLY F C   1 
ATOM   1265 O  O   . GLY B 1 16  ? 13.986 1.817   2.004   1.00 11.53 ? 16  GLY F O   1 
ATOM   1266 N  N   . ILE B 1 17  ? 15.272 1.873   0.112   1.00 12.08 ? 17  ILE F N   1 
ATOM   1267 C  CA  . ILE B 1 17  ? 16.299 0.949   0.546   1.00 12.92 ? 17  ILE F CA  1 
ATOM   1268 C  C   . ILE B 1 17  ? 17.608 1.611   0.197   1.00 10.50 ? 17  ILE F C   1 
ATOM   1269 O  O   . ILE B 1 17  ? 17.829 1.925   -0.973  1.00 10.26 ? 17  ILE F O   1 
ATOM   1270 C  CB  . ILE B 1 17  ? 16.216 -0.399  -0.205  1.00 15.28 ? 17  ILE F CB  1 
ATOM   1271 C  CG1 . ILE B 1 17  ? 14.849 -1.064  0.020   1.00 18.31 ? 17  ILE F CG1 1 
ATOM   1272 C  CG2 . ILE B 1 17  ? 17.375 -1.315  0.193   1.00 16.69 ? 17  ILE F CG2 1 
ATOM   1273 C  CD1 . ILE B 1 17  ? 14.641 -1.646  1.402   1.00 19.60 ? 17  ILE F CD1 1 
ATOM   1274 N  N   . ILE B 1 18  ? 18.467 1.797   1.195   1.00 10.56 ? 18  ILE F N   1 
ATOM   1275 C  CA  . ILE B 1 18  ? 19.788 2.383   0.995   1.00 10.97 ? 18  ILE F CA  1 
ATOM   1276 C  C   . ILE B 1 18  ? 20.874 1.438   1.514   1.00 9.82  ? 18  ILE F C   1 
ATOM   1277 O  O   . ILE B 1 18  ? 20.810 0.953   2.656   1.00 9.76  ? 18  ILE F O   1 
ATOM   1278 C  CB  . ILE B 1 18  ? 19.887 3.771   1.670   1.00 10.14 ? 18  ILE F CB  1 
ATOM   1279 C  CG1 . ILE B 1 18  ? 18.772 4.715   1.171   1.00 10.57 ? 18  ILE F CG1 1 
ATOM   1280 C  CG2 . ILE B 1 18  ? 21.254 4.389   1.435   1.00 10.50 ? 18  ILE F CG2 1 
ATOM   1281 C  CD1 . ILE B 1 18  ? 18.844 5.120   -0.291  1.00 9.98  ? 18  ILE F CD1 1 
ATOM   1282 N  N   . ASN B 1 19  ? 21.855 1.171   0.650   1.00 11.29 ? 19  ASN F N   1 
ATOM   1283 C  CA  . ASN B 1 19  ? 22.992 0.307   0.940   1.00 10.36 ? 19  ASN F CA  1 
ATOM   1284 C  C   . ASN B 1 19  ? 24.234 1.157   1.147   1.00 9.45  ? 19  ASN F C   1 
ATOM   1285 O  O   . ASN B 1 19  ? 24.379 2.205   0.519   1.00 10.13 ? 19  ASN F O   1 
ATOM   1286 C  CB  . ASN B 1 19  ? 23.236 -0.641  -0.233  1.00 11.20 ? 19  ASN F CB  1 
ATOM   1287 C  CG  . ASN B 1 19  ? 22.043 -1.518  -0.531  1.00 11.81 ? 19  ASN F CG  1 
ATOM   1288 O  OD1 . ASN B 1 19  ? 21.851 -2.555  0.104   1.00 12.33 ? 19  ASN F OD1 1 
ATOM   1289 N  ND2 . ASN B 1 19  ? 21.226 -1.107  -1.501  1.00 11.85 ? 19  ASN F ND2 1 
ATOM   1290 N  N   . PHE B 1 20  ? 25.116 0.708   2.033   1.00 10.03 ? 20  PHE F N   1 
ATOM   1291 C  CA  . PHE B 1 20  ? 26.388 1.367   2.312   1.00 10.89 ? 20  PHE F CA  1 
ATOM   1292 C  C   . PHE B 1 20  ? 27.468 0.317   2.183   1.00 8.89  ? 20  PHE F C   1 
ATOM   1293 O  O   . PHE B 1 20  ? 27.325 -0.769  2.752   1.00 10.97 ? 20  PHE F O   1 
ATOM   1294 C  CB  . PHE B 1 20  ? 26.443 1.922   3.742   1.00 8.93  ? 20  PHE F CB  1 
ATOM   1295 C  CG  . PHE B 1 20  ? 25.383 2.945   4.049   1.00 9.61  ? 20  PHE F CG  1 
ATOM   1296 C  CD1 . PHE B 1 20  ? 24.096 2.554   4.430   1.00 10.09 ? 20  PHE F CD1 1 
ATOM   1297 C  CD2 . PHE B 1 20  ? 25.669 4.309   3.973   1.00 9.63  ? 20  PHE F CD2 1 
ATOM   1298 C  CE1 . PHE B 1 20  ? 23.117 3.500   4.715   1.00 9.03  ? 20  PHE F CE1 1 
ATOM   1299 C  CE2 . PHE B 1 20  ? 24.694 5.255   4.253   1.00 10.48 ? 20  PHE F CE2 1 
ATOM   1300 C  CZ  . PHE B 1 20  ? 23.421 4.852   4.631   1.00 9.47  ? 20  PHE F CZ  1 
ATOM   1301 N  N   . GLU B 1 21  ? 28.547 0.634   1.469   1.00 10.80 ? 21  GLU F N   1 
ATOM   1302 C  CA  . GLU B 1 21  ? 29.689 -0.271  1.369   1.00 11.57 ? 21  GLU F CA  1 
ATOM   1303 C  C   . GLU B 1 21  ? 30.997 0.488   1.528   1.00 9.97  ? 21  GLU F C   1 
ATOM   1304 O  O   . GLU B 1 21  ? 31.217 1.521   0.878   1.00 11.60 ? 21  GLU F O   1 
ATOM   1305 C  CB  . GLU B 1 21  ? 29.669 -1.029  0.037   1.00 14.08 ? 21  GLU F CB  1 
ATOM   1306 C  CG  . GLU B 1 21  ? 30.759 -2.093  -0.089  0.70 17.10 ? 21  GLU F CG  1 
ATOM   1307 C  CD  . GLU B 1 21  ? 30.656 -2.917  -1.363  0.70 22.67 ? 21  GLU F CD  1 
ATOM   1308 O  OE1 . GLU B 1 21  ? 29.557 -3.002  -1.953  0.50 22.44 ? 21  GLU F OE1 1 
ATOM   1309 O  OE2 . GLU B 1 21  ? 31.685 -3.494  -1.773  0.50 25.52 ? 21  GLU F OE2 1 
ATOM   1310 N  N   . GLN B 1 22  ? 31.865 -0.036  2.387   1.00 11.76 ? 22  GLN F N   1 
ATOM   1311 C  CA  . GLN B 1 22  ? 33.172 0.559   2.647   1.00 12.77 ? 22  GLN F CA  1 
ATOM   1312 C  C   . GLN B 1 22  ? 34.225 -0.540  2.543   1.00 13.48 ? 22  GLN F C   1 
ATOM   1313 O  O   . GLN B 1 22  ? 34.247 -1.462  3.357   1.00 15.41 ? 22  GLN F O   1 
ATOM   1314 C  CB  . GLN B 1 22  ? 33.175 1.200   4.033   1.00 12.29 ? 22  GLN F CB  1 
ATOM   1315 C  CG  . GLN B 1 22  ? 34.395 2.048   4.333   1.00 12.04 ? 22  GLN F CG  1 
ATOM   1316 C  CD  . GLN B 1 22  ? 34.363 2.648   5.730   1.00 11.07 ? 22  GLN F CD  1 
ATOM   1317 O  OE1 . GLN B 1 22  ? 33.783 2.072   6.653   1.00 12.84 ? 22  GLN F OE1 1 
ATOM   1318 N  NE2 . GLN B 1 22  ? 34.975 3.815   5.890   1.00 11.12 ? 22  GLN F NE2 1 
ATOM   1319 N  N   . LYS B 1 23  ? 35.092 -0.438  1.536   1.00 15.57 ? 23  LYS F N   1 
ATOM   1320 C  CA  . LYS B 1 23  ? 36.094 -1.479  1.256   1.00 18.15 ? 23  LYS F CA  1 
ATOM   1321 C  C   . LYS B 1 23  ? 37.186 -1.575  2.326   1.00 18.92 ? 23  LYS F C   1 
ATOM   1322 O  O   . LYS B 1 23  ? 37.620 -2.674  2.664   1.00 21.25 ? 23  LYS F O   1 
ATOM   1323 C  CB  . LYS B 1 23  ? 36.725 -1.270  -0.128  1.00 20.50 ? 23  LYS F CB  1 
ATOM   1324 C  CG  . LYS B 1 23  ? 35.772 -1.514  -1.288  1.00 24.56 ? 23  LYS F CG  1 
ATOM   1325 C  CD  . LYS B 1 23  ? 34.955 -2.989  -1.036  0.00 27.62 ? 23  LYS F CD  1 
ATOM   1326 C  CE  . LYS B 1 23  ? 35.811 -4.078  -1.636  0.00 24.97 ? 23  LYS F CE  1 
ATOM   1327 N  NZ  . LYS B 1 23  ? 35.106 -5.383  -1.566  0.00 23.47 ? 23  LYS F NZ  1 
ATOM   1328 N  N   . GLU B 1 24  ? 37.621 -0.431  2.854   1.00 24.61 ? 24  GLU F N   1 
ATOM   1329 C  CA  . GLU B 1 24  ? 38.552 -0.389  3.994   1.00 31.19 ? 24  GLU F CA  1 
ATOM   1330 C  C   . GLU B 1 24  ? 38.158 0.717   4.952   1.00 22.06 ? 24  GLU F C   1 
ATOM   1331 O  O   . GLU B 1 24  ? 37.499 1.671   4.556   1.00 21.11 ? 24  GLU F O   1 
ATOM   1332 C  CB  . GLU B 1 24  ? 40.017 -0.229  3.546   1.00 37.86 ? 24  GLU F CB  1 
ATOM   1333 C  CG  . GLU B 1 24  ? 40.340 0.987   2.687   0.50 39.23 ? 24  GLU F CG  1 
ATOM   1334 C  CD  . GLU B 1 24  ? 39.899 0.851   1.243   0.50 34.68 ? 24  GLU F CD  1 
ATOM   1335 O  OE1 . GLU B 1 24  ? 40.061 -0.234  0.644   0.50 33.21 ? 24  GLU F OE1 1 
ATOM   1336 O  OE2 . GLU B 1 24  ? 39.385 1.848   0.702   0.50 34.40 ? 24  GLU F OE2 1 
ATOM   1337 N  N   . SER B 1 25  ? 38.565 0.586   6.212   0.70 23.21 ? 25  SER F N   1 
ATOM   1338 C  CA  . SER B 1 25  ? 38.180 1.548   7.256   0.70 22.35 ? 25  SER F CA  1 
ATOM   1339 C  C   . SER B 1 25  ? 38.615 2.973   6.919   0.70 21.37 ? 25  SER F C   1 
ATOM   1340 O  O   . SER B 1 25  ? 37.935 3.938   7.270   0.70 19.59 ? 25  SER F O   1 
ATOM   1341 C  CB  . SER B 1 25  ? 38.767 1.136   8.604   0.70 25.25 ? 25  SER F CB  1 
ATOM   1342 O  OG  . SER B 1 25  ? 40.174 1.045   8.524   0.70 25.09 ? 25  SER F OG  1 
ATOM   1343 N  N   . ASN B 1 26  ? 39.735 3.088   6.207   1.00 20.52 ? 26  ASN F N   1 
ATOM   1344 C  CA  . ASN B 1 26  ? 40.267 4.377   5.761   1.00 25.45 ? 26  ASN F CA  1 
ATOM   1345 C  C   . ASN B 1 26  ? 39.720 4.860   4.399   1.00 19.00 ? 26  ASN F C   1 
ATOM   1346 O  O   . ASN B 1 26  ? 40.292 5.759   3.785   1.00 14.91 ? 26  ASN F O   1 
ATOM   1347 C  CB  . ASN B 1 26  ? 41.796 4.285   5.697   1.00 30.53 ? 26  ASN F CB  1 
ATOM   1348 C  CG  . ASN B 1 26  ? 42.292 4.382   7.027   0.00 40.71 ? 26  ASN F CG  1 
ATOM   1349 O  OD1 . ASN B 1 26  ? 41.671 4.843   7.975   0.00 55.54 ? 26  ASN F OD1 1 
ATOM   1350 N  ND2 . ASN B 1 26  ? 43.555 3.956   7.126   0.00 49.36 ? 26  ASN F ND2 1 
ATOM   1351 N  N   . GLY B 1 27  ? 38.610 4.301   3.937   1.00 12.78 ? 27  GLY F N   1 
ATOM   1352 C  CA  . GLY B 1 27  ? 38.151 4.572   2.588   1.00 16.55 ? 27  GLY F CA  1 
ATOM   1353 C  C   . GLY B 1 27  ? 36.789 5.201   2.549   1.00 11.72 ? 27  GLY F C   1 
ATOM   1354 O  O   . GLY B 1 27  ? 36.100 5.279   3.574   1.00 11.35 ? 27  GLY F O   1 
ATOM   1355 N  N   . PRO B 1 28  ? 36.381 5.644   1.353   1.00 14.22 ? 28  PRO F N   1 
ATOM   1356 C  CA  . PRO B 1 28  ? 35.064 6.216   1.209   1.00 14.22 ? 28  PRO F CA  1 
ATOM   1357 C  C   . PRO B 1 28  ? 33.992 5.157   1.339   1.00 11.87 ? 28  PRO F C   1 
ATOM   1358 O  O   . PRO B 1 28  ? 34.255 3.962   1.152   1.00 12.97 ? 28  PRO F O   1 
ATOM   1359 C  CB  . PRO B 1 28  ? 35.087 6.782   -0.211  1.00 16.25 ? 28  PRO F CB  1 
ATOM   1360 C  CG  . PRO B 1 28  ? 36.005 5.871   -0.938  1.00 16.96 ? 28  PRO F CG  1 
ATOM   1361 C  CD  . PRO B 1 28  ? 37.087 5.578   0.059   1.00 15.48 ? 28  PRO F CD  1 
ATOM   1362 N  N   . VAL B 1 29  ? 32.794 5.616   1.664   1.00 12.27 ? 29  VAL F N   1 
ATOM   1363 C  CA  . VAL B 1 29  ? 31.627 4.777   1.731   1.00 11.59 ? 29  VAL F CA  1 
ATOM   1364 C  C   . VAL B 1 29  ? 30.786 5.045   0.493   1.00 10.11 ? 29  VAL F C   1 
ATOM   1365 O  O   . VAL B 1 29  ? 30.399 6.189   0.232   1.00 11.22 ? 29  VAL F O   1 
ATOM   1366 C  CB  . VAL B 1 29  ? 30.804 5.068   2.995   1.00 10.88 ? 29  VAL F CB  1 
ATOM   1367 C  CG1 . VAL B 1 29  ? 29.589 4.161   3.072   1.00 12.12 ? 29  VAL F CG1 1 
ATOM   1368 C  CG2 . VAL B 1 29  ? 31.675 4.911   4.238   1.00 11.87 ? 29  VAL F CG2 1 
ATOM   1369 N  N   . LYS B 1 30  ? 30.518 3.985   -0.262  1.00 11.07 ? 30  LYS F N   1 
ATOM   1370 C  CA  . LYS B 1 30  ? 29.599 4.014   -1.386  1.00 11.75 ? 30  LYS F CA  1 
ATOM   1371 C  C   . LYS B 1 30  ? 28.195 3.864   -0.817  1.00 10.27 ? 30  LYS F C   1 
ATOM   1372 O  O   . LYS B 1 30  ? 27.952 2.962   -0.019  1.00 11.23 ? 30  LYS F O   1 
ATOM   1373 C  CB  . LYS B 1 30  ? 29.916 2.855   -2.341  1.00 12.74 ? 30  LYS F CB  1 
ATOM   1374 C  CG  . LYS B 1 30  ? 29.130 2.841   -3.637  1.00 17.12 ? 30  LYS F CG  1 
ATOM   1375 C  CD  . LYS B 1 30  ? 29.634 1.737   -4.567  1.00 22.09 ? 30  LYS F CD  1 
ATOM   1376 C  CE  . LYS B 1 30  ? 28.980 1.778   -5.944  1.00 29.89 ? 30  LYS F CE  1 
ATOM   1377 N  NZ  . LYS B 1 30  ? 27.598 1.223   -5.952  1.00 36.52 ? 30  LYS F NZ  1 
ATOM   1378 N  N   . VAL B 1 31  ? 27.293 4.751   -1.218  1.00 13.25 ? 31  VAL F N   1 
ATOM   1379 C  CA  . VAL B 1 31  ? 25.908 4.767   -0.770  1.00 12.72 ? 31  VAL F CA  1 
ATOM   1380 C  C   . VAL B 1 31  ? 25.037 4.626   -2.005  1.00 10.86 ? 31  VAL F C   1 
ATOM   1381 O  O   . VAL B 1 31  ? 25.108 5.463   -2.907  1.00 12.26 ? 31  VAL F O   1 
ATOM   1382 C  CB  . VAL B 1 31  ? 25.551 6.093   -0.053  1.00 11.20 ? 31  VAL F CB  1 
ATOM   1383 C  CG1 . VAL B 1 31  ? 24.146 6.029   0.541   1.00 9.09  ? 31  VAL F CG1 1 
ATOM   1384 C  CG2 . VAL B 1 31  ? 26.573 6.428   1.021   1.00 11.54 ? 31  VAL F CG2 1 
ATOM   1385 N  N   . TRP B 1 32  ? 24.227 3.572   -2.066  1.00 9.66  ? 32  TRP F N   1 
ATOM   1386 C  CA  . TRP B 1 32  ? 23.384 3.342   -3.240  1.00 11.14 ? 32  TRP F CA  1 
ATOM   1387 C  C   . TRP B 1 32  ? 22.048 2.734   -2.900  1.00 10.18 ? 32  TRP F C   1 
ATOM   1388 O  O   . TRP B 1 32  ? 21.926 1.951   -1.948  1.00 10.14 ? 32  TRP F O   1 
ATOM   1389 C  CB  . TRP B 1 32  ? 24.101 2.458   -4.272  1.00 10.38 ? 32  TRP F CB  1 
ATOM   1390 C  CG  . TRP B 1 32  ? 24.382 1.015   -3.827  1.00 12.52 ? 32  TRP F CG  1 
ATOM   1391 C  CD1 . TRP B 1 32  ? 25.489 0.565   -3.166  1.00 13.07 ? 32  TRP F CD1 1 
ATOM   1392 C  CD2 . TRP B 1 32  ? 23.553 -0.134  -4.043  1.00 15.28 ? 32  TRP F CD2 1 
ATOM   1393 N  NE1 . TRP B 1 32  ? 25.405 -0.796  -2.962  1.00 15.18 ? 32  TRP F NE1 1 
ATOM   1394 C  CE2 . TRP B 1 32  ? 24.223 -1.249  -3.480  1.00 16.34 ? 32  TRP F CE2 1 
ATOM   1395 C  CE3 . TRP B 1 32  ? 22.304 -0.332  -4.647  1.00 17.55 ? 32  TRP F CE3 1 
ATOM   1396 C  CZ2 . TRP B 1 32  ? 23.684 -2.543  -3.497  1.00 18.61 ? 32  TRP F CZ2 1 
ATOM   1397 C  CZ3 . TRP B 1 32  ? 21.766 -1.628  -4.668  1.00 18.75 ? 32  TRP F CZ3 1 
ATOM   1398 C  CH2 . TRP B 1 32  ? 22.462 -2.714  -4.100  1.00 20.30 ? 32  TRP F CH2 1 
ATOM   1399 N  N   . GLY B 1 33  ? 21.050 3.074   -3.707  1.00 9.95  ? 33  GLY F N   1 
ATOM   1400 C  CA  . GLY B 1 33  ? 19.745 2.473   -3.569  1.00 13.52 ? 33  GLY F CA  1 
ATOM   1401 C  C   . GLY B 1 33  ? 18.685 3.306   -4.228  1.00 11.35 ? 33  GLY F C   1 
ATOM   1402 O  O   . GLY B 1 33  ? 18.949 3.993   -5.220  1.00 11.84 ? 33  GLY F O   1 
ATOM   1403 N  N   . SER B 1 34  ? 17.480 3.234   -3.684  1.00 11.72 ? 34  SER F N   1 
ATOM   1404 C  CA  . SER B 1 34  ? 16.326 3.839   -4.311  1.00 13.99 ? 34  SER F CA  1 
ATOM   1405 C  C   . SER B 1 34  ? 15.317 4.278   -3.267  1.00 13.57 ? 34  SER F C   1 
ATOM   1406 O  O   . SER B 1 34  ? 15.114 3.587   -2.273  1.00 13.10 ? 34  SER F O   1 
ATOM   1407 C  CB  . SER B 1 34  ? 15.682 2.846   -5.280  1.00 15.31 ? 34  SER F CB  1 
ATOM   1408 O  OG  . SER B 1 34  ? 14.800 3.520   -6.147  1.00 20.28 ? 34  SER F OG  1 
ATOM   1409 N  N   . ILE B 1 35  ? 14.711 5.439   -3.493  1.00 16.65 ? 35  ILE F N   1 
ATOM   1410 C  CA  . ILE B 1 35  ? 13.615 5.937   -2.663  1.00 12.31 ? 35  ILE F CA  1 
ATOM   1411 C  C   . ILE B 1 35  ? 12.471 6.314   -3.595  1.00 11.34 ? 35  ILE F C   1 
ATOM   1412 O  O   . ILE B 1 35  ? 12.685 7.031   -4.578  1.00 14.98 ? 35  ILE F O   1 
ATOM   1413 C  CB  . ILE B 1 35  ? 14.018 7.172   -1.829  1.00 8.46  ? 35  ILE F CB  1 
ATOM   1414 C  CG1 . ILE B 1 35  ? 15.300 6.904   -1.036  1.00 10.90 ? 35  ILE F CG1 1 
ATOM   1415 C  CG2 . ILE B 1 35  ? 12.881 7.567   -0.890  1.00 8.13  ? 35  ILE F CG2 1 
ATOM   1416 C  CD1 . ILE B 1 35  ? 15.893 8.132   -0.376  1.00 10.02 ? 35  ILE F CD1 1 
ATOM   1417 N  N   . LYS B 1 36  ? 11.263 5.853   -3.271  1.00 11.99 ? 36  LYS F N   1 
ATOM   1418 C  CA  . LYS B 1 36  ? 10.065 6.160   -4.059  1.00 14.57 ? 36  LYS F CA  1 
ATOM   1419 C  C   . LYS B 1 36  ? 9.034  6.920   -3.230  1.00 13.76 ? 36  LYS F C   1 
ATOM   1420 O  O   . LYS B 1 36  ? 9.121  6.978   -1.998  1.00 14.13 ? 36  LYS F O   1 
ATOM   1421 C  CB  . LYS B 1 36  ? 9.450  4.882   -4.651  1.00 16.47 ? 36  LYS F CB  1 
ATOM   1422 C  CG  . LYS B 1 36  ? 8.894  3.882   -3.644  1.00 17.86 ? 36  LYS F CG  1 
ATOM   1423 C  CD  . LYS B 1 36  ? 8.261  2.678   -4.331  1.00 22.42 ? 36  LYS F CD  1 
ATOM   1424 C  CE  . LYS B 1 36  ? 8.293  1.435   -3.448  0.00 36.87 ? 36  LYS F CE  1 
ATOM   1425 N  NZ  . LYS B 1 36  ? 7.984  0.186   -4.235  0.00 38.90 ? 36  LYS F NZ  1 
ATOM   1426 N  N   . GLY B 1 37  ? 8.056  7.498   -3.927  1.00 14.80 ? 37  GLY F N   1 
ATOM   1427 C  CA  . GLY B 1 37  ? 6.955  8.231   -3.294  1.00 15.40 ? 37  GLY F CA  1 
ATOM   1428 C  C   . GLY B 1 37  ? 7.259  9.674   -2.928  1.00 15.60 ? 37  GLY F C   1 
ATOM   1429 O  O   . GLY B 1 37  ? 6.548  10.272  -2.129  1.00 16.06 ? 37  GLY F O   1 
ATOM   1430 N  N   . LEU B 1 38  ? 8.295  10.237  -3.543  1.00 11.17 ? 38  LEU F N   1 
ATOM   1431 C  CA  . LEU B 1 38  ? 8.734  11.600  -3.269  1.00 13.04 ? 38  LEU F CA  1 
ATOM   1432 C  C   . LEU B 1 38  ? 8.171  12.563  -4.293  1.00 11.93 ? 38  LEU F C   1 
ATOM   1433 O  O   . LEU B 1 38  ? 7.841  12.174  -5.407  1.00 13.02 ? 38  LEU F O   1 
ATOM   1434 C  CB  . LEU B 1 38  ? 10.260 11.669  -3.328  1.00 12.05 ? 38  LEU F CB  1 
ATOM   1435 C  CG  . LEU B 1 38  ? 11.002 10.886  -2.242  1.00 11.19 ? 38  LEU F CG  1 
ATOM   1436 C  CD1 . LEU B 1 38  ? 12.459 10.713  -2.626  1.00 10.88 ? 38  LEU F CD1 1 
ATOM   1437 C  CD2 . LEU B 1 38  ? 10.879 11.588  -0.891  1.00 10.85 ? 38  LEU F CD2 1 
ATOM   1438 N  N   . THR B 1 39  ? 8.058  13.828  -3.913  1.00 12.39 ? 39  THR F N   1 
ATOM   1439 C  CA  . THR B 1 39  ? 7.770  14.883  -4.882  1.00 12.48 ? 39  THR F CA  1 
ATOM   1440 C  C   . THR B 1 39  ? 9.013  15.131  -5.734  1.00 12.48 ? 39  THR F C   1 
ATOM   1441 O  O   . THR B 1 39  ? 10.151 14.961  -5.279  1.00 11.57 ? 39  THR F O   1 
ATOM   1442 C  CB  . THR B 1 39  ? 7.310  16.192  -4.211  1.00 13.28 ? 39  THR F CB  1 
ATOM   1443 O  OG1 . THR B 1 39  ? 8.278  16.625  -3.249  1.00 13.12 ? 39  THR F OG1 1 
ATOM   1444 C  CG2 . THR B 1 39  ? 5.980  15.988  -3.535  1.00 13.56 ? 39  THR F CG2 1 
ATOM   1445 N  N   . GLU B 1 40  ? 8.788  15.513  -6.982  1.00 12.49 ? 40  GLU F N   1 
ATOM   1446 C  CA  . GLU B 1 40  ? 9.889  15.762  -7.900  1.00 13.35 ? 40  GLU F CA  1 
ATOM   1447 C  C   . GLU B 1 40  ? 10.736 16.919  -7.353  1.00 12.57 ? 40  GLU F C   1 
ATOM   1448 O  O   . GLU B 1 40  ? 10.199 17.931  -6.892  1.00 14.46 ? 40  GLU F O   1 
ATOM   1449 C  CB  . GLU B 1 40  ? 9.346  16.054  -9.305  1.00 14.21 ? 40  GLU F CB  1 
ATOM   1450 C  CG  . GLU B 1 40  ? 10.391 16.014  -10.419 1.00 14.00 ? 40  GLU F CG  1 
ATOM   1451 C  CD  . GLU B 1 40  ? 10.805 17.384  -10.885 1.00 15.39 ? 40  GLU F CD  1 
ATOM   1452 O  OE1 . GLU B 1 40  ? 10.924 18.270  -10.019 1.00 17.15 ? 40  GLU F OE1 1 
ATOM   1453 O  OE2 . GLU B 1 40  ? 11.007 17.571  -12.106 1.00 14.65 ? 40  GLU F OE2 1 
ATOM   1454 N  N   . GLY B 1 41  ? 12.051 16.724  -7.350  1.00 12.30 ? 41  GLY F N   1 
ATOM   1455 C  CA  . GLY B 1 41  ? 13.014 17.734  -6.919  1.00 10.47 ? 41  GLY F CA  1 
ATOM   1456 C  C   . GLY B 1 41  ? 13.988 17.205  -5.885  1.00 9.36  ? 41  GLY F C   1 
ATOM   1457 O  O   . GLY B 1 41  ? 14.199 15.995  -5.760  1.00 10.99 ? 41  GLY F O   1 
ATOM   1458 N  N   . LEU B 1 42  ? 14.570 18.127  -5.129  1.00 9.58  ? 42  LEU F N   1 
ATOM   1459 C  CA  . LEU B 1 42  ? 15.596 17.801  -4.151  1.00 8.90  ? 42  LEU F CA  1 
ATOM   1460 C  C   . LEU B 1 42  ? 15.009 17.525  -2.770  1.00 9.01  ? 42  LEU F C   1 
ATOM   1461 O  O   . LEU B 1 42  ? 14.085 18.212  -2.326  1.00 8.92  ? 42  LEU F O   1 
ATOM   1462 C  CB  . LEU B 1 42  ? 16.616 18.937  -4.072  1.00 9.66  ? 42  LEU F CB  1 
ATOM   1463 C  CG  . LEU B 1 42  ? 17.401 19.216  -5.359  1.00 10.55 ? 42  LEU F CG  1 
ATOM   1464 C  CD1 . LEU B 1 42  ? 18.337 20.379  -5.130  1.00 13.07 ? 42  LEU F CD1 1 
ATOM   1465 C  CD2 . LEU B 1 42  ? 18.208 18.011  -5.793  1.00 11.61 ? 42  LEU F CD2 1 
ATOM   1466 N  N   . HIS B 1 43  ? 15.566 16.519  -2.100  1.00 10.01 ? 43  HIS F N   1 
ATOM   1467 C  CA  . HIS B 1 43  ? 15.150 16.142  -0.753  1.00 11.82 ? 43  HIS F CA  1 
ATOM   1468 C  C   . HIS B 1 43  ? 16.362 15.943  0.138   1.00 8.12  ? 43  HIS F C   1 
ATOM   1469 O  O   . HIS B 1 43  ? 17.242 15.137  -0.170  1.00 7.75  ? 43  HIS F O   1 
ATOM   1470 C  CB  . HIS B 1 43  ? 14.318 14.865  -0.825  1.00 10.97 ? 43  HIS F CB  1 
ATOM   1471 C  CG  . HIS B 1 43  ? 13.018 15.054  -1.531  1.00 9.52  ? 43  HIS F CG  1 
ATOM   1472 N  ND1 . HIS B 1 43  ? 11.875 15.471  -0.884  1.00 10.49 ? 43  HIS F ND1 1 
ATOM   1473 C  CD2 . HIS B 1 43  ? 12.691 14.928  -2.837  1.00 14.04 ? 43  HIS F CD2 1 
ATOM   1474 C  CE1 . HIS B 1 43  ? 10.890 15.566  -1.760  1.00 11.21 ? 43  HIS F CE1 1 
ATOM   1475 N  NE2 . HIS B 1 43  ? 11.362 15.249  -2.954  1.00 10.85 ? 43  HIS F NE2 1 
ATOM   1476 N  N   . GLY B 1 44  ? 16.388 16.665  1.260   1.00 7.86  ? 44  GLY F N   1 
ATOM   1477 C  CA  . GLY B 1 44  ? 17.483 16.589  2.221   1.00 7.08  ? 44  GLY F CA  1 
ATOM   1478 C  C   . GLY B 1 44  ? 17.732 15.157  2.669   1.00 6.67  ? 44  GLY F C   1 
ATOM   1479 O  O   . GLY B 1 44  ? 16.787 14.411  2.872   1.00 7.22  ? 44  GLY F O   1 
ATOM   1480 N  N   . PHE B 1 45  ? 19.001 14.802  2.837   1.00 6.31  ? 45  PHE F N   1 
ATOM   1481 C  CA  . PHE B 1 45  ? 19.418 13.408  3.066   1.00 6.37  ? 45  PHE F CA  1 
ATOM   1482 C  C   . PHE B 1 45  ? 20.461 13.436  4.174   1.00 6.10  ? 45  PHE F C   1 
ATOM   1483 O  O   . PHE B 1 45  ? 21.594 13.856  3.952   1.00 6.17  ? 45  PHE F O   1 
ATOM   1484 C  CB  . PHE B 1 45  ? 19.974 12.837  1.744   1.00 6.10  ? 45  PHE F CB  1 
ATOM   1485 C  CG  . PHE B 1 45  ? 20.145 11.321  1.702   1.00 7.48  ? 45  PHE F CG  1 
ATOM   1486 C  CD1 . PHE B 1 45  ? 19.100 10.455  2.014   1.00 7.74  ? 45  PHE F CD1 1 
ATOM   1487 C  CD2 . PHE B 1 45  ? 21.352 10.776  1.272   1.00 8.33  ? 45  PHE F CD2 1 
ATOM   1488 C  CE1 . PHE B 1 45  ? 19.267 9.075   1.917   1.00 8.42  ? 45  PHE F CE1 1 
ATOM   1489 C  CE2 . PHE B 1 45  ? 21.525 9.400   1.180   1.00 8.95  ? 45  PHE F CE2 1 
ATOM   1490 C  CZ  . PHE B 1 45  ? 20.478 8.554   1.506   1.00 9.98  ? 45  PHE F CZ  1 
ATOM   1491 N  N   . HIS B 1 46  ? 20.067 12.997  5.374   1.00 5.66  ? 46  HIS F N   1 
ATOM   1492 C  CA  . HIS B 1 46  ? 20.882 13.174  6.580   1.00 5.52  ? 46  HIS F CA  1 
ATOM   1493 C  C   . HIS B 1 46  ? 21.039 11.880  7.376   1.00 5.27  ? 46  HIS F C   1 
ATOM   1494 O  O   . HIS B 1 46  ? 20.108 11.091  7.448   1.00 5.90  ? 46  HIS F O   1 
ATOM   1495 C  CB  . HIS B 1 46  ? 20.237 14.184  7.540   1.00 5.51  ? 46  HIS F CB  1 
ATOM   1496 C  CG  . HIS B 1 46  ? 20.013 15.541  6.949   1.00 7.10  ? 46  HIS F CG  1 
ATOM   1497 N  ND1 . HIS B 1 46  ? 18.959 16.354  7.322   1.00 8.74  ? 46  HIS F ND1 1 
ATOM   1498 C  CD2 . HIS B 1 46  ? 20.710 16.225  6.015   1.00 7.51  ? 46  HIS F CD2 1 
ATOM   1499 C  CE1 . HIS B 1 46  ? 19.024 17.484  6.637   1.00 11.56 ? 46  HIS F CE1 1 
ATOM   1500 N  NE2 . HIS B 1 46  ? 20.072 17.428  5.832   1.00 8.82  ? 46  HIS F NE2 1 
ATOM   1501 N  N   . VAL B 1 47  ? 22.192 11.722  8.012   1.00 4.52  ? 47  VAL F N   1 
ATOM   1502 C  CA  . VAL B 1 47  ? 22.336 10.793  9.143   1.00 5.05  ? 47  VAL F CA  1 
ATOM   1503 C  C   . VAL B 1 47  ? 22.122 11.634  10.400  1.00 5.56  ? 47  VAL F C   1 
ATOM   1504 O  O   . VAL B 1 47  ? 22.870 12.598  10.670  1.00 5.85  ? 47  VAL F O   1 
ATOM   1505 C  CB  . VAL B 1 47  ? 23.696 10.075  9.201   1.00 5.38  ? 47  VAL F CB  1 
ATOM   1506 C  CG1 . VAL B 1 47  ? 23.751 9.089   10.372  1.00 5.51  ? 47  VAL F CG1 1 
ATOM   1507 C  CG2 . VAL B 1 47  ? 23.973 9.346   7.892   1.00 5.14  ? 47  VAL F CG2 1 
ATOM   1508 N  N   . HIS B 1 48  ? 21.064 11.282  11.118  1.00 5.76  ? 48  HIS F N   1 
ATOM   1509 C  CA  . HIS B 1 48  ? 20.745 11.847  12.412  1.00 6.94  ? 48  HIS F CA  1 
ATOM   1510 C  C   . HIS B 1 48  ? 21.344 10.970  13.502  1.00 6.32  ? 48  HIS F C   1 
ATOM   1511 O  O   . HIS B 1 48  ? 21.597 9.770   13.283  1.00 7.21  ? 48  HIS F O   1 
ATOM   1512 C  CB  . HIS B 1 48  ? 19.231 11.977  12.545  1.00 7.66  ? 48  HIS F CB  1 
ATOM   1513 C  CG  . HIS B 1 48  ? 18.672 13.159  11.819  1.00 7.67  ? 48  HIS F CG  1 
ATOM   1514 N  ND1 . HIS B 1 48  ? 18.231 14.273  12.491  1.00 8.17  ? 48  HIS F ND1 1 
ATOM   1515 C  CD2 . HIS B 1 48  ? 18.520 13.430  10.498  1.00 7.91  ? 48  HIS F CD2 1 
ATOM   1516 C  CE1 . HIS B 1 48  ? 17.796 15.165  11.627  1.00 8.95  ? 48  HIS F CE1 1 
ATOM   1517 N  NE2 . HIS B 1 48  ? 17.973 14.692  10.409  1.00 8.37  ? 48  HIS F NE2 1 
ATOM   1518 N  N   . GLU B 1 49  ? 21.588 11.570  14.665  1.00 6.54  ? 49  GLU F N   1 
ATOM   1519 C  CA  . GLU B 1 49  ? 22.459 10.986  15.685  1.00 6.48  ? 49  GLU F CA  1 
ATOM   1520 C  C   . GLU B 1 49  ? 21.992 9.652   16.264  1.00 6.74  ? 49  GLU F C   1 
ATOM   1521 O  O   . GLU B 1 49  ? 22.799 8.732   16.429  1.00 7.90  ? 49  GLU F O   1 
ATOM   1522 C  CB  . GLU B 1 49  ? 22.644 11.969  16.835  1.00 6.56  ? 49  GLU F CB  1 
ATOM   1523 C  CG  . GLU B 1 49  ? 23.619 11.509  17.905  0.70 5.77  ? 49  GLU F CG  1 
ATOM   1524 C  CD  . GLU B 1 49  ? 23.831 12.552  18.973  0.70 5.64  ? 49  GLU F CD  1 
ATOM   1525 O  OE1 . GLU B 1 49  ? 23.128 13.598  18.935  0.70 5.81  ? 49  GLU F OE1 1 
ATOM   1526 O  OE2 . GLU B 1 49  ? 24.696 12.312  19.839  0.70 5.94  ? 49  GLU F OE2 1 
ATOM   1527 N  N   . PHE B 1 50  ? 20.717 9.569   16.622  1.00 6.53  ? 50  PHE F N   1 
ATOM   1528 C  CA  . PHE B 1 50  ? 20.207 8.397   17.364  1.00 6.77  ? 50  PHE F CA  1 
ATOM   1529 C  C   . PHE B 1 50  ? 19.459 7.464   16.449  1.00 7.15  ? 50  PHE F C   1 
ATOM   1530 O  O   . PHE B 1 50  ? 18.640 7.907   15.633  1.00 7.28  ? 50  PHE F O   1 
ATOM   1531 C  CB  . PHE B 1 50  ? 19.292 8.822   18.513  1.00 7.68  ? 50  PHE F CB  1 
ATOM   1532 C  CG  . PHE B 1 50  ? 19.882 9.896   19.370  1.00 9.64  ? 50  PHE F CG  1 
ATOM   1533 C  CD1 . PHE B 1 50  ? 21.112 9.704   19.979  1.00 10.05 ? 50  PHE F CD1 1 
ATOM   1534 C  CD2 . PHE B 1 50  ? 19.235 11.121  19.527  1.00 10.05 ? 50  PHE F CD2 1 
ATOM   1535 C  CE1 . PHE B 1 50  ? 21.689 10.700  20.754  1.00 11.86 ? 50  PHE F CE1 1 
ATOM   1536 C  CE2 . PHE B 1 50  ? 19.806 12.123  20.305  1.00 11.43 ? 50  PHE F CE2 1 
ATOM   1537 C  CZ  . PHE B 1 50  ? 21.038 11.920  20.904  1.00 11.38 ? 50  PHE F CZ  1 
ATOM   1538 N  N   . GLY B 1 51  ? 19.706 6.166   16.623  1.00 6.70  ? 51  GLY F N   1 
ATOM   1539 C  CA  . GLY B 1 51  ? 18.917 5.128   15.960  1.00 7.71  ? 51  GLY F CA  1 
ATOM   1540 C  C   . GLY B 1 51  ? 17.660 4.823   16.740  1.00 7.94  ? 51  GLY F C   1 
ATOM   1541 O  O   . GLY B 1 51  ? 17.337 3.660   16.994  1.00 7.97  ? 51  GLY F O   1 
ATOM   1542 N  N   . ASP B 1 52  ? 16.946 5.875   17.112  1.00 10.10 ? 52  ASP F N   1 
ATOM   1543 C  CA  . ASP B 1 52  ? 15.824 5.791   18.013  1.00 10.68 ? 52  ASP F CA  1 
ATOM   1544 C  C   . ASP B 1 52  ? 14.638 6.195   17.174  1.00 9.70  ? 52  ASP F C   1 
ATOM   1545 O  O   . ASP B 1 52  ? 14.477 7.379   16.844  1.00 10.08 ? 52  ASP F O   1 
ATOM   1546 C  CB  . ASP B 1 52  ? 16.030 6.736   19.205  1.00 11.23 ? 52  ASP F CB  1 
ATOM   1547 C  CG  . ASP B 1 52  ? 14.904 6.661   20.233  1.00 13.05 ? 52  ASP F CG  1 
ATOM   1548 O  OD1 . ASP B 1 52  ? 13.788 6.220   19.879  1.00 12.85 ? 52  ASP F OD1 1 
ATOM   1549 O  OD2 . ASP B 1 52  ? 15.140 7.056   21.399  1.00 14.46 ? 52  ASP F OD2 1 
ATOM   1550 N  N   . ASN B 1 53  ? 13.824 5.217   16.800  1.00 11.60 ? 53  ASN F N   1 
ATOM   1551 C  CA  . ASN B 1 53  ? 12.617 5.491   16.020  1.00 13.61 ? 53  ASN F CA  1 
ATOM   1552 C  C   . ASN B 1 53  ? 11.361 5.120   16.822  1.00 12.49 ? 53  ASN F C   1 
ATOM   1553 O  O   . ASN B 1 53  ? 10.324 4.768   16.262  1.00 13.45 ? 53  ASN F O   1 
ATOM   1554 C  CB  . ASN B 1 53  ? 12.703 4.810   14.643  1.00 16.48 ? 53  ASN F CB  1 
ATOM   1555 C  CG  . ASN B 1 53  ? 13.776 5.438   13.727  1.00 18.78 ? 53  ASN F CG  1 
ATOM   1556 O  OD1 . ASN B 1 53  ? 14.251 6.573   13.940  1.00 22.39 ? 53  ASN F OD1 1 
ATOM   1557 N  ND2 . ASN B 1 53  ? 14.155 4.697   12.691  1.00 19.82 ? 53  ASN F ND2 1 
ATOM   1558 N  N   . THR B 1 54  ? 11.443 5.275   18.138  1.00 11.53 ? 54  THR F N   1 
ATOM   1559 C  CA  . THR B 1 54  ? 10.335 4.915   19.023  1.00 13.78 ? 54  THR F CA  1 
ATOM   1560 C  C   . THR B 1 54  ? 9.104  5.790   18.809  1.00 14.33 ? 54  THR F C   1 
ATOM   1561 O  O   . THR B 1 54  ? 7.984  5.309   18.937  1.00 14.47 ? 54  THR F O   1 
ATOM   1562 C  CB  . THR B 1 54  ? 10.750 4.939   20.501  1.00 15.47 ? 54  THR F CB  1 
ATOM   1563 O  OG1 . THR B 1 54  ? 11.363 6.184   20.804  1.00 15.50 ? 54  THR F OG1 1 
ATOM   1564 C  CG2 . THR B 1 54  ? 11.747 3.828   20.788  1.00 15.83 ? 54  THR F CG2 1 
ATOM   1565 N  N   . ALA B 1 55  ? 9.315  7.062   18.474  1.00 16.07 ? 55  ALA F N   1 
ATOM   1566 C  CA  . ALA B 1 55  ? 8.217  7.949   18.071  1.00 20.50 ? 55  ALA F CA  1 
ATOM   1567 C  C   . ALA B 1 55  ? 8.308  8.298   16.587  1.00 21.02 ? 55  ALA F C   1 
ATOM   1568 O  O   . ALA B 1 55  ? 7.936  9.390   16.173  1.00 21.36 ? 55  ALA F O   1 
ATOM   1569 C  CB  . ALA B 1 55  ? 8.218  9.210   18.917  1.00 22.31 ? 55  ALA F CB  1 
ATOM   1570 N  N   . GLY B 1 56  ? 8.755  7.341   15.783  1.00 18.73 ? 56  GLY F N   1 
ATOM   1571 C  CA  . GLY B 1 56  ? 9.030  7.586   14.377  1.00 18.92 ? 56  GLY F CA  1 
ATOM   1572 C  C   . GLY B 1 56  ? 10.289 8.413   14.230  1.00 18.14 ? 56  GLY F C   1 
ATOM   1573 O  O   . GLY B 1 56  ? 11.173 8.376   15.086  1.00 19.10 ? 56  GLY F O   1 
ATOM   1574 N  N   . CYS B 1 57  ? 10.350 9.197   13.163  1.00 14.31 ? 57  CYS F N   1 
ATOM   1575 C  CA  . CYS B 1 57  ? 11.566 9.928   12.827  1.00 13.25 ? 57  CYS F CA  1 
ATOM   1576 C  C   . CYS B 1 57  ? 11.894 11.070  13.784  1.00 14.74 ? 57  CYS F C   1 
ATOM   1577 O  O   . CYS B 1 57  ? 13.050 11.481  13.879  1.00 13.71 ? 57  CYS F O   1 
ATOM   1578 C  CB  . CYS B 1 57  ? 11.473 10.463  11.401  1.00 12.00 ? 57  CYS F CB  1 
ATOM   1579 S  SG  . CYS B 1 57  ? 11.117 9.170   10.186  1.00 13.85 ? 57  CYS F SG  1 
ATOM   1580 N  N   . THR B 1 58  ? 10.889 11.564  14.501  1.00 13.31 ? 58  THR F N   1 
ATOM   1581 C  CA  . THR B 1 58  ? 11.099 12.648  15.464  1.00 17.51 ? 58  THR F CA  1 
ATOM   1582 C  C   . THR B 1 58  ? 12.055 12.335  16.630  1.00 14.48 ? 58  THR F C   1 
ATOM   1583 O  O   . THR B 1 58  ? 12.641 13.250  17.181  1.00 20.79 ? 58  THR F O   1 
ATOM   1584 C  CB  . THR B 1 58  ? 9.759  13.212  16.002  1.00 23.34 ? 58  THR F CB  1 
ATOM   1585 O  OG1 . THR B 1 58  ? 10.004 14.432  16.717  1.00 26.67 ? 58  THR F OG1 1 
ATOM   1586 C  CG2 . THR B 1 58  ? 9.060  12.242  16.916  1.00 23.99 ? 58  THR F CG2 1 
ATOM   1587 N  N   A SER B 1 59  ? 12.200 11.056  16.988  0.50 13.28 ? 59  SER F N   1 
ATOM   1588 N  N   B SER B 1 59  ? 12.206 11.060  16.982  0.50 11.96 ? 59  SER F N   1 
ATOM   1589 C  CA  A SER B 1 59  ? 13.119 10.628  18.058  0.50 12.43 ? 59  SER F CA  1 
ATOM   1590 C  CA  B SER B 1 59  ? 13.120 10.641  18.051  0.50 11.55 ? 59  SER F CA  1 
ATOM   1591 C  C   A SER B 1 59  ? 14.598 10.530  17.642  0.50 11.64 ? 59  SER F C   1 
ATOM   1592 C  C   B SER B 1 59  ? 14.598 10.526  17.640  0.50 10.97 ? 59  SER F C   1 
ATOM   1593 O  O   A SER B 1 59  ? 15.459 10.289  18.491  0.50 10.85 ? 59  SER F O   1 
ATOM   1594 O  O   B SER B 1 59  ? 15.456 10.279  18.490  0.50 10.19 ? 59  SER F O   1 
ATOM   1595 C  CB  A SER B 1 59  ? 12.679 9.264   18.618  0.50 12.80 ? 59  SER F CB  1 
ATOM   1596 C  CB  B SER B 1 59  ? 12.643 9.301   18.617  0.50 11.28 ? 59  SER F CB  1 
ATOM   1597 O  OG  A SER B 1 59  ? 11.385 9.306   19.191  0.50 12.97 ? 59  SER F OG  1 
ATOM   1598 O  OG  B SER B 1 59  ? 12.026 8.524   17.606  0.50 11.08 ? 59  SER F OG  1 
ATOM   1599 N  N   . ALA B 1 60  ? 14.902 10.709  16.356  1.00 10.75 ? 60  ALA F N   1 
ATOM   1600 C  CA  . ALA B 1 60  ? 16.272 10.514  15.851  1.00 11.81 ? 60  ALA F CA  1 
ATOM   1601 C  C   . ALA B 1 60  ? 17.293 11.583  16.281  1.00 9.34  ? 60  ALA F C   1 
ATOM   1602 O  O   . ALA B 1 60  ? 18.500 11.396  16.106  1.00 9.38  ? 60  ALA F O   1 
ATOM   1603 C  CB  . ALA B 1 60  ? 16.257 10.374  14.331  1.00 12.60 ? 60  ALA F CB  1 
ATOM   1604 N  N   . GLY B 1 61  ? 16.822 12.703  16.825  1.00 5.87  ? 61  GLY F N   1 
ATOM   1605 C  CA  . GLY B 1 61  ? 17.715 13.741  17.318  1.00 5.40  ? 61  GLY F CA  1 
ATOM   1606 C  C   . GLY B 1 61  ? 18.298 14.620  16.222  1.00 6.41  ? 61  GLY F C   1 
ATOM   1607 O  O   . GLY B 1 61  ? 17.778 14.643  15.105  1.00 7.03  ? 61  GLY F O   1 
ATOM   1608 N  N   . PRO B 1 62  ? 19.390 15.349  16.539  1.00 7.40  ? 62  PRO F N   1 
ATOM   1609 C  CA  . PRO B 1 62  ? 20.012 16.287  15.595  1.00 7.62  ? 62  PRO F CA  1 
ATOM   1610 C  C   . PRO B 1 62  ? 20.837 15.589  14.517  1.00 7.94  ? 62  PRO F C   1 
ATOM   1611 O  O   . PRO B 1 62  ? 20.938 14.360  14.518  1.00 6.84  ? 62  PRO F O   1 
ATOM   1612 C  CB  . PRO B 1 62  ? 20.916 17.129  16.504  1.00 9.43  ? 62  PRO F CB  1 
ATOM   1613 C  CG  . PRO B 1 62  ? 21.298 16.192  17.601  1.00 8.36  ? 62  PRO F CG  1 
ATOM   1614 C  CD  . PRO B 1 62  ? 20.069 15.372  17.850  1.00 8.59  ? 62  PRO F CD  1 
ATOM   1615 N  N   . HIS B 1 63  ? 21.439 16.372  13.621  1.00 8.66  ? 63  HIS F N   1 
ATOM   1616 C  CA  . HIS B 1 63  ? 22.377 15.836  12.634  1.00 6.82  ? 63  HIS F CA  1 
ATOM   1617 C  C   . HIS B 1 63  ? 23.531 15.185  13.379  1.00 6.77  ? 63  HIS F C   1 
ATOM   1618 O  O   . HIS B 1 63  ? 23.979 15.697  14.405  1.00 6.30  ? 63  HIS F O   1 
ATOM   1619 C  CB  . HIS B 1 63  ? 22.920 16.943  11.716  1.00 7.30  ? 63  HIS F CB  1 
ATOM   1620 C  CG  . HIS B 1 63  ? 21.874 17.579  10.859  1.00 9.18  ? 63  HIS F CG  1 
ATOM   1621 N  ND1 . HIS B 1 63  ? 22.179 18.376  9.774   1.00 8.68  ? 63  HIS F ND1 1 
ATOM   1622 C  CD2 . HIS B 1 63  ? 20.520 17.534  10.925  1.00 9.83  ? 63  HIS F CD2 1 
ATOM   1623 C  CE1 . HIS B 1 63  ? 21.058 18.794  9.216   1.00 8.22  ? 63  HIS F CE1 1 
ATOM   1624 N  NE2 . HIS B 1 63  ? 20.037 18.303  9.894   1.00 10.11 ? 63  HIS F NE2 1 
ATOM   1625 N  N   . PHE B 1 64  ? 23.982 14.027  12.895  1.00 6.05  ? 64  PHE F N   1 
ATOM   1626 C  CA  . PHE B 1 64  ? 25.142 13.381  13.478  1.00 6.33  ? 64  PHE F CA  1 
ATOM   1627 C  C   . PHE B 1 64  ? 26.358 14.289  13.275  1.00 6.10  ? 64  PHE F C   1 
ATOM   1628 O  O   . PHE B 1 64  ? 26.766 14.559  12.137  1.00 6.60  ? 64  PHE F O   1 
ATOM   1629 C  CB  . PHE B 1 64  ? 25.344 11.980  12.878  1.00 6.11  ? 64  PHE F CB  1 
ATOM   1630 C  CG  . PHE B 1 64  ? 26.552 11.251  13.411  1.00 6.22  ? 64  PHE F CG  1 
ATOM   1631 C  CD1 . PHE B 1 64  ? 26.799 11.183  14.778  1.00 6.45  ? 64  PHE F CD1 1 
ATOM   1632 C  CD2 . PHE B 1 64  ? 27.428 10.585  12.546  1.00 5.94  ? 64  PHE F CD2 1 
ATOM   1633 C  CE1 . PHE B 1 64  ? 27.910 10.521  15.270  1.00 6.43  ? 64  PHE F CE1 1 
ATOM   1634 C  CE2 . PHE B 1 64  ? 28.534 9.903   13.042  1.00 6.23  ? 64  PHE F CE2 1 
ATOM   1635 C  CZ  . PHE B 1 64  ? 28.773 9.865   14.408  1.00 6.49  ? 64  PHE F CZ  1 
ATOM   1636 N  N   . ASN B 1 65  ? 26.900 14.782  14.394  1.00 6.24  ? 65  ASN F N   1 
ATOM   1637 C  CA  . ASN B 1 65  ? 27.922 15.818  14.388  1.00 6.26  ? 65  ASN F CA  1 
ATOM   1638 C  C   . ASN B 1 65  ? 28.980 15.553  15.457  1.00 6.27  ? 65  ASN F C   1 
ATOM   1639 O  O   . ASN B 1 65  ? 29.175 16.354  16.385  1.00 6.68  ? 65  ASN F O   1 
ATOM   1640 C  CB  . ASN B 1 65  ? 27.265 17.190  14.593  1.00 5.94  ? 65  ASN F CB  1 
ATOM   1641 C  CG  . ASN B 1 65  ? 28.255 18.346  14.477  1.00 6.84  ? 65  ASN F CG  1 
ATOM   1642 O  OD1 . ASN B 1 65  ? 29.305 18.219  13.843  1.00 6.96  ? 65  ASN F OD1 1 
ATOM   1643 N  ND2 . ASN B 1 65  ? 27.917 19.487  15.081  1.00 7.93  ? 65  ASN F ND2 1 
ATOM   1644 N  N   . PRO B 1 66  ? 29.714 14.439  15.318  1.00 6.59  ? 66  PRO F N   1 
ATOM   1645 C  CA  . PRO B 1 66  ? 30.689 14.107  16.352  1.00 7.26  ? 66  PRO F CA  1 
ATOM   1646 C  C   . PRO B 1 66  ? 31.830 15.111  16.516  1.00 7.36  ? 66  PRO F C   1 
ATOM   1647 O  O   . PRO B 1 66  ? 32.397 15.180  17.592  1.00 7.22  ? 66  PRO F O   1 
ATOM   1648 C  CB  . PRO B 1 66  ? 31.221 12.739  15.903  1.00 6.26  ? 66  PRO F CB  1 
ATOM   1649 C  CG  . PRO B 1 66  ? 31.006 12.718  14.431  1.00 7.36  ? 66  PRO F CG  1 
ATOM   1650 C  CD  . PRO B 1 66  ? 29.740 13.475  14.205  1.00 6.70  ? 66  PRO F CD  1 
ATOM   1651 N  N   . LEU B 1 67  ? 32.124 15.912  15.486  1.00 8.17  ? 67  LEU F N   1 
ATOM   1652 C  CA  . LEU B 1 67  ? 33.245 16.863  15.510  1.00 8.82  ? 67  LEU F CA  1 
ATOM   1653 C  C   . LEU B 1 67  ? 32.840 18.297  15.848  1.00 8.92  ? 67  LEU F C   1 
ATOM   1654 O  O   . LEU B 1 67  ? 33.691 19.175  15.838  1.00 9.87  ? 67  LEU F O   1 
ATOM   1655 C  CB  . LEU B 1 67  ? 33.997 16.843  14.172  1.00 9.24  ? 67  LEU F CB  1 
ATOM   1656 C  CG  . LEU B 1 67  ? 34.687 15.527  13.799  0.50 9.64  ? 67  LEU F CG  1 
ATOM   1657 C  CD1 . LEU B 1 67  ? 35.194 15.579  12.365  0.50 9.48  ? 67  LEU F CD1 1 
ATOM   1658 C  CD2 . LEU B 1 67  ? 35.834 15.237  14.747  0.50 10.96 ? 67  LEU F CD2 1 
ATOM   1659 N  N   . SER B 1 68  ? 31.564 18.527  16.161  1.00 9.55  ? 68  SER F N   1 
ATOM   1660 C  CA  . SER B 1 68  ? 31.081 19.848  16.612  1.00 9.49  ? 68  SER F CA  1 
ATOM   1661 C  C   . SER B 1 68  ? 31.280 20.938  15.569  1.00 10.14 ? 68  SER F C   1 
ATOM   1662 O  O   . SER B 1 68  ? 31.691 22.051  15.895  1.00 11.59 ? 68  SER F O   1 
ATOM   1663 C  CB  . SER B 1 68  ? 31.747 20.260  17.933  1.00 9.77  ? 68  SER F CB  1 
ATOM   1664 O  OG  . SER B 1 68  ? 31.508 19.305  18.930  1.00 10.26 ? 68  SER F OG  1 
ATOM   1665 N  N   . ARG B 1 69  ? 30.991 20.600  14.318  1.00 10.49 ? 69  ARG F N   1 
ATOM   1666 C  CA  . ARG B 1 69  ? 31.087 21.523  13.196  1.00 11.53 ? 69  ARG F CA  1 
ATOM   1667 C  C   . ARG B 1 69  ? 29.715 22.092  12.891  1.00 10.25 ? 69  ARG F C   1 
ATOM   1668 O  O   . ARG B 1 69  ? 28.723 21.701  13.499  1.00 10.31 ? 69  ARG F O   1 
ATOM   1669 C  CB  . ARG B 1 69  ? 31.624 20.791  11.966  1.00 13.03 ? 69  ARG F CB  1 
ATOM   1670 C  CG  . ARG B 1 69  ? 32.954 20.093  12.173  1.00 17.23 ? 69  ARG F CG  1 
ATOM   1671 C  CD  . ARG B 1 69  ? 34.077 21.069  12.470  1.00 21.71 ? 69  ARG F CD  1 
ATOM   1672 N  NE  . ARG B 1 69  ? 35.338 20.368  12.708  1.00 26.15 ? 69  ARG F NE  1 
ATOM   1673 C  CZ  . ARG B 1 69  ? 36.110 19.807  11.775  1.00 29.15 ? 69  ARG F CZ  1 
ATOM   1674 N  NH1 . ARG B 1 69  ? 35.786 19.839  10.476  1.00 36.91 ? 69  ARG F NH1 1 
ATOM   1675 N  NH2 . ARG B 1 69  ? 37.235 19.199  12.151  1.00 33.83 ? 69  ARG F NH2 1 
ATOM   1676 N  N   . LYS B 1 70  ? 29.676 23.037  11.954  1.00 10.97 ? 70  LYS F N   1 
ATOM   1677 C  CA  . LYS B 1 70  ? 28.426 23.596  11.449  1.00 10.38 ? 70  LYS F CA  1 
ATOM   1678 C  C   . LYS B 1 70  ? 27.908 22.795  10.243  1.00 10.20 ? 70  LYS F C   1 
ATOM   1679 O  O   . LYS B 1 70  ? 28.630 21.997  9.639   1.00 10.26 ? 70  LYS F O   1 
ATOM   1680 C  CB  . LYS B 1 70  ? 28.623 25.072  11.064  1.00 10.30 ? 70  LYS F CB  1 
ATOM   1681 C  CG  . LYS B 1 70  ? 29.117 25.934  12.228  1.00 12.68 ? 70  LYS F CG  1 
ATOM   1682 C  CD  . LYS B 1 70  ? 29.204 27.411  11.874  1.00 14.83 ? 70  LYS F CD  1 
ATOM   1683 C  CE  . LYS B 1 70  ? 29.837 28.227  13.037  0.00 30.18 ? 70  LYS F CE  1 
ATOM   1684 N  NZ  . LYS B 1 70  ? 30.037 29.647  12.634  0.00 40.74 ? 70  LYS F NZ  1 
ATOM   1685 N  N   . HIS B 1 71  ? 26.646 23.020  9.908   1.00 8.63  ? 71  HIS F N   1 
ATOM   1686 C  CA  . HIS B 1 71  ? 26.001 22.331  8.802   1.00 9.99  ? 71  HIS F CA  1 
ATOM   1687 C  C   . HIS B 1 71  ? 26.547 22.766  7.445   1.00 9.08  ? 71  HIS F C   1 
ATOM   1688 O  O   . HIS B 1 71  ? 26.829 23.941  7.224   1.00 11.10 ? 71  HIS F O   1 
ATOM   1689 C  CB  . HIS B 1 71  ? 24.497 22.566  8.836   1.00 10.39 ? 71  HIS F CB  1 
ATOM   1690 C  CG  . HIS B 1 71  ? 23.750 21.837  7.767   1.00 8.70  ? 71  HIS F CG  1 
ATOM   1691 N  ND1 . HIS B 1 71  ? 23.514 20.474  7.797   1.00 8.82  ? 71  HIS F ND1 1 
ATOM   1692 C  CD2 . HIS B 1 71  ? 23.208 22.286  6.613   1.00 9.65  ? 71  HIS F CD2 1 
ATOM   1693 C  CE1 . HIS B 1 71  ? 22.849 20.128  6.714   1.00 9.25  ? 71  HIS F CE1 1 
ATOM   1694 N  NE2 . HIS B 1 71  ? 22.653 21.205  5.976   1.00 8.41  ? 71  HIS F NE2 1 
ATOM   1695 N  N   . GLY B 1 72  ? 26.690 21.802  6.544   1.00 9.67  ? 72  GLY F N   1 
ATOM   1696 C  CA  . GLY B 1 72  ? 27.114 22.082  5.186   1.00 10.03 ? 72  GLY F CA  1 
ATOM   1697 C  C   . GLY B 1 72  ? 26.626 21.011  4.241   1.00 10.23 ? 72  GLY F C   1 
ATOM   1698 O  O   . GLY B 1 72  ? 25.782 20.188  4.593   1.00 10.14 ? 72  GLY F O   1 
ATOM   1699 N  N   . GLY B 1 73  ? 27.119 21.083  3.015   1.00 9.13  ? 73  GLY F N   1 
ATOM   1700 C  CA  . GLY B 1 73  ? 26.906 20.047  2.033   1.00 10.28 ? 73  GLY F CA  1 
ATOM   1701 C  C   . GLY B 1 73  ? 28.026 19.031  2.120   1.00 10.13 ? 73  GLY F C   1 
ATOM   1702 O  O   . GLY B 1 73  ? 29.071 19.294  2.739   1.00 10.17 ? 73  GLY F O   1 
ATOM   1703 N  N   . PRO B 1 74  ? 27.829 17.863  1.489   1.00 9.87  ? 74  PRO F N   1 
ATOM   1704 C  CA  . PRO B 1 74  ? 28.812 16.785  1.575   1.00 9.43  ? 74  PRO F CA  1 
ATOM   1705 C  C   . PRO B 1 74  ? 30.197 17.151  1.038   1.00 11.59 ? 74  PRO F C   1 
ATOM   1706 O  O   . PRO B 1 74  ? 31.197 16.620  1.528   1.00 13.22 ? 74  PRO F O   1 
ATOM   1707 C  CB  . PRO B 1 74  ? 28.180 15.657  0.751   1.00 9.45  ? 74  PRO F CB  1 
ATOM   1708 C  CG  . PRO B 1 74  ? 27.086 16.280  -0.043  1.00 10.25 ? 74  PRO F CG  1 
ATOM   1709 C  CD  . PRO B 1 74  ? 26.628 17.464  0.740   1.00 9.45  ? 74  PRO F CD  1 
ATOM   1710 N  N   . LYS B 1 75  ? 30.248 18.053  0.054   1.00 10.81 ? 75  LYS F N   1 
ATOM   1711 C  CA  . LYS B 1 75  ? 31.516 18.472  -0.551  1.00 14.83 ? 75  LYS F CA  1 
ATOM   1712 C  C   . LYS B 1 75  ? 32.262 19.530  0.263   1.00 14.24 ? 75  LYS F C   1 
ATOM   1713 O  O   . LYS B 1 75  ? 33.411 19.843  -0.059  1.00 17.78 ? 75  LYS F O   1 
ATOM   1714 C  CB  . LYS B 1 75  ? 31.292 18.989  -1.980  1.00 16.56 ? 75  LYS F CB  1 
ATOM   1715 C  CG  . LYS B 1 75  ? 30.878 17.918  -2.978  1.00 19.89 ? 75  LYS F CG  1 
ATOM   1716 C  CD  . LYS B 1 75  ? 31.104 18.235  -4.334  0.00 33.01 ? 75  LYS F CD  1 
ATOM   1717 C  CE  . LYS B 1 75  ? 30.102 19.319  -4.697  0.00 38.76 ? 75  LYS F CE  1 
ATOM   1718 N  NZ  . LYS B 1 75  ? 30.164 19.671  -6.142  0.00 35.24 ? 75  LYS F NZ  1 
ATOM   1719 N  N   . ASP B 1 76  ? 31.633 20.071  1.311   1.00 9.49  ? 76  ASP F N   1 
ATOM   1720 C  CA  . ASP B 1 76  ? 32.234 21.120  2.119   1.00 9.19  ? 76  ASP F CA  1 
ATOM   1721 C  C   . ASP B 1 76  ? 33.102 20.521  3.215   1.00 10.22 ? 76  ASP F C   1 
ATOM   1722 O  O   . ASP B 1 76  ? 32.769 19.480  3.787   1.00 14.01 ? 76  ASP F O   1 
ATOM   1723 C  CB  . ASP B 1 76  ? 31.168 22.001  2.783   1.00 8.26  ? 76  ASP F CB  1 
ATOM   1724 C  CG  . ASP B 1 76  ? 30.235 22.661  1.794   1.00 9.04  ? 76  ASP F CG  1 
ATOM   1725 O  OD1 . ASP B 1 76  ? 30.614 22.891  0.626   1.00 14.21 ? 76  ASP F OD1 1 
ATOM   1726 O  OD2 . ASP B 1 76  ? 29.094 22.953  2.195   1.00 12.18 ? 76  ASP F OD2 1 
ATOM   1727 N  N   . GLU B 1 77  ? 34.222 21.178  3.496   1.00 13.96 ? 77  GLU F N   1 
ATOM   1728 C  CA  . GLU B 1 77  ? 35.050 20.836  4.654   1.00 17.80 ? 77  GLU F CA  1 
ATOM   1729 C  C   . GLU B 1 77  ? 34.278 21.085  5.941   1.00 16.28 ? 77  GLU F C   1 
ATOM   1730 O  O   . GLU B 1 77  ? 34.310 20.261  6.854   1.00 17.96 ? 77  GLU F O   1 
ATOM   1731 C  CB  . GLU B 1 77  ? 36.342 21.656  4.665   1.00 24.01 ? 77  GLU F CB  1 
ATOM   1732 C  CG  . GLU B 1 77  ? 37.348 21.216  5.720   1.00 26.85 ? 77  GLU F CG  1 
ATOM   1733 C  CD  . GLU B 1 77  ? 37.804 19.871  5.398   0.00 42.89 ? 77  GLU F CD  1 
ATOM   1734 O  OE1 . GLU B 1 77  ? 37.496 19.345  4.308   0.00 46.77 ? 77  GLU F OE1 1 
ATOM   1735 O  OE2 . GLU B 1 77  ? 38.471 19.281  6.273   0.00 49.59 ? 77  GLU F OE2 1 
ATOM   1736 N  N   . GLU B 1 78  ? 33.589 22.224  6.000   1.00 15.98 ? 78  GLU F N   1 
ATOM   1737 C  CA  . GLU B 1 78  ? 32.737 22.554  7.131   1.00 12.96 ? 78  GLU F CA  1 
ATOM   1738 C  C   . GLU B 1 78  ? 31.376 21.896  6.944   1.00 10.47 ? 78  GLU F C   1 
ATOM   1739 O  O   . GLU B 1 78  ? 30.509 22.393  6.217   1.00 10.92 ? 78  GLU F O   1 
ATOM   1740 C  CB  . GLU B 1 78  ? 32.595 24.076  7.305   1.00 13.40 ? 78  GLU F CB  1 
ATOM   1741 C  CG  . GLU B 1 78  ? 31.971 24.476  8.641   1.00 16.69 ? 78  GLU F CG  1 
ATOM   1742 C  CD  . GLU B 1 78  ? 32.836 24.138  9.849   0.50 14.56 ? 78  GLU F CD  1 
ATOM   1743 O  OE1 . GLU B 1 78  ? 34.079 24.082  9.725   0.50 15.91 ? 78  GLU F OE1 1 
ATOM   1744 O  OE2 . GLU B 1 78  ? 32.271 23.937  10.938  0.50 12.29 ? 78  GLU F OE2 1 
ATOM   1745 N  N   . ARG B 1 79  ? 31.214 20.754  7.605   1.00 8.16  ? 79  ARG F N   1 
ATOM   1746 C  CA  . ARG B 1 79  ? 29.968 19.998  7.567   1.00 8.29  ? 79  ARG F CA  1 
ATOM   1747 C  C   . ARG B 1 79  ? 29.861 19.110  8.801   1.00 7.80  ? 79  ARG F C   1 
ATOM   1748 O  O   . ARG B 1 79  ? 30.855 18.832  9.475   1.00 8.22  ? 79  ARG F O   1 
ATOM   1749 C  CB  . ARG B 1 79  ? 29.909 19.125  6.309   1.00 8.70  ? 79  ARG F CB  1 
ATOM   1750 C  CG  . ARG B 1 79  ? 31.047 18.121  6.220   1.00 8.96  ? 79  ARG F CG  1 
ATOM   1751 C  CD  . ARG B 1 79  ? 30.851 17.129  5.091   1.00 8.32  ? 79  ARG F CD  1 
ATOM   1752 N  NE  . ARG B 1 79  ? 30.147 15.918  5.519   1.00 8.89  ? 79  ARG F NE  1 
ATOM   1753 C  CZ  . ARG B 1 79  ? 30.052 14.801  4.798   1.00 8.25  ? 79  ARG F CZ  1 
ATOM   1754 N  NH1 . ARG B 1 79  ? 30.615 14.725  3.595   1.00 10.01 ? 79  ARG F NH1 1 
ATOM   1755 N  NH2 . ARG B 1 79  ? 29.401 13.747  5.284   1.00 10.77 ? 79  ARG F NH2 1 
ATOM   1756 N  N   . HIS B 1 80  ? 28.642 18.664  9.067   1.00 5.97  ? 80  HIS F N   1 
ATOM   1757 C  CA  . HIS B 1 80  ? 28.408 17.574  10.010  1.00 5.99  ? 80  HIS F CA  1 
ATOM   1758 C  C   . HIS B 1 80  ? 28.743 16.258  9.327   1.00 6.47  ? 80  HIS F C   1 
ATOM   1759 O  O   . HIS B 1 80  ? 28.573 16.142  8.113   1.00 6.71  ? 80  HIS F O   1 
ATOM   1760 C  CB  . HIS B 1 80  ? 26.946 17.531  10.418  1.00 6.31  ? 80  HIS F CB  1 
ATOM   1761 C  CG  . HIS B 1 80  ? 26.457 18.797  11.041  1.00 6.78  ? 80  HIS F CG  1 
ATOM   1762 N  ND1 . HIS B 1 80  ? 25.190 19.304  10.838  1.00 6.94  ? 80  HIS F ND1 1 
ATOM   1763 C  CD2 . HIS B 1 80  ? 27.077 19.652  11.884  1.00 6.39  ? 80  HIS F CD2 1 
ATOM   1764 C  CE1 . HIS B 1 80  ? 25.047 20.399  11.562  1.00 6.68  ? 80  HIS F CE1 1 
ATOM   1765 N  NE2 . HIS B 1 80  ? 26.179 20.637  12.196  1.00 7.46  ? 80  HIS F NE2 1 
ATOM   1766 N  N   . VAL B 1 81  ? 29.168 15.251  10.092  1.00 6.60  ? 81  VAL F N   1 
ATOM   1767 C  CA  . VAL B 1 81  ? 29.379 13.917  9.507   1.00 7.12  ? 81  VAL F CA  1 
ATOM   1768 C  C   . VAL B 1 81  ? 28.123 13.431  8.777   1.00 7.13  ? 81  VAL F C   1 
ATOM   1769 O  O   . VAL B 1 81  ? 28.218 12.896  7.669   1.00 7.39  ? 81  VAL F O   1 
ATOM   1770 C  CB  . VAL B 1 81  ? 29.885 12.878  10.539  1.00 7.39  ? 81  VAL F CB  1 
ATOM   1771 C  CG1 . VAL B 1 81  ? 29.853 11.460  9.962   1.00 6.14  ? 81  VAL F CG1 1 
ATOM   1772 C  CG2 . VAL B 1 81  ? 31.309 13.210  10.949  1.00 9.17  ? 81  VAL F CG2 1 
ATOM   1773 N  N   . GLY B 1 82  ? 26.950 13.669  9.354   1.00 7.86  ? 82  GLY F N   1 
ATOM   1774 C  CA  . GLY B 1 82  ? 25.694 13.229  8.752   1.00 8.44  ? 82  GLY F CA  1 
ATOM   1775 C  C   . GLY B 1 82  ? 25.153 14.035  7.579   1.00 6.99  ? 82  GLY F C   1 
ATOM   1776 O  O   . GLY B 1 82  ? 24.043 13.779  7.130   1.00 7.36  ? 82  GLY F O   1 
ATOM   1777 N  N   . ASP B 1 83  ? 25.922 15.001  7.073   1.00 6.36  ? 83  ASP F N   1 
ATOM   1778 C  CA  . ASP B 1 83  ? 25.464 15.845  5.978   1.00 5.71  ? 83  ASP F CA  1 
ATOM   1779 C  C   . ASP B 1 83  ? 25.743 15.230  4.617   1.00 6.64  ? 83  ASP F C   1 
ATOM   1780 O  O   . ASP B 1 83  ? 26.794 15.480  4.014   1.00 7.97  ? 83  ASP F O   1 
ATOM   1781 C  CB  . ASP B 1 83  ? 26.139 17.209  6.075   1.00 5.62  ? 83  ASP F CB  1 
ATOM   1782 C  CG  . ASP B 1 83  ? 25.678 18.002  7.265   1.00 6.51  ? 83  ASP F CG  1 
ATOM   1783 O  OD1 . ASP B 1 83  ? 24.640 17.649  7.880   1.00 7.28  ? 83  ASP F OD1 1 
ATOM   1784 O  OD2 . ASP B 1 83  ? 26.359 18.995  7.600   1.00 6.48  ? 83  ASP F OD2 1 
ATOM   1785 N  N   . LEU B 1 84  ? 24.775 14.465  4.126   1.00 6.04  ? 84  LEU F N   1 
ATOM   1786 C  CA  . LEU B 1 84  ? 24.859 13.818  2.826   1.00 5.85  ? 84  LEU F CA  1 
ATOM   1787 C  C   . LEU B 1 84  ? 24.112 14.582  1.737   1.00 6.74  ? 84  LEU F C   1 
ATOM   1788 O  O   . LEU B 1 84  ? 23.935 14.062  0.637   1.00 7.97  ? 84  LEU F O   1 
ATOM   1789 C  CB  . LEU B 1 84  ? 24.370 12.365  2.936   1.00 6.15  ? 84  LEU F CB  1 
ATOM   1790 C  CG  . LEU B 1 84  ? 25.235 11.495  3.847   1.00 7.44  ? 84  LEU F CG  1 
ATOM   1791 C  CD1 . LEU B 1 84  ? 24.655 10.088  3.915   1.00 7.33  ? 84  LEU F CD1 1 
ATOM   1792 C  CD2 . LEU B 1 84  ? 26.696 11.479  3.426   1.00 8.37  ? 84  LEU F CD2 1 
ATOM   1793 N  N   . GLY B 1 85  ? 23.704 15.822  2.012   1.00 7.19  ? 85  GLY F N   1 
ATOM   1794 C  CA  . GLY B 1 85  ? 23.185 16.693  0.976   1.00 9.05  ? 85  GLY F CA  1 
ATOM   1795 C  C   . GLY B 1 85  ? 21.747 16.418  0.621   1.00 8.34  ? 85  GLY F C   1 
ATOM   1796 O  O   . GLY B 1 85  ? 20.865 16.429  1.496   1.00 9.04  ? 85  GLY F O   1 
ATOM   1797 N  N   . ASN B 1 86  ? 21.514 16.212  -0.674  1.00 8.02  ? 86  ASN F N   1 
ATOM   1798 C  CA  . ASN B 1 86  ? 20.197 15.961  -1.221  1.00 7.72  ? 86  ASN F CA  1 
ATOM   1799 C  C   . ASN B 1 86  ? 20.219 14.755  -2.137  1.00 8.74  ? 86  ASN F C   1 
ATOM   1800 O  O   . ASN B 1 86  ? 21.224 14.483  -2.807  1.00 10.28 ? 86  ASN F O   1 
ATOM   1801 C  CB  . ASN B 1 86  ? 19.716 17.144  -2.057  1.00 7.01  ? 86  ASN F CB  1 
ATOM   1802 C  CG  . ASN B 1 86  ? 19.412 18.366  -1.222  1.00 8.62  ? 86  ASN F CG  1 
ATOM   1803 O  OD1 . ASN B 1 86  ? 18.469 18.368  -0.437  1.00 9.31  ? 86  ASN F OD1 1 
ATOM   1804 N  ND2 . ASN B 1 86  ? 20.189 19.421  -1.414  1.00 9.32  ? 86  ASN F ND2 1 
ATOM   1805 N  N   . VAL B 1 87  ? 19.089 14.059  -2.167  1.00 8.57  ? 87  VAL F N   1 
ATOM   1806 C  CA  . VAL B 1 87  ? 18.774 13.127  -3.232  1.00 8.71  ? 87  VAL F CA  1 
ATOM   1807 C  C   . VAL B 1 87  ? 17.773 13.795  -4.162  1.00 9.67  ? 87  VAL F C   1 
ATOM   1808 O  O   . VAL B 1 87  ? 17.061 14.730  -3.767  1.00 9.79  ? 87  VAL F O   1 
ATOM   1809 C  CB  . VAL B 1 87  ? 18.250 11.776  -2.698  1.00 9.31  ? 87  VAL F CB  1 
ATOM   1810 C  CG1 . VAL B 1 87  ? 19.283 11.174  -1.768  1.00 10.11 ? 87  VAL F CG1 1 
ATOM   1811 C  CG2 . VAL B 1 87  ? 16.894 11.913  -2.010  1.00 11.01 ? 87  VAL F CG2 1 
ATOM   1812 N  N   . THR B 1 88  ? 17.741 13.320  -5.401  1.00 11.18 ? 88  THR F N   1 
ATOM   1813 C  CA  . THR B 1 88  ? 16.930 13.931  -6.452  1.00 12.08 ? 88  THR F CA  1 
ATOM   1814 C  C   . THR B 1 88  ? 15.873 12.957  -6.918  1.00 11.90 ? 88  THR F C   1 
ATOM   1815 O  O   . THR B 1 88  ? 16.206 11.882  -7.404  1.00 12.89 ? 88  THR F O   1 
ATOM   1816 C  CB  . THR B 1 88  ? 17.803 14.349  -7.638  1.00 12.72 ? 88  THR F CB  1 
ATOM   1817 O  OG1 . THR B 1 88  ? 18.813 15.242  -7.172  1.00 13.07 ? 88  THR F OG1 1 
ATOM   1818 C  CG2 . THR B 1 88  ? 16.972 15.038  -8.719  1.00 13.58 ? 88  THR F CG2 1 
ATOM   1819 N  N   . ALA B 1 89  ? 14.607 13.345  -6.770  1.00 11.63 ? 89  ALA F N   1 
ATOM   1820 C  CA  . ALA B 1 89  ? 13.479 12.559  -7.244  1.00 12.39 ? 89  ALA F CA  1 
ATOM   1821 C  C   . ALA B 1 89  ? 13.033 13.050  -8.617  1.00 13.14 ? 89  ALA F C   1 
ATOM   1822 O  O   . ALA B 1 89  ? 12.940 14.260  -8.851  1.00 13.56 ? 89  ALA F O   1 
ATOM   1823 C  CB  . ALA B 1 89  ? 12.320 12.630  -6.259  1.00 12.16 ? 89  ALA F CB  1 
ATOM   1824 N  N   . ASP B 1 90  ? 12.736 12.096  -9.498  1.00 14.06 ? 90  ASP F N   1 
ATOM   1825 C  CA  . ASP B 1 90  ? 12.232 12.376  -10.846 1.00 15.36 ? 90  ASP F CA  1 
ATOM   1826 C  C   . ASP B 1 90  ? 10.717 12.634  -10.824 1.00 15.86 ? 90  ASP F C   1 
ATOM   1827 O  O   . ASP B 1 90  ? 10.096 12.618  -9.757  1.00 15.51 ? 90  ASP F O   1 
ATOM   1828 C  CB  . ASP B 1 90  ? 12.638 11.246  -11.828 1.00 16.69 ? 90  ASP F CB  1 
ATOM   1829 C  CG  . ASP B 1 90  ? 12.001 9.875   -11.516 0.80 16.33 ? 90  ASP F CG  1 
ATOM   1830 O  OD1 . ASP B 1 90  ? 10.944 9.789   -10.856 0.80 16.16 ? 90  ASP F OD1 1 
ATOM   1831 O  OD2 . ASP B 1 90  ? 12.574 8.858   -11.974 0.80 18.17 ? 90  ASP F OD2 1 
ATOM   1832 N  N   . LYS B 1 91  ? 10.117 12.855  -11.994 1.00 16.34 ? 91  LYS F N   1 
ATOM   1833 C  CA  . LYS B 1 91  ? 8.663  13.080  -12.085 1.00 16.26 ? 91  LYS F CA  1 
ATOM   1834 C  C   . LYS B 1 91  ? 7.793  11.864  -11.709 1.00 15.91 ? 91  LYS F C   1 
ATOM   1835 O  O   . LYS B 1 91  ? 6.605  12.037  -11.446 1.00 16.18 ? 91  LYS F O   1 
ATOM   1836 C  CB  . LYS B 1 91  ? 8.262  13.620  -13.471 1.00 16.06 ? 91  LYS F CB  1 
ATOM   1837 C  CG  . LYS B 1 91  ? 8.489  15.125  -13.650 1.00 17.37 ? 91  LYS F CG  1 
ATOM   1838 C  CD  . LYS B 1 91  ? 7.558  15.966  -12.779 1.00 19.33 ? 91  LYS F CD  1 
ATOM   1839 C  CE  . LYS B 1 91  ? 7.343  17.355  -13.354 1.00 21.32 ? 91  LYS F CE  1 
ATOM   1840 N  NZ  . LYS B 1 91  ? 6.851  18.327  -12.341 1.00 24.19 ? 91  LYS F NZ  1 
ATOM   1841 N  N   . ASP B 1 92  ? 8.372  10.657  -11.685 1.00 15.25 ? 92  ASP F N   1 
ATOM   1842 C  CA  . ASP B 1 92  ? 7.701  9.461   -11.131 1.00 16.42 ? 92  ASP F CA  1 
ATOM   1843 C  C   . ASP B 1 92  ? 7.864  9.323   -9.616  1.00 13.58 ? 92  ASP F C   1 
ATOM   1844 O  O   . ASP B 1 92  ? 7.335  8.384   -9.018  1.00 16.90 ? 92  ASP F O   1 
ATOM   1845 C  CB  . ASP B 1 92  ? 8.218  8.176   -11.797 1.00 19.80 ? 92  ASP F CB  1 
ATOM   1846 C  CG  . ASP B 1 92  ? 7.835  8.077   -13.256 1.00 24.05 ? 92  ASP F CG  1 
ATOM   1847 O  OD1 . ASP B 1 92  ? 6.719  8.502   -13.627 1.00 27.46 ? 92  ASP F OD1 1 
ATOM   1848 O  OD2 . ASP B 1 92  ? 8.653  7.550   -14.031 1.00 31.71 ? 92  ASP F OD2 1 
ATOM   1849 N  N   . GLY B 1 93  ? 8.605  10.243  -9.006  1.00 13.15 ? 93  GLY F N   1 
ATOM   1850 C  CA  . GLY B 1 93  ? 8.774  10.271  -7.559  1.00 13.60 ? 93  GLY F CA  1 
ATOM   1851 C  C   . GLY B 1 93  ? 9.855  9.357   -7.037  1.00 13.00 ? 93  GLY F C   1 
ATOM   1852 O  O   . GLY B 1 93  ? 9.918  9.100   -5.827  1.00 12.45 ? 93  GLY F O   1 
ATOM   1853 N  N   . VAL B 1 94  ? 10.729 8.909   -7.935  1.00 13.38 ? 94  VAL F N   1 
ATOM   1854 C  CA  . VAL B 1 94  ? 11.797 7.978   -7.606  1.00 15.42 ? 94  VAL F CA  1 
ATOM   1855 C  C   . VAL B 1 94  ? 13.138 8.714   -7.567  1.00 13.78 ? 94  VAL F C   1 
ATOM   1856 O  O   . VAL B 1 94  ? 13.520 9.394   -8.524  1.00 15.52 ? 94  VAL F O   1 
ATOM   1857 C  CB  . VAL B 1 94  ? 11.865 6.820   -8.621  1.00 15.71 ? 94  VAL F CB  1 
ATOM   1858 C  CG1 . VAL B 1 94  ? 12.979 5.850   -8.265  1.00 11.50 ? 94  VAL F CG1 1 
ATOM   1859 C  CG2 . VAL B 1 94  ? 10.533 6.086   -8.688  1.00 17.22 ? 94  VAL F CG2 1 
ATOM   1860 N  N   . ALA B 1 95  ? 13.840 8.561   -6.449  1.00 13.64 ? 95  ALA F N   1 
ATOM   1861 C  CA  . ALA B 1 95  ? 15.210 9.015   -6.309  1.00 12.75 ? 95  ALA F CA  1 
ATOM   1862 C  C   . ALA B 1 95  ? 16.142 7.817   -6.371  1.00 12.85 ? 95  ALA F C   1 
ATOM   1863 O  O   . ALA B 1 95  ? 16.101 6.946   -5.494  1.00 13.93 ? 95  ALA F O   1 
ATOM   1864 C  CB  . ALA B 1 95  ? 15.391 9.747   -4.989  1.00 12.13 ? 95  ALA F CB  1 
ATOM   1865 N  N   . ASP B 1 96  ? 16.969 7.762   -7.411  1.00 11.69 ? 96  ASP F N   1 
ATOM   1866 C  CA  . ASP B 1 96  ? 18.018 6.758   -7.488  1.00 14.73 ? 96  ASP F CA  1 
ATOM   1867 C  C   . ASP B 1 96  ? 19.245 7.358   -6.817  1.00 14.72 ? 96  ASP F C   1 
ATOM   1868 O  O   . ASP B 1 96  ? 19.753 8.394   -7.225  1.00 16.81 ? 96  ASP F O   1 
ATOM   1869 C  CB  . ASP B 1 96  ? 18.271 6.325   -8.936  1.00 15.26 ? 96  ASP F CB  1 
ATOM   1870 C  CG  . ASP B 1 96  ? 17.120 5.490   -9.498  0.50 13.85 ? 96  ASP F CG  1 
ATOM   1871 O  OD1 . ASP B 1 96  ? 16.704 4.517   -8.827  0.50 11.61 ? 96  ASP F OD1 1 
ATOM   1872 O  OD2 . ASP B 1 96  ? 16.625 5.814   -10.600 0.50 14.27 ? 96  ASP F OD2 1 
ATOM   1873 N  N   . VAL B 1 97  ? 19.678 6.724   -5.738  1.00 13.64 ? 97  VAL F N   1 
ATOM   1874 C  CA  . VAL B 1 97  ? 20.767 7.231   -4.937  1.00 15.89 ? 97  VAL F CA  1 
ATOM   1875 C  C   . VAL B 1 97  ? 22.062 6.565   -5.366  1.00 14.28 ? 97  VAL F C   1 
ATOM   1876 O  O   . VAL B 1 97  ? 22.144 5.334   -5.464  1.00 14.11 ? 97  VAL F O   1 
ATOM   1877 C  CB  . VAL B 1 97  ? 20.510 6.993   -3.442  1.00 13.96 ? 97  VAL F CB  1 
ATOM   1878 C  CG1 . VAL B 1 97  ? 21.632 7.578   -2.602  1.00 14.14 ? 97  VAL F CG1 1 
ATOM   1879 C  CG2 . VAL B 1 97  ? 19.166 7.594   -3.052  1.00 15.10 ? 97  VAL F CG2 1 
ATOM   1880 N  N   . SER B 1 98  ? 23.058 7.401   -5.632  1.00 17.83 ? 98  SER F N   1 
ATOM   1881 C  CA  . SER B 1 98  ? 24.411 6.974   -5.908  1.00 18.48 ? 98  SER F CA  1 
ATOM   1882 C  C   . SER B 1 98  ? 25.327 8.077   -5.386  1.00 20.29 ? 98  SER F C   1 
ATOM   1883 O  O   . SER B 1 98  ? 25.438 9.147   -5.996  1.00 26.24 ? 98  SER F O   1 
ATOM   1884 C  CB  . SER B 1 98  ? 24.607 6.758   -7.409  1.00 20.99 ? 98  SER F CB  1 
ATOM   1885 O  OG  . SER B 1 98  ? 25.923 6.315   -7.678  1.00 24.17 ? 98  SER F OG  1 
ATOM   1886 N  N   . ILE B 1 99  ? 25.943 7.824   -4.238  1.00 23.78 ? 99  ILE F N   1 
ATOM   1887 C  CA  . ILE B 1 99  ? 26.809 8.783   -3.546  1.00 28.97 ? 99  ILE F CA  1 
ATOM   1888 C  C   . ILE B 1 99  ? 28.069 8.018   -3.179  1.00 17.88 ? 99  ILE F C   1 
ATOM   1889 O  O   . ILE B 1 99  ? 28.003 6.829   -2.890  1.00 16.70 ? 99  ILE F O   1 
ATOM   1890 C  CB  . ILE B 1 99  ? 26.133 9.308   -2.243  1.00 28.84 ? 99  ILE F CB  1 
ATOM   1891 C  CG1 . ILE B 1 99  ? 24.992 10.278  -2.568  1.00 29.60 ? 99  ILE F CG1 1 
ATOM   1892 C  CG2 . ILE B 1 99  ? 27.125 9.992   -1.301  1.00 24.04 ? 99  ILE F CG2 1 
ATOM   1893 C  CD1 . ILE B 1 99  ? 23.984 10.429  -1.442  1.00 30.66 ? 99  ILE F CD1 1 
ATOM   1894 N  N   . GLU B 1 100 ? 29.206 8.701   -3.199  1.00 15.30 ? 100 GLU F N   1 
ATOM   1895 C  CA  . GLU B 1 100 ? 30.403 8.239   -2.508  1.00 15.05 ? 100 GLU F CA  1 
ATOM   1896 C  C   . GLU B 1 100 ? 30.766 9.352   -1.525  1.00 12.69 ? 100 GLU F C   1 
ATOM   1897 O  O   . GLU B 1 100 ? 30.810 10.535  -1.889  1.00 13.29 ? 100 GLU F O   1 
ATOM   1898 C  CB  . GLU B 1 100 ? 31.533 7.967   -3.500  1.00 18.49 ? 100 GLU F CB  1 
ATOM   1899 C  CG  . GLU B 1 100 ? 32.833 7.512   -2.861  1.00 20.74 ? 100 GLU F CG  1 
ATOM   1900 C  CD  . GLU B 1 100 ? 33.959 7.367   -3.866  1.00 26.53 ? 100 GLU F CD  1 
ATOM   1901 O  OE1 . GLU B 1 100 ? 33.932 6.394   -4.650  1.00 32.31 ? 100 GLU F OE1 1 
ATOM   1902 O  OE2 . GLU B 1 100 ? 34.876 8.219   -3.855  1.00 27.20 ? 100 GLU F OE2 1 
ATOM   1903 N  N   . ASP B 1 101 ? 31.014 8.983   -0.278  1.00 13.03 ? 101 ASP F N   1 
ATOM   1904 C  CA  . ASP B 1 101 ? 31.318 9.969   0.741   1.00 11.58 ? 101 ASP F CA  1 
ATOM   1905 C  C   . ASP B 1 101 ? 32.512 9.551   1.566   1.00 10.75 ? 101 ASP F C   1 
ATOM   1906 O  O   . ASP B 1 101 ? 32.617 8.394   1.985   1.00 12.24 ? 101 ASP F O   1 
ATOM   1907 C  CB  . ASP B 1 101 ? 30.119 10.187  1.645   1.00 9.15  ? 101 ASP F CB  1 
ATOM   1908 C  CG  . ASP B 1 101 ? 30.264 11.426  2.495   1.00 10.15 ? 101 ASP F CG  1 
ATOM   1909 O  OD1 . ASP B 1 101 ? 30.064 12.529  1.939   1.00 11.76 ? 101 ASP F OD1 1 
ATOM   1910 O  OD2 . ASP B 1 101 ? 30.604 11.309  3.697   1.00 10.50 ? 101 ASP F OD2 1 
ATOM   1911 N  N   . SER B 1 102 ? 33.387 10.516  1.819   1.00 11.33 ? 102 SER F N   1 
ATOM   1912 C  CA  . SER B 1 102 ? 34.658 10.283  2.477   1.00 12.58 ? 102 SER F CA  1 
ATOM   1913 C  C   . SER B 1 102 ? 34.649 10.590  3.991   1.00 11.17 ? 102 SER F C   1 
ATOM   1914 O  O   . SER B 1 102 ? 35.642 10.345  4.670   1.00 12.16 ? 102 SER F O   1 
ATOM   1915 C  CB  . SER B 1 102 ? 35.734 11.107  1.740   1.00 12.87 ? 102 SER F CB  1 
ATOM   1916 O  OG  A SER B 1 102 ? 36.225 10.223  0.748   0.60 17.40 ? 102 SER F OG  1 
ATOM   1917 O  OG  B SER B 1 102 ? 35.615 12.407  2.293   0.40 13.62 ? 102 SER F OG  1 
ATOM   1918 N  N   . VAL B 1 103 ? 33.532 11.109  4.508   1.00 8.32  ? 103 VAL F N   1 
ATOM   1919 C  CA  . VAL B 1 103 ? 33.453 11.592  5.895   1.00 7.33  ? 103 VAL F CA  1 
ATOM   1920 C  C   . VAL B 1 103 ? 32.659 10.633  6.784   1.00 6.82  ? 103 VAL F C   1 
ATOM   1921 O  O   . VAL B 1 103 ? 33.100 10.324  7.892   1.00 7.90  ? 103 VAL F O   1 
ATOM   1922 C  CB  . VAL B 1 103 ? 32.846 13.004  5.937   1.00 9.57  ? 103 VAL F CB  1 
ATOM   1923 C  CG1 . VAL B 1 103 ? 32.679 13.480  7.375   1.00 10.07 ? 103 VAL F CG1 1 
ATOM   1924 C  CG2 . VAL B 1 103 ? 33.712 13.982  5.143   1.00 9.49  ? 103 VAL F CG2 1 
ATOM   1925 N  N   . ILE B 1 104 ? 31.498 10.171  6.324   1.00 6.59  ? 104 ILE F N   1 
ATOM   1926 C  CA  . ILE B 1 104 ? 30.837 9.040   7.003   1.00 8.95  ? 104 ILE F CA  1 
ATOM   1927 C  C   . ILE B 1 104 ? 31.770 7.830   6.987   1.00 9.09  ? 104 ILE F C   1 
ATOM   1928 O  O   . ILE B 1 104 ? 32.661 7.723   6.136   1.00 9.51  ? 104 ILE F O   1 
ATOM   1929 C  CB  . ILE B 1 104 ? 29.468 8.632   6.391   1.00 10.95 ? 104 ILE F CB  1 
ATOM   1930 C  CG1 . ILE B 1 104 ? 29.607 8.209   4.916   1.00 11.74 ? 104 ILE F CG1 1 
ATOM   1931 C  CG2 . ILE B 1 104 ? 28.451 9.758   6.559   1.00 9.23  ? 104 ILE F CG2 1 
ATOM   1932 C  CD1 . ILE B 1 104 ? 28.356 7.618   4.309   1.00 10.63 ? 104 ILE F CD1 1 
ATOM   1933 N  N   . SER B 1 105 ? 31.561 6.925   7.934   1.00 8.65  ? 105 SER F N   1 
ATOM   1934 C  CA  . SER B 1 105 ? 32.278 5.657   7.961   1.00 9.52  ? 105 SER F CA  1 
ATOM   1935 C  C   . SER B 1 105 ? 31.375 4.568   8.521   1.00 9.42  ? 105 SER F C   1 
ATOM   1936 O  O   . SER B 1 105 ? 30.314 4.854   9.086   1.00 9.00  ? 105 SER F O   1 
ATOM   1937 C  CB  . SER B 1 105 ? 33.534 5.786   8.814   1.00 10.26 ? 105 SER F CB  1 
ATOM   1938 O  OG  . SER B 1 105 ? 34.348 4.642   8.698   1.00 9.57  ? 105 SER F OG  1 
ATOM   1939 N  N   . LEU B 1 106 ? 31.800 3.323   8.333   1.00 9.10  ? 106 LEU F N   1 
ATOM   1940 C  CA  . LEU B 1 106 ? 31.149 2.185   8.949   1.00 10.19 ? 106 LEU F CA  1 
ATOM   1941 C  C   . LEU B 1 106 ? 31.985 1.629   10.108  1.00 10.41 ? 106 LEU F C   1 
ATOM   1942 O  O   . LEU B 1 106 ? 31.686 0.559   10.617  1.00 12.25 ? 106 LEU F O   1 
ATOM   1943 C  CB  . LEU B 1 106 ? 30.829 1.119   7.892   1.00 13.44 ? 106 LEU F CB  1 
ATOM   1944 C  CG  . LEU B 1 106 ? 29.993 1.620   6.711   1.00 11.34 ? 106 LEU F CG  1 
ATOM   1945 C  CD1 . LEU B 1 106 ? 29.703 0.465   5.757   1.00 9.17  ? 106 LEU F CD1 1 
ATOM   1946 C  CD2 . LEU B 1 106 ? 28.685 2.269   7.152   1.00 7.29  ? 106 LEU F CD2 1 
ATOM   1947 N  N   . SER B 1 107 ? 32.994 2.391   10.546  1.00 14.33 ? 107 SER F N   1 
ATOM   1948 C  CA  . SER B 1 107 ? 33.742 2.102   11.774  1.00 11.27 ? 107 SER F CA  1 
ATOM   1949 C  C   . SER B 1 107 ? 34.297 3.392   12.406  1.00 11.27 ? 107 SER F C   1 
ATOM   1950 O  O   . SER B 1 107 ? 34.306 4.452   11.772  1.00 12.78 ? 107 SER F O   1 
ATOM   1951 C  CB  . SER B 1 107 ? 34.875 1.113   11.487  1.00 13.88 ? 107 SER F CB  1 
ATOM   1952 O  OG  . SER B 1 107 ? 35.915 1.722   10.749  1.00 17.96 ? 107 SER F OG  1 
ATOM   1953 N  N   . GLY B 1 108 ? 34.736 3.296   13.663  1.00 13.31 ? 108 GLY F N   1 
ATOM   1954 C  CA  . GLY B 1 108 ? 35.327 4.440   14.378  1.00 11.63 ? 108 GLY F CA  1 
ATOM   1955 C  C   . GLY B 1 108 ? 34.285 5.456   14.815  1.00 13.22 ? 108 GLY F C   1 
ATOM   1956 O  O   . GLY B 1 108 ? 33.096 5.211   14.683  1.00 12.67 ? 108 GLY F O   1 
ATOM   1957 N  N   . ASP B 1 109 ? 34.712 6.615   15.323  1.00 14.72 ? 109 ASP F N   1 
ATOM   1958 C  CA  . ASP B 1 109 ? 33.724 7.581   15.836  1.00 15.40 ? 109 ASP F CA  1 
ATOM   1959 C  C   . ASP B 1 109 ? 32.980 8.392   14.761  1.00 13.45 ? 109 ASP F C   1 
ATOM   1960 O  O   . ASP B 1 109 ? 32.116 9.189   15.114  1.00 14.59 ? 109 ASP F O   1 
ATOM   1961 C  CB  . ASP B 1 109 ? 34.288 8.476   16.959  1.00 16.72 ? 109 ASP F CB  1 
ATOM   1962 C  CG  . ASP B 1 109 ? 35.225 9.554   16.472  1.00 16.54 ? 109 ASP F CG  1 
ATOM   1963 O  OD1 . ASP B 1 109 ? 35.493 9.664   15.254  1.00 18.37 ? 109 ASP F OD1 1 
ATOM   1964 O  OD2 . ASP B 1 109 ? 35.701 10.299  17.347  1.00 15.51 ? 109 ASP F OD2 1 
ATOM   1965 N  N   . HIS B 1 110 ? 33.289 8.184   13.473  1.00 13.13 ? 110 HIS F N   1 
ATOM   1966 C  CA  . HIS B 1 110 ? 32.394 8.666   12.404  1.00 15.55 ? 110 HIS F CA  1 
ATOM   1967 C  C   . HIS B 1 110 ? 31.443 7.576   11.913  1.00 9.02  ? 110 HIS F C   1 
ATOM   1968 O  O   . HIS B 1 110 ? 30.769 7.744   10.895  1.00 9.02  ? 110 HIS F O   1 
ATOM   1969 C  CB  . HIS B 1 110 ? 33.179 9.222   11.218  1.00 16.03 ? 110 HIS F CB  1 
ATOM   1970 C  CG  . HIS B 1 110 ? 34.083 10.352  11.578  1.00 14.62 ? 110 HIS F CG  1 
ATOM   1971 N  ND1 . HIS B 1 110 ? 34.996 10.879  10.696  1.00 16.67 ? 110 HIS F ND1 1 
ATOM   1972 C  CD2 . HIS B 1 110 ? 34.222 11.052  12.727  1.00 15.69 ? 110 HIS F CD2 1 
ATOM   1973 C  CE1 . HIS B 1 110 ? 35.671 11.846  11.287  1.00 15.65 ? 110 HIS F CE1 1 
ATOM   1974 N  NE2 . HIS B 1 110 ? 35.213 11.979  12.517  1.00 17.49 ? 110 HIS F NE2 1 
ATOM   1975 N  N   . CYS B 1 111 ? 31.364 6.479   12.667  1.00 8.83  ? 111 CYS F N   1 
ATOM   1976 C  CA  . CYS B 1 111 ? 30.530 5.353   12.291  1.00 9.32  ? 111 CYS F CA  1 
ATOM   1977 C  C   . CYS B 1 111 ? 29.058 5.730   12.347  1.00 7.59  ? 111 CYS F C   1 
ATOM   1978 O  O   . CYS B 1 111 ? 28.613 6.359   13.308  1.00 9.09  ? 111 CYS F O   1 
ATOM   1979 C  CB  . CYS B 1 111 ? 30.787 4.171   13.213  1.00 9.22  ? 111 CYS F CB  1 
ATOM   1980 S  SG  . CYS B 1 111 ? 29.917 2.682   12.740  1.00 11.03 ? 111 CYS F SG  1 
ATOM   1981 N  N   . ILE B 1 112 ? 28.322 5.350   11.305  1.00 6.92  ? 112 ILE F N   1 
ATOM   1982 C  CA  . ILE B 1 112 ? 26.894 5.650   11.195  1.00 6.75  ? 112 ILE F CA  1 
ATOM   1983 C  C   . ILE B 1 112 ? 25.988 4.442   11.417  1.00 6.23  ? 112 ILE F C   1 
ATOM   1984 O  O   . ILE B 1 112 ? 24.769 4.574   11.376  1.00 6.53  ? 112 ILE F O   1 
ATOM   1985 C  CB  . ILE B 1 112 ? 26.541 6.328   9.842   1.00 6.42  ? 112 ILE F CB  1 
ATOM   1986 C  CG1 . ILE B 1 112 ? 26.808 5.411   8.635   1.00 6.65  ? 112 ILE F CG1 1 
ATOM   1987 C  CG2 . ILE B 1 112 ? 27.283 7.655   9.720   1.00 6.75  ? 112 ILE F CG2 1 
ATOM   1988 C  CD1 . ILE B 1 112 ? 26.249 5.941   7.335   1.00 7.46  ? 112 ILE F CD1 1 
ATOM   1989 N  N   . ILE B 1 113 ? 26.568 3.262   11.631  1.00 6.03  ? 113 ILE F N   1 
ATOM   1990 C  CA  . ILE B 1 113 ? 25.768 2.093   11.980  1.00 6.60  ? 113 ILE F CA  1 
ATOM   1991 C  C   . ILE B 1 113 ? 25.121 2.361   13.346  1.00 6.80  ? 113 ILE F C   1 
ATOM   1992 O  O   . ILE B 1 113 ? 25.777 2.875   14.268  1.00 6.98  ? 113 ILE F O   1 
ATOM   1993 C  CB  . ILE B 1 113 ? 26.612 0.795   11.972  1.00 7.64  ? 113 ILE F CB  1 
ATOM   1994 C  CG1 . ILE B 1 113 ? 26.917 0.363   10.526  1.00 9.40  ? 113 ILE F CG1 1 
ATOM   1995 C  CG2 . ILE B 1 113 ? 25.896 -0.339  12.696  1.00 7.62  ? 113 ILE F CG2 1 
ATOM   1996 C  CD1 . ILE B 1 113 ? 28.165 -0.488  10.384  1.00 10.35 ? 113 ILE F CD1 1 
ATOM   1997 N  N   . GLY B 1 114 ? 23.834 2.038   13.450  1.00 5.77  ? 114 GLY F N   1 
ATOM   1998 C  CA  . GLY B 1 114 ? 23.062 2.266   14.669  1.00 5.48  ? 114 GLY F CA  1 
ATOM   1999 C  C   . GLY B 1 114 ? 22.454 3.651   14.763  1.00 6.07  ? 114 GLY F C   1 
ATOM   2000 O  O   . GLY B 1 114 ? 21.837 3.984   15.771  1.00 7.46  ? 114 GLY F O   1 
ATOM   2001 N  N   . ARG B 1 115 ? 22.610 4.456   13.715  1.00 7.07  ? 115 ARG F N   1 
ATOM   2002 C  CA  . ARG B 1 115 ? 22.054 5.801   13.673  1.00 7.16  ? 115 ARG F CA  1 
ATOM   2003 C  C   . ARG B 1 115 ? 20.919 5.809   12.655  1.00 7.36  ? 115 ARG F C   1 
ATOM   2004 O  O   . ARG B 1 115 ? 20.597 4.772   12.074  1.00 7.36  ? 115 ARG F O   1 
ATOM   2005 C  CB  . ARG B 1 115 ? 23.165 6.799   13.364  1.00 7.71  ? 115 ARG F CB  1 
ATOM   2006 C  CG  . ARG B 1 115 ? 24.294 6.706   14.387  1.00 8.00  ? 115 ARG F CG  1 
ATOM   2007 C  CD  . ARG B 1 115 ? 25.277 7.861   14.331  1.00 8.60  ? 115 ARG F CD  1 
ATOM   2008 N  NE  . ARG B 1 115 ? 26.426 7.623   15.218  1.00 9.07  ? 115 ARG F NE  1 
ATOM   2009 C  CZ  . ARG B 1 115 ? 26.473 7.890   16.523  1.00 8.89  ? 115 ARG F CZ  1 
ATOM   2010 N  NH1 . ARG B 1 115 ? 25.431 8.421   17.155  1.00 7.90  ? 115 ARG F NH1 1 
ATOM   2011 N  NH2 . ARG B 1 115 ? 27.593 7.656   17.200  1.00 9.66  ? 115 ARG F NH2 1 
ATOM   2012 N  N   . THR B 1 116 ? 20.277 6.950   12.473  1.00 7.11  ? 116 THR F N   1 
ATOM   2013 C  CA  . THR B 1 116 ? 19.076 7.028   11.656  1.00 7.27  ? 116 THR F CA  1 
ATOM   2014 C  C   . THR B 1 116 ? 19.347 7.788   10.369  1.00 6.71  ? 116 THR F C   1 
ATOM   2015 O  O   . THR B 1 116 ? 19.792 8.936   10.400  1.00 7.85  ? 116 THR F O   1 
ATOM   2016 C  CB  . THR B 1 116 ? 17.924 7.706   12.416  1.00 7.58  ? 116 THR F CB  1 
ATOM   2017 O  OG1 . THR B 1 116 ? 17.572 6.913   13.558  1.00 8.01  ? 116 THR F OG1 1 
ATOM   2018 C  CG2 . THR B 1 116 ? 16.687 7.855   11.542  1.00 6.78  ? 116 THR F CG2 1 
ATOM   2019 N  N   . LEU B 1 117 ? 19.057 7.147   9.241   1.00 6.96  ? 117 LEU F N   1 
ATOM   2020 C  CA  . LEU B 1 117 ? 19.054 7.827   7.953   1.00 5.83  ? 117 LEU F CA  1 
ATOM   2021 C  C   . LEU B 1 117 ? 17.678 8.439   7.727   1.00 6.48  ? 117 LEU F C   1 
ATOM   2022 O  O   . LEU B 1 117 ? 16.667 7.790   7.969   1.00 6.92  ? 117 LEU F O   1 
ATOM   2023 C  CB  . LEU B 1 117 ? 19.390 6.841   6.833   1.00 5.36  ? 117 LEU F CB  1 
ATOM   2024 C  CG  . LEU B 1 117 ? 19.588 7.409   5.426   1.00 5.79  ? 117 LEU F CG  1 
ATOM   2025 C  CD1 . LEU B 1 117 ? 20.840 8.259   5.348   1.00 6.73  ? 117 LEU F CD1 1 
ATOM   2026 C  CD2 . LEU B 1 117 ? 19.681 6.273   4.421   1.00 6.15  ? 117 LEU F CD2 1 
ATOM   2027 N  N   . VAL B 1 118 ? 17.654 9.698   7.273   1.00 6.76  ? 118 VAL F N   1 
ATOM   2028 C  CA  . VAL B 1 118 ? 16.421 10.478  7.107   1.00 6.75  ? 118 VAL F CA  1 
ATOM   2029 C  C   . VAL B 1 118 ? 16.400 11.113  5.717   1.00 6.56  ? 118 VAL F C   1 
ATOM   2030 O  O   . VAL B 1 118 ? 17.398 11.693  5.285   1.00 7.13  ? 118 VAL F O   1 
ATOM   2031 C  CB  . VAL B 1 118 ? 16.309 11.605  8.168   1.00 6.77  ? 118 VAL F CB  1 
ATOM   2032 C  CG1 . VAL B 1 118 ? 15.023 12.406  7.993   1.00 7.20  ? 118 VAL F CG1 1 
ATOM   2033 C  CG2 . VAL B 1 118 ? 16.377 11.022  9.576   1.00 7.22  ? 118 VAL F CG2 1 
ATOM   2034 N  N   . VAL B 1 119 ? 15.257 11.015  5.046   1.00 5.21  ? 119 VAL F N   1 
ATOM   2035 C  CA  . VAL B 1 119 ? 14.991 11.789  3.828   1.00 6.67  ? 119 VAL F CA  1 
ATOM   2036 C  C   . VAL B 1 119 ? 13.910 12.830  4.136   1.00 7.40  ? 119 VAL F C   1 
ATOM   2037 O  O   . VAL B 1 119 ? 12.897 12.533  4.789   1.00 7.83  ? 119 VAL F O   1 
ATOM   2038 C  CB  . VAL B 1 119 ? 14.648 10.897  2.597   1.00 7.25  ? 119 VAL F CB  1 
ATOM   2039 C  CG1 . VAL B 1 119 ? 13.384 10.081  2.805   1.00 7.90  ? 119 VAL F CG1 1 
ATOM   2040 C  CG2 . VAL B 1 119 ? 14.533 11.735  1.334   1.00 7.33  ? 119 VAL F CG2 1 
ATOM   2041 N  N   . HIS B 1 120 ? 14.139 14.050  3.654   1.00 8.55  ? 120 HIS F N   1 
ATOM   2042 C  CA  . HIS B 1 120 ? 13.360 15.220  4.054   1.00 9.31  ? 120 HIS F CA  1 
ATOM   2043 C  C   . HIS B 1 120 ? 12.380 15.712  3.011   1.00 10.15 ? 120 HIS F C   1 
ATOM   2044 O  O   . HIS B 1 120 ? 12.502 15.411  1.824   1.00 10.26 ? 120 HIS F O   1 
ATOM   2045 C  CB  . HIS B 1 120 ? 14.303 16.361  4.410   1.00 8.91  ? 120 HIS F CB  1 
ATOM   2046 C  CG  . HIS B 1 120 ? 14.816 16.290  5.804   1.00 8.04  ? 120 HIS F CG  1 
ATOM   2047 N  ND1 . HIS B 1 120 ? 14.124 16.817  6.873   1.00 9.81  ? 120 HIS F ND1 1 
ATOM   2048 C  CD2 . HIS B 1 120 ? 15.944 15.745  6.313   1.00 9.55  ? 120 HIS F CD2 1 
ATOM   2049 C  CE1 . HIS B 1 120 ? 14.809 16.606  7.979   1.00 10.68 ? 120 HIS F CE1 1 
ATOM   2050 N  NE2 . HIS B 1 120 ? 15.915 15.951  7.671   1.00 10.87 ? 120 HIS F NE2 1 
ATOM   2051 N  N   . GLU B 1 121 ? 11.427 16.500  3.500   1.00 11.58 ? 121 GLU F N   1 
ATOM   2052 C  CA  . GLU B 1 121 ? 10.377 17.144  2.711   1.00 13.22 ? 121 GLU F CA  1 
ATOM   2053 C  C   . GLU B 1 121 ? 10.910 18.064  1.606   1.00 12.90 ? 121 GLU F C   1 
ATOM   2054 O  O   . GLU B 1 121 ? 10.445 18.015  0.464   1.00 13.78 ? 121 GLU F O   1 
ATOM   2055 C  CB  . GLU B 1 121 ? 9.518  17.972  3.666   1.00 15.15 ? 121 GLU F CB  1 
ATOM   2056 C  CG  . GLU B 1 121 ? 8.291  18.638  3.064   1.00 16.55 ? 121 GLU F CG  1 
ATOM   2057 C  CD  . GLU B 1 121 ? 7.726  19.746  3.941   0.70 17.50 ? 121 GLU F CD  1 
ATOM   2058 O  OE1 . GLU B 1 121 ? 8.261  20.017  5.042   0.70 14.67 ? 121 GLU F OE1 1 
ATOM   2059 O  OE2 . GLU B 1 121 ? 6.733  20.358  3.509   0.70 19.50 ? 121 GLU F OE2 1 
ATOM   2060 N  N   . LYS B 1 122 ? 11.870 18.903  1.976   1.00 13.33 ? 122 LYS F N   1 
ATOM   2061 C  CA  . LYS B 1 122 ? 12.370 19.983  1.126   1.00 12.30 ? 122 LYS F CA  1 
ATOM   2062 C  C   . LYS B 1 122 ? 13.861 19.796  0.895   1.00 10.96 ? 122 LYS F C   1 
ATOM   2063 O  O   . LYS B 1 122 ? 14.489 18.869  1.426   1.00 10.18 ? 122 LYS F O   1 
ATOM   2064 C  CB  . LYS B 1 122 ? 12.081 21.347  1.785   1.00 14.53 ? 122 LYS F CB  1 
ATOM   2065 C  CG  . LYS B 1 122 ? 10.614 21.537  2.157   1.00 17.92 ? 122 LYS F CG  1 
ATOM   2066 C  CD  . LYS B 1 122 ? 10.264 22.962  2.566   1.00 20.45 ? 122 LYS F CD  1 
ATOM   2067 C  CE  . LYS B 1 122 ? 10.926 23.384  3.864   1.00 22.64 ? 122 LYS F CE  1 
ATOM   2068 N  NZ  . LYS B 1 122 ? 10.325 24.639  4.396   0.10 22.57 ? 122 LYS F NZ  1 
ATOM   2069 N  N   . ALA B 1 123 ? 14.427 20.660  0.071   1.00 10.20 ? 123 ALA F N   1 
ATOM   2070 C  CA  . ALA B 1 123 ? 15.853 20.635  -0.173  1.00 11.43 ? 123 ALA F CA  1 
ATOM   2071 C  C   . ALA B 1 123 ? 16.622 21.115  1.057   1.00 10.16 ? 123 ALA F C   1 
ATOM   2072 O  O   . ALA B 1 123 ? 16.194 22.036  1.767   1.00 11.59 ? 123 ALA F O   1 
ATOM   2073 C  CB  . ALA B 1 123 ? 16.196 21.485  -1.375  1.00 10.74 ? 123 ALA F CB  1 
ATOM   2074 N  N   . ASP B 1 124 ? 17.731 20.439  1.323   1.00 10.70 ? 124 ASP F N   1 
ATOM   2075 C  CA  . ASP B 1 124 ? 18.773 20.918  2.211   1.00 10.48 ? 124 ASP F CA  1 
ATOM   2076 C  C   . ASP B 1 124 ? 19.471 22.054  1.460   1.00 9.90  ? 124 ASP F C   1 
ATOM   2077 O  O   . ASP B 1 124 ? 19.947 21.862  0.343   1.00 10.53 ? 124 ASP F O   1 
ATOM   2078 C  CB  . ASP B 1 124 ? 19.738 19.764  2.523   1.00 10.61 ? 124 ASP F CB  1 
ATOM   2079 C  CG  . ASP B 1 124 ? 20.781 20.104  3.581   1.00 10.45 ? 124 ASP F CG  1 
ATOM   2080 O  OD1 . ASP B 1 124 ? 21.156 21.285  3.744   1.00 11.14 ? 124 ASP F OD1 1 
ATOM   2081 O  OD2 . ASP B 1 124 ? 21.266 19.162  4.236   1.00 9.87  ? 124 ASP F OD2 1 
ATOM   2082 N  N   . ASP B 1 125 ? 19.506 23.238  2.064   1.00 10.27 ? 125 ASP F N   1 
ATOM   2083 C  CA  . ASP B 1 125 ? 20.172 24.400  1.445   1.00 9.72  ? 125 ASP F CA  1 
ATOM   2084 C  C   . ASP B 1 125 ? 21.705 24.373  1.609   1.00 9.83  ? 125 ASP F C   1 
ATOM   2085 O  O   . ASP B 1 125 ? 22.386 25.305  1.184   1.00 10.84 ? 125 ASP F O   1 
ATOM   2086 C  CB  . ASP B 1 125 ? 19.550 25.732  1.931   1.00 9.40  ? 125 ASP F CB  1 
ATOM   2087 C  CG  . ASP B 1 125 ? 19.786 26.021  3.413   1.00 10.44 ? 125 ASP F CG  1 
ATOM   2088 O  OD1 . ASP B 1 125 ? 20.795 25.560  3.992   1.00 9.79  ? 125 ASP F OD1 1 
ATOM   2089 O  OD2 . ASP B 1 125 ? 18.950 26.757  3.991   1.00 11.49 ? 125 ASP F OD2 1 
ATOM   2090 N  N   . LEU B 1 126 ? 22.238 23.320  2.244   1.00 9.93  ? 126 LEU F N   1 
ATOM   2091 C  CA  . LEU B 1 126 ? 23.690 23.063  2.346   1.00 9.91  ? 126 LEU F CA  1 
ATOM   2092 C  C   . LEU B 1 126 ? 24.462 24.165  3.088   1.00 9.60  ? 126 LEU F C   1 
ATOM   2093 O  O   . LEU B 1 126 ? 25.665 24.354  2.880   1.00 10.95 ? 126 LEU F O   1 
ATOM   2094 C  CB  . LEU B 1 126 ? 24.307 22.772  0.962   1.00 9.35  ? 126 LEU F CB  1 
ATOM   2095 C  CG  . LEU B 1 126 ? 23.525 21.787  0.083   1.00 9.03  ? 126 LEU F CG  1 
ATOM   2096 C  CD1 . LEU B 1 126 ? 24.231 21.549  -1.235  1.00 10.22 ? 126 LEU F CD1 1 
ATOM   2097 C  CD2 . LEU B 1 126 ? 23.303 20.447  0.778   1.00 8.90  ? 126 LEU F CD2 1 
ATOM   2098 N  N   . GLY B 1 127 ? 23.766 24.864  3.977   1.00 8.31  ? 127 GLY F N   1 
ATOM   2099 C  CA  . GLY B 1 127 ? 24.347 25.973  4.719   1.00 8.90  ? 127 GLY F CA  1 
ATOM   2100 C  C   . GLY B 1 127 ? 24.408 27.286  3.954   1.00 10.11 ? 127 GLY F C   1 
ATOM   2101 O  O   . GLY B 1 127 ? 25.072 28.216  4.408   1.00 13.33 ? 127 GLY F O   1 
ATOM   2102 N  N   . LYS B 1 128 ? 23.692 27.375  2.829   1.00 9.86  ? 128 LYS F N   1 
ATOM   2103 C  CA  . LYS B 1 128 ? 23.693 28.554  1.945   1.00 13.84 ? 128 LYS F CA  1 
ATOM   2104 C  C   . LYS B 1 128 ? 22.259 29.084  1.761   1.00 14.06 ? 128 LYS F C   1 
ATOM   2105 O  O   . LYS B 1 128 ? 21.864 29.458  0.655   1.00 16.83 ? 128 LYS F O   1 
ATOM   2106 C  CB  . LYS B 1 128 ? 24.284 28.189  0.568   1.00 16.77 ? 128 LYS F CB  1 
ATOM   2107 C  CG  . LYS B 1 128 ? 25.630 27.479  0.576   1.00 18.82 ? 128 LYS F CG  1 
ATOM   2108 C  CD  . LYS B 1 128 ? 26.771 28.379  1.027   1.00 21.46 ? 128 LYS F CD  1 
ATOM   2109 C  CE  . LYS B 1 128 ? 28.126 27.819  0.616   0.10 22.73 ? 128 LYS F CE  1 
ATOM   2110 N  NZ  . LYS B 1 128 ? 29.194 28.854  0.653   0.10 22.77 ? 128 LYS F NZ  1 
ATOM   2111 N  N   . GLY B 1 129 ? 21.483 29.104  2.845   1.00 12.90 ? 129 GLY F N   1 
ATOM   2112 C  CA  . GLY B 1 129 ? 20.105 29.607  2.828   1.00 12.63 ? 129 GLY F CA  1 
ATOM   2113 C  C   . GLY B 1 129 ? 19.947 31.057  3.258   1.00 12.47 ? 129 GLY F C   1 
ATOM   2114 O  O   . GLY B 1 129 ? 18.895 31.654  3.038   1.00 15.02 ? 129 GLY F O   1 
ATOM   2115 N  N   . GLY B 1 130 ? 20.978 31.606  3.896   1.00 12.17 ? 130 GLY F N   1 
ATOM   2116 C  CA  . GLY B 1 130 ? 20.973 32.997  4.350   1.00 12.01 ? 130 GLY F CA  1 
ATOM   2117 C  C   . GLY B 1 130 ? 20.229 33.284  5.649   1.00 14.74 ? 130 GLY F C   1 
ATOM   2118 O  O   . GLY B 1 130 ? 19.809 34.422  5.874   1.00 15.67 ? 130 GLY F O   1 
ATOM   2119 N  N   . ASN B 1 131 ? 20.049 32.268  6.496   1.00 16.76 ? 131 ASN F N   1 
ATOM   2120 C  CA  . ASN B 1 131 ? 19.521 32.454  7.858   1.00 17.65 ? 131 ASN F CA  1 
ATOM   2121 C  C   . ASN B 1 131 ? 20.277 31.581  8.865   1.00 15.35 ? 131 ASN F C   1 
ATOM   2122 O  O   . ASN B 1 131 ? 21.091 30.746  8.471   1.00 16.68 ? 131 ASN F O   1 
ATOM   2123 C  CB  . ASN B 1 131 ? 17.998 32.218  7.913   1.00 19.32 ? 131 ASN F CB  1 
ATOM   2124 C  CG  . ASN B 1 131 ? 17.587 30.775  7.642   1.00 17.75 ? 131 ASN F CG  1 
ATOM   2125 O  OD1 . ASN B 1 131 ? 18.413 29.870  7.518   1.00 17.43 ? 131 ASN F OD1 1 
ATOM   2126 N  ND2 . ASN B 1 131 ? 16.278 30.560  7.552   1.00 20.92 ? 131 ASN F ND2 1 
ATOM   2127 N  N   . GLU B 1 132 ? 20.003 31.772  10.155  1.00 14.97 ? 132 GLU F N   1 
ATOM   2128 C  CA  . GLU B 1 132 ? 20.692 31.013  11.218  1.00 12.87 ? 132 GLU F CA  1 
ATOM   2129 C  C   . GLU B 1 132 ? 20.442 29.504  11.122  1.00 14.79 ? 132 GLU F C   1 
ATOM   2130 O  O   . GLU B 1 132 ? 21.364 28.699  11.324  1.00 16.17 ? 132 GLU F O   1 
ATOM   2131 C  CB  . GLU B 1 132 ? 20.294 31.514  12.612  1.00 17.29 ? 132 GLU F CB  1 
ATOM   2132 C  CG  . GLU B 1 132 ? 21.231 31.276  13.699  0.00 29.95 ? 132 GLU F CG  1 
ATOM   2133 C  CD  . GLU B 1 132 ? 20.623 31.395  15.083  0.00 28.06 ? 132 GLU F CD  1 
ATOM   2134 O  OE1 . GLU B 1 132 ? 19.717 32.234  15.266  0.00 39.25 ? 132 GLU F OE1 1 
ATOM   2135 O  OE2 . GLU B 1 132 ? 21.052 30.648  15.989  0.00 16.55 ? 132 GLU F OE2 1 
ATOM   2136 N  N   . GLU B 1 133 ? 19.207 29.135  10.788  1.00 13.24 ? 133 GLU F N   1 
ATOM   2137 C  CA  . GLU B 1 133 ? 18.823 27.729  10.683  1.00 13.89 ? 133 GLU F CA  1 
ATOM   2138 C  C   . GLU B 1 133 ? 19.615 27.016  9.588   1.00 12.04 ? 133 GLU F C   1 
ATOM   2139 O  O   . GLU B 1 133 ? 19.933 25.835  9.725   1.00 11.95 ? 133 GLU F O   1 
ATOM   2140 C  CB  . GLU B 1 133 ? 17.315 27.586  10.440  1.00 12.84 ? 133 GLU F CB  1 
ATOM   2141 C  CG  . GLU B 1 133 ? 16.801 26.155  10.590  0.70 13.99 ? 133 GLU F CG  1 
ATOM   2142 C  CD  . GLU B 1 133 ? 15.288 26.031  10.462  0.70 15.89 ? 133 GLU F CD  1 
ATOM   2143 O  OE1 . GLU B 1 133 ? 14.567 26.999  10.783  0.70 18.53 ? 133 GLU F OE1 1 
ATOM   2144 O  OE2 . GLU B 1 133 ? 14.815 24.954  10.030  0.70 20.83 ? 133 GLU F OE2 1 
ATOM   2145 N  N   . SER B 1 134 ? 19.951 27.738  8.515   1.00 12.47 ? 134 SER F N   1 
ATOM   2146 C  CA  . SER B 1 134 ? 20.713 27.165  7.407   1.00 10.39 ? 134 SER F CA  1 
ATOM   2147 C  C   . SER B 1 134 ? 22.002 26.477  7.850   1.00 11.46 ? 134 SER F C   1 
ATOM   2148 O  O   . SER B 1 134 ? 22.314 25.407  7.354   1.00 9.36  ? 134 SER F O   1 
ATOM   2149 C  CB  . SER B 1 134 ? 21.034 28.229  6.354   1.00 9.53  ? 134 SER F CB  1 
ATOM   2150 O  OG  . SER B 1 134 ? 21.759 27.646  5.292   1.00 10.04 ? 134 SER F OG  1 
ATOM   2151 N  N   . THR B 1 135 ? 22.724 27.060  8.806   1.00 16.77 ? 135 THR F N   1 
ATOM   2152 C  CA  . THR B 1 135 ? 23.997 26.491  9.249   1.00 15.90 ? 135 THR F CA  1 
ATOM   2153 C  C   . THR B 1 135 ? 23.858 25.556  10.457  1.00 13.83 ? 135 THR F C   1 
ATOM   2154 O  O   . THR B 1 135 ? 24.859 25.151  11.054  1.00 13.26 ? 135 THR F O   1 
ATOM   2155 C  CB  . THR B 1 135 ? 25.030 27.600  9.509   1.00 20.94 ? 135 THR F CB  1 
ATOM   2156 O  OG1 . THR B 1 135 ? 24.549 28.472  10.533  1.00 25.65 ? 135 THR F OG1 1 
ATOM   2157 C  CG2 . THR B 1 135 ? 25.269 28.393  8.219   1.00 25.45 ? 135 THR F CG2 1 
ATOM   2158 N  N   . LYS B 1 136 ? 22.625 25.180  10.782  1.00 12.94 ? 136 LYS F N   1 
ATOM   2159 C  CA  . LYS B 1 136 ? 22.360 24.142  11.773  1.00 13.82 ? 136 LYS F CA  1 
ATOM   2160 C  C   . LYS B 1 136 ? 21.683 22.933  11.135  1.00 12.37 ? 136 LYS F C   1 
ATOM   2161 O  O   . LYS B 1 136 ? 22.156 21.812  11.301  1.00 12.83 ? 136 LYS F O   1 
ATOM   2162 C  CB  . LYS B 1 136 ? 21.534 24.716  12.919  1.00 17.12 ? 136 LYS F CB  1 
ATOM   2163 C  CG  . LYS B 1 136 ? 22.264 25.839  13.634  1.00 20.76 ? 136 LYS F CG  1 
ATOM   2164 C  CD  . LYS B 1 136 ? 21.626 26.170  14.970  1.00 25.47 ? 136 LYS F CD  1 
ATOM   2165 C  CE  . LYS B 1 136 ? 22.416 27.250  15.689  1.00 32.14 ? 136 LYS F CE  1 
ATOM   2166 N  NZ  . LYS B 1 136 ? 21.815 27.588  17.008  1.00 37.43 ? 136 LYS F NZ  1 
ATOM   2167 N  N   . THR B 1 137 ? 20.586 23.153  10.410  1.00 11.74 ? 137 THR F N   1 
ATOM   2168 C  CA  . THR B 1 137 ? 19.817 22.054  9.813   1.00 12.00 ? 137 THR F CA  1 
ATOM   2169 C  C   . THR B 1 137 ? 19.746 22.036  8.288   1.00 10.26 ? 137 THR F C   1 
ATOM   2170 O  O   . THR B 1 137 ? 19.412 21.005  7.708   1.00 10.97 ? 137 THR F O   1 
ATOM   2171 C  CB  . THR B 1 137 ? 18.353 22.043  10.304  1.00 14.10 ? 137 THR F CB  1 
ATOM   2172 O  OG1 . THR B 1 137 ? 17.646 23.155  9.744   1.00 14.49 ? 137 THR F OG1 1 
ATOM   2173 C  CG2 . THR B 1 137 ? 18.273 22.059  11.824  1.00 14.39 ? 137 THR F CG2 1 
ATOM   2174 N  N   . GLY B 1 138 ? 19.986 23.176  7.650   1.00 9.78  ? 138 GLY F N   1 
ATOM   2175 C  CA  . GLY B 1 138 ? 19.812 23.290  6.215   1.00 8.25  ? 138 GLY F CA  1 
ATOM   2176 C  C   . GLY B 1 138 ? 18.389 23.483  5.725   1.00 9.97  ? 138 GLY F C   1 
ATOM   2177 O  O   . GLY B 1 138 ? 18.155 23.463  4.517   1.00 10.17 ? 138 GLY F O   1 
ATOM   2178 N  N   . ASN B 1 139 ? 17.440 23.684  6.637   1.00 10.34 ? 139 ASN F N   1 
ATOM   2179 C  CA  . ASN B 1 139 ? 16.070 24.072  6.287   1.00 10.95 ? 139 ASN F CA  1 
ATOM   2180 C  C   . ASN B 1 139 ? 15.353 23.075  5.369   1.00 10.63 ? 139 ASN F C   1 
ATOM   2181 O  O   . ASN B 1 139 ? 14.617 23.484  4.479   1.00 11.83 ? 139 ASN F O   1 
ATOM   2182 C  CB  . ASN B 1 139 ? 16.062 25.482  5.648   1.00 9.78  ? 139 ASN F CB  1 
ATOM   2183 C  CG  . ASN B 1 139 ? 16.405 26.577  6.637   1.00 12.28 ? 139 ASN F CG  1 
ATOM   2184 O  OD1 . ASN B 1 139 ? 15.642 26.835  7.563   1.00 15.47 ? 139 ASN F OD1 1 
ATOM   2185 N  ND2 . ASN B 1 139 ? 17.543 27.239  6.435   1.00 12.84 ? 139 ASN F ND2 1 
ATOM   2186 N  N   . ALA B 1 140 ? 15.548 21.773  5.596   1.00 10.59 ? 140 ALA F N   1 
ATOM   2187 C  CA  . ALA B 1 140 ? 14.960 20.744  4.724   1.00 12.02 ? 140 ALA F CA  1 
ATOM   2188 C  C   . ALA B 1 140 ? 13.530 20.305  5.092   1.00 12.75 ? 140 ALA F C   1 
ATOM   2189 O  O   . ALA B 1 140 ? 12.992 19.372  4.486   1.00 12.08 ? 140 ALA F O   1 
ATOM   2190 C  CB  . ALA B 1 140 ? 15.884 19.535  4.638   1.00 11.85 ? 140 ALA F CB  1 
ATOM   2191 N  N   . GLY B 1 141 ? 12.912 20.972  6.061   1.00 15.73 ? 141 GLY F N   1 
ATOM   2192 C  CA  . GLY B 1 141 ? 11.539 20.682  6.433   1.00 16.59 ? 141 GLY F CA  1 
ATOM   2193 C  C   . GLY B 1 141 ? 11.378 19.333  7.111   1.00 12.48 ? 141 GLY F C   1 
ATOM   2194 O  O   . GLY B 1 141 ? 12.321 18.792  7.704   1.00 11.99 ? 141 GLY F O   1 
ATOM   2195 N  N   . SER B 1 142 ? 10.178 18.784  6.978   1.00 11.16 ? 142 SER F N   1 
ATOM   2196 C  CA  . SER B 1 142 ? 9.764  17.606  7.740   1.00 14.49 ? 142 SER F CA  1 
ATOM   2197 C  C   . SER B 1 142 ? 10.540 16.344  7.355   1.00 12.04 ? 142 SER F C   1 
ATOM   2198 O  O   . SER B 1 142 ? 11.123 16.259  6.265   1.00 11.06 ? 142 SER F O   1 
ATOM   2199 C  CB  . SER B 1 142 ? 8.249  17.381  7.598   1.00 20.26 ? 142 SER F CB  1 
ATOM   2200 O  OG  . SER B 1 142 ? 7.893  16.893  6.319   0.70 14.63 ? 142 SER F OG  1 
ATOM   2201 N  N   . ARG B 1 143 ? 10.559 15.391  8.282   1.00 10.66 ? 143 ARG F N   1 
ATOM   2202 C  CA  . ARG B 1 143 ? 11.207 14.086  8.088   1.00 9.54  ? 143 ARG F CA  1 
ATOM   2203 C  C   . ARG B 1 143 ? 10.204 13.132  7.453   1.00 9.75  ? 143 ARG F C   1 
ATOM   2204 O  O   . ARG B 1 143 ? 9.286  12.656  8.113   1.00 11.25 ? 143 ARG F O   1 
ATOM   2205 C  CB  . ARG B 1 143 ? 11.721 13.541  9.425   1.00 10.31 ? 143 ARG F CB  1 
ATOM   2206 C  CG  . ARG B 1 143 ? 12.686 14.487  10.111  1.00 10.24 ? 143 ARG F CG  1 
ATOM   2207 C  CD  . ARG B 1 143 ? 13.144 14.037  11.485  1.00 10.92 ? 143 ARG F CD  1 
ATOM   2208 N  NE  . ARG B 1 143 ? 14.025 15.053  12.054  1.00 11.96 ? 143 ARG F NE  1 
ATOM   2209 C  CZ  . ARG B 1 143 ? 14.647 14.977  13.226  1.00 11.58 ? 143 ARG F CZ  1 
ATOM   2210 N  NH1 . ARG B 1 143 ? 14.507 13.910  14.018  1.00 12.13 ? 143 ARG F NH1 1 
ATOM   2211 N  NH2 . ARG B 1 143 ? 15.424 15.985  13.613  1.00 12.42 ? 143 ARG F NH2 1 
ATOM   2212 N  N   . LEU B 1 144 ? 10.371 12.872  6.159   1.00 9.22  ? 144 LEU F N   1 
ATOM   2213 C  CA  . LEU B 1 144 ? 9.356  12.127  5.408   1.00 9.66  ? 144 LEU F CA  1 
ATOM   2214 C  C   . LEU B 1 144 ? 9.443  10.648  5.690   1.00 9.42  ? 144 LEU F C   1 
ATOM   2215 O  O   . LEU B 1 144 ? 8.422  9.973   5.769   1.00 10.74 ? 144 LEU F O   1 
ATOM   2216 C  CB  . LEU B 1 144 ? 9.488  12.345  3.902   1.00 11.74 ? 144 LEU F CB  1 
ATOM   2217 C  CG  . LEU B 1 144 ? 9.214  13.748  3.370   1.00 14.20 ? 144 LEU F CG  1 
ATOM   2218 C  CD1 . LEU B 1 144 ? 9.311  13.723  1.850   1.00 16.76 ? 144 LEU F CD1 1 
ATOM   2219 C  CD2 . LEU B 1 144 ? 7.855  14.272  3.816   1.00 16.03 ? 144 LEU F CD2 1 
ATOM   2220 N  N   . ALA B 1 145 ? 10.673 10.162  5.803   1.00 9.07  ? 145 ALA F N   1 
ATOM   2221 C  CA  . ALA B 1 145 ? 10.939 8.754   6.050   1.00 8.92  ? 145 ALA F CA  1 
ATOM   2222 C  C   . ALA B 1 145 ? 12.321 8.577   6.649   1.00 7.87  ? 145 ALA F C   1 
ATOM   2223 O  O   . ALA B 1 145 ? 13.219 9.399   6.455   1.00 7.66  ? 145 ALA F O   1 
ATOM   2224 C  CB  . ALA B 1 145 ? 10.825 7.959   4.756   1.00 9.65  ? 145 ALA F CB  1 
ATOM   2225 N  N   . CYS B 1 146 ? 12.469 7.494   7.397   1.00 7.25  ? 146 CYS F N   1 
ATOM   2226 C  CA  . CYS B 1 146 ? 13.708 7.206   8.078   1.00 7.02  ? 146 CYS F CA  1 
ATOM   2227 C  C   . CYS B 1 146 ? 13.804 5.741   8.429   1.00 6.61  ? 146 CYS F C   1 
ATOM   2228 O  O   . CYS B 1 146 ? 12.831 5.011   8.331   1.00 7.57  ? 146 CYS F O   1 
ATOM   2229 C  CB  . CYS B 1 146 ? 13.811 8.028   9.355   1.00 8.30  ? 146 CYS F CB  1 
ATOM   2230 S  SG  . CYS B 1 146 ? 12.492 7.687   10.541  1.00 10.47 ? 146 CYS F SG  1 
ATOM   2231 N  N   . GLY B 1 147 ? 14.994 5.340   8.835   1.00 6.21  ? 147 GLY F N   1 
ATOM   2232 C  CA  . GLY B 1 147 ? 15.224 3.996   9.359   1.00 7.02  ? 147 GLY F CA  1 
ATOM   2233 C  C   . GLY B 1 147 ? 16.551 3.924   10.056  1.00 6.99  ? 147 GLY F C   1 
ATOM   2234 O  O   . GLY B 1 147 ? 17.386 4.810   9.915   1.00 7.43  ? 147 GLY F O   1 
ATOM   2235 N  N   . VAL B 1 148 ? 16.750 2.856   10.815  1.00 6.96  ? 148 VAL F N   1 
ATOM   2236 C  CA  . VAL B 1 148 ? 17.988 2.661   11.545  1.00 7.91  ? 148 VAL F CA  1 
ATOM   2237 C  C   . VAL B 1 148 ? 18.971 1.950   10.627  1.00 7.27  ? 148 VAL F C   1 
ATOM   2238 O  O   . VAL B 1 148 ? 18.601 0.986   9.940   1.00 8.40  ? 148 VAL F O   1 
ATOM   2239 C  CB  . VAL B 1 148 ? 17.753 1.862   12.842  1.00 8.32  ? 148 VAL F CB  1 
ATOM   2240 C  CG1 . VAL B 1 148 ? 19.036 1.744   13.650  1.00 9.23  ? 148 VAL F CG1 1 
ATOM   2241 C  CG2 . VAL B 1 148 ? 16.659 2.515   13.682  1.00 8.58  ? 148 VAL F CG2 1 
ATOM   2242 N  N   . ILE B 1 149 ? 20.219 2.409   10.630  1.00 6.04  ? 149 ILE F N   1 
ATOM   2243 C  CA  . ILE B 1 149 ? 21.267 1.840   9.779   1.00 6.73  ? 149 ILE F CA  1 
ATOM   2244 C  C   . ILE B 1 149 ? 21.834 0.592   10.456  1.00 6.59  ? 149 ILE F C   1 
ATOM   2245 O  O   . ILE B 1 149 ? 22.382 0.663   11.557  1.00 7.09  ? 149 ILE F O   1 
ATOM   2246 C  CB  . ILE B 1 149 ? 22.388 2.872   9.511   1.00 7.08  ? 149 ILE F CB  1 
ATOM   2247 C  CG1 . ILE B 1 149 ? 21.820 4.090   8.776   1.00 7.28  ? 149 ILE F CG1 1 
ATOM   2248 C  CG2 . ILE B 1 149 ? 23.518 2.257   8.691   1.00 7.28  ? 149 ILE F CG2 1 
ATOM   2249 C  CD1 . ILE B 1 149 ? 22.744 5.292   8.716   1.00 7.71  ? 149 ILE F CD1 1 
ATOM   2250 N  N   . GLY B 1 150 ? 21.715 -0.550  9.782   1.00 6.17  ? 150 GLY F N   1 
ATOM   2251 C  CA  . GLY B 1 150 ? 22.153 -1.816  10.355  1.00 6.07  ? 150 GLY F CA  1 
ATOM   2252 C  C   . GLY B 1 150 ? 23.300 -2.457  9.613   1.00 6.86  ? 150 GLY F C   1 
ATOM   2253 O  O   . GLY B 1 150 ? 23.533 -2.178  8.435   1.00 7.09  ? 150 GLY F O   1 
ATOM   2254 N  N   . ILE B 1 151 ? 24.001 -3.346  10.314  1.00 7.21  ? 151 ILE F N   1 
ATOM   2255 C  CA  . ILE B 1 151 ? 25.072 -4.143  9.728   1.00 8.04  ? 151 ILE F CA  1 
ATOM   2256 C  C   . ILE B 1 151 ? 24.448 -5.121  8.727   1.00 7.52  ? 151 ILE F C   1 
ATOM   2257 O  O   . ILE B 1 151 ? 23.453 -5.775  9.025   1.00 7.76  ? 151 ILE F O   1 
ATOM   2258 C  CB  . ILE B 1 151 ? 25.830 -4.953  10.809  1.00 8.21  ? 151 ILE F CB  1 
ATOM   2259 C  CG1 . ILE B 1 151 ? 26.570 -4.011  11.762  1.00 8.51  ? 151 ILE F CG1 1 
ATOM   2260 C  CG2 . ILE B 1 151 ? 26.820 -5.935  10.180  1.00 8.76  ? 151 ILE F CG2 1 
ATOM   2261 C  CD1 . ILE B 1 151 ? 27.051 -4.666  13.041  1.00 11.13 ? 151 ILE F CD1 1 
ATOM   2262 N  N   . ALA B 1 152 ? 25.058 -5.205  7.548   1.00 8.30  ? 152 ALA F N   1 
ATOM   2263 C  CA  . ALA B 1 152 ? 24.643 -6.110  6.481   1.00 9.96  ? 152 ALA F CA  1 
ATOM   2264 C  C   . ALA B 1 152 ? 25.709 -7.181  6.264   1.00 10.66 ? 152 ALA F C   1 
ATOM   2265 O  O   . ALA B 1 152 ? 26.867 -7.030  6.660   1.00 10.39 ? 152 ALA F O   1 
ATOM   2266 C  CB  . ALA B 1 152 ? 24.424 -5.329  5.193   1.00 10.89 ? 152 ALA F CB  1 
ATOM   2267 N  N   . GLN B 1 153 ? 25.305 -8.265  5.615   1.00 11.53 ? 153 GLN F N   1 
ATOM   2268 C  CA  . GLN B 1 153 ? 26.220 -9.355  5.321   1.00 12.89 ? 153 GLN F CA  1 
ATOM   2269 C  C   . GLN B 1 153 ? 27.282 -8.963  4.305   1.00 15.56 ? 153 GLN F C   1 
ATOM   2270 O  O   . GLN B 1 153 ? 27.013 -8.278  3.313   1.00 17.31 ? 153 GLN F O   1 
ATOM   2271 C  CB  . GLN B 1 153 ? 25.433 -10.536 4.800   1.00 12.87 ? 153 GLN F CB  1 
ATOM   2272 C  CG  . GLN B 1 153 ? 26.233 -11.803 4.575   1.00 14.29 ? 153 GLN F CG  1 
ATOM   2273 C  CD  . GLN B 1 153 ? 25.322 -12.919 4.134   1.00 13.15 ? 153 GLN F CD  1 
ATOM   2274 O  OE1 . GLN B 1 153 ? 24.226 -13.089 4.679   1.00 18.50 ? 153 GLN F OE1 1 
ATOM   2275 N  NE2 . GLN B 1 153 ? 25.749 -13.677 3.145   1.00 19.80 ? 153 GLN F NE2 1 
ATOM   2276 O  OXT . GLN B 1 153 ? 28.436 -9.353  4.472   1.00 17.54 ? 153 GLN F OXT 1 
HETATM 2277 ZN ZN  . ZN  C 2 .   ? 21.272 -18.981 19.500  1.00 8.12  ? 501 ZN  A ZN  1 
HETATM 2278 ZN ZN  . ZN  D 2 .   ? 15.607 -16.071 16.311  0.80 7.43  ? 502 ZN  A ZN  1 
HETATM 2279 C  C11 . 9JT E 3 .   ? 34.106 -1.646  18.132  0.70 20.77 ? 503 9JT A C11 1 
HETATM 2280 C  C12 . 9JT E 3 .   ? 34.487 -0.659  19.065  0.70 20.98 ? 503 9JT A C12 1 
HETATM 2281 C  C13 . 9JT E 3 .   ? 35.824 -0.522  19.433  0.70 21.95 ? 503 9JT A C13 1 
HETATM 2282 C  C14 . 9JT E 3 .   ? 36.790 -1.357  18.880  0.70 21.58 ? 503 9JT A C14 1 
HETATM 2283 C  C15 . 9JT E 3 .   ? 36.426 -2.329  17.955  0.70 21.95 ? 503 9JT A C15 1 
HETATM 2284 O  O09 . 9JT E 3 .   ? 31.653 -0.374  18.846  0.70 16.29 ? 503 9JT A O09 1 
HETATM 2285 C  C08 . 9JT E 3 .   ? 31.718 -1.228  17.986  0.70 16.02 ? 503 9JT A C08 1 
HETATM 2286 C  C07 . 9JT E 3 .   ? 30.496 -1.502  17.150  0.70 14.33 ? 503 9JT A C07 1 
HETATM 2287 C  C06 . 9JT E 3 .   ? 30.692 -1.704  15.764  0.70 12.16 ? 503 9JT A C06 1 
HETATM 2288 C  C05 . 9JT E 3 .   ? 29.624 -1.961  14.912  0.70 11.76 ? 503 9JT A C05 1 
HETATM 2289 C  C04 . 9JT E 3 .   ? 28.340 -2.002  15.439  0.70 12.18 ? 503 9JT A C04 1 
HETATM 2290 C  C03 . 9JT E 3 .   ? 28.139 -1.788  16.805  0.70 13.36 ? 503 9JT A C03 1 
HETATM 2291 C  C02 . 9JT E 3 .   ? 29.196 -1.524  17.680  0.70 15.34 ? 503 9JT A C02 1 
HETATM 2292 SE SE1 . 9JT E 3 .   ? 28.846 -1.300  19.219  0.70 20.15 ? 503 9JT A SE1 1 
HETATM 2293 N  N10 . 9JT E 3 .   ? 32.840 -1.896  17.687  0.70 17.61 ? 503 9JT A N10 1 
HETATM 2294 C  C16 . 9JT E 3 .   ? 35.097 -2.468  17.586  0.70 20.91 ? 503 9JT A C16 1 
HETATM 2295 S  S   . SO4 F 4 .   ? 15.627 -18.482 14.195  0.80 8.29  ? 504 SO4 A S   1 
HETATM 2296 O  O1  . SO4 F 4 .   ? 16.930 -18.774 13.558  0.80 9.33  ? 504 SO4 A O1  1 
HETATM 2297 O  O2  . SO4 F 4 .   ? 14.875 -17.562 13.352  0.80 8.37  ? 504 SO4 A O2  1 
HETATM 2298 O  O3  . SO4 F 4 .   ? 14.807 -19.703 14.370  0.80 10.08 ? 504 SO4 A O3  1 
HETATM 2299 O  O4  . SO4 F 4 .   ? 15.877 -17.909 15.543  0.80 7.41  ? 504 SO4 A O4  1 
HETATM 2300 ZN ZN  . ZN  G 2 .   ? 24.029 19.001  9.192   1.00 8.15  ? 501 ZN  F ZN  1 
HETATM 2301 ZN ZN  . ZN  H 2 .   ? 17.539 15.966  8.790   0.80 8.15  ? 502 ZN  F ZN  1 
HETATM 2302 C  C11 . 9JT I 3 .   ? 33.432 3.760   17.786  0.70 16.71 ? 503 9JT F C11 1 
HETATM 2303 C  C12 . 9JT I 3 .   ? 34.587 2.956   17.699  0.70 17.10 ? 503 9JT F C12 1 
HETATM 2304 C  C13 . 9JT I 3 .   ? 35.819 3.404   18.170  0.70 17.15 ? 503 9JT F C13 1 
HETATM 2305 C  C14 . 9JT I 3 .   ? 35.927 4.668   18.739  0.70 17.39 ? 503 9JT F C14 1 
HETATM 2306 C  C15 . 9JT I 3 .   ? 34.797 5.473   18.841  0.70 16.90 ? 503 9JT F C15 1 
HETATM 2307 O  O09 . 9JT I 3 .   ? 32.573 1.337   16.484  0.70 16.17 ? 503 9JT F O09 1 
HETATM 2308 C  C08 . 9JT I 3 .   ? 31.822 2.243   16.774  0.70 15.29 ? 503 9JT F C08 1 
HETATM 2309 C  C07 . 9JT I 3 .   ? 30.368 1.976   16.562  0.70 15.64 ? 503 9JT F C07 1 
HETATM 2310 C  C06 . 9JT I 3 .   ? 29.593 2.107   17.728  0.70 13.79 ? 503 9JT F C06 1 
HETATM 2311 C  C05 . 9JT I 3 .   ? 28.226 1.888   17.705  0.70 13.35 ? 503 9JT F C05 1 
HETATM 2312 C  C04 . 9JT I 3 .   ? 27.641 1.515   16.503  0.70 13.85 ? 503 9JT F C04 1 
HETATM 2313 C  C03 . 9JT I 3 .   ? 28.408 1.369   15.344  0.70 14.66 ? 503 9JT F C03 1 
HETATM 2314 C  C02 . 9JT I 3 .   ? 29.789 1.584   15.333  0.70 17.06 ? 503 9JT F C02 1 
HETATM 2315 SE SE1 . 9JT I 3 .   ? 30.566 1.396   13.933  0.70 18.25 ? 503 9JT F SE1 1 
HETATM 2316 N  N10 . 9JT I 3 .   ? 32.183 3.408   17.346  0.70 15.13 ? 503 9JT F N10 1 
HETATM 2317 C  C16 . 9JT I 3 .   ? 33.562 5.028   18.372  0.70 16.51 ? 503 9JT F C16 1 
HETATM 2318 S  S   . SO4 J 4 .   ? 16.424 18.311  10.562  0.80 9.73  ? 504 SO4 F S   1 
HETATM 2319 O  O1  . SO4 J 4 .   ? 17.399 17.756  9.598   0.80 9.33  ? 504 SO4 F O1  1 
HETATM 2320 O  O2  . SO4 J 4 .   ? 15.825 19.517  9.943   0.80 10.62 ? 504 SO4 F O2  1 
HETATM 2321 O  O3  . SO4 J 4 .   ? 17.173 18.689  11.774  0.80 10.99 ? 504 SO4 F O3  1 
HETATM 2322 O  O4  . SO4 J 4 .   ? 15.334 17.382  10.933  0.80 9.70  ? 504 SO4 F O4  1 
HETATM 2323 O  O   . HOH K 5 .   ? 35.658 -11.294 22.395  1.00 24.30 ? 601 HOH A O   1 
HETATM 2324 O  O   . HOH K 5 .   ? 18.778 -18.690 11.935  1.00 28.41 ? 602 HOH A O   1 
HETATM 2325 O  O   . HOH K 5 .   ? 31.227 -25.472 31.729  1.00 32.94 ? 603 HOH A O   1 
HETATM 2326 O  O   . HOH K 5 .   ? 36.300 -8.218  23.224  1.00 14.31 ? 604 HOH A O   1 
HETATM 2327 O  O   . HOH K 5 .   ? 29.076 -25.424 28.748  1.00 18.63 ? 605 HOH A O   1 
HETATM 2328 O  O   . HOH K 5 .   ? 33.771 -11.032 15.516  1.00 35.27 ? 606 HOH A O   1 
HETATM 2329 O  O   . HOH K 5 .   ? 18.066 7.468   25.638  1.00 28.61 ? 607 HOH A O   1 
HETATM 2330 O  O   . HOH K 5 .   ? 34.254 -17.059 16.111  1.00 30.36 ? 608 HOH A O   1 
HETATM 2331 O  O   . HOH K 5 .   ? 33.979 -20.573 30.030  1.00 37.00 ? 609 HOH A O   1 
HETATM 2332 O  O   . HOH K 5 .   ? 2.042  -19.048 22.994  1.00 34.31 ? 610 HOH A O   1 
HETATM 2333 O  O   . HOH K 5 .   ? 17.400 -14.780 8.136   1.00 21.48 ? 611 HOH A O   1 
HETATM 2334 O  O   . HOH K 5 .   ? 24.026 -21.654 34.496  1.00 31.76 ? 612 HOH A O   1 
HETATM 2335 O  O   . HOH K 5 .   ? 31.784 1.496   20.625  1.00 31.69 ? 613 HOH A O   1 
HETATM 2336 O  O   . HOH K 5 .   ? 10.105 -4.058  32.189  1.00 25.86 ? 614 HOH A O   1 
HETATM 2337 O  O   . HOH K 5 .   ? 31.063 -24.695 20.810  1.00 31.44 ? 615 HOH A O   1 
HETATM 2338 O  O   . HOH K 5 .   ? 9.544  -9.406  33.406  1.00 32.13 ? 616 HOH A O   1 
HETATM 2339 O  O   . HOH K 5 .   ? 33.470 -3.689  33.391  1.00 74.56 ? 617 HOH A O   1 
HETATM 2340 O  O   . HOH K 5 .   ? 19.651 -24.375 28.427  1.00 19.74 ? 618 HOH A O   1 
HETATM 2341 O  O   . HOH K 5 .   ? 29.383 0.191   26.491  1.00 34.34 ? 619 HOH A O   1 
HETATM 2342 O  O   . HOH K 5 .   ? 22.005 -28.574 25.276  1.00 36.95 ? 620 HOH A O   1 
HETATM 2343 O  O   . HOH K 5 .   ? 6.025  -10.486 31.248  1.00 26.20 ? 621 HOH A O   1 
HETATM 2344 O  O   . HOH K 5 .   ? 11.340 -3.427  6.712   1.00 27.02 ? 622 HOH A O   1 
HETATM 2345 O  O   . HOH K 5 .   ? 5.266  -10.802 11.565  1.00 29.51 ? 623 HOH A O   1 
HETATM 2346 O  O   . HOH K 5 .   ? 27.401 -4.898  16.426  1.00 26.66 ? 624 HOH A O   1 
HETATM 2347 O  O   . HOH K 5 .   ? 10.495 -14.535 30.812  1.00 33.16 ? 625 HOH A O   1 
HETATM 2348 O  O   . HOH K 5 .   ? 7.981  -16.902 32.690  1.00 21.00 ? 626 HOH A O   1 
HETATM 2349 O  O   . HOH K 5 .   ? 31.166 -1.801  26.788  1.00 43.03 ? 627 HOH A O   1 
HETATM 2350 O  O   . HOH K 5 .   ? 35.003 -19.257 21.006  1.00 29.40 ? 628 HOH A O   1 
HETATM 2351 O  O   . HOH K 5 .   ? 14.459 -20.314 17.103  1.00 11.88 ? 629 HOH A O   1 
HETATM 2352 O  O   . HOH K 5 .   ? 11.689 -27.567 21.074  1.00 22.50 ? 630 HOH A O   1 
HETATM 2353 O  O   . HOH K 5 .   ? 24.277 5.952   24.314  1.00 16.61 ? 631 HOH A O   1 
HETATM 2354 O  O   . HOH K 5 .   ? 16.642 3.255   25.296  1.00 22.26 ? 632 HOH A O   1 
HETATM 2355 O  O   . HOH K 5 .   ? 11.250 -1.439  13.643  1.00 16.46 ? 633 HOH A O   1 
HETATM 2356 O  O   . HOH K 5 .   ? 31.200 -8.730  16.314  1.00 27.53 ? 634 HOH A O   1 
HETATM 2357 O  O   . HOH K 5 .   ? 9.886  -24.664 21.011  1.00 22.10 ? 635 HOH A O   1 
HETATM 2358 O  O   . HOH K 5 .   ? -1.461 -7.087  30.901  1.00 24.37 ? 636 HOH A O   1 
HETATM 2359 O  O   . HOH K 5 .   ? 28.957 -16.749 22.791  1.00 10.06 ? 637 HOH A O   1 
HETATM 2360 O  O   . HOH K 5 .   ? 23.951 -24.976 24.611  1.00 27.41 ? 638 HOH A O   1 
HETATM 2361 O  O   . HOH K 5 .   ? 28.420 -7.218  28.968  1.00 31.99 ? 639 HOH A O   1 
HETATM 2362 O  O   . HOH K 5 .   ? -4.905 -7.478  33.252  1.00 30.69 ? 640 HOH A O   1 
HETATM 2363 O  O   . HOH K 5 .   ? 32.350 -6.457  23.333  1.00 13.25 ? 641 HOH A O   1 
HETATM 2364 O  O   . HOH K 5 .   ? 3.645  -5.470  13.981  1.00 17.96 ? 642 HOH A O   1 
HETATM 2365 O  O   . HOH K 5 .   ? 29.185 1.927   21.724  1.00 23.94 ? 643 HOH A O   1 
HETATM 2366 O  O   . HOH K 5 .   ? -1.460 -5.780  18.789  1.00 34.39 ? 644 HOH A O   1 
HETATM 2367 O  O   . HOH K 5 .   ? 12.824 -3.016  10.434  1.00 32.91 ? 645 HOH A O   1 
HETATM 2368 O  O   . HOH K 5 .   ? 12.699 -19.802 12.687  1.00 29.15 ? 646 HOH A O   1 
HETATM 2369 O  O   . HOH K 5 .   ? 28.831 -16.142 20.121  1.00 8.40  ? 647 HOH A O   1 
HETATM 2370 O  O   . HOH K 5 .   ? 7.667  -11.061 10.505  1.00 29.26 ? 648 HOH A O   1 
HETATM 2371 O  O   . HOH K 5 .   ? 19.607 -22.497 30.829  1.00 29.70 ? 649 HOH A O   1 
HETATM 2372 O  O   . HOH K 5 .   ? 2.302  -21.392 17.194  1.00 41.70 ? 650 HOH A O   1 
HETATM 2373 O  O   . HOH K 5 .   ? 29.680 -17.909 27.497  1.00 14.38 ? 651 HOH A O   1 
HETATM 2374 O  O   . HOH K 5 .   ? 23.637 -24.437 26.865  1.00 29.46 ? 652 HOH A O   1 
HETATM 2375 O  O   . HOH K 5 .   ? 11.869 -10.679 33.162  1.00 37.81 ? 653 HOH A O   1 
HETATM 2376 O  O   . HOH K 5 .   ? 15.847 -13.915 29.227  1.00 21.15 ? 654 HOH A O   1 
HETATM 2377 O  O   . HOH K 5 .   ? 0.552  -13.090 18.114  1.00 15.26 ? 655 HOH A O   1 
HETATM 2378 O  O   . HOH K 5 .   ? 14.529 0.108   16.067  1.00 7.79  ? 656 HOH A O   1 
HETATM 2379 O  O   . HOH K 5 .   ? 22.528 -8.370  4.924   1.00 18.78 ? 657 HOH A O   1 
HETATM 2380 O  O   . HOH K 5 .   ? 30.347 -8.118  31.024  1.00 33.12 ? 658 HOH A O   1 
HETATM 2381 O  O   . HOH K 5 .   ? 16.121 -8.591  1.511   1.00 21.19 ? 659 HOH A O   1 
HETATM 2382 O  O   . HOH K 5 .   ? -5.245 -7.631  25.736  1.00 27.20 ? 660 HOH A O   1 
HETATM 2383 O  O   . HOH K 5 .   ? 32.381 -4.105  25.574  1.00 26.43 ? 661 HOH A O   1 
HETATM 2384 O  O   . HOH K 5 .   ? -0.423 -16.262 32.681  1.00 14.24 ? 662 HOH A O   1 
HETATM 2385 O  O   . HOH K 5 .   ? 13.482 -12.740 29.801  1.00 19.62 ? 663 HOH A O   1 
HETATM 2386 O  O   . HOH K 5 .   ? 32.707 -18.211 24.273  1.00 28.43 ? 664 HOH A O   1 
HETATM 2387 O  O   . HOH K 5 .   ? 2.254  -14.594 19.578  1.00 12.78 ? 665 HOH A O   1 
HETATM 2388 O  O   . HOH K 5 .   ? 5.054  -6.094  34.879  1.00 38.61 ? 666 HOH A O   1 
HETATM 2389 O  O   . HOH K 5 .   ? 27.204 -2.039  32.951  1.00 21.34 ? 667 HOH A O   1 
HETATM 2390 O  O   . HOH K 5 .   ? 20.591 -12.828 30.822  1.00 12.23 ? 668 HOH A O   1 
HETATM 2391 O  O   . HOH K 5 .   ? 26.017 -16.988 30.129  1.00 13.26 ? 669 HOH A O   1 
HETATM 2392 O  O   . HOH K 5 .   ? 3.181  -8.887  31.289  1.00 23.75 ? 670 HOH A O   1 
HETATM 2393 O  O   . HOH K 5 .   ? 27.163 -14.110 13.970  1.00 14.62 ? 671 HOH A O   1 
HETATM 2394 O  O   . HOH K 5 .   ? 18.296 2.769   27.115  1.00 32.97 ? 672 HOH A O   1 
HETATM 2395 O  O   . HOH K 5 .   ? 19.262 -6.920  1.677   1.00 40.31 ? 673 HOH A O   1 
HETATM 2396 O  O   . HOH K 5 .   ? 23.982 10.713  24.004  1.00 30.46 ? 674 HOH A O   1 
HETATM 2397 O  O   . HOH K 5 .   ? 24.513 7.851   26.317  1.00 40.51 ? 675 HOH A O   1 
HETATM 2398 O  O   . HOH K 5 .   ? 36.607 -3.281  26.108  1.00 26.30 ? 676 HOH A O   1 
HETATM 2399 O  O   . HOH K 5 .   ? 35.679 -5.906  21.954  1.00 25.28 ? 677 HOH A O   1 
HETATM 2400 O  O   . HOH K 5 .   ? 18.354 -30.917 23.030  1.00 38.07 ? 678 HOH A O   1 
HETATM 2401 O  O   . HOH K 5 .   ? 10.142 -5.613  10.918  1.00 39.82 ? 679 HOH A O   1 
HETATM 2402 O  O   . HOH K 5 .   ? 18.293 -18.199 23.901  1.00 7.59  ? 680 HOH A O   1 
HETATM 2403 O  O   . HOH K 5 .   ? 2.685  -17.116 18.612  1.00 16.90 ? 681 HOH A O   1 
HETATM 2404 O  O   . HOH K 5 .   ? 17.716 -2.688  7.682   1.00 9.14  ? 682 HOH A O   1 
HETATM 2405 O  O   . HOH K 5 .   ? -7.379 -13.048 27.894  1.00 30.87 ? 683 HOH A O   1 
HETATM 2406 O  O   . HOH K 5 .   ? 3.478  -9.445  14.244  1.00 16.67 ? 684 HOH A O   1 
HETATM 2407 O  O   . HOH K 5 .   ? 30.237 -8.383  12.387  1.00 33.29 ? 685 HOH A O   1 
HETATM 2408 O  O   . HOH K 5 .   ? 14.245 -1.021  12.969  1.00 16.50 ? 686 HOH A O   1 
HETATM 2409 O  O   . HOH K 5 .   ? 24.092 -1.664  33.183  1.00 22.81 ? 687 HOH A O   1 
HETATM 2410 O  O   . HOH K 5 .   ? 16.405 -36.596 18.060  1.00 24.33 ? 688 HOH A O   1 
HETATM 2411 O  O   . HOH K 5 .   ? 3.528  -20.139 20.996  1.00 31.12 ? 689 HOH A O   1 
HETATM 2412 O  O   . HOH K 5 .   ? 9.249  -11.338 29.857  1.00 11.65 ? 690 HOH A O   1 
HETATM 2413 O  O   . HOH K 5 .   ? 0.351  1.725   20.765  1.00 31.19 ? 691 HOH A O   1 
HETATM 2414 O  O   . HOH K 5 .   ? 26.262 -20.144 14.199  1.00 19.29 ? 692 HOH A O   1 
HETATM 2415 O  O   . HOH K 5 .   ? 29.276 1.579   28.828  1.00 30.61 ? 693 HOH A O   1 
HETATM 2416 O  O   . HOH K 5 .   ? 6.682  -23.253 22.157  1.00 24.96 ? 694 HOH A O   1 
HETATM 2417 O  O   . HOH K 5 .   ? 16.322 -30.951 14.087  1.00 32.99 ? 695 HOH A O   1 
HETATM 2418 O  O   . HOH K 5 .   ? 9.670  -16.062 10.084  1.00 21.11 ? 696 HOH A O   1 
HETATM 2419 O  O   . HOH K 5 .   ? 25.140 -22.622 16.080  1.00 18.22 ? 697 HOH A O   1 
HETATM 2420 O  O   . HOH K 5 .   ? 21.838 -25.937 25.879  1.00 42.24 ? 698 HOH A O   1 
HETATM 2421 O  O   . HOH K 5 .   ? 12.809 -19.230 29.279  1.00 21.14 ? 699 HOH A O   1 
HETATM 2422 O  O   . HOH K 5 .   ? 24.155 -13.127 31.376  1.00 15.86 ? 700 HOH A O   1 
HETATM 2423 O  O   . HOH K 5 .   ? 12.094 -23.484 27.101  1.00 19.10 ? 701 HOH A O   1 
HETATM 2424 O  O   . HOH K 5 .   ? 1.587  -5.036  11.213  1.00 30.57 ? 702 HOH A O   1 
HETATM 2425 O  O   . HOH K 5 .   ? 30.063 -6.200  16.637  1.00 33.13 ? 703 HOH A O   1 
HETATM 2426 O  O   . HOH K 5 .   ? 28.248 -9.589  11.186  1.00 21.62 ? 704 HOH A O   1 
HETATM 2427 O  O   . HOH K 5 .   ? 31.167 -10.768 28.020  1.00 26.87 ? 705 HOH A O   1 
HETATM 2428 O  O   . HOH K 5 .   ? 8.746  0.920   10.643  1.00 24.22 ? 706 HOH A O   1 
HETATM 2429 O  O   . HOH K 5 .   ? 24.392 8.708   22.194  1.00 22.65 ? 707 HOH A O   1 
HETATM 2430 O  O   . HOH K 5 .   ? 8.751  -9.289  8.892   1.00 30.38 ? 708 HOH A O   1 
HETATM 2431 O  O   . HOH K 5 .   ? 33.293 2.702   31.749  1.00 34.28 ? 709 HOH A O   1 
HETATM 2432 O  O   . HOH K 5 .   ? 6.387  -0.501  18.739  1.00 33.08 ? 710 HOH A O   1 
HETATM 2433 O  O   . HOH K 5 .   ? 21.511 -19.536 14.283  1.00 23.76 ? 711 HOH A O   1 
HETATM 2434 O  O   . HOH K 5 .   ? 19.157 -19.871 30.361  1.00 15.29 ? 712 HOH A O   1 
HETATM 2435 O  O   . HOH K 5 .   ? 11.512 -23.302 14.310  1.00 25.28 ? 713 HOH A O   1 
HETATM 2436 O  O   . HOH K 5 .   ? 17.872 -11.590 33.543  1.00 25.66 ? 714 HOH A O   1 
HETATM 2437 O  O   . HOH K 5 .   ? 16.677 10.779  21.993  1.00 36.38 ? 715 HOH A O   1 
HETATM 2438 O  O   . HOH K 5 .   ? 30.609 -8.621  26.870  1.00 34.70 ? 716 HOH A O   1 
HETATM 2439 O  O   . HOH K 5 .   ? 34.278 0.735   24.676  1.00 33.84 ? 717 HOH A O   1 
HETATM 2440 O  O   . HOH K 5 .   ? 10.645 -3.273  11.725  1.00 32.88 ? 718 HOH A O   1 
HETATM 2441 O  O   . HOH K 5 .   ? -3.084 -13.117 24.442  1.00 21.19 ? 719 HOH A O   1 
HETATM 2442 O  O   . HOH K 5 .   ? -6.674 -14.278 26.045  1.00 22.82 ? 720 HOH A O   1 
HETATM 2443 O  O   . HOH K 5 .   ? 15.000 -17.239 29.259  1.00 27.62 ? 721 HOH A O   1 
HETATM 2444 O  O   . HOH K 5 .   ? 23.995 -10.267 33.739  1.00 31.13 ? 722 HOH A O   1 
HETATM 2445 O  O   . HOH K 5 .   ? 11.844 -10.634 30.425  1.00 15.46 ? 723 HOH A O   1 
HETATM 2446 O  O   . HOH K 5 .   ? 21.448 -10.740 4.937   1.00 38.48 ? 724 HOH A O   1 
HETATM 2447 O  O   . HOH K 5 .   ? 11.640 -15.606 3.043   1.00 40.38 ? 725 HOH A O   1 
HETATM 2448 O  O   . HOH K 5 .   ? 8.271  -17.796 9.187   1.00 33.41 ? 726 HOH A O   1 
HETATM 2449 O  O   . HOH K 5 .   ? 4.614  -2.353  23.452  1.00 40.20 ? 727 HOH A O   1 
HETATM 2450 O  O   . HOH K 5 .   ? 16.254 -4.594  33.487  1.00 30.40 ? 728 HOH A O   1 
HETATM 2451 O  O   . HOH K 5 .   ? 29.483 -12.899 13.558  1.00 30.22 ? 729 HOH A O   1 
HETATM 2452 O  O   . HOH K 5 .   ? 4.652  -0.883  21.162  1.00 36.31 ? 730 HOH A O   1 
HETATM 2453 O  O   . HOH K 5 .   ? 10.736 -14.065 9.020   1.00 41.39 ? 731 HOH A O   1 
HETATM 2454 O  O   . HOH K 5 .   ? -4.336 -15.418 25.801  1.00 28.91 ? 732 HOH A O   1 
HETATM 2455 O  O   . HOH K 5 .   ? 12.117 -16.933 30.662  1.00 30.06 ? 733 HOH A O   1 
HETATM 2456 O  O   . HOH K 5 .   ? 35.243 -1.496  22.398  1.00 32.62 ? 734 HOH A O   1 
HETATM 2457 O  O   . HOH K 5 .   ? 18.193 -29.897 12.011  1.00 35.55 ? 735 HOH A O   1 
HETATM 2458 O  O   . HOH K 5 .   ? 34.581 -18.564 26.171  1.00 60.03 ? 736 HOH A O   1 
HETATM 2459 O  O   . HOH K 5 .   ? 35.084 -3.902  24.016  1.00 40.97 ? 737 HOH A O   1 
HETATM 2460 O  O   . HOH K 5 .   ? 3.186  -12.537 11.443  1.00 38.55 ? 738 HOH A O   1 
HETATM 2461 O  O   . HOH K 5 .   ? 34.003 -1.760  13.989  1.00 33.21 ? 739 HOH A O   1 
HETATM 2462 O  O   . HOH K 5 .   ? 30.821 -10.657 14.301  1.00 24.97 ? 740 HOH A O   1 
HETATM 2463 O  O   . HOH K 5 .   ? 0.952  -19.206 18.364  1.00 35.34 ? 741 HOH A O   1 
HETATM 2464 O  O   . HOH K 5 .   ? 8.201  -5.618  9.217   1.00 46.05 ? 742 HOH A O   1 
HETATM 2465 O  O   . HOH K 5 .   ? 2.442  -12.101 13.940  1.00 20.56 ? 743 HOH A O   1 
HETATM 2466 O  O   . HOH K 5 .   ? 18.742 -25.380 12.299  1.00 30.80 ? 744 HOH A O   1 
HETATM 2467 O  O   . HOH K 5 .   ? 10.264 -25.471 24.026  1.00 27.07 ? 745 HOH A O   1 
HETATM 2468 O  O   . HOH K 5 .   ? 12.529 -2.304  34.032  1.00 41.04 ? 746 HOH A O   1 
HETATM 2469 O  O   . HOH K 5 .   ? 5.688  -8.687  35.081  1.00 34.80 ? 747 HOH A O   1 
HETATM 2470 O  O   . HOH K 5 .   ? 1.026  -2.833  26.376  1.00 33.46 ? 748 HOH A O   1 
HETATM 2471 O  O   . HOH K 5 .   ? 27.254 -2.214  35.889  1.00 31.47 ? 749 HOH A O   1 
HETATM 2472 O  O   . HOH K 5 .   ? 17.981 -13.619 31.204  1.00 15.69 ? 750 HOH A O   1 
HETATM 2473 O  O   . HOH K 5 .   ? -3.333 -5.567  16.853  1.00 49.96 ? 751 HOH A O   1 
HETATM 2474 O  O   . HOH K 5 .   ? 30.240 -16.516 25.115  1.00 19.61 ? 752 HOH A O   1 
HETATM 2475 O  O   . HOH K 5 .   ? 9.395  -5.147  34.683  1.00 35.36 ? 753 HOH A O   1 
HETATM 2476 O  O   . HOH K 5 .   ? 0.105  -4.877  30.913  1.00 27.14 ? 754 HOH A O   1 
HETATM 2477 O  O   . HOH K 5 .   ? 25.797 5.255   35.039  1.00 40.42 ? 755 HOH A O   1 
HETATM 2478 O  O   . HOH K 5 .   ? 24.720 -26.347 28.195  1.00 25.98 ? 756 HOH A O   1 
HETATM 2479 O  O   . HOH K 5 .   ? 4.203  -10.516 33.175  1.00 49.55 ? 757 HOH A O   1 
HETATM 2480 O  O   . HOH K 5 .   ? 27.323 3.825   20.953  1.00 32.80 ? 758 HOH A O   1 
HETATM 2481 O  O   . HOH K 5 .   ? 17.494 -15.834 32.695  1.00 30.87 ? 759 HOH A O   1 
HETATM 2482 O  O   . HOH K 5 .   ? 26.782 6.120   22.953  1.00 27.88 ? 760 HOH A O   1 
HETATM 2483 O  O   . HOH K 5 .   ? 0.819  -2.913  29.106  1.00 31.63 ? 761 HOH A O   1 
HETATM 2484 O  O   . HOH K 5 .   ? 16.805 -18.645 31.082  1.00 28.37 ? 762 HOH A O   1 
HETATM 2485 O  O   . HOH K 5 .   ? 1.105  -13.504 15.590  1.00 22.27 ? 763 HOH A O   1 
HETATM 2486 O  O   . HOH K 5 .   ? -1.305 -12.316 11.862  1.00 38.06 ? 764 HOH A O   1 
HETATM 2487 O  O   . HOH K 5 .   ? -1.530 -13.190 14.343  1.00 25.89 ? 765 HOH A O   1 
HETATM 2488 O  O   . HOH K 5 .   ? 1.718  -16.085 16.173  1.00 34.26 ? 766 HOH A O   1 
HETATM 2489 O  O   . HOH K 5 .   ? 35.074 -16.570 24.410  1.00 27.41 ? 767 HOH A O   1 
HETATM 2490 O  O   . HOH L 5 .   ? 43.269 5.846   7.843   1.00 32.98 ? 601 HOH F O   1 
HETATM 2491 O  O   . HOH L 5 .   ? 40.687 3.848   9.332   1.00 36.04 ? 602 HOH F O   1 
HETATM 2492 O  O   . HOH L 5 .   ? 38.031 2.508   -1.203  1.00 36.07 ? 603 HOH F O   1 
HETATM 2493 O  O   . HOH L 5 .   ? 14.614 14.603  16.683  0.50 9.57  ? 604 HOH F O   1 
HETATM 2494 O  O   . HOH L 5 .   ? 14.197 9.357   21.917  1.00 85.20 ? 605 HOH F O   1 
HETATM 2495 O  O   . HOH L 5 .   ? 37.998 8.534   1.430   1.00 38.01 ? 606 HOH F O   1 
HETATM 2496 O  O   . HOH L 5 .   ? 6.249  11.233  4.789   1.00 22.62 ? 607 HOH F O   1 
HETATM 2497 O  O   . HOH L 5 .   ? 37.177 13.534  4.007   1.00 36.29 ? 608 HOH F O   1 
HETATM 2498 O  O   . HOH L 5 .   ? 34.567 0.653   14.999  1.00 24.08 ? 609 HOH F O   1 
HETATM 2499 O  O   . HOH L 5 .   ? 27.367 28.116  5.587   1.00 29.27 ? 610 HOH F O   1 
HETATM 2500 O  O   . HOH L 5 .   ? 34.192 17.315  3.753   1.00 27.15 ? 611 HOH F O   1 
HETATM 2501 O  O   . HOH L 5 .   ? 20.863 14.718  -5.671  1.00 19.80 ? 612 HOH F O   1 
HETATM 2502 O  O   . HOH L 5 .   ? 32.921 25.213  13.105  1.00 26.06 ? 613 HOH F O   1 
HETATM 2503 O  O   . HOH L 5 .   ? 21.062 -4.975  -0.446  1.00 23.97 ? 614 HOH F O   1 
HETATM 2504 O  O   . HOH L 5 .   ? 12.620 2.741   11.906  1.00 34.00 ? 615 HOH F O   1 
HETATM 2505 O  O   . HOH L 5 .   ? 17.632 10.259  -8.866  1.00 26.95 ? 616 HOH F O   1 
HETATM 2506 O  O   . HOH L 5 .   ? 36.748 4.632   9.729   1.00 30.39 ? 617 HOH F O   1 
HETATM 2507 O  O   . HOH L 5 .   ? 16.942 20.165  7.564   1.00 11.84 ? 618 HOH F O   1 
HETATM 2508 O  O   . HOH L 5 .   ? 19.971 16.717  -8.995  1.00 16.89 ? 619 HOH F O   1 
HETATM 2509 O  O   . HOH L 5 .   ? 12.625 1.294   8.628   1.00 17.88 ? 620 HOH F O   1 
HETATM 2510 O  O   . HOH L 5 .   ? 5.550  11.781  -6.638  1.00 32.96 ? 621 HOH F O   1 
HETATM 2511 O  O   . HOH L 5 .   ? 23.600 -3.529  1.811   1.00 25.00 ? 622 HOH F O   1 
HETATM 2512 O  O   . HOH L 5 .   ? 27.406 24.288  0.677   1.00 24.02 ? 623 HOH F O   1 
HETATM 2513 O  O   . HOH L 5 .   ? 32.149 -1.674  11.937  1.00 29.30 ? 624 HOH F O   1 
HETATM 2514 O  O   . HOH L 5 .   ? 5.936  12.492  -0.832  1.00 20.75 ? 625 HOH F O   1 
HETATM 2515 O  O   . HOH L 5 .   ? 15.175 22.216  9.836   1.00 35.22 ? 626 HOH F O   1 
HETATM 2516 O  O   . HOH L 5 .   ? 5.730  9.205   8.146   1.00 32.01 ? 627 HOH F O   1 
HETATM 2517 O  O   . HOH L 5 .   ? 24.143 13.238  22.258  1.00 27.97 ? 628 HOH F O   1 
HETATM 2518 O  O   . HOH L 5 .   ? 27.536 26.395  7.941   1.00 33.11 ? 629 HOH F O   1 
HETATM 2519 O  O   . HOH L 5 .   ? 33.633 15.570  1.510   1.00 33.86 ? 630 HOH F O   1 
HETATM 2520 O  O   . HOH L 5 .   ? 16.660 -0.229  8.596   1.00 7.96  ? 631 HOH F O   1 
HETATM 2521 O  O   . HOH L 5 .   ? 35.164 7.131   5.469   1.00 22.93 ? 632 HOH F O   1 
HETATM 2522 O  O   . HOH L 5 .   ? 36.182 2.131   1.014   1.00 29.62 ? 633 HOH F O   1 
HETATM 2523 O  O   . HOH L 5 .   ? 9.279  3.268   14.325  1.00 34.45 ? 634 HOH F O   1 
HETATM 2524 O  O   . HOH L 5 .   ? 21.351 4.161   -7.723  1.00 46.08 ? 635 HOH F O   1 
HETATM 2525 O  O   . HOH L 5 .   ? 6.300  3.940   4.257   1.00 38.69 ? 636 HOH F O   1 
HETATM 2526 O  O   . HOH L 5 .   ? 34.521 10.125  -1.302  1.00 29.67 ? 637 HOH F O   1 
HETATM 2527 O  O   . HOH L 5 .   ? 9.554  18.695  -4.413  1.00 29.93 ? 638 HOH F O   1 
HETATM 2528 O  O   . HOH L 5 .   ? 24.613 13.762  -1.936  1.00 21.40 ? 639 HOH F O   1 
HETATM 2529 O  O   . HOH L 5 .   ? 4.083  9.224   -1.907  1.00 30.67 ? 640 HOH F O   1 
HETATM 2530 O  O   . HOH L 5 .   ? 30.713 16.222  12.717  1.00 11.08 ? 641 HOH F O   1 
HETATM 2531 O  O   . HOH L 5 .   ? 36.167 18.603  16.725  1.00 15.04 ? 642 HOH F O   1 
HETATM 2532 O  O   . HOH L 5 .   ? 10.046 8.379   21.641  1.00 27.65 ? 643 HOH F O   1 
HETATM 2533 O  O   . HOH L 5 .   ? 30.086 6.772   15.531  1.00 24.36 ? 644 HOH F O   1 
HETATM 2534 O  O   . HOH L 5 .   ? 29.072 25.005  6.155   1.00 31.60 ? 645 HOH F O   1 
HETATM 2535 O  O   . HOH L 5 .   ? 17.442 18.636  14.466  1.00 27.27 ? 646 HOH F O   1 
HETATM 2536 O  O   . HOH L 5 .   ? 33.188 17.209  19.257  1.00 10.29 ? 647 HOH F O   1 
HETATM 2537 O  O   . HOH L 5 .   ? 23.035 12.709  -3.766  1.00 24.84 ? 648 HOH F O   1 
HETATM 2538 O  O   . HOH L 5 .   ? 12.564 25.211  5.823   1.00 39.58 ? 649 HOH F O   1 
HETATM 2539 O  O   . HOH L 5 .   ? 28.279 8.690   19.618  1.00 45.66 ? 650 HOH F O   1 
HETATM 2540 O  O   . HOH L 5 .   ? 32.246 16.762  10.559  1.00 11.61 ? 651 HOH F O   1 
HETATM 2541 O  O   . HOH L 5 .   ? 15.495 24.665  1.788   1.00 21.60 ? 652 HOH F O   1 
HETATM 2542 O  O   . HOH L 5 .   ? 31.447 24.699  15.319  1.00 35.35 ? 653 HOH F O   1 
HETATM 2543 O  O   . HOH L 5 .   ? 15.501 6.126   23.938  1.00 38.21 ? 654 HOH F O   1 
HETATM 2544 O  O   . HOH L 5 .   ? 14.426 29.707  10.447  1.00 37.85 ? 655 HOH F O   1 
HETATM 2545 O  O   . HOH L 5 .   ? 16.658 27.438  2.659   1.00 20.46 ? 656 HOH F O   1 
HETATM 2546 O  O   . HOH L 5 .   ? 12.803 16.198  -13.651 1.00 18.82 ? 657 HOH F O   1 
HETATM 2547 O  O   . HOH L 5 .   ? 18.440 6.080   -12.637 1.00 47.22 ? 658 HOH F O   1 
HETATM 2548 O  O   . HOH L 5 .   ? 29.399 -6.006  6.923   1.00 15.83 ? 659 HOH F O   1 
HETATM 2549 O  O   . HOH L 5 .   ? 7.356  6.958   -6.665  1.00 21.01 ? 660 HOH F O   1 
HETATM 2550 O  O   . HOH L 5 .   ? 14.989 8.503   -10.676 1.00 27.67 ? 661 HOH F O   1 
HETATM 2551 O  O   . HOH L 5 .   ? 17.514 8.228   22.164  1.00 14.96 ? 662 HOH F O   1 
HETATM 2552 O  O   . HOH L 5 .   ? 29.561 12.802  -0.762  1.00 14.50 ? 663 HOH F O   1 
HETATM 2553 O  O   . HOH L 5 .   ? 14.814 2.567   17.348  1.00 10.96 ? 664 HOH F O   1 
HETATM 2554 O  O   . HOH L 5 .   ? 37.464 6.782   15.618  1.00 30.86 ? 665 HOH F O   1 
HETATM 2555 O  O   . HOH L 5 .   ? 28.004 25.733  3.468   1.00 42.29 ? 666 HOH F O   1 
HETATM 2556 O  O   . HOH L 5 .   ? 23.452 30.729  4.813   1.00 23.21 ? 667 HOH F O   1 
HETATM 2557 O  O   . HOH L 5 .   ? 11.235 3.276   9.807   1.00 26.36 ? 668 HOH F O   1 
HETATM 2558 O  O   . HOH L 5 .   ? 23.840 18.151  3.887   1.00 12.22 ? 669 HOH F O   1 
HETATM 2559 O  O   . HOH L 5 .   ? 27.802 4.579   15.314  1.00 29.16 ? 670 HOH F O   1 
HETATM 2560 O  O   . HOH L 5 .   ? 25.613 22.914  13.734  1.00 29.80 ? 671 HOH F O   1 
HETATM 2561 O  O   . HOH L 5 .   ? 14.835 0.801   10.887  1.00 17.50 ? 672 HOH F O   1 
HETATM 2562 O  O   . HOH L 5 .   ? 7.959  9.526   11.724  1.00 29.62 ? 673 HOH F O   1 
HETATM 2563 O  O   . HOH L 5 .   ? 19.297 29.160  -0.450  1.00 36.86 ? 674 HOH F O   1 
HETATM 2564 O  O   . HOH L 5 .   ? 25.900 14.092  16.929  1.00 9.03  ? 675 HOH F O   1 
HETATM 2565 O  O   . HOH L 5 .   ? 35.455 7.008   12.016  1.00 12.04 ? 676 HOH F O   1 
HETATM 2566 O  O   . HOH L 5 .   ? 20.473 23.356  -1.991  1.00 21.71 ? 677 HOH F O   1 
HETATM 2567 O  O   . HOH L 5 .   ? 25.671 9.581   19.715  1.00 19.54 ? 678 HOH F O   1 
HETATM 2568 O  O   . HOH L 5 .   ? 7.936  10.379  9.182   1.00 28.54 ? 679 HOH F O   1 
HETATM 2569 O  O   . HOH L 5 .   ? 32.879 13.113  0.732   1.00 19.63 ? 680 HOH F O   1 
HETATM 2570 O  O   . HOH L 5 .   ? 19.333 36.373  7.917   1.00 30.83 ? 681 HOH F O   1 
HETATM 2571 O  O   . HOH L 5 .   ? 8.011  14.133  -1.052  1.00 13.73 ? 682 HOH F O   1 
HETATM 2572 O  O   . HOH L 5 .   ? 31.668 11.998  -4.221  1.00 32.44 ? 683 HOH F O   1 
HETATM 2573 O  O   . HOH L 5 .   ? 35.248 9.376   20.044  1.00 14.06 ? 684 HOH F O   1 
HETATM 2574 O  O   . HOH L 5 .   ? 29.899 5.183   17.381  1.00 28.66 ? 685 HOH F O   1 
HETATM 2575 O  O   . HOH L 5 .   ? 16.936 30.880  11.200  1.00 24.45 ? 686 HOH F O   1 
HETATM 2576 O  O   . HOH L 5 .   ? 7.887  16.764  -0.051  1.00 20.35 ? 687 HOH F O   1 
HETATM 2577 O  O   . HOH L 5 .   ? 22.058 19.196  -3.612  1.00 18.79 ? 688 HOH F O   1 
HETATM 2578 O  O   . HOH L 5 .   ? 34.699 17.411  6.513   1.00 24.02 ? 689 HOH F O   1 
HETATM 2579 O  O   . HOH L 5 .   ? 13.336 23.184  7.915   1.00 22.82 ? 690 HOH F O   1 
HETATM 2580 O  O   . HOH L 5 .   ? 35.824 -1.386  5.815   1.00 29.72 ? 691 HOH F O   1 
HETATM 2581 O  O   . HOH L 5 .   ? 21.987 19.866  13.484  1.00 42.51 ? 692 HOH F O   1 
HETATM 2582 O  O   . HOH L 5 .   ? 25.299 19.963  16.315  0.50 4.61  ? 693 HOH F O   1 
HETATM 2583 O  O   . HOH L 5 .   ? 19.603 11.086  -5.992  1.00 16.17 ? 694 HOH F O   1 
HETATM 2584 O  O   . HOH L 5 .   ? 37.836 8.435   4.090   1.00 22.52 ? 695 HOH F O   1 
HETATM 2585 O  O   . HOH L 5 .   ? 33.747 24.462  4.047   1.00 26.27 ? 696 HOH F O   1 
HETATM 2586 O  O   . HOH L 5 .   ? 9.848  20.666  -8.018  1.00 30.40 ? 697 HOH F O   1 
HETATM 2587 O  O   . HOH L 5 .   ? 19.803 18.865  13.703  1.00 31.91 ? 698 HOH F O   1 
HETATM 2588 O  O   . HOH L 5 .   ? 1.009  6.673   -2.966  1.00 30.65 ? 699 HOH F O   1 
HETATM 2589 O  O   . HOH L 5 .   ? 9.185  15.924  10.903  1.00 23.19 ? 700 HOH F O   1 
HETATM 2590 O  O   . HOH L 5 .   ? 5.979  15.607  -8.108  1.00 25.95 ? 701 HOH F O   1 
HETATM 2591 O  O   . HOH L 5 .   ? 13.042 23.159  -0.945  1.00 23.20 ? 702 HOH F O   1 
HETATM 2592 O  O   . HOH L 5 .   ? 26.025 -3.036  1.212   1.00 37.62 ? 703 HOH F O   1 
HETATM 2593 O  O   . HOH L 5 .   ? 28.370 -8.837  8.611   1.00 22.16 ? 704 HOH F O   1 
HETATM 2594 O  O   . HOH L 5 .   ? 28.821 22.691  16.772  1.00 38.09 ? 705 HOH F O   1 
HETATM 2595 O  O   . HOH L 5 .   ? 40.343 -1.768  7.063   1.00 41.60 ? 706 HOH F O   1 
HETATM 2596 O  O   . HOH L 5 .   ? 33.368 10.124  -5.768  1.00 42.14 ? 707 HOH F O   1 
HETATM 2597 O  O   . HOH L 5 .   ? 27.327 4.702   -5.423  1.00 34.81 ? 708 HOH F O   1 
HETATM 2598 O  O   . HOH L 5 .   ? 34.839 23.723  1.822   1.00 35.45 ? 709 HOH F O   1 
HETATM 2599 O  O   . HOH L 5 .   ? 11.755 5.332   23.785  1.00 48.87 ? 710 HOH F O   1 
HETATM 2600 O  O   . HOH L 5 .   ? 5.184  12.373  1.794   1.00 26.91 ? 711 HOH F O   1 
HETATM 2601 O  O   . HOH L 5 .   ? 29.197 -10.942 7.074   1.00 33.61 ? 712 HOH F O   1 
HETATM 2602 O  O   . HOH L 5 .   ? 23.974 16.787  -2.557  1.00 22.55 ? 713 HOH F O   1 
HETATM 2603 O  O   . HOH L 5 .   ? 27.856 19.709  -1.243  1.00 18.95 ? 714 HOH F O   1 
HETATM 2604 O  O   . HOH L 5 .   ? 28.805 11.597  -4.480  1.00 29.79 ? 715 HOH F O   1 
HETATM 2605 O  O   . HOH L 5 .   ? 16.849 33.586  14.426  1.00 39.40 ? 716 HOH F O   1 
HETATM 2606 O  O   . HOH L 5 .   ? 23.849 -8.624  2.244   1.00 32.71 ? 717 HOH F O   1 
HETATM 2607 O  O   . HOH L 5 .   ? 21.944 10.598  -5.009  1.00 19.67 ? 718 HOH F O   1 
HETATM 2608 O  O   . HOH L 5 .   ? 17.832 34.235  11.199  1.00 31.09 ? 719 HOH F O   1 
HETATM 2609 O  O   . HOH L 5 .   ? 23.471 21.642  14.509  1.00 57.29 ? 720 HOH F O   1 
HETATM 2610 O  O   . HOH L 5 .   ? 21.642 13.248  -7.626  1.00 33.04 ? 721 HOH F O   1 
HETATM 2611 O  O   . HOH L 5 .   ? 38.450 3.432   12.600  1.00 44.14 ? 722 HOH F O   1 
HETATM 2612 O  O   . HOH L 5 .   ? 36.604 7.844   9.691   1.00 32.36 ? 723 HOH F O   1 
HETATM 2613 O  O   . HOH L 5 .   ? 24.445 1.901   -7.620  1.00 49.07 ? 724 HOH F O   1 
HETATM 2614 O  O   . HOH L 5 .   ? 22.187 17.032  -5.245  1.00 36.51 ? 725 HOH F O   1 
HETATM 2615 O  O   . HOH L 5 .   ? 41.959 0.837   11.718  1.00 42.05 ? 726 HOH F O   1 
HETATM 2616 O  O   . HOH L 5 .   ? 17.109 29.768  13.824  1.00 32.61 ? 727 HOH F O   1 
HETATM 2617 O  O   . HOH L 5 .   ? 29.216 5.448   19.974  1.00 31.55 ? 728 HOH F O   1 
HETATM 2618 O  O   . HOH L 5 .   ? 6.918  20.029  -4.689  1.00 39.64 ? 729 HOH F O   1 
HETATM 2619 O  O   . HOH L 5 .   ? 34.464 16.349  9.088   1.00 21.04 ? 730 HOH F O   1 
HETATM 2620 O  O   . HOH L 5 .   ? 36.533 14.269  9.170   1.00 29.62 ? 731 HOH F O   1 
HETATM 2621 O  O   . HOH L 5 .   ? 17.260 25.204  -0.640  1.00 31.07 ? 732 HOH F O   1 
HETATM 2622 O  O   . HOH L 5 .   ? 14.372 28.076  3.943   1.00 35.81 ? 733 HOH F O   1 
HETATM 2623 O  O   . HOH L 5 .   ? 10.794 23.783  8.339   1.00 55.88 ? 734 HOH F O   1 
HETATM 2624 O  O   . HOH L 5 .   ? 16.452 9.040   24.841  1.00 32.12 ? 735 HOH F O   1 
HETATM 2625 O  O   . HOH L 5 .   ? 7.538  4.370   -7.839  1.00 30.67 ? 736 HOH F O   1 
HETATM 2626 O  O   . HOH L 5 .   ? 35.923 2.249   -2.588  1.00 38.79 ? 737 HOH F O   1 
HETATM 2627 O  O   . HOH L 5 .   ? 27.546 13.592  -2.411  1.00 18.85 ? 738 HOH F O   1 
HETATM 2628 O  O   . HOH L 5 .   ? 30.170 -5.984  9.538   1.00 33.13 ? 739 HOH F O   1 
HETATM 2629 O  O   . HOH L 5 .   ? 30.455 -3.731  11.492  1.00 38.22 ? 740 HOH F O   1 
HETATM 2630 O  O   . HOH L 5 .   ? 11.377 -1.077  8.727   1.00 40.55 ? 741 HOH F O   1 
HETATM 2631 O  O   . HOH L 5 .   ? 19.777 20.874  15.410  1.00 42.23 ? 742 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 2 ZN  1   502 502 ZN  ZN  A . 
E 3 9JT 1   503 503 9JT DR1 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 9JT 1   503 503 9JT DR1 F . 
J 4 SO4 1   504 504 SO4 SO4 F . 
K 5 HOH 1   601 1   HOH HOH A . 
K 5 HOH 2   602 22  HOH HOH A . 
K 5 HOH 3   603 24  HOH HOH A . 
K 5 HOH 4   604 139 HOH HOH A . 
K 5 HOH 5   605 246 HOH HOH A . 
K 5 HOH 6   606 151 HOH HOH A . 
K 5 HOH 7   607 299 HOH HOH A . 
K 5 HOH 8   608 97  HOH HOH A . 
K 5 HOH 9   609 41  HOH HOH A . 
K 5 HOH 10  610 107 HOH HOH A . 
K 5 HOH 11  611 11  HOH HOH A . 
K 5 HOH 12  612 63  HOH HOH A . 
K 5 HOH 13  613 31  HOH HOH A . 
K 5 HOH 14  614 141 HOH HOH A . 
K 5 HOH 15  615 129 HOH HOH A . 
K 5 HOH 16  616 59  HOH HOH A . 
K 5 HOH 17  617 215 HOH HOH A . 
K 5 HOH 18  618 124 HOH HOH A . 
K 5 HOH 19  619 306 HOH HOH A . 
K 5 HOH 20  620 163 HOH HOH A . 
K 5 HOH 21  621 136 HOH HOH A . 
K 5 HOH 22  622 66  HOH HOH A . 
K 5 HOH 23  623 58  HOH HOH A . 
K 5 HOH 24  624 155 HOH HOH A . 
K 5 HOH 25  625 137 HOH HOH A . 
K 5 HOH 26  626 54  HOH HOH A . 
K 5 HOH 27  627 301 HOH HOH A . 
K 5 HOH 28  628 96  HOH HOH A . 
K 5 HOH 29  629 5   HOH HOH A . 
K 5 HOH 30  630 160 HOH HOH A . 
K 5 HOH 31  631 170 HOH HOH A . 
K 5 HOH 32  632 91  HOH HOH A . 
K 5 HOH 33  633 82  HOH HOH A . 
K 5 HOH 34  634 152 HOH HOH A . 
K 5 HOH 35  635 158 HOH HOH A . 
K 5 HOH 36  636 274 HOH HOH A . 
K 5 HOH 37  637 130 HOH HOH A . 
K 5 HOH 38  638 128 HOH HOH A . 
K 5 HOH 39  639 147 HOH HOH A . 
K 5 HOH 40  640 140 HOH HOH A . 
K 5 HOH 41  641 150 HOH HOH A . 
K 5 HOH 42  642 86  HOH HOH A . 
K 5 HOH 43  643 149 HOH HOH A . 
K 5 HOH 44  644 276 HOH HOH A . 
K 5 HOH 45  645 77  HOH HOH A . 
K 5 HOH 46  646 76  HOH HOH A . 
K 5 HOH 47  647 122 HOH HOH A . 
K 5 HOH 48  648 286 HOH HOH A . 
K 5 HOH 49  649 125 HOH HOH A . 
K 5 HOH 50  650 157 HOH HOH A . 
K 5 HOH 51  651 126 HOH HOH A . 
K 5 HOH 52  652 270 HOH HOH A . 
K 5 HOH 53  653 292 HOH HOH A . 
K 5 HOH 54  654 131 HOH HOH A . 
K 5 HOH 55  655 104 HOH HOH A . 
K 5 HOH 56  656 168 HOH HOH A . 
K 5 HOH 57  657 114 HOH HOH A . 
K 5 HOH 58  658 283 HOH HOH A . 
K 5 HOH 59  659 6   HOH HOH A . 
K 5 HOH 60  660 4   HOH HOH A . 
K 5 HOH 61  661 148 HOH HOH A . 
K 5 HOH 62  662 16  HOH HOH A . 
K 5 HOH 63  663 132 HOH HOH A . 
K 5 HOH 64  664 296 HOH HOH A . 
K 5 HOH 65  665 106 HOH HOH A . 
K 5 HOH 66  666 33  HOH HOH A . 
K 5 HOH 67  667 101 HOH HOH A . 
K 5 HOH 68  668 146 HOH HOH A . 
K 5 HOH 69  669 123 HOH HOH A . 
K 5 HOH 70  670 138 HOH HOH A . 
K 5 HOH 71  671 195 HOH HOH A . 
K 5 HOH 72  672 93  HOH HOH A . 
K 5 HOH 73  673 307 HOH HOH A . 
K 5 HOH 74  674 173 HOH HOH A . 
K 5 HOH 75  675 171 HOH HOH A . 
K 5 HOH 76  676 281 HOH HOH A . 
K 5 HOH 77  677 153 HOH HOH A . 
K 5 HOH 78  678 162 HOH HOH A . 
K 5 HOH 79  679 115 HOH HOH A . 
K 5 HOH 80  680 159 HOH HOH A . 
K 5 HOH 81  681 156 HOH HOH A . 
K 5 HOH 82  682 112 HOH HOH A . 
K 5 HOH 83  683 213 HOH HOH A . 
K 5 HOH 84  684 166 HOH HOH A . 
K 5 HOH 85  685 302 HOH HOH A . 
K 5 HOH 86  686 18  HOH HOH A . 
K 5 HOH 87  687 100 HOH HOH A . 
K 5 HOH 88  688 20  HOH HOH A . 
K 5 HOH 89  689 279 HOH HOH A . 
K 5 HOH 90  690 135 HOH HOH A . 
K 5 HOH 91  691 40  HOH HOH A . 
K 5 HOH 92  692 229 HOH HOH A . 
K 5 HOH 93  693 94  HOH HOH A . 
K 5 HOH 94  694 10  HOH HOH A . 
K 5 HOH 95  695 165 HOH HOH A . 
K 5 HOH 96  696 15  HOH HOH A . 
K 5 HOH 97  697 19  HOH HOH A . 
K 5 HOH 98  698 161 HOH HOH A . 
K 5 HOH 99  699 205 HOH HOH A . 
K 5 HOH 100 700 145 HOH HOH A . 
K 5 HOH 101 701 206 HOH HOH A . 
K 5 HOH 102 702 305 HOH HOH A . 
K 5 HOH 103 703 154 HOH HOH A . 
K 5 HOH 104 704 111 HOH HOH A . 
K 5 HOH 105 705 68  HOH HOH A . 
K 5 HOH 106 706 287 HOH HOH A . 
K 5 HOH 107 707 169 HOH HOH A . 
K 5 HOH 108 708 119 HOH HOH A . 
K 5 HOH 109 709 39  HOH HOH A . 
K 5 HOH 110 710 90  HOH HOH A . 
K 5 HOH 111 711 47  HOH HOH A . 
K 5 HOH 112 712 310 HOH HOH A . 
K 5 HOH 113 713 13  HOH HOH A . 
K 5 HOH 114 714 143 HOH HOH A . 
K 5 HOH 115 715 8   HOH HOH A . 
K 5 HOH 116 716 297 HOH HOH A . 
K 5 HOH 117 717 300 HOH HOH A . 
K 5 HOH 118 718 167 HOH HOH A . 
K 5 HOH 119 719 105 HOH HOH A . 
K 5 HOH 120 720 184 HOH HOH A . 
K 5 HOH 121 721 133 HOH HOH A . 
K 5 HOH 122 722 144 HOH HOH A . 
K 5 HOH 123 723 80  HOH HOH A . 
K 5 HOH 124 724 32  HOH HOH A . 
K 5 HOH 125 725 186 HOH HOH A . 
K 5 HOH 126 726 278 HOH HOH A . 
K 5 HOH 127 727 89  HOH HOH A . 
K 5 HOH 128 728 142 HOH HOH A . 
K 5 HOH 129 729 308 HOH HOH A . 
K 5 HOH 130 730 88  HOH HOH A . 
K 5 HOH 131 731 26  HOH HOH A . 
K 5 HOH 132 732 53  HOH HOH A . 
K 5 HOH 133 733 204 HOH HOH A . 
K 5 HOH 134 734 273 HOH HOH A . 
K 5 HOH 135 735 164 HOH HOH A . 
K 5 HOH 136 736 69  HOH HOH A . 
K 5 HOH 137 737 83  HOH HOH A . 
K 5 HOH 138 738 81  HOH HOH A . 
K 5 HOH 139 739 285 HOH HOH A . 
K 5 HOH 140 740 92  HOH HOH A . 
K 5 HOH 141 741 109 HOH HOH A . 
K 5 HOH 142 742 290 HOH HOH A . 
K 5 HOH 143 743 113 HOH HOH A . 
K 5 HOH 144 744 34  HOH HOH A . 
K 5 HOH 145 745 110 HOH HOH A . 
K 5 HOH 146 746 298 HOH HOH A . 
K 5 HOH 147 747 57  HOH HOH A . 
K 5 HOH 148 748 304 HOH HOH A . 
K 5 HOH 149 749 85  HOH HOH A . 
K 5 HOH 150 750 102 HOH HOH A . 
K 5 HOH 151 751 293 HOH HOH A . 
K 5 HOH 152 752 99  HOH HOH A . 
K 5 HOH 153 753 103 HOH HOH A . 
K 5 HOH 154 754 65  HOH HOH A . 
K 5 HOH 155 755 289 HOH HOH A . 
K 5 HOH 156 756 79  HOH HOH A . 
K 5 HOH 157 757 51  HOH HOH A . 
K 5 HOH 158 758 74  HOH HOH A . 
K 5 HOH 159 759 84  HOH HOH A . 
K 5 HOH 160 760 117 HOH HOH A . 
K 5 HOH 161 761 277 HOH HOH A . 
K 5 HOH 162 762 98  HOH HOH A . 
K 5 HOH 163 763 87  HOH HOH A . 
K 5 HOH 164 764 30  HOH HOH A . 
K 5 HOH 165 765 95  HOH HOH A . 
K 5 HOH 166 766 284 HOH HOH A . 
K 5 HOH 167 767 7   HOH HOH A . 
L 5 HOH 1   601 46  HOH HOH F . 
L 5 HOH 2   602 28  HOH HOH F . 
L 5 HOH 3   603 183 HOH HOH F . 
L 5 HOH 4   604 134 HOH HOH F . 
L 5 HOH 5   605 61  HOH HOH F . 
L 5 HOH 6   606 43  HOH HOH F . 
L 5 HOH 7   607 178 HOH HOH F . 
L 5 HOH 8   608 240 HOH HOH F . 
L 5 HOH 9   609 64  HOH HOH F . 
L 5 HOH 10  610 303 HOH HOH F . 
L 5 HOH 11  611 71  HOH HOH F . 
L 5 HOH 12  612 226 HOH HOH F . 
L 5 HOH 13  613 294 HOH HOH F . 
L 5 HOH 14  614 118 HOH HOH F . 
L 5 HOH 15  615 268 HOH HOH F . 
L 5 HOH 16  616 228 HOH HOH F . 
L 5 HOH 17  617 243 HOH HOH F . 
L 5 HOH 18  618 260 HOH HOH F . 
L 5 HOH 19  619 227 HOH HOH F . 
L 5 HOH 20  620 175 HOH HOH F . 
L 5 HOH 21  621 309 HOH HOH F . 
L 5 HOH 22  622 181 HOH HOH F . 
L 5 HOH 23  623 219 HOH HOH F . 
L 5 HOH 24  624 73  HOH HOH F . 
L 5 HOH 25  625 190 HOH HOH F . 
L 5 HOH 26  626 25  HOH HOH F . 
L 5 HOH 27  627 3   HOH HOH F . 
L 5 HOH 28  628 108 HOH HOH F . 
L 5 HOH 29  629 269 HOH HOH F . 
L 5 HOH 30  630 217 HOH HOH F . 
L 5 HOH 31  631 262 HOH HOH F . 
L 5 HOH 32  632 242 HOH HOH F . 
L 5 HOH 33  633 29  HOH HOH F . 
L 5 HOH 34  634 72  HOH HOH F . 
L 5 HOH 35  635 233 HOH HOH F . 
L 5 HOH 36  636 177 HOH HOH F . 
L 5 HOH 37  637 241 HOH HOH F . 
L 5 HOH 38  638 192 HOH HOH F . 
L 5 HOH 39  639 223 HOH HOH F . 
L 5 HOH 40  640 75  HOH HOH F . 
L 5 HOH 41  641 207 HOH HOH F . 
L 5 HOH 42  642 211 HOH HOH F . 
L 5 HOH 43  643 14  HOH HOH F . 
L 5 HOH 44  644 248 HOH HOH F . 
L 5 HOH 45  645 216 HOH HOH F . 
L 5 HOH 46  646 27  HOH HOH F . 
L 5 HOH 47  647 210 HOH HOH F . 
L 5 HOH 48  648 224 HOH HOH F . 
L 5 HOH 49  649 275 HOH HOH F . 
L 5 HOH 50  650 127 HOH HOH F . 
L 5 HOH 51  651 221 HOH HOH F . 
L 5 HOH 52  652 252 HOH HOH F . 
L 5 HOH 53  653 42  HOH HOH F . 
L 5 HOH 54  654 203 HOH HOH F . 
L 5 HOH 55  655 271 HOH HOH F . 
L 5 HOH 56  656 254 HOH HOH F . 
L 5 HOH 57  657 194 HOH HOH F . 
L 5 HOH 58  658 232 HOH HOH F . 
L 5 HOH 59  659 263 HOH HOH F . 
L 5 HOH 60  660 230 HOH HOH F . 
L 5 HOH 61  661 78  HOH HOH F . 
L 5 HOH 62  662 174 HOH HOH F . 
L 5 HOH 63  663 238 HOH HOH F . 
L 5 HOH 64  664 202 HOH HOH F . 
L 5 HOH 65  665 245 HOH HOH F . 
L 5 HOH 66  666 255 HOH HOH F . 
L 5 HOH 67  667 62  HOH HOH F . 
L 5 HOH 68  668 261 HOH HOH F . 
L 5 HOH 69  669 253 HOH HOH F . 
L 5 HOH 70  670 249 HOH HOH F . 
L 5 HOH 71  671 222 HOH HOH F . 
L 5 HOH 72  672 17  HOH HOH F . 
L 5 HOH 73  673 55  HOH HOH F . 
L 5 HOH 74  674 36  HOH HOH F . 
L 5 HOH 75  675 208 HOH HOH F . 
L 5 HOH 76  676 244 HOH HOH F . 
L 5 HOH 77  677 56  HOH HOH F . 
L 5 HOH 78  678 201 HOH HOH F . 
L 5 HOH 79  679 67  HOH HOH F . 
L 5 HOH 80  680 239 HOH HOH F . 
L 5 HOH 81  681 256 HOH HOH F . 
L 5 HOH 82  682 191 HOH HOH F . 
L 5 HOH 83  683 236 HOH HOH F . 
L 5 HOH 84  684 247 HOH HOH F . 
L 5 HOH 85  685 272 HOH HOH F . 
L 5 HOH 86  686 259 HOH HOH F . 
L 5 HOH 87  687 251 HOH HOH F . 
L 5 HOH 88  688 120 HOH HOH F . 
L 5 HOH 89  689 220 HOH HOH F . 
L 5 HOH 90  690 21  HOH HOH F . 
L 5 HOH 91  691 182 HOH HOH F . 
L 5 HOH 92  692 52  HOH HOH F . 
L 5 HOH 93  693 209 HOH HOH F . 
L 5 HOH 94  694 231 HOH HOH F . 
L 5 HOH 95  695 185 HOH HOH F . 
L 5 HOH 96  696 45  HOH HOH F . 
L 5 HOH 97  697 196 HOH HOH F . 
L 5 HOH 98  698 48  HOH HOH F . 
L 5 HOH 99  699 295 HOH HOH F . 
L 5 HOH 100 700 9   HOH HOH F . 
L 5 HOH 101 701 193 HOH HOH F . 
L 5 HOH 102 702 12  HOH HOH F . 
L 5 HOH 103 703 267 HOH HOH F . 
L 5 HOH 104 704 264 HOH HOH F . 
L 5 HOH 105 705 212 HOH HOH F . 
L 5 HOH 106 706 291 HOH HOH F . 
L 5 HOH 107 707 189 HOH HOH F . 
L 5 HOH 108 708 235 HOH HOH F . 
L 5 HOH 109 709 44  HOH HOH F . 
L 5 HOH 110 710 70  HOH HOH F . 
L 5 HOH 111 711 179 HOH HOH F . 
L 5 HOH 112 712 265 HOH HOH F . 
L 5 HOH 113 713 225 HOH HOH F . 
L 5 HOH 114 714 218 HOH HOH F . 
L 5 HOH 115 715 237 HOH HOH F . 
L 5 HOH 116 716 23  HOH HOH F . 
L 5 HOH 117 717 266 HOH HOH F . 
L 5 HOH 118 718 234 HOH HOH F . 
L 5 HOH 119 719 258 HOH HOH F . 
L 5 HOH 120 720 49  HOH HOH F . 
L 5 HOH 121 721 282 HOH HOH F . 
L 5 HOH 122 722 197 HOH HOH F . 
L 5 HOH 123 723 180 HOH HOH F . 
L 5 HOH 124 724 200 HOH HOH F . 
L 5 HOH 125 725 121 HOH HOH F . 
L 5 HOH 126 726 60  HOH HOH F . 
L 5 HOH 127 727 257 HOH HOH F . 
L 5 HOH 128 728 250 HOH HOH F . 
L 5 HOH 129 729 35  HOH HOH F . 
L 5 HOH 130 730 214 HOH HOH F . 
L 5 HOH 131 731 2   HOH HOH F . 
L 5 HOH 132 732 198 HOH HOH F . 
L 5 HOH 133 733 199 HOH HOH F . 
L 5 HOH 134 734 288 HOH HOH F . 
L 5 HOH 135 735 172 HOH HOH F . 
L 5 HOH 136 736 188 HOH HOH F . 
L 5 HOH 137 737 176 HOH HOH F . 
L 5 HOH 138 738 187 HOH HOH F . 
L 5 HOH 139 739 38  HOH HOH F . 
L 5 HOH 140 740 37  HOH HOH F . 
L 5 HOH 141 741 116 HOH HOH F . 
L 5 HOH 142 742 50  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)' 2260  ? 
1 MORE         -135  ? 
1 'SSA (A^2)'  13810 ? 
# 
_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 ? D ZN . ? A ZN 502 ? 1_555 NE2 ? A HIS 48  ? A HIS 48  ? 1_555 122.8 ? 
2  ND1 ? A HIS 46  ? A HIS 46  ? 1_555 ZN ? D ZN . ? A ZN 502 ? 1_555 NE2 ? A HIS 120 ? A HIS 120 ? 1_555 96.8  ? 
3  NE2 ? A HIS 48  ? A HIS 48  ? 1_555 ZN ? D ZN . ? A ZN 502 ? 1_555 NE2 ? A HIS 120 ? A HIS 120 ? 1_555 126.5 ? 
4  ND1 ? A HIS 46  ? A HIS 46  ? 1_555 ZN ? D ZN . ? A ZN 502 ? 1_555 O4  ? F SO4 .   ? A SO4 504 ? 1_555 100.7 ? 
5  NE2 ? A HIS 48  ? A HIS 48  ? 1_555 ZN ? D ZN . ? A ZN 502 ? 1_555 O4  ? F SO4 .   ? A SO4 504 ? 1_555 105.2 ? 
6  NE2 ? A HIS 120 ? A HIS 120 ? 1_555 ZN ? D ZN . ? A ZN 502 ? 1_555 O4  ? F SO4 .   ? A SO4 504 ? 1_555 100.1 ? 
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_555 101.8 ? 
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_555 107.9 ? 
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_555 124.5 ? 
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_555 105.7 ? 
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 95.8  ? 
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_555 118.6 ? 
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_555 121.0 ? 
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 99.4  ? 
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_555 127.0 ? 
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 99.7  ? 
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_555 104.4 ? 
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_555 100.4 ? 
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_555 100.5 ? 
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_555 109.4 ? 
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_555 125.0 ? 
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_555 105.1 ? 
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 96.6  ? 
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_555 117.5 ? 
# 
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 
# 
_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' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            citation 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  2 'Structure model' '_citation.country'                 
2  2 'Structure model' '_citation.journal_abbrev'          
3  2 'Structure model' '_citation.journal_id_CSD'          
4  2 'Structure model' '_citation.journal_id_ISSN'         
5  2 'Structure model' '_citation.journal_volume'          
6  2 'Structure model' '_citation.page_first'              
7  2 'Structure model' '_citation.page_last'               
8  2 'Structure model' '_citation.pdbx_database_id_DOI'    
9  2 'Structure model' '_citation.pdbx_database_id_PubMed' 
10 2 'Structure model' '_citation.title'                   
11 2 'Structure model' '_citation.year'                    
# 
loop_
_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 SG  A CYS 111 ? ? SE1 A 9JT 503 ? ? 1.87 
2 1 SG  F CYS 111 ? ? SE1 F 9JT 503 ? ? 1.87 
3 1 OD1 F ASN 26  ? ? O   F HOH 601 ? ? 1.89 
4 1 CG  F ASN 26  ? ? O   F HOH 601 ? ? 1.94 
5 1 OD1 F ASN 26  ? ? O   F HOH 602 ? ? 1.95 
6 1 ND2 F ASN 26  ? ? O   F HOH 601 ? ? 2.04 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 NZ A LYS 136 ? ? 1_555 O F HOH 661 ? ? 2_645 0.59 
2 1 CE A LYS 136 ? ? 1_555 O F HOH 661 ? ? 2_645 1.69 
# 
_pdbx_validate_rmsd_bond.id                        1 
_pdbx_validate_rmsd_bond.PDB_model_num             1 
_pdbx_validate_rmsd_bond.auth_atom_id_1            CG 
_pdbx_validate_rmsd_bond.auth_asym_id_1            A 
_pdbx_validate_rmsd_bond.auth_comp_id_1            GLU 
_pdbx_validate_rmsd_bond.auth_seq_id_1             132 
_pdbx_validate_rmsd_bond.PDB_ins_code_1            ? 
_pdbx_validate_rmsd_bond.label_alt_id_1            ? 
_pdbx_validate_rmsd_bond.auth_atom_id_2            CD 
_pdbx_validate_rmsd_bond.auth_asym_id_2            A 
_pdbx_validate_rmsd_bond.auth_comp_id_2            GLU 
_pdbx_validate_rmsd_bond.auth_seq_id_2             132 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            ? 
_pdbx_validate_rmsd_bond.bond_value                1.412 
_pdbx_validate_rmsd_bond.bond_target_value         1.515 
_pdbx_validate_rmsd_bond.bond_deviation            -0.103 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.015 
_pdbx_validate_rmsd_bond.linker_flag               N 
# 
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-selanyl-benzamide' 9JT 
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 SAXS                ? 
2 1 'mass spectrometry' ? 
3 1 'gel filtration'    ? 
# 
