data_6Z3V
# 
_entry.id   6Z3V 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.332 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   6Z3V         
WWPDB D_1292108848 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        6Z3V 
_pdbx_database_status.recvd_initial_deposition_date   2020-05-22 
_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.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Amporndanai, K.' 1 0000-0001-8527-9394 
'Hasnain, S.S.'   2 0000-0002-2854-4718 
# 
_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                   NE 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Ebiomedicine 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2352-3964 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            59 
_citation.language                  ? 
_citation.page_first                102980 
_citation.page_last                 102980 
_citation.title                     
'Novel Selenium-based compounds with therapeutic potential for SOD1-linked amyotrophic lateral sclerosis.' 
_citation.year                      2020 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.ebiom.2020.102980 
_citation.pdbx_database_id_PubMed   32862101 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Amporndanai, K.' 1 ? 
primary 'Rogers, M.'      2 ? 
primary 'Watanabe, S.'    3 ? 
primary 'Yamanaka, K.'    4 ? 
primary 
;O'Neill, P.M.
;
5 ? 
primary 'Hasnain, S.S.'   6 ? 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   106.870 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     6Z3V 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     39.070 
_cell.length_a_esd                 ? 
_cell.length_b                     68.090 
_cell.length_b_esd                 ? 
_cell.length_c                     50.860 
_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                         6Z3V 
_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]'                                          15855.613 2   1.15.1.1 A4V ? ? 
2 non-polymer syn 'ZINC ION'                                                              65.409    4   ?        ?   ? ? 
3 non-polymer syn '5-fluoranyl-~{N}-(3-morpholin-4-ylcarbonylphenyl)-2-selanyl-benzamide' 407.298   2   ?        ?   ? ? 
4 non-polymer syn 'SULFATE ION'                                                           96.063    5   ?        ?   ? ? 
5 water       nat water                                                                   18.015    288 ?        ?   ? ? 
# 
_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       
;ATKVVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;ATKVVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_entity_poly.pdbx_strand_id                 AAA,BBB 
_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   VAL 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 BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_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                       pET303C 
_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 6Z3V AAA 1 ? 153 ? P00441 2 ? 154 ? 1 153 
2 1 6Z3V BBB 1 ? 153 ? P00441 2 ? 154 ? 1 153 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 6Z3V VAL AAA 4 ? UNP P00441 ALA 5 'engineered mutation' 4 1 
2 6Z3V VAL BBB 4 ? UNP P00441 ALA 5 'engineered mutation' 4 2 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                                                                 ? 'C3 H7 N O2'         89.093  
ARG 'L-peptide linking' y ARGININE                                                                ? 'C6 H15 N4 O2 1'     175.209 
ASN 'L-peptide linking' y ASPARAGINE                                                              ? 'C4 H8 N2 O3'        132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                                                         ? 'C4 H7 N O4'         133.103 
CYS 'L-peptide linking' y CYSTEINE                                                                ? 'C3 H7 N O2 S'       121.158 
GLN 'L-peptide linking' y GLUTAMINE                                                               ? 'C5 H10 N2 O3'       146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                                                         ? 'C5 H9 N O4'         147.129 
GLY 'peptide linking'   y GLYCINE                                                                 ? 'C2 H5 N O2'         75.067  
HIS 'L-peptide linking' y HISTIDINE                                                               ? 'C6 H10 N3 O2 1'     156.162 
HOH non-polymer         . WATER                                                                   ? 'H2 O'               18.015  
ILE 'L-peptide linking' y ISOLEUCINE                                                              ? 'C6 H13 N O2'        131.173 
LEU 'L-peptide linking' y LEUCINE                                                                 ? 'C6 H13 N O2'        131.173 
LYS 'L-peptide linking' y LYSINE                                                                  ? 'C6 H15 N2 O2 1'     147.195 
PHE 'L-peptide linking' y PHENYLALANINE                                                           ? 'C9 H11 N O2'        165.189 
PRO 'L-peptide linking' y PROLINE                                                                 ? 'C5 H9 N O2'         115.130 
Q6H non-polymer         . '5-fluoranyl-~{N}-(3-morpholin-4-ylcarbonylphenyl)-2-selanyl-benzamide' ? 'C18 H17 F N2 O3 Se' 407.298 
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                   6Z3V 
_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            2.04 
_exptl_crystal.density_method              ? 
_exptl_crystal.density_percent_sol         39.75 
_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              4.7 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp            292 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '100mM NaOAc pH 4.7, 150mM NaCl, 2.7M ammonium sulphate' 
_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.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      mirrors 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS3 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         2020-01-26 
_diffrn_detector.pdbx_frequency               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    'Double crystal' 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9686 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'DIAMOND BEAMLINE I24' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9686 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I24 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate            7.912 
_reflns.entry_id                         6Z3V 
_reflns.data_reduction_details           ? 
_reflns.data_reduction_method            ? 
_reflns.d_resolution_high                1.25 
_reflns.d_resolution_low                 39.60 
_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                       69892 
_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             92.3 
_reflns.R_free_details                   ? 
_reflns.Rmerge_F_all                     ? 
_reflns.Rmerge_F_obs                     ? 
_reflns.Friedel_coverage                 ? 
_reflns.number_gt                        ? 
_reflns.threshold_expression             ? 
_reflns.pdbx_redundancy                  3.2 
_reflns.pdbx_Rmerge_I_obs                0.078 
_reflns.pdbx_Rmerge_I_all                ? 
_reflns.pdbx_Rsym_value                  ? 
_reflns.pdbx_netI_over_av_sigmaI         ? 
_reflns.pdbx_netI_over_sigmaI            8.0 
_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                  0.106 
_reflns.pdbx_Rpim_I_all                  0.072 
_reflns.pdbx_d_opt                       ? 
_reflns.pdbx_number_measured_all         ? 
_reflns.pdbx_diffrn_id                   1 
_reflns.pdbx_ordinal                     1 
_reflns.pdbx_CC_half                     0.999 
_reflns.pdbx_CC_star                     ? 
_reflns.pdbx_R_split                     ? 
# 
_reflns_shell.d_res_high                  1.25 
_reflns_shell.d_res_low                   1.27 
_reflns_shell.meanI_over_sigI_all         ? 
_reflns_shell.meanI_over_sigI_obs         2.2 
_reflns_shell.number_measured_all         ? 
_reflns_shell.number_measured_obs         ? 
_reflns_shell.number_possible             ? 
_reflns_shell.number_unique_all           ? 
_reflns_shell.number_unique_obs           3562 
_reflns_shell.percent_possible_all        99.3 
_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                0.562 
_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             3.2 
_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             0.756 
_reflns_shell.pdbx_Rpim_I_all             0.501 
_reflns_shell.pdbx_rejects                ? 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_CC_half                0.524 
_reflns_shell.pdbx_CC_star                ? 
_reflns_shell.pdbx_R_split                ? 
# 
_refine.aniso_B[1][1]                            0.224 
_refine.aniso_B[1][2]                            0.000 
_refine.aniso_B[1][3]                            0.196 
_refine.aniso_B[2][2]                            -0.412 
_refine.aniso_B[2][3]                            0.000 
_refine.aniso_B[3][3]                            0.058 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               13.096 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.965 
_refine.correlation_coeff_Fo_to_Fc_free          0.962 
_refine.details                                  'Hydrogens have been added in their 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                                 6Z3V 
_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                            1.25 
_refine.ls_d_res_low                             39.60 
_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                     69865 
_refine.ls_number_reflns_R_free                  3480 
_refine.ls_number_reflns_R_work                  66385 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.281 
_refine.ls_percent_reflns_R_free                 4.981 
_refine.ls_R_factor_all                          0.178 
_refine.ls_R_factor_obs                          ? 
_refine.ls_R_factor_R_free                       0.1912 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1776 
_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                    'MASK BULK SOLVENT' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      1UXM 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.049 
_refine.pdbx_overall_ESU_R_Free                  0.048 
_refine.pdbx_solvent_vdw_probe_radii             1.200 
_refine.pdbx_solvent_ion_probe_radii             0.800 
_refine.pdbx_solvent_shrinkage_radii             0.800 
_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                             0.799 
_refine.overall_SU_ML                            0.035 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        2220 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         79 
_refine_hist.number_atoms_solvent             288 
_refine_hist.number_atoms_total               2587 
_refine_hist.d_res_high                       1.25 
_refine_hist.d_res_low                        39.60 
# 
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' ? 0.015  0.013  2381  ? r_bond_refined_d               ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.017  2129  ? r_bond_other_d                 ? ? 
'X-RAY DIFFRACTION' ? 1.901  1.657  3228  ? r_angle_refined_deg            ? ? 
'X-RAY DIFFRACTION' ? 1.571  1.612  4973  ? r_angle_other_deg              ? ? 
'X-RAY DIFFRACTION' ? 7.079  5.000  318   ? r_dihedral_angle_1_deg         ? ? 
'X-RAY DIFFRACTION' ? 35.589 24.423 104   ? r_dihedral_angle_2_deg         ? ? 
'X-RAY DIFFRACTION' ? 11.760 15.000 378   ? r_dihedral_angle_3_deg         ? ? 
'X-RAY DIFFRACTION' ? 21.389 15.000 2     ? r_dihedral_angle_other_3_deg   ? ? 
'X-RAY DIFFRACTION' ? 14.327 15.000 8     ? r_dihedral_angle_4_deg         ? ? 
'X-RAY DIFFRACTION' ? 0.089  0.200  298   ? r_chiral_restr                 ? ? 
'X-RAY DIFFRACTION' ? 0.011  0.020  2770  ? r_gen_planes_refined           ? ? 
'X-RAY DIFFRACTION' ? 0.005  0.020  450   ? r_gen_planes_other             ? ? 
'X-RAY DIFFRACTION' ? 0.260  0.200  804   ? r_nbd_refined                  ? ? 
'X-RAY DIFFRACTION' ? 0.187  0.200  2097  ? r_symmetry_nbd_other           ? ? 
'X-RAY DIFFRACTION' ? 0.160  0.200  1163  ? r_nbtor_refined                ? ? 
'X-RAY DIFFRACTION' ? 0.085  0.200  1208  ? r_symmetry_nbtor_other         ? ? 
'X-RAY DIFFRACTION' ? 0.155  0.200  39    ? r_xyhbond_nbd_refined          ? ? 
'X-RAY DIFFRACTION' ? 0.209  0.200  9     ? r_metal_ion_refined            ? ? 
'X-RAY DIFFRACTION' ? 0.293  0.200  63    ? r_symmetry_nbd_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.242  0.200  75    ? r_nbd_other                    ? ? 
'X-RAY DIFFRACTION' ? 0.147  0.200  6     ? r_symmetry_xyhbond_nbd_refined ? ? 
'X-RAY DIFFRACTION' ? 1.221  1.127  1251  ? r_mcbond_it                    ? ? 
'X-RAY DIFFRACTION' ? 1.221  1.128  1252  ? r_mcbond_other                 ? ? 
'X-RAY DIFFRACTION' ? 1.856  1.698  1572  ? r_mcangle_it                   ? ? 
'X-RAY DIFFRACTION' ? 1.858  1.696  1571  ? r_mcangle_other                ? ? 
'X-RAY DIFFRACTION' ? 2.695  1.496  1130  ? r_scbond_it                    ? ? 
'X-RAY DIFFRACTION' ? 2.645  1.472  1111  ? r_scbond_other                 ? ? 
'X-RAY DIFFRACTION' ? 3.961  2.123  1654  ? r_scangle_it                   ? ? 
'X-RAY DIFFRACTION' ? 3.922  2.081  1625  ? r_scangle_other                ? ? 
'X-RAY DIFFRACTION' ? 4.442  23.617 10371 ? r_lrange_it                    ? ? 
'X-RAY DIFFRACTION' ? 4.287  23.027 10052 ? r_lrange_other                 ? ? 
'X-RAY DIFFRACTION' ? 0.127  0.050  4523  ? r_ncsr_local_group_1           ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
'X-RAY DIFFRACTION' 1.250 1.282 . . 255 4886 99.2279 . . . 0.319 . 0.315 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 1.282 1.318 . . 271 4730 99.5818 . . . 0.291 . 0.269 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 1.318 1.356 . . 251 4670 99.6154 . . . 0.266 . 0.233 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 1.356 1.397 . . 240 4552 99.7710 . . . 0.209 . 0.215 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 1.397 1.443 . . 230 4361 99.7827 . . . 0.208 . 0.188 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 1.443 1.494 . . 234 4224 99.7315 . . . 0.213 . 0.177 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 1.494 1.550 . . 203 4126 99.7236 . . . 0.203 . 0.176 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 1.550 1.613 . . 194 3958 99.8797 . . . 0.204 . 0.171 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 1.613 1.685 . . 218 3741 99.3974 . . . 0.191 . 0.164 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 1.685 1.767 . . 211 3590 99.3985 . . . 0.178 . 0.163 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 1.767 1.863 . . 162 3446 98.7681 . . . 0.178 . 0.163 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 1.863 1.975 . . 179 3199 98.7719 . . . 0.169 . 0.158 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 1.975 2.112 . . 153 3051 98.9805 . . . 0.180 . 0.164 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 2.112 2.280 . . 143 2839 98.8399 . . . 0.181 . 0.162 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 2.280 2.498 . . 131 2620 98.8147 . . . 0.208 . 0.169 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 2.498 2.791 . . 91  2392 98.4146 . . . 0.199 . 0.178 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 2.791 3.221 . . 113 2081 98.3857 . . . 0.150 . 0.168 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 3.221 3.941 . . 99  1756 98.5654 . . . 0.172 . 0.160 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 3.941 5.555 . . 62  1381 98.4311 . . . 0.133 . 0.165 . . . . . . . . . . . 
'X-RAY DIFFRACTION' 5.555 39.60 . . 40  782  98.2079 . . . 0.249 . 0.224 . . . . . . . . . . . 
# 
_struct_ncs_dom.id            1 
_struct_ncs_dom.details       'Chains AAA BBB' 
_struct_ncs_dom.pdbx_ens_id   1 
# 
_struct_ncs_ens.details       ? 
_struct_ncs_ens.id            1 
_struct_ncs_ens.point_group   ? 
# 
_struct.entry_id                     6Z3V 
_struct.title                        
'A4V mutant of human SOD1 bound with N-aryl benzoisoselenazolone derivative 13 in P21 space group' 
_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        6Z3V 
_struct_keywords.text            'SOD1, Motor neuron disease, ebselen, OXIDOREDUCTASE' 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 2 ? 
F N N 4 ? 
G N N 4 ? 
H N N 2 ? 
I N N 3 ? 
J N N 2 ? 
K N N 4 ? 
L N N 4 ? 
M N N 4 ? 
N N N 5 ? 
O 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 CYS A 57  ? GLY A 61  ? CYS AAA 57  GLY AAA 61  5 ? 5 
HELX_P HELX_P2 AA2 SER A 107 ? CYS A 111 ? SER AAA 107 CYS AAA 111 5 ? 5 
HELX_P HELX_P3 AA3 GLU A 133 ? GLY A 138 ? GLU AAA 133 GLY AAA 138 1 ? 6 
HELX_P HELX_P4 AA4 GLY B 56  ? GLY B 61  ? GLY BBB 56  GLY BBB 61  5 ? 6 
HELX_P HELX_P5 AA5 GLU B 133 ? GLY B 138 ? GLU BBB 133 GLY BBB 138 1 ? 6 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1  disulf ?    ? A CYS 57  SG  ? ? ? 1_555 A CYS 146 SG ? ? AAA CYS 57  AAA CYS 146 1_555 ? ? ? ? ? ? ? 2.125 ? ? 
disulf2  disulf ?    ? B CYS 57  SG  ? ? ? 1_555 B CYS 146 SG ? ? BBB CYS 57  BBB CYS 146 1_555 ? ? ? ? ? ? ? 2.119 ? ? 
covale1  covale none ? A CYS 111 SG  ? ? ? 1_555 D Q6H .   SE ? ? AAA CYS 111 AAA Q6H 202 1_555 ? ? ? ? ? ? ? 2.270 ? ? 
covale2  covale none ? B CYS 111 SG  ? ? ? 1_555 I Q6H .   SE ? ? BBB CYS 111 BBB Q6H 202 1_555 ? ? ? ? ? ? ? 2.283 ? ? 
metalc1  metalc ?    ? A HIS 48  NE2 ? ? ? 1_555 E ZN  .   ZN ? ? AAA HIS 48  AAA ZN  203 1_555 ? ? ? ? ? ? ? 2.068 ? ? 
metalc2  metalc ?    ? A HIS 63  ND1 ? ? ? 1_555 C ZN  .   ZN ? ? AAA HIS 63  AAA ZN  201 1_555 ? ? ? ? ? ? ? 1.990 ? ? 
metalc3  metalc ?    ? A HIS 71  ND1 ? ? ? 1_555 C ZN  .   ZN ? ? AAA HIS 71  AAA ZN  201 1_555 ? ? ? ? ? ? ? 2.049 ? ? 
metalc4  metalc ?    ? A HIS 80  ND1 ? ? ? 1_555 C ZN  .   ZN ? ? AAA HIS 80  AAA ZN  201 1_555 ? ? ? ? ? ? ? 2.046 ? ? 
metalc5  metalc ?    ? A ASP 83  OD1 ? ? ? 1_555 C ZN  .   ZN ? ? AAA ASP 83  AAA ZN  201 1_555 ? ? ? ? ? ? ? 1.956 ? ? 
metalc6  metalc ?    ? E ZN  .   ZN  ? ? ? 1_555 G SO4 .   O1 ? ? AAA ZN  203 AAA SO4 205 1_555 ? ? ? ? ? ? ? 2.119 ? ? 
metalc7  metalc ?    ? B HIS 46  ND1 ? ? ? 1_555 J ZN  .   ZN ? ? BBB HIS 46  BBB ZN  203 1_555 ? ? ? ? ? ? ? 2.577 ? ? 
metalc8  metalc ?    ? B HIS 48  NE2 ? ? ? 1_555 J ZN  .   ZN ? ? BBB HIS 48  BBB ZN  203 1_555 ? ? ? ? ? ? ? 2.092 ? ? 
metalc9  metalc ?    ? B HIS 63  ND1 ? ? ? 1_555 H ZN  .   ZN ? ? BBB HIS 63  BBB ZN  201 1_555 ? ? ? ? ? ? ? 2.003 ? ? 
metalc10 metalc ?    ? B HIS 71  ND1 ? ? ? 1_555 H ZN  .   ZN ? ? BBB HIS 71  BBB ZN  201 1_555 ? ? ? ? ? ? ? 2.056 ? ? 
metalc11 metalc ?    ? B HIS 80  ND1 ? ? ? 1_555 H ZN  .   ZN ? ? BBB HIS 80  BBB ZN  201 1_555 ? ? ? ? ? ? ? 2.029 ? ? 
metalc12 metalc ?    ? B ASP 83  OD1 ? ? ? 1_555 H ZN  .   ZN ? ? BBB ASP 83  BBB ZN  201 1_555 ? ? ? ? ? ? ? 2.022 ? ? 
metalc13 metalc ?    ? J ZN  .   ZN  ? ? ? 1_555 M SO4 .   O4 ? ? BBB ZN  203 BBB SO4 206 1_555 ? ? ? ? ? ? ? 2.103 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
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          A 
_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           AAA 
_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   A 
_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    AAA 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       -2.74 
# 
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 AAA 95  ASP AAA 101 
AA1 2 VAL A 29  ? LYS A 36  ? VAL AAA 29  LYS AAA 36  
AA1 3 VAL A 14  ? GLN A 22  ? VAL AAA 14  GLN AAA 22  
AA1 4 THR A 2   ? GLY A 10  ? THR AAA 2   GLY AAA 10  
AA1 5 GLY A 150 ? ILE A 151 ? GLY AAA 150 ILE AAA 151 
AA2 1 ASP A 83  ? ALA A 89  ? ASP AAA 83  ALA AAA 89  
AA2 2 GLY A 41  ? HIS A 48  ? GLY AAA 41  HIS AAA 48  
AA2 3 THR A 116 ? HIS A 120 ? THR AAA 116 HIS AAA 120 
AA2 4 ARG A 143 ? VAL A 148 ? ARG AAA 143 VAL AAA 148 
AA3 1 ALA B 95  ? ASP B 101 ? ALA BBB 95  ASP BBB 101 
AA3 2 VAL B 29  ? LYS B 36  ? VAL BBB 29  LYS BBB 36  
AA3 3 GLN B 15  ? GLN B 22  ? GLN BBB 15  GLN BBB 22  
AA3 4 THR B 2   ? LYS B 9   ? THR BBB 2   LYS BBB 9   
AA3 5 GLY B 150 ? ILE B 151 ? GLY BBB 150 ILE BBB 151 
AA4 1 ASP B 83  ? ALA B 89  ? ASP BBB 83  ALA BBB 89  
AA4 2 GLY B 41  ? HIS B 48  ? GLY BBB 41  HIS BBB 48  
AA4 3 THR B 116 ? HIS B 120 ? THR BBB 116 HIS BBB 120 
AA4 4 ARG B 143 ? VAL B 148 ? ARG BBB 143 VAL BBB 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 ASP A 101 ? O ASP AAA 101 N VAL A 29  ? N VAL AAA 29  
AA1 2 3 O TRP A 32  ? O TRP AAA 32  N ASN A 19  ? N ASN AAA 19  
AA1 3 4 O PHE A 20  ? O PHE AAA 20  N VAL A 4   ? N VAL AAA 4   
AA1 4 5 N VAL A 5   ? N VAL AAA 5   O GLY A 150 ? O GLY AAA 150 
AA2 1 2 O ALA A 89  ? O ALA AAA 89  N GLY A 41  ? N GLY AAA 41  
AA2 2 3 N HIS A 48  ? N HIS AAA 48  O THR A 116 ? O THR AAA 116 
AA2 3 4 N LEU A 117 ? N LEU AAA 117 O GLY A 147 ? O GLY AAA 147 
AA3 1 2 O ALA B 95  ? O ALA BBB 95  N ILE B 35  ? N ILE BBB 35  
AA3 2 3 O TRP B 32  ? O TRP BBB 32  N ASN B 19  ? N ASN BBB 19  
AA3 3 4 O PHE B 20  ? O PHE BBB 20  N VAL B 4   ? N VAL BBB 4   
AA3 4 5 N VAL B 5   ? N VAL BBB 5   O GLY B 150 ? O GLY BBB 150 
AA4 1 2 O ALA B 89  ? O ALA BBB 89  N GLY B 41  ? N GLY BBB 41  
AA4 2 3 N HIS B 48  ? N HIS BBB 48  O THR B 116 ? O THR BBB 116 
AA4 3 4 N LEU B 117 ? N LEU BBB 117 O GLY B 147 ? O GLY BBB 147 
# 
_atom_sites.entry_id                    6Z3V 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.fract_transf_matrix[1][1]   0.025595 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.007762 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.014686 
_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]   0.020546 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
C  2.310  20.844 1.020 10.208 1.589 0.569  0.865 51.651 0.216   
F  3.539  10.282 2.641 4.294  1.517 0.262  1.024 26.148 0.304   
H  0.493  10.511 0.323 26.126 0.140 3.142  0.041 57.800 0.003   
N  12.222 0.006  3.135 9.893  2.014 28.997 1.167 0.583  -11.538 
O  3.049  13.277 2.287 5.701  1.546 0.324  0.867 32.909 0.251   
S  6.905  1.468  5.203 22.215 1.438 0.254  1.586 56.172 1.046   
SE 17.006 2.410  5.822 0.273  3.974 15.237 4.356 43.816 -1.064  
ZN 14.082 3.266  7.036 0.233  5.165 10.316 2.411 58.710 1.030   
# 
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   ? 17.205  -6.399  3.354   1.000 30.387 ? 1   ALA AAA N   1 
ATOM   2    C  CA  . ALA A 1 1   ? 16.207  -5.289  3.135   1.000 28.107 ? 1   ALA AAA CA  1 
ATOM   3    C  C   . ALA A 1 1   ? 15.080  -5.346  4.181   1.000 23.147 ? 1   ALA AAA C   1 
ATOM   4    O  O   . ALA A 1 1   ? 14.701  -6.430  4.635   1.000 26.860 ? 1   ALA AAA O   1 
ATOM   5    C  CB  . ALA A 1 1   ? 15.623  -5.343  1.746   1.000 29.642 ? 1   ALA AAA CB  1 
ATOM   6    N  N   . THR A 1 2   ? 14.597  -4.178  4.580   1.000 15.959 ? 2   THR AAA N   1 
ATOM   7    C  CA  . THR A 1 2   ? 13.481  -4.015  5.525   1.000 14.156 ? 2   THR AAA CA  1 
ATOM   8    C  C   . THR A 1 2   ? 12.264  -3.554  4.721   1.000 12.587 ? 2   THR AAA C   1 
ATOM   9    O  O   . THR A 1 2   ? 12.360  -2.625  3.884   1.000 11.955 ? 2   THR AAA O   1 
ATOM   10   C  CB  . THR A 1 2   ? 13.834  -3.004  6.611   1.000 15.867 ? 2   THR AAA CB  1 
ATOM   11   O  OG1 . THR A 1 2   ? 15.028  -3.500  7.226   1.000 20.160 ? 2   THR AAA OG1 1 
ATOM   12   C  CG2 . THR A 1 2   ? 12.748  -2.844  7.645   1.000 17.729 ? 2   THR AAA CG2 1 
ATOM   13   N  N   . LYS A 1 3   ? 11.111  -4.171  4.976   1.000 10.595 ? 3   LYS AAA N   1 
ATOM   14   C  CA  . LYS A 1 3   ? 9.847   -3.878  4.272   1.000 10.530 ? 3   LYS AAA CA  1 
ATOM   15   C  C   . LYS A 1 3   ? 8.794   -3.540  5.334   1.000 9.208  ? 3   LYS AAA C   1 
ATOM   16   O  O   . LYS A 1 3   ? 8.673   -4.264  6.355   1.000 9.082  ? 3   LYS AAA O   1 
ATOM   17   C  CB  . LYS A 1 3   ? 9.376   -5.068  3.435   1.000 13.090 ? 3   LYS AAA CB  1 
ATOM   18   C  CG  . LYS A 1 3   ? 10.310  -5.458  2.297   1.000 18.613 ? 3   LYS AAA CG  1 
ATOM   19   C  CD  . LYS A 1 3   ? 9.933   -6.794  1.654   1.000 22.749 ? 3   LYS AAA CD  1 
ATOM   20   C  CE  . LYS A 1 3   ? 10.983  -7.274  0.671   1.000 29.106 ? 3   LYS AAA CE  1 
ATOM   21   N  NZ  . LYS A 1 3   ? 10.748  -8.662  0.213   1.000 34.089 ? 3   LYS AAA NZ  1 
ATOM   22   N  N   . VAL A 1 4   ? 8.062   -2.473  5.103   1.000 7.889  ? 4   VAL AAA N   1 
ATOM   23   C  CA  . VAL A 1 4   ? 7.057   -1.880  6.014   1.000 7.874  ? 4   VAL AAA CA  1 
ATOM   24   C  C   . VAL A 1 4   ? 5.823   -1.520  5.215   1.000 8.365  ? 4   VAL AAA C   1 
ATOM   25   O  O   . VAL A 1 4   ? 5.933   -1.385  3.972   1.000 8.267  ? 4   VAL AAA O   1 
ATOM   26   C  CB  . VAL A 1 4   ? 7.745   -0.709  6.726   1.000 9.523  ? 4   VAL AAA CB  1 
ATOM   27   C  CG1 . VAL A 1 4   ? 6.812   0.371   7.222   1.000 10.385 ? 4   VAL AAA CG1 1 
ATOM   28   C  CG2 . VAL A 1 4   ? 8.707   -1.195  7.784   1.000 9.759  ? 4   VAL AAA CG2 1 
ATOM   29   N  N   . VAL A 1 5   ? 4.662   -1.480  5.847   1.000 7.433  ? 5   VAL AAA N   1 
ATOM   30   C  CA  . VAL A 1 5   ? 3.412   -1.257  5.093   1.000 8.012  ? 5   VAL AAA CA  1 
ATOM   31   C  C   . VAL A 1 5   ? 2.462   -0.455  5.958   1.000 7.989  ? 5   VAL AAA C   1 
ATOM   32   O  O   . VAL A 1 5   ? 2.531   -0.484  7.211   1.000 9.040  ? 5   VAL AAA O   1 
ATOM   33   C  CB  . VAL A 1 5   ? 2.830   -2.613  4.680   1.000 8.864  ? 5   VAL AAA CB  1 
ATOM   34   C  CG1 . VAL A 1 5   ? 2.446   -3.438  5.895   1.000 9.409  ? 5   VAL AAA CG1 1 
ATOM   35   C  CG2 . VAL A 1 5   ? 1.677   -2.523  3.692   1.000 11.187 ? 5   VAL AAA CG2 1 
ATOM   36   N  N   . CYS A 1 6   ? 1.562   0.235   5.320   1.000 8.255  ? 6   CYS AAA N   1 
ATOM   37   C  CA  . CYS A 1 6   ? 0.505   0.980   5.997   1.000 7.904  ? 6   CYS AAA CA  1 
ATOM   38   C  C   . CYS A 1 6   ? -0.776  0.908   5.192   1.000 7.993  ? 6   CYS AAA C   1 
ATOM   39   O  O   . CYS A 1 6   ? -0.761  1.220   3.991   1.000 8.189  ? 6   CYS AAA O   1 
ATOM   40   C  CB  . CYS A 1 6   ? 0.926   2.430   6.173   1.000 8.260  ? 6   CYS AAA CB  1 
ATOM   41   S  SG  . CYS A 1 6   ? -0.209  3.383   7.204   1.000 9.905  ? 6   CYS AAA SG  1 
ATOM   42   N  N   . VAL A 1 7   ? -1.867  0.609   5.841   1.000 7.630  ? 7   VAL AAA N   1 
ATOM   43   C  CA  . VAL A 1 7   ? -3.216  0.585   5.230   1.000 8.125  ? 7   VAL AAA CA  1 
ATOM   44   C  C   . VAL A 1 7   ? -3.903  1.851   5.698   1.000 8.689  ? 7   VAL AAA C   1 
ATOM   45   O  O   . VAL A 1 7   ? -4.093  2.066   6.898   1.000 9.627  ? 7   VAL AAA O   1 
ATOM   46   C  CB  . VAL A 1 7   ? -4.008  -0.672  5.599   1.000 9.554  ? 7   VAL AAA CB  1 
ATOM   47   C  CG1 . VAL A 1 7   ? -5.406  -0.589  5.032   1.000 9.357  ? 7   VAL AAA CG1 1 
ATOM   48   C  CG2 . VAL A 1 7   ? -3.259  -1.895  5.158   1.000 10.710 ? 7   VAL AAA CG2 1 
ATOM   49   N  N   . LEU A 1 8   ? -4.255  2.701   4.765   1.000 9.088  ? 8   LEU AAA N   1 
ATOM   50   C  CA  . LEU A 1 8   ? -4.924  3.984   5.063   1.000 9.450  ? 8   LEU AAA CA  1 
ATOM   51   C  C   . LEU A 1 8   ? -6.429  3.783   4.994   1.000 10.044 ? 8   LEU AAA C   1 
ATOM   52   O  O   . LEU A 1 8   ? -6.919  3.332   3.930   1.000 10.430 ? 8   LEU AAA O   1 
ATOM   53   C  CB  . LEU A 1 8   ? -4.503  5.042   4.043   1.000 9.727  ? 8   LEU AAA CB  1 
ATOM   54   C  CG  . LEU A 1 8   ? -3.027  5.414   4.053   1.000 11.194 ? 8   LEU AAA CG  1 
ATOM   55   C  CD1 . LEU A 1 8   ? -2.700  6.360   2.901   1.000 11.315 ? 8   LEU AAA CD1 1 
ATOM   56   C  CD2 . LEU A 1 8   ? -2.604  6.072   5.349   1.000 11.700 ? 8   LEU AAA CD2 1 
ATOM   57   N  N   . LYS A 1 9   ? -7.156  4.235   5.982   1.000 9.565  ? 9   LYS AAA N   1 
ATOM   58   C  CA  . LYS A 1 9   ? -8.635  4.161   5.970   1.000 11.474 ? 9   LYS AAA CA  1 
ATOM   59   C  C   . LYS A 1 9   ? -9.180  5.415   6.621   1.000 11.838 ? 9   LYS AAA C   1 
ATOM   60   O  O   . LYS A 1 9   ? -8.557  5.928   7.585   1.000 12.395 ? 9   LYS AAA O   1 
ATOM   61   C  CB  . LYS A 1 9   ? -9.129  2.939   6.741   1.000 13.820 ? 9   LYS AAA CB  1 
ATOM   62   C  CG  . LYS A 1 9   ? -8.896  1.612   6.059   1.000 16.888 ? 9   LYS AAA CG  1 
ATOM   63   C  CD  . LYS A 1 9   ? -9.675  0.447   6.700   1.000 21.974 ? 9   LYS AAA CD  1 
ATOM   64   C  CE  . LYS A 1 9   ? -9.959  -0.671  5.707   1.000 28.031 ? 9   LYS AAA CE  1 
ATOM   65   N  NZ  . LYS A 1 9   ? -9.053  -1.824  5.904   1.000 31.592 ? 9   LYS AAA NZ  1 
ATOM   66   N  N   . GLY A 1 10  ? -10.302 5.838   6.001   0.800 12.834 ? 10  GLY AAA N   1 
ATOM   67   C  CA  . GLY A 1 10  ? -11.116 7.018   6.297   0.800 13.963 ? 10  GLY AAA CA  1 
ATOM   68   C  C   . GLY A 1 10  ? -12.415 7.029   5.503   0.800 14.661 ? 10  GLY AAA C   1 
ATOM   69   O  O   . GLY A 1 10  ? -12.587 6.255   4.518   0.800 15.293 ? 10  GLY AAA O   1 
ATOM   70   N  N   . ASP A 1 11  ? -13.268 7.961   5.885   1.000 17.970 ? 11  ASP AAA N   1 
ATOM   71   C  CA  . ASP A 1 11  ? -14.628 8.184   5.340   1.000 18.359 ? 11  ASP AAA CA  1 
ATOM   72   C  C   . ASP A 1 11  ? -14.580 8.547   3.851   1.000 19.822 ? 11  ASP AAA C   1 
ATOM   73   O  O   . ASP A 1 11  ? -13.734 9.406   3.407   1.000 19.030 ? 11  ASP AAA O   1 
ATOM   74   C  CB  . ASP A 1 11  ? -15.295 9.310   6.112   1.000 23.847 ? 11  ASP AAA CB  1 
ATOM   75   C  CG  . ASP A 1 11  ? -16.106 8.736   7.238   1.000 28.700 ? 11  ASP AAA CG  1 
ATOM   76   O  OD1 . ASP A 1 11  ? -16.556 7.603   7.065   1.000 33.395 ? 11  ASP AAA OD1 1 
ATOM   77   O  OD2 . ASP A 1 11  ? -16.258 9.417   8.250   1.000 33.641 ? 11  ASP AAA OD2 1 
ATOM   78   N  N   . GLY A 1 12  ? -15.449 7.947   3.057   0.800 20.890 ? 12  GLY AAA N   1 
ATOM   79   C  CA  . GLY A 1 12  ? -15.597 8.337   1.638   0.800 21.011 ? 12  GLY AAA CA  1 
ATOM   80   C  C   . GLY A 1 12  ? -16.078 7.178   0.770   0.800 19.391 ? 12  GLY AAA C   1 
ATOM   81   O  O   . GLY A 1 12  ? -17.131 7.312   0.132   0.800 20.504 ? 12  GLY AAA O   1 
ATOM   82   N  N   . PRO A 1 13  ? -15.399 5.996   0.691   0.800 18.375 ? 13  PRO AAA N   1 
ATOM   83   C  CA  . PRO A 1 13  ? -14.119 5.701   1.362   0.800 17.550 ? 13  PRO AAA CA  1 
ATOM   84   C  C   . PRO A 1 13  ? -12.852 6.371   0.775   0.800 15.403 ? 13  PRO AAA C   1 
ATOM   85   O  O   . PRO A 1 13  ? -12.651 6.318   -0.386  0.800 14.766 ? 13  PRO AAA O   1 
ATOM   86   C  CB  . PRO A 1 13  ? -13.963 4.164   1.165   0.800 18.659 ? 13  PRO AAA CB  1 
ATOM   87   C  CG  . PRO A 1 13  ? -15.316 3.658   0.663   0.800 20.462 ? 13  PRO AAA CG  1 
ATOM   88   C  CD  . PRO A 1 13  ? -15.896 4.832   -0.079  0.800 19.047 ? 13  PRO AAA CD  1 
ATOM   89   N  N   . VAL A 1 14  ? -12.008 7.002   1.589   1.000 18.365 ? 14  VAL AAA N   1 
ATOM   90   C  CA  . VAL A 1 14  ? -10.601 7.343   1.189   1.000 15.823 ? 14  VAL AAA CA  1 
ATOM   91   C  C   . VAL A 1 14  ? -9.795  6.169   1.677   1.000 14.557 ? 14  VAL AAA C   1 
ATOM   92   O  O   . VAL A 1 14  ? -9.799  5.969   2.891   1.000 18.236 ? 14  VAL AAA O   1 
ATOM   93   C  CB  . VAL A 1 14  ? -10.063 8.668   1.751   1.000 15.539 ? 14  VAL AAA CB  1 
ATOM   94   C  CG1 . VAL A 1 14  ? -8.563  8.866   1.511   1.000 16.159 ? 14  VAL AAA CG1 1 
ATOM   95   C  CG2 . VAL A 1 14  ? -10.812 9.848   1.191   1.000 16.544 ? 14  VAL AAA CG2 1 
ATOM   96   N  N   . GLN A 1 15  ? -9.220  5.370   0.805   1.000 14.597 ? 15  GLN AAA N   1 
ATOM   97   C  CA  . GLN A 1 15  ? -8.507  4.183   1.276   1.000 15.296 ? 15  GLN AAA CA  1 
ATOM   98   C  C   . GLN A 1 15  ? -7.273  3.974   0.431   1.000 13.470 ? 15  GLN AAA C   1 
ATOM   99   O  O   . GLN A 1 15  ? -7.283  4.297   -0.766  1.000 14.655 ? 15  GLN AAA O   1 
ATOM   100  C  CB  . GLN A 1 15  ? -9.432  2.986   1.282   1.000 21.115 ? 15  GLN AAA CB  1 
ATOM   101  C  CG  . GLN A 1 15  ? -9.793  2.476   -0.079  1.000 24.019 ? 15  GLN AAA CG  1 
ATOM   102  C  CD  . GLN A 1 15  ? -10.694 1.284   0.126   1.000 30.458 ? 15  GLN AAA CD  1 
ATOM   103  O  OE1 . GLN A 1 15  ? -11.784 1.413   0.689   1.000 34.332 ? 15  GLN AAA OE1 1 
ATOM   104  N  NE2 . GLN A 1 15  ? -10.208 0.115   -0.269  1.000 34.589 ? 15  GLN AAA NE2 1 
ATOM   105  N  N   . GLY A 1 16  ? -6.237  3.427   1.020   1.000 11.180 ? 16  GLY AAA N   1 
ATOM   106  C  CA  . GLY A 1 16  ? -4.981  3.289   0.311   1.000 12.397 ? 16  GLY AAA CA  1 
ATOM   107  C  C   . GLY A 1 16  ? -4.121  2.224   0.935   1.000 10.423 ? 16  GLY AAA C   1 
ATOM   108  O  O   . GLY A 1 16  ? -4.376  1.788   2.113   1.000 11.160 ? 16  GLY AAA O   1 
ATOM   109  N  N   . ILE A 1 17  ? -3.119  1.843   0.203   1.000 9.573  ? 17  ILE AAA N   1 
ATOM   110  C  CA  . ILE A 1 17  ? -2.110  0.844   0.646   1.000 10.050 ? 17  ILE AAA CA  1 
ATOM   111  C  C   . ILE A 1 17  ? -0.776  1.433   0.283   1.000 9.510  ? 17  ILE AAA C   1 
ATOM   112  O  O   . ILE A 1 17  ? -0.530  1.755   -0.927  1.000 9.989  ? 17  ILE AAA O   1 
ATOM   113  C  CB  . ILE A 1 17  ? -2.323  -0.534  -0.019  1.000 12.763 ? 17  ILE AAA CB  1 
ATOM   114  C  CG1 . ILE A 1 17  ? -3.700  -1.136  0.247   1.000 18.208 ? 17  ILE AAA CG1 1 
ATOM   115  C  CG2 . ILE A 1 17  ? -1.230  -1.490  0.375   1.000 13.880 ? 17  ILE AAA CG2 1 
ATOM   116  C  CD1 . ILE A 1 17  ? -3.829  -1.811  1.597   1.000 20.019 ? 17  ILE AAA CD1 1 
ATOM   117  N  N   . ILE A 1 18  ? 0.093   1.632   1.257   1.000 8.185  ? 18  ILE AAA N   1 
ATOM   118  C  CA  . ILE A 1 18  ? 1.420   2.269   1.029   1.000 8.573  ? 18  ILE AAA CA  1 
ATOM   119  C  C   . ILE A 1 18  ? 2.507   1.324   1.518   1.000 8.582  ? 18  ILE AAA C   1 
ATOM   120  O  O   . ILE A 1 18  ? 2.440   0.835   2.691   1.000 9.571  ? 18  ILE AAA O   1 
ATOM   121  C  CB  . ILE A 1 18  ? 1.535   3.644   1.700   1.000 8.804  ? 18  ILE AAA CB  1 
ATOM   122  C  CG1 . ILE A 1 18  ? 0.405   4.581   1.260   1.000 9.704  ? 18  ILE AAA CG1 1 
ATOM   123  C  CG2 . ILE A 1 18  ? 2.913   4.214   1.455   1.000 9.049  ? 18  ILE AAA CG2 1 
ATOM   124  C  CD1 . ILE A 1 18  ? 0.465   5.012   -0.197  1.000 11.362 ? 18  ILE AAA CD1 1 
ATOM   125  N  N   . ASN A 1 19  ? 3.459   1.011   0.655   1.000 8.792  ? 19  ASN AAA N   1 
ATOM   126  C  CA  . ASN A 1 19  ? 4.594   0.115   0.973   1.000 9.808  ? 19  ASN AAA CA  1 
ATOM   127  C  C   . ASN A 1 19  ? 5.844   0.956   1.106   1.000 9.575  ? 19  ASN AAA C   1 
ATOM   128  O  O   . ASN A 1 19  ? 6.037   1.988   0.404   1.000 8.585  ? 19  ASN AAA O   1 
ATOM   129  C  CB  . ASN A 1 19  ? 4.793   -0.896  -0.148  1.000 12.303 ? 19  ASN AAA CB  1 
ATOM   130  C  CG  . ASN A 1 19  ? 3.532   -1.683  -0.387  1.000 14.707 ? 19  ASN AAA CG  1 
ATOM   131  O  OD1 . ASN A 1 19  ? 3.166   -2.513  0.393   1.000 16.901 ? 19  ASN AAA OD1 1 
ATOM   132  N  ND2 . ASN A 1 19  ? 2.808   -1.350  -1.432  1.000 17.695 ? 19  ASN AAA ND2 1 
ATOM   133  N  N   . PHE A 1 20  ? 6.723   0.516   1.976   1.000 9.023  ? 20  PHE AAA N   1 
ATOM   134  C  CA  . PHE A 1 20  ? 8.006   1.178   2.249   1.000 9.247  ? 20  PHE AAA CA  1 
ATOM   135  C  C   . PHE A 1 20  ? 9.082   0.115   2.176   1.000 8.813  ? 20  PHE AAA C   1 
ATOM   136  O  O   . PHE A 1 20  ? 8.923   -0.994  2.769   1.000 9.853  ? 20  PHE AAA O   1 
ATOM   137  C  CB  . PHE A 1 20  ? 8.050   1.793   3.658   1.000 8.904  ? 20  PHE AAA CB  1 
ATOM   138  C  CG  . PHE A 1 20  ? 7.014   2.861   3.947   1.000 9.265  ? 20  PHE AAA CG  1 
ATOM   139  C  CD1 . PHE A 1 20  ? 5.700   2.533   4.248   1.000 9.635  ? 20  PHE AAA CD1 1 
ATOM   140  C  CD2 . PHE A 1 20  ? 7.388   4.180   3.954   1.000 9.265  ? 20  PHE AAA CD2 1 
ATOM   141  C  CE1 . PHE A 1 20  ? 4.784   3.539   4.557   1.000 9.988  ? 20  PHE AAA CE1 1 
ATOM   142  C  CE2 . PHE A 1 20  ? 6.466   5.182   4.204   1.000 9.671  ? 20  PHE AAA CE2 1 
ATOM   143  C  CZ  . PHE A 1 20  ? 5.178   4.852   4.536   1.000 10.460 ? 20  PHE AAA CZ  1 
ATOM   144  N  N   . GLU A 1 21  ? 10.225  0.419   1.562   1.000 9.647  ? 21  GLU AAA N   1 
ATOM   145  C  CA  . GLU A 1 21  ? 11.345  -0.544  1.535   1.000 11.019 ? 21  GLU AAA CA  1 
ATOM   146  C  C   . GLU A 1 21  ? 12.664  0.199   1.721   1.000 9.986  ? 21  GLU AAA C   1 
ATOM   147  O  O   . GLU A 1 21  ? 12.855  1.276   1.108   1.000 10.535 ? 21  GLU AAA O   1 
ATOM   148  C  CB  . GLU A 1 21  ? 11.336  -1.339  0.213   1.000 14.065 ? 21  GLU AAA CB  1 
ATOM   149  C  CG  . GLU A 1 21  ? 12.429  -2.413  0.094   1.000 19.439 ? 21  GLU AAA CG  1 
ATOM   150  C  CD  . GLU A 1 21  ? 12.104  -3.624  -0.771  1.000 23.972 ? 21  GLU AAA CD  1 
ATOM   151  O  OE1 . GLU A 1 21  ? 11.132  -3.578  -1.529  1.000 29.329 ? 21  GLU AAA OE1 1 
ATOM   152  O  OE2 . GLU A 1 21  ? 12.797  -4.657  -0.630  1.000 32.363 ? 21  GLU AAA OE2 1 
ATOM   153  N  N   . GLN A 1 22  ? 13.548  -0.363  2.505   1.000 9.865  ? 22  GLN AAA N   1 
ATOM   154  C  CA  . GLN A 1 22  ? 14.875  0.212   2.746   1.000 11.397 ? 22  GLN AAA CA  1 
ATOM   155  C  C   . GLN A 1 22  ? 15.898  -0.910  2.594   1.000 12.337 ? 22  GLN AAA C   1 
ATOM   156  O  O   . GLN A 1 22  ? 15.838  -1.866  3.319   1.000 14.294 ? 22  GLN AAA O   1 
ATOM   157  C  CB  . GLN A 1 22  ? 14.924  0.890   4.107   1.000 10.073 ? 22  GLN AAA CB  1 
ATOM   158  C  CG  . GLN A 1 22  ? 16.184  1.692   4.345   1.000 10.978 ? 22  GLN AAA CG  1 
ATOM   159  C  CD  . GLN A 1 22  ? 16.151  2.356   5.695   1.000 10.831 ? 22  GLN AAA CD  1 
ATOM   160  O  OE1 . GLN A 1 22  ? 15.569  1.850   6.650   1.000 12.229 ? 22  GLN AAA OE1 1 
ATOM   161  N  NE2 . GLN A 1 22  ? 16.799  3.502   5.858   1.000 11.200 ? 22  GLN AAA NE2 1 
ATOM   162  N  N   . LYS A 1 23  ? 16.799  -0.793  1.612   1.000 14.776 ? 23  LYS AAA N   1 
ATOM   163  C  CA  . LYS A 1 23  ? 17.846  -1.838  1.362   1.000 17.811 ? 23  LYS AAA CA  1 
ATOM   164  C  C   . LYS A 1 23  ? 18.888  -1.813  2.468   1.000 19.107 ? 23  LYS AAA C   1 
ATOM   165  O  O   . LYS A 1 23  ? 19.347  -2.906  2.874   1.000 23.292 ? 23  LYS AAA O   1 
ATOM   166  C  CB  . LYS A 1 23  ? 18.473  -1.615  -0.013  1.000 22.236 ? 23  LYS AAA CB  1 
ATOM   167  C  CG  . LYS A 1 23  ? 17.470  -1.761  -1.159  1.000 26.382 ? 23  LYS AAA CG  1 
ATOM   168  C  CD  . LYS A 1 23  ? 18.092  -1.896  -2.537  1.000 32.018 ? 23  LYS AAA CD  1 
ATOM   169  C  CE  . LYS A 1 23  ? 17.342  -1.197  -3.652  1.000 34.750 ? 23  LYS AAA CE  1 
ATOM   170  N  NZ  . LYS A 1 23  ? 18.258  -0.837  -4.764  1.000 37.991 ? 23  LYS AAA NZ  1 
ATOM   171  N  N   . GLU A 1 24  ? 19.257  -0.650  2.981   1.000 19.515 ? 24  GLU AAA N   1 
ATOM   172  C  CA  . GLU A 1 24  ? 20.203  -0.598  4.134   1.000 21.504 ? 24  GLU AAA CA  1 
ATOM   173  C  C   . GLU A 1 24  ? 19.892  0.594   5.023   1.000 19.323 ? 24  GLU AAA C   1 
ATOM   174  O  O   . GLU A 1 24  ? 19.340  1.569   4.513   1.000 18.497 ? 24  GLU AAA O   1 
ATOM   175  C  CB  . GLU A 1 24  ? 21.663  -0.511  3.702   1.000 25.859 ? 24  GLU AAA CB  1 
ATOM   176  C  CG  . GLU A 1 24  ? 21.935  0.673   2.795   1.000 29.975 ? 24  GLU AAA CG  1 
ATOM   177  C  CD  . GLU A 1 24  ? 23.354  0.649   2.241   1.000 38.968 ? 24  GLU AAA CD  1 
ATOM   178  O  OE1 . GLU A 1 24  ? 24.206  -0.042  2.833   1.000 51.183 ? 24  GLU AAA OE1 1 
ATOM   179  O  OE2 . GLU A 1 24  ? 23.607  1.308   1.224   1.000 44.519 ? 24  GLU AAA OE2 1 
ATOM   180  N  N   . SER A 1 25  ? 20.304  0.539   6.287   1.000 19.862 ? 25  SER AAA N   1 
ATOM   181  C  CA  . SER A 1 25  ? 19.880  1.537   7.294   1.000 21.373 ? 25  SER AAA CA  1 
ATOM   182  C  C   . SER A 1 25  ? 20.442  2.916   6.956   1.000 18.941 ? 25  SER AAA C   1 
ATOM   183  O  O   . SER A 1 25  ? 19.833  3.913   7.387   1.000 22.466 ? 25  SER AAA O   1 
ATOM   184  C  CB  . SER A 1 25  ? 20.259  1.100   8.668   1.000 22.312 ? 25  SER AAA CB  1 
ATOM   185  O  OG  . SER A 1 25  ? 21.658  1.229   8.862   1.000 25.573 ? 25  SER AAA OG  1 
ATOM   186  N  N   . ASN A 1 26  ? 21.537  3.016   6.199   1.000 18.460 ? 26  ASN AAA N   1 
ATOM   187  C  CA  . ASN A 1 26  ? 22.132  4.330   5.838   1.000 20.679 ? 26  ASN AAA CA  1 
ATOM   188  C  C   . ASN A 1 26  ? 21.627  4.756   4.457   1.000 19.460 ? 26  ASN AAA C   1 
ATOM   189  O  O   . ASN A 1 26  ? 22.191  5.728   3.897   1.000 21.842 ? 26  ASN AAA O   1 
ATOM   190  C  CB  . ASN A 1 26  ? 23.656  4.320   5.891   1.000 22.754 ? 26  ASN AAA CB  1 
ATOM   191  C  CG  . ASN A 1 26  ? 24.290  3.255   5.034   1.000 26.360 ? 26  ASN AAA CG  1 
ATOM   192  O  OD1 . ASN A 1 26  ? 23.671  2.249   4.690   1.000 29.198 ? 26  ASN AAA OD1 1 
ATOM   193  N  ND2 . ASN A 1 26  ? 25.571  3.428   4.742   1.000 31.180 ? 26  ASN AAA ND2 1 
ATOM   194  N  N   . GLY A 1 27  ? 20.620  4.072   3.921   1.000 16.249 ? 27  GLY AAA N   1 
ATOM   195  C  CA  . GLY A 1 27  ? 20.125  4.363   2.575   1.000 14.850 ? 27  GLY AAA CA  1 
ATOM   196  C  C   . GLY A 1 27  ? 18.705  4.896   2.573   1.000 12.750 ? 27  GLY AAA C   1 
ATOM   197  O  O   . GLY A 1 27  ? 18.016  4.968   3.590   1.000 12.838 ? 27  GLY AAA O   1 
ATOM   198  N  N   . PRO A 1 28  ? 18.242  5.278   1.385   1.000 12.128 ? 28  PRO AAA N   1 
ATOM   199  C  CA  . PRO A 1 28  ? 16.914  5.875   1.238   1.000 12.265 ? 28  PRO AAA CA  1 
ATOM   200  C  C   . PRO A 1 28  ? 15.818  4.835   1.390   1.000 11.053 ? 28  PRO AAA C   1 
ATOM   201  O  O   . PRO A 1 28  ? 16.027  3.622   1.289   1.000 11.870 ? 28  PRO AAA O   1 
ATOM   202  C  CB  . PRO A 1 28  ? 16.976  6.442   -0.177  1.000 15.567 ? 28  PRO AAA CB  1 
ATOM   203  C  CG  . PRO A 1 28  ? 17.876  5.495   -0.888  1.000 16.568 ? 28  PRO AAA CG  1 
ATOM   204  C  CD  . PRO A 1 28  ? 18.979  5.184   0.105   1.000 13.880 ? 28  PRO AAA CD  1 
ATOM   205  N  N   . VAL A 1 29  ? 14.643  5.369   1.673   1.000 10.660 ? 29  VAL AAA N   1 
ATOM   206  C  CA  . VAL A 1 29  ? 13.427  4.534   1.733   1.000 9.985  ? 29  VAL AAA CA  1 
ATOM   207  C  C   . VAL A 1 29  ? 12.611  4.789   0.464   1.000 9.416  ? 29  VAL AAA C   1 
ATOM   208  O  O   . VAL A 1 29  ? 12.312  5.962   0.170   1.000 10.476 ? 29  VAL AAA O   1 
ATOM   209  C  CB  . VAL A 1 29  ? 12.613  4.862   2.989   1.000 9.346  ? 29  VAL AAA CB  1 
ATOM   210  C  CG1 . VAL A 1 29  ? 11.329  4.049   3.033   1.000 9.907  ? 29  VAL AAA CG1 1 
ATOM   211  C  CG2 . VAL A 1 29  ? 13.465  4.712   4.249   1.000 10.102 ? 29  VAL AAA CG2 1 
ATOM   212  N  N   . LYS A 1 30  ? 12.212  3.724   -0.203  1.000 9.877  ? 30  LYS AAA N   1 
ATOM   213  C  CA  . LYS A 1 30  ? 11.308  3.780   -1.366  1.000 10.771 ? 30  LYS AAA CA  1 
ATOM   214  C  C   . LYS A 1 30  ? 9.891   3.648   -0.811  1.000 10.085 ? 30  LYS AAA C   1 
ATOM   215  O  O   . LYS A 1 30  ? 9.637   2.738   0.002   1.000 9.767  ? 30  LYS AAA O   1 
ATOM   216  C  CB  . LYS A 1 30  ? 11.689  2.654   -2.317  1.000 14.031 ? 30  LYS AAA CB  1 
ATOM   217  C  CG  . LYS A 1 30  ? 12.921  2.936   -3.185  1.000 20.253 ? 30  LYS AAA CG  1 
ATOM   218  C  CD  . LYS A 1 30  ? 13.248  1.812   -4.147  1.000 24.440 ? 30  LYS AAA CD  1 
ATOM   219  C  CE  . LYS A 1 30  ? 14.520  2.032   -4.949  1.000 28.726 ? 30  LYS AAA CE  1 
ATOM   220  N  NZ  . LYS A 1 30  ? 14.718  0.929   -5.922  1.000 35.701 ? 30  LYS AAA NZ  1 
ATOM   221  N  N   . VAL A 1 31  ? 8.986   4.497   -1.246  1.000 9.732  ? 31  VAL AAA N   1 
ATOM   222  C  CA  . VAL A 1 31  ? 7.583   4.563   -0.778  1.000 10.261 ? 31  VAL AAA CA  1 
ATOM   223  C  C   . VAL A 1 31  ? 6.718   4.401   -2.013  1.000 10.661 ? 31  VAL AAA C   1 
ATOM   224  O  O   . VAL A 1 31  ? 6.884   5.205   -2.982  1.000 12.488 ? 31  VAL AAA O   1 
ATOM   225  C  CB  . VAL A 1 31  ? 7.305   5.880   -0.055  1.000 10.915 ? 31  VAL AAA CB  1 
ATOM   226  C  CG1 . VAL A 1 31  ? 5.890   5.879   0.519   1.000 11.957 ? 31  VAL AAA CG1 1 
ATOM   227  C  CG2 . VAL A 1 31  ? 8.350   6.144   1.023   1.000 10.888 ? 31  VAL AAA CG2 1 
ATOM   228  N  N   . TRP A 1 32  ? 5.840   3.442   -2.065  1.000 9.882  ? 32  TRP AAA N   1 
ATOM   229  C  CA  . TRP A 1 32  ? 4.980   3.296   -3.254  1.000 10.233 ? 32  TRP AAA CA  1 
ATOM   230  C  C   . TRP A 1 32  ? 3.649   2.714   -2.867  1.000 9.658  ? 32  TRP AAA C   1 
ATOM   231  O  O   . TRP A 1 32  ? 3.553   1.918   -1.941  1.000 10.238 ? 32  TRP AAA O   1 
ATOM   232  C  CB  . TRP A 1 32  ? 5.699   2.493   -4.344  1.000 12.416 ? 32  TRP AAA CB  1 
ATOM   233  C  CG  . TRP A 1 32  ? 5.821   1.040   -4.062  1.000 13.621 ? 32  TRP AAA CG  1 
ATOM   234  C  CD1 . TRP A 1 32  ? 5.003   0.071   -4.551  1.000 15.436 ? 32  TRP AAA CD1 1 
ATOM   235  C  CD2 . TRP A 1 32  ? 6.779   0.364   -3.239  1.000 13.437 ? 32  TRP AAA CD2 1 
ATOM   236  N  NE1 . TRP A 1 32  ? 5.358   -1.145  -4.045  1.000 16.939 ? 32  TRP AAA NE1 1 
ATOM   237  C  CE2 . TRP A 1 32  ? 6.485   -1.017  -3.275  1.000 13.493 ? 32  TRP AAA CE2 1 
ATOM   238  C  CE3 . TRP A 1 32  ? 7.860   0.781   -2.465  1.000 15.616 ? 32  TRP AAA CE3 1 
ATOM   239  C  CZ2 . TRP A 1 32  ? 7.193   -1.967  -2.568  1.000 16.596 ? 32  TRP AAA CZ2 1 
ATOM   240  C  CZ3 . TRP A 1 32  ? 8.542   -0.160  -1.717  1.000 15.937 ? 32  TRP AAA CZ3 1 
ATOM   241  C  CH2 . TRP A 1 32  ? 8.242   -1.518  -1.808  1.000 16.210 ? 32  TRP AAA CH2 1 
ATOM   242  N  N   . GLY A 1 33  ? 2.643   3.018   -3.669  1.000 9.337  ? 33  GLY AAA N   1 
ATOM   243  C  CA  . GLY A 1 33  ? 1.325   2.432   -3.503  1.000 9.157  ? 33  GLY AAA CA  1 
ATOM   244  C  C   . GLY A 1 33  ? 0.286   3.289   -4.137  1.000 9.462  ? 33  GLY AAA C   1 
ATOM   245  O  O   . GLY A 1 33  ? 0.596   4.032   -5.094  1.000 10.895 ? 33  GLY AAA O   1 
ATOM   246  N  N   A SER A 1 34  ? -0.937  3.208   -3.646  0.300 9.685  ? 34  SER AAA N   1 
ATOM   247  N  N   B SER A 1 34  ? -0.928  3.204   -3.629  0.700 10.296 ? 34  SER AAA N   1 
ATOM   248  C  CA  A SER A 1 34  ? -2.076  3.910   -4.274  0.300 10.145 ? 34  SER AAA CA  1 
ATOM   249  C  CA  B SER A 1 34  ? -2.117  3.813   -4.267  0.700 12.037 ? 34  SER AAA CA  1 
ATOM   250  C  C   A SER A 1 34  ? -3.070  4.285   -3.185  0.300 10.002 ? 34  SER AAA C   1 
ATOM   251  C  C   B SER A 1 34  ? -3.064  4.289   -3.174  0.700 10.629 ? 34  SER AAA C   1 
ATOM   252  O  O   A SER A 1 34  ? -3.157  3.569   -2.166  0.300 10.617 ? 34  SER AAA O   1 
ATOM   253  O  O   B SER A 1 34  ? -3.196  3.588   -2.172  0.700 11.573 ? 34  SER AAA O   1 
ATOM   254  C  CB  A SER A 1 34  ? -2.708  3.062   -5.338  0.300 10.650 ? 34  SER AAA CB  1 
ATOM   255  C  CB  B SER A 1 34  ? -2.802  2.817   -5.161  0.700 14.026 ? 34  SER AAA CB  1 
ATOM   256  O  OG  A SER A 1 34  ? -3.351  1.968   -4.735  0.300 11.079 ? 34  SER AAA OG  1 
ATOM   257  O  OG  B SER A 1 34  ? -3.702  3.490   -6.019  0.700 20.556 ? 34  SER AAA OG  1 
ATOM   258  N  N   . ILE A 1 35  ? -3.752  5.400   -3.416  1.000 10.009 ? 35  ILE AAA N   1 
ATOM   259  C  CA  . ILE A 1 35  ? -4.845  5.877   -2.527  1.000 10.058 ? 35  ILE AAA CA  1 
ATOM   260  C  C   . ILE A 1 35  ? -6.019  6.230   -3.435  1.000 11.676 ? 35  ILE AAA C   1 
ATOM   261  O  O   . ILE A 1 35  ? -5.789  6.895   -4.431  1.000 13.208 ? 35  ILE AAA O   1 
ATOM   262  C  CB  . ILE A 1 35  ? -4.397  7.117   -1.729  1.000 9.822  ? 35  ILE AAA CB  1 
ATOM   263  C  CG1 . ILE A 1 35  ? -3.056  6.895   -1.012  1.000 10.375 ? 35  ILE AAA CG1 1 
ATOM   264  C  CG2 . ILE A 1 35  ? -5.500  7.503   -0.754  1.000 10.342 ? 35  ILE AAA CG2 1 
ATOM   265  C  CD1 . ILE A 1 35  ? -2.508  8.127   -0.360  1.000 9.919  ? 35  ILE AAA CD1 1 
ATOM   266  N  N   . LYS A 1 36  ? -7.210  5.792   -3.106  1.000 10.855 ? 36  LYS AAA N   1 
ATOM   267  C  CA  . LYS A 1 36  ? -8.384  6.128   -3.924  1.000 12.230 ? 36  LYS AAA CA  1 
ATOM   268  C  C   . LYS A 1 36  ? -9.394  6.887   -3.086  1.000 12.172 ? 36  LYS AAA C   1 
ATOM   269  O  O   . LYS A 1 36  ? -9.289  6.914   -1.836  1.000 12.316 ? 36  LYS AAA O   1 
ATOM   270  C  CB  . LYS A 1 36  ? -8.995  4.887   -4.554  1.000 14.310 ? 36  LYS AAA CB  1 
ATOM   271  C  CG  . LYS A 1 36  ? -9.478  3.829   -3.595  1.000 17.898 ? 36  LYS AAA CG  1 
ATOM   272  C  CD  . LYS A 1 36  ? -9.978  2.625   -4.348  1.000 19.670 ? 36  LYS AAA CD  1 
ATOM   273  C  CE  . LYS A 1 36  ? -10.466 1.549   -3.412  1.000 22.862 ? 36  LYS AAA CE  1 
ATOM   274  N  NZ  . LYS A 1 36  ? -11.343 0.575   -4.096  1.000 27.223 ? 36  LYS AAA NZ  1 
ATOM   275  N  N   . GLY A 1 37  ? -10.358 7.498   -3.750  1.000 11.327 ? 37  GLY AAA N   1 
ATOM   276  C  CA  . GLY A 1 37  ? -11.441 8.227   -3.077  1.000 11.761 ? 37  GLY AAA CA  1 
ATOM   277  C  C   . GLY A 1 37  ? -11.094 9.673   -2.782  1.000 12.084 ? 37  GLY AAA C   1 
ATOM   278  O  O   . GLY A 1 37  ? -11.855 10.318  -2.062  1.000 12.412 ? 37  GLY AAA O   1 
ATOM   279  N  N   . LEU A 1 38  ? -10.029 10.229  -3.371  1.000 11.546 ? 38  LEU AAA N   1 
ATOM   280  C  CA  . LEU A 1 38  ? -9.573  11.601  -3.088  1.000 11.177 ? 38  LEU AAA CA  1 
ATOM   281  C  C   . LEU A 1 38  ? -10.174 12.585  -4.094  1.000 11.477 ? 38  LEU AAA C   1 
ATOM   282  O  O   . LEU A 1 38  ? -10.372 12.205  -5.275  1.000 14.797 ? 38  LEU AAA O   1 
ATOM   283  C  CB  . LEU A 1 38  ? -8.033  11.649  -3.182  1.000 10.684 ? 38  LEU AAA CB  1 
ATOM   284  C  CG  . LEU A 1 38  ? -7.255  10.876  -2.103  1.000 11.386 ? 38  LEU AAA CG  1 
ATOM   285  C  CD1 . LEU A 1 38  ? -5.804  10.624  -2.495  1.000 11.785 ? 38  LEU AAA CD1 1 
ATOM   286  C  CD2 . LEU A 1 38  ? -7.356  11.551  -0.736  1.000 12.143 ? 38  LEU AAA CD2 1 
ATOM   287  N  N   . THR A 1 39  ? -10.253 13.835  -3.709  1.000 12.474 ? 39  THR AAA N   1 
ATOM   288  C  CA  . THR A 1 39  ? -10.541 14.930  -4.647  1.000 13.227 ? 39  THR AAA CA  1 
ATOM   289  C  C   . THR A 1 39  ? -9.325  15.105  -5.536  1.000 13.411 ? 39  THR AAA C   1 
ATOM   290  O  O   . THR A 1 39  ? -8.147  14.931  -5.114  1.000 12.725 ? 39  THR AAA O   1 
ATOM   291  C  CB  . THR A 1 39  ? -10.917 16.202  -3.912  1.000 13.962 ? 39  THR AAA CB  1 
ATOM   292  O  OG1 . THR A 1 39  ? -9.844  16.564  -3.049  1.000 15.926 ? 39  THR AAA OG1 1 
ATOM   293  C  CG2 . THR A 1 39  ? -12.192 16.061  -3.110  1.000 15.444 ? 39  THR AAA CG2 1 
ATOM   294  N  N   . GLU A 1 40  ? -9.527  15.552  -6.751  1.000 12.838 ? 40  GLU AAA N   1 
ATOM   295  C  CA  . GLU A 1 40  ? -8.409  15.769  -7.696  1.000 13.231 ? 40  GLU AAA CA  1 
ATOM   296  C  C   . GLU A 1 40  ? -7.546  16.906  -7.162  1.000 12.659 ? 40  GLU AAA C   1 
ATOM   297  O  O   . GLU A 1 40  ? -8.032  17.916  -6.683  1.000 13.817 ? 40  GLU AAA O   1 
ATOM   298  C  CB  . GLU A 1 40  ? -9.020  16.065  -9.062  1.000 14.316 ? 40  GLU AAA CB  1 
ATOM   299  C  CG  . GLU A 1 40  ? -7.983  15.921  -10.144 1.000 17.292 ? 40  GLU AAA CG  1 
ATOM   300  C  CD  . GLU A 1 40  ? -7.533  17.219  -10.727 1.000 19.333 ? 40  GLU AAA CD  1 
ATOM   301  O  OE1 . GLU A 1 40  ? -7.355  18.168  -9.943  1.000 21.399 ? 40  GLU AAA OE1 1 
ATOM   302  O  OE2 . GLU A 1 40  ? -7.362  17.299  -11.999 1.000 18.307 ? 40  GLU AAA OE2 1 
ATOM   303  N  N   . GLY A 1 41  ? -6.229  16.722  -7.195  1.000 11.411 ? 41  GLY AAA N   1 
ATOM   304  C  CA  . GLY A 1 41  ? -5.258  17.718  -6.791  1.000 10.370 ? 41  GLY AAA CA  1 
ATOM   305  C  C   . GLY A 1 41  ? -4.317  17.164  -5.733  1.000 9.877  ? 41  GLY AAA C   1 
ATOM   306  O  O   . GLY A 1 41  ? -4.118  15.920  -5.644  1.000 11.459 ? 41  GLY AAA O   1 
ATOM   307  N  N   . LEU A 1 42  ? -3.670  18.058  -5.054  1.000 9.184  ? 42  LEU AAA N   1 
ATOM   308  C  CA  . LEU A 1 42  ? -2.617  17.717  -4.085  1.000 9.068  ? 42  LEU AAA CA  1 
ATOM   309  C  C   . LEU A 1 42  ? -3.212  17.466  -2.705  1.000 9.157  ? 42  LEU AAA C   1 
ATOM   310  O  O   . LEU A 1 42  ? -4.096  18.188  -2.217  1.000 10.252 ? 42  LEU AAA O   1 
ATOM   311  C  CB  . LEU A 1 42  ? -1.637  18.884  -3.990  1.000 10.280 ? 42  LEU AAA CB  1 
ATOM   312  C  CG  . LEU A 1 42  ? -0.858  19.201  -5.281  1.000 13.029 ? 42  LEU AAA CG  1 
ATOM   313  C  CD1 . LEU A 1 42  ? -0.054  20.483  -5.117  1.000 16.685 ? 42  LEU AAA CD1 1 
ATOM   314  C  CD2 . LEU A 1 42  ? 0.068   18.057  -5.668  1.000 14.652 ? 42  LEU AAA CD2 1 
ATOM   315  N  N   . HIS A 1 43  ? -2.612  16.483  -2.034  1.000 8.298  ? 43  HIS AAA N   1 
ATOM   316  C  CA  . HIS A 1 43  ? -2.993  16.110  -0.653  1.000 8.083  ? 43  HIS AAA CA  1 
ATOM   317  C  C   . HIS A 1 43  ? -1.761  15.960  0.208   1.000 7.979  ? 43  HIS AAA C   1 
ATOM   318  O  O   . HIS A 1 43  ? -0.910  15.139  -0.135  1.000 9.158  ? 43  HIS AAA O   1 
ATOM   319  C  CB  . HIS A 1 43  ? -3.845  14.838  -0.690  1.000 9.002  ? 43  HIS AAA CB  1 
ATOM   320  C  CG  . HIS A 1 43  ? -5.153  15.039  -1.389  1.000 9.254  ? 43  HIS AAA CG  1 
ATOM   321  N  ND1 . HIS A 1 43  ? -6.252  15.499  -0.705  1.000 10.499 ? 43  HIS AAA ND1 1 
ATOM   322  C  CD2 . HIS A 1 43  ? -5.504  14.858  -2.685  1.000 10.732 ? 43  HIS AAA CD2 1 
ATOM   323  C  CE1 . HIS A 1 43  ? -7.244  15.594  -1.589  1.000 11.213 ? 43  HIS AAA CE1 1 
ATOM   324  N  NE2 . HIS A 1 43  ? -6.812  15.233  -2.800  1.000 11.041 ? 43  HIS AAA NE2 1 
ATOM   325  N  N   . GLY A 1 44  ? -1.714  16.647  1.337   1.000 8.037  ? 44  GLY AAA N   1 
ATOM   326  C  CA  . GLY A 1 44  ? -0.580  16.495  2.252   1.000 8.668  ? 44  GLY AAA CA  1 
ATOM   327  C  C   . GLY A 1 44  ? -0.411  15.072  2.713   1.000 8.511  ? 44  GLY AAA C   1 
ATOM   328  O  O   . GLY A 1 44  ? -1.434  14.386  2.909   1.000 8.732  ? 44  GLY AAA O   1 
ATOM   329  N  N   . PHE A 1 45  ? 0.833   14.663  2.879   1.000 8.606  ? 45  PHE AAA N   1 
ATOM   330  C  CA  . PHE A 1 45  ? 1.191   13.249  3.092   1.000 7.759  ? 45  PHE AAA CA  1 
ATOM   331  C  C   . PHE A 1 45  ? 2.275   13.238  4.152   1.000 8.055  ? 45  PHE AAA C   1 
ATOM   332  O  O   . PHE A 1 45  ? 3.422   13.643  3.838   1.000 9.302  ? 45  PHE AAA O   1 
ATOM   333  C  CB  . PHE A 1 45  ? 1.627   12.624  1.775   1.000 7.927  ? 45  PHE AAA CB  1 
ATOM   334  C  CG  . PHE A 1 45  ? 1.775   11.134  1.757   1.000 9.035  ? 45  PHE AAA CG  1 
ATOM   335  C  CD1 . PHE A 1 45  ? 0.701   10.295  2.016   1.000 9.404  ? 45  PHE AAA CD1 1 
ATOM   336  C  CD2 . PHE A 1 45  ? 2.970   10.578  1.407   1.000 8.776  ? 45  PHE AAA CD2 1 
ATOM   337  C  CE1 . PHE A 1 45  ? 0.844   8.933   1.865   1.000 10.143 ? 45  PHE AAA CE1 1 
ATOM   338  C  CE2 . PHE A 1 45  ? 3.096   9.202   1.294   1.000 9.914  ? 45  PHE AAA CE2 1 
ATOM   339  C  CZ  . PHE A 1 45  ? 2.029   8.394   1.522   1.000 10.047 ? 45  PHE AAA CZ  1 
ATOM   340  N  N   . HIS A 1 46  ? 1.915   12.811  5.355   1.000 7.956  ? 46  HIS AAA N   1 
ATOM   341  C  CA  . HIS A 1 46  ? 2.849   12.967  6.489   1.000 7.894  ? 46  HIS AAA CA  1 
ATOM   342  C  C   . HIS A 1 46  ? 2.881   11.727  7.376   1.000 7.050  ? 46  HIS AAA C   1 
ATOM   343  O  O   . HIS A 1 46  ? 1.846   11.080  7.561   1.000 7.401  ? 46  HIS AAA O   1 
ATOM   344  C  CB  . HIS A 1 46  ? 2.476   14.130  7.379   1.000 10.030 ? 46  HIS AAA CB  1 
ATOM   345  C  CG  . HIS A 1 46  ? 2.214   15.391  6.652   1.000 10.642 ? 46  HIS AAA CG  1 
ATOM   346  N  ND1 . HIS A 1 46  ? 1.010   15.926  6.680   1.000 12.728 ? 46  HIS AAA ND1 1 
ATOM   347  C  CD2 . HIS A 1 46  ? 2.975   16.130  5.849   1.000 12.110 ? 46  HIS AAA CD2 1 
ATOM   348  C  CE1 . HIS A 1 46  ? 1.017   17.009  5.911   1.000 13.170 ? 46  HIS AAA CE1 1 
ATOM   349  N  NE2 . HIS A 1 46  ? 2.196   17.181  5.431   1.000 13.210 ? 46  HIS AAA NE2 1 
ATOM   350  N  N   . VAL A 1 47  ? 4.036   11.501  7.980   1.000 6.603  ? 47  VAL AAA N   1 
ATOM   351  C  CA  . VAL A 1 47  ? 4.119   10.587  9.150   1.000 7.332  ? 47  VAL AAA CA  1 
ATOM   352  C  C   . VAL A 1 47  ? 3.873   11.458  10.384  1.000 6.994  ? 47  VAL AAA C   1 
ATOM   353  O  O   . VAL A 1 47  ? 4.570   12.476  10.597  1.000 7.961  ? 47  VAL AAA O   1 
ATOM   354  C  CB  . VAL A 1 47  ? 5.465   9.869   9.237   1.000 7.641  ? 47  VAL AAA CB  1 
ATOM   355  C  CG1 . VAL A 1 47  ? 5.484   8.904   10.429  1.000 7.206  ? 47  VAL AAA CG1 1 
ATOM   356  C  CG2 . VAL A 1 47  ? 5.753   9.096   7.976   1.000 8.749  ? 47  VAL AAA CG2 1 
ATOM   357  N  N   . HIS A 1 48  ? 2.887   11.103  11.177  1.000 6.971  ? 48  HIS AAA N   1 
ATOM   358  C  CA  . HIS A 1 48  ? 2.521   11.746  12.459  1.000 7.469  ? 48  HIS AAA CA  1 
ATOM   359  C  C   . HIS A 1 48  ? 3.126   10.970  13.618  1.000 8.119  ? 48  HIS AAA C   1 
ATOM   360  O  O   . HIS A 1 48  ? 3.463   9.789   13.501  1.000 8.609  ? 48  HIS AAA O   1 
ATOM   361  C  CB  . HIS A 1 48  ? 1.000   11.887  12.564  1.000 7.479  ? 48  HIS AAA CB  1 
ATOM   362  C  CG  . HIS A 1 48  ? 0.462   12.947  11.654  1.000 7.677  ? 48  HIS AAA CG  1 
ATOM   363  N  ND1 . HIS A 1 48  ? -0.158  14.048  12.162  1.000 8.746  ? 48  HIS AAA ND1 1 
ATOM   364  C  CD2 . HIS A 1 48  ? 0.411   13.078  10.281  1.000 8.100  ? 48  HIS AAA CD2 1 
ATOM   365  C  CE1 . HIS A 1 48  ? -0.590  14.819  11.117  1.000 8.565  ? 48  HIS AAA CE1 1 
ATOM   366  N  NE2 . HIS A 1 48  ? -0.255  14.242  9.982   1.000 8.932  ? 48  HIS AAA NE2 1 
ATOM   367  N  N   . GLU A 1 49  ? 3.239   11.632  14.771  1.000 8.572  ? 49  GLU AAA N   1 
ATOM   368  C  CA  . GLU A 1 49  ? 4.081   11.172  15.879  1.000 9.807  ? 49  GLU AAA CA  1 
ATOM   369  C  C   . GLU A 1 49  ? 3.532   9.924   16.555  1.000 9.255  ? 49  GLU AAA C   1 
ATOM   370  O  O   . GLU A 1 49  ? 4.355   9.132   16.979  1.000 12.518 ? 49  GLU AAA O   1 
ATOM   371  C  CB  . GLU A 1 49  ? 4.103   12.271  16.924  1.000 11.757 ? 49  GLU AAA CB  1 
ATOM   372  C  CG  . GLU A 1 49  ? 5.050   11.986  18.087  1.000 12.562 ? 49  GLU AAA CG  1 
ATOM   373  C  CD  . GLU A 1 49  ? 5.182   13.161  19.043  1.000 13.564 ? 49  GLU AAA CD  1 
ATOM   374  O  OE1 . GLU A 1 49  ? 4.456   14.182  18.862  1.000 15.006 ? 49  GLU AAA OE1 1 
ATOM   375  O  OE2 . GLU A 1 49  ? 5.969   12.970  20.035  1.000 19.444 ? 49  GLU AAA OE2 1 
ATOM   376  N  N   . PHE A 1 50  ? 2.246   9.765   16.701  1.000 8.715  ? 50  PHE AAA N   1 
ATOM   377  C  CA  . PHE A 1 50  ? 1.739   8.622   17.503  1.000 9.703  ? 50  PHE AAA CA  1 
ATOM   378  C  C   . PHE A 1 50  ? 1.105   7.597   16.576  1.000 9.704  ? 50  PHE AAA C   1 
ATOM   379  O  O   . PHE A 1 50  ? 0.267   8.015   15.753  1.000 9.914  ? 50  PHE AAA O   1 
ATOM   380  C  CB  . PHE A 1 50  ? 0.781   9.081   18.605  1.000 10.187 ? 50  PHE AAA CB  1 
ATOM   381  C  CG  . PHE A 1 50  ? 1.329   10.214  19.434  1.000 12.254 ? 50  PHE AAA CG  1 
ATOM   382  C  CD1 . PHE A 1 50  ? 2.497   10.045  20.130  1.000 12.209 ? 50  PHE AAA CD1 1 
ATOM   383  C  CD2 . PHE A 1 50  ? 0.659   11.425  19.534  1.000 12.993 ? 50  PHE AAA CD2 1 
ATOM   384  C  CE1 . PHE A 1 50  ? 3.043   11.096  20.868  1.000 13.667 ? 50  PHE AAA CE1 1 
ATOM   385  C  CE2 . PHE A 1 50  ? 1.185   12.459  20.298  1.000 14.250 ? 50  PHE AAA CE2 1 
ATOM   386  C  CZ  . PHE A 1 50  ? 2.391   12.287  20.916  1.000 14.186 ? 50  PHE AAA CZ  1 
ATOM   387  N  N   . GLY A 1 51  ? 1.391   6.314   16.806  1.000 9.424  ? 51  GLY AAA N   1 
ATOM   388  C  CA  . GLY A 1 51  ? 0.652   5.201   16.159  1.000 8.959  ? 51  GLY AAA CA  1 
ATOM   389  C  C   . GLY A 1 51  ? -0.605  4.921   16.939  1.000 9.867  ? 51  GLY AAA C   1 
ATOM   390  O  O   . GLY A 1 51  ? -0.854  3.737   17.269  1.000 10.569 ? 51  GLY AAA O   1 
ATOM   391  N  N   . ASP A 1 52  ? -1.370  5.952   17.247  1.000 10.527 ? 52  ASP AAA N   1 
ATOM   392  C  CA  . ASP A 1 52  ? -2.570  5.895   18.110  1.000 10.310 ? 52  ASP AAA CA  1 
ATOM   393  C  C   . ASP A 1 52  ? -3.731  6.284   17.258  1.000 10.211 ? 52  ASP AAA C   1 
ATOM   394  O  O   . ASP A 1 52  ? -3.835  7.471   16.891  1.000 10.816 ? 52  ASP AAA O   1 
ATOM   395  C  CB  . ASP A 1 52  ? -2.423  6.809   19.323  1.000 10.788 ? 52  ASP AAA CB  1 
ATOM   396  C  CG  . ASP A 1 52  ? -3.571  6.661   20.306  1.000 11.461 ? 52  ASP AAA CG  1 
ATOM   397  O  OD1 . ASP A 1 52  ? -4.651  6.213   19.877  1.000 12.434 ? 52  ASP AAA OD1 1 
ATOM   398  O  OD2 . ASP A 1 52  ? -3.365  7.076   21.464  1.000 16.251 ? 52  ASP AAA OD2 1 
ATOM   399  N  N   . ASN A 1 53  ? -4.549  5.333   16.866  1.000 10.039 ? 53  ASN AAA N   1 
ATOM   400  C  CA  . ASN A 1 53  ? -5.739  5.619   16.049  1.000 12.050 ? 53  ASN AAA CA  1 
ATOM   401  C  C   . ASN A 1 53  ? -7.000  5.281   16.847  1.000 11.813 ? 53  ASN AAA C   1 
ATOM   402  O  O   . ASN A 1 53  ? -8.044  5.013   16.251  1.000 13.197 ? 53  ASN AAA O   1 
ATOM   403  C  CB  . ASN A 1 53  ? -5.649  4.929   14.708  1.000 13.415 ? 53  ASN AAA CB  1 
ATOM   404  C  CG  . ASN A 1 53  ? -4.533  5.453   13.824  1.000 12.418 ? 53  ASN AAA CG  1 
ATOM   405  O  OD1 . ASN A 1 53  ? -3.810  6.432   14.119  1.000 16.051 ? 53  ASN AAA OD1 1 
ATOM   406  N  ND2 . ASN A 1 53  ? -4.368  4.828   12.700  1.000 12.557 ? 53  ASN AAA ND2 1 
ATOM   407  N  N   . THR A 1 54  ? -6.866  5.263   18.155  1.000 12.608 ? 54  THR AAA N   1 
ATOM   408  C  CA  . THR A 1 54  ? -7.997  4.901   19.037  1.000 13.840 ? 54  THR AAA CA  1 
ATOM   409  C  C   . THR A 1 54  ? -9.173  5.841   18.831  1.000 14.617 ? 54  THR AAA C   1 
ATOM   410  O  O   . THR A 1 54  ? -10.307 5.357   18.939  1.000 15.190 ? 54  THR AAA O   1 
ATOM   411  C  CB  . THR A 1 54  ? -7.546  4.846   20.494  1.000 14.469 ? 54  THR AAA CB  1 
ATOM   412  O  OG1 . THR A 1 54  ? -7.019  6.113   20.884  1.000 15.323 ? 54  THR AAA OG1 1 
ATOM   413  C  CG2 . THR A 1 54  ? -6.563  3.723   20.740  1.000 14.852 ? 54  THR AAA CG2 1 
ATOM   414  N  N   . ALA A 1 55  ? -8.947  7.126   18.547  1.000 15.302 ? 55  ALA AAA N   1 
ATOM   415  C  CA  . ALA A 1 55  ? -10.077 8.038   18.253  1.000 17.510 ? 55  ALA AAA CA  1 
ATOM   416  C  C   . ALA A 1 55  ? -9.976  8.470   16.798  1.000 18.387 ? 55  ALA AAA C   1 
ATOM   417  O  O   . ALA A 1 55  ? -10.275 9.643   16.458  1.000 26.023 ? 55  ALA AAA O   1 
ATOM   418  C  CB  . ALA A 1 55  ? -10.089 9.223   19.204  1.000 20.924 ? 55  ALA AAA CB  1 
ATOM   419  N  N   . GLY A 1 56  ? -9.577  7.558   15.928  1.000 15.008 ? 56  GLY AAA N   1 
ATOM   420  C  CA  . GLY A 1 56  ? -9.385  7.878   14.501  1.000 17.102 ? 56  GLY AAA CA  1 
ATOM   421  C  C   . GLY A 1 56  ? -8.056  8.564   14.285  1.000 17.620 ? 56  GLY AAA C   1 
ATOM   422  O  O   . GLY A 1 56  ? -7.058  8.166   14.959  1.000 21.988 ? 56  GLY AAA O   1 
ATOM   423  N  N   . CYS A 1 57  ? -7.997  9.461   13.300  1.000 13.736 ? 57  CYS AAA N   1 
ATOM   424  C  CA  . CYS A 1 57  ? -6.705  10.037  12.888  1.000 13.947 ? 57  CYS AAA CA  1 
ATOM   425  C  C   . CYS A 1 57  ? -6.262  11.173  13.821  1.000 13.207 ? 57  CYS AAA C   1 
ATOM   426  O  O   . CYS A 1 57  ? -5.050  11.453  13.865  1.000 12.361 ? 57  CYS AAA O   1 
ATOM   427  C  CB  . CYS A 1 57  ? -6.815  10.511  11.446  1.000 12.695 ? 57  CYS AAA CB  1 
ATOM   428  S  SG  . CYS A 1 57  ? -7.236  9.185   10.286  1.000 14.869 ? 57  CYS AAA SG  1 
ATOM   429  N  N   . THR A 1 58  ? -7.177  11.748  14.593  1.000 14.508 ? 58  THR AAA N   1 
ATOM   430  C  CA  . THR A 1 58  ? -6.779  12.851  15.500  1.000 14.870 ? 58  THR AAA CA  1 
ATOM   431  C  C   . THR A 1 58  ? -5.800  12.368  16.570  1.000 13.468 ? 58  THR AAA C   1 
ATOM   432  O  O   . THR A 1 58  ? -4.891  13.159  16.959  1.000 12.739 ? 58  THR AAA O   1 
ATOM   433  C  CB  . THR A 1 58  ? -8.007  13.481  16.129  1.000 17.457 ? 58  THR AAA CB  1 
ATOM   434  O  OG1 . THR A 1 58  ? -8.706  12.478  16.884  1.000 17.381 ? 58  THR AAA OG1 1 
ATOM   435  C  CG2 . THR A 1 58  ? -8.873  14.148  15.086  1.000 20.461 ? 58  THR AAA CG2 1 
ATOM   436  N  N   . SER A 1 59  ? -5.918  11.122  17.035  1.000 11.111 ? 59  SER AAA N   1 
ATOM   437  C  CA  A SER A 1 59  ? -5.088  10.615  18.153  0.500 11.534 ? 59  SER AAA CA  1 
ATOM   438  C  CA  B SER A 1 59  ? -5.102  10.580  18.141  0.500 12.045 ? 59  SER AAA CA  1 
ATOM   439  C  C   . SER A 1 59  ? -3.626  10.484  17.714  1.000 10.893 ? 59  SER AAA C   1 
ATOM   440  O  O   . SER A 1 59  ? -2.744  10.312  18.563  1.000 10.941 ? 59  SER AAA O   1 
ATOM   441  C  CB  A SER A 1 59  ? -5.628  9.326   18.744  0.500 11.920 ? 59  SER AAA CB  1 
ATOM   442  C  CB  B SER A 1 59  ? -5.678  9.238   18.581  0.500 12.872 ? 59  SER AAA CB  1 
ATOM   443  O  OG  A SER A 1 59  ? -6.272  8.518   17.798  0.500 10.993 ? 59  SER AAA OG  1 
ATOM   444  O  OG  B SER A 1 59  ? -7.030  9.345   19.023  0.500 14.095 ? 59  SER AAA OG  1 
ATOM   445  N  N   . ALA A 1 60  ? -3.362  10.612  16.406  1.000 11.995 ? 60  ALA AAA N   1 
ATOM   446  C  CA  . ALA A 1 60  ? -2.007  10.530  15.855  1.000 11.679 ? 60  ALA AAA CA  1 
ATOM   447  C  C   . ALA A 1 60  ? -1.113  11.700  16.250  1.000 10.600 ? 60  ALA AAA C   1 
ATOM   448  O  O   . ALA A 1 60  ? 0.083   11.615  16.087  1.000 10.704 ? 60  ALA AAA O   1 
ATOM   449  C  CB  . ALA A 1 60  ? -2.110  10.435  14.364  1.000 14.567 ? 60  ALA AAA CB  1 
ATOM   450  N  N   . GLY A 1 61  ? -1.683  12.798  16.727  1.000 9.519  ? 61  GLY AAA N   1 
ATOM   451  C  CA  . GLY A 1 61  ? -0.835  13.920  17.147  1.000 9.466  ? 61  GLY AAA CA  1 
ATOM   452  C  C   . GLY A 1 61  ? -0.229  14.652  15.963  1.000 9.293  ? 61  GLY AAA C   1 
ATOM   453  O  O   . GLY A 1 61  ? -0.741  14.569  14.837  1.000 9.920  ? 61  GLY AAA O   1 
ATOM   454  N  N   . PRO A 1 62  ? 0.817   15.459  16.215  1.000 9.421  ? 62  PRO AAA N   1 
ATOM   455  C  CA  . PRO A 1 62  ? 1.381   16.323  15.194  1.000 10.371 ? 62  PRO AAA CA  1 
ATOM   456  C  C   . PRO A 1 62  ? 2.312   15.526  14.294  1.000 9.534  ? 62  PRO AAA C   1 
ATOM   457  O  O   . PRO A 1 62  ? 2.500   14.326  14.422  1.000 9.580  ? 62  PRO AAA O   1 
ATOM   458  C  CB  . PRO A 1 62  ? 2.101   17.377  15.999  1.000 12.499 ? 62  PRO AAA CB  1 
ATOM   459  C  CG  . PRO A 1 62  ? 2.560   16.660  17.180  1.000 12.158 ? 62  PRO AAA CG  1 
ATOM   460  C  CD  . PRO A 1 62  ? 1.443   15.686  17.520  1.000 10.357 ? 62  PRO AAA CD  1 
ATOM   461  N  N   . HIS A 1 63  ? 2.939   16.183  13.337  1.000 8.850  ? 63  HIS AAA N   1 
ATOM   462  C  CA  . HIS A 1 63  ? 3.934   15.535  12.455  1.000 8.348  ? 63  HIS AAA CA  1 
ATOM   463  C  C   . HIS A 1 63  ? 5.082   14.965  13.304  1.000 8.062  ? 63  HIS AAA C   1 
ATOM   464  O  O   . HIS A 1 63  ? 5.522   15.523  14.304  1.000 9.560  ? 63  HIS AAA O   1 
ATOM   465  C  CB  . HIS A 1 63  ? 4.543   16.548  11.475  1.000 8.722  ? 63  HIS AAA CB  1 
ATOM   466  C  CG  . HIS A 1 63  ? 3.554   17.057  10.476  1.000 10.069 ? 63  HIS AAA CG  1 
ATOM   467  N  ND1 . HIS A 1 63  ? 3.890   18.027  9.544   1.000 9.299  ? 63  HIS AAA ND1 1 
ATOM   468  C  CD2 . HIS A 1 63  ? 2.244   16.733  10.290  1.000 11.385 ? 63  HIS AAA CD2 1 
ATOM   469  C  CE1 . HIS A 1 63  ? 2.799   18.277  8.801   1.000 11.377 ? 63  HIS AAA CE1 1 
ATOM   470  N  NE2 . HIS A 1 63  ? 1.745   17.534  9.284   1.000 13.461 ? 63  HIS AAA NE2 1 
ATOM   471  N  N   . PHE A 1 64  ? 5.589   13.830  12.884  1.000 7.673  ? 64  PHE AAA N   1 
ATOM   472  C  CA  . PHE A 1 64  ? 6.748   13.161  13.502  1.000 7.826  ? 64  PHE AAA CA  1 
ATOM   473  C  C   . PHE A 1 64  ? 7.950   14.050  13.313  1.000 7.742  ? 64  PHE AAA C   1 
ATOM   474  O  O   . PHE A 1 64  ? 8.388   14.349  12.224  1.000 7.985  ? 64  PHE AAA O   1 
ATOM   475  C  CB  . PHE A 1 64  ? 6.928   11.791  12.874  1.000 7.802  ? 64  PHE AAA CB  1 
ATOM   476  C  CG  . PHE A 1 64  ? 8.092   10.991  13.401  1.000 9.696  ? 64  PHE AAA CG  1 
ATOM   477  C  CD1 . PHE A 1 64  ? 8.344   10.865  14.763  1.000 10.322 ? 64  PHE AAA CD1 1 
ATOM   478  C  CD2 . PHE A 1 64  ? 8.960   10.365  12.515  1.000 9.446  ? 64  PHE AAA CD2 1 
ATOM   479  C  CE1 . PHE A 1 64  ? 9.416   10.101  15.220  1.000 11.641 ? 64  PHE AAA CE1 1 
ATOM   480  C  CE2 . PHE A 1 64  ? 10.021  9.574   12.975  1.000 10.788 ? 64  PHE AAA CE2 1 
ATOM   481  C  CZ  . PHE A 1 64  ? 10.239  9.455   14.336  1.000 11.519 ? 64  PHE AAA CZ  1 
ATOM   482  N  N   . ASN A 1 65  ? 8.506   14.492  14.441  1.000 9.139  ? 65  ASN AAA N   1 
ATOM   483  C  CA  . ASN A 1 65  ? 9.516   15.576  14.474  1.000 9.357  ? 65  ASN AAA CA  1 
ATOM   484  C  C   . ASN A 1 65  ? 10.550  15.264  15.543  1.000 10.477 ? 65  ASN AAA C   1 
ATOM   485  O  O   . ASN A 1 65  ? 10.764  16.081  16.446  1.000 11.394 ? 65  ASN AAA O   1 
ATOM   486  C  CB  . ASN A 1 65  ? 8.862   16.920  14.683  1.000 9.920  ? 65  ASN AAA CB  1 
ATOM   487  C  CG  . ASN A 1 65  ? 9.811   18.093  14.569  1.000 9.288  ? 65  ASN AAA CG  1 
ATOM   488  O  OD1 . ASN A 1 65  ? 10.839  18.010  13.918  1.000 8.641  ? 65  ASN AAA OD1 1 
ATOM   489  N  ND2 . ASN A 1 65  ? 9.420   19.214  15.128  1.000 10.736 ? 65  ASN AAA ND2 1 
ATOM   490  N  N   . PRO A 1 66  ? 11.273  14.143  15.445  1.000 10.497 ? 66  PRO AAA N   1 
ATOM   491  C  CA  . PRO A 1 66  ? 12.220  13.768  16.491  1.000 11.001 ? 66  PRO AAA CA  1 
ATOM   492  C  C   . PRO A 1 66  ? 13.378  14.754  16.636  1.000 11.995 ? 66  PRO AAA C   1 
ATOM   493  O  O   . PRO A 1 66  ? 14.029  14.755  17.694  1.000 13.611 ? 66  PRO AAA O   1 
ATOM   494  C  CB  . PRO A 1 66  ? 12.699  12.374  16.038  1.000 11.156 ? 66  PRO AAA CB  1 
ATOM   495  C  CG  . PRO A 1 66  ? 12.552  12.393  14.546  1.000 11.009 ? 66  PRO AAA CG  1 
ATOM   496  C  CD  . PRO A 1 66  ? 11.260  13.162  14.346  1.000 10.819 ? 66  PRO AAA CD  1 
ATOM   497  N  N   . LEU A 1 67  ? 13.713  15.517  15.617  1.000 11.164 ? 67  LEU AAA N   1 
ATOM   498  C  CA  . LEU A 1 67  ? 14.873  16.436  15.644  1.000 11.648 ? 67  LEU AAA CA  1 
ATOM   499  C  C   . LEU A 1 67  ? 14.443  17.896  15.882  1.000 11.442 ? 67  LEU AAA C   1 
ATOM   500  O  O   . LEU A 1 67  ? 15.299  18.814  15.819  1.000 12.058 ? 67  LEU AAA O   1 
ATOM   501  C  CB  . LEU A 1 67  ? 15.640  16.301  14.340  1.000 13.772 ? 67  LEU AAA CB  1 
ATOM   502  C  CG  . LEU A 1 67  ? 16.176  14.903  14.066  1.000 16.994 ? 67  LEU AAA CG  1 
ATOM   503  C  CD1 . LEU A 1 67  ? 17.030  14.943  12.815  1.000 21.050 ? 67  LEU AAA CD1 1 
ATOM   504  C  CD2 . LEU A 1 67  ? 16.956  14.344  15.264  1.000 18.625 ? 67  LEU AAA CD2 1 
ATOM   505  N  N   A SER A 1 68  ? 13.182  18.138  16.243  0.300 9.741  ? 68  SER AAA N   1 
ATOM   506  N  N   B SER A 1 68  ? 13.183  18.144  16.218  0.700 12.067 ? 68  SER AAA N   1 
ATOM   507  C  CA  A SER A 1 68  ? 12.693  19.454  16.738  0.300 8.982  ? 68  SER AAA CA  1 
ATOM   508  C  CA  B SER A 1 68  ? 12.707  19.456  16.722  0.700 13.283 ? 68  SER AAA CA  1 
ATOM   509  C  C   A SER A 1 68  ? 12.957  20.545  15.697  0.300 9.692  ? 68  SER AAA C   1 
ATOM   510  C  C   B SER A 1 68  ? 12.967  20.545  15.689  0.700 12.075 ? 68  SER AAA C   1 
ATOM   511  O  O   A SER A 1 68  ? 13.446  21.633  16.072  0.300 10.292 ? 68  SER AAA O   1 
ATOM   512  O  O   B SER A 1 68  ? 13.433  21.658  16.050  0.700 13.330 ? 68  SER AAA O   1 
ATOM   513  C  CB  A SER A 1 68  ? 13.307  19.815  18.090  0.300 8.297  ? 68  SER AAA CB  1 
ATOM   514  C  CB  B SER A 1 68  ? 13.334  19.839  18.047  0.700 16.888 ? 68  SER AAA CB  1 
ATOM   515  O  OG  A SER A 1 68  ? 13.087  18.764  19.034  0.300 6.484  ? 68  SER AAA OG  1 
ATOM   516  O  OG  B SER A 1 68  ? 12.705  21.012  18.515  0.700 26.508 ? 68  SER AAA OG  1 
ATOM   517  N  N   . ARG A 1 69  ? 12.590  20.300  14.431  1.000 10.489 ? 69  ARG AAA N   1 
ATOM   518  C  CA  . ARG A 1 69  ? 12.706  21.311  13.361  1.000 11.325 ? 69  ARG AAA CA  1 
ATOM   519  C  C   . ARG A 1 69  ? 11.362  21.927  13.011  1.000 10.877 ? 69  ARG AAA C   1 
ATOM   520  O  O   . ARG A 1 69  ? 10.322  21.442  13.434  1.000 10.673 ? 69  ARG AAA O   1 
ATOM   521  C  CB  . ARG A 1 69  ? 13.302  20.654  12.116  1.000 12.987 ? 69  ARG AAA CB  1 
ATOM   522  C  CG  . ARG A 1 69  ? 14.596  19.921  12.358  1.000 16.833 ? 69  ARG AAA CG  1 
ATOM   523  C  CD  . ARG A 1 69  ? 15.601  20.867  12.935  1.000 19.960 ? 69  ARG AAA CD  1 
ATOM   524  N  NE  . ARG A 1 69  ? 16.395  21.347  11.840  1.000 27.096 ? 69  ARG AAA NE  1 
ATOM   525  C  CZ  . ARG A 1 69  ? 17.224  20.535  11.180  1.000 31.351 ? 69  ARG AAA CZ  1 
ATOM   526  N  NH1 . ARG A 1 69  ? 17.354  19.259  11.531  1.000 31.413 ? 69  ARG AAA NH1 1 
ATOM   527  N  NH2 . ARG A 1 69  ? 17.894  20.984  10.147  1.000 37.737 ? 69  ARG AAA NH2 1 
ATOM   528  N  N   . LYS A 1 70  ? 11.370  22.953  12.188  1.000 10.706 ? 70  LYS AAA N   1 
ATOM   529  C  CA  . LYS A 1 70  ? 10.131  23.475  11.586  1.000 11.157 ? 70  LYS AAA CA  1 
ATOM   530  C  C   . LYS A 1 70  ? 9.662   22.594  10.414  1.000 10.544 ? 70  LYS AAA C   1 
ATOM   531  O  O   . LYS A 1 70  ? 10.458  21.854  9.840   1.000 10.636 ? 70  LYS AAA O   1 
ATOM   532  C  CB  . LYS A 1 70  ? 10.383  24.907  11.098  1.000 13.195 ? 70  LYS AAA CB  1 
ATOM   533  C  CG  . LYS A 1 70  ? 10.627  25.913  12.214  1.000 15.250 ? 70  LYS AAA CG  1 
ATOM   534  C  CD  . LYS A 1 70  ? 11.239  27.221  11.772  1.000 19.377 ? 70  LYS AAA CD  1 
ATOM   535  C  CE  . LYS A 1 70  ? 10.426  27.988  10.767  1.000 21.393 ? 70  LYS AAA CE  1 
ATOM   536  N  NZ  . LYS A 1 70  ? 11.191  29.199  10.346  1.000 25.468 ? 70  LYS AAA NZ  1 
ATOM   537  N  N   . HIS A 1 71  ? 8.394   22.746  10.070  1.000 10.112 ? 71  HIS AAA N   1 
ATOM   538  C  CA  . HIS A 1 71  ? 7.751   22.035  8.948   1.000 9.896  ? 71  HIS AAA CA  1 
ATOM   539  C  C   . HIS A 1 71  ? 8.375   22.509  7.644   1.000 9.761  ? 71  HIS AAA C   1 
ATOM   540  O  O   . HIS A 1 71  ? 8.550   23.741  7.446   1.000 11.716 ? 71  HIS AAA O   1 
ATOM   541  C  CB  . HIS A 1 71  ? 6.252   22.273  8.966   1.000 10.311 ? 71  HIS AAA CB  1 
ATOM   542  C  CG  . HIS A 1 71  ? 5.557   21.622  7.854   1.000 9.613  ? 71  HIS AAA CG  1 
ATOM   543  N  ND1 . HIS A 1 71  ? 5.332   20.282  7.828   1.000 8.076  ? 71  HIS AAA ND1 1 
ATOM   544  C  CD2 . HIS A 1 71  ? 5.072   22.131  6.691   1.000 9.361  ? 71  HIS AAA CD2 1 
ATOM   545  C  CE1 . HIS A 1 71  ? 4.729   19.968  6.697   1.000 8.812  ? 71  HIS AAA CE1 1 
ATOM   546  N  NE2 . HIS A 1 71  ? 4.576   21.107  5.953   1.000 8.771  ? 71  HIS AAA NE2 1 
ATOM   547  N  N   . GLY A 1 72  ? 8.586   21.599  6.707   1.000 9.517  ? 72  GLY AAA N   1 
ATOM   548  C  CA  . GLY A 1 72  ? 9.047   21.949  5.363   1.000 9.729  ? 72  GLY AAA CA  1 
ATOM   549  C  C   . GLY A 1 72  ? 8.621   20.923  4.360   1.000 10.291 ? 72  GLY AAA C   1 
ATOM   550  O  O   . GLY A 1 72  ? 7.718   20.084  4.641   1.000 10.300 ? 72  GLY AAA O   1 
ATOM   551  N  N   . GLY A 1 73  ? 9.155   21.022  3.160   1.000 9.721  ? 73  GLY AAA N   1 
ATOM   552  C  CA  . GLY A 1 73  ? 8.933   20.010  2.137   1.000 10.174 ? 73  GLY AAA CA  1 
ATOM   553  C  C   . GLY A 1 73  ? 10.013  18.939  2.228   1.000 9.824  ? 73  GLY AAA C   1 
ATOM   554  O  O   . GLY A 1 73  ? 11.064  19.136  2.859   1.000 10.257 ? 73  GLY AAA O   1 
ATOM   555  N  N   . PRO A 1 74  ? 9.823   17.804  1.563   1.000 9.969  ? 74  PRO AAA N   1 
ATOM   556  C  CA  . PRO A 1 74  ? 10.748  16.700  1.690   1.000 10.815 ? 74  PRO AAA CA  1 
ATOM   557  C  C   . PRO A 1 74  ? 12.154  17.027  1.179   1.000 11.783 ? 74  PRO AAA C   1 
ATOM   558  O  O   . PRO A 1 74  ? 13.107  16.429  1.697   1.000 11.973 ? 74  PRO AAA O   1 
ATOM   559  C  CB  . PRO A 1 74  ? 10.083  15.552  0.934   1.000 11.637 ? 74  PRO AAA CB  1 
ATOM   560  C  CG  . PRO A 1 74  ? 9.039   16.206  0.086   1.000 12.004 ? 74  PRO AAA CG  1 
ATOM   561  C  CD  . PRO A 1 74  ? 8.607   17.458  0.816   1.000 10.769 ? 74  PRO AAA CD  1 
ATOM   562  N  N   . LYS A 1 75  ? 12.260  17.957  0.243   1.000 12.934 ? 75  LYS AAA N   1 
ATOM   563  C  CA  . LYS A 1 75  ? 13.575  18.311  -0.339  1.000 15.241 ? 75  LYS AAA CA  1 
ATOM   564  C  C   . LYS A 1 75  ? 14.306  19.293  0.564   1.000 14.806 ? 75  LYS AAA C   1 
ATOM   565  O  O   . LYS A 1 75  ? 15.523  19.534  0.287   1.000 17.090 ? 75  LYS AAA O   1 
ATOM   566  C  CB  . LYS A 1 75  ? 13.443  18.930  -1.736  1.000 17.205 ? 75  LYS AAA CB  1 
ATOM   567  C  CG  . LYS A 1 75  ? 13.012  17.957  -2.816  1.000 21.922 ? 75  LYS AAA CG  1 
ATOM   568  C  CD  . LYS A 1 75  ? 12.850  18.610  -4.191  1.000 27.735 ? 75  LYS AAA CD  1 
ATOM   569  C  CE  . LYS A 1 75  ? 11.642  19.509  -4.302  1.000 30.470 ? 75  LYS AAA CE  1 
ATOM   570  N  NZ  . LYS A 1 75  ? 10.957  19.361  -5.611  1.000 34.911 ? 75  LYS AAA NZ  1 
ATOM   571  N  N   . ASP A 1 76  ? 13.675  19.876  1.578   1.000 12.513 ? 76  ASP AAA N   1 
ATOM   572  C  CA  . ASP A 1 76  ? 14.298  20.915  2.435   1.000 14.356 ? 76  ASP AAA CA  1 
ATOM   573  C  C   . ASP A 1 76  ? 15.124  20.283  3.547   1.000 15.923 ? 76  ASP AAA C   1 
ATOM   574  O  O   . ASP A 1 76  ? 14.705  19.290  4.158   1.000 16.463 ? 76  ASP AAA O   1 
ATOM   575  C  CB  . ASP A 1 76  ? 13.234  21.803  3.053   1.000 14.829 ? 76  ASP AAA CB  1 
ATOM   576  C  CG  . ASP A 1 76  ? 12.401  22.530  2.026   1.000 17.658 ? 76  ASP AAA CG  1 
ATOM   577  O  OD1 . ASP A 1 76  ? 12.908  22.762  0.876   1.000 21.574 ? 76  ASP AAA OD1 1 
ATOM   578  O  OD2 . ASP A 1 76  ? 11.262  22.809  2.363   1.000 17.499 ? 76  ASP AAA OD2 1 
ATOM   579  N  N   . GLU A 1 77  ? 16.226  20.932  3.903   1.000 15.153 ? 77  GLU AAA N   1 
ATOM   580  C  CA  . GLU A 1 77  ? 17.007  20.542  5.097   1.000 15.204 ? 77  GLU AAA CA  1 
ATOM   581  C  C   . GLU A 1 77  ? 16.167  20.830  6.339   1.000 13.702 ? 77  GLU AAA C   1 
ATOM   582  O  O   . GLU A 1 77  ? 16.176  20.020  7.267   1.000 14.943 ? 77  GLU AAA O   1 
ATOM   583  C  CB  . GLU A 1 77  ? 18.354  21.275  5.070   1.000 18.115 ? 77  GLU AAA CB  1 
ATOM   584  C  CG  . GLU A 1 77  ? 19.302  20.749  6.106   1.000 21.215 ? 77  GLU AAA CG  1 
ATOM   585  C  CD  . GLU A 1 77  ? 19.103  21.321  7.491   1.000 22.186 ? 77  GLU AAA CD  1 
ATOM   586  O  OE1 . GLU A 1 77  ? 18.523  22.424  7.607   1.000 23.837 ? 77  GLU AAA OE1 1 
ATOM   587  O  OE2 . GLU A 1 77  ? 19.530  20.647  8.459   1.000 27.015 ? 77  GLU AAA OE2 1 
ATOM   588  N  N   A GLU A 1 78  ? 15.494  21.984  6.396   0.500 12.988 ? 78  GLU AAA N   1 
ATOM   589  N  N   B GLU A 1 78  ? 15.481  21.968  6.329   0.500 13.118 ? 78  GLU AAA N   1 
ATOM   590  C  CA  A GLU A 1 78  ? 14.604  22.317  7.540   0.500 12.490 ? 78  GLU AAA CA  1 
ATOM   591  C  CA  B GLU A 1 78  ? 14.561  22.356  7.410   0.500 12.692 ? 78  GLU AAA CA  1 
ATOM   592  C  C   A GLU A 1 78  ? 13.220  21.698  7.281   0.500 11.145 ? 78  GLU AAA C   1 
ATOM   593  C  C   B GLU A 1 78  ? 13.236  21.631  7.156   0.500 10.856 ? 78  GLU AAA C   1 
ATOM   594  O  O   A GLU A 1 78  ? 12.327  22.371  6.737   0.500 11.382 ? 78  GLU AAA O   1 
ATOM   595  O  O   B GLU A 1 78  ? 12.471  22.079  6.279   0.500 10.802 ? 78  GLU AAA O   1 
ATOM   596  C  CB  A GLU A 1 78  ? 14.502  23.822  7.804   0.500 13.292 ? 78  GLU AAA CB  1 
ATOM   597  C  CB  B GLU A 1 78  ? 14.365  23.870  7.426   0.500 14.048 ? 78  GLU AAA CB  1 
ATOM   598  C  CG  A GLU A 1 78  ? 13.747  24.174  9.073   0.500 14.358 ? 78  GLU AAA CG  1 
ATOM   599  C  CG  B GLU A 1 78  ? 13.488  24.320  8.559   0.500 15.247 ? 78  GLU AAA CG  1 
ATOM   600  C  CD  A GLU A 1 78  ? 14.520  24.063  10.383  0.500 14.980 ? 78  GLU AAA CD  1 
ATOM   601  C  CD  B GLU A 1 78  ? 13.344  25.820  8.678   0.500 17.752 ? 78  GLU AAA CD  1 
ATOM   602  O  OE1 A GLU A 1 78  ? 15.742  23.959  10.310  0.500 18.646 ? 78  GLU AAA OE1 1 
ATOM   603  O  OE1 B GLU A 1 78  ? 12.664  26.424  7.817   0.500 20.176 ? 78  GLU AAA OE1 1 
ATOM   604  O  OE2 A GLU A 1 78  ? 13.908  24.089  11.498  0.500 15.320 ? 78  GLU AAA OE2 1 
ATOM   605  O  OE2 B GLU A 1 78  ? 13.882  26.364  9.660   0.500 21.920 ? 78  GLU AAA OE2 1 
ATOM   606  N  N   . ARG A 1 79  ? 13.001  20.519  7.858   1.000 10.161 ? 79  ARG AAA N   1 
ATOM   607  C  CA  . ARG A 1 79  ? 11.737  19.753  7.719   1.000 9.428  ? 79  ARG AAA CA  1 
ATOM   608  C  C   . ARG A 1 79  ? 11.608  18.903  8.965   1.000 9.239  ? 79  ARG AAA C   1 
ATOM   609  O  O   . ARG A 1 79  ? 12.607  18.614  9.658   1.000 10.136 ? 79  ARG AAA O   1 
ATOM   610  C  CB  . ARG A 1 79  ? 11.735  18.888  6.458   1.000 10.146 ? 79  ARG AAA CB  1 
ATOM   611  C  CG  . ARG A 1 79  ? 12.884  17.897  6.380   1.000 10.503 ? 79  ARG AAA CG  1 
ATOM   612  C  CD  . ARG A 1 79  ? 12.712  16.916  5.246   1.000 10.149 ? 79  ARG AAA CD  1 
ATOM   613  N  NE  . ARG A 1 79  ? 11.888  15.757  5.619   1.000 9.201  ? 79  ARG AAA NE  1 
ATOM   614  C  CZ  . ARG A 1 79  ? 11.850  14.654  4.912   1.000 9.123  ? 79  ARG AAA CZ  1 
ATOM   615  N  NH1 . ARG A 1 79  ? 11.233  13.582  5.377   1.000 9.737  ? 79  ARG AAA NH1 1 
ATOM   616  N  NH2 . ARG A 1 79  ? 12.476  14.588  3.762   1.000 9.907  ? 79  ARG AAA NH2 1 
ATOM   617  N  N   . HIS A 1 80  ? 10.410  18.469  9.212   1.000 9.081  ? 80  HIS AAA N   1 
ATOM   618  C  CA  . HIS A 1 80  ? 10.155  17.346  10.126  1.000 8.144  ? 80  HIS AAA CA  1 
ATOM   619  C  C   . HIS A 1 80  ? 10.559  16.043  9.452   1.000 8.393  ? 80  HIS AAA C   1 
ATOM   620  O  O   . HIS A 1 80  ? 10.403  15.918  8.242   1.000 8.379  ? 80  HIS AAA O   1 
ATOM   621  C  CB  . HIS A 1 80  ? 8.659   17.296  10.465  1.000 8.537  ? 80  HIS AAA CB  1 
ATOM   622  C  CG  . HIS A 1 80  ? 8.114   18.557  11.036  1.000 7.660  ? 80  HIS AAA CG  1 
ATOM   623  N  ND1 . HIS A 1 80  ? 6.835   18.974  10.796  1.000 7.943  ? 80  HIS AAA ND1 1 
ATOM   624  C  CD2 . HIS A 1 80  ? 8.629   19.433  11.945  1.000 9.225  ? 80  HIS AAA CD2 1 
ATOM   625  C  CE1 . HIS A 1 80  ? 6.576   20.057  11.526  1.000 8.486  ? 80  HIS AAA CE1 1 
ATOM   626  N  NE2 . HIS A 1 80  ? 7.660   20.330  12.299  1.000 9.806  ? 80  HIS AAA NE2 1 
ATOM   627  N  N   . VAL A 1 81  ? 10.962  15.046  10.221  1.000 8.232  ? 81  VAL AAA N   1 
ATOM   628  C  CA  . VAL A 1 81  ? 11.222  13.723  9.621   1.000 8.998  ? 81  VAL AAA CA  1 
ATOM   629  C  C   . VAL A 1 81  ? 9.974   13.248  8.865   1.000 7.955  ? 81  VAL AAA C   1 
ATOM   630  O  O   . VAL A 1 81  ? 10.087  12.640  7.782   1.000 8.864  ? 81  VAL AAA O   1 
ATOM   631  C  CB  . VAL A 1 81  ? 11.724  12.700  10.657  1.000 9.058  ? 81  VAL AAA CB  1 
ATOM   632  C  CG1 . VAL A 1 81  ? 11.728  11.295  10.086  1.000 8.979  ? 81  VAL AAA CG1 1 
ATOM   633  C  CG2 . VAL A 1 81  ? 13.112  13.039  11.168  1.000 9.838  ? 81  VAL AAA CG2 1 
ATOM   634  N  N   . GLY A 1 82  ? 8.780   13.501  9.400   1.000 7.186  ? 82  GLY AAA N   1 
ATOM   635  C  CA  . GLY A 1 82  ? 7.549   13.013  8.780   1.000 7.638  ? 82  GLY AAA CA  1 
ATOM   636  C  C   . GLY A 1 82  ? 7.048   13.811  7.611   1.000 7.998  ? 82  GLY AAA C   1 
ATOM   637  O  O   . GLY A 1 82  ? 5.980   13.444  7.085   1.000 8.807  ? 82  GLY AAA O   1 
ATOM   638  N  N   . ASP A 1 83  ? 7.795   14.779  7.093   1.000 8.118  ? 83  ASP AAA N   1 
ATOM   639  C  CA  . ASP A 1 83  ? 7.322   15.647  5.993   1.000 8.051  ? 83  ASP AAA CA  1 
ATOM   640  C  C   . ASP A 1 83  ? 7.581   15.028  4.624   1.000 9.307  ? 83  ASP AAA C   1 
ATOM   641  O  O   . ASP A 1 83  ? 8.659   15.230  4.046   1.000 10.551 ? 83  ASP AAA O   1 
ATOM   642  C  CB  . ASP A 1 83  ? 7.968   17.009  6.123   1.000 8.587  ? 83  ASP AAA CB  1 
ATOM   643  C  CG  . ASP A 1 83  ? 7.486   17.802  7.287   1.000 8.154  ? 83  ASP AAA CG  1 
ATOM   644  O  OD1 . ASP A 1 83  ? 6.403   17.452  7.805   1.000 9.458  ? 83  ASP AAA OD1 1 
ATOM   645  O  OD2 . ASP A 1 83  ? 8.135   18.833  7.627   1.000 8.594  ? 83  ASP AAA OD2 1 
ATOM   646  N  N   . LEU A 1 84  ? 6.603   14.283  4.111   1.000 8.488  ? 84  LEU AAA N   1 
ATOM   647  C  CA  . LEU A 1 84  ? 6.704   13.603  2.800   1.000 9.353  ? 84  LEU AAA CA  1 
ATOM   648  C  C   . LEU A 1 84  ? 5.970   14.409  1.736   1.000 9.334  ? 84  LEU AAA C   1 
ATOM   649  O  O   . LEU A 1 84  ? 5.771   13.874  0.604   1.000 11.874 ? 84  LEU AAA O   1 
ATOM   650  C  CB  . LEU A 1 84  ? 6.207   12.168  2.914   1.000 9.230  ? 84  LEU AAA CB  1 
ATOM   651  C  CG  . LEU A 1 84  ? 7.057   11.299  3.860   1.000 10.577 ? 84  LEU AAA CG  1 
ATOM   652  C  CD1 . LEU A 1 84  ? 6.470   9.899   3.892   1.000 11.780 ? 84  LEU AAA CD1 1 
ATOM   653  C  CD2 . LEU A 1 84  ? 8.537   11.259  3.449   1.000 12.472 ? 84  LEU AAA CD2 1 
ATOM   654  N  N   . GLY A 1 85  ? 5.646   15.658  1.990   1.000 9.217  ? 85  GLY AAA N   1 
ATOM   655  C  CA  . GLY A 1 85  ? 5.141   16.548  0.916   1.000 9.464  ? 85  GLY AAA CA  1 
ATOM   656  C  C   . GLY A 1 85  ? 3.688   16.249  0.580   1.000 9.342  ? 85  GLY AAA C   1 
ATOM   657  O  O   . GLY A 1 85  ? 2.827   16.222  1.457   1.000 10.420 ? 85  GLY AAA O   1 
ATOM   658  N  N   . ASN A 1 86  ? 3.398   16.142  -0.714  1.000 9.569  ? 86  ASN AAA N   1 
ATOM   659  C  CA  . ASN A 1 86  ? 2.028   15.894  -1.237  1.000 9.165  ? 86  ASN AAA CA  1 
ATOM   660  C  C   . ASN A 1 86  ? 2.018   14.659  -2.097  1.000 9.488  ? 86  ASN AAA C   1 
ATOM   661  O  O   . ASN A 1 86  ? 2.981   14.398  -2.803  1.000 11.133 ? 86  ASN AAA O   1 
ATOM   662  C  CB  . ASN A 1 86  ? 1.566   17.072  -2.108  1.000 9.886  ? 86  ASN AAA CB  1 
ATOM   663  C  CG  . ASN A 1 86  ? 1.318   18.304  -1.278  1.000 9.494  ? 86  ASN AAA CG  1 
ATOM   664  O  OD1 . ASN A 1 86  ? 0.374   18.320  -0.488  1.000 10.235 ? 86  ASN AAA OD1 1 
ATOM   665  N  ND2 . ASN A 1 86  ? 2.163   19.326  -1.457  1.000 11.633 ? 86  ASN AAA ND2 1 
ATOM   666  N  N   . VAL A 1 87  ? 0.880   14.030  -2.160  1.000 9.291  ? 87  VAL AAA N   1 
ATOM   667  C  CA  . VAL A 1 87  ? 0.544   13.073  -3.231  1.000 9.448  ? 87  VAL AAA CA  1 
ATOM   668  C  C   . VAL A 1 87  ? -0.474  13.766  -4.114  1.000 9.037  ? 87  VAL AAA C   1 
ATOM   669  O  O   . VAL A 1 87  ? -1.097  14.736  -3.669  1.000 10.041 ? 87  VAL AAA O   1 
ATOM   670  C  CB  . VAL A 1 87  ? 0.057   11.740  -2.664  1.000 10.348 ? 87  VAL AAA CB  1 
ATOM   671  C  CG1 . VAL A 1 87  ? 1.174   11.063  -1.859  1.000 11.682 ? 87  VAL AAA CG1 1 
ATOM   672  C  CG2 . VAL A 1 87  ? -1.233  11.869  -1.888  1.000 11.369 ? 87  VAL AAA CG2 1 
ATOM   673  N  N   . THR A 1 88  ? -0.642  13.241  -5.325  1.000 9.409  ? 88  THR AAA N   1 
ATOM   674  C  CA  . THR A 1 88  ? -1.504  13.860  -6.348  1.000 9.476  ? 88  THR AAA CA  1 
ATOM   675  C  C   . THR A 1 88  ? -2.547  12.887  -6.823  1.000 9.346  ? 88  THR AAA C   1 
ATOM   676  O  O   . THR A 1 88  ? -2.213  11.805  -7.280  1.000 10.424 ? 88  THR AAA O   1 
ATOM   677  C  CB  . THR A 1 88  ? -0.693  14.307  -7.558  1.000 11.246 ? 88  THR AAA CB  1 
ATOM   678  O  OG1 . THR A 1 88  ? 0.289   15.254  -7.163  1.000 13.044 ? 88  THR AAA OG1 1 
ATOM   679  C  CG2 . THR A 1 88  ? -1.577  14.915  -8.616  1.000 13.057 ? 88  THR AAA CG2 1 
ATOM   680  N  N   . ALA A 1 89  ? -3.805  13.263  -6.654  1.000 10.130 ? 89  ALA AAA N   1 
ATOM   681  C  CA  . ALA A 1 89  ? -4.930  12.500  -7.168  1.000 10.450 ? 89  ALA AAA CA  1 
ATOM   682  C  C   . ALA A 1 89  ? -5.356  13.056  -8.537  1.000 11.137 ? 89  ALA AAA C   1 
ATOM   683  O  O   . ALA A 1 89  ? -5.414  14.254  -8.719  1.000 12.312 ? 89  ALA AAA O   1 
ATOM   684  C  CB  . ALA A 1 89  ? -6.056  12.579  -6.179  1.000 11.253 ? 89  ALA AAA CB  1 
ATOM   685  N  N   . ASP A 1 90  ? -5.662  12.115  -9.403  1.000 12.322 ? 90  ASP AAA N   1 
ATOM   686  C  CA  . ASP A 1 90  ? -6.187  12.378  -10.766 1.000 14.173 ? 90  ASP AAA CA  1 
ATOM   687  C  C   . ASP A 1 90  ? -7.697  12.595  -10.689 1.000 14.778 ? 90  ASP AAA C   1 
ATOM   688  O  O   . ASP A 1 90  ? -8.316  12.518  -9.618  1.000 13.425 ? 90  ASP AAA O   1 
ATOM   689  C  CB  . ASP A 1 90  ? -5.769  11.215  -11.674 1.000 15.399 ? 90  ASP AAA CB  1 
ATOM   690  C  CG  . ASP A 1 90  ? -6.458  9.877   -11.412 1.000 18.390 ? 90  ASP AAA CG  1 
ATOM   691  O  OD1 . ASP A 1 90  ? -7.466  9.840   -10.694 1.000 17.309 ? 90  ASP AAA OD1 1 
ATOM   692  O  OD2 . ASP A 1 90  ? -5.981  8.852   -11.941 1.000 20.789 ? 90  ASP AAA OD2 1 
ATOM   693  N  N   . LYS A 1 91  ? -8.333  12.849  -11.830 1.000 16.225 ? 91  LYS AAA N   1 
ATOM   694  C  CA  . LYS A 1 91  ? -9.792  13.118  -11.900 1.000 17.371 ? 91  LYS AAA CA  1 
ATOM   695  C  C   . LYS A 1 91  ? -10.613 11.910  -11.459 1.000 18.434 ? 91  LYS AAA C   1 
ATOM   696  O  O   . LYS A 1 91  ? -11.792 12.131  -11.105 1.000 22.191 ? 91  LYS AAA O   1 
ATOM   697  C  CB  . LYS A 1 91  ? -10.217 13.546  -13.312 1.000 16.820 ? 91  LYS AAA CB  1 
ATOM   698  C  CG  . LYS A 1 91  ? -10.013 15.025  -13.595 1.000 18.518 ? 91  LYS AAA CG  1 
ATOM   699  C  CD  . LYS A 1 91  ? -11.049 15.903  -12.978 1.000 21.303 ? 91  LYS AAA CD  1 
ATOM   700  C  CE  . LYS A 1 91  ? -10.867 17.361  -13.321 1.000 24.397 ? 91  LYS AAA CE  1 
ATOM   701  N  NZ  . LYS A 1 91  ? -11.827 18.177  -12.547 1.000 27.008 ? 91  LYS AAA NZ  1 
ATOM   702  N  N   . ASP A 1 92  ? -10.061 10.703  -11.470 1.000 17.123 ? 92  ASP AAA N   1 
ATOM   703  C  CA  . ASP A 1 92  ? -10.761 9.487   -10.968 1.000 19.147 ? 92  ASP AAA CA  1 
ATOM   704  C  C   . ASP A 1 92  ? -10.577 9.387   -9.444  1.000 15.691 ? 92  ASP AAA C   1 
ATOM   705  O  O   . ASP A 1 92  ? -11.077 8.418   -8.867  1.000 19.229 ? 92  ASP AAA O   1 
ATOM   706  C  CB  . ASP A 1 92  ? -10.290 8.194   -11.642 1.000 21.999 ? 92  ASP AAA CB  1 
ATOM   707  C  CG  . ASP A 1 92  ? -10.815 8.000   -13.056 1.000 29.059 ? 92  ASP AAA CG  1 
ATOM   708  O  OD1 . ASP A 1 92  ? -11.735 8.758   -13.460 1.000 30.499 ? 92  ASP AAA OD1 1 
ATOM   709  O  OD2 . ASP A 1 92  ? -10.278 7.108   -13.750 1.000 32.525 ? 92  ASP AAA OD2 1 
ATOM   710  N  N   . GLY A 1 93  ? -9.881  10.333  -8.827  1.000 14.628 ? 93  GLY AAA N   1 
ATOM   711  C  CA  . GLY A 1 93  ? -9.670  10.336  -7.359  1.000 13.014 ? 93  GLY AAA CA  1 
ATOM   712  C  C   . GLY A 1 93  ? -8.560  9.383   -6.920  1.000 12.390 ? 93  GLY AAA C   1 
ATOM   713  O  O   . GLY A 1 93  ? -8.488  9.053   -5.702  1.000 12.567 ? 93  GLY AAA O   1 
ATOM   714  N  N   . VAL A 1 94  ? -7.700  8.958   -7.830  1.000 12.272 ? 94  VAL AAA N   1 
ATOM   715  C  CA  . VAL A 1 94  ? -6.634  7.991   -7.493  1.000 12.336 ? 94  VAL AAA CA  1 
ATOM   716  C  C   . VAL A 1 94  ? -5.280  8.690   -7.463  1.000 11.471 ? 94  VAL AAA C   1 
ATOM   717  O  O   . VAL A 1 94  ? -4.883  9.356   -8.430  1.000 11.469 ? 94  VAL AAA O   1 
ATOM   718  C  CB  . VAL A 1 94  ? -6.634  6.796   -8.450  1.000 13.209 ? 94  VAL AAA CB  1 
ATOM   719  C  CG1 . VAL A 1 94  ? -5.541  5.804   -8.133  1.000 14.714 ? 94  VAL AAA CG1 1 
ATOM   720  C  CG2 . VAL A 1 94  ? -8.002  6.139   -8.416  1.000 14.757 ? 94  VAL AAA CG2 1 
ATOM   721  N  N   . ALA A 1 95  ? -4.536  8.536   -6.362  1.000 11.070 ? 95  ALA AAA N   1 
ATOM   722  C  CA  . ALA A 1 95  ? -3.144  8.999   -6.273  1.000 11.989 ? 95  ALA AAA CA  1 
ATOM   723  C  C   . ALA A 1 95  ? -2.220  7.800   -6.370  1.000 12.532 ? 95  ALA AAA C   1 
ATOM   724  O  O   . ALA A 1 95  ? -2.203  6.987   -5.488  1.000 16.105 ? 95  ALA AAA O   1 
ATOM   725  C  CB  . ALA A 1 95  ? -2.916  9.765   -4.992  1.000 12.559 ? 95  ALA AAA CB  1 
ATOM   726  N  N   . ASP A 1 96  ? -1.391  7.750   -7.386  1.000 13.697 ? 96  ASP AAA N   1 
ATOM   727  C  CA  . ASP A 1 96  ? -0.306  6.760   -7.492  1.000 15.178 ? 96  ASP AAA CA  1 
ATOM   728  C  C   . ASP A 1 96  ? 0.876   7.333   -6.739  1.000 13.855 ? 96  ASP AAA C   1 
ATOM   729  O  O   . ASP A 1 96  ? 1.356   8.395   -7.082  1.000 16.366 ? 96  ASP AAA O   1 
ATOM   730  C  CB  . ASP A 1 96  ? -0.118  6.393   -8.966  1.000 18.076 ? 96  ASP AAA CB  1 
ATOM   731  C  CG  . ASP A 1 96  ? -1.288  5.541   -9.488  1.000 23.355 ? 96  ASP AAA CG  1 
ATOM   732  O  OD1 . ASP A 1 96  ? -1.774  5.835   -10.585 1.000 30.165 ? 96  ASP AAA OD1 1 
ATOM   733  O  OD2 . ASP A 1 96  ? -1.703  4.547   -8.801  1.000 28.343 ? 96  ASP AAA OD2 1 
ATOM   734  N  N   . VAL A 1 97  ? 1.287   6.669   -5.680  1.000 12.055 ? 97  VAL AAA N   1 
ATOM   735  C  CA  . VAL A 1 97  ? 2.367   7.204   -4.809  1.000 12.188 ? 97  VAL AAA CA  1 
ATOM   736  C  C   . VAL A 1 97  ? 3.674   6.583   -5.236  1.000 11.789 ? 97  VAL AAA C   1 
ATOM   737  O  O   . VAL A 1 97  ? 3.777   5.342   -5.320  1.000 10.791 ? 97  VAL AAA O   1 
ATOM   738  C  CB  . VAL A 1 97  ? 2.058   6.948   -3.331  1.000 13.710 ? 97  VAL AAA CB  1 
ATOM   739  C  CG1 . VAL A 1 97  ? 3.184   7.430   -2.428  1.000 15.278 ? 97  VAL AAA CG1 1 
ATOM   740  C  CG2 . VAL A 1 97  ? 0.705   7.557   -2.969  1.000 14.719 ? 97  VAL AAA CG2 1 
ATOM   741  N  N   . SER A 1 98  ? 4.657   7.438   -5.415  1.000 12.392 ? 98  SER AAA N   1 
ATOM   742  C  CA  . SER A 1 98  ? 5.999   7.002   -5.762  1.000 13.418 ? 98  SER AAA CA  1 
ATOM   743  C  C   . SER A 1 98  ? 6.952   8.052   -5.227  1.000 13.433 ? 98  SER AAA C   1 
ATOM   744  O  O   . SER A 1 98  ? 7.079   9.139   -5.835  1.000 16.300 ? 98  SER AAA O   1 
ATOM   745  C  CB  . SER A 1 98  ? 6.092   6.815   -7.273  1.000 16.032 ? 98  SER AAA CB  1 
ATOM   746  O  OG  . SER A 1 98  ? 7.358   6.220   -7.554  1.000 20.211 ? 98  SER AAA OG  1 
ATOM   747  N  N   . ILE A 1 99  ? 7.638   7.745   -4.130  1.000 12.305 ? 99  ILE AAA N   1 
ATOM   748  C  CA  . ILE A 1 99  ? 8.505   8.705   -3.399  1.000 12.470 ? 99  ILE AAA CA  1 
ATOM   749  C  C   . ILE A 1 99  ? 9.795   7.954   -3.081  1.000 12.655 ? 99  ILE AAA C   1 
ATOM   750  O  O   . ILE A 1 99  ? 9.756   6.739   -2.774  1.000 12.355 ? 99  ILE AAA O   1 
ATOM   751  C  CB  . ILE A 1 99  ? 7.780   9.205   -2.130  1.000 12.980 ? 99  ILE AAA CB  1 
ATOM   752  C  CG1 . ILE A 1 99  ? 6.629   10.164  -2.493  1.000 13.952 ? 99  ILE AAA CG1 1 
ATOM   753  C  CG2 . ILE A 1 99  ? 8.762   9.835   -1.158  1.000 14.347 ? 99  ILE AAA CG2 1 
ATOM   754  C  CD1 . ILE A 1 99  ? 5.677   10.478  -1.356  1.000 15.077 ? 99  ILE AAA CD1 1 
ATOM   755  N  N   . GLU A 1 100 ? 10.922  8.632   -3.112  1.000 11.534 ? 100 GLU AAA N   1 
ATOM   756  C  CA  . GLU A 1 100 ? 12.166  8.144   -2.494  1.000 12.545 ? 100 GLU AAA CA  1 
ATOM   757  C  C   . GLU A 1 100 ? 12.585  9.173   -1.462  1.000 11.887 ? 100 GLU AAA C   1 
ATOM   758  O  O   . GLU A 1 100 ? 12.597  10.370  -1.792  1.000 11.986 ? 100 GLU AAA O   1 
ATOM   759  C  CB  . GLU A 1 100 ? 13.260  7.992   -3.552  1.000 16.507 ? 100 GLU AAA CB  1 
ATOM   760  C  CG  . GLU A 1 100 ? 14.451  7.220   -3.072  1.000 21.334 ? 100 GLU AAA CG  1 
ATOM   761  C  CD  . GLU A 1 100 ? 15.410  6.772   -4.178  1.000 27.737 ? 100 GLU AAA CD  1 
ATOM   762  O  OE1 . GLU A 1 100 ? 15.292  7.301   -5.319  1.000 37.896 ? 100 GLU AAA OE1 1 
ATOM   763  O  OE2 . GLU A 1 100 ? 16.229  5.858   -3.921  1.000 35.344 ? 100 GLU AAA OE2 1 
ATOM   764  N  N   . ASP A 1 101 ? 12.831  8.781   -0.227  1.000 10.045 ? 101 ASP AAA N   1 
ATOM   765  C  CA  . ASP A 1 101 ? 13.128  9.771   0.823   1.000 10.324 ? 101 ASP AAA CA  1 
ATOM   766  C  C   . ASP A 1 101 ? 14.363  9.309   1.602   1.000 10.462 ? 101 ASP AAA C   1 
ATOM   767  O  O   . ASP A 1 101 ? 14.433  8.144   1.972   1.000 12.677 ? 101 ASP AAA O   1 
ATOM   768  C  CB  . ASP A 1 101 ? 11.937  10.022  1.760   1.000 10.168 ? 101 ASP AAA CB  1 
ATOM   769  C  CG  . ASP A 1 101 ? 12.112  11.258  2.608   1.000 10.319 ? 101 ASP AAA CG  1 
ATOM   770  O  OD1 . ASP A 1 101 ? 11.981  12.389  2.040   1.000 12.545 ? 101 ASP AAA OD1 1 
ATOM   771  O  OD2 . ASP A 1 101 ? 12.447  11.107  3.808   1.000 10.494 ? 101 ASP AAA OD2 1 
ATOM   772  N  N   . SER A 1 102 ? 15.231  10.254  1.942   1.000 12.318 ? 102 SER AAA N   1 
ATOM   773  C  CA  A SER A 1 102 ? 16.527  10.011  2.616   0.500 13.090 ? 102 SER AAA CA  1 
ATOM   774  C  CA  B SER A 1 102 ? 16.515  9.978   2.625   0.500 13.885 ? 102 SER AAA CA  1 
ATOM   775  C  C   . SER A 1 102 ? 16.457  10.373  4.101   1.000 12.791 ? 102 SER AAA C   1 
ATOM   776  O  O   . SER A 1 102 ? 17.494  10.217  4.787   1.000 14.578 ? 102 SER AAA O   1 
ATOM   777  C  CB  A SER A 1 102 ? 17.645  10.790  1.941   0.500 14.074 ? 102 SER AAA CB  1 
ATOM   778  C  CB  B SER A 1 102 ? 17.647  10.678  1.912   0.500 16.090 ? 102 SER AAA CB  1 
ATOM   779  O  OG  A SER A 1 102 ? 17.565  12.179  2.204   0.500 15.188 ? 102 SER AAA OG  1 
ATOM   780  O  OG  B SER A 1 102 ? 17.896  10.023  0.670   0.500 20.162 ? 102 SER AAA OG  1 
ATOM   781  N  N   . VAL A 1 103 ? 15.332  10.887  4.577   1.000 10.932 ? 103 VAL AAA N   1 
ATOM   782  C  CA  . VAL A 1 103 ? 15.238  11.383  5.965   1.000 10.952 ? 103 VAL AAA CA  1 
ATOM   783  C  C   . VAL A 1 103 ? 14.448  10.389  6.822   1.000 10.079 ? 103 VAL AAA C   1 
ATOM   784  O  O   . VAL A 1 103 ? 14.887  10.033  7.929   1.000 11.012 ? 103 VAL AAA O   1 
ATOM   785  C  CB  . VAL A 1 103 ? 14.685  12.804  5.974   1.000 10.626 ? 103 VAL AAA CB  1 
ATOM   786  C  CG1 . VAL A 1 103 ? 14.438  13.280  7.375   1.000 11.552 ? 103 VAL AAA CG1 1 
ATOM   787  C  CG2 . VAL A 1 103 ? 15.632  13.731  5.275   1.000 11.133 ? 103 VAL AAA CG2 1 
ATOM   788  N  N   . ILE A 1 104 ? 13.306  9.907   6.349   1.000 8.870  ? 104 ILE AAA N   1 
ATOM   789  C  CA  . ILE A 1 104 ? 12.644  8.789   7.072   1.000 8.999  ? 104 ILE AAA CA  1 
ATOM   790  C  C   . ILE A 1 104 ? 13.600  7.597   7.037   1.000 8.795  ? 104 ILE AAA C   1 
ATOM   791  O  O   . ILE A 1 104 ? 14.421  7.438   6.089   1.000 10.178 ? 104 ILE AAA O   1 
ATOM   792  C  CB  . ILE A 1 104 ? 11.261  8.447   6.499   1.000 8.567  ? 104 ILE AAA CB  1 
ATOM   793  C  CG1 . ILE A 1 104 ? 11.352  8.022   5.032   1.000 8.830  ? 104 ILE AAA CG1 1 
ATOM   794  C  CG2 . ILE A 1 104 ? 10.272  9.568   6.723   1.000 9.147  ? 104 ILE AAA CG2 1 
ATOM   795  C  CD1 . ILE A 1 104 ? 10.087  7.365   4.502   1.000 9.105  ? 104 ILE AAA CD1 1 
ATOM   796  N  N   . SER A 1 105 ? 13.418  6.681   7.970   1.000 9.208  ? 105 SER AAA N   1 
ATOM   797  C  CA  . SER A 1 105 ? 14.156  5.420   7.999   1.000 9.064  ? 105 SER AAA CA  1 
ATOM   798  C  C   . SER A 1 105 ? 13.224  4.321   8.495   1.000 9.011  ? 105 SER AAA C   1 
ATOM   799  O  O   . SER A 1 105 ? 12.173  4.611   9.083   1.000 8.877  ? 105 SER AAA O   1 
ATOM   800  C  CB  . SER A 1 105 ? 15.411  5.551   8.839   1.000 9.419  ? 105 SER AAA CB  1 
ATOM   801  O  OG  . SER A 1 105 ? 16.212  4.398   8.700   1.000 10.657 ? 105 SER AAA OG  1 
ATOM   802  N  N   . LEU A 1 106 ? 13.638  3.084   8.266   1.000 9.552  ? 106 LEU AAA N   1 
ATOM   803  C  CA  . LEU A 1 106 ? 12.989  1.919   8.899   1.000 10.425 ? 106 LEU AAA CA  1 
ATOM   804  C  C   . LEU A 1 106 ? 13.859  1.386   10.038  1.000 11.757 ? 106 LEU AAA C   1 
ATOM   805  O  O   . LEU A 1 106 ? 13.503  0.327   10.544  1.000 13.367 ? 106 LEU AAA O   1 
ATOM   806  C  CB  . LEU A 1 106 ? 12.648  0.884   7.835   1.000 10.672 ? 106 LEU AAA CB  1 
ATOM   807  C  CG  . LEU A 1 106 ? 11.885  1.435   6.628   1.000 11.360 ? 106 LEU AAA CG  1 
ATOM   808  C  CD1 . LEU A 1 106 ? 11.519  0.310   5.646   1.000 12.034 ? 106 LEU AAA CD1 1 
ATOM   809  C  CD2 . LEU A 1 106 ? 10.633  2.201   7.019   1.000 11.177 ? 106 LEU AAA CD2 1 
ATOM   810  N  N   . SER A 1 107 ? 14.816  2.157   10.550  1.000 11.641 ? 107 SER AAA N   1 
ATOM   811  C  CA  . SER A 1 107 ? 15.602  1.827   11.774  1.000 14.262 ? 107 SER AAA CA  1 
ATOM   812  C  C   . SER A 1 107 ? 16.122  3.101   12.447  1.000 15.226 ? 107 SER AAA C   1 
ATOM   813  O  O   . SER A 1 107 ? 16.104  4.184   11.840  1.000 13.595 ? 107 SER AAA O   1 
ATOM   814  C  CB  . SER A 1 107 ? 16.675  0.870   11.427  1.000 19.133 ? 107 SER AAA CB  1 
ATOM   815  O  OG  . SER A 1 107 ? 17.699  1.506   10.707  1.000 25.066 ? 107 SER AAA OG  1 
ATOM   816  N  N   . GLY A 1 108 ? 16.480  3.033   13.738  1.000 16.178 ? 108 GLY AAA N   1 
ATOM   817  C  CA  . GLY A 1 108 ? 17.074  4.185   14.452  1.000 14.827 ? 108 GLY AAA CA  1 
ATOM   818  C  C   . GLY A 1 108 ? 16.064  5.238   14.849  1.000 15.398 ? 108 GLY AAA C   1 
ATOM   819  O  O   . GLY A 1 108 ? 14.834  4.974   14.807  1.000 14.591 ? 108 GLY AAA O   1 
ATOM   820  N  N   . ASP A 1 109 ? 16.513  6.413   15.269  1.000 15.572 ? 109 ASP AAA N   1 
ATOM   821  C  CA  . ASP A 1 109 ? 15.573  7.416   15.817  1.000 14.684 ? 109 ASP AAA CA  1 
ATOM   822  C  C   . ASP A 1 109 ? 14.806  8.134   14.717  1.000 13.669 ? 109 ASP AAA C   1 
ATOM   823  O  O   . ASP A 1 109 ? 13.882  8.898   15.073  1.000 14.905 ? 109 ASP AAA O   1 
ATOM   824  C  CB  . ASP A 1 109 ? 16.265  8.341   16.816  1.000 15.946 ? 109 ASP AAA CB  1 
ATOM   825  C  CG  . ASP A 1 109 ? 17.272  9.316   16.277  1.000 19.232 ? 109 ASP AAA CG  1 
ATOM   826  O  OD1 . ASP A 1 109 ? 17.466  9.380   15.058  1.000 19.355 ? 109 ASP AAA OD1 1 
ATOM   827  O  OD2 . ASP A 1 109 ? 17.928  9.946   17.128  1.000 17.480 ? 109 ASP AAA OD2 1 
ATOM   828  N  N   . HIS A 1 110 ? 15.113  7.907   13.445  1.000 10.724 ? 110 HIS AAA N   1 
ATOM   829  C  CA  . HIS A 1 110 ? 14.233  8.392   12.361  1.000 10.594 ? 110 HIS AAA CA  1 
ATOM   830  C  C   . HIS A 1 110 ? 13.248  7.309   11.933  1.000 9.153  ? 110 HIS AAA C   1 
ATOM   831  O  O   . HIS A 1 110 ? 12.551  7.545   10.935  1.000 9.709  ? 110 HIS AAA O   1 
ATOM   832  C  CB  . HIS A 1 110 ? 15.046  8.832   11.150  1.000 10.581 ? 110 HIS AAA CB  1 
ATOM   833  C  CG  . HIS A 1 110 ? 15.989  9.965   11.337  1.000 12.600 ? 110 HIS AAA CG  1 
ATOM   834  N  ND1 . HIS A 1 110 ? 16.795  10.165  12.467  1.000 14.499 ? 110 HIS AAA ND1 1 
ATOM   835  C  CD2 . HIS A 1 110 ? 16.317  10.919  10.451  1.000 13.431 ? 110 HIS AAA CD2 1 
ATOM   836  C  CE1 . HIS A 1 110 ? 17.536  11.245  12.263  1.000 15.795 ? 110 HIS AAA CE1 1 
ATOM   837  N  NE2 . HIS A 1 110 ? 17.249  11.731  11.075  1.000 15.688 ? 110 HIS AAA NE2 1 
ATOM   838  N  N   . CYS A 1 111 ? 13.185  6.215   12.663  1.000 9.021  ? 111 CYS AAA N   1 
ATOM   839  C  CA  . CYS A 1 111 ? 12.322  5.104   12.254  1.000 9.319  ? 111 CYS AAA CA  1 
ATOM   840  C  C   . CYS A 1 111 ? 10.866  5.519   12.323  1.000 9.063  ? 111 CYS AAA C   1 
ATOM   841  O  O   . CYS A 1 111 ? 10.416  6.105   13.312  1.000 9.126  ? 111 CYS AAA O   1 
ATOM   842  C  CB  . CYS A 1 111 ? 12.573  3.905   13.140  1.000 9.291  ? 111 CYS AAA CB  1 
ATOM   843  S  SG  . CYS A 1 111 ? 11.657  2.474   12.554  1.000 11.248 ? 111 CYS AAA SG  1 
ATOM   844  N  N   . ILE A 1 112 ? 10.095  5.122   11.324  1.000 8.124  ? 112 ILE AAA N   1 
ATOM   845  C  CA  . ILE A 1 112 ? 8.654   5.445   11.248  1.000 8.862  ? 112 ILE AAA CA  1 
ATOM   846  C  C   . ILE A 1 112 ? 7.762   4.278   11.668  1.000 7.889  ? 112 ILE AAA C   1 
ATOM   847  O  O   . ILE A 1 112 ? 6.541   4.438   11.671  1.000 7.963  ? 112 ILE AAA O   1 
ATOM   848  C  CB  . ILE A 1 112 ? 8.314   5.918   9.838   1.000 9.679  ? 112 ILE AAA CB  1 
ATOM   849  C  CG1 . ILE A 1 112 ? 8.586   4.883   8.748   1.000 10.281 ? 112 ILE AAA CG1 1 
ATOM   850  C  CG2 . ILE A 1 112 ? 9.071   7.217   9.609   1.000 9.778  ? 112 ILE AAA CG2 1 
ATOM   851  C  CD1 . ILE A 1 112 ? 8.019   5.324   7.399   1.000 10.805 ? 112 ILE AAA CD1 1 
ATOM   852  N  N   . ILE A 1 113 ? 8.311   3.111   11.949  1.000 7.800  ? 113 ILE AAA N   1 
ATOM   853  C  CA  . ILE A 1 113 ? 7.495   1.951   12.369  1.000 7.703  ? 113 ILE AAA CA  1 
ATOM   854  C  C   . ILE A 1 113 ? 6.785   2.270   13.686  1.000 7.809  ? 113 ILE AAA C   1 
ATOM   855  O  O   . ILE A 1 113 ? 7.398   2.784   14.635  1.000 8.255  ? 113 ILE AAA O   1 
ATOM   856  C  CB  . ILE A 1 113 ? 8.344   0.678   12.470  1.000 7.961  ? 113 ILE AAA CB  1 
ATOM   857  C  CG1 . ILE A 1 113 ? 8.971   0.315   11.121  1.000 9.171  ? 113 ILE AAA CG1 1 
ATOM   858  C  CG2 . ILE A 1 113 ? 7.533   -0.479  13.026  1.000 8.685  ? 113 ILE AAA CG2 1 
ATOM   859  C  CD1 . ILE A 1 113 ? 9.987   -0.762  11.210  1.000 9.287  ? 113 ILE AAA CD1 1 
ATOM   860  N  N   . GLY A 1 114 ? 5.498   1.980   13.755  1.000 7.376  ? 114 GLY AAA N   1 
ATOM   861  C  CA  . GLY A 1 114 ? 4.698   2.272   14.947  1.000 7.517  ? 114 GLY AAA CA  1 
ATOM   862  C  C   . GLY A 1 114 ? 4.169   3.680   14.992  1.000 7.400  ? 114 GLY AAA C   1 
ATOM   863  O  O   . GLY A 1 114 ? 3.532   4.039   15.999  1.000 8.892  ? 114 GLY AAA O   1 
ATOM   864  N  N   . ARG A 1 115 ? 4.455   4.495   13.993  1.000 7.375  ? 115 ARG AAA N   1 
ATOM   865  C  CA  . ARG A 1 115 ? 3.867   5.843   13.846  1.000 6.931  ? 115 ARG AAA CA  1 
ATOM   866  C  C   . ARG A 1 115 ? 2.667   5.761   12.911  1.000 6.821  ? 115 ARG AAA C   1 
ATOM   867  O  O   . ARG A 1 115 ? 2.257   4.662   12.531  1.000 8.065  ? 115 ARG AAA O   1 
ATOM   868  C  CB  . ARG A 1 115 ? 4.966   6.813   13.370  1.000 8.261  ? 115 ARG AAA CB  1 
ATOM   869  C  CG  . ARG A 1 115 ? 6.272   6.733   14.133  1.000 10.696 ? 115 ARG AAA CG  1 
ATOM   870  C  CD  . ARG A 1 115 ? 6.218   7.373   15.475  1.000 12.351 ? 115 ARG AAA CD  1 
ATOM   871  N  NE  . ARG A 1 115 ? 7.489   7.185   16.139  1.000 12.158 ? 115 ARG AAA NE  1 
ATOM   872  C  CZ  . ARG A 1 115 ? 7.808   7.819   17.223  1.000 12.339 ? 115 ARG AAA CZ  1 
ATOM   873  N  NH1 . ARG A 1 115 ? 6.972   8.645   17.777  1.000 13.261 ? 115 ARG AAA NH1 1 
ATOM   874  N  NH2 . ARG A 1 115 ? 8.953   7.525   17.820  1.000 13.385 ? 115 ARG AAA NH2 1 
ATOM   875  N  N   . THR A 1 116 ? 2.057   6.900   12.594  1.000 6.673  ? 116 THR AAA N   1 
ATOM   876  C  CA  . THR A 1 116 ? 0.843   6.918   11.745  1.000 7.046  ? 116 THR AAA CA  1 
ATOM   877  C  C   . THR A 1 116 ? 1.166   7.612   10.430  1.000 7.100  ? 116 THR AAA C   1 
ATOM   878  O  O   . THR A 1 116 ? 1.775   8.697   10.470  1.000 9.104  ? 116 THR AAA O   1 
ATOM   879  C  CB  . THR A 1 116 ? -0.311  7.619   12.454  1.000 7.379  ? 116 THR AAA CB  1 
ATOM   880  O  OG1 . THR A 1 116 ? -0.715  6.847   13.593  1.000 8.495  ? 116 THR AAA OG1 1 
ATOM   881  C  CG2 . THR A 1 116 ? -1.527  7.807   11.569  1.000 7.615  ? 116 THR AAA CG2 1 
ATOM   882  N  N   . LEU A 1 117 ? 0.714   7.084   9.322   1.000 6.759  ? 117 LEU AAA N   1 
ATOM   883  C  CA  . LEU A 1 117 ? 0.734   7.796   8.047   1.000 7.225  ? 117 LEU AAA CA  1 
ATOM   884  C  C   . LEU A 1 117 ? -0.636  8.417   7.801   1.000 6.968  ? 117 LEU AAA C   1 
ATOM   885  O  O   . LEU A 1 117 ? -1.654  7.746   8.018   1.000 7.501  ? 117 LEU AAA O   1 
ATOM   886  C  CB  . LEU A 1 117 ? 1.020   6.809   6.926   1.000 7.441  ? 117 LEU AAA CB  1 
ATOM   887  C  CG  . LEU A 1 117 ? 1.271   7.388   5.528   1.000 8.102  ? 117 LEU AAA CG  1 
ATOM   888  C  CD1 . LEU A 1 117 ? 2.528   8.277   5.448   1.000 9.225  ? 117 LEU AAA CD1 1 
ATOM   889  C  CD2 . LEU A 1 117 ? 1.373   6.216   4.552   1.000 8.937  ? 117 LEU AAA CD2 1 
ATOM   890  N  N   . VAL A 1 118 ? -0.677  9.679   7.415   1.000 6.849  ? 118 VAL AAA N   1 
ATOM   891  C  CA  . VAL A 1 118 ? -1.925  10.438  7.224   1.000 7.244  ? 118 VAL AAA CA  1 
ATOM   892  C  C   . VAL A 1 118 ? -1.919  11.092  5.852   1.000 7.590  ? 118 VAL AAA C   1 
ATOM   893  O  O   . VAL A 1 118 ? -0.913  11.686  5.441   1.000 8.123  ? 118 VAL AAA O   1 
ATOM   894  C  CB  . VAL A 1 118 ? -2.107  11.529  8.289   1.000 7.736  ? 118 VAL AAA CB  1 
ATOM   895  C  CG1 . VAL A 1 118 ? -3.424  12.226  8.079   1.000 9.013  ? 118 VAL AAA CG1 1 
ATOM   896  C  CG2 . VAL A 1 118 ? -1.985  10.938  9.683   1.000 7.622  ? 118 VAL AAA CG2 1 
ATOM   897  N  N   . VAL A 1 119 ? -3.038  10.956  5.139   1.000 8.167  ? 119 VAL AAA N   1 
ATOM   898  C  CA  . VAL A 1 119 ? -3.311  11.743  3.914   1.000 8.436  ? 119 VAL AAA CA  1 
ATOM   899  C  C   . VAL A 1 119 ? -4.359  12.785  4.265   1.000 8.826  ? 119 VAL AAA C   1 
ATOM   900  O  O   . VAL A 1 119 ? -5.377  12.500  4.888   1.000 8.676  ? 119 VAL AAA O   1 
ATOM   901  C  CB  . VAL A 1 119 ? -3.668  10.853  2.712   1.000 8.443  ? 119 VAL AAA CB  1 
ATOM   902  C  CG1 . VAL A 1 119 ? -4.942  10.042  2.890   1.000 9.459  ? 119 VAL AAA CG1 1 
ATOM   903  C  CG2 . VAL A 1 119 ? -3.711  11.725  1.448   1.000 8.629  ? 119 VAL AAA CG2 1 
ATOM   904  N  N   . HIS A 1 120 ? -4.069  14.031  3.869   1.000 8.527  ? 120 HIS AAA N   1 
ATOM   905  C  CA  . HIS A 1 120 ? -4.810  15.224  4.275   1.000 8.802  ? 120 HIS AAA CA  1 
ATOM   906  C  C   . HIS A 1 120 ? -5.751  15.700  3.175   1.000 9.497  ? 120 HIS AAA C   1 
ATOM   907  O  O   . HIS A 1 120 ? -5.640  15.392  2.018   1.000 10.178 ? 120 HIS AAA O   1 
ATOM   908  C  CB  . HIS A 1 120 ? -3.854  16.325  4.731   1.000 8.976  ? 120 HIS AAA CB  1 
ATOM   909  C  CG  . HIS A 1 120 ? -3.186  16.071  6.032   1.000 9.278  ? 120 HIS AAA CG  1 
ATOM   910  N  ND1 . HIS A 1 120 ? -3.659  16.620  7.232   1.000 10.066 ? 120 HIS AAA ND1 1 
ATOM   911  C  CD2 . HIS A 1 120 ? -2.110  15.355  6.365   1.000 9.727  ? 120 HIS AAA CD2 1 
ATOM   912  C  CE1 . HIS A 1 120 ? -2.864  16.246  8.203   1.000 10.472 ? 120 HIS AAA CE1 1 
ATOM   913  N  NE2 . HIS A 1 120 ? -1.912  15.464  7.739   1.000 10.146 ? 120 HIS AAA NE2 1 
ATOM   914  N  N   . GLU A 1 121 ? -6.670  16.521  3.620   1.000 11.669 ? 121 GLU AAA N   1 
ATOM   915  C  CA  . GLU A 1 121 ? -7.724  17.138  2.794   1.000 11.537 ? 121 GLU AAA CA  1 
ATOM   916  C  C   . GLU A 1 121 ? -7.180  18.039  1.684   1.000 11.318 ? 121 GLU AAA C   1 
ATOM   917  O  O   . GLU A 1 121 ? -7.765  18.023  0.614   1.000 12.934 ? 121 GLU AAA O   1 
ATOM   918  C  CB  . GLU A 1 121 ? -8.569  17.924  3.798   1.000 13.845 ? 121 GLU AAA CB  1 
ATOM   919  C  CG  . GLU A 1 121 ? -9.592  18.879  3.231   1.000 18.103 ? 121 GLU AAA CG  1 
ATOM   920  C  CD  . GLU A 1 121 ? -10.093 19.978  4.163   1.000 19.298 ? 121 GLU AAA CD  1 
ATOM   921  O  OE1 . GLU A 1 121 ? -11.017 20.674  3.696   1.000 26.571 ? 121 GLU AAA OE1 1 
ATOM   922  O  OE2 . GLU A 1 121 ? -9.565  20.200  5.299   1.000 20.144 ? 121 GLU AAA OE2 1 
ATOM   923  N  N   . LYS A 1 122 ? -6.156  18.828  2.007   1.000 12.110 ? 122 LYS AAA N   1 
ATOM   924  C  CA  . LYS A 1 122 ? -5.714  19.981  1.184   1.000 13.567 ? 122 LYS AAA CA  1 
ATOM   925  C  C   . LYS A 1 122 ? -4.231  19.773  0.858   1.000 10.913 ? 122 LYS AAA C   1 
ATOM   926  O  O   . LYS A 1 122 ? -3.556  18.906  1.473   1.000 10.423 ? 122 LYS AAA O   1 
ATOM   927  C  CB  . LYS A 1 122 ? -5.924  21.334  1.924   1.000 15.778 ? 122 LYS AAA CB  1 
ATOM   928  C  CG  . LYS A 1 122 ? -7.332  21.653  2.412   1.000 21.112 ? 122 LYS AAA CG  1 
ATOM   929  C  CD  . LYS A 1 122 ? -7.522  23.082  2.859   1.000 24.828 ? 122 LYS AAA CD  1 
ATOM   930  C  CE  . LYS A 1 122 ? -6.452  23.517  3.829   1.000 28.899 ? 122 LYS AAA CE  1 
ATOM   931  N  NZ  . LYS A 1 122 ? -6.817  24.681  4.673   1.000 35.236 ? 122 LYS AAA NZ  1 
ATOM   932  N  N   . ALA A 1 123 ? -3.680  20.659  0.051   1.000 11.473 ? 123 ALA AAA N   1 
ATOM   933  C  CA  . ALA A 1 123 ? -2.255  20.657  -0.266  1.000 10.968 ? 123 ALA AAA CA  1 
ATOM   934  C  C   . ALA A 1 123 ? -1.452  21.096  0.953   1.000 11.600 ? 123 ALA AAA C   1 
ATOM   935  O  O   . ALA A 1 123 ? -1.830  22.001  1.706   1.000 12.072 ? 123 ALA AAA O   1 
ATOM   936  C  CB  . ALA A 1 123 ? -1.964  21.604  -1.407  1.000 12.918 ? 123 ALA AAA CB  1 
ATOM   937  N  N   . ASP A 1 124 ? -0.313  20.467  1.130   1.000 10.360 ? 124 ASP AAA N   1 
ATOM   938  C  CA  . ASP A 1 124 ? 0.739   20.961  2.031   1.000 10.131 ? 124 ASP AAA CA  1 
ATOM   939  C  C   . ASP A 1 124 ? 1.488   22.082  1.306   1.000 10.173 ? 124 ASP AAA C   1 
ATOM   940  O  O   . ASP A 1 124 ? 1.953   21.855  0.202   1.000 10.719 ? 124 ASP AAA O   1 
ATOM   941  C  CB  . ASP A 1 124 ? 1.661   19.794  2.424   1.000 10.551 ? 124 ASP AAA CB  1 
ATOM   942  C  CG  . ASP A 1 124 ? 2.768   20.096  3.408   1.000 11.101 ? 124 ASP AAA CG  1 
ATOM   943  O  OD1 . ASP A 1 124 ? 3.065   21.269  3.672   1.000 10.542 ? 124 ASP AAA OD1 1 
ATOM   944  O  OD2 . ASP A 1 124 ? 3.291   19.097  3.991   1.000 12.870 ? 124 ASP AAA OD2 1 
ATOM   945  N  N   . ASP A 1 125 ? 1.590   23.242  1.925   1.000 10.766 ? 125 ASP AAA N   1 
ATOM   946  C  CA  . ASP A 1 125 ? 2.292   24.411  1.327   1.000 11.084 ? 125 ASP AAA CA  1 
ATOM   947  C  C   . ASP A 1 125 ? 3.800   24.339  1.573   1.000 11.559 ? 125 ASP AAA C   1 
ATOM   948  O  O   . ASP A 1 125 ? 4.539   25.302  1.228   1.000 11.692 ? 125 ASP AAA O   1 
ATOM   949  C  CB  . ASP A 1 125 ? 1.707   25.728  1.819   1.000 12.626 ? 125 ASP AAA CB  1 
ATOM   950  C  CG  . ASP A 1 125 ? 1.875   26.023  3.305   1.000 12.248 ? 125 ASP AAA CG  1 
ATOM   951  O  OD1 . ASP A 1 125 ? 2.812   25.457  3.949   1.000 12.298 ? 125 ASP AAA OD1 1 
ATOM   952  O  OD2 . ASP A 1 125 ? 1.085   26.837  3.820   1.000 14.263 ? 125 ASP AAA OD2 1 
ATOM   953  N  N   . LEU A 1 126 ? 4.270   23.235  2.148   1.000 10.432 ? 126 LEU AAA N   1 
ATOM   954  C  CA  . LEU A 1 126 ? 5.695   22.919  2.348   1.000 10.935 ? 126 LEU AAA CA  1 
ATOM   955  C  C   . LEU A 1 126 ? 6.392   24.018  3.135   1.000 10.080 ? 126 LEU AAA C   1 
ATOM   956  O  O   . LEU A 1 126 ? 7.616   24.187  2.971   1.000 11.699 ? 126 LEU AAA O   1 
ATOM   957  C  CB  . LEU A 1 126 ? 6.395   22.683  1.017   1.000 10.764 ? 126 LEU AAA CB  1 
ATOM   958  C  CG  . LEU A 1 126 ? 5.731   21.703  0.059   1.000 10.923 ? 126 LEU AAA CG  1 
ATOM   959  C  CD1 . LEU A 1 126 ? 6.626   21.382  -1.098  1.000 12.074 ? 126 LEU AAA CD1 1 
ATOM   960  C  CD2 . LEU A 1 126 ? 5.335   20.367  0.686   1.000 11.037 ? 126 LEU AAA CD2 1 
ATOM   961  N  N   . GLY A 1 127 ? 5.694   24.655  4.045   1.000 11.034 ? 127 GLY AAA N   1 
ATOM   962  C  CA  . GLY A 1 127 ? 6.282   25.684  4.903   1.000 11.450 ? 127 GLY AAA CA  1 
ATOM   963  C  C   . GLY A 1 127 ? 6.402   27.038  4.217   1.000 12.826 ? 127 GLY AAA C   1 
ATOM   964  O  O   . GLY A 1 127 ? 7.053   27.938  4.830   1.000 15.105 ? 127 GLY AAA O   1 
ATOM   965  N  N   . LYS A 1 128 ? 5.806   27.243  3.036   1.000 12.386 ? 128 LYS AAA N   1 
ATOM   966  C  CA  . LYS A 1 128 ? 6.009   28.490  2.242   1.000 14.179 ? 128 LYS AAA CA  1 
ATOM   967  C  C   . LYS A 1 128 ? 4.712   29.271  2.190   1.000 14.443 ? 128 LYS AAA C   1 
ATOM   968  O  O   . LYS A 1 128 ? 4.627   30.241  1.406   1.000 15.624 ? 128 LYS AAA O   1 
ATOM   969  C  CB  . LYS A 1 128 ? 6.452   28.139  0.822   1.000 14.736 ? 128 LYS AAA CB  1 
ATOM   970  C  CG  . LYS A 1 128 ? 7.758   27.394  0.750   1.000 17.944 ? 128 LYS AAA CG  1 
ATOM   971  C  CD  . LYS A 1 128 ? 8.940   28.152  1.320   1.000 22.488 ? 128 LYS AAA CD  1 
ATOM   972  C  CE  . LYS A 1 128 ? 10.266  27.776  0.692   1.000 24.222 ? 128 LYS AAA CE  1 
ATOM   973  N  NZ  . LYS A 1 128 ? 10.760  26.497  1.252   1.000 28.385 ? 128 LYS AAA NZ  1 
ATOM   974  N  N   . GLY A 1 129 ? 3.771   29.005  3.085   1.000 14.124 ? 129 GLY AAA N   1 
ATOM   975  C  CA  . GLY A 1 129 ? 2.475   29.671  3.044   1.000 15.392 ? 129 GLY AAA CA  1 
ATOM   976  C  C   . GLY A 1 129 ? 2.488   31.021  3.739   1.000 16.705 ? 129 GLY AAA C   1 
ATOM   977  O  O   . GLY A 1 129 ? 1.465   31.689  3.658   1.000 17.503 ? 129 GLY AAA O   1 
ATOM   978  N  N   . GLY A 1 130 ? 3.554   31.353  4.463   0.700 16.026 ? 130 GLY AAA N   1 
ATOM   979  C  CA  . GLY A 1 130 ? 3.752   32.685  5.069   0.700 21.824 ? 130 GLY AAA CA  1 
ATOM   980  C  C   . GLY A 1 130 ? 2.719   33.001  6.145   0.700 24.460 ? 130 GLY AAA C   1 
ATOM   981  O  O   . GLY A 1 130 ? 2.352   34.178  6.299   0.700 27.867 ? 130 GLY AAA O   1 
ATOM   982  N  N   . ASN A 1 131 ? 2.211   31.991  6.854   1.000 25.440 ? 131 ASN AAA N   1 
ATOM   983  C  CA  . ASN A 1 131 ? 1.457   32.195  8.115   1.000 24.893 ? 131 ASN AAA CA  1 
ATOM   984  C  C   . ASN A 1 131 ? 2.044   31.277  9.169   1.000 24.729 ? 131 ASN AAA C   1 
ATOM   985  O  O   . ASN A 1 131 ? 2.923   30.468  8.835   1.000 27.445 ? 131 ASN AAA O   1 
ATOM   986  C  CB  . ASN A 1 131 ? -0.052  32.045  7.934   1.000 23.411 ? 131 ASN AAA CB  1 
ATOM   987  C  CG  . ASN A 1 131 ? -0.543  30.630  7.673   1.000 27.128 ? 131 ASN AAA CG  1 
ATOM   988  O  OD1 . ASN A 1 131 ? 0.243   29.704  7.552   1.000 22.326 ? 131 ASN AAA OD1 1 
ATOM   989  N  ND2 . ASN A 1 131 ? -1.848  30.440  7.601   1.000 29.038 ? 131 ASN AAA ND2 1 
ATOM   990  N  N   . GLU A 1 132 ? 1.600   31.419  10.421  1.000 23.127 ? 132 GLU AAA N   1 
ATOM   991  C  CA  . GLU A 1 132 ? 2.214   30.676  11.536  1.000 23.198 ? 132 GLU AAA CA  1 
ATOM   992  C  C   . GLU A 1 132 ? 1.958   29.187  11.326  1.000 18.253 ? 132 GLU AAA C   1 
ATOM   993  O  O   . GLU A 1 132 ? 2.905   28.377  11.566  1.000 22.036 ? 132 GLU AAA O   1 
ATOM   994  C  CB  . GLU A 1 132 ? 1.714   31.109  12.910  1.000 27.439 ? 132 GLU AAA CB  1 
ATOM   995  C  CG  . GLU A 1 132 ? 2.695   30.729  14.007  1.000 35.246 ? 132 GLU AAA CG  1 
ATOM   996  C  CD  . GLU A 1 132 ? 2.164   30.856  15.434  1.000 40.661 ? 132 GLU AAA CD  1 
ATOM   997  O  OE1 . GLU A 1 132 ? 1.238   31.682  15.648  1.000 48.270 ? 132 GLU AAA OE1 1 
ATOM   998  O  OE2 . GLU A 1 132 ? 2.670   30.136  16.332  1.000 39.106 ? 132 GLU AAA OE2 1 
ATOM   999  N  N   . GLU A 1 133 ? 0.767   28.824  10.843  1.000 15.014 ? 133 GLU AAA N   1 
ATOM   1000 C  CA  . GLU A 1 133 ? 0.427   27.381  10.712  1.000 13.754 ? 133 GLU AAA CA  1 
ATOM   1001 C  C   . GLU A 1 133 ? 1.323   26.763  9.635   1.000 13.520 ? 133 GLU AAA C   1 
ATOM   1002 O  O   . GLU A 1 133 ? 1.623   25.592  9.708   1.000 12.246 ? 133 GLU AAA O   1 
ATOM   1003 C  CB  . GLU A 1 133 ? -1.054  27.190  10.392  1.000 15.424 ? 133 GLU AAA CB  1 
ATOM   1004 N  N   . SER A 1 134 ? 1.787   27.522  8.631   1.000 13.005 ? 134 SER AAA N   1 
ATOM   1005 C  CA  . SER A 1 134 ? 2.547   26.929  7.510   1.000 11.735 ? 134 SER AAA CA  1 
ATOM   1006 C  C   . SER A 1 134 ? 3.765   26.181  8.039   1.000 11.808 ? 134 SER AAA C   1 
ATOM   1007 O  O   . SER A 1 134 ? 4.052   25.088  7.517   1.000 12.013 ? 134 SER AAA O   1 
ATOM   1008 C  CB  . SER A 1 134 ? 3.015   28.005  6.523   1.000 13.786 ? 134 SER AAA CB  1 
ATOM   1009 O  OG  . SER A 1 134 ? 3.722   27.406  5.458   1.000 13.310 ? 134 SER AAA OG  1 
ATOM   1010 N  N   . THR A 1 135 ? 4.502   26.763  8.996   1.000 11.818 ? 135 THR AAA N   1 
ATOM   1011 C  CA  . THR A 1 135 ? 5.768   26.133  9.480   1.000 13.319 ? 135 THR AAA CA  1 
ATOM   1012 C  C   . THR A 1 135 ? 5.492   25.168  10.636  1.000 12.156 ? 135 THR AAA C   1 
ATOM   1013 O  O   . THR A 1 135 ? 6.490   24.693  11.218  1.000 13.034 ? 135 THR AAA O   1 
ATOM   1014 C  CB  . THR A 1 135 ? 6.881   27.154  9.745   1.000 16.165 ? 135 THR AAA CB  1 
ATOM   1015 O  OG1 . THR A 1 135 ? 6.300   28.215  10.488  1.000 18.201 ? 135 THR AAA OG1 1 
ATOM   1016 C  CG2 . THR A 1 135 ? 7.422   27.720  8.449   1.000 18.821 ? 135 THR AAA CG2 1 
ATOM   1017 N  N   . LYS A 1 136 ? 4.226   24.810  10.850  1.000 11.983 ? 136 LYS AAA N   1 
ATOM   1018 C  CA  . LYS A 1 136 ? 3.833   23.726  11.799  1.000 12.792 ? 136 LYS AAA CA  1 
ATOM   1019 C  C   . LYS A 1 136 ? 3.187   22.566  11.037  1.000 12.235 ? 136 LYS AAA C   1 
ATOM   1020 O  O   . LYS A 1 136 ? 3.649   21.418  11.162  1.000 12.852 ? 136 LYS AAA O   1 
ATOM   1021 C  CB  . LYS A 1 136 ? 2.903   24.301  12.877  1.000 13.394 ? 136 LYS AAA CB  1 
ATOM   1022 C  CG  . LYS A 1 136 ? 3.609   25.315  13.778  1.000 15.605 ? 136 LYS AAA CG  1 
ATOM   1023 C  CD  . LYS A 1 136 ? 2.746   26.091  14.762  1.000 19.511 ? 136 LYS AAA CD  1 
ATOM   1024 C  CE  . LYS A 1 136 ? 1.891   25.223  15.667  1.000 24.765 ? 136 LYS AAA CE  1 
ATOM   1025 N  NZ  . LYS A 1 136 ? 1.521   25.869  16.960  1.000 28.513 ? 136 LYS AAA NZ  1 
ATOM   1026 N  N   . THR A 1 137 ? 2.169   22.819  10.228  1.000 13.081 ? 137 THR AAA N   1 
ATOM   1027 C  CA  . THR A 1 137 ? 1.360   21.755  9.584   1.000 12.731 ? 137 THR AAA CA  1 
ATOM   1028 C  C   . THR A 1 137 ? 1.397   21.839  8.062   1.000 12.075 ? 137 THR AAA C   1 
ATOM   1029 O  O   . THR A 1 137 ? 0.859   20.941  7.413   1.000 13.465 ? 137 THR AAA O   1 
ATOM   1030 C  CB  . THR A 1 137 ? -0.100  21.823  10.036  1.000 12.914 ? 137 THR AAA CB  1 
ATOM   1031 O  OG1 . THR A 1 137 ? -0.627  23.024  9.450   1.000 13.614 ? 137 THR AAA OG1 1 
ATOM   1032 C  CG2 . THR A 1 137 ? -0.277  21.787  11.536  1.000 15.471 ? 137 THR AAA CG2 1 
ATOM   1033 N  N   . GLY A 1 138 ? 1.888   22.943  7.479   1.000 11.465 ? 138 GLY AAA N   1 
ATOM   1034 C  CA  . GLY A 1 138 ? 1.768   23.184  6.025   1.000 11.223 ? 138 GLY AAA CA  1 
ATOM   1035 C  C   . GLY A 1 138 ? 0.346   23.509  5.575   1.000 10.332 ? 138 GLY AAA C   1 
ATOM   1036 O  O   . GLY A 1 138 ? 0.081   23.504  4.366   1.000 11.619 ? 138 GLY AAA O   1 
ATOM   1037 N  N   . ASN A 1 139 ? -0.575  23.750  6.496   1.000 11.584 ? 139 ASN AAA N   1 
ATOM   1038 C  CA  . ASN A 1 139 ? -1.975  24.147  6.144   1.000 12.270 ? 139 ASN AAA CA  1 
ATOM   1039 C  C   . ASN A 1 139 ? -2.663  23.069  5.310   1.000 11.768 ? 139 ASN AAA C   1 
ATOM   1040 O  O   . ASN A 1 139 ? -3.483  23.387  4.465   1.000 12.068 ? 139 ASN AAA O   1 
ATOM   1041 C  CB  . ASN A 1 139 ? -2.036  25.498  5.410   1.000 13.677 ? 139 ASN AAA CB  1 
ATOM   1042 C  CG  . ASN A 1 139 ? -1.706  26.654  6.315   1.000 15.086 ? 139 ASN AAA CG  1 
ATOM   1043 O  OD1 . ASN A 1 139 ? -2.441  26.924  7.255   1.000 16.956 ? 139 ASN AAA OD1 1 
ATOM   1044 N  ND2 . ASN A 1 139 ? -0.559  27.281  6.079   1.000 15.560 ? 139 ASN AAA ND2 1 
ATOM   1045 N  N   . ALA A 1 140 ? -2.391  21.789  5.561   1.000 11.843 ? 140 ALA AAA N   1 
ATOM   1046 C  CA  . ALA A 1 140 ? -2.943  20.691  4.741   1.000 11.829 ? 140 ALA AAA CA  1 
ATOM   1047 C  C   . ALA A 1 140 ? -4.348  20.290  5.189   1.000 11.460 ? 140 ALA AAA C   1 
ATOM   1048 O  O   . ALA A 1 140 ? -4.921  19.407  4.595   1.000 11.497 ? 140 ALA AAA O   1 
ATOM   1049 C  CB  . ALA A 1 140 ? -1.973  19.541  4.747   1.000 11.858 ? 140 ALA AAA CB  1 
ATOM   1050 N  N   . GLY A 1 141 ? -4.857  20.906  6.237   1.000 12.632 ? 141 GLY AAA N   1 
ATOM   1051 C  CA  . GLY A 1 141 ? -6.241  20.649  6.619   1.000 13.332 ? 141 GLY AAA CA  1 
ATOM   1052 C  C   . GLY A 1 141 ? -6.468  19.274  7.223   1.000 12.675 ? 141 GLY AAA C   1 
ATOM   1053 O  O   . GLY A 1 141 ? -5.578  18.715  7.891   1.000 14.231 ? 141 GLY AAA O   1 
ATOM   1054 N  N   . SER A 1 142 ? -7.702  18.840  7.128   1.000 13.683 ? 142 SER AAA N   1 
ATOM   1055 C  CA  . SER A 1 142 ? -8.148  17.705  7.957   1.000 13.256 ? 142 SER AAA CA  1 
ATOM   1056 C  C   . SER A 1 142 ? -7.478  16.402  7.520   1.000 12.843 ? 142 SER AAA C   1 
ATOM   1057 O  O   . SER A 1 142 ? -6.823  16.336  6.465   1.000 13.430 ? 142 SER AAA O   1 
ATOM   1058 C  CB  . SER A 1 142 ? -9.642  17.603  7.958   1.000 15.664 ? 142 SER AAA CB  1 
ATOM   1059 O  OG  . SER A 1 142 ? -10.107 17.156  6.723   1.000 18.048 ? 142 SER AAA OG  1 
ATOM   1060 N  N   . ARG A 1 143 ? -7.682  15.384  8.320   1.000 10.854 ? 143 ARG AAA N   1 
ATOM   1061 C  CA  . ARG A 1 143 ? -7.101  14.050  8.132   1.000 10.184 ? 143 ARG AAA CA  1 
ATOM   1062 C  C   . ARG A 1 143 ? -8.124  13.157  7.448   1.000 10.175 ? 143 ARG AAA C   1 
ATOM   1063 O  O   . ARG A 1 143 ? -9.084  12.781  8.091   1.000 13.516 ? 143 ARG AAA O   1 
ATOM   1064 C  CB  . ARG A 1 143 ? -6.632  13.524  9.483   1.000 9.495  ? 143 ARG AAA CB  1 
ATOM   1065 C  CG  . ARG A 1 143 ? -5.670  14.488  10.145  1.000 10.279 ? 143 ARG AAA CG  1 
ATOM   1066 C  CD  . ARG A 1 143 ? -5.223  14.027  11.500  1.000 10.745 ? 143 ARG AAA CD  1 
ATOM   1067 N  NE  . ARG A 1 143 ? -4.412  15.078  12.071  1.000 11.165 ? 143 ARG AAA NE  1 
ATOM   1068 C  CZ  . ARG A 1 143 ? -3.591  14.979  13.103  1.000 10.769 ? 143 ARG AAA CZ  1 
ATOM   1069 N  NH1 . ARG A 1 143 ? -3.385  13.823  13.733  1.000 12.320 ? 143 ARG AAA NH1 1 
ATOM   1070 N  NH2 . ARG A 1 143 ? -2.894  16.039  13.446  1.000 10.624 ? 143 ARG AAA NH2 1 
ATOM   1071 N  N   . LEU A 1 144 ? -7.933  12.806  6.198   1.000 9.454  ? 144 LEU AAA N   1 
ATOM   1072 C  CA  . LEU A 1 144 ? -8.950  12.068  5.432   1.000 9.380  ? 144 LEU AAA CA  1 
ATOM   1073 C  C   . LEU A 1 144 ? -8.805  10.586  5.709   1.000 9.012  ? 144 LEU AAA C   1 
ATOM   1074 O  O   . LEU A 1 144 ? -9.809  9.880   5.726   1.000 9.903  ? 144 LEU AAA O   1 
ATOM   1075 C  CB  . LEU A 1 144 ? -8.733  12.295  3.935   1.000 10.747 ? 144 LEU AAA CB  1 
ATOM   1076 C  CG  . LEU A 1 144 ? -8.901  13.712  3.419   1.000 13.296 ? 144 LEU AAA CG  1 
ATOM   1077 C  CD1 . LEU A 1 144 ? -8.693  13.656  1.908   1.000 14.187 ? 144 LEU AAA CD1 1 
ATOM   1078 C  CD2 . LEU A 1 144 ? -10.259 14.284  3.780   1.000 15.959 ? 144 LEU AAA CD2 1 
ATOM   1079 N  N   . ALA A 1 145 ? -7.601  10.078  5.896   1.000 8.338  ? 145 ALA AAA N   1 
ATOM   1080 C  CA  . ALA A 1 145 ? -7.369  8.636   6.083   1.000 8.613  ? 145 ALA AAA CA  1 
ATOM   1081 C  C   . ALA A 1 145 ? -6.020  8.462   6.749   1.000 8.142  ? 145 ALA AAA C   1 
ATOM   1082 O  O   . ALA A 1 145 ? -5.141  9.316   6.570   1.000 7.924  ? 145 ALA AAA O   1 
ATOM   1083 C  CB  . ALA A 1 145 ? -7.491  7.837   4.786   1.000 8.735  ? 145 ALA AAA CB  1 
ATOM   1084 N  N   . CYS A 1 146 ? -5.877  7.399   7.503   1.000 7.618  ? 146 CYS AAA N   1 
ATOM   1085 C  CA  . CYS A 1 146 ? -4.620  7.166   8.219   1.000 8.126  ? 146 CYS AAA CA  1 
ATOM   1086 C  C   . CYS A 1 146 ? -4.514  5.701   8.538   1.000 7.358  ? 146 CYS AAA C   1 
ATOM   1087 O  O   . CYS A 1 146 ? -5.488  4.942   8.407   1.000 7.356  ? 146 CYS AAA O   1 
ATOM   1088 C  CB  . CYS A 1 146 ? -4.547  7.986   9.503   1.000 9.684  ? 146 CYS AAA CB  1 
ATOM   1089 S  SG  . CYS A 1 146 ? -5.855  7.623   10.699  1.000 13.003 ? 146 CYS AAA SG  1 
ATOM   1090 N  N   . GLY A 1 147 ? -3.333  5.320   8.939   1.000 7.382  ? 147 GLY AAA N   1 
ATOM   1091 C  CA  . GLY A 1 147 ? -3.098  3.954   9.437   1.000 7.174  ? 147 GLY AAA CA  1 
ATOM   1092 C  C   . GLY A 1 147 ? -1.787  3.910   10.183  1.000 7.016  ? 147 GLY AAA C   1 
ATOM   1093 O  O   . GLY A 1 147 ? -0.962  4.815   10.060  1.000 7.560  ? 147 GLY AAA O   1 
ATOM   1094 N  N   . VAL A 1 148 ? -1.602  2.891   10.996  1.000 6.992  ? 148 VAL AAA N   1 
ATOM   1095 C  CA  . VAL A 1 148 ? -0.363  2.697   11.768  1.000 7.653  ? 148 VAL AAA CA  1 
ATOM   1096 C  C   . VAL A 1 148 ? 0.604   1.957   10.860  1.000 7.199  ? 148 VAL AAA C   1 
ATOM   1097 O  O   . VAL A 1 148 ? 0.219   0.984   10.176  1.000 9.046  ? 148 VAL AAA O   1 
ATOM   1098 C  CB  . VAL A 1 148 ? -0.670  1.963   13.087  1.000 8.837  ? 148 VAL AAA CB  1 
ATOM   1099 C  CG1 . VAL A 1 148 ? 0.581   1.728   13.894  1.000 8.729  ? 148 VAL AAA CG1 1 
ATOM   1100 C  CG2 . VAL A 1 148 ? -1.680  2.699   13.911  1.000 9.298  ? 148 VAL AAA CG2 1 
ATOM   1101 N  N   . ILE A 1 149 ? 1.852   2.325   10.915  1.000 7.682  ? 149 ILE AAA N   1 
ATOM   1102 C  CA  . ILE A 1 149 ? 2.898   1.822   10.002  1.000 7.896  ? 149 ILE AAA CA  1 
ATOM   1103 C  C   . ILE A 1 149 ? 3.485   0.559   10.646  1.000 7.770  ? 149 ILE AAA C   1 
ATOM   1104 O  O   . ILE A 1 149 ? 4.007   0.590   11.787  1.000 8.433  ? 149 ILE AAA O   1 
ATOM   1105 C  CB  . ILE A 1 149 ? 3.948   2.920   9.796   1.000 7.919  ? 149 ILE AAA CB  1 
ATOM   1106 C  CG1 . ILE A 1 149 ? 3.308   4.149   9.146   1.000 9.092  ? 149 ILE AAA CG1 1 
ATOM   1107 C  CG2 . ILE A 1 149 ? 5.111   2.419   8.979   1.000 8.716  ? 149 ILE AAA CG2 1 
ATOM   1108 C  CD1 . ILE A 1 149 ? 4.148   5.379   9.190   1.000 8.911  ? 149 ILE AAA CD1 1 
ATOM   1109 N  N   . GLY A 1 150 ? 3.419   -0.562  9.916   1.000 6.992  ? 150 GLY AAA N   1 
ATOM   1110 C  CA  . GLY A 1 150 ? 3.762   -1.866  10.482  1.000 7.716  ? 150 GLY AAA CA  1 
ATOM   1111 C  C   . GLY A 1 150 ? 4.833   -2.594  9.701   1.000 8.275  ? 150 GLY AAA C   1 
ATOM   1112 O  O   . GLY A 1 150 ? 5.187   -2.240  8.551   1.000 9.135  ? 150 GLY AAA O   1 
ATOM   1113 N  N   . ILE A 1 151 ? 5.397   -3.617  10.322  1.000 8.395  ? 151 ILE AAA N   1 
ATOM   1114 C  CA  . ILE A 1 151 ? 6.457   -4.464  9.732   1.000 10.013 ? 151 ILE AAA CA  1 
ATOM   1115 C  C   . ILE A 1 151 ? 5.840   -5.440  8.752   1.000 10.013 ? 151 ILE AAA C   1 
ATOM   1116 O  O   . ILE A 1 151 ? 4.843   -6.115  9.077   1.000 10.578 ? 151 ILE AAA O   1 
ATOM   1117 C  CB  . ILE A 1 151 ? 7.201   -5.225  10.838  1.000 11.712 ? 151 ILE AAA CB  1 
ATOM   1118 C  CG1 . ILE A 1 151 ? 7.947   -4.261  11.741  1.000 12.328 ? 151 ILE AAA CG1 1 
ATOM   1119 C  CG2 . ILE A 1 151 ? 8.125   -6.276  10.235  1.000 13.289 ? 151 ILE AAA CG2 1 
ATOM   1120 C  CD1 . ILE A 1 151 ? 8.422   -4.870  13.027  1.000 13.963 ? 151 ILE AAA CD1 1 
ATOM   1121 N  N   . ALA A 1 152 ? 6.385   -5.540  7.535   1.000 9.644  ? 152 ALA AAA N   1 
ATOM   1122 C  CA  . ALA A 1 152 ? 5.909   -6.463  6.503   1.000 11.063 ? 152 ALA AAA CA  1 
ATOM   1123 C  C   . ALA A 1 152 ? 6.879   -7.626  6.369   1.000 10.417 ? 152 ALA AAA C   1 
ATOM   1124 O  O   . ALA A 1 152 ? 8.043   -7.560  6.769   1.000 10.989 ? 152 ALA AAA O   1 
ATOM   1125 C  CB  . ALA A 1 152 ? 5.742   -5.690  5.217   1.000 10.603 ? 152 ALA AAA CB  1 
ATOM   1126 N  N   . GLN A 1 153 ? 6.400   -8.655  5.689   1.000 11.208 ? 153 GLN AAA N   1 
ATOM   1127 C  CA  . GLN A 1 153 ? 7.168   -9.869  5.355   1.000 13.717 ? 153 GLN AAA CA  1 
ATOM   1128 C  C   . GLN A 1 153 ? 8.280   -9.531  4.364   1.000 17.371 ? 153 GLN AAA C   1 
ATOM   1129 O  O   . GLN A 1 153 ? 8.059   -8.769  3.398   1.000 20.908 ? 153 GLN AAA O   1 
ATOM   1130 C  CB  . GLN A 1 153 ? 6.176   -10.864 4.750   1.000 13.508 ? 153 GLN AAA CB  1 
ATOM   1131 C  CG  . GLN A 1 153 ? 6.808   -12.224 4.513   1.000 14.927 ? 153 GLN AAA CG  1 
ATOM   1132 C  CD  . GLN A 1 153 ? 5.722   -13.217 4.150   1.000 15.637 ? 153 GLN AAA CD  1 
ATOM   1133 O  OE1 . GLN A 1 153 ? 4.595   -13.180 4.648   1.000 15.588 ? 153 GLN AAA OE1 1 
ATOM   1134 N  NE2 . GLN A 1 153 ? 6.053   -14.110 3.235   1.000 17.698 ? 153 GLN AAA NE2 1 
ATOM   1135 O  OXT . GLN A 1 153 ? 9.380   -10.084 4.602   1.000 20.041 ? 153 GLN AAA OXT 1 
ATOM   1136 N  N   . ALA B 1 1   ? 6.737   4.228   31.547  1.000 32.334 ? 1   ALA BBB N   1 
ATOM   1137 C  CA  . ALA B 1 1   ? 7.730   4.970   30.756  1.000 30.741 ? 1   ALA BBB CA  1 
ATOM   1138 C  C   . ALA B 1 1   ? 7.458   4.794   29.254  1.000 27.650 ? 1   ALA BBB C   1 
ATOM   1139 O  O   . ALA B 1 1   ? 7.449   5.823   28.572  1.000 32.342 ? 1   ALA BBB O   1 
ATOM   1140 C  CB  . ALA B 1 1   ? 9.140   4.575   31.119  1.000 33.693 ? 1   ALA BBB CB  1 
ATOM   1141 N  N   . THR B 1 2   ? 7.277   3.576   28.733  1.000 18.823 ? 2   THR BBB N   1 
ATOM   1142 C  CA  . THR B 1 2   ? 6.887   3.417   27.306  1.000 15.262 ? 2   THR BBB CA  1 
ATOM   1143 C  C   . THR B 1 2   ? 5.428   2.996   27.247  1.000 12.820 ? 2   THR BBB C   1 
ATOM   1144 O  O   . THR B 1 2   ? 4.990   2.143   28.040  1.000 12.038 ? 2   THR BBB O   1 
ATOM   1145 C  CB  . THR B 1 2   ? 7.791   2.450   26.562  1.000 17.200 ? 2   THR BBB CB  1 
ATOM   1146 O  OG1 . THR B 1 2   ? 9.130   2.937   26.741  1.000 20.426 ? 2   THR BBB OG1 1 
ATOM   1147 C  CG2 . THR B 1 2   ? 7.468   2.306   25.094  1.000 18.249 ? 2   THR BBB CG2 1 
ATOM   1148 N  N   . LYS B 1 3   ? 4.665   3.670   26.394  1.000 12.404 ? 3   LYS BBB N   1 
ATOM   1149 C  CA  . LYS B 1 3   ? 3.219   3.447   26.217  1.000 12.376 ? 3   LYS BBB CA  1 
ATOM   1150 C  C   . LYS B 1 3   ? 2.957   3.158   24.746  1.000 10.492 ? 3   LYS BBB C   1 
ATOM   1151 O  O   . LYS B 1 3   ? 3.375   3.936   23.873  1.000 10.645 ? 3   LYS BBB O   1 
ATOM   1152 C  CB  . LYS B 1 3   ? 2.436   4.668   26.680  1.000 15.885 ? 3   LYS BBB CB  1 
ATOM   1153 C  CG  . LYS B 1 3   ? 2.552   4.930   28.176  1.000 23.409 ? 3   LYS BBB CG  1 
ATOM   1154 C  CD  . LYS B 1 3   ? 2.140   6.326   28.611  1.000 30.041 ? 3   LYS BBB CD  1 
ATOM   1155 C  CE  . LYS B 1 3   ? 2.437   6.543   30.077  1.000 33.229 ? 3   LYS BBB CE  1 
ATOM   1156 N  NZ  . LYS B 1 3   ? 1.762   5.516   30.898  1.000 38.570 ? 3   LYS BBB NZ  1 
ATOM   1157 N  N   . VAL B 1 4   ? 2.233   2.084   24.510  1.000 10.102 ? 4   VAL BBB N   1 
ATOM   1158 C  CA  . VAL B 1 4   ? 1.871   1.606   23.162  1.000 10.227 ? 4   VAL BBB CA  1 
ATOM   1159 C  C   . VAL B 1 4   ? 0.382   1.282   23.157  1.000 9.114  ? 4   VAL BBB C   1 
ATOM   1160 O  O   . VAL B 1 4   ? -0.190  1.015   24.228  1.000 9.567  ? 4   VAL BBB O   1 
ATOM   1161 C  CB  . VAL B 1 4   ? 2.824   0.434   22.884  1.000 13.171 ? 4   VAL BBB CB  1 
ATOM   1162 C  CG1 . VAL B 1 4   ? 2.276   -0.666  22.010  1.000 13.855 ? 4   VAL BBB CG1 1 
ATOM   1163 C  CG2 . VAL B 1 4   ? 4.201   0.948   22.496  1.000 11.237 ? 4   VAL BBB CG2 1 
ATOM   1164 N  N   . VAL B 1 5   ? -0.253  1.343   22.019  1.000 9.062  ? 5   VAL BBB N   1 
ATOM   1165 C  CA  . VAL B 1 5   ? -1.709  1.131   21.951  1.000 9.343  ? 5   VAL BBB CA  1 
ATOM   1166 C  C   . VAL B 1 5   ? -2.046  0.407   20.665  1.000 9.210  ? 5   VAL BBB C   1 
ATOM   1167 O  O   . VAL B 1 5   ? -1.294  0.424   19.688  1.000 9.530  ? 5   VAL BBB O   1 
ATOM   1168 C  CB  . VAL B 1 5   ? -2.405  2.488   22.032  1.000 10.792 ? 5   VAL BBB CB  1 
ATOM   1169 C  CG1 . VAL B 1 5   ? -2.079  3.366   20.833  1.000 11.272 ? 5   VAL BBB CG1 1 
ATOM   1170 C  CG2 . VAL B 1 5   ? -3.874  2.456   22.321  1.000 12.919 ? 5   VAL BBB CG2 1 
ATOM   1171 N  N   . CYS B 1 6   ? -3.200  -0.207  20.687  1.000 8.381  ? 6   CYS BBB N   1 
ATOM   1172 C  CA  . CYS B 1 6   ? -3.731  -0.891  19.504  1.000 8.932  ? 6   CYS BBB CA  1 
ATOM   1173 C  C   . CYS B 1 6   ? -5.235  -0.738  19.470  1.000 8.627  ? 6   CYS BBB C   1 
ATOM   1174 O  O   . CYS B 1 6   ? -5.894  -0.989  20.473  1.000 8.911  ? 6   CYS BBB O   1 
ATOM   1175 C  CB  . CYS B 1 6   ? -3.309  -2.342  19.578  1.000 9.758  ? 6   CYS BBB CB  1 
ATOM   1176 S  SG  . CYS B 1 6   ? -3.789  -3.328  18.142  1.000 11.471 ? 6   CYS BBB SG  1 
ATOM   1177 N  N   . VAL B 1 7   ? -5.780  -0.370  18.328  1.000 8.751  ? 7   VAL BBB N   1 
ATOM   1178 C  CA  . VAL B 1 7   ? -7.232  -0.360  18.099  1.000 9.323  ? 7   VAL BBB CA  1 
ATOM   1179 C  C   . VAL B 1 7   ? -7.551  -1.570  17.240  1.000 9.129  ? 7   VAL BBB C   1 
ATOM   1180 O  O   . VAL B 1 7   ? -6.951  -1.756  16.184  1.000 10.602 ? 7   VAL BBB O   1 
ATOM   1181 C  CB  . VAL B 1 7   ? -7.692  0.956   17.467  1.000 12.209 ? 7   VAL BBB CB  1 
ATOM   1182 C  CG1 . VAL B 1 7   ? -7.002  1.270   16.176  1.000 15.067 ? 7   VAL BBB CG1 1 
ATOM   1183 C  CG2 . VAL B 1 7   ? -9.174  0.882   17.230  1.000 13.089 ? 7   VAL BBB CG2 1 
ATOM   1184 N  N   . LEU B 1 8   ? -8.424  -2.439  17.726  1.000 9.024  ? 8   LEU BBB N   1 
ATOM   1185 C  CA  . LEU B 1 8   ? -8.791  -3.678  17.042  1.000 9.201  ? 8   LEU BBB CA  1 
ATOM   1186 C  C   . LEU B 1 8   ? -10.074 -3.461  16.243  1.000 8.802  ? 8   LEU BBB C   1 
ATOM   1187 O  O   . LEU B 1 8   ? -11.097 -3.058  16.856  1.000 9.672  ? 8   LEU BBB O   1 
ATOM   1188 C  CB  . LEU B 1 8   ? -9.003  -4.818  18.040  1.000 10.215 ? 8   LEU BBB CB  1 
ATOM   1189 C  CG  . LEU B 1 8   ? -7.824  -5.199  18.940  1.000 12.782 ? 8   LEU BBB CG  1 
ATOM   1190 C  CD1 . LEU B 1 8   ? -7.165  -4.067  19.701  1.000 17.665 ? 8   LEU BBB CD1 1 
ATOM   1191 C  CD2 . LEU B 1 8   ? -8.285  -6.243  19.956  1.000 16.294 ? 8   LEU BBB CD2 1 
ATOM   1192 N  N   . LYS B 1 9   ? -10.049 -3.811  14.970  1.000 9.158  ? 9   LYS BBB N   1 
ATOM   1193 C  CA  . LYS B 1 9   ? -11.221 -3.696  14.102  1.000 11.585 ? 9   LYS BBB CA  1 
ATOM   1194 C  C   . LYS B 1 9   ? -11.219 -4.906  13.186  1.000 10.529 ? 9   LYS BBB C   1 
ATOM   1195 O  O   . LYS B 1 9   ? -10.186 -5.396  12.849  1.000 10.613 ? 9   LYS BBB O   1 
ATOM   1196 C  CB  . LYS B 1 9   ? -11.232 -2.387  13.306  1.000 13.218 ? 9   LYS BBB CB  1 
ATOM   1197 C  CG  . LYS B 1 9   ? -11.360 -1.098  14.100  1.000 18.110 ? 9   LYS BBB CG  1 
ATOM   1198 C  CD  . LYS B 1 9   ? -11.497 0.104   13.177  1.000 22.775 ? 9   LYS BBB CD  1 
ATOM   1199 C  CE  . LYS B 1 9   ? -11.670 1.409   13.908  1.000 25.965 ? 9   LYS BBB CE  1 
ATOM   1200 N  NZ  . LYS B 1 9   ? -12.647 1.273   15.010  1.000 31.292 ? 9   LYS BBB NZ  1 
ATOM   1201 N  N   . GLY B 1 10  ? -12.370 -5.296  12.662  1.000 12.185 ? 10  GLY BBB N   1 
ATOM   1202 C  CA  . GLY B 1 10  ? -12.473 -6.369  11.663  1.000 13.588 ? 10  GLY BBB CA  1 
ATOM   1203 C  C   . GLY B 1 10  ? -13.714 -6.215  10.812  1.000 16.467 ? 10  GLY BBB C   1 
ATOM   1204 O  O   . GLY B 1 10  ? -14.194 -5.104  10.680  1.000 17.324 ? 10  GLY BBB O   1 
ATOM   1205 N  N   . ASP B 1 11  ? -14.221 -7.331  10.311  1.000 20.022 ? 11  ASP BBB N   1 
ATOM   1206 C  CA  . ASP B 1 11  ? -15.304 -7.327  9.286   1.000 21.991 ? 11  ASP BBB CA  1 
ATOM   1207 C  C   . ASP B 1 11  ? -16.664 -7.398  9.958   1.000 21.434 ? 11  ASP BBB C   1 
ATOM   1208 O  O   . ASP B 1 11  ? -17.649 -7.234  9.245   1.000 22.753 ? 11  ASP BBB O   1 
ATOM   1209 C  CB  . ASP B 1 11  ? -15.109 -8.461  8.281   1.000 25.868 ? 11  ASP BBB CB  1 
ATOM   1210 C  CG  . ASP B 1 11  ? -13.907 -8.227  7.393   1.000 30.565 ? 11  ASP BBB CG  1 
ATOM   1211 O  OD1 . ASP B 1 11  ? -13.372 -9.219  6.867   1.000 37.836 ? 11  ASP BBB OD1 1 
ATOM   1212 O  OD2 . ASP B 1 11  ? -13.490 -7.052  7.262   1.000 34.365 ? 11  ASP BBB OD2 1 
ATOM   1213 N  N   . GLY B 1 12  ? -16.722 -7.649  11.268  1.000 17.443 ? 12  GLY BBB N   1 
ATOM   1214 C  CA  . GLY B 1 12  ? -17.951 -7.908  12.038  1.000 17.245 ? 12  GLY BBB CA  1 
ATOM   1215 C  C   . GLY B 1 12  ? -18.119 -6.876  13.140  1.000 15.849 ? 12  GLY BBB C   1 
ATOM   1216 O  O   . GLY B 1 12  ? -17.668 -5.736  13.024  1.000 15.933 ? 12  GLY BBB O   1 
ATOM   1217 N  N   . PRO B 1 13  ? -18.757 -7.252  14.262  1.000 16.556 ? 13  PRO BBB N   1 
ATOM   1218 C  CA  . PRO B 1 13  ? -19.073 -6.290  15.305  1.000 16.862 ? 13  PRO BBB CA  1 
ATOM   1219 C  C   . PRO B 1 13  ? -17.951 -6.102  16.333  1.000 15.308 ? 13  PRO BBB C   1 
ATOM   1220 O  O   . PRO B 1 13  ? -18.129 -5.322  17.222  1.000 16.515 ? 13  PRO BBB O   1 
ATOM   1221 C  CB  . PRO B 1 13  ? -20.298 -6.920  15.991  1.000 17.853 ? 13  PRO BBB CB  1 
ATOM   1222 C  CG  . PRO B 1 13  ? -20.097 -8.407  15.812  1.000 18.451 ? 13  PRO BBB CG  1 
ATOM   1223 C  CD  . PRO B 1 13  ? -19.332 -8.580  14.516  1.000 18.115 ? 13  PRO BBB CD  1 
ATOM   1224 N  N   . VAL B 1 14  ? -16.850 -6.879  16.234  1.000 14.075 ? 14  VAL BBB N   1 
ATOM   1225 C  CA  . VAL B 1 14  ? -15.807 -6.885  17.288  1.000 13.304 ? 14  VAL BBB CA  1 
ATOM   1226 C  C   . VAL B 1 14  ? -14.912 -5.670  17.129  1.000 12.877 ? 14  VAL BBB C   1 
ATOM   1227 O  O   . VAL B 1 14  ? -14.358 -5.427  16.051  1.000 13.627 ? 14  VAL BBB O   1 
ATOM   1228 C  CB  . VAL B 1 14  ? -15.019 -8.185  17.293  1.000 12.976 ? 14  VAL BBB CB  1 
ATOM   1229 C  CG1 . VAL B 1 14  ? -13.935 -8.176  18.347  1.000 12.859 ? 14  VAL BBB CG1 1 
ATOM   1230 C  CG2 . VAL B 1 14  ? -15.975 -9.365  17.432  1.000 14.778 ? 14  VAL BBB CG2 1 
ATOM   1231 N  N   . GLN B 1 15  ? -14.815 -4.895  18.177  1.000 11.339 ? 15  GLN BBB N   1 
ATOM   1232 C  CA  . GLN B 1 15  ? -13.863 -3.760  18.237  1.000 12.634 ? 15  GLN BBB CA  1 
ATOM   1233 C  C   . GLN B 1 15  ? -13.253 -3.704  19.611  1.000 12.422 ? 15  GLN BBB C   1 
ATOM   1234 O  O   . GLN B 1 15  ? -13.909 -4.044  20.594  1.000 13.714 ? 15  GLN BBB O   1 
ATOM   1235 C  CB  . GLN B 1 15  ? -14.538 -2.433  17.999  1.000 15.829 ? 15  GLN BBB CB  1 
ATOM   1236 C  CG  . GLN B 1 15  ? -15.263 -2.339  16.689  1.000 17.514 ? 15  GLN BBB CG  1 
ATOM   1237 C  CD  . GLN B 1 15  ? -15.720 -0.926  16.434  1.000 20.890 ? 15  GLN BBB CD  1 
ATOM   1238 O  OE1 . GLN B 1 15  ? -16.167 -0.227  17.345  1.000 24.628 ? 15  GLN BBB OE1 1 
ATOM   1239 N  NE2 . GLN B 1 15  ? -15.637 -0.504  15.182  1.000 24.964 ? 15  GLN BBB NE2 1 
ATOM   1240 N  N   . GLY B 1 16  ? -12.050 -3.199  19.709  1.000 11.468 ? 16  GLY BBB N   1 
ATOM   1241 C  CA  . GLY B 1 16  ? -11.364 -3.135  20.999  1.000 11.694 ? 16  GLY BBB CA  1 
ATOM   1242 C  C   . GLY B 1 16  ? -10.342 -2.031  21.033  1.000 9.400  ? 16  GLY BBB C   1 
ATOM   1243 O  O   . GLY B 1 16  ? -9.911  -1.530  19.975  1.000 9.475  ? 16  GLY BBB O   1 
ATOM   1244 N  N   . ILE B 1 17  ? -9.888  -1.731  22.201  1.000 9.024  ? 17  ILE BBB N   1 
ATOM   1245 C  CA  . ILE B 1 17  ? -8.795  -0.791  22.509  1.000 10.079 ? 17  ILE BBB CA  1 
ATOM   1246 C  C   . ILE B 1 17  ? -7.908  -1.479  23.517  1.000 9.100  ? 17  ILE BBB C   1 
ATOM   1247 O  O   . ILE B 1 17  ? -8.416  -1.818  24.636  1.000 8.728  ? 17  ILE BBB O   1 
ATOM   1248 C  CB  . ILE B 1 17  ? -9.304  0.562   23.051  1.000 11.252 ? 17  ILE BBB CB  1 
ATOM   1249 C  CG1 . ILE B 1 17  ? -10.336 1.214   22.128  1.000 15.728 ? 17  ILE BBB CG1 1 
ATOM   1250 C  CG2 . ILE B 1 17  ? -8.133  1.456   23.351  1.000 12.524 ? 17  ILE BBB CG2 1 
ATOM   1251 C  CD1 . ILE B 1 17  ? -9.727  1.643   20.812  1.000 19.865 ? 17  ILE BBB CD1 1 
ATOM   1252 N  N   . ILE B 1 18  ? -6.639  -1.683  23.208  1.000 8.164  ? 18  ILE BBB N   1 
ATOM   1253 C  CA  . ILE B 1 18  ? -5.683  -2.318  24.131  1.000 8.336  ? 18  ILE BBB CA  1 
ATOM   1254 C  C   . ILE B 1 18  ? -4.511  -1.395  24.317  1.000 8.109  ? 18  ILE BBB C   1 
ATOM   1255 O  O   . ILE B 1 18  ? -3.879  -0.990  23.332  1.000 9.125  ? 18  ILE BBB O   1 
ATOM   1256 C  CB  . ILE B 1 18  ? -5.300  -3.712  23.656  1.000 8.924  ? 18  ILE BBB CB  1 
ATOM   1257 C  CG1 . ILE B 1 18  ? -6.531  -4.629  23.518  1.000 10.086 ? 18  ILE BBB CG1 1 
ATOM   1258 C  CG2 . ILE B 1 18  ? -4.252  -4.303  24.565  1.000 8.950  ? 18  ILE BBB CG2 1 
ATOM   1259 C  CD1 . ILE B 1 18  ? -7.214  -5.005  24.810  1.000 11.423 ? 18  ILE BBB CD1 1 
ATOM   1260 N  N   . ASN B 1 19  ? -4.114  -1.184  25.543  1.000 8.020  ? 19  ASN BBB N   1 
ATOM   1261 C  CA  . ASN B 1 19  ? -2.994  -0.371  25.971  1.000 7.866  ? 19  ASN BBB CA  1 
ATOM   1262 C  C   . ASN B 1 19  ? -1.922  -1.287  26.526  1.000 8.221  ? 19  ASN BBB C   1 
ATOM   1263 O  O   . ASN B 1 19  ? -2.243  -2.265  27.204  1.000 8.930  ? 19  ASN BBB O   1 
ATOM   1264 C  CB  . ASN B 1 19  ? -3.401  0.594   27.098  1.000 9.395  ? 19  ASN BBB CB  1 
ATOM   1265 C  CG  . ASN B 1 19  ? -4.599  1.422   26.705  1.000 9.799  ? 19  ASN BBB CG  1 
ATOM   1266 O  OD1 . ASN B 1 19  ? -5.768  1.127   27.020  1.000 12.658 ? 19  ASN BBB OD1 1 
ATOM   1267 N  ND2 . ASN B 1 19  ? -4.329  2.495   26.024  1.000 11.756 ? 19  ASN BBB ND2 1 
ATOM   1268 N  N   . PHE B 1 20  ? -0.698  -0.935  26.259  1.000 8.360  ? 20  PHE BBB N   1 
ATOM   1269 C  CA  . PHE B 1 20  ? 0.491   -1.622  26.786  1.000 7.918  ? 20  PHE BBB CA  1 
ATOM   1270 C  C   . PHE B 1 20  ? 1.406   -0.593  27.428  1.000 8.844  ? 20  PHE BBB C   1 
ATOM   1271 O  O   . PHE B 1 20  ? 1.679   0.500   26.849  1.000 10.061 ? 20  PHE BBB O   1 
ATOM   1272 C  CB  . PHE B 1 20  ? 1.279   -2.253  25.635  1.000 9.261  ? 20  PHE BBB CB  1 
ATOM   1273 C  CG  . PHE B 1 20  ? 0.557   -3.294  24.814  1.000 8.890  ? 20  PHE BBB CG  1 
ATOM   1274 C  CD1 . PHE B 1 20  ? -0.340  -2.921  23.799  1.000 8.703  ? 20  PHE BBB CD1 1 
ATOM   1275 C  CD2 . PHE B 1 20  ? 0.773   -4.641  25.045  1.000 9.869  ? 20  PHE BBB CD2 1 
ATOM   1276 C  CE1 . PHE B 1 20  ? -0.965  -3.884  23.023  1.000 9.541  ? 20  PHE BBB CE1 1 
ATOM   1277 C  CE2 . PHE B 1 20  ? 0.116   -5.597  24.295  1.000 10.015 ? 20  PHE BBB CE2 1 
ATOM   1278 C  CZ  . PHE B 1 20  ? -0.733  -5.202  23.284  1.000 9.791  ? 20  PHE BBB CZ  1 
ATOM   1279 N  N   . GLU B 1 21  ? 1.878   -0.885  28.626  1.000 9.205  ? 21  GLU BBB N   1 
ATOM   1280 C  CA  . GLU B 1 21  ? 2.784   0.052   29.320  1.000 10.521 ? 21  GLU BBB CA  1 
ATOM   1281 C  C   . GLU B 1 21  ? 3.946   -0.743  29.903  1.000 9.337  ? 21  GLU BBB C   1 
ATOM   1282 O  O   . GLU B 1 21  ? 3.711   -1.806  30.519  1.000 10.880 ? 21  GLU BBB O   1 
ATOM   1283 C  CB  . GLU B 1 21  ? 2.023   0.819   30.406  1.000 13.817 ? 21  GLU BBB CB  1 
ATOM   1284 C  CG  . GLU B 1 21  ? 0.894   1.671   29.866  1.000 22.164 ? 21  GLU BBB CG  1 
ATOM   1285 C  CD  . GLU B 1 21  ? 0.093   2.500   30.856  1.000 31.117 ? 21  GLU BBB CD  1 
ATOM   1286 O  OE1 . GLU B 1 21  ? 0.177   2.223   32.080  1.000 43.044 ? 21  GLU BBB OE1 1 
ATOM   1287 O  OE2 . GLU B 1 21  ? -0.636  3.418   30.390  1.000 41.102 ? 21  GLU BBB OE2 1 
ATOM   1288 N  N   . GLN B 1 22  ? 5.138   -0.198  29.796  1.000 9.715  ? 22  GLN BBB N   1 
ATOM   1289 C  CA  . GLN B 1 22  ? 6.352   -0.857  30.311  1.000 11.024 ? 22  GLN BBB CA  1 
ATOM   1290 C  C   . GLN B 1 22  ? 7.147   0.259   30.993  1.000 13.044 ? 22  GLN BBB C   1 
ATOM   1291 O  O   . GLN B 1 22  ? 7.579   1.149   30.309  1.000 14.791 ? 22  GLN BBB O   1 
ATOM   1292 C  CB  . GLN B 1 22  ? 7.107   -1.556  29.186  1.000 11.406 ? 22  GLN BBB CB  1 
ATOM   1293 C  CG  . GLN B 1 22  ? 8.208   -2.446  29.687  1.000 10.771 ? 22  GLN BBB CG  1 
ATOM   1294 C  CD  . GLN B 1 22  ? 8.875   -3.174  28.554  1.000 10.148 ? 22  GLN BBB CD  1 
ATOM   1295 O  OE1 . GLN B 1 22  ? 8.921   -2.682  27.440  1.000 11.455 ? 22  GLN BBB OE1 1 
ATOM   1296 N  NE2 . GLN B 1 22  ? 9.502   -4.292  28.884  1.000 11.102 ? 22  GLN BBB NE2 1 
ATOM   1297 N  N   . LYS B 1 23  ? 7.305   0.153   32.311  1.000 15.851 ? 23  LYS BBB N   1 
ATOM   1298 C  CA  . LYS B 1 23  ? 8.015   1.181   33.122  1.000 18.758 ? 23  LYS BBB CA  1 
ATOM   1299 C  C   . LYS B 1 23  ? 9.513   1.142   32.826  1.000 17.584 ? 23  LYS BBB C   1 
ATOM   1300 O  O   . LYS B 1 23  ? 10.167  2.197   32.793  1.000 20.395 ? 23  LYS BBB O   1 
ATOM   1301 C  CB  . LYS B 1 23  ? 7.791   0.885   34.598  1.000 20.980 ? 23  LYS BBB CB  1 
ATOM   1302 C  CG  . LYS B 1 23  ? 6.347   1.050   35.062  1.000 24.467 ? 23  LYS BBB CG  1 
ATOM   1303 C  CD  . LYS B 1 23  ? 6.071   0.457   36.436  1.000 30.794 ? 23  LYS BBB CD  1 
ATOM   1304 C  CE  . LYS B 1 23  ? 5.963   1.454   37.578  1.000 36.911 ? 23  LYS BBB CE  1 
ATOM   1305 N  NZ  . LYS B 1 23  ? 4.547   1.699   37.956  1.000 38.759 ? 23  LYS BBB NZ  1 
ATOM   1306 N  N   . GLU B 1 24  ? 10.053  -0.051  32.692  1.000 16.493 ? 24  GLU BBB N   1 
ATOM   1307 C  CA  . GLU B 1 24  ? 11.504  -0.230  32.503  1.000 17.744 ? 24  GLU BBB CA  1 
ATOM   1308 C  C   . GLU B 1 24  ? 11.719  -1.326  31.452  1.000 14.685 ? 24  GLU BBB C   1 
ATOM   1309 O  O   . GLU B 1 24  ? 10.899  -2.291  31.407  1.000 12.892 ? 24  GLU BBB O   1 
ATOM   1310 C  CB  . GLU B 1 24  ? 12.130  -0.588  33.856  1.000 24.680 ? 24  GLU BBB CB  1 
ATOM   1311 C  CG  . GLU B 1 24  ? 11.951  0.453   34.947  1.000 29.461 ? 24  GLU BBB CG  1 
ATOM   1312 C  CD  . GLU B 1 24  ? 12.905  1.625   34.808  1.000 36.470 ? 24  GLU BBB CD  1 
ATOM   1313 O  OE1 . GLU B 1 24  ? 13.707  1.631   33.839  1.000 45.204 ? 24  GLU BBB OE1 1 
ATOM   1314 O  OE2 . GLU B 1 24  ? 12.855  2.528   35.670  1.000 43.930 ? 24  GLU BBB OE2 1 
ATOM   1315 N  N   . SER B 1 25  ? 12.811  -1.258  30.714  1.000 15.882 ? 25  SER BBB N   1 
ATOM   1316 C  CA  . SER B 1 25  ? 13.036  -2.217  29.610  1.000 16.786 ? 25  SER BBB CA  1 
ATOM   1317 C  C   . SER B 1 25  ? 13.225  -3.641  30.135  1.000 14.815 ? 25  SER BBB C   1 
ATOM   1318 O  O   . SER B 1 25  ? 12.936  -4.579  29.365  1.000 14.157 ? 25  SER BBB O   1 
ATOM   1319 C  CB  . SER B 1 25  ? 14.151  -1.818  28.716  1.000 18.643 ? 25  SER BBB CB  1 
ATOM   1320 O  OG  . SER B 1 25  ? 15.367  -1.944  29.401  1.000 21.266 ? 25  SER BBB OG  1 
ATOM   1321 N  N   . ASN B 1 26  ? 13.615  -3.833  31.398  1.000 14.104 ? 26  ASN BBB N   1 
ATOM   1322 C  CA  . ASN B 1 26  ? 13.784  -5.197  31.962  1.000 13.941 ? 26  ASN BBB CA  1 
ATOM   1323 C  C   . ASN B 1 26  ? 12.535  -5.598  32.752  1.000 13.699 ? 26  ASN BBB C   1 
ATOM   1324 O  O   . ASN B 1 26  ? 12.554  -6.668  33.376  1.000 15.575 ? 26  ASN BBB O   1 
ATOM   1325 C  CB  . ASN B 1 26  ? 15.035  -5.292  32.833  1.000 16.210 ? 26  ASN BBB CB  1 
ATOM   1326 C  CG  . ASN B 1 26  ? 14.981  -4.410  34.045  1.000 18.659 ? 26  ASN BBB CG  1 
ATOM   1327 O  OD1 . ASN B 1 26  ? 14.143  -3.520  34.142  1.000 21.158 ? 26  ASN BBB OD1 1 
ATOM   1328 N  ND2 . ASN B 1 26  ? 15.836  -4.678  35.023  1.000 20.566 ? 26  ASN BBB ND2 1 
ATOM   1329 N  N   . GLY B 1 27  ? 11.460  -4.824  32.660  1.000 13.029 ? 27  GLY BBB N   1 
ATOM   1330 C  CA  . GLY B 1 27  ? 10.281  -5.075  33.485  1.000 12.238 ? 27  GLY BBB CA  1 
ATOM   1331 C  C   . GLY B 1 27  ? 9.147   -5.665  32.665  1.000 10.826 ? 27  GLY BBB C   1 
ATOM   1332 O  O   . GLY B 1 27  ? 9.202   -5.709  31.422  1.000 12.045 ? 27  GLY BBB O   1 
ATOM   1333 N  N   . PRO B 1 28  ? 8.069   -6.085  33.330  1.000 11.327 ? 28  PRO BBB N   1 
ATOM   1334 C  CA  . PRO B 1 28  ? 6.911   -6.627  32.641  1.000 11.523 ? 28  PRO BBB CA  1 
ATOM   1335 C  C   . PRO B 1 28  ? 6.137   -5.544  31.894  1.000 10.180 ? 28  PRO BBB C   1 
ATOM   1336 O  O   . PRO B 1 28  ? 6.306   -4.351  32.129  1.000 11.511 ? 28  PRO BBB O   1 
ATOM   1337 C  CB  . PRO B 1 28  ? 6.093   -7.221  33.776  1.000 12.556 ? 28  PRO BBB CB  1 
ATOM   1338 C  CG  . PRO B 1 28  ? 6.442   -6.374  34.946  1.000 14.601 ? 28  PRO BBB CG  1 
ATOM   1339 C  CD  . PRO B 1 28  ? 7.927   -6.118  34.790  1.000 13.125 ? 28  PRO BBB CD  1 
ATOM   1340 N  N   . VAL B 1 29  ? 5.318   -6.007  30.984  1.000 9.545  ? 29  VAL BBB N   1 
ATOM   1341 C  CA  . VAL B 1 29  ? 4.381   -5.116  30.259  1.000 9.609  ? 29  VAL BBB CA  1 
ATOM   1342 C  C   . VAL B 1 29  ? 2.992   -5.330  30.848  1.000 10.002 ? 29  VAL BBB C   1 
ATOM   1343 O  O   . VAL B 1 29  ? 2.539   -6.478  30.939  1.000 10.958 ? 29  VAL BBB O   1 
ATOM   1344 C  CB  . VAL B 1 29  ? 4.403   -5.452  28.764  1.000 9.322  ? 29  VAL BBB CB  1 
ATOM   1345 C  CG1 . VAL B 1 29  ? 3.461   -4.525  28.034  1.000 9.013  ? 29  VAL BBB CG1 1 
ATOM   1346 C  CG2 . VAL B 1 29  ? 5.797   -5.370  28.194  1.000 10.158 ? 29  VAL BBB CG2 1 
ATOM   1347 N  N   . LYS B 1 30  ? 2.348   -4.239  31.248  1.000 9.825  ? 30  LYS BBB N   1 
ATOM   1348 C  CA  . LYS B 1 30  ? 0.946   -4.236  31.656  1.000 10.273 ? 30  LYS BBB CA  1 
ATOM   1349 C  C   . LYS B 1 30  ? 0.102   -4.064  30.401  1.000 8.958  ? 30  LYS BBB C   1 
ATOM   1350 O  O   . LYS B 1 30  ? 0.378   -3.127  29.608  1.000 10.207 ? 30  LYS BBB O   1 
ATOM   1351 C  CB  . LYS B 1 30  ? 0.721   -3.092  32.641  1.000 12.847 ? 30  LYS BBB CB  1 
ATOM   1352 C  CG  . LYS B 1 30  ? -0.685  -2.965  33.149  1.000 18.349 ? 30  LYS BBB CG  1 
ATOM   1353 C  CD  . LYS B 1 30  ? -0.853  -1.756  34.076  1.000 23.571 ? 30  LYS BBB CD  1 
ATOM   1354 C  CE  . LYS B 1 30  ? -2.272  -1.647  34.611  1.000 28.330 ? 30  LYS BBB CE  1 
ATOM   1355 N  NZ  . LYS B 1 30  ? -2.427  -2.447  35.847  1.000 33.533 ? 30  LYS BBB NZ  1 
ATOM   1356 N  N   . VAL B 1 31  ? -0.928  -4.870  30.255  1.000 9.722  ? 31  VAL BBB N   1 
ATOM   1357 C  CA  . VAL B 1 31  ? -1.827  -4.880  29.082  1.000 9.652  ? 31  VAL BBB CA  1 
ATOM   1358 C  C   . VAL B 1 31  ? -3.212  -4.645  29.620  1.000 10.896 ? 31  VAL BBB C   1 
ATOM   1359 O  O   . VAL B 1 31  ? -3.662  -5.395  30.520  1.000 12.646 ? 31  VAL BBB O   1 
ATOM   1360 C  CB  . VAL B 1 31  ? -1.725  -6.203  28.339  1.000 10.219 ? 31  VAL BBB CB  1 
ATOM   1361 C  CG1 . VAL B 1 31  ? -2.573  -6.151  27.081  1.000 10.122 ? 31  VAL BBB CG1 1 
ATOM   1362 C  CG2 . VAL B 1 31  ? -0.273  -6.579  28.062  1.000 10.804 ? 31  VAL BBB CG2 1 
ATOM   1363 N  N   . TRP B 1 32  ? -3.886  -3.610  29.195  1.000 10.000 ? 32  TRP BBB N   1 
ATOM   1364 C  CA  . TRP B 1 32  ? -5.229  -3.328  29.739  1.000 10.737 ? 32  TRP BBB CA  1 
ATOM   1365 C  C   . TRP B 1 32  ? -6.074  -2.669  28.681  1.000 9.929  ? 32  TRP BBB C   1 
ATOM   1366 O  O   . TRP B 1 32  ? -5.569  -1.916  27.819  1.000 9.874  ? 32  TRP BBB O   1 
ATOM   1367 C  CB  . TRP B 1 32  ? -5.151  -2.467  31.016  1.000 12.449 ? 32  TRP BBB CB  1 
ATOM   1368 C  CG  . TRP B 1 32  ? -4.605  -1.077  30.842  1.000 15.306 ? 32  TRP BBB CG  1 
ATOM   1369 C  CD1 . TRP B 1 32  ? -3.286  -0.687  30.872  1.000 16.041 ? 32  TRP BBB CD1 1 
ATOM   1370 C  CD2 . TRP B 1 32  ? -5.337  0.118   30.523  1.000 18.337 ? 32  TRP BBB CD2 1 
ATOM   1371 N  NE1 . TRP B 1 32  ? -3.169  0.655   30.648  1.000 18.900 ? 32  TRP BBB NE1 1 
ATOM   1372 C  CE2 . TRP B 1 32  ? -4.405  1.173   30.409  1.000 16.285 ? 32  TRP BBB CE2 1 
ATOM   1373 C  CE3 . TRP B 1 32  ? -6.679  0.378   30.289  1.000 17.069 ? 32  TRP BBB CE3 1 
ATOM   1374 C  CZ2 . TRP B 1 32  ? -4.784  2.483   30.090  1.000 19.395 ? 32  TRP BBB CZ2 1 
ATOM   1375 C  CZ3 . TRP B 1 32  ? -7.062  1.674   29.994  1.000 18.661 ? 32  TRP BBB CZ3 1 
ATOM   1376 C  CH2 . TRP B 1 32  ? -6.129  2.711   29.907  1.000 20.470 ? 32  TRP BBB CH2 1 
ATOM   1377 N  N   . GLY B 1 33  ? -7.369  -2.896  28.772  1.000 9.094  ? 33  GLY BBB N   1 
ATOM   1378 C  CA  . GLY B 1 33  ? -8.331  -2.253  27.880  1.000 8.809  ? 33  GLY BBB CA  1 
ATOM   1379 C  C   . GLY B 1 33  ? -9.548  -3.085  27.759  1.000 8.766  ? 33  GLY BBB C   1 
ATOM   1380 O  O   . GLY B 1 33  ? -9.937  -3.758  28.755  1.000 9.911  ? 33  GLY BBB O   1 
ATOM   1381 N  N   A SER B 1 34  ? -10.266 -2.970  26.653  0.500 9.619  ? 34  SER BBB N   1 
ATOM   1382 N  N   B SER B 1 34  ? -10.213 -3.045  26.641  0.500 8.871  ? 34  SER BBB N   1 
ATOM   1383 C  CA  A SER B 1 34  ? -11.608 -3.564  26.481  0.500 11.242 ? 34  SER BBB CA  1 
ATOM   1384 C  CA  B SER B 1 34  ? -11.470 -3.790  26.537  0.500 9.909  ? 34  SER BBB CA  1 
ATOM   1385 C  C   A SER B 1 34  ? -11.808 -4.028  25.046  0.500 10.895 ? 34  SER BBB C   1 
ATOM   1386 C  C   B SER B 1 34  ? -11.727 -4.103  25.084  0.500 9.903  ? 34  SER BBB C   1 
ATOM   1387 O  O   A SER B 1 34  ? -11.495 -3.260  24.124  0.500 11.185 ? 34  SER BBB O   1 
ATOM   1388 O  O   B SER B 1 34  ? -11.205 -3.395  24.216  0.500 9.848  ? 34  SER BBB O   1 
ATOM   1389 C  CB  A SER B 1 34  ? -12.676 -2.605  26.896  0.500 13.103 ? 34  SER BBB CB  1 
ATOM   1390 C  CB  B SER B 1 34  ? -12.557 -3.027  27.178  0.500 10.830 ? 34  SER BBB CB  1 
ATOM   1391 O  OG  A SER B 1 34  ? -13.917 -3.285  27.042  0.500 17.124 ? 34  SER BBB OG  1 
ATOM   1392 O  OG  B SER B 1 34  ? -12.827 -1.870  26.432  0.500 10.971 ? 34  SER BBB OG  1 
ATOM   1393 N  N   . ILE B 1 35  ? -12.420 -5.198  24.873  1.000 10.619 ? 35  ILE BBB N   1 
ATOM   1394 C  CA  . ILE B 1 35  ? -12.871 -5.657  23.543  1.000 11.176 ? 35  ILE BBB CA  1 
ATOM   1395 C  C   . ILE B 1 35  ? -14.350 -5.942  23.642  1.000 12.165 ? 35  ILE BBB C   1 
ATOM   1396 O  O   . ILE B 1 35  ? -14.739 -6.529  24.657  1.000 12.893 ? 35  ILE BBB O   1 
ATOM   1397 C  CB  . ILE B 1 35  ? -12.091 -6.892  23.078  1.000 12.201 ? 35  ILE BBB CB  1 
ATOM   1398 C  CG1 . ILE B 1 35  ? -10.597 -6.685  23.235  1.000 12.333 ? 35  ILE BBB CG1 1 
ATOM   1399 C  CG2 . ILE B 1 35  ? -12.507 -7.212  21.645  1.000 11.606 ? 35  ILE BBB CG2 1 
ATOM   1400 C  CD1 . ILE B 1 35  ? -9.796  -7.935  23.005  1.000 13.023 ? 35  ILE BBB CD1 1 
ATOM   1401 N  N   . LYS B 1 36  ? -15.105 -5.453  22.713  1.000 11.821 ? 36  LYS BBB N   1 
ATOM   1402 C  CA  . LYS B 1 36  ? -16.567 -5.550  22.792  1.000 13.242 ? 36  LYS BBB CA  1 
ATOM   1403 C  C   . LYS B 1 36  ? -17.087 -6.187  21.524  1.000 12.392 ? 36  LYS BBB C   1 
ATOM   1404 O  O   . LYS B 1 36  ? -16.378 -6.347  20.508  1.000 12.749 ? 36  LYS BBB O   1 
ATOM   1405 C  CB  . LYS B 1 36  ? -17.117 -4.152  23.081  1.000 16.651 ? 36  LYS BBB CB  1 
ATOM   1406 C  CG  . LYS B 1 36  ? -16.640 -3.588  24.410  1.000 20.214 ? 36  LYS BBB CG  1 
ATOM   1407 C  CD  . LYS B 1 36  ? -17.169 -2.220  24.740  1.000 23.826 ? 36  LYS BBB CD  1 
ATOM   1408 C  CE  . LYS B 1 36  ? -16.627 -1.719  26.051  1.000 25.736 ? 36  LYS BBB CE  1 
ATOM   1409 N  NZ  . LYS B 1 36  ? -17.124 -0.360  26.339  1.000 29.675 ? 36  LYS BBB NZ  1 
ATOM   1410 N  N   . GLY B 1 37  ? -18.310 -6.692  21.595  1.000 12.932 ? 37  GLY BBB N   1 
ATOM   1411 C  CA  . GLY B 1 37  ? -18.914 -7.358  20.446  1.000 13.324 ? 37  GLY BBB CA  1 
ATOM   1412 C  C   . GLY B 1 37  ? -18.577 -8.828  20.326  1.000 14.353 ? 37  GLY BBB C   1 
ATOM   1413 O  O   . GLY B 1 37  ? -18.858 -9.438  19.289  1.000 15.444 ? 37  GLY BBB O   1 
ATOM   1414 N  N   . LEU B 1 38  ? -17.998 -9.412  21.378  1.000 13.206 ? 38  LEU BBB N   1 
ATOM   1415 C  CA  . LEU B 1 38  ? -17.561 -10.836 21.381  1.000 12.625 ? 38  LEU BBB CA  1 
ATOM   1416 C  C   . LEU B 1 38  ? -18.686 -11.756 21.859  1.000 14.083 ? 38  LEU BBB C   1 
ATOM   1417 O  O   . LEU B 1 38  ? -19.442 -11.360 22.731  1.000 15.565 ? 38  LEU BBB O   1 
ATOM   1418 C  CB  . LEU B 1 38  ? -16.331 -11.000 22.286  1.000 12.154 ? 38  LEU BBB CB  1 
ATOM   1419 C  CG  . LEU B 1 38  ? -15.049 -10.351 21.803  1.000 11.525 ? 38  LEU BBB CG  1 
ATOM   1420 C  CD1 . LEU B 1 38  ? -14.082 -10.264 22.962  1.000 12.398 ? 38  LEU BBB CD1 1 
ATOM   1421 C  CD2 . LEU B 1 38  ? -14.431 -11.123 20.651  1.000 11.840 ? 38  LEU BBB CD2 1 
ATOM   1422 N  N   . THR B 1 39  ? -18.626 -13.004 21.452  1.000 15.721 ? 39  THR BBB N   1 
ATOM   1423 C  CA  . THR B 1 39  ? -19.452 -14.061 22.081  1.000 17.265 ? 39  THR BBB CA  1 
ATOM   1424 C  C   . THR B 1 39  ? -18.925 -14.341 23.478  1.000 17.766 ? 39  THR BBB C   1 
ATOM   1425 O  O   . THR B 1 39  ? -17.694 -14.262 23.716  1.000 19.158 ? 39  THR BBB O   1 
ATOM   1426 C  CB  . THR B 1 39  ? -19.460 -15.327 21.228  1.000 17.665 ? 39  THR BBB CB  1 
ATOM   1427 O  OG1 . THR B 1 39  ? -18.120 -15.795 21.088  1.000 17.932 ? 39  THR BBB OG1 1 
ATOM   1428 C  CG2 . THR B 1 39  ? -20.093 -15.096 19.874  1.000 18.214 ? 39  THR BBB CG2 1 
ATOM   1429 N  N   . GLU B 1 40  ? -19.773 -14.693 24.424  1.000 16.142 ? 40  GLU BBB N   1 
ATOM   1430 C  CA  . GLU B 1 40  ? -19.345 -15.002 25.804  1.000 17.703 ? 40  GLU BBB CA  1 
ATOM   1431 C  C   . GLU B 1 40  ? -18.324 -16.144 25.764  1.000 16.565 ? 40  GLU BBB C   1 
ATOM   1432 O  O   . GLU B 1 40  ? -18.536 -17.153 25.097  1.000 19.961 ? 40  GLU BBB O   1 
ATOM   1433 C  CB  . GLU B 1 40  ? -20.569 -15.356 26.660  1.000 18.942 ? 40  GLU BBB CB  1 
ATOM   1434 C  CG  . GLU B 1 40  ? -20.285 -15.505 28.140  1.000 20.591 ? 40  GLU BBB CG  1 
ATOM   1435 C  CD  . GLU B 1 40  ? -19.764 -16.880 28.573  1.000 23.486 ? 40  GLU BBB CD  1 
ATOM   1436 O  OE1 . GLU B 1 40  ? -19.916 -17.844 27.841  1.000 28.949 ? 40  GLU BBB OE1 1 
ATOM   1437 O  OE2 . GLU B 1 40  ? -19.124 -16.926 29.586  1.000 36.820 ? 40  GLU BBB OE2 1 
ATOM   1438 N  N   . GLY B 1 41  ? -17.309 -16.013 26.598  1.000 16.171 ? 41  GLY BBB N   1 
ATOM   1439 C  CA  . GLY B 1 41  ? -16.354 -17.092 26.846  1.000 14.121 ? 41  GLY BBB CA  1 
ATOM   1440 C  C   . GLY B 1 41  ? -14.975 -16.664 26.391  1.000 12.693 ? 41  GLY BBB C   1 
ATOM   1441 O  O   . GLY B 1 41  ? -14.696 -15.433 26.233  1.000 13.416 ? 41  GLY BBB O   1 
ATOM   1442 N  N   . LEU B 1 42  ? -14.142 -17.652 26.179  1.000 11.545 ? 42  LEU BBB N   1 
ATOM   1443 C  CA  . LEU B 1 42  ? -12.702 -17.427 25.937  1.000 10.304 ? 42  LEU BBB CA  1 
ATOM   1444 C  C   . LEU B 1 42  ? -12.444 -17.178 24.454  1.000 9.817  ? 42  LEU BBB C   1 
ATOM   1445 O  O   . LEU B 1 42  ? -12.959 -17.895 23.597  1.000 10.706 ? 42  LEU BBB O   1 
ATOM   1446 C  CB  . LEU B 1 42  ? -11.951 -18.659 26.414  1.000 11.109 ? 42  LEU BBB CB  1 
ATOM   1447 C  CG  . LEU B 1 42  ? -11.973 -18.914 27.925  1.000 14.590 ? 42  LEU BBB CG  1 
ATOM   1448 C  CD1 . LEU B 1 42  ? -11.456 -20.320 28.217  1.000 15.902 ? 42  LEU BBB CD1 1 
ATOM   1449 C  CD2 . LEU B 1 42  ? -11.164 -17.918 28.686  1.000 17.034 ? 42  LEU BBB CD2 1 
ATOM   1450 N  N   . HIS B 1 43  ? -11.555 -16.222 24.188  1.000 8.887  ? 43  HIS BBB N   1 
ATOM   1451 C  CA  . HIS B 1 43  ? -11.090 -15.884 22.846  1.000 8.437  ? 43  HIS BBB CA  1 
ATOM   1452 C  C   . HIS B 1 43  ? -9.579  -15.767 22.797  1.000 7.533  ? 43  HIS BBB C   1 
ATOM   1453 O  O   . HIS B 1 43  ? -9.018  -14.992 23.578  1.000 7.675  ? 43  HIS BBB O   1 
ATOM   1454 C  CB  . HIS B 1 43  ? -11.752 -14.584 22.414  1.000 8.774  ? 43  HIS BBB CB  1 
ATOM   1455 C  CG  . HIS B 1 43  ? -13.225 -14.682 22.222  1.000 9.872  ? 43  HIS BBB CG  1 
ATOM   1456 N  ND1 . HIS B 1 43  ? -13.754 -14.973 21.008  1.000 11.477 ? 43  HIS BBB ND1 1 
ATOM   1457 C  CD2 . HIS B 1 43  ? -14.241 -14.484 23.081  1.000 10.311 ? 43  HIS BBB CD2 1 
ATOM   1458 C  CE1 . HIS B 1 43  ? -15.106 -14.953 21.153  1.000 11.379 ? 43  HIS BBB CE1 1 
ATOM   1459 N  NE2 . HIS B 1 43  ? -15.401 -14.668 22.372  1.000 12.323 ? 43  HIS BBB NE2 1 
ATOM   1460 N  N   . GLY B 1 44  ? -8.967  -16.468 21.853  1.000 7.431  ? 44  GLY BBB N   1 
ATOM   1461 C  CA  . GLY B 1 44  ? -7.515  -16.388 21.746  1.000 7.462  ? 44  GLY BBB CA  1 
ATOM   1462 C  C   . GLY B 1 44  ? -7.034  -14.975 21.430  1.000 6.944  ? 44  GLY BBB C   1 
ATOM   1463 O  O   . GLY B 1 44  ? -7.744  -14.218 20.741  1.000 8.098  ? 44  GLY BBB O   1 
ATOM   1464 N  N   . PHE B 1 45  ? -5.882  -14.635 21.960  1.000 7.383  ? 45  PHE BBB N   1 
ATOM   1465 C  CA  . PHE B 1 45  ? -5.394  -13.240 22.037  1.000 7.557  ? 45  PHE BBB CA  1 
ATOM   1466 C  C   . PHE B 1 45  ? -3.902  -13.311 21.772  1.000 7.371  ? 45  PHE BBB C   1 
ATOM   1467 O  O   . PHE B 1 45  ? -3.150  -13.757 22.654  1.000 8.274  ? 45  PHE BBB O   1 
ATOM   1468 C  CB  . PHE B 1 45  ? -5.732  -12.650 23.382  1.000 7.909  ? 45  PHE BBB CB  1 
ATOM   1469 C  CG  . PHE B 1 45  ? -5.466  -11.184 23.558  1.000 8.599  ? 45  PHE BBB CG  1 
ATOM   1470 C  CD1 . PHE B 1 45  ? -6.098  -10.244 22.744  1.000 9.067  ? 45  PHE BBB CD1 1 
ATOM   1471 C  CD2 . PHE B 1 45  ? -4.711  -10.745 24.612  1.000 9.598  ? 45  PHE BBB CD2 1 
ATOM   1472 C  CE1 . PHE B 1 45  ? -5.901  -8.889  22.964  1.000 10.366 ? 45  PHE BBB CE1 1 
ATOM   1473 C  CE2 . PHE B 1 45  ? -4.555  -9.391  24.838  1.000 10.144 ? 45  PHE BBB CE2 1 
ATOM   1474 C  CZ  . PHE B 1 45  ? -5.142  -8.476  24.017  1.000 10.057 ? 45  PHE BBB CZ  1 
ATOM   1475 N  N   . HIS B 1 46  ? -3.454  -12.873 20.603  1.000 6.805  ? 46  HIS BBB N   1 
ATOM   1476 C  CA  . HIS B 1 46  ? -2.059  -13.094 20.192  1.000 7.038  ? 46  HIS BBB CA  1 
ATOM   1477 C  C   . HIS B 1 46  ? -1.472  -11.877 19.497  1.000 6.671  ? 46  HIS BBB C   1 
ATOM   1478 O  O   . HIS B 1 46  ? -2.186  -11.152 18.799  1.000 7.270  ? 46  HIS BBB O   1 
ATOM   1479 C  CB  . HIS B 1 46  ? -1.920  -14.211 19.197  1.000 8.658  ? 46  HIS BBB CB  1 
ATOM   1480 C  CG  . HIS B 1 46  ? -2.600  -15.473 19.581  1.000 9.191  ? 46  HIS BBB CG  1 
ATOM   1481 N  ND1 . HIS B 1 46  ? -3.628  -15.932 18.847  1.000 11.622 ? 46  HIS BBB ND1 1 
ATOM   1482 C  CD2 . HIS B 1 46  ? -2.557  -16.233 20.687  1.000 11.057 ? 46  HIS BBB CD2 1 
ATOM   1483 C  CE1 . HIS B 1 46  ? -4.158  -16.989 19.480  1.000 11.602 ? 46  HIS BBB CE1 1 
ATOM   1484 N  NE2 . HIS B 1 46  ? -3.482  -17.231 20.530  1.000 11.254 ? 46  HIS BBB NE2 1 
ATOM   1485 N  N   . VAL B 1 47  ? -0.160  -11.692 19.630  1.000 6.327  ? 47  VAL BBB N   1 
ATOM   1486 C  CA  . VAL B 1 47  ? 0.618   -10.809 18.721  1.000 6.088  ? 47  VAL BBB CA  1 
ATOM   1487 C  C   . VAL B 1 47  ? 1.067   -11.684 17.564  1.000 6.219  ? 47  VAL BBB C   1 
ATOM   1488 O  O   . VAL B 1 47  ? 1.729   -12.712 17.776  1.000 7.070  ? 47  VAL BBB O   1 
ATOM   1489 C  CB  . VAL B 1 47  ? 1.816   -10.165 19.432  1.000 6.505  ? 47  VAL BBB CB  1 
ATOM   1490 C  CG1 . VAL B 1 47  ? 2.548   -9.218  18.468  1.000 7.319  ? 47  VAL BBB CG1 1 
ATOM   1491 C  CG2 . VAL B 1 47  ? 1.322   -9.415  20.666  1.000 7.290  ? 47  VAL BBB CG2 1 
ATOM   1492 N  N   . HIS B 1 48  ? 0.684   -11.285 16.365  1.000 7.223  ? 48  HIS BBB N   1 
ATOM   1493 C  CA  . HIS B 1 48  ? 1.078   -11.919 15.089  1.000 7.248  ? 48  HIS BBB CA  1 
ATOM   1494 C  C   . HIS B 1 48  ? 2.220   -11.145 14.448  1.000 8.232  ? 48  HIS BBB C   1 
ATOM   1495 O  O   . HIS B 1 48  ? 2.500   -9.976  14.819  1.000 8.407  ? 48  HIS BBB O   1 
ATOM   1496 C  CB  . HIS B 1 48  ? -0.125  -11.992 14.161  1.000 7.192  ? 48  HIS BBB CB  1 
ATOM   1497 C  CG  . HIS B 1 48  ? -1.129  -13.004 14.586  1.000 7.234  ? 48  HIS BBB CG  1 
ATOM   1498 N  ND1 . HIS B 1 48  ? -1.421  -14.096 13.828  1.000 8.376  ? 48  HIS BBB ND1 1 
ATOM   1499 C  CD2 . HIS B 1 48  ? -1.955  -13.093 15.662  1.000 7.601  ? 48  HIS BBB CD2 1 
ATOM   1500 C  CE1 . HIS B 1 48  ? -2.385  -14.796 14.459  1.000 8.886  ? 48  HIS BBB CE1 1 
ATOM   1501 N  NE2 . HIS B 1 48  ? -2.722  -14.206 15.554  1.000 8.561  ? 48  HIS BBB NE2 1 
ATOM   1502 N  N   . GLU B 1 49  ? 2.968   -11.807 13.582  1.000 8.824  ? 49  GLU BBB N   1 
ATOM   1503 C  CA  . GLU B 1 49  ? 4.307   -11.357 13.167  1.000 9.279  ? 49  GLU BBB CA  1 
ATOM   1504 C  C   . GLU B 1 49  ? 4.252   -10.066 12.365  1.000 9.308  ? 49  GLU BBB C   1 
ATOM   1505 O  O   . GLU B 1 49  ? 5.184   -9.283  12.543  1.000 11.271 ? 49  GLU BBB O   1 
ATOM   1506 C  CB  . GLU B 1 49  ? 4.925   -12.443 12.324  1.000 10.631 ? 49  GLU BBB CB  1 
ATOM   1507 C  CG  . GLU B 1 49  ? 6.366   -12.127 11.928  1.000 11.733 ? 49  GLU BBB CG  1 
ATOM   1508 C  CD  . GLU B 1 49  ? 6.994   -13.213 11.087  1.000 14.094 ? 49  GLU BBB CD  1 
ATOM   1509 O  OE1 . GLU B 1 49  ? 6.280   -14.190 10.752  1.000 15.214 ? 49  GLU BBB OE1 1 
ATOM   1510 O  OE2 . GLU B 1 49  ? 8.193   -13.036 10.708  1.000 17.404 ? 49  GLU BBB OE2 1 
ATOM   1511 N  N   . PHE B 1 50  ? 3.317   -9.872  11.467  1.000 8.262  ? 50  PHE BBB N   1 
ATOM   1512 C  CA  . PHE B 1 50  ? 3.385   -8.726  10.529  1.000 8.727  ? 50  PHE BBB CA  1 
ATOM   1513 C  C   . PHE B 1 50  ? 2.347   -7.695  10.937  1.000 8.589  ? 50  PHE BBB C   1 
ATOM   1514 O  O   . PHE B 1 50  ? 1.187   -8.045  11.153  1.000 8.304  ? 50  PHE BBB O   1 
ATOM   1515 C  CB  . PHE B 1 50  ? 3.190   -9.134  9.069   1.000 8.848  ? 50  PHE BBB CB  1 
ATOM   1516 C  CG  . PHE B 1 50  ? 4.047   -10.285 8.676   1.000 9.360  ? 50  PHE BBB CG  1 
ATOM   1517 C  CD1 . PHE B 1 50  ? 5.400   -10.198 8.810   1.000 10.821 ? 50  PHE BBB CD1 1 
ATOM   1518 C  CD2 . PHE B 1 50  ? 3.491   -11.475 8.191   1.000 10.931 ? 50  PHE BBB CD2 1 
ATOM   1519 C  CE1 . PHE B 1 50  ? 6.205   -11.278 8.462   1.000 12.356 ? 50  PHE BBB CE1 1 
ATOM   1520 C  CE2 . PHE B 1 50  ? 4.303   -12.546 7.840   1.000 12.657 ? 50  PHE BBB CE2 1 
ATOM   1521 C  CZ  . PHE B 1 50  ? 5.651   -12.453 8.012   1.000 13.239 ? 50  PHE BBB CZ  1 
ATOM   1522 N  N   . GLY B 1 51  ? 2.750   -6.425  10.949  1.000 8.251  ? 51  GLY BBB N   1 
ATOM   1523 C  CA  . GLY B 1 51  ? 1.857   -5.268  11.047  1.000 8.554  ? 51  GLY BBB CA  1 
ATOM   1524 C  C   . GLY B 1 51  ? 1.272   -4.927  9.704   1.000 8.779  ? 51  GLY BBB C   1 
ATOM   1525 O  O   . GLY B 1 51  ? 1.321   -3.768  9.284   1.000 9.398  ? 51  GLY BBB O   1 
ATOM   1526 N  N   . ASP B 1 52  ? 0.709   -5.923  9.038   1.000 9.898  ? 52  ASP BBB N   1 
ATOM   1527 C  CA  . ASP B 1 52  ? 0.251   -5.840  7.630   1.000 9.722  ? 52  ASP BBB CA  1 
ATOM   1528 C  C   . ASP B 1 52  ? -1.227  -6.164  7.633   1.000 9.299  ? 52  ASP BBB C   1 
ATOM   1529 O  O   . ASP B 1 52  ? -1.550  -7.332  7.940   1.000 10.078 ? 52  ASP BBB O   1 
ATOM   1530 C  CB  . ASP B 1 52  ? 1.040   -6.792  6.734   1.000 10.419 ? 52  ASP BBB CB  1 
ATOM   1531 C  CG  . ASP B 1 52  ? 0.757   -6.605  5.261   1.000 10.600 ? 52  ASP BBB CG  1 
ATOM   1532 O  OD1 . ASP B 1 52  ? -0.277  -6.019  4.940   1.000 11.740 ? 52  ASP BBB OD1 1 
ATOM   1533 O  OD2 . ASP B 1 52  ? 1.627   -7.056  4.426   1.000 13.821 ? 52  ASP BBB OD2 1 
ATOM   1534 N  N   . ASN B 1 53  ? -2.074  -5.234  7.292   1.000 9.877  ? 53  ASN BBB N   1 
ATOM   1535 C  CA  . ASN B 1 53  ? -3.536  -5.425  7.240   1.000 10.796 ? 53  ASN BBB CA  1 
ATOM   1536 C  C   . ASN B 1 53  ? -4.015  -5.296  5.791   1.000 9.951  ? 53  ASN BBB C   1 
ATOM   1537 O  O   . ASN B 1 53  ? -5.185  -5.009  5.580   1.000 10.664 ? 53  ASN BBB O   1 
ATOM   1538 C  CB  . ASN B 1 53  ? -4.280  -4.466  8.180   1.000 11.867 ? 53  ASN BBB CB  1 
ATOM   1539 C  CG  . ASN B 1 53  ? -5.734  -4.814  8.408   1.000 13.826 ? 53  ASN BBB CG  1 
ATOM   1540 O  OD1 . ASN B 1 53  ? -6.650  -3.965  8.305   1.000 21.079 ? 53  ASN BBB OD1 1 
ATOM   1541 N  ND2 . ASN B 1 53  ? -5.934  -6.041  8.809   1.000 14.431 ? 53  ASN BBB ND2 1 
ATOM   1542 N  N   . THR B 1 54  ? -3.120  -5.500  4.842   1.000 10.040 ? 54  THR BBB N   1 
ATOM   1543 C  CA  . THR B 1 54  ? -3.446  -5.274  3.403   1.000 9.790  ? 54  THR BBB CA  1 
ATOM   1544 C  C   . THR B 1 54  ? -4.771  -5.934  3.001   1.000 10.056 ? 54  THR BBB C   1 
ATOM   1545 O  O   . THR B 1 54  ? -5.627  -5.290  2.389   1.000 10.928 ? 54  THR BBB O   1 
ATOM   1546 C  CB  . THR B 1 54  ? -2.340  -5.787  2.486   1.000 9.929  ? 54  THR BBB CB  1 
ATOM   1547 O  OG1 . THR B 1 54  ? -1.142  -5.050  2.746   1.000 12.037 ? 54  THR BBB OG1 1 
ATOM   1548 C  CG2 . THR B 1 54  ? -2.738  -5.620  1.031   1.000 11.665 ? 54  THR BBB CG2 1 
ATOM   1549 N  N   . ALA B 1 55  ? -4.936  -7.193  3.342   1.000 9.951  ? 55  ALA BBB N   1 
ATOM   1550 C  CA  . ALA B 1 55  ? -6.135  -7.966  2.980   1.000 10.798 ? 55  ALA BBB CA  1 
ATOM   1551 C  C   . ALA B 1 55  ? -6.906  -8.313  4.235   1.000 11.405 ? 55  ALA BBB C   1 
ATOM   1552 O  O   . ALA B 1 55  ? -7.587  -9.348  4.253   1.000 15.795 ? 55  ALA BBB O   1 
ATOM   1553 C  CB  . ALA B 1 55  ? -5.742  -9.177  2.185   1.000 11.062 ? 55  ALA BBB CB  1 
ATOM   1554 N  N   . GLY B 1 56  ? -6.849  -7.462  5.246   1.000 10.826 ? 56  GLY BBB N   1 
ATOM   1555 C  CA  . GLY B 1 56  ? -7.459  -7.744  6.544   1.000 10.869 ? 56  GLY BBB CA  1 
ATOM   1556 C  C   . GLY B 1 56  ? -6.526  -8.559  7.420   1.000 9.311  ? 56  GLY BBB C   1 
ATOM   1557 O  O   . GLY B 1 56  ? -5.286  -8.620  7.201   1.000 10.375 ? 56  GLY BBB O   1 
ATOM   1558 N  N   . CYS B 1 57  ? -7.102  -9.100  8.488   1.000 10.155 ? 57  CYS BBB N   1 
ATOM   1559 C  CA  . CYS B 1 57  ? -6.279  -9.672  9.573   1.000 10.073 ? 57  CYS BBB CA  1 
ATOM   1560 C  C   . CYS B 1 57  ? -5.465  -10.885 9.120   1.000 10.060 ? 57  CYS BBB C   1 
ATOM   1561 O  O   . CYS B 1 57  ? -4.475  -11.222 9.757   1.000 9.700  ? 57  CYS BBB O   1 
ATOM   1562 C  CB  . CYS B 1 57  ? -7.173  -10.046 10.743  1.000 10.246 ? 57  CYS BBB CB  1 
ATOM   1563 S  SG  . CYS B 1 57  ? -8.050  -8.654  11.492  1.000 12.757 ? 57  CYS BBB SG  1 
ATOM   1564 N  N   A THR B 1 58  ? -5.872  -11.524 8.042   0.500 10.567 ? 58  THR BBB N   1 
ATOM   1565 N  N   B THR B 1 58  ? -5.878  -11.541 8.030   0.500 9.677  ? 58  THR BBB N   1 
ATOM   1566 C  CA  A THR B 1 58  ? -5.113  -12.675 7.522   0.500 11.126 ? 58  THR BBB CA  1 
ATOM   1567 C  CA  B THR B 1 58  ? -5.104  -12.672 7.452   0.500 9.465  ? 58  THR BBB CA  1 
ATOM   1568 C  C   A THR B 1 58  ? -3.691  -12.232 7.132   0.500 9.954  ? 58  THR BBB C   1 
ATOM   1569 C  C   B THR B 1 58  ? -3.682  -12.225 7.134   0.500 9.028  ? 58  THR BBB C   1 
ATOM   1570 O  O   A THR B 1 58  ? -2.757  -13.051 7.258   0.500 10.050 ? 58  THR BBB O   1 
ATOM   1571 O  O   B THR B 1 58  ? -2.777  -13.062 7.186   0.500 8.986  ? 58  THR BBB O   1 
ATOM   1572 C  CB  A THR B 1 58  ? -5.990  -13.383 6.489   0.500 13.258 ? 58  THR BBB CB  1 
ATOM   1573 C  CB  B THR B 1 58  ? -5.722  -13.302 6.190   0.500 10.278 ? 58  THR BBB CB  1 
ATOM   1574 O  OG1 A THR B 1 58  ? -7.157  -13.870 7.155   0.500 18.831 ? 58  THR BBB OG1 1 
ATOM   1575 O  OG1 B THR B 1 58  ? -6.065  -12.285 5.253   0.500 9.479  ? 58  THR BBB OG1 1 
ATOM   1576 C  CG2 A THR B 1 58  ? -5.318  -14.592 5.912   0.500 12.505 ? 58  THR BBB CG2 1 
ATOM   1577 C  CG2 B THR B 1 58  ? -6.903  -14.198 6.506   0.500 11.347 ? 58  THR BBB CG2 1 
ATOM   1578 N  N   . SER B 1 59  ? -3.500  -10.969 6.733   1.000 8.682  ? 59  SER BBB N   1 
ATOM   1579 C  CA  . SER B 1 59  ? -2.192  -10.491 6.256   1.000 8.809  ? 59  SER BBB CA  1 
ATOM   1580 C  C   . SER B 1 59  ? -1.147  -10.436 7.365   1.000 8.384  ? 59  SER BBB C   1 
ATOM   1581 O  O   . SER B 1 59  ? 0.065   -10.354 7.082   1.000 10.153 ? 59  SER BBB O   1 
ATOM   1582 C  CB  . SER B 1 59  ? -2.355  -9.147  5.555   1.000 8.801  ? 59  SER BBB CB  1 
ATOM   1583 O  OG  . SER B 1 59  ? -3.222  -9.265  4.394   1.000 10.426 ? 59  SER BBB OG  1 
ATOM   1584 N  N   . ALA B 1 60  ? -1.608  -10.543 8.602   1.000 7.991  ? 60  ALA BBB N   1 
ATOM   1585 C  CA  . ALA B 1 60  ? -0.677  -10.445 9.742   1.000 8.205  ? 60  ALA BBB CA  1 
ATOM   1586 C  C   . ALA B 1 60  ? 0.174   -11.698 9.923   1.000 8.606  ? 60  ALA BBB C   1 
ATOM   1587 O  O   . ALA B 1 60  ? 1.121   -11.682 10.730  1.000 8.458  ? 60  ALA BBB O   1 
ATOM   1588 C  CB  . ALA B 1 60  ? -1.452  -10.181 10.988  1.000 8.747  ? 60  ALA BBB CB  1 
ATOM   1589 N  N   . GLY B 1 61  ? -0.117  -12.784 9.208   1.000 8.085  ? 61  GLY BBB N   1 
ATOM   1590 C  CA  . GLY B 1 61  ? 0.749   -13.960 9.269   1.000 8.501  ? 61  GLY BBB CA  1 
ATOM   1591 C  C   . GLY B 1 61  ? 0.610   -14.731 10.574  1.000 8.042  ? 61  GLY BBB C   1 
ATOM   1592 O  O   . GLY B 1 61  ? -0.411  -14.621 11.269  1.000 8.795  ? 61  GLY BBB O   1 
ATOM   1593 N  N   . PRO B 1 62  ? 1.631   -15.533 10.946  1.000 8.584  ? 62  PRO BBB N   1 
ATOM   1594 C  CA  . PRO B 1 62  ? 1.538   -16.458 12.084  1.000 9.243  ? 62  PRO BBB CA  1 
ATOM   1595 C  C   . PRO B 1 62  ? 1.819   -15.696 13.370  1.000 8.713  ? 62  PRO BBB C   1 
ATOM   1596 O  O   . PRO B 1 62  ? 2.041   -14.509 13.421  1.000 8.544  ? 62  PRO BBB O   1 
ATOM   1597 C  CB  . PRO B 1 62  ? 2.631   -17.459 11.734  1.000 11.251 ? 62  PRO BBB CB  1 
ATOM   1598 C  CG  . PRO B 1 62  ? 3.663   -16.659 11.013  1.000 11.300 ? 62  PRO BBB CG  1 
ATOM   1599 C  CD  . PRO B 1 62  ? 2.895   -15.641 10.199  1.000 9.859  ? 62  PRO BBB CD  1 
ATOM   1600 N  N   . HIS B 1 63  ? 1.758   -16.394 14.481  1.000 8.539  ? 63  HIS BBB N   1 
ATOM   1601 C  CA  . HIS B 1 63  ? 2.093   -15.817 15.797  1.000 8.301  ? 63  HIS BBB CA  1 
ATOM   1602 C  C   . HIS B 1 63  ? 3.526   -15.315 15.768  1.000 8.020  ? 63  HIS BBB C   1 
ATOM   1603 O  O   . HIS B 1 63  ? 4.389   -15.932 15.179  1.000 8.955  ? 63  HIS BBB O   1 
ATOM   1604 C  CB  . HIS B 1 63  ? 1.938   -16.822 16.945  1.000 8.512  ? 63  HIS BBB CB  1 
ATOM   1605 C  CG  . HIS B 1 63  ? 0.539   -17.300 17.138  1.000 9.463  ? 63  HIS BBB CG  1 
ATOM   1606 N  ND1 . HIS B 1 63  ? 0.182   -18.250 18.099  1.000 8.677  ? 63  HIS BBB ND1 1 
ATOM   1607 C  CD2 . HIS B 1 63  ? -0.608  -16.959 16.483  1.000 12.160 ? 63  HIS BBB CD2 1 
ATOM   1608 C  CE1 . HIS B 1 63  ? -1.111  -18.477 17.984  1.000 9.415  ? 63  HIS BBB CE1 1 
ATOM   1609 N  NE2 . HIS B 1 63  ? -1.631  -17.698 17.010  1.000 11.474 ? 63  HIS BBB NE2 1 
ATOM   1610 N  N   . PHE B 1 64  ? 3.765   -14.191 16.421  1.000 7.384  ? 64  PHE BBB N   1 
ATOM   1611 C  CA  . PHE B 1 64  ? 5.121   -13.600 16.543  1.000 7.398  ? 64  PHE BBB CA  1 
ATOM   1612 C  C   . PHE B 1 64  ? 5.998   -14.560 17.338  1.000 7.695  ? 64  PHE BBB C   1 
ATOM   1613 O  O   . PHE B 1 64  ? 5.696   -14.865 18.493  1.000 7.804  ? 64  PHE BBB O   1 
ATOM   1614 C  CB  . PHE B 1 64  ? 5.006   -12.225 17.199  1.000 8.346  ? 64  PHE BBB CB  1 
ATOM   1615 C  CG  . PHE B 1 64  ? 6.320   -11.530 17.393  1.000 9.688  ? 64  PHE BBB CG  1 
ATOM   1616 C  CD1 . PHE B 1 64  ? 7.274   -11.453 16.400  1.000 11.187 ? 64  PHE BBB CD1 1 
ATOM   1617 C  CD2 . PHE B 1 64  ? 6.576   -10.895 18.600  1.000 11.088 ? 64  PHE BBB CD2 1 
ATOM   1618 C  CE1 . PHE B 1 64  ? 8.472   -10.784 16.623  1.000 12.428 ? 64  PHE BBB CE1 1 
ATOM   1619 C  CE2 . PHE B 1 64  ? 7.777   -10.223 18.821  1.000 12.593 ? 64  PHE BBB CE2 1 
ATOM   1620 C  CZ  . PHE B 1 64  ? 8.718   -10.179 17.827  1.000 13.501 ? 64  PHE BBB CZ  1 
ATOM   1621 N  N   . ASN B 1 65  ? 7.017   -15.082 16.673  1.000 8.259  ? 65  ASN BBB N   1 
ATOM   1622 C  CA  . ASN B 1 65  ? 7.797   -16.229 17.186  1.000 8.400  ? 65  ASN BBB CA  1 
ATOM   1623 C  C   . ASN B 1 65  ? 9.268   -16.060 16.873  1.000 9.114  ? 65  ASN BBB C   1 
ATOM   1624 O  O   . ASN B 1 65  ? 9.858   -16.944 16.240  1.000 10.668 ? 65  ASN BBB O   1 
ATOM   1625 C  CB  . ASN B 1 65  ? 7.259   -17.525 16.593  1.000 8.486  ? 65  ASN BBB CB  1 
ATOM   1626 C  CG  . ASN B 1 65  ? 7.878   -18.781 17.191  1.000 9.275  ? 65  ASN BBB CG  1 
ATOM   1627 O  OD1 . ASN B 1 65  ? 8.388   -18.760 18.320  1.000 9.387  ? 65  ASN BBB OD1 1 
ATOM   1628 N  ND2 . ASN B 1 65  ? 7.806   -19.909 16.484  1.000 9.948  ? 65  ASN BBB ND2 1 
ATOM   1629 N  N   . PRO B 1 66  ? 9.928   -14.983 17.346  1.000 10.031 ? 66  PRO BBB N   1 
ATOM   1630 C  CA  . PRO B 1 66  ? 11.328  -14.781 16.975  1.000 11.670 ? 66  PRO BBB CA  1 
ATOM   1631 C  C   . PRO B 1 66  ? 12.266  -15.841 17.525  1.000 12.931 ? 66  PRO BBB C   1 
ATOM   1632 O  O   . PRO B 1 66  ? 13.380  -15.956 16.952  1.000 15.366 ? 66  PRO BBB O   1 
ATOM   1633 C  CB  . PRO B 1 66  ? 11.632  -13.411 17.559  1.000 12.351 ? 66  PRO BBB CB  1 
ATOM   1634 C  CG  . PRO B 1 66  ? 10.680  -13.295 18.722  1.000 11.092 ? 66  PRO BBB CG  1 
ATOM   1635 C  CD  . PRO B 1 66  ? 9.392   -13.925 18.213  1.000 9.995  ? 66  PRO BBB CD  1 
ATOM   1636 N  N   . LEU B 1 67  ? 11.894  -16.589 18.555  1.000 13.009 ? 67  LEU BBB N   1 
ATOM   1637 C  CA  . LEU B 1 67  ? 12.772  -17.602 19.187  1.000 13.881 ? 67  LEU BBB CA  1 
ATOM   1638 C  C   . LEU B 1 67  ? 12.435  -19.007 18.705  1.000 13.520 ? 67  LEU BBB C   1 
ATOM   1639 O  O   . LEU B 1 67  ? 12.993  -19.977 19.241  1.000 14.927 ? 67  LEU BBB O   1 
ATOM   1640 C  CB  . LEU B 1 67  ? 12.673  -17.471 20.709  1.000 15.373 ? 67  LEU BBB CB  1 
ATOM   1641 C  CG  . LEU B 1 67  ? 13.004  -16.086 21.273  1.000 19.532 ? 67  LEU BBB CG  1 
ATOM   1642 C  CD1 . LEU B 1 67  ? 12.990  -16.106 22.801  1.000 21.893 ? 67  LEU BBB CD1 1 
ATOM   1643 C  CD2 . LEU B 1 67  ? 14.302  -15.536 20.728  1.000 22.922 ? 67  LEU BBB CD2 1 
ATOM   1644 N  N   . SER B 1 68  ? 11.571  -19.172 17.690  1.000 12.734 ? 68  SER BBB N   1 
ATOM   1645 C  CA  . SER B 1 68  ? 11.356  -20.480 17.016  1.000 13.410 ? 68  SER BBB CA  1 
ATOM   1646 C  C   . SER B 1 68  ? 10.907  -21.536 18.022  1.000 12.807 ? 68  SER BBB C   1 
ATOM   1647 O  O   . SER B 1 68  ? 11.465  -22.645 18.049  1.000 15.772 ? 68  SER BBB O   1 
ATOM   1648 C  CB  . SER B 1 68  ? 12.605  -20.920 16.271  1.000 13.765 ? 68  SER BBB CB  1 
ATOM   1649 O  OG  . SER B 1 68  ? 12.970  -19.982 15.293  1.000 16.523 ? 68  SER BBB OG  1 
ATOM   1650 N  N   . ARG B 1 69  ? 9.924   -21.200 18.843  1.000 11.989 ? 69  ARG BBB N   1 
ATOM   1651 C  CA  . ARG B 1 69  ? 9.329   -22.118 19.823  1.000 12.318 ? 69  ARG BBB CA  1 
ATOM   1652 C  C   . ARG B 1 69  ? 7.991   -22.638 19.325  1.000 11.302 ? 69  ARG BBB C   1 
ATOM   1653 O  O   . ARG B 1 69  ? 7.451   -22.152 18.321  1.000 12.094 ? 69  ARG BBB O   1 
ATOM   1654 C  CB  . ARG B 1 69  ? 9.111   -21.387 21.151  1.000 13.561 ? 69  ARG BBB CB  1 
ATOM   1655 C  CG  . ARG B 1 69  ? 10.366  -20.751 21.713  1.000 17.143 ? 69  ARG BBB CG  1 
ATOM   1656 C  CD  . ARG B 1 69  ? 11.483  -21.748 21.859  1.000 19.889 ? 69  ARG BBB CD  1 
ATOM   1657 N  NE  . ARG B 1 69  ? 11.141  -22.900 22.678  1.000 21.711 ? 69  ARG BBB NE  1 
ATOM   1658 C  CZ  . ARG B 1 69  ? 11.094  -22.899 24.005  1.000 20.333 ? 69  ARG BBB CZ  1 
ATOM   1659 N  NH1 . ARG B 1 69  ? 11.384  -21.785 24.665  1.000 22.386 ? 69  ARG BBB NH1 1 
ATOM   1660 N  NH2 . ARG B 1 69  ? 10.775  -24.012 24.640  1.000 21.962 ? 69  ARG BBB NH2 1 
ATOM   1661 N  N   . LYS B 1 70  ? 7.449   -23.611 20.021  1.000 11.997 ? 70  LYS BBB N   1 
ATOM   1662 C  CA  . LYS B 1 70  ? 6.073   -24.060 19.808  1.000 12.820 ? 70  LYS BBB CA  1 
ATOM   1663 C  C   . LYS B 1 70  ? 5.094   -23.137 20.557  1.000 10.797 ? 70  LYS BBB C   1 
ATOM   1664 O  O   . LYS B 1 70  ? 5.475   -22.416 21.471  1.000 10.310 ? 70  LYS BBB O   1 
ATOM   1665 C  CB  . LYS B 1 70  ? 5.946   -25.503 20.312  1.000 14.303 ? 70  LYS BBB CB  1 
ATOM   1666 C  CG  . LYS B 1 70  ? 6.759   -26.533 19.531  1.000 19.434 ? 70  LYS BBB CG  1 
ATOM   1667 C  CD  . LYS B 1 70  ? 6.470   -27.952 20.000  1.000 24.879 ? 70  LYS BBB CD  1 
ATOM   1668 C  CE  . LYS B 1 70  ? 7.088   -29.034 19.135  1.000 29.355 ? 70  LYS BBB CE  1 
ATOM   1669 N  NZ  . LYS B 1 70  ? 8.569   -28.968 19.135  1.000 32.112 ? 70  LYS BBB NZ  1 
ATOM   1670 N  N   . HIS B 1 71  ? 3.848   -23.218 20.149  1.000 9.788  ? 71  HIS BBB N   1 
ATOM   1671 C  CA  . HIS B 1 71  ? 2.733   -22.460 20.737  1.000 8.929  ? 71  HIS BBB CA  1 
ATOM   1672 C  C   . HIS B 1 71  ? 2.500   -22.917 22.181  1.000 9.501  ? 71  HIS BBB C   1 
ATOM   1673 O  O   . HIS B 1 71  ? 2.441   -24.123 22.446  1.000 10.237 ? 71  HIS BBB O   1 
ATOM   1674 C  CB  . HIS B 1 71  ? 1.472   -22.647 19.904  1.000 7.997  ? 71  HIS BBB CB  1 
ATOM   1675 C  CG  . HIS B 1 71  ? 0.326   -21.855 20.439  1.000 8.215  ? 71  HIS BBB CG  1 
ATOM   1676 N  ND1 . HIS B 1 71  ? 0.216   -20.500 20.318  1.000 7.444  ? 71  HIS BBB ND1 1 
ATOM   1677 C  CD2 . HIS B 1 71  ? -0.741  -22.278 21.125  1.000 8.117  ? 71  HIS BBB CD2 1 
ATOM   1678 C  CE1 . HIS B 1 71  ? -0.843  -20.099 20.962  1.000 7.474  ? 71  HIS BBB CE1 1 
ATOM   1679 N  NE2 . HIS B 1 71  ? -1.484  -21.205 21.446  1.000 7.693  ? 71  HIS BBB NE2 1 
ATOM   1680 N  N   . GLY B 1 72  ? 2.222   -21.980 23.058  1.000 8.953  ? 72  GLY BBB N   1 
ATOM   1681 C  CA  . GLY B 1 72  ? 1.803   -22.293 24.430  1.000 9.299  ? 72  GLY BBB CA  1 
ATOM   1682 C  C   . GLY B 1 72  ? 0.948   -21.203 25.022  1.000 9.331  ? 72  GLY BBB C   1 
ATOM   1683 O  O   . GLY B 1 72  ? 0.436   -20.325 24.297  1.000 9.365  ? 72  GLY BBB O   1 
ATOM   1684 N  N   . GLY B 1 73  ? 0.745   -21.280 26.316  1.000 10.053 ? 73  GLY BBB N   1 
ATOM   1685 C  CA  . GLY B 1 73  ? 0.089   -20.204 27.060  1.000 10.280 ? 73  GLY BBB CA  1 
ATOM   1686 C  C   . GLY B 1 73  ? 1.093   -19.230 27.637  1.000 9.698  ? 73  GLY BBB C   1 
ATOM   1687 O  O   . GLY B 1 73  ? 2.307   -19.479 27.694  1.000 10.094 ? 73  GLY BBB O   1 
ATOM   1688 N  N   . PRO B 1 74  ? 0.629   -18.062 28.126  1.000 10.111 ? 74  PRO BBB N   1 
ATOM   1689 C  CA  . PRO B 1 74  ? 1.537   -17.006 28.531  1.000 10.344 ? 74  PRO BBB CA  1 
ATOM   1690 C  C   . PRO B 1 74  ? 2.401   -17.366 29.741  1.000 10.768 ? 74  PRO BBB C   1 
ATOM   1691 O  O   . PRO B 1 74  ? 3.463   -16.824 29.905  1.000 12.638 ? 74  PRO BBB O   1 
ATOM   1692 C  CB  . PRO B 1 74  ? 0.581   -15.824 28.775  1.000 11.052 ? 74  PRO BBB CB  1 
ATOM   1693 C  CG  . PRO B 1 74  ? -0.789  -16.445 28.953  1.000 11.021 ? 74  PRO BBB CG  1 
ATOM   1694 C  CD  . PRO B 1 74  ? -0.789  -17.676 28.106  1.000 10.376 ? 74  PRO BBB CD  1 
ATOM   1695 N  N   . LYS B 1 75  ? 1.915   -18.296 30.531  1.000 11.978 ? 75  LYS BBB N   1 
ATOM   1696 C  CA  . LYS B 1 75  ? 2.638   -18.692 31.760  1.000 14.945 ? 75  LYS BBB CA  1 
ATOM   1697 C  C   . LYS B 1 75  ? 3.503   -19.909 31.499  1.000 14.651 ? 75  LYS BBB C   1 
ATOM   1698 O  O   . LYS B 1 75  ? 4.169   -20.382 32.429  1.000 15.770 ? 75  LYS BBB O   1 
ATOM   1699 C  CB  . LYS B 1 75  ? 1.660   -18.847 32.922  1.000 18.338 ? 75  LYS BBB CB  1 
ATOM   1700 C  CG  . LYS B 1 75  ? 0.970   -17.531 33.287  1.000 22.493 ? 75  LYS BBB CG  1 
ATOM   1701 C  CD  . LYS B 1 75  ? 1.888   -16.322 33.395  1.000 27.518 ? 75  LYS BBB CD  1 
ATOM   1702 C  CE  . LYS B 1 75  ? 1.161   -14.999 33.575  1.000 31.548 ? 75  LYS BBB CE  1 
ATOM   1703 N  NZ  . LYS B 1 75  ? 2.132   -13.888 33.714  1.000 33.091 ? 75  LYS BBB NZ  1 
ATOM   1704 N  N   . ASP B 1 76  ? 3.638   -20.364 30.276  1.000 12.692 ? 76  ASP BBB N   1 
ATOM   1705 C  CA  . ASP B 1 76  ? 4.523   -21.503 29.900  1.000 12.608 ? 76  ASP BBB CA  1 
ATOM   1706 C  C   . ASP B 1 76  ? 5.903   -21.007 29.508  1.000 12.635 ? 76  ASP BBB C   1 
ATOM   1707 O  O   . ASP B 1 76  ? 6.028   -19.931 28.902  1.000 14.404 ? 76  ASP BBB O   1 
ATOM   1708 C  CB  . ASP B 1 76  ? 3.934   -22.277 28.725  1.000 12.424 ? 76  ASP BBB CB  1 
ATOM   1709 C  CG  . ASP B 1 76  ? 2.657   -22.994 29.056  1.000 14.106 ? 76  ASP BBB CG  1 
ATOM   1710 O  OD1 . ASP B 1 76  ? 2.418   -23.273 30.278  1.000 17.158 ? 76  ASP BBB OD1 1 
ATOM   1711 O  OD2 . ASP B 1 76  ? 1.854   -23.216 28.137  1.000 14.078 ? 76  ASP BBB OD2 1 
ATOM   1712 N  N   . GLU B 1 77  ? 6.938   -21.813 29.724  1.000 12.896 ? 77  GLU BBB N   1 
ATOM   1713 C  CA  . GLU B 1 77  ? 8.267   -21.571 29.119  1.000 13.702 ? 77  GLU BBB CA  1 
ATOM   1714 C  C   . GLU B 1 77  ? 8.141   -21.731 27.603  1.000 11.859 ? 77  GLU BBB C   1 
ATOM   1715 O  O   . GLU B 1 77  ? 8.728   -20.933 26.850  1.000 11.715 ? 77  GLU BBB O   1 
ATOM   1716 C  CB  . GLU B 1 77  ? 9.296   -22.540 29.687  1.000 14.843 ? 77  GLU BBB CB  1 
ATOM   1717 C  CG  . GLU B 1 77  ? 10.707  -22.188 29.266  1.000 16.822 ? 77  GLU BBB CG  1 
ATOM   1718 C  CD  . GLU B 1 77  ? 11.154  -22.702 27.922  1.000 17.775 ? 77  GLU BBB CD  1 
ATOM   1719 O  OE1 . GLU B 1 77  ? 10.576  -23.704 27.480  1.000 21.664 ? 77  GLU BBB OE1 1 
ATOM   1720 O  OE2 . GLU B 1 77  ? 12.051  -22.092 27.337  1.000 22.965 ? 77  GLU BBB OE2 1 
ATOM   1721 N  N   . GLU B 1 78  ? 7.523   -22.817 27.181  1.000 11.472 ? 78  GLU BBB N   1 
ATOM   1722 C  CA  . GLU B 1 78  ? 7.394   -23.141 25.734  1.000 11.280 ? 78  GLU BBB CA  1 
ATOM   1723 C  C   . GLU B 1 78  ? 6.193   -22.356 25.196  1.000 9.543  ? 78  GLU BBB C   1 
ATOM   1724 O  O   . GLU B 1 78  ? 5.083   -22.809 25.301  1.000 11.309 ? 78  GLU BBB O   1 
ATOM   1725 C  CB  . GLU B 1 78  ? 7.263   -24.637 25.521  1.000 12.258 ? 78  GLU BBB CB  1 
ATOM   1726 C  CG  . GLU B 1 78  ? 7.338   -25.041 24.052  1.000 15.068 ? 78  GLU BBB CG  1 
ATOM   1727 C  CD  . GLU B 1 78  ? 7.334   -26.533 23.738  0.500 18.143 ? 78  GLU BBB CD  1 
ATOM   1728 O  OE1 . GLU B 1 78  ? 7.095   -27.335 24.659  0.500 25.466 ? 78  GLU BBB OE1 1 
ATOM   1729 O  OE2 . GLU B 1 78  ? 7.583   -26.897 22.581  0.500 24.061 ? 78  GLU BBB OE2 1 
ATOM   1730 N  N   . ARG B 1 79  ? 6.489   -21.208 24.582  1.000 8.691  ? 79  ARG BBB N   1 
ATOM   1731 C  CA  . ARG B 1 79  ? 5.456   -20.328 23.998  1.000 7.923  ? 79  ARG BBB CA  1 
ATOM   1732 C  C   . ARG B 1 79  ? 6.133   -19.518 22.919  1.000 8.341  ? 79  ARG BBB C   1 
ATOM   1733 O  O   . ARG B 1 79  ? 7.333   -19.309 22.943  1.000 9.081  ? 79  ARG BBB O   1 
ATOM   1734 C  CB  . ARG B 1 79  ? 4.829   -19.437 25.058  1.000 7.696  ? 79  ARG BBB CB  1 
ATOM   1735 C  CG  . ARG B 1 79  ? 5.809   -18.526 25.758  1.000 8.568  ? 79  ARG BBB CG  1 
ATOM   1736 C  CD  . ARG B 1 79  ? 5.179   -17.510 26.678  1.000 8.888  ? 79  ARG BBB CD  1 
ATOM   1737 N  NE  . ARG B 1 79  ? 4.777   -16.312 25.928  1.000 8.826  ? 79  ARG BBB NE  1 
ATOM   1738 C  CZ  . ARG B 1 79  ? 4.384   -15.178 26.493  1.000 8.982  ? 79  ARG BBB CZ  1 
ATOM   1739 N  NH1 . ARG B 1 79  ? 4.174   -14.090 25.770  1.000 8.642  ? 79  ARG BBB NH1 1 
ATOM   1740 N  NH2 . ARG B 1 79  ? 4.220   -15.116 27.808  1.000 9.972  ? 79  ARG BBB NH2 1 
ATOM   1741 N  N   . HIS B 1 80  ? 5.329   -19.009 22.038  1.000 8.022  ? 80  HIS BBB N   1 
ATOM   1742 C  CA  . HIS B 1 80  ? 5.696   -17.901 21.159  1.000 7.792  ? 80  HIS BBB CA  1 
ATOM   1743 C  C   . HIS B 1 80  ? 5.759   -16.613 21.977  1.000 7.064  ? 80  HIS BBB C   1 
ATOM   1744 O  O   . HIS B 1 80  ? 4.970   -16.449 22.890  1.000 7.636  ? 80  HIS BBB O   1 
ATOM   1745 C  CB  . HIS B 1 80  ? 4.669   -17.773 20.045  1.000 7.506  ? 80  HIS BBB CB  1 
ATOM   1746 C  CG  . HIS B 1 80  ? 4.470   -19.006 19.226  1.000 7.993  ? 80  HIS BBB CG  1 
ATOM   1747 N  ND1 . HIS B 1 80  ? 3.236   -19.374 18.733  1.000 7.423  ? 80  HIS BBB ND1 1 
ATOM   1748 C  CD2 . HIS B 1 80  ? 5.366   -19.891 18.732  1.000 9.313  ? 80  HIS BBB CD2 1 
ATOM   1749 C  CE1 . HIS B 1 80  ? 3.384   -20.454 17.991  1.000 8.336  ? 80  HIS BBB CE1 1 
ATOM   1750 N  NE2 . HIS B 1 80  ? 4.668   -20.771 17.949  1.000 8.517  ? 80  HIS BBB NE2 1 
ATOM   1751 N  N   . VAL B 1 81  ? 6.587   -15.676 21.565  1.000 7.368  ? 81  VAL BBB N   1 
ATOM   1752 C  CA  . VAL B 1 81  ? 6.558   -14.356 22.221  1.000 7.796  ? 81  VAL BBB CA  1 
ATOM   1753 C  C   . VAL B 1 81  ? 5.144   -13.795 22.146  1.000 7.595  ? 81  VAL BBB C   1 
ATOM   1754 O  O   . VAL B 1 81  ? 4.684   -13.203 23.139  1.000 7.884  ? 81  VAL BBB O   1 
ATOM   1755 C  CB  . VAL B 1 81  ? 7.582   -13.389 21.619  1.000 8.856  ? 81  VAL BBB CB  1 
ATOM   1756 C  CG1 . VAL B 1 81  ? 7.373   -11.948 22.107  1.000 8.798  ? 81  VAL BBB CG1 1 
ATOM   1757 C  CG2 . VAL B 1 81  ? 8.992   -13.850 21.962  1.000 9.221  ? 81  VAL BBB CG2 1 
ATOM   1758 N  N   . GLY B 1 82  ? 4.443   -13.971 21.037  1.000 7.436  ? 82  GLY BBB N   1 
ATOM   1759 C  CA  . GLY B 1 82  ? 3.101   -13.417 20.889  1.000 7.802  ? 82  GLY BBB CA  1 
ATOM   1760 C  C   . GLY B 1 82  ? 1.984   -14.104 21.627  1.000 8.027  ? 82  GLY BBB C   1 
ATOM   1761 O  O   . GLY B 1 82  ? 0.831   -13.684 21.454  1.000 8.104  ? 82  GLY BBB O   1 
ATOM   1762 N  N   . ASP B 1 83  ? 2.250   -15.138 22.408  1.000 8.064  ? 83  ASP BBB N   1 
ATOM   1763 C  CA  . ASP B 1 83  ? 1.186   -15.956 23.056  1.000 8.002  ? 83  ASP BBB CA  1 
ATOM   1764 C  C   . ASP B 1 83  ? 0.657   -15.320 24.335  1.000 8.579  ? 83  ASP BBB C   1 
ATOM   1765 O  O   . ASP B 1 83  ? 1.242   -15.536 25.389  1.000 10.144 ? 83  ASP BBB O   1 
ATOM   1766 C  CB  . ASP B 1 83  ? 1.693   -17.376 23.273  1.000 8.087  ? 83  ASP BBB CB  1 
ATOM   1767 C  CG  . ASP B 1 83  ? 1.891   -18.136 22.009  1.000 7.999  ? 83  ASP BBB CG  1 
ATOM   1768 O  OD1 . ASP B 1 83  ? 1.326   -17.678 21.005  1.000 7.137  ? 83  ASP BBB OD1 1 
ATOM   1769 O  OD2 . ASP B 1 83  ? 2.552   -19.225 22.090  1.000 8.239  ? 83  ASP BBB OD2 1 
ATOM   1770 N  N   . LEU B 1 84  ? -0.391  -14.526 24.212  1.000 7.833  ? 84  LEU BBB N   1 
ATOM   1771 C  CA  . LEU B 1 84  ? -1.007  -13.839 25.368  1.000 8.570  ? 84  LEU BBB CA  1 
ATOM   1772 C  C   . LEU B 1 84  ? -2.248  -14.589 25.840  1.000 8.987  ? 84  LEU BBB C   1 
ATOM   1773 O  O   . LEU B 1 84  ? -3.027  -14.029 26.652  1.000 11.388 ? 84  LEU BBB O   1 
ATOM   1774 C  CB  . LEU B 1 84  ? -1.281  -12.381 25.004  1.000 8.950  ? 84  LEU BBB CB  1 
ATOM   1775 C  CG  . LEU B 1 84  ? -0.029  -11.543 24.719  1.000 9.629  ? 84  LEU BBB CG  1 
ATOM   1776 C  CD1 . LEU B 1 84  ? -0.416  -10.113 24.418  1.000 9.591  ? 84  LEU BBB CD1 1 
ATOM   1777 C  CD2 . LEU B 1 84  ? 0.956   -11.593 25.902  1.000 11.797 ? 84  LEU BBB CD2 1 
ATOM   1778 N  N   . GLY B 1 85  ? -2.470  -15.810 25.438  1.000 8.391  ? 85  GLY BBB N   1 
ATOM   1779 C  CA  . GLY B 1 85  ? -3.526  -16.642 26.008  1.000 8.875  ? 85  GLY BBB CA  1 
ATOM   1780 C  C   . GLY B 1 85  ? -4.899  -16.284 25.477  1.000 9.006  ? 85  GLY BBB C   1 
ATOM   1781 O  O   . GLY B 1 85  ? -5.105  -16.209 24.260  1.000 9.615  ? 85  GLY BBB O   1 
ATOM   1782 N  N   . ASN B 1 86  ? -5.854  -16.194 26.392  1.000 9.302  ? 86  ASN BBB N   1 
ATOM   1783 C  CA  . ASN B 1 86  ? -7.255  -15.854 26.078  1.000 8.350  ? 86  ASN BBB CA  1 
ATOM   1784 C  C   . ASN B 1 86  ? -7.695  -14.608 26.828  1.000 8.430  ? 86  ASN BBB C   1 
ATOM   1785 O  O   . ASN B 1 86  ? -7.253  -14.408 27.944  1.000 11.151 ? 86  ASN BBB O   1 
ATOM   1786 C  CB  . ASN B 1 86  ? -8.189  -16.991 26.481  1.000 9.037  ? 86  ASN BBB CB  1 
ATOM   1787 C  CG  . ASN B 1 86  ? -8.009  -18.223 25.636  1.000 10.049 ? 86  ASN BBB CG  1 
ATOM   1788 O  OD1 . ASN B 1 86  ? -8.395  -18.228 24.472  1.000 9.986  ? 86  ASN BBB OD1 1 
ATOM   1789 N  ND2 . ASN B 1 86  ? -7.430  -19.254 26.241  1.000 11.135 ? 86  ASN BBB ND2 1 
ATOM   1790 N  N   . VAL B 1 87  ? -8.576  -13.867 26.192  1.000 8.870  ? 87  VAL BBB N   1 
ATOM   1791 C  CA  . VAL B 1 87  ? -9.408  -12.898 26.936  1.000 9.311  ? 87  VAL BBB CA  1 
ATOM   1792 C  C   . VAL B 1 87  ? -10.741 -13.591 27.175  1.000 9.747  ? 87  VAL BBB C   1 
ATOM   1793 O  O   . VAL B 1 87  ? -11.102 -14.507 26.445  1.000 10.554 ? 87  VAL BBB O   1 
ATOM   1794 C  CB  . VAL B 1 87  ? -9.515  -11.562 26.175  1.000 10.140 ? 87  VAL BBB CB  1 
ATOM   1795 C  CG1 . VAL B 1 87  ? -8.146  -10.941 26.015  1.000 10.798 ? 87  VAL BBB CG1 1 
ATOM   1796 C  CG2 . VAL B 1 87  ? -10.182 -11.685 24.852  1.000 11.126 ? 87  VAL BBB CG2 1 
ATOM   1797 N  N   . THR B 1 88  ? -11.488 -13.068 28.150  1.000 9.930  ? 88  THR BBB N   1 
ATOM   1798 C  CA  . THR B 1 88  ? -12.809 -13.622 28.493  1.000 10.708 ? 88  THR BBB CA  1 
ATOM   1799 C  C   . THR B 1 88  ? -13.876 -12.544 28.306  1.000 10.928 ? 88  THR BBB C   1 
ATOM   1800 O  O   . THR B 1 88  ? -13.817 -11.508 28.987  1.000 12.193 ? 88  THR BBB O   1 
ATOM   1801 C  CB  . THR B 1 88  ? -12.885 -14.131 29.922  1.000 11.837 ? 88  THR BBB CB  1 
ATOM   1802 O  OG1 . THR B 1 88  ? -11.898 -15.129 30.075  1.000 14.508 ? 88  THR BBB OG1 1 
ATOM   1803 C  CG2 . THR B 1 88  ? -14.242 -14.723 30.230  1.000 14.134 ? 88  THR BBB CG2 1 
ATOM   1804 N  N   . ALA B 1 89  ? -14.799 -12.822 27.411  1.000 11.404 ? 89  ALA BBB N   1 
ATOM   1805 C  CA  . ALA B 1 89  ? -15.956 -11.941 27.215  1.000 11.883 ? 89  ALA BBB CA  1 
ATOM   1806 C  C   . ALA B 1 89  ? -17.068 -12.358 28.179  1.000 13.661 ? 89  ALA BBB C   1 
ATOM   1807 O  O   . ALA B 1 89  ? -17.393 -13.540 28.254  1.000 15.090 ? 89  ALA BBB O   1 
ATOM   1808 C  CB  . ALA B 1 89  ? -16.403 -11.968 25.806  1.000 12.223 ? 89  ALA BBB CB  1 
ATOM   1809 N  N   . ASP B 1 90  ? -17.712 -11.334 28.729  1.000 15.901 ? 90  ASP BBB N   1 
ATOM   1810 C  CA  . ASP B 1 90  ? -18.760 -11.519 29.754  1.000 16.061 ? 90  ASP BBB CA  1 
ATOM   1811 C  C   . ASP B 1 90  ? -20.059 -11.772 29.000  1.000 14.996 ? 90  ASP BBB C   1 
ATOM   1812 O  O   . ASP B 1 90  ? -20.116 -11.889 27.772  1.000 15.011 ? 90  ASP BBB O   1 
ATOM   1813 C  CB  . ASP B 1 90  ? -18.740 -10.345 30.730  1.000 16.730 ? 90  ASP BBB CB  1 
ATOM   1814 C  CG  . ASP B 1 90  ? -19.240 -9.013  30.166  1.000 16.186 ? 90  ASP BBB CG  1 
ATOM   1815 O  OD1 . ASP B 1 90  ? -19.842 -8.989  29.078  1.000 16.020 ? 90  ASP BBB OD1 1 
ATOM   1816 O  OD2 . ASP B 1 90  ? -18.988 -8.008  30.819  1.000 19.053 ? 90  ASP BBB OD2 1 
ATOM   1817 N  N   . LYS B 1 91  ? -21.157 -11.877 29.765  1.000 15.703 ? 91  LYS BBB N   1 
ATOM   1818 C  CA  . LYS B 1 91  ? -22.473 -12.191 29.175  1.000 15.955 ? 91  LYS BBB CA  1 
ATOM   1819 C  C   . LYS B 1 91  ? -22.949 -11.093 28.209  1.000 14.425 ? 91  LYS BBB C   1 
ATOM   1820 O  O   . LYS B 1 91  ? -23.811 -11.355 27.379  1.000 16.843 ? 91  LYS BBB O   1 
ATOM   1821 C  CB  . LYS B 1 91  ? -23.507 -12.331 30.294  1.000 16.138 ? 91  LYS BBB CB  1 
ATOM   1822 C  CG  . LYS B 1 91  ? -23.648 -11.069 31.136  1.000 16.001 ? 91  LYS BBB CG  1 
ATOM   1823 C  CD  . LYS B 1 91  ? -24.548 -11.258 32.332  1.000 16.563 ? 91  LYS BBB CD  1 
ATOM   1824 C  CE  . LYS B 1 91  ? -24.794 -9.963  33.086  1.000 17.034 ? 91  LYS BBB CE  1 
ATOM   1825 N  NZ  . LYS B 1 91  ? -25.491 -8.963  32.238  1.000 18.146 ? 91  LYS BBB NZ  1 
ATOM   1826 N  N   . ASP B 1 92  ? -22.350 -9.895  28.290  1.000 13.444 ? 92  ASP BBB N   1 
ATOM   1827 C  CA  . ASP B 1 92  ? -22.689 -8.715  27.453  1.000 14.308 ? 92  ASP BBB CA  1 
ATOM   1828 C  C   . ASP B 1 92  ? -21.679 -8.560  26.325  1.000 14.235 ? 92  ASP BBB C   1 
ATOM   1829 O  O   . ASP B 1 92  ? -21.741 -7.507  25.634  1.000 16.747 ? 92  ASP BBB O   1 
ATOM   1830 C  CB  . ASP B 1 92  ? -22.796 -7.474  28.318  1.000 13.579 ? 92  ASP BBB CB  1 
ATOM   1831 C  CG  . ASP B 1 92  ? -23.837 -7.712  29.404  1.000 14.221 ? 92  ASP BBB CG  1 
ATOM   1832 O  OD1 . ASP B 1 92  ? -24.921 -8.158  29.009  1.000 16.989 ? 92  ASP BBB OD1 1 
ATOM   1833 O  OD2 . ASP B 1 92  ? -23.536 -7.511  30.611  1.000 17.509 ? 92  ASP BBB OD2 1 
ATOM   1834 N  N   . GLY B 1 93  ? -20.815 -9.550  26.106  1.000 13.953 ? 93  GLY BBB N   1 
ATOM   1835 C  CA  . GLY B 1 93  ? -19.851 -9.534  24.981  1.000 13.181 ? 93  GLY BBB CA  1 
ATOM   1836 C  C   . GLY B 1 93  ? -18.665 -8.627  25.223  1.000 12.083 ? 93  GLY BBB C   1 
ATOM   1837 O  O   . GLY B 1 93  ? -17.904 -8.351  24.219  1.000 12.811 ? 93  GLY BBB O   1 
ATOM   1838 N  N   . VAL B 1 94  ? -18.408 -8.250  26.453  1.000 11.647 ? 94  VAL BBB N   1 
ATOM   1839 C  CA  . VAL B 1 94  ? -17.307 -7.335  26.814  1.000 12.134 ? 94  VAL BBB CA  1 
ATOM   1840 C  C   . VAL B 1 94  ? -16.212 -8.146  27.487  1.000 12.867 ? 94  VAL BBB C   1 
ATOM   1841 O  O   . VAL B 1 94  ? -16.475 -8.805  28.549  1.000 13.331 ? 94  VAL BBB O   1 
ATOM   1842 C  CB  . VAL B 1 94  ? -17.813 -6.227  27.741  1.000 13.627 ? 94  VAL BBB CB  1 
ATOM   1843 C  CG1 . VAL B 1 94  ? -16.686 -5.329  28.206  1.000 14.470 ? 94  VAL BBB CG1 1 
ATOM   1844 C  CG2 . VAL B 1 94  ? -18.936 -5.462  27.044  1.000 15.280 ? 94  VAL BBB CG2 1 
ATOM   1845 N  N   . ALA B 1 95  ? -15.008 -8.052  26.954  1.000 11.496 ? 95  ALA BBB N   1 
ATOM   1846 C  CA  . ALA B 1 95  ? -13.817 -8.586  27.619  1.000 11.423 ? 95  ALA BBB CA  1 
ATOM   1847 C  C   . ALA B 1 95  ? -13.064 -7.430  28.212  1.000 12.170 ? 95  ALA BBB C   1 
ATOM   1848 O  O   . ALA B 1 95  ? -12.497 -6.605  27.443  1.000 14.192 ? 95  ALA BBB O   1 
ATOM   1849 C  CB  . ALA B 1 95  ? -12.970 -9.328  26.639  1.000 11.193 ? 95  ALA BBB CB  1 
ATOM   1850 N  N   . ASP B 1 96  ? -13.013 -7.319  29.514  1.000 12.350 ? 96  ASP BBB N   1 
ATOM   1851 C  CA  . ASP B 1 96  ? -12.148 -6.345  30.188  1.000 14.092 ? 96  ASP BBB CA  1 
ATOM   1852 C  C   . ASP B 1 96  ? -10.790 -7.002  30.331  1.000 14.051 ? 96  ASP BBB C   1 
ATOM   1853 O  O   . ASP B 1 96  ? -10.682 -8.053  30.923  1.000 15.574 ? 96  ASP BBB O   1 
ATOM   1854 C  CB  . ASP B 1 96  ? -12.763 -5.923  31.517  1.000 15.815 ? 96  ASP BBB CB  1 
ATOM   1855 C  CG  . ASP B 1 96  ? -13.977 -5.043  31.257  1.000 21.573 ? 96  ASP BBB CG  1 
ATOM   1856 O  OD1 . ASP B 1 96  ? -13.841 -4.035  30.480  1.000 22.689 ? 96  ASP BBB OD1 1 
ATOM   1857 O  OD2 . ASP B 1 96  ? -15.079 -5.414  31.757  1.000 28.507 ? 96  ASP BBB OD2 1 
ATOM   1858 N  N   . VAL B 1 97  ? -9.793  -6.426  29.704  1.000 12.861 ? 97  VAL BBB N   1 
ATOM   1859 C  CA  . VAL B 1 97  ? -8.462  -7.062  29.619  1.000 13.266 ? 97  VAL BBB CA  1 
ATOM   1860 C  C   . VAL B 1 97  ? -7.607  -6.464  30.675  1.000 12.329 ? 97  VAL BBB C   1 
ATOM   1861 O  O   . VAL B 1 97  ? -7.499  -5.250  30.819  1.000 11.904 ? 97  VAL BBB O   1 
ATOM   1862 C  CB  . VAL B 1 97  ? -7.858  -6.907  28.230  1.000 13.334 ? 97  VAL BBB CB  1 
ATOM   1863 C  CG1 . VAL B 1 97  ? -6.445  -7.502  28.155  1.000 15.476 ? 97  VAL BBB CG1 1 
ATOM   1864 C  CG2 . VAL B 1 97  ? -8.764  -7.490  27.197  1.000 15.756 ? 97  VAL BBB CG2 1 
ATOM   1865 N  N   . SER B 1 98  ? -6.933  -7.372  31.340  1.000 14.003 ? 98  SER BBB N   1 
ATOM   1866 C  CA  . SER B 1 98  ? -6.003  -7.071  32.408  1.000 16.480 ? 98  SER BBB CA  1 
ATOM   1867 C  C   . SER B 1 98  ? -4.983  -8.199  32.480  1.000 16.757 ? 98  SER BBB C   1 
ATOM   1868 O  O   . SER B 1 98  ? -5.303  -9.288  32.975  1.000 19.710 ? 98  SER BBB O   1 
ATOM   1869 C  CB  . SER B 1 98  ? -6.753  -6.912  33.689  1.000 20.366 ? 98  SER BBB CB  1 
ATOM   1870 O  OG  . SER B 1 98  ? -5.884  -6.374  34.641  1.000 25.209 ? 98  SER BBB OG  1 
ATOM   1871 N  N   . ILE B 1 99  ? -3.809  -7.970  31.893  1.000 15.142 ? 99  ILE BBB N   1 
ATOM   1872 C  CA  . ILE B 1 99  ? -2.741  -8.992  31.746  1.000 15.057 ? 99  ILE BBB CA  1 
ATOM   1873 C  C   . ILE B 1 99  ? -1.457  -8.302  32.206  1.000 14.334 ? 99  ILE BBB C   1 
ATOM   1874 O  O   . ILE B 1 99  ? -1.243  -7.086  31.948  1.000 13.929 ? 99  ILE BBB O   1 
ATOM   1875 C  CB  . ILE B 1 99  ? -2.663  -9.485  30.287  1.000 14.330 ? 99  ILE BBB CB  1 
ATOM   1876 C  CG1 . ILE B 1 99  ? -3.860  -10.373 29.931  1.000 17.096 ? 99  ILE BBB CG1 1 
ATOM   1877 C  CG2 . ILE B 1 99  ? -1.346  -10.167 29.994  1.000 16.679 ? 99  ILE BBB CG2 1 
ATOM   1878 C  CD1 . ILE B 1 99  ? -3.978  -10.665 28.444  1.000 19.324 ? 99  ILE BBB CD1 1 
ATOM   1879 N  N   . GLU B 1 100 ? -0.577  -9.018  32.880  1.000 12.972 ? 100 GLU BBB N   1 
ATOM   1880 C  CA  . GLU B 1 100 ? 0.825   -8.602  33.040  1.000 13.009 ? 100 GLU BBB CA  1 
ATOM   1881 C  C   . GLU B 1 100 ? 1.635   -9.682  32.350  1.000 11.326 ? 100 GLU BBB C   1 
ATOM   1882 O  O   . GLU B 1 100 ? 1.372   -10.868 32.635  1.000 12.547 ? 100 GLU BBB O   1 
ATOM   1883 C  CB  . GLU B 1 100 ? 1.190   -8.483  34.521  1.000 17.279 ? 100 GLU BBB CB  1 
ATOM   1884 C  CG  . GLU B 1 100 ? 2.572   -7.934  34.726  1.000 23.239 ? 100 GLU BBB CG  1 
ATOM   1885 C  CD  . GLU B 1 100 ? 3.117   -7.867  36.143  1.000 28.902 ? 100 GLU BBB CD  1 
ATOM   1886 O  OE1 . GLU B 1 100 ? 2.727   -6.933  36.841  1.000 34.769 ? 100 GLU BBB OE1 1 
ATOM   1887 O  OE2 . GLU B 1 100 ? 3.991   -8.714  36.508  1.000 33.419 ? 100 GLU BBB OE2 1 
ATOM   1888 N  N   . ASP B 1 101 ? 2.553   -9.311  31.473  1.000 9.588  ? 101 ASP BBB N   1 
ATOM   1889 C  CA  . ASP B 1 101 ? 3.331   -10.335 30.729  1.000 9.752  ? 101 ASP BBB CA  1 
ATOM   1890 C  C   . ASP B 1 101 ? 4.807   -9.968  30.787  1.000 9.574  ? 101 ASP BBB C   1 
ATOM   1891 O  O   . ASP B 1 101 ? 5.178   -8.812  30.618  1.000 10.352 ? 101 ASP BBB O   1 
ATOM   1892 C  CB  . ASP B 1 101 ? 2.877   -10.525 29.279  1.000 8.798  ? 101 ASP BBB CB  1 
ATOM   1893 C  CG  . ASP B 1 101 ? 3.440   -11.784 28.620  1.000 9.000  ? 101 ASP BBB CG  1 
ATOM   1894 O  OD1 . ASP B 1 101 ? 2.973   -12.852 29.003  1.000 10.155 ? 101 ASP BBB OD1 1 
ATOM   1895 O  OD2 . ASP B 1 101 ? 4.396   -11.685 27.814  1.000 9.439  ? 101 ASP BBB OD2 1 
ATOM   1896 N  N   . SER B 1 102 ? 5.645   -11.000 31.001  1.000 10.159 ? 102 SER BBB N   1 
ATOM   1897 C  CA  . SER B 1 102 ? 7.101   -10.874 31.137  1.000 10.805 ? 102 SER BBB CA  1 
ATOM   1898 C  C   . SER B 1 102 ? 7.860   -11.178 29.855  1.000 10.143 ? 102 SER BBB C   1 
ATOM   1899 O  O   . SER B 1 102 ? 9.088   -11.024 29.882  1.000 11.260 ? 102 SER BBB O   1 
ATOM   1900 C  CB  . SER B 1 102 ? 7.617   -11.771 32.272  1.000 13.226 ? 102 SER BBB CB  1 
ATOM   1901 O  OG  . SER B 1 102 ? 7.084   -11.292 33.501  1.000 17.817 ? 102 SER BBB OG  1 
ATOM   1902 N  N   . VAL B 1 103 ? 7.207   -11.706 28.827  1.000 9.223  ? 103 VAL BBB N   1 
ATOM   1903 C  CA  . VAL B 1 103 ? 7.911   -12.145 27.605  1.000 9.482  ? 103 VAL BBB CA  1 
ATOM   1904 C  C   . VAL B 1 103 ? 7.796   -11.074 26.517  1.000 8.805  ? 103 VAL BBB C   1 
ATOM   1905 O  O   . VAL B 1 103 ? 8.790   -10.757 25.889  1.000 10.191 ? 103 VAL BBB O   1 
ATOM   1906 C  CB  . VAL B 1 103 ? 7.396   -13.526 27.194  1.000 9.582  ? 103 VAL BBB CB  1 
ATOM   1907 C  CG1 . VAL B 1 103 ? 7.995   -13.962 25.872  1.000 10.355 ? 103 VAL BBB CG1 1 
ATOM   1908 C  CG2 . VAL B 1 103 ? 7.679   -14.556 28.269  1.000 10.061 ? 103 VAL BBB CG2 1 
ATOM   1909 N  N   . ILE B 1 104 ? 6.621   -10.550 26.234  1.000 8.648  ? 104 ILE BBB N   1 
ATOM   1910 C  CA  . ILE B 1 104 ? 6.549   -9.403  25.298  1.000 8.479  ? 104 ILE BBB CA  1 
ATOM   1911 C  C   . ILE B 1 104 ? 7.337   -8.225  25.863  1.000 8.152  ? 104 ILE BBB C   1 
ATOM   1912 O  O   . ILE B 1 104 ? 7.531   -8.146  27.103  1.000 10.709 ? 104 ILE BBB O   1 
ATOM   1913 C  CB  . ILE B 1 104 ? 5.098   -9.001  24.984  1.000 7.987  ? 104 ILE BBB CB  1 
ATOM   1914 C  CG1 . ILE B 1 104 ? 4.349   -8.565  26.247  1.000 8.713  ? 104 ILE BBB CG1 1 
ATOM   1915 C  CG2 . ILE B 1 104 ? 4.363   -10.109 24.230  1.000 8.684  ? 104 ILE BBB CG2 1 
ATOM   1916 C  CD1 . ILE B 1 104 ? 3.058   -7.809  25.980  1.000 8.516  ? 104 ILE BBB CD1 1 
ATOM   1917 N  N   . SER B 1 105 ? 7.758   -7.324  25.005  1.000 8.088  ? 105 SER BBB N   1 
ATOM   1918 C  CA  . SER B 1 105 ? 8.428   -6.090  25.432  1.000 8.863  ? 105 SER BBB CA  1 
ATOM   1919 C  C   . SER B 1 105 ? 8.038   -4.978  24.496  1.000 9.666  ? 105 SER BBB C   1 
ATOM   1920 O  O   . SER B 1 105 ? 7.526   -5.221  23.378  1.000 9.371  ? 105 SER BBB O   1 
ATOM   1921 C  CB  . SER B 1 105 ? 9.895   -6.317  25.480  1.000 9.435  ? 105 SER BBB CB  1 
ATOM   1922 O  OG  . SER B 1 105 ? 10.535  -5.245  26.128  1.000 11.129 ? 105 SER BBB OG  1 
ATOM   1923 N  N   . LEU B 1 106 ? 8.354   -3.747  24.901  1.000 9.423  ? 106 LEU BBB N   1 
ATOM   1924 C  CA  . LEU B 1 106 ? 8.196   -2.551  24.028  1.000 9.737  ? 106 LEU BBB CA  1 
ATOM   1925 C  C   . LEU B 1 106 ? 9.576   -2.068  23.567  1.000 10.409 ? 106 LEU BBB C   1 
ATOM   1926 O  O   . LEU B 1 106 ? 9.644   -0.957  22.997  1.000 12.172 ? 106 LEU BBB O   1 
ATOM   1927 C  CB  . LEU B 1 106 ? 7.400   -1.469  24.768  1.000 9.838  ? 106 LEU BBB CB  1 
ATOM   1928 C  CG  . LEU B 1 106 ? 6.063   -1.957  25.325  1.000 10.606 ? 106 LEU BBB CG  1 
ATOM   1929 C  CD1 . LEU B 1 106 ? 5.269   -0.789  25.928  1.000 11.276 ? 106 LEU BBB CD1 1 
ATOM   1930 C  CD2 . LEU B 1 106 ? 5.204   -2.642  24.295  1.000 11.809 ? 106 LEU BBB CD2 1 
ATOM   1931 N  N   . SER B 1 107 ? 10.594  -2.914  23.680  1.000 10.847 ? 107 SER BBB N   1 
ATOM   1932 C  CA  . SER B 1 107 ? 11.927  -2.619  23.093  1.000 12.014 ? 107 SER BBB CA  1 
ATOM   1933 C  C   . SER B 1 107 ? 12.666  -3.944  22.894  1.000 13.772 ? 107 SER BBB C   1 
ATOM   1934 O  O   . SER B 1 107 ? 12.245  -4.988  23.441  1.000 12.788 ? 107 SER BBB O   1 
ATOM   1935 C  CB  . SER B 1 107 ? 12.694  -1.646  23.942  1.000 15.602 ? 107 SER BBB CB  1 
ATOM   1936 O  OG  . SER B 1 107 ? 12.952  -2.211  25.183  1.000 17.675 ? 107 SER BBB OG  1 
ATOM   1937 N  N   . GLY B 1 108 ? 13.716  -3.920  22.062  1.000 13.218 ? 108 GLY BBB N   1 
ATOM   1938 C  CA  . GLY B 1 108 ? 14.575  -5.088  21.752  1.000 13.460 ? 108 GLY BBB CA  1 
ATOM   1939 C  C   . GLY B 1 108 ? 13.907  -6.138  20.882  1.000 13.993 ? 108 GLY BBB C   1 
ATOM   1940 O  O   . GLY B 1 108 ? 12.945  -5.839  20.167  1.000 14.406 ? 108 GLY BBB O   1 
ATOM   1941 N  N   . ASP B 1 109 ? 14.470  -7.339  20.865  0.500 10.671 ? 109 ASP BBB N   1 
ATOM   1942 C  CA  . ASP B 1 109 ? 14.079  -8.384  19.894  0.500 11.000 ? 109 ASP BBB CA  1 
ATOM   1943 C  C   . ASP B 1 109 ? 12.695  -8.926  20.243  0.500 9.935  ? 109 ASP BBB C   1 
ATOM   1944 O  O   . ASP B 1 109 ? 12.092  -9.505  19.371  0.500 9.401  ? 109 ASP BBB O   1 
ATOM   1945 C  CB  . ASP B 1 109 ? 15.074  -9.544  19.938  0.500 12.534 ? 109 ASP BBB CB  1 
ATOM   1946 C  CG  . ASP B 1 109 ? 16.475  -9.234  19.437  0.500 14.403 ? 109 ASP BBB CG  1 
ATOM   1947 O  OD1 . ASP B 1 109 ? 16.624  -8.330  18.591  0.500 15.650 ? 109 ASP BBB OD1 1 
ATOM   1948 O  OD2 . ASP B 1 109 ? 17.408  -9.925  19.902  0.500 15.380 ? 109 ASP BBB OD2 1 
ATOM   1949 N  N   . HIS B 1 110 ? 12.201  -8.730  21.470  1.000 12.626 ? 110 HIS BBB N   1 
ATOM   1950 C  CA  . HIS B 1 110 ? 10.828  -9.170  21.833  1.000 11.742 ? 110 HIS BBB CA  1 
ATOM   1951 C  C   . HIS B 1 110 ? 9.847   -8.019  21.620  1.000 10.701 ? 110 HIS BBB C   1 
ATOM   1952 O  O   . HIS B 1 110 ? 8.659   -8.163  22.038  1.000 10.500 ? 110 HIS BBB O   1 
ATOM   1953 C  CB  . HIS B 1 110 ? 10.721  -9.663  23.262  1.000 13.586 ? 110 HIS BBB CB  1 
ATOM   1954 C  CG  . HIS B 1 110 ? 11.482  -10.902 23.525  1.000 15.188 ? 110 HIS BBB CG  1 
ATOM   1955 N  ND1 . HIS B 1 110 ? 11.193  -11.743 24.550  1.000 16.110 ? 110 HIS BBB ND1 1 
ATOM   1956 C  CD2 . HIS B 1 110 ? 12.405  -11.523 22.762  1.000 19.280 ? 110 HIS BBB CD2 1 
ATOM   1957 C  CE1 . HIS B 1 110 ? 12.040  -12.763 24.518  1.000 17.545 ? 110 HIS BBB CE1 1 
ATOM   1958 N  NE2 . HIS B 1 110 ? 12.751  -12.665 23.426  1.000 20.858 ? 110 HIS BBB NE2 1 
ATOM   1959 N  N   . CYS B 1 111 ? 10.270  -6.932  21.005  1.000 11.112 ? 111 CYS BBB N   1 
ATOM   1960 C  CA  . CYS B 1 111 ? 9.408   -5.760  20.834  1.000 10.268 ? 111 CYS BBB CA  1 
ATOM   1961 C  C   . CYS B 1 111 ? 8.228   -6.096  19.945  1.000 9.433  ? 111 CYS BBB C   1 
ATOM   1962 O  O   . CYS B 1 111 ? 8.375   -6.704  18.880  1.000 10.652 ? 111 CYS BBB O   1 
ATOM   1963 C  CB  . CYS B 1 111 ? 10.197  -4.618  20.232  1.000 10.808 ? 111 CYS BBB CB  1 
ATOM   1964 S  SG  . CYS B 1 111 ? 9.249   -3.102  20.141  1.000 12.440 ? 111 CYS BBB SG  1 
ATOM   1965 N  N   . ILE B 1 112 ? 7.062   -5.621  20.355  1.000 8.209  ? 112 ILE BBB N   1 
ATOM   1966 C  CA  . ILE B 1 112 ? 5.806   -5.866  19.609  1.000 8.101  ? 112 ILE BBB CA  1 
ATOM   1967 C  C   . ILE B 1 112 ? 5.333   -4.657  18.826  1.000 7.232  ? 112 ILE BBB C   1 
ATOM   1968 O  O   . ILE B 1 112 ? 4.340   -4.781  18.155  1.000 8.233  ? 112 ILE BBB O   1 
ATOM   1969 C  CB  . ILE B 1 112 ? 4.716   -6.350  20.567  1.000 8.864  ? 112 ILE BBB CB  1 
ATOM   1970 C  CG1 . ILE B 1 112 ? 4.362   -5.316  21.639  1.000 9.184  ? 112 ILE BBB CG1 1 
ATOM   1971 C  CG2 . ILE B 1 112 ? 5.146   -7.669  21.135  1.000 10.411 ? 112 ILE BBB CG2 1 
ATOM   1972 C  CD1 . ILE B 1 112 ? 3.150   -5.700  22.492  1.000 11.086 ? 112 ILE BBB CD1 1 
ATOM   1973 N  N   . ILE B 1 113 ? 6.012   -3.521  18.907  1.000 7.280  ? 113 ILE BBB N   1 
ATOM   1974 C  CA  . ILE B 1 113 ? 5.639   -2.330  18.110  1.000 7.212  ? 113 ILE BBB CA  1 
ATOM   1975 C  C   . ILE B 1 113 ? 5.745   -2.676  16.623  1.000 7.032  ? 113 ILE BBB C   1 
ATOM   1976 O  O   . ILE B 1 113 ? 6.745   -3.227  16.174  1.000 8.511  ? 113 ILE BBB O   1 
ATOM   1977 C  CB  . ILE B 1 113 ? 6.505   -1.107  18.498  1.000 8.051  ? 113 ILE BBB CB  1 
ATOM   1978 C  CG1 . ILE B 1 113 ? 6.287   -0.734  19.967  1.000 8.891  ? 113 ILE BBB CG1 1 
ATOM   1979 C  CG2 . ILE B 1 113 ? 6.234   0.072   17.602  1.000 8.419  ? 113 ILE BBB CG2 1 
ATOM   1980 C  CD1 . ILE B 1 113 ? 7.277   0.270   20.528  1.000 9.644  ? 113 ILE BBB CD1 1 
ATOM   1981 N  N   . GLY B 1 114 ? 4.750   -2.291  15.884  1.000 7.218  ? 114 GLY BBB N   1 
ATOM   1982 C  CA  . GLY B 1 114 ? 4.698   -2.538  14.431  1.000 7.580  ? 114 GLY BBB CA  1 
ATOM   1983 C  C   . GLY B 1 114 ? 4.282   -3.951  14.084  1.000 7.774  ? 114 GLY BBB C   1 
ATOM   1984 O  O   . GLY B 1 114 ? 4.235   -4.274  12.897  1.000 8.033  ? 114 GLY BBB O   1 
ATOM   1985 N  N   . ARG B 1 115 ? 3.869   -4.736  15.060  1.000 7.970  ? 115 ARG BBB N   1 
ATOM   1986 C  CA  . ARG B 1 115 ? 3.293   -6.074  14.840  1.000 7.985  ? 115 ARG BBB CA  1 
ATOM   1987 C  C   . ARG B 1 115 ? 1.784   -5.935  14.962  1.000 7.916  ? 115 ARG BBB C   1 
ATOM   1988 O  O   . ARG B 1 115 ? 1.285   -4.819  15.104  1.000 9.141  ? 115 ARG BBB O   1 
ATOM   1989 C  CB  . ARG B 1 115 ? 3.874   -7.099  15.824  1.000 8.954  ? 115 ARG BBB CB  1 
ATOM   1990 C  CG  . ARG B 1 115 ? 5.386   -7.094  15.996  1.000 12.809 ? 115 ARG BBB CG  1 
ATOM   1991 C  CD  . ARG B 1 115 ? 6.100   -7.808  14.931  1.000 15.026 ? 115 ARG BBB CD  1 
ATOM   1992 N  NE  . ARG B 1 115 ? 7.549   -7.719  15.058  1.000 13.354 ? 115 ARG BBB NE  1 
ATOM   1993 C  CZ  . ARG B 1 115 ? 8.341   -8.338  14.212  1.000 12.675 ? 115 ARG BBB CZ  1 
ATOM   1994 N  NH1 . ARG B 1 115 ? 7.858   -9.079  13.261  1.000 13.570 ? 115 ARG BBB NH1 1 
ATOM   1995 N  NH2 . ARG B 1 115 ? 9.650   -8.176  14.313  1.000 14.629 ? 115 ARG BBB NH2 1 
ATOM   1996 N  N   . THR B 1 116 ? 1.039   -7.032  14.835  1.000 7.535  ? 116 THR BBB N   1 
ATOM   1997 C  CA  . THR B 1 116 ? -0.440  -6.986  14.866  1.000 7.939  ? 116 THR BBB CA  1 
ATOM   1998 C  C   . THR B 1 116 ? -0.978  -7.728  16.069  1.000 7.472  ? 116 THR BBB C   1 
ATOM   1999 O  O   . THR B 1 116 ? -0.547  -8.866  16.344  1.000 8.649  ? 116 THR BBB O   1 
ATOM   2000 C  CB  . THR B 1 116 ? -1.052  -7.584  13.602  1.000 8.285  ? 116 THR BBB CB  1 
ATOM   2001 O  OG1 . THR B 1 116 ? -0.694  -6.748  12.501  1.000 8.776  ? 116 THR BBB OG1 1 
ATOM   2002 C  CG2 . THR B 1 116 ? -2.553  -7.682  13.654  1.000 8.608  ? 116 THR BBB CG2 1 
ATOM   2003 N  N   . LEU B 1 117 ? -1.886  -7.129  16.812  1.000 7.400  ? 117 LEU BBB N   1 
ATOM   2004 C  CA  . LEU B 1 117 ? -2.653  -7.822  17.864  1.000 6.919  ? 117 LEU BBB CA  1 
ATOM   2005 C  C   . LEU B 1 117 ? -3.944  -8.353  17.254  1.000 6.721  ? 117 LEU BBB C   1 
ATOM   2006 O  O   . LEU B 1 117 ? -4.616  -7.609  16.555  1.000 7.567  ? 117 LEU BBB O   1 
ATOM   2007 C  CB  . LEU B 1 117 ? -2.918  -6.825  18.993  1.000 7.129  ? 117 LEU BBB CB  1 
ATOM   2008 C  CG  . LEU B 1 117 ? -3.541  -7.397  20.259  1.000 7.886  ? 117 LEU BBB CG  1 
ATOM   2009 C  CD1 . LEU B 1 117 ? -2.582  -8.364  20.969  1.000 8.962  ? 117 LEU BBB CD1 1 
ATOM   2010 C  CD2 . LEU B 1 117 ? -3.939  -6.263  21.181  1.000 8.531  ? 117 LEU BBB CD2 1 
ATOM   2011 N  N   . VAL B 1 118 ? -4.292  -9.593  17.529  1.000 6.552  ? 118 VAL BBB N   1 
ATOM   2012 C  CA  . VAL B 1 118 ? -5.471  -10.271 16.974  1.000 6.976  ? 118 VAL BBB CA  1 
ATOM   2013 C  C   . VAL B 1 118 ? -6.272  -10.885 18.102  1.000 7.532  ? 118 VAL BBB C   1 
ATOM   2014 O  O   . VAL B 1 118 ? -5.692  -11.584 18.959  1.000 8.388  ? 118 VAL BBB O   1 
ATOM   2015 C  CB  . VAL B 1 118 ? -5.077  -11.390 15.990  1.000 7.213  ? 118 VAL BBB CB  1 
ATOM   2016 C  CG1 . VAL B 1 118 ? -6.316  -12.000 15.355  1.000 7.813  ? 118 VAL BBB CG1 1 
ATOM   2017 C  CG2 . VAL B 1 118 ? -4.162  -10.842 14.912  1.000 8.037  ? 118 VAL BBB CG2 1 
ATOM   2018 N  N   . VAL B 1 119 ? -7.586  -10.729 18.029  1.000 7.373  ? 119 VAL BBB N   1 
ATOM   2019 C  CA  . VAL B 1 119 ? -8.538  -11.482 18.884  1.000 8.081  ? 119 VAL BBB CA  1 
ATOM   2020 C  C   . VAL B 1 119 ? -9.257  -12.459 17.975  1.000 7.645  ? 119 VAL BBB C   1 
ATOM   2021 O  O   . VAL B 1 119 ? -9.718  -12.117 16.893  1.000 8.548  ? 119 VAL BBB O   1 
ATOM   2022 C  CB  . VAL B 1 119 ? -9.461  -10.581 19.715  1.000 7.762  ? 119 VAL BBB CB  1 
ATOM   2023 C  CG1 . VAL B 1 119 ? -10.367 -9.701  18.874  1.000 8.348  ? 119 VAL BBB CG1 1 
ATOM   2024 C  CG2 . VAL B 1 119 ? -10.307 -11.422 20.670  1.000 8.171  ? 119 VAL BBB CG2 1 
ATOM   2025 N  N   . HIS B 1 120 ? -9.309  -13.711 18.451  1.000 8.226  ? 120 HIS BBB N   1 
ATOM   2026 C  CA  . HIS B 1 120 ? -9.778  -14.873 17.677  1.000 8.738  ? 120 HIS BBB CA  1 
ATOM   2027 C  C   . HIS B 1 120 ? -11.206 -15.290 18.045  1.000 9.562  ? 120 HIS BBB C   1 
ATOM   2028 O  O   . HIS B 1 120 ? -11.729 -14.994 19.077  1.000 10.354 ? 120 HIS BBB O   1 
ATOM   2029 C  CB  . HIS B 1 120 ? -8.787  -16.033 17.836  1.000 9.319  ? 120 HIS BBB CB  1 
ATOM   2030 C  CG  . HIS B 1 120 ? -7.508  -15.819 17.121  1.000 9.424  ? 120 HIS BBB CG  1 
ATOM   2031 N  ND1 . HIS B 1 120 ? -7.235  -16.362 15.835  1.000 9.818  ? 120 HIS BBB ND1 1 
ATOM   2032 C  CD2 . HIS B 1 120 ? -6.367  -15.179 17.469  1.000 9.649  ? 120 HIS BBB CD2 1 
ATOM   2033 C  CE1 . HIS B 1 120 ? -6.021  -16.019 15.479  1.000 10.687 ? 120 HIS BBB CE1 1 
ATOM   2034 N  NE2 . HIS B 1 120 ? -5.461  -15.353 16.426  1.000 10.578 ? 120 HIS BBB NE2 1 
ATOM   2035 N  N   . GLU B 1 121 ? -11.744 -16.077 17.129  1.000 13.018 ? 121 GLU BBB N   1 
ATOM   2036 C  CA  . GLU B 1 121 ? -13.119 -16.614 17.173  1.000 13.448 ? 121 GLU BBB CA  1 
ATOM   2037 C  C   . GLU B 1 121 ? -13.322 -17.581 18.337  1.000 13.414 ? 121 GLU BBB C   1 
ATOM   2038 O  O   . GLU B 1 121 ? -14.345 -17.487 19.039  1.000 13.177 ? 121 GLU BBB O   1 
ATOM   2039 C  CB  . GLU B 1 121 ? -13.308 -17.309 15.824  1.000 16.948 ? 121 GLU BBB CB  1 
ATOM   2040 C  CG  . GLU B 1 121 ? -14.554 -18.166 15.628  1.000 19.487 ? 121 GLU BBB CG  1 
ATOM   2041 C  CD  . GLU B 1 121 ? -14.476 -19.185 14.476  1.000 22.251 ? 121 GLU BBB CD  1 
ATOM   2042 O  OE1 . GLU B 1 121 ? -15.565 -19.640 14.069  1.000 31.333 ? 121 GLU BBB OE1 1 
ATOM   2043 O  OE2 . GLU B 1 121 ? -13.379 -19.585 14.001  1.000 23.585 ? 121 GLU BBB OE2 1 
ATOM   2044 N  N   . LYS B 1 122 ? -12.352 -18.478 18.544  1.000 13.172 ? 122 LYS BBB N   1 
ATOM   2045 C  CA  . LYS B 1 122 ? -12.471 -19.644 19.460  1.000 12.388 ? 122 LYS BBB CA  1 
ATOM   2046 C  C   . LYS B 1 122 ? -11.455 -19.474 20.590  1.000 12.289 ? 122 LYS BBB C   1 
ATOM   2047 O  O   . LYS B 1 122 ? -10.549 -18.589 20.530  1.000 11.112 ? 122 LYS BBB O   1 
ATOM   2048 C  CB  . LYS B 1 122 ? -12.181 -20.961 18.726  1.000 15.025 ? 122 LYS BBB CB  1 
ATOM   2049 C  CG  . LYS B 1 122 ? -13.083 -21.258 17.549  1.000 17.839 ? 122 LYS BBB CG  1 
ATOM   2050 C  CD  . LYS B 1 122 ? -12.679 -22.511 16.803  1.000 22.216 ? 122 LYS BBB CD  1 
ATOM   2051 C  CE  . LYS B 1 122 ? -13.477 -22.638 15.520  1.000 26.773 ? 122 LYS BBB CE  1 
ATOM   2052 N  NZ  . LYS B 1 122 ? -13.267 -23.965 14.896  1.000 30.704 ? 122 LYS BBB NZ  1 
ATOM   2053 N  N   . ALA B 1 123 ? -11.567 -20.279 21.626  1.000 11.096 ? 123 ALA BBB N   1 
ATOM   2054 C  CA  . ALA B 1 123 ? -10.545 -20.341 22.683  1.000 10.776 ? 123 ALA BBB CA  1 
ATOM   2055 C  C   . ALA B 1 123 ? -9.233  -20.841 22.108  1.000 10.666 ? 123 ALA BBB C   1 
ATOM   2056 O  O   . ALA B 1 123 ? -9.215  -21.737 21.285  1.000 10.895 ? 123 ALA BBB O   1 
ATOM   2057 C  CB  . ALA B 1 123 ? -11.024 -21.253 23.792  1.000 11.872 ? 123 ALA BBB CB  1 
ATOM   2058 N  N   . ASP B 1 124 ? -8.164  -20.284 22.643  1.000 10.234 ? 124 ASP BBB N   1 
ATOM   2059 C  CA  . ASP B 1 124 ? -6.807  -20.831 22.480  1.000 9.695  ? 124 ASP BBB CA  1 
ATOM   2060 C  C   . ASP B 1 124 ? -6.651  -21.979 23.475  1.000 9.253  ? 124 ASP BBB C   1 
ATOM   2061 O  O   . ASP B 1 124 ? -6.843  -21.785 24.662  1.000 10.347 ? 124 ASP BBB O   1 
ATOM   2062 C  CB  . ASP B 1 124 ? -5.799  -19.719 22.666  1.000 9.835  ? 124 ASP BBB CB  1 
ATOM   2063 C  CG  . ASP B 1 124 ? -4.350  -20.095 22.492  1.000 10.451 ? 124 ASP BBB CG  1 
ATOM   2064 O  OD1 . ASP B 1 124 ? -4.015  -21.274 22.459  1.000 9.612  ? 124 ASP BBB OD1 1 
ATOM   2065 O  OD2 . ASP B 1 124 ? -3.531  -19.140 22.401  1.000 12.064 ? 124 ASP BBB OD2 1 
ATOM   2066 N  N   . ASP B 1 125 ? -6.304  -23.175 22.969  1.000 9.369  ? 125 ASP BBB N   1 
ATOM   2067 C  CA  . ASP B 1 125 ? -6.103  -24.350 23.862  1.000 9.322  ? 125 ASP BBB CA  1 
ATOM   2068 C  C   . ASP B 1 125 ? -4.749  -24.328 24.537  1.000 9.535  ? 125 ASP BBB C   1 
ATOM   2069 O  O   . ASP B 1 125 ? -4.410  -25.266 25.271  1.000 10.792 ? 125 ASP BBB O   1 
ATOM   2070 C  CB  . ASP B 1 125 ? -6.379  -25.657 23.148  1.000 10.159 ? 125 ASP BBB CB  1 
ATOM   2071 C  CG  . ASP B 1 125 ? -5.448  -25.949 21.976  1.000 10.273 ? 125 ASP BBB CG  1 
ATOM   2072 O  OD1 . ASP B 1 125 ? -4.274  -25.509 22.014  1.000 9.899  ? 125 ASP BBB OD1 1 
ATOM   2073 O  OD2 . ASP B 1 125 ? -5.864  -26.702 21.047  1.000 12.093 ? 125 ASP BBB OD2 1 
ATOM   2074 N  N   . LEU B 1 126 ? -3.947  -23.274 24.325  1.000 9.489  ? 126 LEU BBB N   1 
ATOM   2075 C  CA  . LEU B 1 126 ? -2.647  -23.049 25.002  1.000 9.828  ? 126 LEU BBB CA  1 
ATOM   2076 C  C   . LEU B 1 126 ? -1.697  -24.214 24.746  1.000 10.406 ? 126 LEU BBB C   1 
ATOM   2077 O  O   . LEU B 1 126 ? -0.807  -24.454 25.553  1.000 11.174 ? 126 LEU BBB O   1 
ATOM   2078 C  CB  . LEU B 1 126 ? -2.832  -22.795 26.504  1.000 11.146 ? 126 LEU BBB CB  1 
ATOM   2079 C  CG  . LEU B 1 126 ? -3.864  -21.734 26.882  1.000 12.767 ? 126 LEU BBB CG  1 
ATOM   2080 C  CD1 . LEU B 1 126 ? -3.835  -21.482 28.395  1.000 13.378 ? 126 LEU BBB CD1 1 
ATOM   2081 C  CD2 . LEU B 1 126 ? -3.690  -20.421 26.155  1.000 10.667 ? 126 LEU BBB CD2 1 
ATOM   2082 N  N   . GLY B 1 127 ? -1.809  -24.837 23.586  1.000 9.732  ? 127 GLY BBB N   1 
ATOM   2083 C  CA  . GLY B 1 127 ? -0.919  -25.960 23.242  1.000 11.053 ? 127 GLY BBB CA  1 
ATOM   2084 C  C   . GLY B 1 127 ? -1.384  -27.282 23.834  1.000 11.481 ? 127 GLY BBB C   1 
ATOM   2085 O  O   . GLY B 1 127 ? -0.641  -28.260 23.731  1.000 14.457 ? 127 GLY BBB O   1 
ATOM   2086 N  N   . LYS B 1 128 ? -2.559  -27.336 24.460  1.000 11.527 ? 128 LYS BBB N   1 
ATOM   2087 C  CA  . LYS B 1 128 ? -3.092  -28.568 25.151  1.000 12.166 ? 128 LYS BBB CA  1 
ATOM   2088 C  C   . LYS B 1 128 ? -4.376  -29.042 24.471  1.000 12.610 ? 128 LYS BBB C   1 
ATOM   2089 O  O   . LYS B 1 128 ? -5.393  -29.424 25.132  1.000 15.041 ? 128 LYS BBB O   1 
ATOM   2090 C  CB  . LYS B 1 128 ? -3.364  -28.225 26.619  1.000 14.346 ? 128 LYS BBB CB  1 
ATOM   2091 C  CG  . LYS B 1 128 ? -2.152  -27.720 27.348  1.000 16.129 ? 128 LYS BBB CG  1 
ATOM   2092 C  CD  . LYS B 1 128 ? -1.146  -28.803 27.536  1.000 20.786 ? 128 LYS BBB CD  1 
ATOM   2093 C  CE  . LYS B 1 128 ? 0.125   -28.358 28.215  1.000 25.578 ? 128 LYS BBB CE  1 
ATOM   2094 N  NZ  . LYS B 1 128 ? -0.125  -27.889 29.602  1.000 30.417 ? 128 LYS BBB NZ  1 
ATOM   2095 N  N   . GLY B 1 129 ? -4.366  -29.082 23.169  1.000 11.360 ? 129 GLY BBB N   1 
ATOM   2096 C  CA  . GLY B 1 129 ? -5.521  -29.568 22.407  1.000 11.288 ? 129 GLY BBB CA  1 
ATOM   2097 C  C   . GLY B 1 129 ? -5.358  -30.995 21.962  1.000 12.011 ? 129 GLY BBB C   1 
ATOM   2098 O  O   . GLY B 1 129 ? -6.370  -31.540 21.501  1.000 13.880 ? 129 GLY BBB O   1 
ATOM   2099 N  N   . GLY B 1 130 ? -4.147  -31.522 21.961  1.000 10.961 ? 130 GLY BBB N   1 
ATOM   2100 C  CA  . GLY B 1 130 ? -3.929  -32.920 21.560  1.000 12.455 ? 130 GLY BBB CA  1 
ATOM   2101 C  C   . GLY B 1 130 ? -3.856  -33.133 20.068  1.000 13.127 ? 130 GLY BBB C   1 
ATOM   2102 O  O   . GLY B 1 130 ? -4.050  -34.288 19.646  1.000 14.851 ? 130 GLY BBB O   1 
ATOM   2103 N  N   . ASN B 1 131 ? -3.660  -32.104 19.247  1.000 12.714 ? 131 ASN BBB N   1 
ATOM   2104 C  CA  . ASN B 1 131 ? -3.368  -32.303 17.811  1.000 13.160 ? 131 ASN BBB CA  1 
ATOM   2105 C  C   . ASN B 1 131 ? -2.186  -31.426 17.426  1.000 11.892 ? 131 ASN BBB C   1 
ATOM   2106 O  O   . ASN B 1 131 ? -1.652  -30.667 18.211  1.000 11.312 ? 131 ASN BBB O   1 
ATOM   2107 C  CB  . ASN B 1 131 ? -4.572  -32.066 16.910  1.000 13.361 ? 131 ASN BBB CB  1 
ATOM   2108 C  CG  . ASN B 1 131 ? -5.096  -30.650 16.924  1.000 13.923 ? 131 ASN BBB CG  1 
ATOM   2109 O  OD1 . ASN B 1 131 ? -4.504  -29.793 17.530  1.000 12.860 ? 131 ASN BBB OD1 1 
ATOM   2110 N  ND2 . ASN B 1 131 ? -6.238  -30.372 16.294  1.000 17.783 ? 131 ASN BBB ND2 1 
ATOM   2111 N  N   . GLU B 1 132 ? -1.685  -31.606 16.217  1.000 13.942 ? 132 GLU BBB N   1 
ATOM   2112 C  CA  . GLU B 1 132 ? -0.494  -30.864 15.751  1.000 14.999 ? 132 GLU BBB CA  1 
ATOM   2113 C  C   . GLU B 1 132 ? -0.827  -29.373 15.684  1.000 12.992 ? 132 GLU BBB C   1 
ATOM   2114 O  O   . GLU B 1 132 ? 0.060   -28.563 16.043  1.000 13.612 ? 132 GLU BBB O   1 
ATOM   2115 C  CB  . GLU B 1 132 ? -0.089  -31.413 14.386  1.000 19.779 ? 132 GLU BBB CB  1 
ATOM   2116 C  CG  . GLU B 1 132 ? 1.211   -30.833 13.849  1.000 24.267 ? 132 GLU BBB CG  1 
ATOM   2117 C  CD  . GLU B 1 132 ? 1.464   -31.219 12.403  1.000 31.081 ? 132 GLU BBB CD  1 
ATOM   2118 O  OE1 . GLU B 1 132 ? 0.472   -31.261 11.623  1.000 45.129 ? 132 GLU BBB OE1 1 
ATOM   2119 O  OE2 . GLU B 1 132 ? 2.639   -31.457 12.043  1.000 41.134 ? 132 GLU BBB OE2 1 
ATOM   2120 N  N   . GLU B 1 133 ? -2.016  -28.981 15.286  1.000 11.716 ? 133 GLU BBB N   1 
ATOM   2121 C  CA  . GLU B 1 133 ? -2.354  -27.539 15.140  1.000 12.712 ? 133 GLU BBB CA  1 
ATOM   2122 C  C   . GLU B 1 133 ? -2.304  -26.864 16.509  1.000 11.229 ? 133 GLU BBB C   1 
ATOM   2123 O  O   . GLU B 1 133 ? -1.991  -25.686 16.627  1.000 10.830 ? 133 GLU BBB O   1 
ATOM   2124 C  CB  . GLU B 1 133 ? -3.700  -27.372 14.439  1.000 16.485 ? 133 GLU BBB CB  1 
ATOM   2125 C  CG  . GLU B 1 133 ? -4.041  -25.931 14.122  1.000 19.945 ? 133 GLU BBB CG  1 
ATOM   2126 C  CD  . GLU B 1 133 ? -3.269  -25.213 12.999  1.000 25.819 ? 133 GLU BBB CD  1 
ATOM   2127 O  OE1 . GLU B 1 133 ? -2.106  -25.643 12.610  1.000 28.148 ? 133 GLU BBB OE1 1 
ATOM   2128 O  OE2 . GLU B 1 133 ? -3.832  -24.189 12.481  1.000 32.150 ? 133 GLU BBB OE2 1 
ATOM   2129 N  N   . SER B 1 134 ? -2.563  -27.610 17.581  1.000 10.499 ? 134 SER BBB N   1 
ATOM   2130 C  CA  . SER B 1 134 ? -2.547  -27.035 18.944  1.000 10.426 ? 134 SER BBB CA  1 
ATOM   2131 C  C   . SER B 1 134 ? -1.185  -26.396 19.221  1.000 11.249 ? 134 SER BBB C   1 
ATOM   2132 O  O   . SER B 1 134 ? -1.133  -25.339 19.845  1.000 11.179 ? 134 SER BBB O   1 
ATOM   2133 C  CB  . SER B 1 134 ? -2.894  -28.084 19.955  1.000 11.048 ? 134 SER BBB CB  1 
ATOM   2134 O  OG  . SER B 1 134 ? -2.800  -27.567 21.278  1.000 10.595 ? 134 SER BBB OG  1 
ATOM   2135 N  N   . THR B 1 135 ? -0.120  -27.029 18.727  1.000 12.169 ? 135 THR BBB N   1 
ATOM   2136 C  CA  . THR B 1 135 ? 1.292   -26.630 18.911  1.000 13.139 ? 135 THR BBB CA  1 
ATOM   2137 C  C   . THR B 1 135 ? 1.694   -25.463 18.008  1.000 11.427 ? 135 THR BBB C   1 
ATOM   2138 O  O   . THR B 1 135 ? 2.865   -25.062 18.112  1.000 11.922 ? 135 THR BBB O   1 
ATOM   2139 C  CB  . THR B 1 135 ? 2.252   -27.807 18.573  1.000 16.051 ? 135 THR BBB CB  1 
ATOM   2140 O  OG1 . THR B 1 135 ? 2.410   -27.955 17.150  1.000 19.659 ? 135 THR BBB OG1 1 
ATOM   2141 C  CG2 . THR B 1 135 ? 1.818   -29.095 19.199  1.000 15.945 ? 135 THR BBB CG2 1 
ATOM   2142 N  N   . LYS B 1 136 ? 0.820   -25.023 17.122  1.000 12.432 ? 136 LYS BBB N   1 
ATOM   2143 C  CA  . LYS B 1 136 ? 1.113   -23.920 16.168  1.000 12.572 ? 136 LYS BBB CA  1 
ATOM   2144 C  C   . LYS B 1 136 ? 0.205   -22.742 16.433  1.000 11.717 ? 136 LYS BBB C   1 
ATOM   2145 O  O   . LYS B 1 136 ? 0.713   -21.602 16.545  1.000 12.206 ? 136 LYS BBB O   1 
ATOM   2146 C  CB  . LYS B 1 136 ? 1.049   -24.451 14.737  1.000 16.434 ? 136 LYS BBB CB  1 
ATOM   2147 C  CG  . LYS B 1 136 ? 2.340   -25.186 14.366  1.000 20.272 ? 136 LYS BBB CG  1 
ATOM   2148 C  CD  . LYS B 1 136 ? 2.236   -26.293 13.342  1.000 27.342 ? 136 LYS BBB CD  1 
ATOM   2149 C  CE  . LYS B 1 136 ? 3.546   -27.032 13.185  1.000 25.939 ? 136 LYS BBB CE  1 
ATOM   2150 N  NZ  . LYS B 1 136 ? 3.824   -27.281 11.747  1.000 26.475 ? 136 LYS BBB NZ  1 
ATOM   2151 N  N   . THR B 1 137 ? -1.097  -22.965 16.515  1.000 10.353 ? 137 THR BBB N   1 
ATOM   2152 C  CA  . THR B 1 137 ? -2.043  -21.846 16.603  1.000 10.772 ? 137 THR BBB CA  1 
ATOM   2153 C  C   . THR B 1 137 ? -2.901  -21.906 17.871  1.000 10.181 ? 137 THR BBB C   1 
ATOM   2154 O  O   . THR B 1 137 ? -3.694  -20.964 18.133  1.000 11.378 ? 137 THR BBB O   1 
ATOM   2155 C  CB  . THR B 1 137 ? -2.998  -21.825 15.406  1.000 12.318 ? 137 THR BBB CB  1 
ATOM   2156 O  OG1 . THR B 1 137 ? -3.824  -22.993 15.525  1.000 13.827 ? 137 THR BBB OG1 1 
ATOM   2157 C  CG2 . THR B 1 137 ? -2.290  -21.740 14.069  1.000 13.889 ? 137 THR BBB CG2 1 
ATOM   2158 N  N   . GLY B 1 138 ? -2.891  -23.035 18.594  1.000 9.346  ? 138 GLY BBB N   1 
ATOM   2159 C  CA  . GLY B 1 138 ? -3.816  -23.235 19.714  1.000 9.468  ? 138 GLY BBB CA  1 
ATOM   2160 C  C   . GLY B 1 138 ? -5.253  -23.500 19.276  1.000 9.287  ? 138 GLY BBB C   1 
ATOM   2161 O  O   . GLY B 1 138 ? -6.162  -23.443 20.096  1.000 9.292  ? 138 GLY BBB O   1 
ATOM   2162 N  N   . ASN B 1 139 ? -5.474  -23.716 17.987  1.000 10.329 ? 139 ASN BBB N   1 
ATOM   2163 C  CA  . ASN B 1 139 ? -6.817  -24.001 17.435  1.000 10.156 ? 139 ASN BBB CA  1 
ATOM   2164 C  C   . ASN B 1 139 ? -7.804  -22.870 17.765  1.000 10.574 ? 139 ASN BBB C   1 
ATOM   2165 O  O   . ASN B 1 139 ? -9.009  -23.133 17.977  1.000 10.918 ? 139 ASN BBB O   1 
ATOM   2166 C  CB  . ASN B 1 139 ? -7.369  -25.335 17.949  1.000 11.181 ? 139 ASN BBB CB  1 
ATOM   2167 C  CG  . ASN B 1 139 ? -6.633  -26.532 17.407  1.000 12.353 ? 139 ASN BBB CG  1 
ATOM   2168 O  OD1 . ASN B 1 139 ? -6.596  -26.764 16.197  1.000 14.197 ? 139 ASN BBB OD1 1 
ATOM   2169 N  ND2 . ASN B 1 139 ? -5.915  -27.211 18.279  1.000 12.820 ? 139 ASN BBB ND2 1 
ATOM   2170 N  N   . ALA B 1 140 ? -7.358  -21.619 17.727  1.000 10.791 ? 140 ALA BBB N   1 
ATOM   2171 C  CA  . ALA B 1 140 ? -8.231  -20.482 18.104  1.000 11.200 ? 140 ALA BBB CA  1 
ATOM   2172 C  C   . ALA B 1 140 ? -9.080  -19.972 16.946  1.000 11.584 ? 140 ALA BBB C   1 
ATOM   2173 O  O   . ALA B 1 140 ? -9.868  -19.046 17.154  1.000 12.077 ? 140 ALA BBB O   1 
ATOM   2174 C  CB  . ALA B 1 140 ? -7.371  -19.392 18.718  1.000 11.366 ? 140 ALA BBB CB  1 
ATOM   2175 N  N   . GLY B 1 141 ? -9.003  -20.592 15.782  1.000 12.525 ? 141 GLY BBB N   1 
ATOM   2176 C  CA  . GLY B 1 141 ? -9.880  -20.243 14.656  1.000 13.279 ? 141 GLY BBB CA  1 
ATOM   2177 C  C   . GLY B 1 141 ? -9.646  -18.834 14.125  1.000 12.772 ? 141 GLY BBB C   1 
ATOM   2178 O  O   . GLY B 1 141 ? -8.528  -18.316 14.109  1.000 14.529 ? 141 GLY BBB O   1 
ATOM   2179 N  N   . SER B 1 142 ? -10.707 -18.310 13.556  1.000 13.364 ? 142 SER BBB N   1 
ATOM   2180 C  CA  . SER B 1 142 ? -10.592 -17.156 12.656  1.000 13.602 ? 142 SER BBB CA  1 
ATOM   2181 C  C   . SER B 1 142 ? -10.229 -15.892 13.444  1.000 11.977 ? 142 SER BBB C   1 
ATOM   2182 O  O   . SER B 1 142 ? -10.289 -15.870 14.690  1.000 13.662 ? 142 SER BBB O   1 
ATOM   2183 C  CB  . SER B 1 142 ? -11.834 -17.040 11.834  1.000 15.257 ? 142 SER BBB CB  1 
ATOM   2184 O  OG  . SER B 1 142 ? -12.867 -16.484 12.593  1.000 20.678 ? 142 SER BBB OG  1 
ATOM   2185 N  N   . ARG B 1 143 ? -9.956  -14.852 12.706  1.000 10.951 ? 143 ARG BBB N   1 
ATOM   2186 C  CA  . ARG B 1 143 ? -9.487  -13.568 13.237  1.000 9.741  ? 143 ARG BBB CA  1 
ATOM   2187 C  C   . ARG B 1 143 ? -10.637 -12.595 13.240  1.000 9.821  ? 143 ARG BBB C   1 
ATOM   2188 O  O   . ARG B 1 143 ? -11.063 -12.165 12.148  1.000 12.966 ? 143 ARG BBB O   1 
ATOM   2189 C  CB  . ARG B 1 143 ? -8.305  -13.083 12.415  1.000 9.577  ? 143 ARG BBB CB  1 
ATOM   2190 C  CG  . ARG B 1 143 ? -7.196  -14.114 12.335  1.000 9.567  ? 143 ARG BBB CG  1 
ATOM   2191 C  CD  . ARG B 1 143 ? -6.005  -13.735 11.489  1.000 10.095 ? 143 ARG BBB CD  1 
ATOM   2192 N  NE  . ARG B 1 143 ? -5.071  -14.832 11.499  1.000 10.139 ? 143 ARG BBB NE  1 
ATOM   2193 C  CZ  . ARG B 1 143 ? -3.797  -14.797 11.134  1.000 8.822  ? 143 ARG BBB CZ  1 
ATOM   2194 N  NH1 . ARG B 1 143 ? -3.202  -13.668 10.788  1.000 9.153  ? 143 ARG BBB NH1 1 
ATOM   2195 N  NH2 . ARG B 1 143 ? -3.081  -15.886 11.270  1.000 9.243  ? 143 ARG BBB NH2 1 
ATOM   2196 N  N   . LEU B 1 144 ? -11.166 -12.265 14.399  1.000 9.238  ? 144 LEU BBB N   1 
ATOM   2197 C  CA  . LEU B 1 144 ? -12.385 -11.429 14.487  1.000 10.512 ? 144 LEU BBB CA  1 
ATOM   2198 C  C   . LEU B 1 144 ? -12.031 -9.964  14.341  1.000 10.061 ? 144 LEU BBB C   1 
ATOM   2199 O  O   . LEU B 1 144 ? -12.771 -9.202  13.700  1.000 10.330 ? 144 LEU BBB O   1 
ATOM   2200 C  CB  . LEU B 1 144 ? -13.076 -11.641 15.817  1.000 11.322 ? 144 LEU BBB CB  1 
ATOM   2201 C  CG  . LEU B 1 144 ? -13.557 -13.055 16.120  1.000 13.263 ? 144 LEU BBB CG  1 
ATOM   2202 C  CD1 . LEU B 1 144 ? -14.228 -13.089 17.474  1.000 14.794 ? 144 LEU BBB CD1 1 
ATOM   2203 C  CD2 . LEU B 1 144 ? -14.506 -13.559 15.086  1.000 15.176 ? 144 LEU BBB CD2 1 
ATOM   2204 N  N   . ALA B 1 145 ? -10.907 -9.521  14.904  1.000 9.604  ? 145 ALA BBB N   1 
ATOM   2205 C  CA  . ALA B 1 145 ? -10.486 -8.117  14.858  1.000 9.222  ? 145 ALA BBB CA  1 
ATOM   2206 C  C   . ALA B 1 145 ? -8.999  -8.051  15.105  1.000 8.034  ? 145 ALA BBB C   1 
ATOM   2207 O  O   . ALA B 1 145 ? -8.444  -8.947  15.732  1.000 8.199  ? 145 ALA BBB O   1 
ATOM   2208 C  CB  . ALA B 1 145 ? -11.250 -7.290  15.829  1.000 8.951  ? 145 ALA BBB CB  1 
ATOM   2209 N  N   . CYS B 1 146 ? -8.369  -7.042  14.548  1.000 8.015  ? 146 CYS BBB N   1 
ATOM   2210 C  CA  . CYS B 1 146 ? -6.929  -6.870  14.725  1.000 8.268  ? 146 CYS BBB CA  1 
ATOM   2211 C  C   . CYS B 1 146 ? -6.538  -5.424  14.577  1.000 7.866  ? 146 CYS BBB C   1 
ATOM   2212 O  O   . CYS B 1 146 ? -7.329  -4.601  14.077  1.000 7.991  ? 146 CYS BBB O   1 
ATOM   2213 C  CB  . CYS B 1 146 ? -6.192  -7.698  13.690  1.000 9.197  ? 146 CYS BBB CB  1 
ATOM   2214 S  SG  . CYS B 1 146 ? -6.524  -7.265  11.972  1.000 11.270 ? 146 CYS BBB SG  1 
ATOM   2215 N  N   . GLY B 1 147 ? -5.316  -5.121  14.933  1.000 7.657  ? 147 GLY BBB N   1 
ATOM   2216 C  CA  . GLY B 1 147 ? -4.775  -3.780  14.671  1.000 7.830  ? 147 GLY BBB CA  1 
ATOM   2217 C  C   . GLY B 1 147 ? -3.273  -3.812  14.768  1.000 7.395  ? 147 GLY BBB C   1 
ATOM   2218 O  O   . GLY B 1 147 ? -2.706  -4.734  15.354  1.000 7.902  ? 147 GLY BBB O   1 
ATOM   2219 N  N   . VAL B 1 148 ? -2.616  -2.796  14.224  1.000 7.682  ? 148 VAL BBB N   1 
ATOM   2220 C  CA  . VAL B 1 148 ? -1.148  -2.657  14.301  1.000 7.765  ? 148 VAL BBB CA  1 
ATOM   2221 C  C   . VAL B 1 148 ? -0.815  -1.957  15.594  1.000 8.120  ? 148 VAL BBB C   1 
ATOM   2222 O  O   . VAL B 1 148 ? -1.501  -0.955  15.968  1.000 9.937  ? 148 VAL BBB O   1 
ATOM   2223 C  CB  . VAL B 1 148 ? -0.615  -1.908  13.069  1.000 9.305  ? 148 VAL BBB CB  1 
ATOM   2224 C  CG1 . VAL B 1 148 ? 0.889   -1.773  13.092  1.000 9.027  ? 148 VAL BBB CG1 1 
ATOM   2225 C  CG2 . VAL B 1 148 ? -1.043  -2.595  11.778  1.000 9.888  ? 148 VAL BBB CG2 1 
ATOM   2226 N  N   . ILE B 1 149 ? 0.201   -2.420  16.269  1.000 8.008  ? 149 ILE BBB N   1 
ATOM   2227 C  CA  . ILE B 1 149 ? 0.580   -1.931  17.611  1.000 8.652  ? 149 ILE BBB CA  1 
ATOM   2228 C  C   . ILE B 1 149 ? 1.459   -0.692  17.433  1.000 8.322  ? 149 ILE BBB C   1 
ATOM   2229 O  O   . ILE B 1 149 ? 2.522   -0.765  16.773  1.000 9.341  ? 149 ILE BBB O   1 
ATOM   2230 C  CB  . ILE B 1 149 ? 1.266   -3.061  18.356  1.000 9.573  ? 149 ILE BBB CB  1 
ATOM   2231 C  CG1 . ILE B 1 149 ? 0.327   -4.257  18.542  1.000 9.802  ? 149 ILE BBB CG1 1 
ATOM   2232 C  CG2 . ILE B 1 149 ? 1.790   -2.585  19.684  1.000 10.060 ? 149 ILE BBB CG2 1 
ATOM   2233 C  CD1 . ILE B 1 149 ? 1.010   -5.535  18.916  1.000 10.517 ? 149 ILE BBB CD1 1 
ATOM   2234 N  N   . GLY B 1 150 ? 1.015   0.434   17.962  1.000 8.885  ? 150 GLY BBB N   1 
ATOM   2235 C  CA  . GLY B 1 150 ? 1.693   1.711   17.708  1.000 8.555  ? 150 GLY BBB CA  1 
ATOM   2236 C  C   . GLY B 1 150 ? 2.109   2.444   18.948  1.000 9.186  ? 150 GLY BBB C   1 
ATOM   2237 O  O   . GLY B 1 150 ? 1.658   2.153   20.048  1.000 9.911  ? 150 GLY BBB O   1 
ATOM   2238 N  N   . ILE B 1 151 ? 2.994   3.396   18.755  1.000 9.303  ? 151 ILE BBB N   1 
ATOM   2239 C  CA  . ILE B 1 151 ? 3.563   4.223   19.846  1.000 9.779  ? 151 ILE BBB CA  1 
ATOM   2240 C  C   . ILE B 1 151 ? 2.545   5.276   20.285  1.000 9.492  ? 151 ILE BBB C   1 
ATOM   2241 O  O   . ILE B 1 151 ? 1.995   5.981   19.475  1.000 10.090 ? 151 ILE BBB O   1 
ATOM   2242 C  CB  . ILE B 1 151 ? 4.857   4.878   19.344  1.000 10.985 ? 151 ILE BBB CB  1 
ATOM   2243 C  CG1 . ILE B 1 151 ? 5.912   3.825   19.053  1.000 11.845 ? 151 ILE BBB CG1 1 
ATOM   2244 C  CG2 . ILE B 1 151 ? 5.351   5.970   20.304  1.000 12.391 ? 151 ILE BBB CG2 1 
ATOM   2245 C  CD1 . ILE B 1 151 ? 7.076   4.296   18.233  1.000 13.350 ? 151 ILE BBB CD1 1 
ATOM   2246 N  N   . ALA B 1 152 ? 2.277   5.357   21.597  1.000 9.893  ? 152 ALA BBB N   1 
ATOM   2247 C  CA  . ALA B 1 152 ? 1.324   6.318   22.158  1.000 11.145 ? 152 ALA BBB CA  1 
ATOM   2248 C  C   . ALA B 1 152 ? 2.082   7.447   22.862  1.000 11.792 ? 152 ALA BBB C   1 
ATOM   2249 O  O   . ALA B 1 152 ? 3.285   7.296   23.212  1.000 12.297 ? 152 ALA BBB O   1 
ATOM   2250 C  CB  . ALA B 1 152 ? 0.429   5.617   23.160  1.000 10.924 ? 152 ALA BBB CB  1 
ATOM   2251 N  N   . GLN B 1 153 ? 1.368   8.525   23.145  1.000 11.802 ? 153 GLN BBB N   1 
ATOM   2252 C  CA  . GLN B 1 153 ? 1.920   9.672   23.873  1.000 14.107 ? 153 GLN BBB CA  1 
ATOM   2253 C  C   . GLN B 1 153 ? 2.140   9.265   25.333  1.000 18.232 ? 153 GLN BBB C   1 
ATOM   2254 O  O   . GLN B 1 153 ? 1.344   8.571   25.961  1.000 20.530 ? 153 GLN BBB O   1 
ATOM   2255 C  CB  . GLN B 1 153 ? 0.946   10.831  23.780  1.000 14.351 ? 153 GLN BBB CB  1 
ATOM   2256 C  CG  . GLN B 1 153 ? 1.488   12.126  24.349  1.000 15.452 ? 153 GLN BBB CG  1 
ATOM   2257 C  CD  . GLN B 1 153 ? 0.471   13.232  24.125  1.000 16.969 ? 153 GLN BBB CD  1 
ATOM   2258 O  OE1 . GLN B 1 153 ? -0.034  13.790  25.087  1.000 21.804 ? 153 GLN BBB OE1 1 
ATOM   2259 N  NE2 . GLN B 1 153 ? 0.020   13.424  22.890  1.000 22.474 ? 153 GLN BBB NE2 1 
ATOM   2260 O  OXT . GLN B 1 153 ? 3.175   9.689   25.901  1.000 20.476 ? 153 GLN BBB OXT 1 
HETATM 2261 ZN ZN  . ZN  C 2 .   ? 5.701   18.728  9.111   0.900 7.546  ? 201 ZN  AAA ZN  1 
HETATM 2262 C  C1  . Q6H D 3 .   ? 10.838  1.771   17.988  1.000 17.737 ? 202 Q6H AAA C1  1 
HETATM 2263 C  C2  . Q6H D 3 .   ? 10.067  1.870   16.886  1.000 17.031 ? 202 Q6H AAA C2  1 
HETATM 2264 C  C3  . Q6H D 3 .   ? 10.638  1.625   15.621  1.000 16.767 ? 202 Q6H AAA C3  1 
HETATM 2265 C  C4  . Q6H D 3 .   ? 11.983  1.212   15.348  1.000 16.083 ? 202 Q6H AAA C4  1 
HETATM 2266 C  C5  . Q6H D 3 .   ? 12.725  1.157   16.597  1.000 18.186 ? 202 Q6H AAA C5  1 
HETATM 2267 C  C6  . Q6H D 3 .   ? 14.151  0.714   16.481  1.000 20.159 ? 202 Q6H AAA C6  1 
HETATM 2268 C  C10 . Q6H D 3 .   ? 17.090  0.373   16.208  1.000 25.493 ? 202 Q6H AAA C10 1 
HETATM 2269 C  C11 . Q6H D 3 .   ? 18.487  0.241   16.287  1.000 26.046 ? 202 Q6H AAA C11 1 
HETATM 2270 C  C12 . Q6H D 3 .   ? 19.156  0.827   17.341  1.000 27.824 ? 202 Q6H AAA C12 1 
HETATM 2271 C  C13 . Q6H D 3 .   ? 19.315  -0.455  15.255  1.000 29.054 ? 202 Q6H AAA C13 1 
HETATM 2272 C  C14 . Q6H D 3 .   ? 20.070  -2.461  14.034  1.000 30.802 ? 202 Q6H AAA C14 1 
HETATM 2273 C  C15 . Q6H D 3 .   ? 18.946  -3.024  13.166  1.000 30.853 ? 202 Q6H AAA C15 1 
HETATM 2274 F  F   . Q6H D 3 .   ? 10.311  2.002   19.195  1.000 21.408 ? 202 Q6H AAA F   1 
HETATM 2275 SE SE  . Q6H D 3 .   ? 12.628  0.867   13.830  0.800 13.478 ? 202 Q6H AAA SE  1 
HETATM 2276 C  C   . Q6H D 3 .   ? 12.144  1.422   17.826  1.000 17.369 ? 202 Q6H AAA C   1 
HETATM 2277 O  O   . Q6H D 3 .   ? 14.441  -0.099  15.609  1.000 21.098 ? 202 Q6H AAA O   1 
HETATM 2278 N  N   . Q6H D 3 .   ? 15.032  1.277   17.261  1.000 22.364 ? 202 Q6H AAA N   1 
HETATM 2279 C  C7  . Q6H D 3 .   ? 16.392  1.092   17.198  1.000 22.480 ? 202 Q6H AAA C7  1 
HETATM 2280 C  C8  . Q6H D 3 .   ? 18.473  1.530   18.319  1.000 26.913 ? 202 Q6H AAA C8  1 
HETATM 2281 C  C9  . Q6H D 3 .   ? 17.088  1.672   18.258  1.000 26.574 ? 202 Q6H AAA C9  1 
HETATM 2282 O  O2  . Q6H D 3 .   ? 19.995  0.304   14.522  1.000 29.642 ? 202 Q6H AAA O2  1 
HETATM 2283 N  N1  . Q6H D 3 .   ? 19.341  -1.787  15.126  1.000 29.612 ? 202 Q6H AAA N1  1 
HETATM 2284 C  C17 . Q6H D 3 .   ? 18.668  -2.746  15.998  1.000 28.529 ? 202 Q6H AAA C17 1 
HETATM 2285 C  C16 . Q6H D 3 .   ? 17.615  -3.449  15.138  1.000 28.445 ? 202 Q6H AAA C16 1 
HETATM 2286 O  O1  . Q6H D 3 .   ? 18.156  -3.960  13.917  1.000 29.403 ? 202 Q6H AAA O1  1 
HETATM 2287 ZN ZN  . ZN  E 2 .   ? -0.740  15.834  8.755   0.300 9.644  ? 203 ZN  AAA ZN  1 
HETATM 2288 S  S   . SO4 F 4 .   ? -4.352  23.164  9.438   0.700 28.124 ? 204 SO4 AAA S   1 
HETATM 2289 O  O1  . SO4 F 4 .   ? -3.319  22.173  9.654   0.700 27.438 ? 204 SO4 AAA O1  1 
HETATM 2290 O  O2  . SO4 F 4 .   ? -4.788  23.162  8.048   0.700 20.415 ? 204 SO4 AAA O2  1 
HETATM 2291 O  O3  . SO4 F 4 .   ? -5.469  22.863  10.292  0.700 32.956 ? 204 SO4 AAA O3  1 
HETATM 2292 O  O4  . SO4 F 4 .   ? -3.813  24.460  9.779   0.700 27.105 ? 204 SO4 AAA O4  1 
HETATM 2293 S  S   . SO4 G 4 .   ? -1.861  18.134  10.770  0.700 19.559 ? 205 SO4 AAA S   1 
HETATM 2294 O  O1  . SO4 G 4 .   ? -0.950  17.706  9.725   0.700 21.104 ? 205 SO4 AAA O1  1 
HETATM 2295 O  O2  . SO4 G 4 .   ? -2.508  19.362  10.324  0.700 28.257 ? 205 SO4 AAA O2  1 
HETATM 2296 O  O3  . SO4 G 4 .   ? -1.097  18.333  11.963  0.700 27.410 ? 205 SO4 AAA O3  1 
HETATM 2297 O  O4  . SO4 G 4 .   ? -2.886  17.167  10.975  0.700 24.068 ? 205 SO4 AAA O4  1 
HETATM 2298 ZN ZN  . ZN  H 2 .   ? 1.389   -19.024 19.497  1.000 7.504  ? 201 ZN  BBB ZN  1 
HETATM 2299 C  C1  . Q6H I 3 .   ? 11.227  -2.629  14.933  1.000 20.319 ? 202 Q6H BBB C1  1 
HETATM 2300 C  C2  . Q6H I 3 .   ? 10.045  -2.286  15.535  1.000 19.326 ? 202 Q6H BBB C2  1 
HETATM 2301 C  C3  . Q6H I 3 .   ? 9.994   -2.036  16.931  1.000 20.731 ? 202 Q6H BBB C3  1 
HETATM 2302 C  C4  . Q6H I 3 .   ? 11.091  -1.998  17.844  1.000 18.459 ? 202 Q6H BBB C4  1 
HETATM 2303 C  C5  . Q6H I 3 .   ? 12.329  -2.367  17.085  1.000 18.607 ? 202 Q6H BBB C5  1 
HETATM 2304 C  C6  . Q6H I 3 .   ? 13.599  -2.389  17.763  1.000 19.522 ? 202 Q6H BBB C6  1 
HETATM 2305 C  C10 . Q6H I 3 .   ? 16.276  -2.674  18.761  1.000 19.730 ? 202 Q6H BBB C10 1 
HETATM 2306 C  C11 . Q6H I 3 .   ? 17.392  -2.935  19.518  1.000 20.078 ? 202 Q6H BBB C11 1 
HETATM 2307 C  C12 . Q6H I 3 .   ? 17.793  -4.271  19.719  1.000 19.291 ? 202 Q6H BBB C12 1 
HETATM 2308 C  C13 . Q6H I 3 .   ? 18.075  -1.722  20.092  1.000 23.800 ? 202 Q6H BBB C13 1 
HETATM 2309 C  C14 . Q6H I 3 .   ? 20.200  -2.304  18.904  1.000 24.258 ? 202 Q6H BBB C14 1 
HETATM 2310 C  C15 . Q6H I 3 .   ? 21.252  -2.951  19.784  1.000 23.432 ? 202 Q6H BBB C15 1 
HETATM 2311 F  F   . Q6H I 3 .   ? 11.242  -2.857  13.593  1.000 23.516 ? 202 Q6H BBB F   1 
HETATM 2312 SE SE  . Q6H I 3 .   ? 10.904  -1.685  19.458  0.800 15.420 ? 202 Q6H BBB SE  1 
HETATM 2313 C  C   . Q6H I 3 .   ? 12.378  -2.628  15.705  1.000 20.059 ? 202 Q6H BBB C   1 
HETATM 2314 O  O   . Q6H I 3 .   ? 13.831  -1.436  18.502  1.000 21.195 ? 202 Q6H BBB O   1 
HETATM 2315 N  N   . Q6H I 3 .   ? 14.369  -3.447  17.487  1.000 19.309 ? 202 Q6H BBB N   1 
HETATM 2316 C  C7  . Q6H I 3 .   ? 15.530  -3.707  18.159  1.000 18.705 ? 202 Q6H BBB C7  1 
HETATM 2317 C  C8  . Q6H I 3 .   ? 17.103  -5.314  19.120  1.000 18.119 ? 202 Q6H BBB C8  1 
HETATM 2318 C  C9  . Q6H I 3 .   ? 15.931  -5.038  18.337  1.000 17.290 ? 202 Q6H BBB C9  1 
HETATM 2319 O  O2  . Q6H I 3 .   ? 17.436  -0.919  20.775  1.000 24.237 ? 202 Q6H BBB O2  1 
HETATM 2320 N  N1  . Q6H I 3 .   ? 19.364  -1.489  19.807  1.000 23.910 ? 202 Q6H BBB N1  1 
HETATM 2321 C  C17 . Q6H I 3 .   ? 20.106  -0.411  20.472  1.000 23.310 ? 202 Q6H BBB C17 1 
HETATM 2322 C  C16 . Q6H I 3 .   ? 21.251  -1.069  21.270  1.000 22.470 ? 202 Q6H BBB C16 1 
HETATM 2323 O  O1  . Q6H I 3 .   ? 22.016  -1.916  20.389  1.000 21.953 ? 202 Q6H BBB O1  1 
HETATM 2324 ZN ZN  . ZN  J 2 .   ? -3.869  -15.795 16.285  0.300 10.444 ? 203 ZN  BBB ZN  1 
HETATM 2325 S  S   . SO4 K 4 .   ? -6.963  -22.787 13.386  0.500 17.256 ? 204 SO4 BBB S   1 
HETATM 2326 O  O1  . SO4 K 4 .   ? -6.401  -24.052 13.048  0.500 21.440 ? 204 SO4 BBB O1  1 
HETATM 2327 O  O2  . SO4 K 4 .   ? -7.486  -22.132 12.213  0.500 22.429 ? 204 SO4 BBB O2  1 
HETATM 2328 O  O3  . SO4 K 4 .   ? -5.937  -21.976 13.983  0.500 17.658 ? 204 SO4 BBB O3  1 
HETATM 2329 O  O4  . SO4 K 4 .   ? -8.050  -22.979 14.341  0.700 17.833 ? 204 SO4 BBB O4  1 
HETATM 2330 S  S   . SO4 L 4 .   ? 8.902   -32.472 18.253  1.000 61.320 ? 205 SO4 BBB S   1 
HETATM 2331 O  O1  . SO4 L 4 .   ? 10.108  -33.074 17.746  1.000 53.313 ? 205 SO4 BBB O1  1 
HETATM 2332 O  O2  . SO4 L 4 .   ? 8.211   -31.816 17.171  1.000 56.253 ? 205 SO4 BBB O2  1 
HETATM 2333 O  O3  . SO4 L 4 .   ? 8.050   -33.483 18.824  1.000 65.338 ? 205 SO4 BBB O3  1 
HETATM 2334 O  O4  . SO4 L 4 .   ? 9.222   -31.515 19.283  1.000 61.875 ? 205 SO4 BBB O4  1 
HETATM 2335 S  S   . SO4 M 4 .   ? -3.837  -18.131 14.006  0.500 17.186 ? 206 SO4 BBB S   1 
HETATM 2336 O  O1  . SO4 M 4 .   ? -2.597  -18.596 13.474  0.500 21.464 ? 206 SO4 BBB O1  1 
HETATM 2337 O  O2  . SO4 M 4 .   ? -4.393  -17.126 13.185  0.500 19.556 ? 206 SO4 BBB O2  1 
HETATM 2338 O  O3  . SO4 M 4 .   ? -4.802  -19.215 14.148  0.500 20.756 ? 206 SO4 BBB O3  1 
HETATM 2339 O  O4  . SO4 M 4 .   ? -3.593  -17.646 15.326  0.500 15.474 ? 206 SO4 BBB O4  1 
HETATM 2340 O  O   . HOH N 5 .   ? 7.843   4.169   -7.303  1.000 30.468 ? 301 HOH AAA O   1 
HETATM 2341 O  O   . HOH N 5 .   ? -5.088  17.827  11.058  1.000 26.761 ? 302 HOH AAA O   1 
HETATM 2342 O  O   . HOH N 5 .   ? 0.052   34.351  5.702   1.000 25.204 ? 303 HOH AAA O   1 
HETATM 2343 O  O   . HOH N 5 .   ? 15.033  24.301  13.605  1.000 30.174 ? 304 HOH AAA O   1 
HETATM 2344 O  O   . HOH N 5 .   ? -5.650  16.230  -13.419 1.000 23.108 ? 305 HOH AAA O   1 
HETATM 2345 O  O   . HOH N 5 .   ? 20.071  8.830   0.788   1.000 34.956 ? 306 HOH AAA O   1 
HETATM 2346 O  O   . HOH N 5 .   ? 12.347  23.448  18.039  1.000 21.964 ? 307 HOH AAA O   1 
HETATM 2347 O  O   . HOH N 5 .   ? -7.578  12.603  19.165  1.000 20.739 ? 308 HOH AAA O   1 
HETATM 2348 O  O   . HOH N 5 .   ? 11.092  24.822  6.580   1.000 30.239 ? 309 HOH AAA O   1 
HETATM 2349 O  O   . HOH N 5 .   ? 11.068  -8.131  4.640   1.000 42.692 ? 310 HOH AAA O   1 
HETATM 2350 O  O   . HOH N 5 .   ? 16.772  -0.140  7.859   1.000 28.895 ? 311 HOH AAA O   1 
HETATM 2351 O  O   . HOH N 5 .   ? -7.641  -3.822  4.920   1.000 25.632 ? 312 HOH AAA O   1 
HETATM 2352 O  O   . HOH N 5 .   ? 18.631  4.771   9.698   1.000 20.014 ? 313 HOH AAA O   1 
HETATM 2353 O  O   . HOH N 5 .   ? 9.486   24.106  0.893   1.000 19.894 ? 314 HOH AAA O   1 
HETATM 2354 O  O   . HOH N 5 .   ? -3.086  8.923   -10.352 1.000 26.567 ? 315 HOH AAA O   1 
HETATM 2355 O  O   . HOH N 5 .   ? -5.921  2.853   11.784  1.000 18.609 ? 316 HOH AAA O   1 
HETATM 2356 O  O   . HOH N 5 .   ? 15.030  16.755  19.164  1.000 15.499 ? 317 HOH AAA O   1 
HETATM 2357 O  O   . HOH N 5 .   ? -5.995  1.418   8.666   1.000 20.562 ? 318 HOH AAA O   1 
HETATM 2358 O  O   . HOH N 5 .   ? 6.029   30.350  5.402   1.000 23.414 ? 319 HOH AAA O   1 
HETATM 2359 O  O   . HOH N 5 .   ? -8.352  19.816  -1.295  1.000 26.789 ? 320 HOH AAA O   1 
HETATM 2360 O  O   . HOH N 5 .   ? -1.363  8.588   22.439  1.000 19.550 ? 321 HOH AAA O   1 
HETATM 2361 O  O   . HOH N 5 .   ? -1.178  19.006  14.571  1.000 20.466 ? 322 HOH AAA O   1 
HETATM 2362 O  O   . HOH N 5 .   ? 14.068  16.718  10.901  1.000 13.582 ? 323 HOH AAA O   1 
HETATM 2363 O  O   . HOH N 5 .   ? 2.521   14.549  -5.819  1.000 18.885 ? 324 HOH AAA O   1 
HETATM 2364 O  O   . HOH N 5 .   ? 5.100   -3.482  2.009   1.000 24.297 ? 325 HOH AAA O   1 
HETATM 2365 O  O   . HOH N 5 .   ? 9.039   4.921   15.312  1.000 13.119 ? 326 HOH AAA O   1 
HETATM 2366 O  O   . HOH N 5 .   ? 15.646  15.502  1.718   1.000 26.089 ? 327 HOH AAA O   1 
HETATM 2367 O  O   . HOH N 5 .   ? 9.581   27.966  5.797   1.000 31.645 ? 328 HOH AAA O   1 
HETATM 2368 O  O   . HOH N 5 .   ? -12.135 11.073  4.820   1.000 21.320 ? 329 HOH AAA O   1 
HETATM 2369 O  O   . HOH N 5 .   ? 12.399  8.624   17.325  1.000 27.683 ? 330 HOH AAA O   1 
HETATM 2370 O  O   . HOH N 5 .   ? -8.000  8.458   21.831  1.000 18.281 ? 331 HOH AAA O   1 
HETATM 2371 O  O   . HOH N 5 .   ? 13.787  -2.266  11.334  1.000 22.630 ? 332 HOH AAA O   1 
HETATM 2372 O  O   . HOH N 5 .   ? 6.674   13.866  -1.968  1.000 16.578 ? 333 HOH AAA O   1 
HETATM 2373 O  O   . HOH N 5 .   ? 11.453  12.636  -0.627  1.000 16.775 ? 334 HOH AAA O   1 
HETATM 2374 O  O   . HOH N 5 .   ? 3.515   -3.163  -3.936  1.000 35.695 ? 335 HOH AAA O   1 
HETATM 2375 O  O   . HOH N 5 .   ? -17.817 6.846   -2.480  1.000 30.569 ? 336 HOH AAA O   1 
HETATM 2376 O  O   . HOH N 5 .   ? 0.992   17.102  -9.061  1.000 12.128 ? 337 HOH AAA O   1 
HETATM 2377 O  O   . HOH N 5 .   ? 16.276  17.049  3.980   1.000 26.737 ? 338 HOH AAA O   1 
HETATM 2378 O  O   . HOH N 5 .   ? -12.410 12.557  -0.577  1.000 21.019 ? 339 HOH AAA O   1 
HETATM 2379 O  O   . HOH N 5 .   ? 12.360  15.971  12.890  1.000 9.785  ? 340 HOH AAA O   1 
HETATM 2380 O  O   . HOH N 5 .   ? -11.223 7.025   -6.506  1.000 19.873 ? 341 HOH AAA O   1 
HETATM 2381 O  O   . HOH N 5 .   ? -1.715  -0.192  8.608   1.000 7.405  ? 342 HOH AAA O   1 
HETATM 2382 O  O   . HOH N 5 .   ? -3.358  24.293  1.639   1.000 21.327 ? 343 HOH AAA O   1 
HETATM 2383 O  O   . HOH N 5 .   ? 17.037  6.962   5.364   1.000 22.963 ? 344 HOH AAA O   1 
HETATM 2384 O  O   . HOH N 5 .   ? 5.544   18.282  14.260  1.000 17.450 ? 345 HOH AAA O   1 
HETATM 2385 O  O   . HOH N 5 .   ? 16.140  9.798   -1.451  1.000 26.026 ? 346 HOH AAA O   1 
HETATM 2386 O  O   . HOH N 5 .   ? 17.238  6.691   12.099  1.000 15.784 ? 347 HOH AAA O   1 
HETATM 2387 O  O   . HOH N 5 .   ? 5.842   18.046  3.815   1.000 12.036 ? 348 HOH AAA O   1 
HETATM 2388 O  O   . HOH N 5 .   ? 15.299  22.893  -0.506  1.000 30.694 ? 349 HOH AAA O   1 
HETATM 2389 O  O   . HOH N 5 .   ? -1.001  10.067  -9.057  1.000 23.471 ? 350 HOH AAA O   1 
HETATM 2390 O  O   . HOH N 5 .   ? 13.353  4.685   17.141  1.000 29.279 ? 351 HOH AAA O   1 
HETATM 2391 O  O   . HOH N 5 .   ? 13.684  -8.858  3.713   1.000 46.936 ? 352 HOH AAA O   1 
HETATM 2392 O  O   . HOH N 5 .   ? 3.075   19.392  12.996  1.000 15.699 ? 353 HOH AAA O   1 
HETATM 2393 O  O   . HOH N 5 .   ? 4.867   12.664  -3.925  1.000 22.295 ? 354 HOH AAA O   1 
HETATM 2394 O  O   . HOH N 5 .   ? -10.427 9.900   11.985  1.000 31.845 ? 355 HOH AAA O   1 
HETATM 2395 O  O   . HOH N 5 .   ? 18.164  1.813   1.125   1.000 18.278 ? 356 HOH AAA O   1 
HETATM 2396 O  O   . HOH N 5 .   ? -9.278  3.561   14.189  1.000 28.797 ? 357 HOH AAA O   1 
HETATM 2397 O  O   . HOH N 5 .   ? -4.797  15.891  16.318  1.000 15.435 ? 358 HOH AAA O   1 
HETATM 2398 O  O   . HOH N 5 .   ? 17.617  9.385   7.802   1.000 28.234 ? 359 HOH AAA O   1 
HETATM 2399 O  O   . HOH N 5 .   ? -9.107  20.004  -8.229  1.000 26.710 ? 360 HOH AAA O   1 
HETATM 2400 O  O   . HOH N 5 .   ? 7.033   22.661  13.747  1.000 25.921 ? 361 HOH AAA O   1 
HETATM 2401 O  O   . HOH N 5 .   ? -3.459  2.674   17.375  1.000 10.510 ? 362 HOH AAA O   1 
HETATM 2402 O  O   . HOH N 5 .   ? 0.384   6.105   -12.376 1.000 27.621 ? 363 HOH AAA O   1 
HETATM 2403 O  O   . HOH N 5 .   ? -10.255 16.856  -0.009  1.000 20.491 ? 364 HOH AAA O   1 
HETATM 2404 O  O   . HOH N 5 .   ? 3.419   8.937   -8.929  1.000 27.111 ? 365 HOH AAA O   1 
HETATM 2405 O  O   . HOH N 5 .   ? 3.077   3.632   -7.454  1.000 21.213 ? 366 HOH AAA O   1 
HETATM 2406 O  O   . HOH N 5 .   ? 11.143  -10.406 2.399   1.000 32.155 ? 367 HOH AAA O   1 
HETATM 2407 O  O   . HOH N 5 .   ? 9.904   25.616  3.815   1.000 26.321 ? 368 HOH AAA O   1 
HETATM 2408 O  O   . HOH N 5 .   ? 11.633  22.076  -1.563  1.000 24.034 ? 369 HOH AAA O   1 
HETATM 2409 O  O   . HOH N 5 .   ? 9.855   -11.677 6.906   1.000 26.547 ? 370 HOH AAA O   1 
HETATM 2410 O  O   . HOH N 5 .   ? 9.450   -9.363  8.456   1.000 19.496 ? 371 HOH AAA O   1 
HETATM 2411 O  O   . HOH N 5 .   ? 17.823  9.071   19.844  1.000 16.304 ? 372 HOH AAA O   1 
HETATM 2412 O  O   . HOH N 5 .   ? 6.874   19.201  16.425  1.000 21.465 ? 373 HOH AAA O   1 
HETATM 2413 O  O   . HOH N 5 .   ? 7.808   13.751  17.113  1.000 18.163 ? 374 HOH AAA O   1 
HETATM 2414 O  O   . HOH N 5 .   ? -0.620  30.620  2.018   1.000 20.336 ? 375 HOH AAA O   1 
HETATM 2415 O  O   . HOH N 5 .   ? 17.051  23.166  2.313   1.000 29.212 ? 376 HOH AAA O   1 
HETATM 2416 O  O   . HOH N 5 .   ? 7.011   10.033  20.282  1.000 26.316 ? 377 HOH AAA O   1 
HETATM 2417 O  O   . HOH N 5 .   ? 18.102  14.004  9.552   1.000 26.086 ? 378 HOH AAA O   1 
HETATM 2418 O  O   . HOH N 5 .   ? 1.242   11.057  -5.999  1.000 15.916 ? 379 HOH AAA O   1 
HETATM 2419 O  O   . HOH N 5 .   ? 21.307  -1.954  7.326   1.000 32.674 ? 380 HOH AAA O   1 
HETATM 2420 O  O   . HOH N 5 .   ? -10.196 14.283  -0.862  1.000 15.484 ? 381 HOH AAA O   1 
HETATM 2421 O  O   . HOH N 5 .   ? 1.957   23.136  -2.382  1.000 19.813 ? 382 HOH AAA O   1 
HETATM 2422 O  O   . HOH N 5 .   ? -7.431  3.373   9.853   1.000 25.411 ? 383 HOH AAA O   1 
HETATM 2423 O  O   . HOH N 5 .   ? 10.856  5.399   17.370  1.000 23.969 ? 384 HOH AAA O   1 
HETATM 2424 O  O   . HOH N 5 .   ? 18.095  18.337  16.375  1.000 16.814 ? 385 HOH AAA O   1 
HETATM 2425 O  O   . HOH N 5 .   ? 19.082  -5.362  1.365   1.000 35.221 ? 386 HOH AAA O   1 
HETATM 2426 O  O   . HOH N 5 .   ? 4.215   18.864  -3.448  1.000 16.757 ? 387 HOH AAA O   1 
HETATM 2427 O  O   . HOH N 5 .   ? 16.697  17.186  6.842   1.000 28.955 ? 388 HOH AAA O   1 
HETATM 2428 O  O   . HOH N 5 .   ? 9.926   30.597  8.125   1.000 36.997 ? 389 HOH AAA O   1 
HETATM 2429 O  O   . HOH N 5 .   ? 15.817  24.212  4.496   1.000 22.496 ? 390 HOH AAA O   1 
HETATM 2430 O  O   . HOH N 5 .   ? 7.389   25.500  13.877  1.000 31.255 ? 391 HOH AAA O   1 
HETATM 2431 O  O   . HOH N 5 .   ? 10.757  -6.422  6.809   1.000 14.145 ? 392 HOH AAA O   1 
HETATM 2432 O  O   . HOH N 5 .   ? 7.322   -3.053  1.428   1.000 30.109 ? 393 HOH AAA O   1 
HETATM 2433 O  O   . HOH N 5 .   ? -3.862  1.049   11.342  1.000 13.387 ? 394 HOH AAA O   1 
HETATM 2434 O  O   . HOH N 5 .   ? 10.258  19.752  -0.949  1.000 13.739 ? 395 HOH AAA O   1 
HETATM 2435 O  O   . HOH N 5 .   ? 5.370   10.514  -7.808  1.000 27.471 ? 396 HOH AAA O   1 
HETATM 2436 O  O   . HOH N 5 .   ? -12.307 16.062  -7.604  1.000 26.588 ? 397 HOH AAA O   1 
HETATM 2437 O  O   . HOH N 5 .   ? -1.954  11.171  21.277  1.000 24.890 ? 398 HOH AAA O   1 
HETATM 2438 O  O   . HOH N 5 .   ? 14.670  13.007  0.980   1.000 19.412 ? 399 HOH AAA O   1 
HETATM 2439 O  O   . HOH N 5 .   ? 17.537  -1.809  5.757   1.000 24.890 ? 400 HOH AAA O   1 
HETATM 2440 O  O   . HOH N 5 .   ? 19.159  12.773  4.686   1.000 30.223 ? 401 HOH AAA O   1 
HETATM 2441 O  O   . HOH N 5 .   ? -0.267  33.588  11.422  1.000 28.784 ? 402 HOH AAA O   1 
HETATM 2442 O  O   . HOH N 5 .   ? 19.529  6.677   15.661  1.000 28.708 ? 403 HOH AAA O   1 
HETATM 2443 O  O   . HOH N 5 .   ? -7.796  23.711  8.108   1.000 36.573 ? 404 HOH AAA O   1 
HETATM 2444 O  O   . HOH N 5 .   ? -1.757  30.579  10.965  1.000 24.557 ? 405 HOH AAA O   1 
HETATM 2445 O  O   . HOH N 5 .   ? -9.034  15.768  11.070  1.000 22.180 ? 406 HOH AAA O   1 
HETATM 2446 O  O   . HOH N 5 .   ? -4.982  23.256  -0.997  1.000 19.345 ? 407 HOH AAA O   1 
HETATM 2447 O  O   . HOH N 5 .   ? 10.394  11.472  -4.230  1.000 19.656 ? 408 HOH AAA O   1 
HETATM 2448 O  O   . HOH N 5 .   ? 3.875   10.439  -5.064  1.000 12.978 ? 409 HOH AAA O   1 
HETATM 2449 O  O   . HOH N 5 .   ? 12.468  18.996  22.105  1.000 27.805 ? 410 HOH AAA O   1 
HETATM 2450 O  O   . HOH N 5 .   ? 13.973  24.791  16.385  1.000 41.386 ? 411 HOH AAA O   1 
HETATM 2451 O  O   . HOH N 5 .   ? -10.239 20.652  -13.825 1.000 25.528 ? 412 HOH AAA O   1 
HETATM 2452 O  O   . HOH N 5 .   ? -7.135  0.652   -1.105  1.000 26.843 ? 413 HOH AAA O   1 
HETATM 2453 O  O   . HOH N 5 .   ? 19.861  8.038   4.053   1.000 30.012 ? 414 HOH AAA O   1 
HETATM 2454 O  O   . HOH N 5 .   ? 10.439  10.382  18.609  1.000 28.085 ? 415 HOH AAA O   1 
HETATM 2455 O  O   . HOH N 5 .   ? -7.973  10.823  -14.460 1.000 31.613 ? 416 HOH AAA O   1 
HETATM 2456 O  O   . HOH N 5 .   ? 19.316  17.689  13.838  1.000 30.280 ? 417 HOH AAA O   1 
HETATM 2457 O  O   . HOH N 5 .   ? 8.713   18.614  -3.134  1.000 21.571 ? 418 HOH AAA O   1 
HETATM 2458 O  O   . HOH N 5 .   ? -6.674  21.694  13.294  1.000 39.748 ? 419 HOH AAA O   1 
HETATM 2459 O  O   . HOH N 5 .   ? 6.274   17.008  -2.497  1.000 10.860 ? 420 HOH AAA O   1 
HETATM 2460 O  O   . HOH N 5 .   ? -13.184 12.619  2.138   1.000 31.287 ? 421 HOH AAA O   1 
HETATM 2461 O  O   . HOH N 5 .   ? 3.323   13.422  -7.468  1.000 28.743 ? 422 HOH AAA O   1 
HETATM 2462 O  O   . HOH N 5 .   ? -9.561  12.420  12.026  1.000 29.848 ? 423 HOH AAA O   1 
HETATM 2463 O  O   . HOH N 5 .   ? 18.637  12.108  7.613   1.000 41.193 ? 424 HOH AAA O   1 
HETATM 2464 O  O   . HOH N 5 .   ? 5.293   -2.445  -7.425  1.000 38.516 ? 425 HOH AAA O   1 
HETATM 2465 O  O   . HOH N 5 .   ? 18.682  4.949   17.813  1.000 36.336 ? 426 HOH AAA O   1 
HETATM 2466 O  O   . HOH N 5 .   ? 20.511  2.048   -0.567  1.000 28.927 ? 427 HOH AAA O   1 
HETATM 2467 O  O   . HOH N 5 .   ? 20.154  4.034   11.896  1.000 31.057 ? 428 HOH AAA O   1 
HETATM 2468 O  O   . HOH N 5 .   ? 13.784  26.038  4.256   1.000 31.364 ? 429 HOH AAA O   1 
HETATM 2469 O  O   . HOH N 5 .   ? 3.885   17.016  -5.456  1.000 20.944 ? 430 HOH AAA O   1 
HETATM 2470 O  O   . HOH N 5 .   ? 19.854  6.870   13.358  1.000 35.576 ? 431 HOH AAA O   1 
HETATM 2471 O  O   . HOH N 5 .   ? 18.483  7.700   9.842   1.000 24.844 ? 432 HOH AAA O   1 
HETATM 2472 O  O   . HOH N 5 .   ? -1.939  29.891  13.664  1.000 26.629 ? 433 HOH AAA O   1 
HETATM 2473 O  O   . HOH N 5 .   ? 10.423  15.647  -3.685  1.000 31.223 ? 434 HOH AAA O   1 
HETATM 2474 O  O   . HOH N 5 .   ? 3.282   21.038  15.427  1.000 25.362 ? 435 HOH AAA O   1 
HETATM 2475 O  O   . HOH N 5 .   ? -12.037 15.204  17.321  1.000 24.628 ? 436 HOH AAA O   1 
HETATM 2476 O  O   . HOH N 5 .   ? 3.712   5.282   -9.733  1.000 31.668 ? 437 HOH AAA O   1 
HETATM 2477 O  O   . HOH N 5 .   ? -14.488 13.844  -1.970  1.000 29.635 ? 438 HOH AAA O   1 
HETATM 2478 O  O   . HOH N 5 .   ? -1.175  25.645  13.219  1.000 28.349 ? 439 HOH AAA O   1 
HETATM 2479 O  O   . HOH N 5 .   ? 9.413   13.459  -2.343  1.000 17.431 ? 440 HOH AAA O   1 
HETATM 2480 O  O   . HOH N 5 .   ? 11.981  -6.303  9.299   1.000 26.479 ? 441 HOH AAA O   1 
HETATM 2481 O  O   . HOH N 5 .   ? 11.895  -4.157  11.061  1.000 28.631 ? 442 HOH AAA O   1 
HETATM 2482 O  O   . HOH O 5 .   ? 10.447  -9.084  29.895  1.000 16.642 ? 301 HOH BBB O   1 
HETATM 2483 O  O   . HOH O 5 .   ? -17.428 -17.779 22.481  1.000 23.583 ? 302 HOH BBB O   1 
HETATM 2484 O  O   . HOH O 5 .   ? -1.272  -18.690 11.310  1.000 24.111 ? 303 HOH BBB O   1 
HETATM 2485 O  O   . HOH O 5 .   ? -21.097 -6.619  31.148  1.000 31.385 ? 304 HOH BBB O   1 
HETATM 2486 O  O   . HOH O 5 .   ? -3.944  -12.513 3.816   0.500 12.288 ? 305 HOH BBB O   1 
HETATM 2487 O  O   . HOH O 5 .   ? -14.833 -17.988 21.527  1.000 19.003 ? 306 HOH BBB O   1 
HETATM 2488 O  O   . HOH O 5 .   ? -21.989 -11.025 22.371  1.000 22.156 ? 307 HOH BBB O   1 
HETATM 2489 O  O   . HOH O 5 .   ? 1.802   -28.480 24.598  1.000 30.299 ? 308 HOH BBB O   1 
HETATM 2490 O  O   . HOH O 5 .   ? -15.064 -4.791  13.626  1.000 19.181 ? 309 HOH BBB O   1 
HETATM 2491 O  O   . HOH O 5 .   ? 10.930  -1.107  26.889  1.000 19.697 ? 310 HOH BBB O   1 
HETATM 2492 O  O   . HOH O 5 .   ? 0.299   -22.502 31.601  1.000 25.569 ? 311 HOH BBB O   1 
HETATM 2493 O  O   . HOH O 5 .   ? -14.073 -9.844  30.989  1.000 27.124 ? 312 HOH BBB O   1 
HETATM 2494 O  O   . HOH O 5 .   ? 3.621   -8.636  5.047   1.000 17.833 ? 313 HOH BBB O   1 
HETATM 2495 O  O   . HOH O 5 .   ? 14.953  -18.524 16.232  1.000 25.794 ? 314 HOH BBB O   1 
HETATM 2496 O  O   . HOH O 5 .   ? -0.395  -24.574 28.379  1.000 20.442 ? 315 HOH BBB O   1 
HETATM 2497 O  O   . HOH O 5 .   ? 14.561  -1.222  21.031  1.000 22.907 ? 316 HOH BBB O   1 
HETATM 2498 O  O   . HOH O 5 .   ? 14.190  -21.124 13.247  1.000 30.762 ? 317 HOH BBB O   1 
HETATM 2499 O  O   . HOH O 5 .   ? 12.746  -9.943  16.849  1.000 28.966 ? 318 HOH BBB O   1 
HETATM 2500 O  O   . HOH O 5 .   ? -6.314  -17.497 11.391  1.000 25.015 ? 319 HOH BBB O   1 
HETATM 2501 O  O   . HOH O 5 .   ? -13.687 -9.787  11.259  1.000 24.495 ? 320 HOH BBB O   1 
HETATM 2502 O  O   . HOH O 5 .   ? -3.893  0.227   16.131  1.000 8.262  ? 321 HOH BBB O   1 
HETATM 2503 O  O   . HOH O 5 .   ? -23.512 -5.537  25.249  1.000 27.251 ? 322 HOH BBB O   1 
HETATM 2504 O  O   . HOH O 5 .   ? 4.780   7.853   27.013  1.000 32.476 ? 323 HOH BBB O   1 
HETATM 2505 O  O   . HOH O 5 .   ? -10.383 -23.154 13.033  1.000 37.566 ? 324 HOH BBB O   1 
HETATM 2506 O  O   . HOH O 5 .   ? -1.817  3.349   25.635  1.000 24.779 ? 325 HOH BBB O   1 
HETATM 2507 O  O   . HOH O 5 .   ? 8.514   -5.459  16.507  1.000 14.598 ? 326 HOH BBB O   1 
HETATM 2508 O  O   . HOH O 5 .   ? -9.385  -3.821  32.088  1.000 25.167 ? 327 HOH BBB O   1 
HETATM 2509 O  O   . HOH O 5 .   ? 13.168  -5.231  26.672  1.000 17.899 ? 328 HOH BBB O   1 
HETATM 2510 O  O   . HOH O 5 .   ? -8.499  -27.196 20.817  1.000 20.912 ? 329 HOH BBB O   1 
HETATM 2511 O  O   . HOH O 5 .   ? 2.711   -26.739 21.800  1.000 23.220 ? 330 HOH BBB O   1 
HETATM 2512 O  O   . HOH O 5 .   ? -7.178  -1.256  13.532  1.000 14.113 ? 331 HOH BBB O   1 
HETATM 2513 O  O   . HOH O 5 .   ? 10.734  1.436   22.329  1.000 22.368 ? 332 HOH BBB O   1 
HETATM 2514 O  O   . HOH O 5 .   ? 12.404  -3.162  36.200  1.000 29.361 ? 333 HOH BBB O   1 
HETATM 2515 O  O   . HOH O 5 .   ? -9.208  -14.674 30.158  1.000 19.975 ? 334 HOH BBB O   1 
HETATM 2516 O  O   . HOH O 5 .   ? -3.726  -14.018 29.294  1.000 17.423 ? 335 HOH BBB O   1 
HETATM 2517 O  O   . HOH O 5 .   ? -5.224  5.077   26.068  1.000 20.377 ? 336 HOH BBB O   1 
HETATM 2518 O  O   . HOH O 5 .   ? 9.179   -16.790 20.043  1.000 10.367 ? 337 HOH BBB O   1 
HETATM 2519 O  O   . HOH O 5 .   ? 4.824   -22.652 33.817  1.000 22.909 ? 338 HOH BBB O   1 
HETATM 2520 O  O   . HOH O 5 .   ? 4.486   -10.866 34.275  1.000 25.486 ? 339 HOH BBB O   1 
HETATM 2521 O  O   . HOH O 5 .   ? -3.190  -15.706 7.804   1.000 14.393 ? 340 HOH BBB O   1 
HETATM 2522 O  O   . HOH O 5 .   ? -27.343 -7.270  29.958  1.000 19.901 ? 341 HOH BBB O   1 
HETATM 2523 O  O   . HOH O 5 .   ? 6.484   -20.293 14.103  1.000 19.840 ? 342 HOH BBB O   1 
HETATM 2524 O  O   . HOH O 5 .   ? 9.461   -18.280 27.035  1.000 20.320 ? 343 HOH BBB O   1 
HETATM 2525 O  O   . HOH O 5 .   ? 4.211   -18.677 14.933  1.000 22.259 ? 344 HOH BBB O   1 
HETATM 2526 O  O   . HOH O 5 .   ? 9.393   -17.492 22.653  1.000 13.697 ? 345 HOH BBB O   1 
HETATM 2527 O  O   . HOH O 5 .   ? 0.933   -13.030 30.859  1.000 14.015 ? 346 HOH BBB O   1 
HETATM 2528 O  O   . HOH O 5 .   ? 15.039  -8.066  16.339  1.000 24.708 ? 347 HOH BBB O   1 
HETATM 2529 O  O   . HOH O 5 .   ? -1.456  -18.166 23.957  1.000 10.109 ? 348 HOH BBB O   1 
HETATM 2530 O  O   . HOH O 5 .   ? 10.779  -7.259  17.613  1.000 26.081 ? 349 HOH BBB O   1 
HETATM 2531 O  O   . HOH O 5 .   ? -11.652 -2.395  30.942  1.000 19.972 ? 350 HOH BBB O   1 
HETATM 2532 O  O   . HOH O 5 .   ? 9.296   -10.307 11.226  1.000 27.153 ? 351 HOH BBB O   1 
HETATM 2533 O  O   . HOH O 5 .   ? 3.804   -25.233 24.603  1.000 20.283 ? 352 HOH BBB O   1 
HETATM 2534 O  O   . HOH O 5 .   ? 15.586  -1.763  32.532  1.000 33.858 ? 353 HOH BBB O   1 
HETATM 2535 O  O   . HOH O 5 .   ? -6.168  -13.004 30.096  1.000 20.798 ? 354 HOH BBB O   1 
HETATM 2536 O  O   . HOH O 5 .   ? -26.125 -8.251  26.494  1.000 23.375 ? 355 HOH BBB O   1 
HETATM 2537 O  O   . HOH O 5 .   ? 8.634   -7.904  29.667  1.000 19.811 ? 356 HOH BBB O   1 
HETATM 2538 O  O   . HOH O 5 .   ? 6.528   -17.460 30.133  1.000 16.263 ? 357 HOH BBB O   1 
HETATM 2539 O  O   . HOH O 5 .   ? -1.538  -30.707 22.602  1.000 18.030 ? 358 HOH BBB O   1 
HETATM 2540 O  O   . HOH O 5 .   ? -0.733  -2.657  7.721   1.000 9.757  ? 359 HOH BBB O   1 
HETATM 2541 O  O   . HOH O 5 .   ? -9.866  -24.373 20.557  1.000 23.032 ? 360 HOH BBB O   1 
HETATM 2542 O  O   . HOH O 5 .   ? -7.596  -3.257  11.609  1.000 17.394 ? 361 HOH BBB O   1 
HETATM 2543 O  O   . HOH O 5 .   ? 16.958  -7.697  22.154  1.000 21.214 ? 362 HOH BBB O   1 
HETATM 2544 O  O   . HOH O 5 .   ? 17.097  -4.116  28.852  1.000 32.956 ? 363 HOH BBB O   1 
HETATM 2545 O  O   . HOH O 5 .   ? -0.146  -31.535 20.450  1.000 24.962 ? 364 HOH BBB O   1 
HETATM 2546 O  O   . HOH O 5 .   ? -18.747 -11.724 17.616  1.000 28.630 ? 365 HOH BBB O   1 
HETATM 2547 O  O   . HOH O 5 .   ? 7.672   -14.573 13.959  1.000 14.015 ? 366 HOH BBB O   1 
HETATM 2548 O  O   . HOH O 5 .   ? 13.236  -7.607  23.928  1.000 19.851 ? 367 HOH BBB O   1 
HETATM 2549 O  O   . HOH O 5 .   ? 8.024   -2.487  33.416  1.000 19.112 ? 368 HOH BBB O   1 
HETATM 2550 O  O   . HOH O 5 .   ? 10.799  -9.500  27.467  1.000 21.597 ? 369 HOH BBB O   1 
HETATM 2551 O  O   . HOH O 5 .   ? 5.602   8.810   22.534  1.000 25.189 ? 370 HOH BBB O   1 
HETATM 2552 O  O   . HOH O 5 .   ? -2.123  -30.089 11.505  1.000 22.011 ? 371 HOH BBB O   1 
HETATM 2553 O  O   . HOH O 5 .   ? -7.530  -22.989 27.158  1.000 17.239 ? 372 HOH BBB O   1 
HETATM 2554 O  O   . HOH O 5 .   ? -20.419 -6.079  23.541  1.000 17.015 ? 373 HOH BBB O   1 
HETATM 2555 O  O   . HOH O 5 .   ? 1.393   -19.486 14.744  1.000 16.217 ? 374 HOH BBB O   1 
HETATM 2556 O  O   . HOH O 5 .   ? -1.400  8.307   25.194  1.000 22.442 ? 375 HOH BBB O   1 
HETATM 2557 O  O   . HOH O 5 .   ? -17.248 -4.055  10.738  1.000 32.521 ? 376 HOH BBB O   1 
HETATM 2558 O  O   . HOH O 5 .   ? 4.947   -27.588 15.855  1.000 40.847 ? 377 HOH BBB O   1 
HETATM 2559 O  O   . HOH O 5 .   ? -12.563 -16.952 32.194  1.000 8.637  ? 378 HOH BBB O   1 
HETATM 2560 O  O   . HOH O 5 .   ? -8.704  -12.337 4.117   1.000 26.258 ? 379 HOH BBB O   1 
HETATM 2561 O  O   . HOH O 5 .   ? 11.031  -6.080  15.722  1.000 22.012 ? 380 HOH BBB O   1 
HETATM 2562 O  O   . HOH O 5 .   ? -3.662  -7.485  9.891   1.000 15.381 ? 381 HOH BBB O   1 
HETATM 2563 O  O   . HOH O 5 .   ? -15.553 -8.376  13.887  1.000 20.220 ? 382 HOH BBB O   1 
HETATM 2564 O  O   . HOH O 5 .   ? -17.195 -13.383 18.948  1.000 18.691 ? 383 HOH BBB O   1 
HETATM 2565 O  O   . HOH O 5 .   ? 5.452   5.959   24.762  1.000 16.941 ? 384 HOH BBB O   1 
HETATM 2566 O  O   . HOH O 5 .   ? -10.345 -10.781 29.578  1.000 15.904 ? 385 HOH BBB O   1 
HETATM 2567 O  O   . HOH O 5 .   ? -3.792  -30.667 13.680  1.000 18.204 ? 386 HOH BBB O   1 
HETATM 2568 O  O   . HOH O 5 .   ? 4.490   -13.655 31.449  1.000 15.330 ? 387 HOH BBB O   1 
HETATM 2569 O  O   . HOH O 5 .   ? -16.728 -16.084 18.070  1.000 22.449 ? 388 HOH BBB O   1 
HETATM 2570 O  O   . HOH O 5 .   ? -6.821  -18.874 29.105  1.000 17.571 ? 389 HOH BBB O   1 
HETATM 2571 O  O   . HOH O 5 .   ? -0.510  -19.975 30.386  1.000 19.126 ? 390 HOH BBB O   1 
HETATM 2572 O  O   . HOH O 5 .   ? 3.100   -5.654  2.281   1.000 26.213 ? 391 HOH BBB O   1 
HETATM 2573 O  O   . HOH O 5 .   ? -4.404  -0.520  13.552  1.000 11.892 ? 392 HOH BBB O   1 
HETATM 2574 O  O   . HOH O 5 .   ? 0.836   -4.433  0.616   1.000 17.387 ? 393 HOH BBB O   1 
HETATM 2575 O  O   . HOH O 5 .   ? -7.709  -32.542 14.887  1.000 28.870 ? 394 HOH BBB O   1 
HETATM 2576 O  O   . HOH O 5 .   ? 2.239   -11.132 5.203   1.000 19.665 ? 395 HOH BBB O   1 
HETATM 2577 O  O   . HOH O 5 .   ? -14.441 -6.146  34.574  1.000 25.762 ? 396 HOH BBB O   1 
HETATM 2578 O  O   . HOH O 5 .   ? -6.931  -0.997  8.341   1.000 25.692 ? 397 HOH BBB O   1 
HETATM 2579 O  O   . HOH O 5 .   ? -11.584 -9.760  10.451  1.000 27.832 ? 398 HOH BBB O   1 
HETATM 2580 O  O   . HOH O 5 .   ? 9.585   -22.955 15.727  1.000 36.710 ? 399 HOH BBB O   1 
HETATM 2581 O  O   . HOH O 5 .   ? -13.655 -22.451 21.577  1.000 22.354 ? 400 HOH BBB O   1 
HETATM 2582 O  O   . HOH O 5 .   ? -3.194  -5.355  11.550  1.000 19.298 ? 401 HOH BBB O   1 
HETATM 2583 O  O   . HOH O 5 .   ? 5.296   11.114  24.298  1.000 27.764 ? 402 HOH BBB O   1 
HETATM 2584 O  O   . HOH O 5 .   ? -8.701  -11.310 6.616   1.000 27.784 ? 403 HOH BBB O   1 
HETATM 2585 O  O   . HOH O 5 .   ? 4.951   -22.743 15.631  1.000 14.959 ? 404 HOH BBB O   1 
HETATM 2586 O  O   . HOH O 5 .   ? -22.783 -14.442 23.834  1.000 23.001 ? 405 HOH BBB O   1 
HETATM 2587 O  O   . HOH O 5 .   ? -10.096 -8.282  8.701   1.000 22.864 ? 406 HOH BBB O   1 
HETATM 2588 O  O   . HOH O 5 .   ? -9.135  -5.562  9.919   1.000 26.834 ? 407 HOH BBB O   1 
HETATM 2589 O  O   . HOH O 5 .   ? -9.570  -15.034 9.617   1.000 19.911 ? 408 HOH BBB O   1 
HETATM 2590 O  O   . HOH O 5 .   ? -9.474  -10.175 1.900   1.000 22.956 ? 409 HOH BBB O   1 
HETATM 2591 O  O   . HOH O 5 .   ? -1.841  -11.843 33.450  1.000 23.543 ? 410 HOH BBB O   1 
HETATM 2592 O  O   . HOH O 5 .   ? -9.244  -11.979 8.786   1.000 22.710 ? 411 HOH BBB O   1 
HETATM 2593 O  O   . HOH O 5 .   ? 15.974  -3.095  37.864  1.000 31.228 ? 412 HOH BBB O   1 
HETATM 2594 O  O   . HOH O 5 .   ? 3.538   -0.401  33.541  1.000 37.509 ? 413 HOH BBB O   1 
HETATM 2595 O  O   . HOH O 5 .   ? -20.732 -11.995 33.087  1.000 25.746 ? 414 HOH BBB O   1 
HETATM 2596 O  O   . HOH O 5 .   ? -7.656  -10.531 30.409  1.000 14.443 ? 415 HOH BBB O   1 
HETATM 2597 O  O   . HOH O 5 .   ? 11.936  -8.610  11.838  1.000 36.365 ? 416 HOH BBB O   1 
HETATM 2598 O  O   . HOH O 5 .   ? 0.568   -10.079 3.285   1.000 29.397 ? 417 HOH BBB O   1 
HETATM 2599 O  O   . HOH O 5 .   ? -9.145  -1.994  9.646   1.000 25.568 ? 418 HOH BBB O   1 
HETATM 2600 O  O   . HOH O 5 .   ? -4.448  -17.134 29.436  1.000 13.873 ? 419 HOH BBB O   1 
HETATM 2601 O  O   . HOH O 5 .   ? -2.725  -34.359 14.314  1.000 27.602 ? 420 HOH BBB O   1 
HETATM 2602 O  O   . HOH O 5 .   ? -4.878  -3.098  11.239  1.000 16.545 ? 421 HOH BBB O   1 
HETATM 2603 O  O   . HOH O 5 .   ? 11.758  -11.060 14.671  1.000 28.190 ? 422 HOH BBB O   1 
HETATM 2604 O  O   . HOH O 5 .   ? -5.530  -17.061 8.624   1.000 26.136 ? 423 HOH BBB O   1 
HETATM 2605 O  O   . HOH O 5 .   ? -8.097  -16.688 9.475   1.000 35.533 ? 424 HOH BBB O   1 
HETATM 2606 O  O   . HOH O 5 .   ? 18.211  -3.342  23.582  1.000 31.808 ? 425 HOH BBB O   1 
HETATM 2607 O  O   . HOH O 5 .   ? -2.248  5.759   26.304  1.000 29.347 ? 426 HOH BBB O   1 
HETATM 2608 O  O   . HOH O 5 .   ? 12.489  -5.719  13.254  1.000 27.739 ? 427 HOH BBB O   1 
HETATM 2609 O  O   . HOH O 5 .   ? -8.025  -16.976 30.784  1.000 21.134 ? 428 HOH BBB O   1 
HETATM 2610 O  O   . HOH O 5 .   ? -9.372  -13.229 32.370  1.000 30.809 ? 429 HOH BBB O   1 
HETATM 2611 O  O   . HOH O 5 .   ? -9.790  -27.930 18.459  1.000 28.137 ? 430 HOH BBB O   1 
HETATM 2612 O  O   . HOH O 5 .   ? -9.828  -24.977 23.819  1.000 27.303 ? 431 HOH BBB O   1 
HETATM 2613 O  O   . HOH O 5 .   ? -4.193  -0.992  9.624   1.000 15.304 ? 432 HOH BBB O   1 
HETATM 2614 O  O   . HOH O 5 .   ? -22.336 -17.267 22.569  1.000 43.382 ? 433 HOH BBB O   1 
HETATM 2615 O  O   . HOH O 5 .   ? -16.753 -10.919 13.862  1.000 32.520 ? 434 HOH BBB O   1 
HETATM 2616 O  O   . HOH O 5 .   ? 4.374   -26.593 28.022  1.000 26.847 ? 435 HOH BBB O   1 
HETATM 2617 O  O   . HOH O 5 .   ? 13.279  1.235   21.740  1.000 28.412 ? 436 HOH BBB O   1 
HETATM 2618 O  O   . HOH O 5 .   ? 9.896   -16.568 25.024  1.000 27.989 ? 437 HOH BBB O   1 
HETATM 2619 O  O   . HOH O 5 .   ? 0.806   -20.843 12.134  1.000 28.109 ? 438 HOH BBB O   1 
HETATM 2620 O  O   . HOH O 5 .   ? -6.589  -17.835 5.413   1.000 33.110 ? 439 HOH BBB O   1 
HETATM 2621 O  O   . HOH O 5 .   ? -1.683  -13.779 31.219  1.000 16.342 ? 440 HOH BBB O   1 
HETATM 2622 O  O   . HOH O 5 .   ? 8.640   -2.509  36.183  1.000 29.928 ? 441 HOH BBB O   1 
HETATM 2623 O  O   . HOH O 5 .   ? 7.918   5.586   23.262  1.000 28.609 ? 442 HOH BBB O   1 
HETATM 2624 O  O   . HOH O 5 .   ? 8.632   3.423   21.871  1.000 32.641 ? 443 HOH BBB O   1 
HETATM 2625 O  O   . HOH O 5 .   ? -7.989  1.374   12.876  1.000 18.860 ? 444 HOH BBB O   1 
HETATM 2626 O  O   . HOH O 5 .   ? -18.204 -12.200 15.284  1.000 32.760 ? 445 HOH BBB O   1 
HETATM 2627 O  O   . HOH O 5 .   ? -17.698 -15.125 15.215  1.000 34.107 ? 446 HOH BBB 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 AAA . n 
A 1 2   THR 2   2   2   THR THR AAA . n 
A 1 3   LYS 3   3   3   LYS LYS AAA . n 
A 1 4   VAL 4   4   4   VAL VAL AAA . n 
A 1 5   VAL 5   5   5   VAL VAL AAA . n 
A 1 6   CYS 6   6   6   CYS CYS AAA . n 
A 1 7   VAL 7   7   7   VAL VAL AAA . n 
A 1 8   LEU 8   8   8   LEU LEU AAA . n 
A 1 9   LYS 9   9   9   LYS LYS AAA . n 
A 1 10  GLY 10  10  10  GLY GLY AAA . n 
A 1 11  ASP 11  11  11  ASP ASP AAA . n 
A 1 12  GLY 12  12  12  GLY GLY AAA . n 
A 1 13  PRO 13  13  13  PRO PRO AAA . n 
A 1 14  VAL 14  14  14  VAL VAL AAA . n 
A 1 15  GLN 15  15  15  GLN GLN AAA . n 
A 1 16  GLY 16  16  16  GLY GLY AAA . n 
A 1 17  ILE 17  17  17  ILE ILE AAA . n 
A 1 18  ILE 18  18  18  ILE ILE AAA . n 
A 1 19  ASN 19  19  19  ASN ASN AAA . n 
A 1 20  PHE 20  20  20  PHE PHE AAA . n 
A 1 21  GLU 21  21  21  GLU GLU AAA . n 
A 1 22  GLN 22  22  22  GLN GLN AAA . n 
A 1 23  LYS 23  23  23  LYS LYS AAA . n 
A 1 24  GLU 24  24  24  GLU GLU AAA . n 
A 1 25  SER 25  25  25  SER SER AAA . n 
A 1 26  ASN 26  26  26  ASN ASN AAA . n 
A 1 27  GLY 27  27  27  GLY GLY AAA . n 
A 1 28  PRO 28  28  28  PRO PRO AAA . n 
A 1 29  VAL 29  29  29  VAL VAL AAA . n 
A 1 30  LYS 30  30  30  LYS LYS AAA . n 
A 1 31  VAL 31  31  31  VAL VAL AAA . n 
A 1 32  TRP 32  32  32  TRP TRP AAA . n 
A 1 33  GLY 33  33  33  GLY GLY AAA . n 
A 1 34  SER 34  34  34  SER SER AAA . n 
A 1 35  ILE 35  35  35  ILE ILE AAA . n 
A 1 36  LYS 36  36  36  LYS LYS AAA . n 
A 1 37  GLY 37  37  37  GLY GLY AAA . n 
A 1 38  LEU 38  38  38  LEU LEU AAA . n 
A 1 39  THR 39  39  39  THR THR AAA . n 
A 1 40  GLU 40  40  40  GLU GLU AAA . n 
A 1 41  GLY 41  41  41  GLY GLY AAA . n 
A 1 42  LEU 42  42  42  LEU LEU AAA . n 
A 1 43  HIS 43  43  43  HIS HIS AAA . n 
A 1 44  GLY 44  44  44  GLY GLY AAA . n 
A 1 45  PHE 45  45  45  PHE PHE AAA . n 
A 1 46  HIS 46  46  46  HIS HIS AAA . n 
A 1 47  VAL 47  47  47  VAL VAL AAA . n 
A 1 48  HIS 48  48  48  HIS HIS AAA . n 
A 1 49  GLU 49  49  49  GLU GLU AAA . n 
A 1 50  PHE 50  50  50  PHE PHE AAA . n 
A 1 51  GLY 51  51  51  GLY GLY AAA . n 
A 1 52  ASP 52  52  52  ASP ASP AAA . n 
A 1 53  ASN 53  53  53  ASN ASN AAA . n 
A 1 54  THR 54  54  54  THR THR AAA . n 
A 1 55  ALA 55  55  55  ALA ALA AAA . n 
A 1 56  GLY 56  56  56  GLY GLY AAA . n 
A 1 57  CYS 57  57  57  CYS CYS AAA . n 
A 1 58  THR 58  58  58  THR THR AAA . n 
A 1 59  SER 59  59  59  SER SER AAA . n 
A 1 60  ALA 60  60  60  ALA ALA AAA . n 
A 1 61  GLY 61  61  61  GLY GLY AAA . n 
A 1 62  PRO 62  62  62  PRO PRO AAA . n 
A 1 63  HIS 63  63  63  HIS HIS AAA . n 
A 1 64  PHE 64  64  64  PHE PHE AAA . n 
A 1 65  ASN 65  65  65  ASN ASN AAA . n 
A 1 66  PRO 66  66  66  PRO PRO AAA . n 
A 1 67  LEU 67  67  67  LEU LEU AAA . n 
A 1 68  SER 68  68  68  SER SER AAA . n 
A 1 69  ARG 69  69  69  ARG ARG AAA . n 
A 1 70  LYS 70  70  70  LYS LYS AAA . n 
A 1 71  HIS 71  71  71  HIS HIS AAA . n 
A 1 72  GLY 72  72  72  GLY GLY AAA . n 
A 1 73  GLY 73  73  73  GLY GLY AAA . n 
A 1 74  PRO 74  74  74  PRO PRO AAA . n 
A 1 75  LYS 75  75  75  LYS LYS AAA . n 
A 1 76  ASP 76  76  76  ASP ASP AAA . n 
A 1 77  GLU 77  77  77  GLU GLU AAA . n 
A 1 78  GLU 78  78  78  GLU GLU AAA . n 
A 1 79  ARG 79  79  79  ARG ARG AAA . n 
A 1 80  HIS 80  80  80  HIS HIS AAA . n 
A 1 81  VAL 81  81  81  VAL VAL AAA . n 
A 1 82  GLY 82  82  82  GLY GLY AAA . n 
A 1 83  ASP 83  83  83  ASP ASP AAA . n 
A 1 84  LEU 84  84  84  LEU LEU AAA . n 
A 1 85  GLY 85  85  85  GLY GLY AAA . n 
A 1 86  ASN 86  86  86  ASN ASN AAA . n 
A 1 87  VAL 87  87  87  VAL VAL AAA . n 
A 1 88  THR 88  88  88  THR THR AAA . n 
A 1 89  ALA 89  89  89  ALA ALA AAA . n 
A 1 90  ASP 90  90  90  ASP ASP AAA . n 
A 1 91  LYS 91  91  91  LYS LYS AAA . n 
A 1 92  ASP 92  92  92  ASP ASP AAA . n 
A 1 93  GLY 93  93  93  GLY GLY AAA . n 
A 1 94  VAL 94  94  94  VAL VAL AAA . n 
A 1 95  ALA 95  95  95  ALA ALA AAA . n 
A 1 96  ASP 96  96  96  ASP ASP AAA . n 
A 1 97  VAL 97  97  97  VAL VAL AAA . n 
A 1 98  SER 98  98  98  SER SER AAA . n 
A 1 99  ILE 99  99  99  ILE ILE AAA . n 
A 1 100 GLU 100 100 100 GLU GLU AAA . n 
A 1 101 ASP 101 101 101 ASP ASP AAA . n 
A 1 102 SER 102 102 102 SER SER AAA . n 
A 1 103 VAL 103 103 103 VAL VAL AAA . n 
A 1 104 ILE 104 104 104 ILE ILE AAA . n 
A 1 105 SER 105 105 105 SER SER AAA . n 
A 1 106 LEU 106 106 106 LEU LEU AAA . n 
A 1 107 SER 107 107 107 SER SER AAA . n 
A 1 108 GLY 108 108 108 GLY GLY AAA . n 
A 1 109 ASP 109 109 109 ASP ASP AAA . n 
A 1 110 HIS 110 110 110 HIS HIS AAA . n 
A 1 111 CYS 111 111 111 CYS CYS AAA . n 
A 1 112 ILE 112 112 112 ILE ILE AAA . n 
A 1 113 ILE 113 113 113 ILE ILE AAA . n 
A 1 114 GLY 114 114 114 GLY GLY AAA . n 
A 1 115 ARG 115 115 115 ARG ARG AAA . n 
A 1 116 THR 116 116 116 THR THR AAA . n 
A 1 117 LEU 117 117 117 LEU LEU AAA . n 
A 1 118 VAL 118 118 118 VAL VAL AAA . n 
A 1 119 VAL 119 119 119 VAL VAL AAA . n 
A 1 120 HIS 120 120 120 HIS HIS AAA . n 
A 1 121 GLU 121 121 121 GLU GLU AAA . n 
A 1 122 LYS 122 122 122 LYS LYS AAA . n 
A 1 123 ALA 123 123 123 ALA ALA AAA . n 
A 1 124 ASP 124 124 124 ASP ASP AAA . n 
A 1 125 ASP 125 125 125 ASP ASP AAA . n 
A 1 126 LEU 126 126 126 LEU LEU AAA . n 
A 1 127 GLY 127 127 127 GLY GLY AAA . n 
A 1 128 LYS 128 128 128 LYS LYS AAA . n 
A 1 129 GLY 129 129 129 GLY GLY AAA . n 
A 1 130 GLY 130 130 130 GLY GLY AAA . n 
A 1 131 ASN 131 131 131 ASN ASN AAA . n 
A 1 132 GLU 132 132 132 GLU GLU AAA . n 
A 1 133 GLU 133 133 133 GLU GLU AAA . n 
A 1 134 SER 134 134 134 SER SER AAA . n 
A 1 135 THR 135 135 135 THR THR AAA . n 
A 1 136 LYS 136 136 136 LYS LYS AAA . n 
A 1 137 THR 137 137 137 THR THR AAA . n 
A 1 138 GLY 138 138 138 GLY GLY AAA . n 
A 1 139 ASN 139 139 139 ASN ASN AAA . n 
A 1 140 ALA 140 140 140 ALA ALA AAA . n 
A 1 141 GLY 141 141 141 GLY GLY AAA . n 
A 1 142 SER 142 142 142 SER SER AAA . n 
A 1 143 ARG 143 143 143 ARG ARG AAA . n 
A 1 144 LEU 144 144 144 LEU LEU AAA . n 
A 1 145 ALA 145 145 145 ALA ALA AAA . n 
A 1 146 CYS 146 146 146 CYS CYS AAA . n 
A 1 147 GLY 147 147 147 GLY GLY AAA . n 
A 1 148 VAL 148 148 148 VAL VAL AAA . n 
A 1 149 ILE 149 149 149 ILE ILE AAA . n 
A 1 150 GLY 150 150 150 GLY GLY AAA . n 
A 1 151 ILE 151 151 151 ILE ILE AAA . n 
A 1 152 ALA 152 152 152 ALA ALA AAA . n 
A 1 153 GLN 153 153 153 GLN GLN AAA . n 
B 1 1   ALA 1   1   1   ALA ALA BBB . n 
B 1 2   THR 2   2   2   THR THR BBB . n 
B 1 3   LYS 3   3   3   LYS LYS BBB . n 
B 1 4   VAL 4   4   4   VAL VAL BBB . n 
B 1 5   VAL 5   5   5   VAL VAL BBB . n 
B 1 6   CYS 6   6   6   CYS CYS BBB . n 
B 1 7   VAL 7   7   7   VAL VAL BBB . n 
B 1 8   LEU 8   8   8   LEU LEU BBB . n 
B 1 9   LYS 9   9   9   LYS LYS BBB . n 
B 1 10  GLY 10  10  10  GLY GLY BBB . n 
B 1 11  ASP 11  11  11  ASP ASP BBB . n 
B 1 12  GLY 12  12  12  GLY GLY BBB . n 
B 1 13  PRO 13  13  13  PRO PRO BBB . n 
B 1 14  VAL 14  14  14  VAL VAL BBB . n 
B 1 15  GLN 15  15  15  GLN GLN BBB . n 
B 1 16  GLY 16  16  16  GLY GLY BBB . n 
B 1 17  ILE 17  17  17  ILE ILE BBB . n 
B 1 18  ILE 18  18  18  ILE ILE BBB . n 
B 1 19  ASN 19  19  19  ASN ASN BBB . n 
B 1 20  PHE 20  20  20  PHE PHE BBB . n 
B 1 21  GLU 21  21  21  GLU GLU BBB . n 
B 1 22  GLN 22  22  22  GLN GLN BBB . n 
B 1 23  LYS 23  23  23  LYS LYS BBB . n 
B 1 24  GLU 24  24  24  GLU GLU BBB . n 
B 1 25  SER 25  25  25  SER SER BBB . n 
B 1 26  ASN 26  26  26  ASN ASN BBB . n 
B 1 27  GLY 27  27  27  GLY GLY BBB . n 
B 1 28  PRO 28  28  28  PRO PRO BBB . n 
B 1 29  VAL 29  29  29  VAL VAL BBB . n 
B 1 30  LYS 30  30  30  LYS LYS BBB . n 
B 1 31  VAL 31  31  31  VAL VAL BBB . n 
B 1 32  TRP 32  32  32  TRP TRP BBB . n 
B 1 33  GLY 33  33  33  GLY GLY BBB . n 
B 1 34  SER 34  34  34  SER SER BBB . n 
B 1 35  ILE 35  35  35  ILE ILE BBB . n 
B 1 36  LYS 36  36  36  LYS LYS BBB . n 
B 1 37  GLY 37  37  37  GLY GLY BBB . n 
B 1 38  LEU 38  38  38  LEU LEU BBB . n 
B 1 39  THR 39  39  39  THR THR BBB . n 
B 1 40  GLU 40  40  40  GLU GLU BBB . n 
B 1 41  GLY 41  41  41  GLY GLY BBB . n 
B 1 42  LEU 42  42  42  LEU LEU BBB . n 
B 1 43  HIS 43  43  43  HIS HIS BBB . n 
B 1 44  GLY 44  44  44  GLY GLY BBB . n 
B 1 45  PHE 45  45  45  PHE PHE BBB . n 
B 1 46  HIS 46  46  46  HIS HIS BBB . n 
B 1 47  VAL 47  47  47  VAL VAL BBB . n 
B 1 48  HIS 48  48  48  HIS HIS BBB . n 
B 1 49  GLU 49  49  49  GLU GLU BBB . n 
B 1 50  PHE 50  50  50  PHE PHE BBB . n 
B 1 51  GLY 51  51  51  GLY GLY BBB . n 
B 1 52  ASP 52  52  52  ASP ASP BBB . n 
B 1 53  ASN 53  53  53  ASN ASN BBB . n 
B 1 54  THR 54  54  54  THR THR BBB . n 
B 1 55  ALA 55  55  55  ALA ALA BBB . n 
B 1 56  GLY 56  56  56  GLY GLY BBB . n 
B 1 57  CYS 57  57  57  CYS CYS BBB . n 
B 1 58  THR 58  58  58  THR THR BBB . n 
B 1 59  SER 59  59  59  SER SER BBB . n 
B 1 60  ALA 60  60  60  ALA ALA BBB . n 
B 1 61  GLY 61  61  61  GLY GLY BBB . n 
B 1 62  PRO 62  62  62  PRO PRO BBB . n 
B 1 63  HIS 63  63  63  HIS HIS BBB . n 
B 1 64  PHE 64  64  64  PHE PHE BBB . n 
B 1 65  ASN 65  65  65  ASN ASN BBB . n 
B 1 66  PRO 66  66  66  PRO PRO BBB . n 
B 1 67  LEU 67  67  67  LEU LEU BBB . n 
B 1 68  SER 68  68  68  SER SER BBB . n 
B 1 69  ARG 69  69  69  ARG ARG BBB . n 
B 1 70  LYS 70  70  70  LYS LYS BBB . n 
B 1 71  HIS 71  71  71  HIS HIS BBB . n 
B 1 72  GLY 72  72  72  GLY GLY BBB . n 
B 1 73  GLY 73  73  73  GLY GLY BBB . n 
B 1 74  PRO 74  74  74  PRO PRO BBB . n 
B 1 75  LYS 75  75  75  LYS LYS BBB . n 
B 1 76  ASP 76  76  76  ASP ASP BBB . n 
B 1 77  GLU 77  77  77  GLU GLU BBB . n 
B 1 78  GLU 78  78  78  GLU GLU BBB . n 
B 1 79  ARG 79  79  79  ARG ARG BBB . n 
B 1 80  HIS 80  80  80  HIS HIS BBB . n 
B 1 81  VAL 81  81  81  VAL VAL BBB . n 
B 1 82  GLY 82  82  82  GLY GLY BBB . n 
B 1 83  ASP 83  83  83  ASP ASP BBB . n 
B 1 84  LEU 84  84  84  LEU LEU BBB . n 
B 1 85  GLY 85  85  85  GLY GLY BBB . n 
B 1 86  ASN 86  86  86  ASN ASN BBB . n 
B 1 87  VAL 87  87  87  VAL VAL BBB . n 
B 1 88  THR 88  88  88  THR THR BBB . n 
B 1 89  ALA 89  89  89  ALA ALA BBB . n 
B 1 90  ASP 90  90  90  ASP ASP BBB . n 
B 1 91  LYS 91  91  91  LYS LYS BBB . n 
B 1 92  ASP 92  92  92  ASP ASP BBB . n 
B 1 93  GLY 93  93  93  GLY GLY BBB . n 
B 1 94  VAL 94  94  94  VAL VAL BBB . n 
B 1 95  ALA 95  95  95  ALA ALA BBB . n 
B 1 96  ASP 96  96  96  ASP ASP BBB . n 
B 1 97  VAL 97  97  97  VAL VAL BBB . n 
B 1 98  SER 98  98  98  SER SER BBB . n 
B 1 99  ILE 99  99  99  ILE ILE BBB . n 
B 1 100 GLU 100 100 100 GLU GLU BBB . n 
B 1 101 ASP 101 101 101 ASP ASP BBB . n 
B 1 102 SER 102 102 102 SER SER BBB . n 
B 1 103 VAL 103 103 103 VAL VAL BBB . n 
B 1 104 ILE 104 104 104 ILE ILE BBB . n 
B 1 105 SER 105 105 105 SER SER BBB . n 
B 1 106 LEU 106 106 106 LEU LEU BBB . n 
B 1 107 SER 107 107 107 SER SER BBB . n 
B 1 108 GLY 108 108 108 GLY GLY BBB . n 
B 1 109 ASP 109 109 109 ASP ASP BBB . n 
B 1 110 HIS 110 110 110 HIS HIS BBB . n 
B 1 111 CYS 111 111 111 CYS CYS BBB . n 
B 1 112 ILE 112 112 112 ILE ILE BBB . n 
B 1 113 ILE 113 113 113 ILE ILE BBB . n 
B 1 114 GLY 114 114 114 GLY GLY BBB . n 
B 1 115 ARG 115 115 115 ARG ARG BBB . n 
B 1 116 THR 116 116 116 THR THR BBB . n 
B 1 117 LEU 117 117 117 LEU LEU BBB . n 
B 1 118 VAL 118 118 118 VAL VAL BBB . n 
B 1 119 VAL 119 119 119 VAL VAL BBB . n 
B 1 120 HIS 120 120 120 HIS HIS BBB . n 
B 1 121 GLU 121 121 121 GLU GLU BBB . n 
B 1 122 LYS 122 122 122 LYS LYS BBB . n 
B 1 123 ALA 123 123 123 ALA ALA BBB . n 
B 1 124 ASP 124 124 124 ASP ASP BBB . n 
B 1 125 ASP 125 125 125 ASP ASP BBB . n 
B 1 126 LEU 126 126 126 LEU LEU BBB . n 
B 1 127 GLY 127 127 127 GLY GLY BBB . n 
B 1 128 LYS 128 128 128 LYS LYS BBB . n 
B 1 129 GLY 129 129 129 GLY GLY BBB . n 
B 1 130 GLY 130 130 130 GLY GLY BBB . n 
B 1 131 ASN 131 131 131 ASN ASN BBB . n 
B 1 132 GLU 132 132 132 GLU GLU BBB . n 
B 1 133 GLU 133 133 133 GLU GLU BBB . n 
B 1 134 SER 134 134 134 SER SER BBB . n 
B 1 135 THR 135 135 135 THR THR BBB . n 
B 1 136 LYS 136 136 136 LYS LYS BBB . n 
B 1 137 THR 137 137 137 THR THR BBB . n 
B 1 138 GLY 138 138 138 GLY GLY BBB . n 
B 1 139 ASN 139 139 139 ASN ASN BBB . n 
B 1 140 ALA 140 140 140 ALA ALA BBB . n 
B 1 141 GLY 141 141 141 GLY GLY BBB . n 
B 1 142 SER 142 142 142 SER SER BBB . n 
B 1 143 ARG 143 143 143 ARG ARG BBB . n 
B 1 144 LEU 144 144 144 LEU LEU BBB . n 
B 1 145 ALA 145 145 145 ALA ALA BBB . n 
B 1 146 CYS 146 146 146 CYS CYS BBB . n 
B 1 147 GLY 147 147 147 GLY GLY BBB . n 
B 1 148 VAL 148 148 148 VAL VAL BBB . n 
B 1 149 ILE 149 149 149 ILE ILE BBB . n 
B 1 150 GLY 150 150 150 GLY GLY BBB . n 
B 1 151 ILE 151 151 151 ILE ILE BBB . n 
B 1 152 ALA 152 152 152 ALA ALA BBB . n 
B 1 153 GLN 153 153 153 GLN GLN BBB . 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   201 154 ZN  ZN  AAA . 
D 3 Q6H 1   202 301 Q6H 214 AAA . 
E 2 ZN  1   203 1   ZN  ZN  AAA . 
F 4 SO4 1   204 2   SO4 SO4 AAA . 
G 4 SO4 1   205 6   SO4 SO4 AAA . 
H 2 ZN  1   201 154 ZN  ZN  BBB . 
I 3 Q6H 1   202 201 Q6H 214 BBB . 
J 2 ZN  1   203 2   ZN  ZN  BBB . 
K 4 SO4 1   204 1   SO4 SO4 BBB . 
L 4 SO4 1   205 5   SO4 SO4 BBB . 
M 4 SO4 1   206 7   SO4 SO4 BBB . 
N 5 HOH 1   301 259 HOH HOH AAA . 
N 5 HOH 2   302 306 HOH HOH AAA . 
N 5 HOH 3   303 202 HOH HOH AAA . 
N 5 HOH 4   304 297 HOH HOH AAA . 
N 5 HOH 5   305 273 HOH HOH AAA . 
N 5 HOH 6   306 282 HOH HOH AAA . 
N 5 HOH 7   307 246 HOH HOH AAA . 
N 5 HOH 8   308 129 HOH HOH AAA . 
N 5 HOH 9   309 187 HOH HOH AAA . 
N 5 HOH 10  310 206 HOH HOH AAA . 
N 5 HOH 11  311 169 HOH HOH AAA . 
N 5 HOH 12  312 117 HOH HOH AAA . 
N 5 HOH 13  313 61  HOH HOH AAA . 
N 5 HOH 14  314 124 HOH HOH AAA . 
N 5 HOH 15  315 295 HOH HOH AAA . 
N 5 HOH 16  316 40  HOH HOH AAA . 
N 5 HOH 17  317 22  HOH HOH AAA . 
N 5 HOH 18  318 126 HOH HOH AAA . 
N 5 HOH 19  319 102 HOH HOH AAA . 
N 5 HOH 20  320 199 HOH HOH AAA . 
N 5 HOH 21  321 27  HOH HOH AAA . 
N 5 HOH 22  322 103 HOH HOH AAA . 
N 5 HOH 23  323 15  HOH HOH AAA . 
N 5 HOH 24  324 82  HOH HOH AAA . 
N 5 HOH 25  325 122 HOH HOH AAA . 
N 5 HOH 26  326 24  HOH HOH AAA . 
N 5 HOH 27  327 258 HOH HOH AAA . 
N 5 HOH 28  328 204 HOH HOH AAA . 
N 5 HOH 29  329 120 HOH HOH AAA . 
N 5 HOH 30  330 83  HOH HOH AAA . 
N 5 HOH 31  331 123 HOH HOH AAA . 
N 5 HOH 32  332 132 HOH HOH AAA . 
N 5 HOH 33  333 47  HOH HOH AAA . 
N 5 HOH 34  334 97  HOH HOH AAA . 
N 5 HOH 35  335 280 HOH HOH AAA . 
N 5 HOH 36  336 301 HOH HOH AAA . 
N 5 HOH 37  337 11  HOH HOH AAA . 
N 5 HOH 38  338 147 HOH HOH AAA . 
N 5 HOH 39  339 118 HOH HOH AAA . 
N 5 HOH 40  340 5   HOH HOH AAA . 
N 5 HOH 41  341 63  HOH HOH AAA . 
N 5 HOH 42  342 4   HOH HOH AAA . 
N 5 HOH 43  343 104 HOH HOH AAA . 
N 5 HOH 44  344 143 HOH HOH AAA . 
N 5 HOH 45  345 92  HOH HOH AAA . 
N 5 HOH 46  346 191 HOH HOH AAA . 
N 5 HOH 47  347 20  HOH HOH AAA . 
N 5 HOH 48  348 9   HOH HOH AAA . 
N 5 HOH 49  349 190 HOH HOH AAA . 
N 5 HOH 50  350 140 HOH HOH AAA . 
N 5 HOH 51  351 192 HOH HOH AAA . 
N 5 HOH 52  352 208 HOH HOH AAA . 
N 5 HOH 53  353 43  HOH HOH AAA . 
N 5 HOH 54  354 125 HOH HOH AAA . 
N 5 HOH 55  355 185 HOH HOH AAA . 
N 5 HOH 56  356 53  HOH HOH AAA . 
N 5 HOH 57  357 276 HOH HOH AAA . 
N 5 HOH 58  358 39  HOH HOH AAA . 
N 5 HOH 59  359 197 HOH HOH AAA . 
N 5 HOH 60  360 174 HOH HOH AAA . 
N 5 HOH 61  361 271 HOH HOH AAA . 
N 5 HOH 62  362 7   HOH HOH AAA . 
N 5 HOH 63  363 250 HOH HOH AAA . 
N 5 HOH 64  364 109 HOH HOH AAA . 
N 5 HOH 65  365 254 HOH HOH AAA . 
N 5 HOH 66  366 151 HOH HOH AAA . 
N 5 HOH 67  367 207 HOH HOH AAA . 
N 5 HOH 68  368 188 HOH HOH AAA . 
N 5 HOH 69  369 150 HOH HOH AAA . 
N 5 HOH 70  370 170 HOH HOH AAA . 
N 5 HOH 71  371 130 HOH HOH AAA . 
N 5 HOH 72  372 51  HOH HOH AAA . 
N 5 HOH 73  373 148 HOH HOH AAA . 
N 5 HOH 74  374 45  HOH HOH AAA . 
N 5 HOH 75  375 100 HOH HOH AAA . 
N 5 HOH 76  376 265 HOH HOH AAA . 
N 5 HOH 77  377 181 HOH HOH AAA . 
N 5 HOH 78  378 116 HOH HOH AAA . 
N 5 HOH 79  379 35  HOH HOH AAA . 
N 5 HOH 80  380 153 HOH HOH AAA . 
N 5 HOH 81  381 96  HOH HOH AAA . 
N 5 HOH 82  382 84  HOH HOH AAA . 
N 5 HOH 83  383 274 HOH HOH AAA . 
N 5 HOH 84  384 131 HOH HOH AAA . 
N 5 HOH 85  385 44  HOH HOH AAA . 
N 5 HOH 86  386 304 HOH HOH AAA . 
N 5 HOH 87  387 48  HOH HOH AAA . 
N 5 HOH 88  388 257 HOH HOH AAA . 
N 5 HOH 89  389 203 HOH HOH AAA . 
N 5 HOH 90  390 93  HOH HOH AAA . 
N 5 HOH 91  391 272 HOH HOH AAA . 
N 5 HOH 92  392 52  HOH HOH AAA . 
N 5 HOH 93  393 178 HOH HOH AAA . 
N 5 HOH 94  394 17  HOH HOH AAA . 
N 5 HOH 95  395 14  HOH HOH AAA . 
N 5 HOH 96  396 253 HOH HOH AAA . 
N 5 HOH 97  397 134 HOH HOH AAA . 
N 5 HOH 98  398 186 HOH HOH AAA . 
N 5 HOH 99  399 71  HOH HOH AAA . 
N 5 HOH 100 400 141 HOH HOH AAA . 
N 5 HOH 101 401 284 HOH HOH AAA . 
N 5 HOH 102 402 264 HOH HOH AAA . 
N 5 HOH 103 403 198 HOH HOH AAA . 
N 5 HOH 104 404 293 HOH HOH AAA . 
N 5 HOH 105 405 263 HOH HOH AAA . 
N 5 HOH 106 406 85  HOH HOH AAA . 
N 5 HOH 107 407 54  HOH HOH AAA . 
N 5 HOH 108 408 67  HOH HOH AAA . 
N 5 HOH 109 409 13  HOH HOH AAA . 
N 5 HOH 110 410 232 HOH HOH AAA . 
N 5 HOH 111 411 245 HOH HOH AAA . 
N 5 HOH 112 412 171 HOH HOH AAA . 
N 5 HOH 113 413 277 HOH HOH AAA . 
N 5 HOH 114 414 283 HOH HOH AAA . 
N 5 HOH 115 415 183 HOH HOH AAA . 
N 5 HOH 116 416 233 HOH HOH AAA . 
N 5 HOH 117 417 267 HOH HOH AAA . 
N 5 HOH 118 418 106 HOH HOH AAA . 
N 5 HOH 119 419 294 HOH HOH AAA . 
N 5 HOH 120 420 19  HOH HOH AAA . 
N 5 HOH 121 421 180 HOH HOH AAA . 
N 5 HOH 122 422 255 HOH HOH AAA . 
N 5 HOH 123 423 184 HOH HOH AAA . 
N 5 HOH 124 424 285 HOH HOH AAA . 
N 5 HOH 125 425 281 HOH HOH AAA . 
N 5 HOH 126 426 193 HOH HOH AAA . 
N 5 HOH 127 427 179 HOH HOH AAA . 
N 5 HOH 128 428 160 HOH HOH AAA . 
N 5 HOH 129 429 189 HOH HOH AAA . 
N 5 HOH 130 430 110 HOH HOH AAA . 
N 5 HOH 131 431 195 HOH HOH AAA . 
N 5 HOH 132 432 196 HOH HOH AAA . 
N 5 HOH 133 433 262 HOH HOH AAA . 
N 5 HOH 134 434 302 HOH HOH AAA . 
N 5 HOH 135 435 72  HOH HOH AAA . 
N 5 HOH 136 436 155 HOH HOH AAA . 
N 5 HOH 137 437 252 HOH HOH AAA . 
N 5 HOH 138 438 305 HOH HOH AAA . 
N 5 HOH 139 439 260 HOH HOH AAA . 
N 5 HOH 140 440 62  HOH HOH AAA . 
N 5 HOH 141 441 163 HOH HOH AAA . 
N 5 HOH 142 442 162 HOH HOH AAA . 
O 5 HOH 1   301 60  HOH HOH BBB . 
O 5 HOH 2   302 222 HOH HOH BBB . 
O 5 HOH 3   303 223 HOH HOH BBB . 
O 5 HOH 4   304 241 HOH HOH BBB . 
O 5 HOH 5   305 154 HOH HOH BBB . 
O 5 HOH 6   306 69  HOH HOH BBB . 
O 5 HOH 7   307 299 HOH HOH BBB . 
O 5 HOH 8   308 236 HOH HOH BBB . 
O 5 HOH 9   309 111 HOH HOH BBB . 
O 5 HOH 10  310 114 HOH HOH BBB . 
O 5 HOH 11  311 239 HOH HOH BBB . 
O 5 HOH 12  312 240 HOH HOH BBB . 
O 5 HOH 13  313 49  HOH HOH BBB . 
O 5 HOH 14  314 229 HOH HOH BBB . 
O 5 HOH 15  315 94  HOH HOH BBB . 
O 5 HOH 16  316 157 HOH HOH BBB . 
O 5 HOH 17  317 230 HOH HOH BBB . 
O 5 HOH 18  318 167 HOH HOH BBB . 
O 5 HOH 19  319 225 HOH HOH BBB . 
O 5 HOH 20  320 137 HOH HOH BBB . 
O 5 HOH 21  321 2   HOH HOH BBB . 
O 5 HOH 22  322 279 HOH HOH BBB . 
O 5 HOH 23  323 209 HOH HOH BBB . 
O 5 HOH 24  324 287 HOH HOH BBB . 
O 5 HOH 25  325 152 HOH HOH BBB . 
O 5 HOH 26  326 59  HOH HOH BBB . 
O 5 HOH 27  327 243 HOH HOH BBB . 
O 5 HOH 28  328 89  HOH HOH BBB . 
O 5 HOH 29  329 119 HOH HOH BBB . 
O 5 HOH 30  330 235 HOH HOH BBB . 
O 5 HOH 31  331 26  HOH HOH BBB . 
O 5 HOH 32  332 139 HOH HOH BBB . 
O 5 HOH 33  333 215 HOH HOH BBB . 
O 5 HOH 34  334 135 HOH HOH BBB . 
O 5 HOH 35  335 80  HOH HOH BBB . 
O 5 HOH 36  336 115 HOH HOH BBB . 
O 5 HOH 37  337 6   HOH HOH BBB . 
O 5 HOH 38  338 161 HOH HOH BBB . 
O 5 HOH 39  339 217 HOH HOH BBB . 
O 5 HOH 40  340 36  HOH HOH BBB . 
O 5 HOH 41  341 95  HOH HOH BBB . 
O 5 HOH 42  342 112 HOH HOH BBB . 
O 5 HOH 43  343 88  HOH HOH BBB . 
O 5 HOH 44  344 290 HOH HOH BBB . 
O 5 HOH 45  345 18  HOH HOH BBB . 
O 5 HOH 46  346 32  HOH HOH BBB . 
O 5 HOH 47  347 168 HOH HOH BBB . 
O 5 HOH 48  348 3   HOH HOH BBB . 
O 5 HOH 49  349 166 HOH HOH BBB . 
O 5 HOH 50  350 242 HOH HOH BBB . 
O 5 HOH 51  351 173 HOH HOH BBB . 
O 5 HOH 52  352 68  HOH HOH BBB . 
O 5 HOH 53  353 216 HOH HOH BBB . 
O 5 HOH 54  354 145 HOH HOH BBB . 
O 5 HOH 55  355 248 HOH HOH BBB . 
O 5 HOH 56  356 65  HOH HOH BBB . 
O 5 HOH 57  357 57  HOH HOH BBB . 
O 5 HOH 58  358 77  HOH HOH BBB . 
O 5 HOH 59  359 8   HOH HOH BBB . 
O 5 HOH 60  360 78  HOH HOH BBB . 
O 5 HOH 61  361 64  HOH HOH BBB . 
O 5 HOH 62  362 70  HOH HOH BBB . 
O 5 HOH 63  363 278 HOH HOH BBB . 
O 5 HOH 64  364 237 HOH HOH BBB . 
O 5 HOH 65  365 218 HOH HOH BBB . 
O 5 HOH 66  366 28  HOH HOH BBB . 
O 5 HOH 67  367 76  HOH HOH BBB . 
O 5 HOH 68  368 41  HOH HOH BBB . 
O 5 HOH 69  369 247 HOH HOH BBB . 
O 5 HOH 70  370 182 HOH HOH BBB . 
O 5 HOH 71  371 251 HOH HOH BBB . 
O 5 HOH 72  372 46  HOH HOH BBB . 
O 5 HOH 73  373 75  HOH HOH BBB . 
O 5 HOH 74  374 37  HOH HOH BBB . 
O 5 HOH 75  375 310 HOH HOH BBB . 
O 5 HOH 76  376 308 HOH HOH BBB . 
O 5 HOH 77  377 238 HOH HOH BBB . 
O 5 HOH 78  378 1   HOH HOH BBB . 
O 5 HOH 79  379 270 HOH HOH BBB . 
O 5 HOH 80  380 127 HOH HOH BBB . 
O 5 HOH 81  381 73  HOH HOH BBB . 
O 5 HOH 82  382 121 HOH HOH BBB . 
O 5 HOH 83  383 128 HOH HOH BBB . 
O 5 HOH 84  384 86  HOH HOH BBB . 
O 5 HOH 85  385 21  HOH HOH BBB . 
O 5 HOH 86  386 55  HOH HOH BBB . 
O 5 HOH 87  387 30  HOH HOH BBB . 
O 5 HOH 88  388 91  HOH HOH BBB . 
O 5 HOH 89  389 56  HOH HOH BBB . 
O 5 HOH 90  390 33  HOH HOH BBB . 
O 5 HOH 91  391 300 HOH HOH BBB . 
O 5 HOH 92  392 10  HOH HOH BBB . 
O 5 HOH 93  393 38  HOH HOH BBB . 
O 5 HOH 94  394 244 HOH HOH BBB . 
O 5 HOH 95  395 87  HOH HOH BBB . 
O 5 HOH 96  396 261 HOH HOH BBB . 
O 5 HOH 97  397 175 HOH HOH BBB . 
O 5 HOH 98  398 138 HOH HOH BBB . 
O 5 HOH 99  399 234 HOH HOH BBB . 
O 5 HOH 100 400 101 HOH HOH BBB . 
O 5 HOH 101 401 99  HOH HOH BBB . 
O 5 HOH 102 402 210 HOH HOH BBB . 
O 5 HOH 103 403 269 HOH HOH BBB . 
O 5 HOH 104 404 29  HOH HOH BBB . 
O 5 HOH 105 405 90  HOH HOH BBB . 
O 5 HOH 106 406 81  HOH HOH BBB . 
O 5 HOH 107 407 177 HOH HOH BBB . 
O 5 HOH 108 408 34  HOH HOH BBB . 
O 5 HOH 109 409 142 HOH HOH BBB . 
O 5 HOH 110 410 309 HOH HOH BBB . 
O 5 HOH 111 411 268 HOH HOH BBB . 
O 5 HOH 112 412 146 HOH HOH BBB . 
O 5 HOH 113 413 214 HOH HOH BBB . 
O 5 HOH 114 414 205 HOH HOH BBB . 
O 5 HOH 115 415 31  HOH HOH BBB . 
O 5 HOH 116 416 165 HOH HOH BBB . 
O 5 HOH 117 417 228 HOH HOH BBB . 
O 5 HOH 118 418 176 HOH HOH BBB . 
O 5 HOH 119 419 23  HOH HOH BBB . 
O 5 HOH 120 420 136 HOH HOH BBB . 
O 5 HOH 121 421 42  HOH HOH BBB . 
O 5 HOH 122 422 172 HOH HOH BBB . 
O 5 HOH 123 423 227 HOH HOH BBB . 
O 5 HOH 124 424 226 HOH HOH BBB . 
O 5 HOH 125 425 158 HOH HOH BBB . 
O 5 HOH 126 426 212 HOH HOH BBB . 
O 5 HOH 127 427 164 HOH HOH BBB . 
O 5 HOH 128 428 105 HOH HOH BBB . 
O 5 HOH 129 429 256 HOH HOH BBB . 
O 5 HOH 130 430 291 HOH HOH BBB . 
O 5 HOH 131 431 249 HOH HOH BBB . 
O 5 HOH 132 432 58  HOH HOH BBB . 
O 5 HOH 133 433 231 HOH HOH BBB . 
O 5 HOH 134 434 220 HOH HOH BBB . 
O 5 HOH 135 435 194 HOH HOH BBB . 
O 5 HOH 136 436 156 HOH HOH BBB . 
O 5 HOH 137 437 303 HOH HOH BBB . 
O 5 HOH 138 438 296 HOH HOH BBB . 
O 5 HOH 139 439 149 HOH HOH BBB . 
O 5 HOH 140 440 50  HOH HOH BBB . 
O 5 HOH 141 441 213 HOH HOH BBB . 
O 5 HOH 142 442 211 HOH HOH BBB . 
O 5 HOH 143 443 159 HOH HOH BBB . 
O 5 HOH 144 444 66  HOH HOH BBB . 
O 5 HOH 145 445 219 HOH HOH BBB . 
O 5 HOH 146 446 221 HOH HOH BBB . 
# 
_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,M,N,O 
# 
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)' 2970  ? 
1 MORE         -170  ? 
1 'SSA (A^2)'  13960 ? 
# 
_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  NE2 ? A HIS 48 ? AAA HIS 48 ? 1_555 ZN ? E ZN . ? AAA ZN 203 ? 1_555 O1  ? G SO4 .  ? AAA SO4 205 ? 1_555 115.6 ? 
2  ND1 ? A HIS 63 ? AAA HIS 63 ? 1_555 ZN ? C ZN . ? AAA ZN 201 ? 1_555 ND1 ? A HIS 71 ? AAA HIS 71  ? 1_555 103.9 ? 
3  ND1 ? A HIS 63 ? AAA HIS 63 ? 1_555 ZN ? C ZN . ? AAA ZN 201 ? 1_555 ND1 ? A HIS 80 ? AAA HIS 80  ? 1_555 111.6 ? 
4  ND1 ? A HIS 71 ? AAA HIS 71 ? 1_555 ZN ? C ZN . ? AAA ZN 201 ? 1_555 ND1 ? A HIS 80 ? AAA HIS 80  ? 1_555 121.6 ? 
5  ND1 ? A HIS 63 ? AAA HIS 63 ? 1_555 ZN ? C ZN . ? AAA ZN 201 ? 1_555 OD1 ? A ASP 83 ? AAA ASP 83  ? 1_555 104.0 ? 
6  ND1 ? A HIS 71 ? AAA HIS 71 ? 1_555 ZN ? C ZN . ? AAA ZN 201 ? 1_555 OD1 ? A ASP 83 ? AAA ASP 83  ? 1_555 98.1  ? 
7  ND1 ? A HIS 80 ? AAA HIS 80 ? 1_555 ZN ? C ZN . ? AAA ZN 201 ? 1_555 OD1 ? A ASP 83 ? AAA ASP 83  ? 1_555 115.4 ? 
8  ND1 ? B HIS 46 ? BBB HIS 46 ? 1_555 ZN ? J ZN . ? BBB ZN 203 ? 1_555 NE2 ? B HIS 48 ? BBB HIS 48  ? 1_555 109.7 ? 
9  ND1 ? B HIS 46 ? BBB HIS 46 ? 1_555 ZN ? J ZN . ? BBB ZN 203 ? 1_555 O4  ? M SO4 .  ? BBB SO4 206 ? 1_555 113.2 ? 
10 NE2 ? B HIS 48 ? BBB HIS 48 ? 1_555 ZN ? J ZN . ? BBB ZN 203 ? 1_555 O4  ? M SO4 .  ? BBB SO4 206 ? 1_555 115.9 ? 
11 ND1 ? B HIS 63 ? BBB HIS 63 ? 1_555 ZN ? H ZN . ? BBB ZN 201 ? 1_555 ND1 ? B HIS 71 ? BBB HIS 71  ? 1_555 102.3 ? 
12 ND1 ? B HIS 63 ? BBB HIS 63 ? 1_555 ZN ? H ZN . ? BBB ZN 201 ? 1_555 ND1 ? B HIS 80 ? BBB HIS 80  ? 1_555 110.6 ? 
13 ND1 ? B HIS 71 ? BBB HIS 71 ? 1_555 ZN ? H ZN . ? BBB ZN 201 ? 1_555 ND1 ? B HIS 80 ? BBB HIS 80  ? 1_555 123.1 ? 
14 ND1 ? B HIS 63 ? BBB HIS 63 ? 1_555 ZN ? H ZN . ? BBB ZN 201 ? 1_555 OD1 ? B ASP 83 ? BBB ASP 83  ? 1_555 104.2 ? 
15 ND1 ? B HIS 71 ? BBB HIS 71 ? 1_555 ZN ? H ZN . ? BBB ZN 201 ? 1_555 OD1 ? B ASP 83 ? BBB ASP 83  ? 1_555 99.3  ? 
16 ND1 ? B HIS 80 ? BBB HIS 80 ? 1_555 ZN ? H ZN . ? BBB ZN 201 ? 1_555 OD1 ? B ASP 83 ? BBB ASP 83  ? 1_555 115.1 ? 
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2020-09-16 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
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  ? ? ? 5.8.0258 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? DIALS   ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? 0.7.4    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP  ? ? ? .        4 
# 
_pdbx_entry_details.entry_id                 6Z3V 
_pdbx_entry_details.has_ligand_of_interest   Y 
_pdbx_entry_details.compound_details         ? 
_pdbx_entry_details.source_details           ? 
_pdbx_entry_details.nonpolymer_details       ? 
_pdbx_entry_details.sequence_details         ? 
# 
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 NE2 AAA HIS 120 ? ? ZN AAA ZN  203 ? ? 1.59 
2 1 NE2 BBB HIS 120 ? ? ZN BBB ZN  203 ? ? 1.66 
3 1 OG  AAA SER 98  ? ? O  AAA HOH 301 ? ? 2.12 
4 1 O   AAA HOH 324 ? ? O  AAA HOH 422 ? ? 2.15 
5 1 O   BBB HOH 301 ? ? O  BBB HOH 356 ? ? 2.18 
# 
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 O   AAA HOH 416 ? ? 1_555 O   BBB HOH 399 ? ? 2_555 2.07 
2 1 OE1 AAA GLU 40  ? ? 1_555 OE1 BBB GLU 49  ? ? 2_555 2.16 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    ASN 
_pdbx_validate_torsion.auth_asym_id    BBB 
_pdbx_validate_torsion.auth_seq_id     65 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             -141.54 
_pdbx_validate_torsion.psi             59.43 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 Y 1 AAA GLU 133 ? CG  ? A GLU 133 CG  
2 1 Y 1 AAA GLU 133 ? CD  ? A GLU 133 CD  
3 1 Y 1 AAA GLU 133 ? OE1 ? A GLU 133 OE1 
4 1 Y 1 AAA GLU 133 ? OE2 ? A GLU 133 OE2 
# 
_pdbx_audit_support.funding_organization   'Other private' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           WA1128 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        Q6H 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   Q6H 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'                                                              ZN  
3 '5-fluoranyl-~{N}-(3-morpholin-4-ylcarbonylphenyl)-2-selanyl-benzamide' Q6H 
4 'SULFATE ION'                                                           SO4 
5 water                                                                   HOH 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
