data_7T8G
# 
_entry.id   7T8G 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.365 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   7T8G         pdb_00007t8g 10.2210/pdb7t8g/pdb 
WWPDB D_1000261811 ?            ?                   
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        7T8G 
_pdbx_database_status.recvd_initial_deposition_date   2021-12-16 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'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                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
;Disease Onset and its course are delayed by on-target Cellular SOD1 Engagement of Organo-selenium drug compounds for Amyotrophic Lateral Sclerosis
;
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Amporndanai, K.' 1 0000-0001-8527-9394 
primary 'Watanabe, S.'    2 0000-0001-8038-7919 
primary 'Awais, R.'       3 0000-0003-1169-4493 
primary 'Latham, C.'      4 ?                   
primary 'O Neill, P.M.'   5 0000-0003-4338-0317 
primary 'Yamanaka, K.'    6 0000-0003-4655-0035 
primary 'Hasnain, S.S.'   7 0000-0002-2854-4718 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   106.290 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     7T8G 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     38.840 
_cell.length_a_esd                 ? 
_cell.length_b                     67.790 
_cell.length_b_esd                 ? 
_cell.length_c                     51.160 
_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                         7T8G 
_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]'                  15841.586 2   1.15.1.1 G93A ? ? 
2 non-polymer syn 'ZINC ION'                                      65.409    4   ?        ?    ? ? 
3 non-polymer syn '~{N}-(pyridin-3-ylmethyl)-2-selanyl-benzamide' 291.207   2   ?        ?    ? ? 
4 non-polymer syn 'ACETATE ION'                                   59.044    1   ?        ?    ? ? 
5 non-polymer syn 'SULFATE ION'                                   96.063    2   ?        ?    ? ? 
6 non-polymer syn 'SELENIUM ATOM'                                 78.960    1   ?        ?    ? ? 
7 water       nat water                                           18.015    327 ?        ?    ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Superoxide dismutase 1,hSod1' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDAVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDAVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_entity_poly.pdbx_strand_id                 A,F 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ALA n 
1 2   THR n 
1 3   LYS n 
1 4   ALA n 
1 5   VAL n 
1 6   CYS n 
1 7   VAL n 
1 8   LEU n 
1 9   LYS n 
1 10  GLY n 
1 11  ASP n 
1 12  GLY n 
1 13  PRO n 
1 14  VAL n 
1 15  GLN n 
1 16  GLY n 
1 17  ILE n 
1 18  ILE n 
1 19  ASN n 
1 20  PHE n 
1 21  GLU n 
1 22  GLN n 
1 23  LYS n 
1 24  GLU n 
1 25  SER n 
1 26  ASN n 
1 27  GLY n 
1 28  PRO n 
1 29  VAL n 
1 30  LYS n 
1 31  VAL n 
1 32  TRP n 
1 33  GLY n 
1 34  SER n 
1 35  ILE n 
1 36  LYS n 
1 37  GLY n 
1 38  LEU n 
1 39  THR n 
1 40  GLU n 
1 41  GLY n 
1 42  LEU n 
1 43  HIS n 
1 44  GLY n 
1 45  PHE n 
1 46  HIS n 
1 47  VAL n 
1 48  HIS n 
1 49  GLU n 
1 50  PHE n 
1 51  GLY n 
1 52  ASP n 
1 53  ASN n 
1 54  THR n 
1 55  ALA n 
1 56  GLY n 
1 57  CYS n 
1 58  THR n 
1 59  SER n 
1 60  ALA n 
1 61  GLY n 
1 62  PRO n 
1 63  HIS n 
1 64  PHE n 
1 65  ASN n 
1 66  PRO n 
1 67  LEU n 
1 68  SER n 
1 69  ARG n 
1 70  LYS n 
1 71  HIS n 
1 72  GLY n 
1 73  GLY n 
1 74  PRO n 
1 75  LYS n 
1 76  ASP n 
1 77  GLU n 
1 78  GLU n 
1 79  ARG n 
1 80  HIS n 
1 81  VAL n 
1 82  GLY n 
1 83  ASP n 
1 84  LEU n 
1 85  GLY n 
1 86  ASN n 
1 87  VAL n 
1 88  THR n 
1 89  ALA n 
1 90  ASP n 
1 91  LYS n 
1 92  ASP n 
1 93  ALA 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               'BL21(DE3)' 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    SODC_HUMAN 
_struct_ref.pdbx_db_accession          P00441 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_struct_ref.pdbx_align_begin           2 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7T8G A 1 ? 153 ? P00441 2 ? 154 ? 1 153 
2 1 7T8G F 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 7T8G ALA A 93 ? UNP P00441 GLY 94 'engineered mutation' 93 1 
2 7T8G ALA F 93 ? UNP P00441 GLY 94 'engineered mutation' 93 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 
ACT non-polymer         . 'ACETATE ION'                                   ? 'C2 H3 O2 -1'     59.044  
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 
Q8H non-polymer         . '~{N}-(pyridin-3-ylmethyl)-2-selanyl-benzamide' ? 'C13 H12 N2 O Se' 291.207 
SE  non-polymer         . 'SELENIUM ATOM'                                 ? Se                78.960  
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                   7T8G 
_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         39.72 
_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                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 X 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-01-22 
_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   0.9800 
_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        0.9800 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   I24 
_diffrn_source.pdbx_synchrotron_site       Diamond 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       7T8G 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.350 
_reflns.d_resolution_low                               37.280 
_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                                     54318 
_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                           97.300 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                2.900 
_reflns.pdbx_Rmerge_I_obs                              0.056 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          11.100 
_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                                0.068 
_reflns.pdbx_Rpim_I_all                                0.037 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       160074 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.996 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_all 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
_reflns_shell.pdbx_R_split 
_reflns_shell.pdbx_percent_possible_ellipsoidal 
_reflns_shell.pdbx_percent_possible_spherical 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous 
_reflns_shell.pdbx_percent_possible_spherical_anomalous 
_reflns_shell.pdbx_redundancy_anomalous 
_reflns_shell.pdbx_CC_half_anomalous 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous 
_reflns_shell.pdbx_percent_possible_anomalous 
1.350 1.370  ? ? 3900 ? ? ? 2167 78.800 ? ? ? ? 0.448 ? ? ? ? ? ? ? ? 1.800 ? ? ? 1.800  0.597 0.391 ? 1 1 0.791 ? ? ? ? ? ? ? ? ? 
? 
7.390 37.280 ? ? 1042 ? ? ? 348  96.200 ? ? ? ? 0.048 ? ? ? ? ? ? ? ? 3.000 ? ? ? 22.000 0.058 0.033 ? 2 1 0.987 ? ? ? ? ? ? ? ? ? 
? 
# 
_refine.aniso_B[1][1]                            0.6400 
_refine.aniso_B[1][2]                            -0.0000 
_refine.aniso_B[1][3]                            0.3500 
_refine.aniso_B[2][2]                            -1.2200 
_refine.aniso_B[2][3]                            -0.0000 
_refine.aniso_B[3][3]                            0.3200 
_refine.B_iso_max                                54.920 
_refine.B_iso_mean                               19.1170 
_refine.B_iso_min                                10.840 
_refine.correlation_coeff_Fo_to_Fc               0.9670 
_refine.correlation_coeff_Fo_to_Fc_free          0.9590 
_refine.details                                  
'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS U VALUES      : REFINED INDIVIDUALLY' 
_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                                 7T8G 
_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                            1.3500 
_refine.ls_d_res_low                             37.280 
_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                     51688 
_refine.ls_number_reflns_R_free                  2606 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    97.1900 
_refine.ls_percent_reflns_R_free                 4.8000 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1897 
_refine.ls_R_factor_R_free                       0.2020 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1891 
_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 
_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                          0.000 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      2WKO 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.0660 
_refine.pdbx_overall_ESU_R_Free                  0.0630 
_refine.pdbx_solvent_vdw_probe_radii             1.2000 
_refine.pdbx_solvent_ion_probe_radii             0.8000 
_refine.pdbx_solvent_shrinkage_radii             0.8000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             1.1400 
_refine.overall_SU_ML                            0.0460 
_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                         final 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.3500 
_refine_hist.d_res_low                        37.280 
_refine_hist.number_atoms_solvent             327 
_refine_hist.number_atoms_total               2565 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       306 
_refine_hist.pdbx_B_iso_mean_ligand           26.96 
_refine_hist.pdbx_B_iso_mean_solvent          32.84 
_refine_hist.pdbx_number_atoms_protein        2185 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         53 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.012  0.013  2323 ? r_bond_refined_d       ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.017  2090 ? r_bond_other_d         ? ? 
'X-RAY DIFFRACTION' ? 1.502  1.631  3154 ? r_angle_refined_deg    ? ? 
'X-RAY DIFFRACTION' ? 1.463  1.587  4841 ? r_angle_other_deg      ? ? 
'X-RAY DIFFRACTION' ? 7.175  5.000  318  ? r_dihedral_angle_1_deg ? ? 
'X-RAY DIFFRACTION' ? 36.033 24.038 104  ? r_dihedral_angle_2_deg ? ? 
'X-RAY DIFFRACTION' ? 14.061 15.000 352  ? r_dihedral_angle_3_deg ? ? 
'X-RAY DIFFRACTION' ? 17.876 15.000 8    ? r_dihedral_angle_4_deg ? ? 
'X-RAY DIFFRACTION' ? 0.061  0.200  300  ? r_chiral_restr         ? ? 
'X-RAY DIFFRACTION' ? 0.006  0.020  3062 ? r_gen_planes_refined   ? ? 
'X-RAY DIFFRACTION' ? 0.003  0.020  500  ? r_gen_planes_other     ? ? 
# 
loop_
_refine_ls_restr_ncs.pdbx_refine_id 
_refine_ls_restr_ncs.dom_id 
_refine_ls_restr_ncs.ncs_model_details 
_refine_ls_restr_ncs.rms_dev_B_iso 
_refine_ls_restr_ncs.rms_dev_position 
_refine_ls_restr_ncs.weight_B_iso 
_refine_ls_restr_ncs.weight_position 
_refine_ls_restr_ncs.pdbx_ordinal 
_refine_ls_restr_ncs.pdbx_type 
_refine_ls_restr_ncs.pdbx_asym_id 
_refine_ls_restr_ncs.pdbx_auth_asym_id 
_refine_ls_restr_ncs.pdbx_number 
_refine_ls_restr_ncs.pdbx_rms 
_refine_ls_restr_ncs.pdbx_weight 
_refine_ls_restr_ncs.pdbx_ens_id 
'X-RAY DIFFRACTION' 1 ? ? 0.110 ? 0.050 1 'interatomic distance' ? A 4440 ? ? 1 
'X-RAY DIFFRACTION' 2 ? ? 0.110 ? 0.050 2 'interatomic distance' ? F 4440 ? ? 1 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.3500 
_refine_ls_shell.d_res_low                        1.3850 
_refine_ls_shell.number_reflns_all                3326 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             133 
_refine_ls_shell.number_reflns_R_work             3193 
_refine_ls_shell.percent_reflns_obs               80.4400 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free                  0.2670 
_refine_ls_shell.R_factor_R_free_error            0.0000 
_refine_ls_shell.R_factor_R_work                  0.2790 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
# 
loop_
_struct_ncs_dom.pdbx_ens_id 
_struct_ncs_dom.id 
_struct_ncs_dom.details 
1 1 A 
1 2 F 
# 
loop_
_struct_ncs_dom_lim.pdbx_ens_id 
_struct_ncs_dom_lim.dom_id 
_struct_ncs_dom_lim.pdbx_component_id 
_struct_ncs_dom_lim.pdbx_refine_code 
_struct_ncs_dom_lim.beg_auth_asym_id 
_struct_ncs_dom_lim.beg_auth_seq_id 
_struct_ncs_dom_lim.end_auth_asym_id 
_struct_ncs_dom_lim.end_auth_seq_id 
_struct_ncs_dom_lim.selection_details 
_struct_ncs_dom_lim.beg_label_asym_id 
_struct_ncs_dom_lim.beg_label_comp_id 
_struct_ncs_dom_lim.beg_label_seq_id 
_struct_ncs_dom_lim.beg_label_alt_id 
_struct_ncs_dom_lim.end_label_asym_id 
_struct_ncs_dom_lim.end_label_comp_id 
_struct_ncs_dom_lim.end_label_seq_id 
_struct_ncs_dom_lim.end_label_alt_id 
1 1 0 0 A 1 A 153 ? ? ? ? ? ? ? ? ? 
1 2 0 0 F 1 F 153 ? ? ? ? ? ? ? ? ? 
# 
_struct_ncs_ens.id        1 
_struct_ncs_ens.details   ? 
# 
_struct.entry_id                     7T8G 
_struct.title                        'G93A mutant of human SOD1 bound with MR6-8-2 in P21 space group' 
_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        7T8G 
_struct_keywords.text            'SOD1, ALS, Drug discovery, 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 5 ? 
H N N 3 ? 
I N N 2 ? 
J N N 2 ? 
K N N 6 ? 
L N N 5 ? 
M N N 7 ? 
N N N 7 ? 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 ALA A 55  ? GLY A 61  ? ALA A 55  GLY A 61  5 ? 7 
HELX_P HELX_P2 AA2 SER A 107 ? CYS A 111 ? SER A 107 CYS A 111 5 ? 5 
HELX_P HELX_P3 AA3 ASN A 131 ? LYS A 136 ? ASN A 131 LYS A 136 5 ? 6 
HELX_P HELX_P4 AA4 GLY B 56  ? GLY B 61  ? GLY F 56  GLY F 61  5 ? 6 
HELX_P HELX_P5 AA5 GLU B 132 ? LYS B 136 ? GLU F 132 LYS F 136 5 ? 5 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1  disulf ?    ? A CYS 57  SG  ? ? ? 1_555 A CYS 146 SG ? ? A CYS 57  A CYS 146 1_555 ? ? ? ? ? ? ? 2.129 ? ? 
disulf2  disulf ?    ? B CYS 57  SG  ? ? ? 1_555 B CYS 146 SG ? ? F CYS 57  F CYS 146 1_555 ? ? ? ? ? ? ? 2.147 ? ? 
covale1  covale none ? A CYS 111 SG  ? ? ? 1_555 D Q8H .   SE A ? A CYS 111 A Q8H 202 1_555 ? ? ? ? ? ? ? 2.235 ? ? 
covale2  covale none ? B CYS 111 SG  A ? ? 1_555 H Q8H .   SE A ? F CYS 111 F Q8H 201 1_555 ? ? ? ? ? ? ? 2.251 ? ? 
covale3  covale one  ? B CYS 111 SG  B ? ? 1_555 K SE  .   SE B ? F CYS 111 F SE  204 1_555 ? ? ? ? ? ? ? 1.955 ? ? 
metalc1  metalc ?    ? A HIS 46  ND1 ? ? ? 1_555 E ZN  .   ZN ? ? A HIS 46  A ZN  203 1_555 ? ? ? ? ? ? ? 2.201 ? ? 
metalc2  metalc ?    ? A HIS 48  NE2 ? ? ? 1_555 E ZN  .   ZN ? ? A HIS 48  A ZN  203 1_555 ? ? ? ? ? ? ? 2.055 ? ? 
metalc3  metalc ?    ? A HIS 63  ND1 ? ? ? 1_555 C ZN  .   ZN ? ? A HIS 63  A ZN  201 1_555 ? ? ? ? ? ? ? 2.036 ? ? 
metalc4  metalc ?    ? A HIS 71  ND1 ? ? ? 1_555 C ZN  .   ZN ? ? A HIS 71  A ZN  201 1_555 ? ? ? ? ? ? ? 2.045 ? ? 
metalc5  metalc ?    ? A HIS 80  ND1 ? ? ? 1_555 C ZN  .   ZN ? ? A HIS 80  A ZN  201 1_555 ? ? ? ? ? ? ? 2.006 ? ? 
metalc6  metalc ?    ? A ASP 83  OD1 ? ? ? 1_555 C ZN  .   ZN ? ? A ASP 83  A ZN  201 1_555 ? ? ? ? ? ? ? 1.926 ? ? 
metalc7  metalc ?    ? A HIS 120 NE2 ? ? ? 1_555 E ZN  .   ZN ? ? A HIS 120 A ZN  203 1_555 ? ? ? ? ? ? ? 1.831 ? ? 
metalc8  metalc ?    ? E ZN  .   ZN  ? ? ? 1_555 G SO4 .   O3 ? ? A ZN  203 A SO4 205 1_555 ? ? ? ? ? ? ? 2.006 ? ? 
metalc9  metalc ?    ? B HIS 46  ND1 ? ? ? 1_555 J ZN  .   ZN ? ? F HIS 46  F ZN  203 1_555 ? ? ? ? ? ? ? 2.204 ? ? 
metalc10 metalc ?    ? B HIS 48  NE2 ? ? ? 1_555 J ZN  .   ZN ? ? F HIS 48  F ZN  203 1_555 ? ? ? ? ? ? ? 2.040 ? ? 
metalc11 metalc ?    ? B HIS 63  ND1 ? ? ? 1_555 I ZN  .   ZN ? ? F HIS 63  F ZN  202 1_555 ? ? ? ? ? ? ? 2.025 ? ? 
metalc12 metalc ?    ? B HIS 71  ND1 ? ? ? 1_555 I ZN  .   ZN ? ? F HIS 71  F ZN  202 1_555 ? ? ? ? ? ? ? 2.048 ? ? 
metalc13 metalc ?    ? B HIS 80  ND1 ? ? ? 1_555 I ZN  .   ZN ? ? F HIS 80  F ZN  202 1_555 ? ? ? ? ? ? ? 1.994 ? ? 
metalc14 metalc ?    ? B ASP 83  OD1 ? ? ? 1_555 I ZN  .   ZN ? ? F ASP 83  F ZN  202 1_555 ? ? ? ? ? ? ? 1.945 ? ? 
metalc15 metalc ?    ? B HIS 120 NE2 ? ? ? 1_555 J ZN  .   ZN ? ? F HIS 120 F ZN  203 1_555 ? ? ? ? ? ? ? 1.881 ? ? 
metalc16 metalc ?    ? J ZN  .   ZN  ? ? ? 1_555 L SO4 .   O2 ? ? F ZN  203 F SO4 205 1_555 ? ? ? ? ? ? ? 1.983 ? ? 
# 
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           A 
_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    A 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       1.28 
# 
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 VAL A 94  ? ASP A 101 ? VAL A 94  ASP A 101 
AA1 2 VAL A 29  ? LYS A 36  ? VAL A 29  LYS A 36  
AA1 3 VAL A 14  ? GLN A 22  ? VAL A 14  GLN A 22  
AA1 4 THR A 2   ? GLY A 10  ? THR A 2   GLY A 10  
AA1 5 GLY A 150 ? ILE A 151 ? GLY A 150 ILE A 151 
AA2 1 ASP A 83  ? ALA A 89  ? ASP A 83  ALA A 89  
AA2 2 GLY A 41  ? HIS A 48  ? GLY A 41  HIS A 48  
AA2 3 THR A 116 ? HIS A 120 ? THR A 116 HIS A 120 
AA2 4 ARG A 143 ? VAL A 148 ? ARG A 143 VAL A 148 
AA3 1 VAL B 94  ? ASP B 101 ? VAL F 94  ASP F 101 
AA3 2 VAL B 29  ? LYS B 36  ? VAL F 29  LYS F 36  
AA3 3 GLN B 15  ? GLN B 22  ? GLN F 15  GLN F 22  
AA3 4 THR B 2   ? LYS B 9   ? THR F 2   LYS F 9   
AA3 5 GLY B 150 ? ILE B 151 ? GLY F 150 ILE F 151 
AA4 1 ASP B 83  ? ALA B 89  ? ASP F 83  ALA F 89  
AA4 2 GLY B 41  ? HIS B 48  ? GLY F 41  HIS F 48  
AA4 3 THR B 116 ? HIS B 120 ? THR F 116 HIS F 120 
AA4 4 ARG B 143 ? VAL B 148 ? ARG F 143 VAL F 148 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 O ASP A 101 ? O ASP A 101 N VAL A 29  ? N VAL A 29  
AA1 2 3 O TRP A 32  ? O TRP A 32  N ASN A 19  ? N ASN A 19  
AA1 3 4 O ILE A 18  ? O ILE A 18  N CYS A 6   ? N CYS A 6   
AA1 4 5 N VAL A 5   ? N VAL A 5   O GLY A 150 ? O GLY A 150 
AA2 1 2 O VAL A 87  ? O VAL A 87  N HIS A 43  ? N HIS A 43  
AA2 2 3 N HIS A 48  ? N HIS A 48  O THR A 116 ? O THR A 116 
AA2 3 4 N LEU A 117 ? N LEU A 117 O GLY A 147 ? O GLY A 147 
AA3 1 2 O ILE B 99  ? O ILE F 99  N VAL B 31  ? N VAL F 31  
AA3 2 3 O TRP B 32  ? O TRP F 32  N ASN B 19  ? N ASN F 19  
AA3 3 4 O GLN B 22  ? O GLN F 22  N THR B 2   ? N THR F 2   
AA3 4 5 N VAL B 5   ? N VAL F 5   O GLY B 150 ? O GLY F 150 
AA4 1 2 O ALA B 89  ? O ALA F 89  N GLY B 41  ? N GLY F 41  
AA4 2 3 N HIS B 48  ? N HIS F 48  O THR B 116 ? O THR F 116 
AA4 3 4 N VAL B 119 ? N VAL F 119 O ALA B 145 ? O ALA F 145 
# 
_atom_sites.entry_id                    7T8G 
_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]   0.025747 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.007524 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.014751 
_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]   0.020364 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
N  
O  
S  
SE 
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . ALA A 1 1   ? -4.802  -6.079  21.364  1.00 31.77 ? 1   ALA A N   1 
ATOM   2    C  CA  . ALA A 1 1   ? -3.856  -4.940  21.371  1.00 29.11 ? 1   ALA A CA  1 
ATOM   3    C  C   . ALA A 1 1   ? -2.856  -5.060  20.217  1.00 27.40 ? 1   ALA A C   1 
ATOM   4    O  O   . ALA A 1 1   ? -2.607  -6.170  19.733  1.00 28.65 ? 1   ALA A O   1 
ATOM   5    C  CB  . ALA A 1 1   ? -3.130  -4.865  22.687  1.00 30.72 ? 1   ALA A CB  1 
ATOM   6    N  N   . THR A 1 2   ? -2.285  -3.921  19.834  1.00 22.37 ? 2   THR A N   1 
ATOM   7    C  CA  . THR A 1 2   ? -1.194  -3.783  18.839  1.00 19.94 ? 2   THR A CA  1 
ATOM   8    C  C   . THR A 1 2   ? 0.029   -3.251  19.587  1.00 17.43 ? 2   THR A C   1 
ATOM   9    O  O   . THR A 1 2   ? -0.133  -2.416  20.488  1.00 16.37 ? 2   THR A O   1 
ATOM   10   C  CB  . THR A 1 2   ? -1.589  -2.861  17.679  1.00 21.83 ? 2   THR A CB  1 
ATOM   11   O  OG1 . THR A 1 2   ? -2.830  -3.338  17.147  1.00 24.59 ? 2   THR A OG1 1 
ATOM   12   C  CG2 . THR A 1 2   ? -0.551  -2.816  16.576  1.00 22.12 ? 2   THR A CG2 1 
ATOM   13   N  N   . LYS A 1 3   ? 1.206   -3.774  19.263  1.00 15.76 ? 3   LYS A N   1 
ATOM   14   C  CA  . LYS A 1 3   ? 2.465   -3.381  19.923  1.00 15.32 ? 3   LYS A CA  1 
ATOM   15   C  C   . LYS A 1 3   ? 3.507   -3.052  18.867  1.00 14.05 ? 3   LYS A C   1 
ATOM   16   O  O   . LYS A 1 3   ? 3.539   -3.684  17.791  1.00 14.62 ? 3   LYS A O   1 
ATOM   17   C  CB  . LYS A 1 3   ? 2.978   -4.492  20.837  1.00 16.42 ? 3   LYS A CB  1 
ATOM   18   C  CG  . LYS A 1 3   ? 2.078   -4.792  22.027  1.00 19.40 ? 3   LYS A CG  1 
ATOM   19   C  CD  . LYS A 1 3   ? 2.626   -5.935  22.873  1.00 22.17 ? 3   LYS A CD  1 
ATOM   20   C  CE  . LYS A 1 3   ? 3.772   -5.576  23.798  1.00 26.11 ? 3   LYS A CE  1 
ATOM   21   N  NZ  . LYS A 1 3   ? 5.102   -5.867  23.206  1.00 30.17 ? 3   LYS A NZ  1 
ATOM   22   N  N   . ALA A 1 4   ? 4.361   -2.094  19.199  1.00 12.59 ? 4   ALA A N   1 
ATOM   23   C  CA  . ALA A 1 4   ? 5.498   -1.718  18.348  1.00 12.19 ? 4   ALA A CA  1 
ATOM   24   C  C   . ALA A 1 4   ? 6.693   -1.452  19.250  1.00 12.58 ? 4   ALA A C   1 
ATOM   25   O  O   . ALA A 1 4   ? 6.537   -1.345  20.488  1.00 13.13 ? 4   ALA A O   1 
ATOM   26   C  CB  . ALA A 1 4   ? 5.168   -0.536  17.476  1.00 12.99 ? 4   ALA A CB  1 
ATOM   27   N  N   . VAL A 1 5   ? 7.873   -1.391  18.646  1.00 12.05 ? 5   VAL A N   1 
ATOM   28   C  CA  . VAL A 1 5   ? 9.127   -1.257  19.423  1.00 12.54 ? 5   VAL A CA  1 
ATOM   29   C  C   . VAL A 1 5   ? 10.113  -0.506  18.551  1.00 12.31 ? 5   VAL A C   1 
ATOM   30   O  O   . VAL A 1 5   ? 10.016  -0.560  17.301  1.00 13.17 ? 5   VAL A O   1 
ATOM   31   C  CB  . VAL A 1 5   ? 9.647   -2.637  19.848  1.00 12.90 ? 5   VAL A CB  1 
ATOM   32   C  CG1 . VAL A 1 5   ? 10.028  -3.481  18.638  1.00 13.41 ? 5   VAL A CG1 1 
ATOM   33   C  CG2 . VAL A 1 5   ? 10.802  -2.532  20.840  1.00 13.83 ? 5   VAL A CG2 1 
ATOM   34   N  N   . CYS A 1 6   ? 11.022  0.201   19.193  1.00 12.64 ? 6   CYS A N   1 
ATOM   35   C  CA  . CYS A 1 6   ? 12.054  0.965   18.498  1.00 12.00 ? 6   CYS A CA  1 
ATOM   36   C  C   . CYS A 1 6   ? 13.339  0.898   19.301  1.00 13.35 ? 6   CYS A C   1 
ATOM   37   O  O   . CYS A 1 6   ? 13.299  1.186   20.509  1.00 13.34 ? 6   CYS A O   1 
ATOM   38   C  CB  . CYS A 1 6   ? 11.612  2.408   18.370  1.00 12.00 ? 6   CYS A CB  1 
ATOM   39   S  SG  . CYS A 1 6   ? 12.781  3.391   17.406  1.00 14.39 ? 6   CYS A SG  1 
ATOM   40   N  N   . VAL A 1 7   ? 14.417  0.496   18.655  1.00 13.23 ? 7   VAL A N   1 
ATOM   41   C  CA  . VAL A 1 7   ? 15.780  0.575   19.236  1.00 14.66 ? 7   VAL A CA  1 
ATOM   42   C  C   . VAL A 1 7   ? 16.411  1.880   18.773  1.00 15.04 ? 7   VAL A C   1 
ATOM   43   O  O   . VAL A 1 7   ? 16.623  2.055   17.569  1.00 15.74 ? 7   VAL A O   1 
ATOM   44   C  CB  . VAL A 1 7   ? 16.606  -0.655  18.839  1.00 15.80 ? 7   VAL A CB  1 
ATOM   45   C  CG1 . VAL A 1 7   ? 17.996  -0.558  19.429  1.00 17.11 ? 7   VAL A CG1 1 
ATOM   46   C  CG2 . VAL A 1 7   ? 15.917  -1.939  19.252  1.00 16.23 ? 7   VAL A CG2 1 
ATOM   47   N  N   . LEU A 1 8   ? 16.688  2.772   19.719  1.00 14.98 ? 8   LEU A N   1 
ATOM   48   C  CA  . LEU A 1 8   ? 17.357  4.065   19.425  1.00 14.99 ? 8   LEU A CA  1 
ATOM   49   C  C   . LEU A 1 8   ? 18.865  3.867   19.497  1.00 16.17 ? 8   LEU A C   1 
ATOM   50   O  O   . LEU A 1 8   ? 19.328  3.353   20.514  1.00 16.02 ? 8   LEU A O   1 
ATOM   51   C  CB  . LEU A 1 8   ? 16.913  5.088   20.469  1.00 15.95 ? 8   LEU A CB  1 
ATOM   52   C  CG  . LEU A 1 8   ? 15.439  5.474   20.402  1.00 16.72 ? 8   LEU A CG  1 
ATOM   53   C  CD1 . LEU A 1 8   ? 15.065  6.373   21.584  1.00 16.93 ? 8   LEU A CD1 1 
ATOM   54   C  CD2 . LEU A 1 8   ? 15.141  6.158   19.096  1.00 17.80 ? 8   LEU A CD2 1 
ATOM   55   N  N   . LYS A 1 9   ? 19.584  4.251   18.451  1.00 16.24 ? 9   LYS A N   1 
ATOM   56   C  CA  . LYS A 1 9   ? 21.066  4.174   18.459  1.00 18.80 ? 9   LYS A CA  1 
ATOM   57   C  C   . LYS A 1 9   ? 21.644  5.432   17.837  1.00 18.80 ? 9   LYS A C   1 
ATOM   58   O  O   . LYS A 1 9   ? 21.067  5.953   16.880  1.00 17.16 ? 9   LYS A O   1 
ATOM   59   C  CB  . LYS A 1 9   ? 21.568  2.940   17.717  1.00 21.16 ? 9   LYS A CB  1 
ATOM   60   C  CG  . LYS A 1 9   ? 21.344  1.624   18.443  1.00 24.09 ? 9   LYS A CG  1 
ATOM   61   C  CD  . LYS A 1 9   ? 22.076  0.466   17.779  1.00 27.17 ? 9   LYS A CD  1 
ATOM   62   C  CE  . LYS A 1 9   ? 21.314  -0.843  17.814  1.00 30.40 ? 9   LYS A CE  1 
ATOM   63   N  NZ  . LYS A 1 9   ? 21.641  -1.657  19.007  1.00 31.77 ? 9   LYS A NZ  1 
ATOM   64   N  N   . GLY A 1 10  ? 22.711  5.903   18.485  1.00 21.29 ? 10  GLY A N   1 
ATOM   65   C  CA  . GLY A 1 10  ? 23.532  7.028   18.038  1.00 21.83 ? 10  GLY A CA  1 
ATOM   66   C  C   . GLY A 1 10  ? 24.785  7.124   18.879  1.00 21.40 ? 10  GLY A C   1 
ATOM   67   O  O   . GLY A 1 10  ? 24.917  6.364   19.878  1.00 20.19 ? 10  GLY A O   1 
ATOM   68   N  N   . ASP A 1 11  ? 25.654  8.054   18.498  1.00 22.03 ? 11  ASP A N   1 
ATOM   69   C  CA  . ASP A 1 11  ? 27.017  8.231   19.057  1.00 23.41 ? 11  ASP A CA  1 
ATOM   70   C  C   . ASP A 1 11  ? 26.919  8.658   20.526  1.00 22.57 ? 11  ASP A C   1 
ATOM   71   O  O   . ASP A 1 11  ? 26.066  9.504   20.861  1.00 22.93 ? 11  ASP A O   1 
ATOM   72   C  CB  . ASP A 1 11  ? 27.802  9.252   18.235  1.00 25.74 ? 11  ASP A CB  1 
ATOM   73   C  CG  . ASP A 1 11  ? 28.085  8.811   16.808  0.70 29.57 ? 11  ASP A CG  1 
ATOM   74   O  OD1 . ASP A 1 11  ? 27.316  7.977   16.286  0.70 32.28 ? 11  ASP A OD1 1 
ATOM   75   O  OD2 . ASP A 1 11  ? 29.057  9.326   16.217  0.70 33.06 ? 11  ASP A OD2 1 
ATOM   76   N  N   . GLY A 1 12  ? 27.764  8.104   21.363  1.00 23.48 ? 12  GLY A N   1 
ATOM   77   C  CA  . GLY A 1 12  ? 27.823  8.484   22.783  1.00 24.16 ? 12  GLY A CA  1 
ATOM   78   C  C   . GLY A 1 12  ? 28.396  7.324   23.625  1.00 24.77 ? 12  GLY A C   1 
ATOM   79   O  O   . GLY A 1 12  ? 29.463  7.598   24.201  1.00 26.48 ? 12  GLY A O   1 
ATOM   80   N  N   . PRO A 1 13  ? 27.802  6.083   23.730  1.00 25.04 ? 13  PRO A N   1 
ATOM   81   C  CA  . PRO A 1 13  ? 26.566  5.741   23.017  1.00 23.93 ? 13  PRO A CA  1 
ATOM   82   C  C   . PRO A 1 13  ? 25.293  6.362   23.620  1.00 23.05 ? 13  PRO A C   1 
ATOM   83   O  O   . PRO A 1 13  ? 25.137  6.302   24.819  1.00 24.10 ? 13  PRO A O   1 
ATOM   84   C  CB  . PRO A 1 13  ? 26.463  4.209   23.153  1.00 26.66 ? 13  PRO A CB  1 
ATOM   85   C  CG  . PRO A 1 13  ? 27.760  3.750   23.792  1.00 27.39 ? 13  PRO A CG  1 
ATOM   86   C  CD  . PRO A 1 13  ? 28.301  4.956   24.532  1.00 25.88 ? 13  PRO A CD  1 
ATOM   87   N  N   . VAL A 1 14  ? 24.451  7.018   22.811  1.00 23.32 ? 14  VAL A N   1 
ATOM   88   C  CA  . VAL A 1 14  ? 23.025  7.267   23.192  1.00 22.19 ? 14  VAL A CA  1 
ATOM   89   C  C   . VAL A 1 14  ? 22.250  6.061   22.671  1.00 21.79 ? 14  VAL A C   1 
ATOM   90   O  O   . VAL A 1 14  ? 22.281  5.799   21.458  1.00 24.17 ? 14  VAL A O   1 
ATOM   91   C  CB  . VAL A 1 14  ? 22.433  8.583   22.654  1.00 21.87 ? 14  VAL A CB  1 
ATOM   92   C  CG1 . VAL A 1 14  ? 20.941  8.690   22.989  1.00 21.77 ? 14  VAL A CG1 1 
ATOM   93   C  CG2 . VAL A 1 14  ? 23.180  9.792   23.190  1.00 22.39 ? 14  VAL A CG2 1 
ATOM   94   N  N   . GLN A 1 15  ? 21.616  5.326   23.566  1.00 22.18 ? 15  GLN A N   1 
ATOM   95   C  CA  . GLN A 1 15  ? 21.058  3.983   23.278  1.00 22.46 ? 15  GLN A CA  1 
ATOM   96   C  C   . GLN A 1 15  ? 19.762  3.856   24.066  1.00 20.49 ? 15  GLN A C   1 
ATOM   97   O  O   . GLN A 1 15  ? 19.740  4.206   25.243  1.00 20.04 ? 15  GLN A O   1 
ATOM   98   C  CB  . GLN A 1 15  ? 22.106  2.918   23.621  1.00 24.87 ? 15  GLN A CB  1 
ATOM   99   C  CG  . GLN A 1 15  ? 21.543  1.594   24.116  1.00 26.65 ? 15  GLN A CG  1 
ATOM   100  N  N   . GLY A 1 16  ? 18.696  3.395   23.436  1.00 17.03 ? 16  GLY A N   1 
ATOM   101  C  CA  . GLY A 1 16  ? 17.427  3.238   24.144  1.00 18.18 ? 16  GLY A CA  1 
ATOM   102  C  C   . GLY A 1 16  ? 16.559  2.190   23.501  1.00 16.59 ? 16  GLY A C   1 
ATOM   103  O  O   . GLY A 1 16  ? 16.828  1.783   22.370  1.00 17.64 ? 16  GLY A O   1 
ATOM   104  N  N   . ILE A 1 17  ? 15.577  1.762   24.260  1.00 16.64 ? 17  ILE A N   1 
ATOM   105  C  CA  . ILE A 1 17  ? 14.495  0.860   23.803  1.00 16.29 ? 17  ILE A CA  1 
ATOM   106  C  C   . ILE A 1 17  ? 13.189  1.544   24.177  1.00 14.87 ? 17  ILE A C   1 
ATOM   107  O  O   . ILE A 1 17  ? 12.975  1.862   25.362  1.00 14.35 ? 17  ILE A O   1 
ATOM   108  C  CB  . ILE A 1 17  ? 14.598  -0.537  24.430  1.00 18.53 ? 17  ILE A CB  1 
ATOM   109  C  CG1 . ILE A 1 17  ? 15.975  -1.167  24.217  1.00 22.28 ? 17  ILE A CG1 1 
ATOM   110  C  CG2 . ILE A 1 17  ? 13.467  -1.407  23.906  1.00 19.70 ? 17  ILE A CG2 1 
ATOM   111  C  CD1 . ILE A 1 17  ? 16.250  -1.610  22.816  1.00 23.25 ? 17  ILE A CD1 1 
ATOM   112  N  N   . ILE A 1 18  ? 12.327  1.733   23.191  1.00 14.13 ? 18  ILE A N   1 
ATOM   113  C  CA  . ILE A 1 18  ? 11.010  2.371   23.398  1.00 13.88 ? 18  ILE A CA  1 
ATOM   114  C  C   . ILE A 1 18  ? 9.933   1.434   22.876  1.00 13.15 ? 18  ILE A C   1 
ATOM   115  O  O   . ILE A 1 18  ? 10.078  0.923   21.760  1.00 14.18 ? 18  ILE A O   1 
ATOM   116  C  CB  . ILE A 1 18  ? 10.952  3.742   22.721  1.00 13.83 ? 18  ILE A CB  1 
ATOM   117  C  CG1 . ILE A 1 18  ? 12.027  4.690   23.260  1.00 14.41 ? 18  ILE A CG1 1 
ATOM   118  C  CG2 . ILE A 1 18  ? 9.572   4.342   22.865  1.00 14.06 ? 18  ILE A CG2 1 
ATOM   119  C  CD1 . ILE A 1 18  ? 11.856  5.091   24.705  1.00 16.20 ? 18  ILE A CD1 1 
ATOM   120  N  N   . ASN A 1 19  ? 8.967   1.153   23.738  1.00 13.64 ? 19  ASN A N   1 
ATOM   121  C  CA  . ASN A 1 19  ? 7.826   0.258   23.477  1.00 14.20 ? 19  ASN A CA  1 
ATOM   122  C  C   . ASN A 1 19  ? 6.579   1.100   23.259  1.00 13.54 ? 19  ASN A C   1 
ATOM   123  O  O   . ASN A 1 19  ? 6.455   2.161   23.892  1.00 14.52 ? 19  ASN A O   1 
ATOM   124  C  CB  . ASN A 1 19  ? 7.632   -0.700  24.647  1.00 15.15 ? 19  ASN A CB  1 
ATOM   125  C  CG  . ASN A 1 19  ? 8.894   -1.471  24.948  1.00 16.83 ? 19  ASN A CG  1 
ATOM   126  O  OD1 . ASN A 1 19  ? 9.215   -2.420  24.251  1.00 19.16 ? 19  ASN A OD1 1 
ATOM   127  N  ND2 . ASN A 1 19  ? 9.646   -1.049  25.949  1.00 18.36 ? 19  ASN A ND2 1 
ATOM   128  N  N   . PHE A 1 20  ? 5.702   0.646   22.377  1.00 12.71 ? 20  PHE A N   1 
ATOM   129  C  CA  . PHE A 1 20  ? 4.400   1.268   22.078  1.00 13.56 ? 20  PHE A CA  1 
ATOM   130  C  C   . PHE A 1 20  ? 3.340   0.190   22.230  1.00 13.92 ? 20  PHE A C   1 
ATOM   131  O  O   . PHE A 1 20  ? 3.525   -0.919  21.728  1.00 14.12 ? 20  PHE A O   1 
ATOM   132  C  CB  . PHE A 1 20  ? 4.369   1.816   20.654  1.00 13.29 ? 20  PHE A CB  1 
ATOM   133  C  CG  . PHE A 1 20  ? 5.461   2.810   20.318  1.00 13.42 ? 20  PHE A CG  1 
ATOM   134  C  CD1 . PHE A 1 20  ? 6.735   2.402   19.938  1.00 13.52 ? 20  PHE A CD1 1 
ATOM   135  C  CD2 . PHE A 1 20  ? 5.211   4.170   20.386  1.00 14.40 ? 20  PHE A CD2 1 
ATOM   136  C  CE1 . PHE A 1 20  ? 7.722   3.327   19.618  1.00 13.71 ? 20  PHE A CE1 1 
ATOM   137  C  CE2 . PHE A 1 20  ? 6.195   5.091   20.068  1.00 14.22 ? 20  PHE A CE2 1 
ATOM   138  C  CZ  . PHE A 1 20  ? 7.453   4.668   19.696  1.00 13.92 ? 20  PHE A CZ  1 
ATOM   139  N  N   . GLU A 1 21  ? 2.238   0.518   22.888  1.00 15.52 ? 21  GLU A N   1 
ATOM   140  C  CA  . GLU A 1 21  ? 1.108   -0.425  23.005  1.00 17.57 ? 21  GLU A CA  1 
ATOM   141  C  C   . GLU A 1 21  ? -0.179  0.358   22.824  1.00 15.63 ? 21  GLU A C   1 
ATOM   142  O  O   . GLU A 1 21  ? -0.295  1.441   23.388  1.00 14.92 ? 21  GLU A O   1 
ATOM   143  C  CB  . GLU A 1 21  ? 1.143   -1.159  24.338  1.00 19.65 ? 21  GLU A CB  1 
ATOM   144  C  CG  . GLU A 1 21  ? 0.074   -2.234  24.447  1.00 24.52 ? 21  GLU A CG  1 
ATOM   145  C  CD  . GLU A 1 21  ? 0.255   -3.219  25.586  1.00 28.27 ? 21  GLU A CD  1 
ATOM   146  O  OE1 . GLU A 1 21  ? 1.319   -3.200  26.216  1.00 33.92 ? 21  GLU A OE1 1 
ATOM   147  O  OE2 . GLU A 1 21  ? -0.680  -4.000  25.836  1.00 36.19 ? 21  GLU A OE2 1 
ATOM   148  N  N   . GLN A 1 22  ? -1.093  -0.183  22.031  1.00 15.76 ? 22  GLN A N   1 
ATOM   149  C  CA  . GLN A 1 22  ? -2.423  0.409   21.782  1.00 16.45 ? 22  GLN A CA  1 
ATOM   150  C  C   . GLN A 1 22  ? -3.454  -0.700  21.975  1.00 17.17 ? 22  GLN A C   1 
ATOM   151  O  O   . GLN A 1 22  ? -3.399  -1.676  21.238  1.00 17.30 ? 22  GLN A O   1 
ATOM   152  C  CB  . GLN A 1 22  ? -2.415  1.046   20.398  1.00 16.44 ? 22  GLN A CB  1 
ATOM   153  C  CG  . GLN A 1 22  ? -3.662  1.874   20.127  1.00 16.73 ? 22  GLN A CG  1 
ATOM   154  C  CD  . GLN A 1 22  ? -3.650  2.503   18.757  1.00 16.15 ? 22  GLN A CD  1 
ATOM   155  O  OE1 . GLN A 1 22  ? -3.066  1.947   17.824  1.00 17.95 ? 22  GLN A OE1 1 
ATOM   156  N  NE2 . GLN A 1 22  ? -4.290  3.654   18.612  1.00 15.82 ? 22  GLN A NE2 1 
ATOM   157  N  N   . LYS A 1 23  ? -4.359  -0.523  22.936  1.00 19.45 ? 23  LYS A N   1 
ATOM   158  C  CA  . LYS A 1 23  ? -5.410  -1.526  23.255  1.00 21.54 ? 23  LYS A CA  1 
ATOM   159  C  C   . LYS A 1 23  ? -6.424  -1.623  22.110  1.00 22.90 ? 23  LYS A C   1 
ATOM   160  O  O   . LYS A 1 23  ? -6.884  -2.748  21.841  1.00 24.30 ? 23  LYS A O   1 
ATOM   161  C  CB  . LYS A 1 23  ? -6.120  -1.176  24.564  1.00 22.50 ? 23  LYS A CB  1 
ATOM   162  N  N   . GLU A 1 24  ? -6.780  -0.496  21.487  1.00 23.26 ? 24  GLU A N   1 
ATOM   163  C  CA  . GLU A 1 24  ? -7.780  -0.405  20.388  1.00 24.06 ? 24  GLU A CA  1 
ATOM   164  C  C   . GLU A 1 24  ? -7.405  0.749   19.455  1.00 22.50 ? 24  GLU A C   1 
ATOM   165  O  O   . GLU A 1 24  ? -6.789  1.713   19.935  1.00 21.72 ? 24  GLU A O   1 
ATOM   166  C  CB  . GLU A 1 24  ? -9.201  -0.241  20.943  1.00 26.09 ? 24  GLU A CB  1 
ATOM   167  C  CG  . GLU A 1 24  ? -9.291  0.519   22.257  1.00 28.42 ? 24  GLU A CG  1 
ATOM   168  N  N   . SER A 1 25  ? -7.774  0.658   18.176  1.00 22.54 ? 25  SER A N   1 
ATOM   169  C  CA  . SER A 1 25  ? -7.409  1.645   17.121  1.00 23.98 ? 25  SER A CA  1 
ATOM   170  C  C   . SER A 1 25  ? -7.959  3.038   17.470  1.00 24.24 ? 25  SER A C   1 
ATOM   171  O  O   . SER A 1 25  ? -7.361  4.045   17.039  1.00 25.17 ? 25  SER A O   1 
ATOM   172  C  CB  . SER A 1 25  ? -7.842  1.195   15.743  1.00 25.24 ? 25  SER A CB  1 
ATOM   173  O  OG  . SER A 1 25  ? -9.257  1.130   15.653  1.00 26.76 ? 25  SER A OG  1 
ATOM   174  N  N   . ASN A 1 26  ? -9.046  3.110   18.243  1.00 24.31 ? 26  ASN A N   1 
ATOM   175  C  CA  . ASN A 1 26  ? -9.669  4.398   18.657  1.00 24.47 ? 26  ASN A CA  1 
ATOM   176  C  C   . ASN A 1 26  ? -9.124  4.828   20.029  1.00 24.05 ? 26  ASN A C   1 
ATOM   177  O  O   . ASN A 1 26  ? -9.682  5.790   20.616  1.00 24.40 ? 26  ASN A O   1 
ATOM   178  C  CB  . ASN A 1 26  ? -11.201 4.325   18.624  1.00 26.28 ? 26  ASN A CB  1 
ATOM   179  C  CG  . ASN A 1 26  ? -11.793 3.245   19.502  1.00 30.03 ? 26  ASN A CG  1 
ATOM   180  O  OD1 . ASN A 1 26  ? -11.153 2.234   19.763  1.00 32.59 ? 26  ASN A OD1 1 
ATOM   181  N  ND2 . ASN A 1 26  ? -13.023 3.433   19.953  1.00 31.34 ? 26  ASN A ND2 1 
ATOM   182  N  N   . GLY A 1 27  ? -8.084  4.162   20.531  1.00 21.36 ? 27  GLY A N   1 
ATOM   183  C  CA  . GLY A 1 27  ? -7.552  4.410   21.877  1.00 19.74 ? 27  GLY A CA  1 
ATOM   184  C  C   . GLY A 1 27  ? -6.165  5.045   21.863  1.00 19.49 ? 27  GLY A C   1 
ATOM   185  O  O   . GLY A 1 27  ? -5.486  5.124   20.835  1.00 19.19 ? 27  GLY A O   1 
ATOM   186  N  N   . PRO A 1 28  ? -5.706  5.508   23.040  1.00 19.15 ? 28  PRO A N   1 
ATOM   187  C  CA  . PRO A 1 28  ? -4.373  6.083   23.173  1.00 18.65 ? 28  PRO A CA  1 
ATOM   188  C  C   . PRO A 1 28  ? -3.279  5.018   23.027  1.00 17.24 ? 28  PRO A C   1 
ATOM   189  O  O   . PRO A 1 28  ? -3.514  3.835   23.202  1.00 17.56 ? 28  PRO A O   1 
ATOM   190  C  CB  . PRO A 1 28  ? -4.379  6.696   24.581  1.00 20.32 ? 28  PRO A CB  1 
ATOM   191  C  CG  . PRO A 1 28  ? -5.410  5.899   25.338  1.00 21.70 ? 28  PRO A CG  1 
ATOM   192  C  CD  . PRO A 1 28  ? -6.449  5.500   24.312  1.00 19.97 ? 28  PRO A CD  1 
ATOM   193  N  N   . VAL A 1 29  ? -2.078  5.498   22.717  1.00 16.43 ? 29  VAL A N   1 
ATOM   194  C  CA  . VAL A 1 29  ? -0.854  4.667   22.624  1.00 15.98 ? 29  VAL A CA  1 
ATOM   195  C  C   . VAL A 1 29  ? -0.028  4.936   23.879  1.00 15.96 ? 29  VAL A C   1 
ATOM   196  O  O   . VAL A 1 29  ? 0.267   6.116   24.138  1.00 16.49 ? 29  VAL A O   1 
ATOM   197  C  CB  . VAL A 1 29  ? -0.053  4.982   21.348  1.00 15.48 ? 29  VAL A CB  1 
ATOM   198  C  CG1 . VAL A 1 29  ? 1.187   4.108   21.263  1.00 15.45 ? 29  VAL A CG1 1 
ATOM   199  C  CG2 . VAL A 1 29  ? -0.915  4.849   20.100  1.00 16.14 ? 29  VAL A CG2 1 
ATOM   200  N  N   . LYS A 1 30  ? 0.301   3.895   24.631  1.00 16.54 ? 30  LYS A N   1 
ATOM   201  C  CA  . LYS A 1 30  ? 1.253   3.972   25.765  1.00 18.28 ? 30  LYS A CA  1 
ATOM   202  C  C   . LYS A 1 30  ? 2.656   3.831   25.175  1.00 17.76 ? 30  LYS A C   1 
ATOM   203  O  O   . LYS A 1 30  ? 2.873   2.911   24.364  1.00 17.23 ? 30  LYS A O   1 
ATOM   204  C  CB  . LYS A 1 30  ? 0.946   2.876   26.790  1.00 20.35 ? 30  LYS A CB  1 
ATOM   205  C  CG  . LYS A 1 30  ? 1.772   2.926   28.068  1.00 24.77 ? 30  LYS A CG  1 
ATOM   206  C  CD  . LYS A 1 30  ? 1.732   1.652   28.863  1.00 27.52 ? 30  LYS A CD  1 
ATOM   207  C  CE  . LYS A 1 30  ? 2.779   1.588   29.954  1.00 29.22 ? 30  LYS A CE  1 
ATOM   208  N  NZ  . LYS A 1 30  ? 3.331   0.219   30.088  1.00 32.02 ? 30  LYS A NZ  1 
ATOM   209  N  N   . VAL A 1 31  ? 3.557   4.725   25.557  1.00 17.39 ? 31  VAL A N   1 
ATOM   210  C  CA  . VAL A 1 31  ? 4.963   4.758   25.073  1.00 17.49 ? 31  VAL A CA  1 
ATOM   211  C  C   . VAL A 1 31  ? 5.837   4.645   26.313  1.00 17.91 ? 31  VAL A C   1 
ATOM   212  O  O   . VAL A 1 31  ? 5.703   5.504   27.202  1.00 19.78 ? 31  VAL A O   1 
ATOM   213  C  CB  . VAL A 1 31  ? 5.251   6.064   24.308  1.00 16.91 ? 31  VAL A CB  1 
ATOM   214  C  CG1 . VAL A 1 31  ? 6.657   6.087   23.723  1.00 17.00 ? 31  VAL A CG1 1 
ATOM   215  C  CG2 . VAL A 1 31  ? 4.213   6.339   23.240  1.00 16.45 ? 31  VAL A CG2 1 
ATOM   216  N  N   . TRP A 1 32  ? 6.683   3.639   26.416  1.00 17.44 ? 32  TRP A N   1 
ATOM   217  C  CA  . TRP A 1 32  ? 7.525   3.495   27.621  1.00 16.86 ? 32  TRP A CA  1 
ATOM   218  C  C   . TRP A 1 32  ? 8.844   2.826   27.264  1.00 16.46 ? 32  TRP A C   1 
ATOM   219  O  O   . TRP A 1 32  ? 8.910   2.061   26.304  1.00 15.63 ? 32  TRP A O   1 
ATOM   220  C  CB  . TRP A 1 32  ? 6.772   2.740   28.712  1.00 18.62 ? 32  TRP A CB  1 
ATOM   221  C  CG  . TRP A 1 32  ? 6.653   1.274   28.465  1.00 20.13 ? 32  TRP A CG  1 
ATOM   222  C  CD1 . TRP A 1 32  ? 7.457   0.294   28.967  1.00 21.34 ? 32  TRP A CD1 1 
ATOM   223  C  CD2 . TRP A 1 32  ? 5.680   0.612   27.643  1.00 20.15 ? 32  TRP A CD2 1 
ATOM   224  N  NE1 . TRP A 1 32  ? 7.045   -0.933  28.533  1.00 22.88 ? 32  TRP A NE1 1 
ATOM   225  C  CE2 . TRP A 1 32  ? 5.945   -0.771  27.730  1.00 20.78 ? 32  TRP A CE2 1 
ATOM   226  C  CE3 . TRP A 1 32  ? 4.616   1.055   26.853  1.00 21.20 ? 32  TRP A CE3 1 
ATOM   227  C  CZ2 . TRP A 1 32  ? 5.191   -1.711  27.036  1.00 21.58 ? 32  TRP A CZ2 1 
ATOM   228  C  CZ3 . TRP A 1 32  ? 3.867   0.126   26.169  1.00 22.55 ? 32  TRP A CZ3 1 
ATOM   229  C  CH2 . TRP A 1 32  ? 4.151   -1.237  26.267  1.00 21.36 ? 32  TRP A CH2 1 
ATOM   230  N  N   . GLY A 1 33  ? 9.851   3.091   28.083  1.00 15.68 ? 33  GLY A N   1 
ATOM   231  C  CA  . GLY A 1 33  ? 11.153  2.442   27.982  1.00 16.04 ? 33  GLY A CA  1 
ATOM   232  C  C   . GLY A 1 33  ? 12.195  3.329   28.603  1.00 17.74 ? 33  GLY A C   1 
ATOM   233  O  O   . GLY A 1 33  ? 11.864  4.080   29.513  1.00 19.15 ? 33  GLY A O   1 
ATOM   234  N  N   . SER A 1 34  ? 13.419  3.245   28.134  1.00 17.33 ? 34  SER A N   1 
ATOM   235  C  CA  A SER A 1 34  ? 14.566  3.924   28.780  0.50 17.97 ? 34  SER A CA  1 
ATOM   236  C  CA  B SER A 1 34  ? 14.561  3.933   28.779  0.50 18.05 ? 34  SER A CA  1 
ATOM   237  C  C   . SER A 1 34  ? 15.567  4.318   27.703  1.00 17.33 ? 34  SER A C   1 
ATOM   238  O  O   . SER A 1 34  ? 15.687  3.563   26.725  1.00 17.66 ? 34  SER A O   1 
ATOM   239  C  CB  A SER A 1 34  ? 15.192  3.023   29.812  0.50 18.41 ? 34  SER A CB  1 
ATOM   240  C  CB  B SER A 1 34  ? 15.183  3.059   29.844  0.50 18.66 ? 34  SER A CB  1 
ATOM   241  O  OG  A SER A 1 34  ? 16.247  3.689   30.488  0.50 20.05 ? 34  SER A OG  1 
ATOM   242  O  OG  B SER A 1 34  ? 15.885  1.966   29.278  0.50 20.45 ? 34  SER A OG  1 
ATOM   243  N  N   . ILE A 1 35  ? 16.235  5.442   27.901  1.00 16.84 ? 35  ILE A N   1 
ATOM   244  C  CA  . ILE A 1 35  ? 17.309  5.909   26.981  1.00 17.06 ? 35  ILE A CA  1 
ATOM   245  C  C   . ILE A 1 35  ? 18.501  6.273   27.847  1.00 18.32 ? 35  ILE A C   1 
ATOM   246  O  O   . ILE A 1 35  ? 18.298  7.026   28.797  1.00 19.50 ? 35  ILE A O   1 
ATOM   247  C  CB  . ILE A 1 35  ? 16.852  7.102   26.132  1.00 17.06 ? 35  ILE A CB  1 
ATOM   248  C  CG1 . ILE A 1 35  ? 15.491  6.859   25.479  1.00 18.26 ? 35  ILE A CG1 1 
ATOM   249  C  CG2 . ILE A 1 35  ? 17.932  7.464   25.115  1.00 17.36 ? 35  ILE A CG2 1 
ATOM   250  C  CD1 . ILE A 1 35  ? 14.890  8.094   24.842  1.00 18.59 ? 35  ILE A CD1 1 
ATOM   251  N  N   . LYS A 1 36  ? 19.676  5.750   27.533  1.00 18.09 ? 36  LYS A N   1 
ATOM   252  C  CA  . LYS A 1 36  ? 20.894  6.017   28.335  1.00 19.57 ? 36  LYS A CA  1 
ATOM   253  C  C   . LYS A 1 36  ? 21.868  6.857   27.506  1.00 20.33 ? 36  LYS A C   1 
ATOM   254  O  O   . LYS A 1 36  ? 21.746  6.924   26.260  1.00 20.06 ? 36  LYS A O   1 
ATOM   255  C  CB  . LYS A 1 36  ? 21.515  4.710   28.822  1.00 20.64 ? 36  LYS A CB  1 
ATOM   256  C  CG  . LYS A 1 36  ? 22.229  3.896   27.758  1.00 23.38 ? 36  LYS A CG  1 
ATOM   257  N  N   . GLY A 1 37  ? 22.797  7.519   28.190  1.00 19.42 ? 37  GLY A N   1 
ATOM   258  C  CA  . GLY A 1 37  ? 23.853  8.317   27.551  1.00 19.03 ? 37  GLY A CA  1 
ATOM   259  C  C   . GLY A 1 37  ? 23.424  9.738   27.226  1.00 18.33 ? 37  GLY A C   1 
ATOM   260  O  O   . GLY A 1 37  ? 24.115  10.381  26.429  1.00 19.33 ? 37  GLY A O   1 
ATOM   261  N  N   . LEU A 1 38  ? 22.310  10.225  27.783  1.00 18.00 ? 38  LEU A N   1 
ATOM   262  C  CA  . LEU A 1 38  ? 21.818  11.604  27.529  1.00 18.60 ? 38  LEU A CA  1 
ATOM   263  C  C   . LEU A 1 38  ? 22.401  12.580  28.553  1.00 19.56 ? 38  LEU A C   1 
ATOM   264  O  O   . LEU A 1 38  ? 22.596  12.181  29.718  1.00 22.92 ? 38  LEU A O   1 
ATOM   265  C  CB  . LEU A 1 38  ? 20.290  11.639  27.602  1.00 18.57 ? 38  LEU A CB  1 
ATOM   266  C  CG  . LEU A 1 38  ? 19.565  10.917  26.470  1.00 18.71 ? 38  LEU A CG  1 
ATOM   267  C  CD1 . LEU A 1 38  ? 18.085  10.816  26.787  1.00 17.79 ? 38  LEU A CD1 1 
ATOM   268  C  CD2 . LEU A 1 38  ? 19.796  11.637  25.145  1.00 17.68 ? 38  LEU A CD2 1 
ATOM   269  N  N   . THR A 1 39  ? 22.624  13.819  28.134  1.00 20.33 ? 39  THR A N   1 
ATOM   270  C  CA  . THR A 1 39  ? 22.939  14.937  29.059  1.00 20.24 ? 39  THR A CA  1 
ATOM   271  C  C   . THR A 1 39  ? 21.708  15.210  29.926  1.00 21.31 ? 39  THR A C   1 
ATOM   272  O  O   . THR A 1 39  ? 20.564  15.059  29.446  1.00 19.39 ? 39  THR A O   1 
ATOM   273  C  CB  . THR A 1 39  ? 23.437  16.177  28.312  1.00 20.46 ? 39  THR A CB  1 
ATOM   274  O  OG1 . THR A 1 39  ? 22.405  16.647  27.443  1.00 22.46 ? 39  THR A OG1 1 
ATOM   275  C  CG2 . THR A 1 39  ? 24.723  15.897  27.564  1.00 21.15 ? 39  THR A CG2 1 
ATOM   276  N  N   . GLU A 1 40  ? 21.936  15.626  31.170  1.00 21.20 ? 40  GLU A N   1 
ATOM   277  C  CA  . GLU A 1 40  ? 20.830  15.951  32.104  1.00 21.50 ? 40  GLU A CA  1 
ATOM   278  C  C   . GLU A 1 40  ? 19.973  17.062  31.493  1.00 20.93 ? 40  GLU A C   1 
ATOM   279  O  O   . GLU A 1 40  ? 20.536  18.040  30.970  1.00 22.52 ? 40  GLU A O   1 
ATOM   280  C  CB  . GLU A 1 40  ? 21.391  16.394  33.452  1.00 22.37 ? 40  GLU A CB  1 
ATOM   281  C  CG  . GLU A 1 40  ? 20.319  16.851  34.423  1.00 22.77 ? 40  GLU A CG  1 
ATOM   282  C  CD  . GLU A 1 40  ? 20.847  17.491  35.686  1.00 24.77 ? 40  GLU A CD  1 
ATOM   283  O  OE1 . GLU A 1 40  ? 21.957  18.082  35.649  1.00 26.14 ? 40  GLU A OE1 1 
ATOM   284  O  OE2 . GLU A 1 40  ? 20.131  17.399  36.688  1.00 23.08 ? 40  GLU A OE2 1 
ATOM   285  N  N   . GLY A 1 41  ? 18.652  16.891  31.521  1.00 20.67 ? 41  GLY A N   1 
ATOM   286  C  CA  . GLY A 1 41  ? 17.693  17.892  31.039  1.00 19.64 ? 41  GLY A CA  1 
ATOM   287  C  C   . GLY A 1 41  ? 16.753  17.341  29.979  1.00 18.67 ? 41  GLY A C   1 
ATOM   288  O  O   . GLY A 1 41  ? 16.661  16.107  29.870  1.00 18.91 ? 41  GLY A O   1 
ATOM   289  N  N   . LEU A 1 42  ? 16.107  18.234  29.243  1.00 17.71 ? 42  LEU A N   1 
ATOM   290  C  CA  . LEU A 1 42  ? 15.036  17.909  28.262  1.00 19.17 ? 42  LEU A CA  1 
ATOM   291  C  C   . LEU A 1 42  ? 15.698  17.561  26.931  1.00 18.10 ? 42  LEU A C   1 
ATOM   292  O  O   . LEU A 1 42  ? 16.640  18.258  26.495  1.00 18.21 ? 42  LEU A O   1 
ATOM   293  C  CB  . LEU A 1 42  ? 14.068  19.081  28.074  1.00 19.67 ? 42  LEU A CB  1 
ATOM   294  C  CG  . LEU A 1 42  ? 12.922  19.175  29.078  1.00 22.58 ? 42  LEU A CG  1 
ATOM   295  C  CD1 . LEU A 1 42  ? 13.463  19.519  30.441  1.00 22.60 ? 42  LEU A CD1 1 
ATOM   296  C  CD2 . LEU A 1 42  ? 11.884  20.196  28.646  1.00 22.83 ? 42  LEU A CD2 1 
ATOM   297  N  N   . HIS A 1 43  ? 15.143  16.567  26.257  1.00 17.16 ? 43  HIS A N   1 
ATOM   298  C  CA  . HIS A 1 43  ? 15.550  16.168  24.890  1.00 16.94 ? 43  HIS A CA  1 
ATOM   299  C  C   . HIS A 1 43  ? 14.305  16.017  24.026  1.00 16.05 ? 43  HIS A C   1 
ATOM   300  O  O   . HIS A 1 43  ? 13.437  15.208  24.401  1.00 15.79 ? 43  HIS A O   1 
ATOM   301  C  CB  . HIS A 1 43  ? 16.346  14.871  24.975  1.00 16.89 ? 43  HIS A CB  1 
ATOM   302  C  CG  . HIS A 1 43  ? 17.643  15.061  25.680  1.00 17.26 ? 43  HIS A CG  1 
ATOM   303  N  ND1 . HIS A 1 43  ? 18.775  15.485  25.017  1.00 19.17 ? 43  HIS A ND1 1 
ATOM   304  C  CD2 . HIS A 1 43  ? 17.966  14.965  26.984  1.00 18.92 ? 43  HIS A CD2 1 
ATOM   305  C  CE1 . HIS A 1 43  ? 19.764  15.600  25.897  1.00 19.51 ? 43  HIS A CE1 1 
ATOM   306  N  NE2 . HIS A 1 43  ? 19.296  15.279  27.104  1.00 19.49 ? 43  HIS A NE2 1 
ATOM   307  N  N   . GLY A 1 44  ? 14.239  16.739  22.912  1.00 16.05 ? 44  GLY A N   1 
ATOM   308  C  CA  . GLY A 1 44  ? 13.120  16.624  21.967  1.00 16.19 ? 44  GLY A CA  1 
ATOM   309  C  C   . GLY A 1 44  ? 12.927  15.184  21.541  1.00 14.78 ? 44  GLY A C   1 
ATOM   310  O  O   . GLY A 1 44  ? 13.917  14.440  21.369  1.00 14.91 ? 44  GLY A O   1 
ATOM   311  N  N   . PHE A 1 45  ? 11.675  14.776  21.396  1.00 14.03 ? 45  PHE A N   1 
ATOM   312  C  CA  . PHE A 1 45  ? 11.310  13.362  21.184  1.00 13.68 ? 45  PHE A CA  1 
ATOM   313  C  C   . PHE A 1 45  ? 10.244  13.335  20.108  1.00 13.66 ? 45  PHE A C   1 
ATOM   314  O  O   . PHE A 1 45  ? 9.126   13.765  20.370  1.00 14.06 ? 45  PHE A O   1 
ATOM   315  C  CB  . PHE A 1 45  ? 10.804  12.785  22.500  1.00 14.21 ? 45  PHE A CB  1 
ATOM   316  C  CG  . PHE A 1 45  ? 10.679  11.287  22.577  1.00 15.06 ? 45  PHE A CG  1 
ATOM   317  C  CD1 . PHE A 1 45  ? 11.769  10.470  22.334  1.00 15.01 ? 45  PHE A CD1 1 
ATOM   318  C  CD2 . PHE A 1 45  ? 9.499   10.711  23.012  1.00 15.54 ? 45  PHE A CD2 1 
ATOM   319  C  CE1 . PHE A 1 45  ? 11.650  9.100   22.475  1.00 16.28 ? 45  PHE A CE1 1 
ATOM   320  C  CE2 . PHE A 1 45  ? 9.387   9.340   23.146  1.00 15.69 ? 45  PHE A CE2 1 
ATOM   321  C  CZ  . PHE A 1 45  ? 10.465  8.542   22.876  1.00 15.51 ? 45  PHE A CZ  1 
ATOM   322  N  N   . HIS A 1 46  ? 10.602  12.886  18.912  1.00 12.71 ? 46  HIS A N   1 
ATOM   323  C  CA  . HIS A 1 46  ? 9.742   13.065  17.727  1.00 13.03 ? 46  HIS A CA  1 
ATOM   324  C  C   . HIS A 1 46  ? 9.642   11.789  16.905  1.00 12.25 ? 46  HIS A C   1 
ATOM   325  O  O   . HIS A 1 46  ? 10.633  11.051  16.759  1.00 12.45 ? 46  HIS A O   1 
ATOM   326  C  CB  . HIS A 1 46  ? 10.296  14.117  16.784  1.00 14.88 ? 46  HIS A CB  1 
ATOM   327  C  CG  . HIS A 1 46  ? 10.547  15.441  17.406  1.00 15.46 ? 46  HIS A CG  1 
ATOM   328  N  ND1 . HIS A 1 46  ? 11.627  16.214  17.036  1.00 18.22 ? 46  HIS A ND1 1 
ATOM   329  C  CD2 . HIS A 1 46  ? 9.853   16.140  18.328  1.00 17.65 ? 46  HIS A CD2 1 
ATOM   330  C  CE1 . HIS A 1 46  ? 11.601  17.333  17.732  1.00 17.76 ? 46  HIS A CE1 1 
ATOM   331  N  NE2 . HIS A 1 46  ? 10.547  17.304  18.530  1.00 18.06 ? 46  HIS A NE2 1 
ATOM   332  N  N   . VAL A 1 47  ? 8.483   11.604  16.296  1.00 11.75 ? 47  VAL A N   1 
ATOM   333  C  CA  . VAL A 1 47  ? 8.363   10.682  15.149  1.00 11.61 ? 47  VAL A CA  1 
ATOM   334  C  C   . VAL A 1 47  ? 8.613   11.490  13.884  1.00 12.00 ? 47  VAL A C   1 
ATOM   335  O  O   . VAL A 1 47  ? 7.879   12.453  13.641  1.00 12.27 ? 47  VAL A O   1 
ATOM   336  C  CB  . VAL A 1 47  ? 7.018   9.949   15.113  1.00 12.31 ? 47  VAL A CB  1 
ATOM   337  C  CG1 . VAL A 1 47  ? 7.013   8.950   13.963  1.00 12.11 ? 47  VAL A CG1 1 
ATOM   338  C  CG2 . VAL A 1 47  ? 6.755   9.237   16.421  1.00 13.01 ? 47  VAL A CG2 1 
ATOM   339  N  N   . HIS A 1 48  ? 9.629   11.098  13.127  1.00 12.40 ? 48  HIS A N   1 
ATOM   340  C  CA  . HIS A 1 48  ? 9.990   11.700  11.830  1.00 12.27 ? 48  HIS A CA  1 
ATOM   341  C  C   . HIS A 1 48  ? 9.374   10.879  10.701  1.00 13.29 ? 48  HIS A C   1 
ATOM   342  O  O   . HIS A 1 48  ? 9.057   9.707   10.900  1.00 13.96 ? 48  HIS A O   1 
ATOM   343  C  CB  . HIS A 1 48  ? 11.509  11.858  11.765  1.00 12.24 ? 48  HIS A CB  1 
ATOM   344  C  CG  . HIS A 1 48  ? 12.034  13.002  12.562  1.00 12.60 ? 48  HIS A CG  1 
ATOM   345  N  ND1 . HIS A 1 48  ? 12.557  14.096  11.936  1.00 13.35 ? 48  HIS A ND1 1 
ATOM   346  C  CD2 . HIS A 1 48  ? 12.142  13.243  13.894  1.00 13.21 ? 48  HIS A CD2 1 
ATOM   347  C  CE1 . HIS A 1 48  ? 12.991  14.952  12.833  1.00 14.41 ? 48  HIS A CE1 1 
ATOM   348  N  NE2 . HIS A 1 48  ? 12.755  14.471  14.025  1.00 13.83 ? 48  HIS A NE2 1 
ATOM   349  N  N   . GLU A 1 49  ? 9.222   11.480  9.535   1.00 13.74 ? 49  GLU A N   1 
ATOM   350  C  CA  . GLU A 1 49  ? 8.366   10.974  8.440   1.00 14.89 ? 49  GLU A CA  1 
ATOM   351  C  C   . GLU A 1 49  ? 8.904   9.667   7.849   1.00 14.41 ? 49  GLU A C   1 
ATOM   352  O  O   . GLU A 1 49  ? 8.087   8.807   7.507   1.00 16.53 ? 49  GLU A O   1 
ATOM   353  C  CB  . GLU A 1 49  ? 8.310   12.027  7.340   1.00 15.29 ? 49  GLU A CB  1 
ATOM   354  C  CG  . GLU A 1 49  ? 7.388   11.613  6.217   1.00 16.67 ? 49  GLU A CG  1 
ATOM   355  C  CD  . GLU A 1 49  ? 7.291   12.595  5.076   1.00 19.17 ? 49  GLU A CD  1 
ATOM   356  O  OE1 . GLU A 1 49  ? 7.939   13.650  5.150   1.00 21.30 ? 49  GLU A OE1 1 
ATOM   357  O  OE2 . GLU A 1 49  ? 6.561   12.291  4.120   1.00 22.42 ? 49  GLU A OE2 1 
ATOM   358  N  N   . PHE A 1 50  ? 10.199  9.528   7.636   1.00 13.55 ? 50  PHE A N   1 
ATOM   359  C  CA  . PHE A 1 50  ? 10.737  8.366   6.896   1.00 13.88 ? 50  PHE A CA  1 
ATOM   360  C  C   . PHE A 1 50  ? 11.422  7.401   7.856   1.00 13.91 ? 50  PHE A C   1 
ATOM   361  O  O   . PHE A 1 50  ? 12.206  7.843   8.704   1.00 14.91 ? 50  PHE A O   1 
ATOM   362  C  CB  . PHE A 1 50  ? 11.707  8.797   5.802   1.00 14.61 ? 50  PHE A CB  1 
ATOM   363  C  CG  . PHE A 1 50  ? 11.150  9.868   4.913   1.00 15.81 ? 50  PHE A CG  1 
ATOM   364  C  CD1 . PHE A 1 50  ? 9.967   9.666   4.237   1.00 15.82 ? 50  PHE A CD1 1 
ATOM   365  C  CD2 . PHE A 1 50  ? 11.795  11.085  4.782   1.00 16.39 ? 50  PHE A CD2 1 
ATOM   366  C  CE1 . PHE A 1 50  ? 9.445   10.662  3.421   1.00 16.79 ? 50  PHE A CE1 1 
ATOM   367  C  CE2 . PHE A 1 50  ? 11.280  12.078  3.965   1.00 16.38 ? 50  PHE A CE2 1 
ATOM   368  C  CZ  . PHE A 1 50  ? 10.105  11.863  3.292   1.00 17.28 ? 50  PHE A CZ  1 
ATOM   369  N  N   . GLY A 1 51  ? 11.140  6.109   7.696   1.00 13.92 ? 51  GLY A N   1 
ATOM   370  C  CA  . GLY A 1 51  ? 11.867  5.010   8.353   1.00 14.43 ? 51  GLY A CA  1 
ATOM   371  C  C   . GLY A 1 51  ? 13.135  4.697   7.589   1.00 14.80 ? 51  GLY A C   1 
ATOM   372  O  O   . GLY A 1 51  ? 13.393  3.538   7.292   1.00 15.40 ? 51  GLY A O   1 
ATOM   373  N  N   . ASP A 1 52  ? 13.892  5.736   7.266   1.00 15.38 ? 52  ASP A N   1 
ATOM   374  C  CA  . ASP A 1 52  ? 15.066  5.673   6.378   1.00 15.70 ? 52  ASP A CA  1 
ATOM   375  C  C   . ASP A 1 52  ? 16.236  6.089   7.244   1.00 16.63 ? 52  ASP A C   1 
ATOM   376  O  O   . ASP A 1 52  ? 16.321  7.279   7.592   1.00 16.60 ? 52  ASP A O   1 
ATOM   377  C  CB  . ASP A 1 52  ? 14.892  6.551   5.135   1.00 17.16 ? 52  ASP A CB  1 
ATOM   378  C  CG  . ASP A 1 52  ? 16.033  6.404   4.147   1.00 18.35 ? 52  ASP A CG  1 
ATOM   379  O  OD1 . ASP A 1 52  ? 17.131  5.972   4.569   1.00 17.97 ? 52  ASP A OD1 1 
ATOM   380  O  OD2 . ASP A 1 52  ? 15.826  6.775   2.975   1.00 20.16 ? 52  ASP A OD2 1 
ATOM   381  N  N   . ASN A 1 53  ? 17.077  5.140   7.614   1.00 16.44 ? 53  ASN A N   1 
ATOM   382  C  CA  . ASN A 1 53  ? 18.282  5.434   8.428   1.00 17.64 ? 53  ASN A CA  1 
ATOM   383  C  C   . ASN A 1 53  ? 19.518  5.118   7.577   1.00 17.92 ? 53  ASN A C   1 
ATOM   384  O  O   . ASN A 1 53  ? 20.579  4.860   8.158   1.00 18.82 ? 53  ASN A O   1 
ATOM   385  C  CB  . ASN A 1 53  ? 18.208  4.745   9.795   1.00 18.58 ? 53  ASN A CB  1 
ATOM   386  C  CG  . ASN A 1 53  ? 17.065  5.207   10.706  0.60 17.61 ? 53  ASN A CG  1 
ATOM   387  O  OD1 . ASN A 1 53  ? 16.836  4.615   11.758  0.60 18.78 ? 53  ASN A OD1 1 
ATOM   388  N  ND2 . ASN A 1 53  ? 16.327  6.259   10.358  0.60 17.77 ? 53  ASN A ND2 1 
ATOM   389  N  N   . THR A 1 54  ? 19.397  5.201   6.256   1.00 18.22 ? 54  THR A N   1 
ATOM   390  C  CA  . THR A 1 54  ? 20.508  4.818   5.342   1.00 20.75 ? 54  THR A CA  1 
ATOM   391  C  C   . THR A 1 54  ? 21.715  5.725   5.573   1.00 21.22 ? 54  THR A C   1 
ATOM   392  O  O   . THR A 1 54  ? 22.841  5.228   5.477   1.00 22.98 ? 54  THR A O   1 
ATOM   393  C  CB  . THR A 1 54  ? 20.098  4.813   3.876   1.00 21.89 ? 54  THR A CB  1 
ATOM   394  O  OG1 . THR A 1 54  ? 19.569  6.098   3.583   1.00 21.58 ? 54  THR A OG1 1 
ATOM   395  C  CG2 . THR A 1 54  ? 19.098  3.724   3.568   1.00 22.50 ? 54  THR A CG2 1 
ATOM   396  N  N   . ALA A 1 55  ? 21.511  6.994   5.894   1.00 22.99 ? 55  ALA A N   1 
ATOM   397  C  CA  . ALA A 1 55  ? 22.627  7.923   6.201   1.00 24.87 ? 55  ALA A CA  1 
ATOM   398  C  C   . ALA A 1 55  ? 22.582  8.330   7.676   1.00 26.27 ? 55  ALA A C   1 
ATOM   399  O  O   . ALA A 1 55  ? 23.023  9.455   8.004   1.00 31.62 ? 55  ALA A O   1 
ATOM   400  C  CB  . ALA A 1 55  ? 22.551  9.109   5.276   1.00 26.42 ? 55  ALA A CB  1 
ATOM   401  N  N   . GLY A 1 56  ? 22.097  7.436   8.537   1.00 24.08 ? 56  GLY A N   1 
ATOM   402  C  CA  . GLY A 1 56  ? 21.792  7.737   9.942   1.00 23.37 ? 56  GLY A CA  1 
ATOM   403  C  C   . GLY A 1 56  ? 20.536  8.574   10.052  1.00 22.16 ? 56  GLY A C   1 
ATOM   404  O  O   . GLY A 1 56  ? 19.704  8.584   9.114   1.00 22.54 ? 56  GLY A O   1 
ATOM   405  N  N   . CYS A 1 57  ? 20.421  9.336   11.133  1.00 20.46 ? 57  CYS A N   1 
ATOM   406  C  CA  . CYS A 1 57  ? 19.141  9.970   11.535  1.00 20.33 ? 57  CYS A CA  1 
ATOM   407  C  C   . CYS A 1 57  ? 18.738  11.091  10.569  1.00 19.85 ? 57  CYS A C   1 
ATOM   408  O  O   . CYS A 1 57  ? 17.535  11.375  10.490  1.00 19.72 ? 57  CYS A O   1 
ATOM   409  C  CB  . CYS A 1 57  ? 19.244  10.459  12.970  1.00 19.82 ? 57  CYS A CB  1 
ATOM   410  S  SG  . CYS A 1 57  ? 19.655  9.119   14.125  1.00 22.48 ? 57  CYS A SG  1 
ATOM   411  N  N   . THR A 1 58  ? 19.665  11.641  9.787   1.00 20.41 ? 58  THR A N   1 
ATOM   412  C  CA  . THR A 1 58  ? 19.339  12.738  8.838   1.00 21.58 ? 58  THR A CA  1 
ATOM   413  C  C   . THR A 1 58  ? 18.360  12.239  7.765   1.00 20.13 ? 58  THR A C   1 
ATOM   414  O  O   . THR A 1 58  ? 17.445  13.023  7.360   1.00 20.48 ? 58  THR A O   1 
ATOM   415  C  CB  . THR A 1 58  ? 20.605  13.354  8.235   1.00 24.39 ? 58  THR A CB  1 
ATOM   416  O  OG1 . THR A 1 58  ? 21.332  12.345  7.525   1.00 24.80 ? 58  THR A OG1 1 
ATOM   417  C  CG2 . THR A 1 58  ? 21.477  13.989  9.295   1.00 26.22 ? 58  THR A CG2 1 
ATOM   418  N  N   . SER A 1 59  ? 18.470  10.978  7.331   1.00 18.35 ? 59  SER A N   1 
ATOM   419  C  CA  A SER A 1 59  ? 17.620  10.457  6.227   0.50 18.04 ? 59  SER A CA  1 
ATOM   420  C  CA  B SER A 1 59  ? 17.621  10.449  6.230   0.50 17.87 ? 59  SER A CA  1 
ATOM   421  C  C   . SER A 1 59  ? 16.154  10.346  6.675   1.00 16.12 ? 59  SER A C   1 
ATOM   422  O  O   . SER A 1 59  ? 15.307  10.114  5.819   1.00 15.81 ? 59  SER A O   1 
ATOM   423  C  CB  A SER A 1 59  ? 18.139  9.149   5.666   0.50 18.11 ? 59  SER A CB  1 
ATOM   424  C  CB  B SER A 1 59  ? 18.132  9.124   5.725   0.50 17.73 ? 59  SER A CB  1 
ATOM   425  O  OG  A SER A 1 59  ? 18.741  8.332   6.659   0.50 18.57 ? 59  SER A OG  1 
ATOM   426  O  OG  B SER A 1 59  ? 19.469  9.234   5.265   0.50 17.76 ? 59  SER A OG  1 
ATOM   427  N  N   . ALA A 1 60  ? 15.868  10.536  7.967   1.00 15.60 ? 60  ALA A N   1 
ATOM   428  C  CA  . ALA A 1 60  ? 14.503  10.382  8.516   1.00 15.70 ? 60  ALA A CA  1 
ATOM   429  C  C   . ALA A 1 60  ? 13.587  11.535  8.086   1.00 15.13 ? 60  ALA A C   1 
ATOM   430  O  O   . ALA A 1 60  ? 12.372  11.392  8.236   1.00 13.69 ? 60  ALA A O   1 
ATOM   431  C  CB  . ALA A 1 60  ? 14.539  10.228  10.014  1.00 16.57 ? 60  ALA A CB  1 
ATOM   432  N  N   . GLY A 1 61  ? 14.120  12.639  7.569   1.00 14.22 ? 61  GLY A N   1 
ATOM   433  C  CA  . GLY A 1 61  ? 13.276  13.737  7.068   1.00 13.95 ? 61  GLY A CA  1 
ATOM   434  C  C   . GLY A 1 61  ? 12.623  14.540  8.180   1.00 13.60 ? 61  GLY A C   1 
ATOM   435  O  O   . GLY A 1 61  ? 13.080  14.538  9.307   1.00 13.30 ? 61  GLY A O   1 
ATOM   436  N  N   . PRO A 1 62  ? 11.539  15.267  7.857   1.00 14.18 ? 62  PRO A N   1 
ATOM   437  C  CA  . PRO A 1 62  ? 10.914  16.173  8.810   1.00 14.16 ? 62  PRO A CA  1 
ATOM   438  C  C   . PRO A 1 62  ? 10.003  15.424  9.789   1.00 13.78 ? 62  PRO A C   1 
ATOM   439  O  O   . PRO A 1 62  ? 9.914   14.217  9.742   1.00 13.62 ? 62  PRO A O   1 
ATOM   440  C  CB  . PRO A 1 62  ? 10.138  17.109  7.879   1.00 15.22 ? 62  PRO A CB  1 
ATOM   441  C  CG  . PRO A 1 62  ? 9.711   16.230  6.755   1.00 15.82 ? 62  PRO A CG  1 
ATOM   442  C  CD  . PRO A 1 62  ? 10.863  15.272  6.558   1.00 15.10 ? 62  PRO A CD  1 
ATOM   443  N  N   . HIS A 1 63  ? 9.373   16.149  10.696  1.00 13.69 ? 63  HIS A N   1 
ATOM   444  C  CA  . HIS A 1 63  ? 8.409   15.567  11.651  1.00 14.09 ? 63  HIS A CA  1 
ATOM   445  C  C   . HIS A 1 63  ? 7.280   14.914  10.872  1.00 14.14 ? 63  HIS A C   1 
ATOM   446  O  O   . HIS A 1 63  ? 6.866   15.422  9.831   1.00 13.75 ? 63  HIS A O   1 
ATOM   447  C  CB  . HIS A 1 63  ? 7.825   16.618  12.575  1.00 15.33 ? 63  HIS A CB  1 
ATOM   448  C  CG  . HIS A 1 63  ? 8.860   17.226  13.443  1.00 15.49 ? 63  HIS A CG  1 
ATOM   449  N  ND1 . HIS A 1 63  ? 8.544   18.095  14.444  1.00 15.51 ? 63  HIS A ND1 1 
ATOM   450  C  CD2 . HIS A 1 63  ? 10.205  17.102  13.455  1.00 18.18 ? 63  HIS A CD2 1 
ATOM   451  C  CE1 . HIS A 1 63  ? 9.646   18.487  15.047  1.00 17.21 ? 63  HIS A CE1 1 
ATOM   452  N  NE2 . HIS A 1 63  ? 10.675  17.911  14.444  1.00 18.12 ? 63  HIS A NE2 1 
ATOM   453  N  N   . PHE A 1 64  ? 6.824   13.782  11.356  1.00 13.07 ? 64  PHE A N   1 
ATOM   454  C  CA  . PHE A 1 64  ? 5.655   13.107  10.752  1.00 12.71 ? 64  PHE A CA  1 
ATOM   455  C  C   . PHE A 1 64  ? 4.443   14.022  10.915  1.00 12.70 ? 64  PHE A C   1 
ATOM   456  O  O   . PHE A 1 64  ? 4.022   14.331  12.046  1.00 13.05 ? 64  PHE A O   1 
ATOM   457  C  CB  . PHE A 1 64  ? 5.476   11.731  11.379  1.00 12.97 ? 64  PHE A CB  1 
ATOM   458  C  CG  . PHE A 1 64  ? 4.316   10.947  10.836  1.00 13.64 ? 64  PHE A CG  1 
ATOM   459  C  CD1 . PHE A 1 64  ? 4.092   10.823  9.475   1.00 14.17 ? 64  PHE A CD1 1 
ATOM   460  C  CD2 . PHE A 1 64  ? 3.424   10.350  11.716  1.00 14.46 ? 64  PHE A CD2 1 
ATOM   461  C  CE1 . PHE A 1 64  ? 3.011   10.090  9.005   1.00 15.32 ? 64  PHE A CE1 1 
ATOM   462  C  CE2 . PHE A 1 64  ? 2.347   9.624   11.241  1.00 14.30 ? 64  PHE A CE2 1 
ATOM   463  C  CZ  . PHE A 1 64  ? 2.155   9.477   9.885   1.00 14.42 ? 64  PHE A CZ  1 
ATOM   464  N  N   . ASN A 1 65  ? 3.915   14.467  9.778   1.00 13.77 ? 65  ASN A N   1 
ATOM   465  C  CA  . ASN A 1 65  ? 2.891   15.537  9.757   1.00 14.89 ? 65  ASN A CA  1 
ATOM   466  C  C   . ASN A 1 65  ? 1.835   15.228  8.704   1.00 15.88 ? 65  ASN A C   1 
ATOM   467  O  O   . ASN A 1 65  ? 1.639   15.996  7.758   1.00 16.27 ? 65  ASN A O   1 
ATOM   468  C  CB  . ASN A 1 65  ? 3.546   16.882  9.491   1.00 15.56 ? 65  ASN A CB  1 
ATOM   469  C  CG  . ASN A 1 65  ? 2.570   18.029  9.599   1.00 16.68 ? 65  ASN A CG  1 
ATOM   470  O  OD1 . ASN A 1 65  ? 1.541   17.926  10.259  1.00 16.02 ? 65  ASN A OD1 1 
ATOM   471  N  ND2 . ASN A 1 65  ? 2.932   19.161  9.019   1.00 17.32 ? 65  ASN A ND2 1 
ATOM   472  N  N   . PRO A 1 66  ? 1.104   14.103  8.828   1.00 15.43 ? 66  PRO A N   1 
ATOM   473  C  CA  . PRO A 1 66  ? 0.139   13.716  7.807   1.00 15.62 ? 66  PRO A CA  1 
ATOM   474  C  C   . PRO A 1 66  ? -1.032  14.705  7.659   1.00 17.37 ? 66  PRO A C   1 
ATOM   475  O  O   . PRO A 1 66  ? -1.636  14.687  6.607   1.00 18.47 ? 66  PRO A O   1 
ATOM   476  C  CB  . PRO A 1 66  ? -0.351  12.328  8.271   1.00 16.05 ? 66  PRO A CB  1 
ATOM   477  C  CG  . PRO A 1 66  ? -0.112  12.331  9.758   1.00 15.61 ? 66  PRO A CG  1 
ATOM   478  C  CD  . PRO A 1 66  ? 1.139   13.163  9.956   1.00 15.27 ? 66  PRO A CD  1 
ATOM   479  N  N   . LEU A 1 67  ? -1.318  15.518  8.680   1.00 17.90 ? 67  LEU A N   1 
ATOM   480  C  CA  . LEU A 1 67  ? -2.481  16.450  8.676   1.00 19.95 ? 67  LEU A CA  1 
ATOM   481  C  C   . LEU A 1 67  ? -2.031  17.881  8.329   1.00 20.87 ? 67  LEU A C   1 
ATOM   482  O  O   . LEU A 1 67  ? -2.871  18.804  8.425   1.00 20.47 ? 67  LEU A O   1 
ATOM   483  C  CB  . LEU A 1 67  ? -3.165  16.384  10.044  1.00 20.88 ? 67  LEU A CB  1 
ATOM   484  C  CG  . LEU A 1 67  ? -3.987  15.128  10.319  1.00 23.91 ? 67  LEU A CG  1 
ATOM   485  C  CD1 . LEU A 1 67  ? -4.555  15.161  11.724  1.00 25.73 ? 67  LEU A CD1 1 
ATOM   486  C  CD2 . LEU A 1 67  ? -5.105  14.993  9.293   1.00 25.11 ? 67  LEU A CD2 1 
ATOM   487  N  N   . SER A 1 68  ? -0.779  18.085  7.909   1.00 19.09 ? 68  SER A N   1 
ATOM   488  C  CA  . SER A 1 68  ? -0.287  19.410  7.438   1.00 20.62 ? 68  SER A CA  1 
ATOM   489  C  C   . SER A 1 68  ? -0.547  20.501  8.496   1.00 21.32 ? 68  SER A C   1 
ATOM   490  O  O   . SER A 1 68  ? -1.077  21.572  8.131   1.00 24.23 ? 68  SER A O   1 
ATOM   491  C  CB  . SER A 1 68  ? -0.929  19.768  6.112   1.00 21.70 ? 68  SER A CB  1 
ATOM   492  O  OG  . SER A 1 68  ? -0.667  18.784  5.131   1.00 21.74 ? 68  SER A OG  1 
ATOM   493  N  N   . ARG A 1 69  ? -0.195  20.261  9.758   1.00 22.00 ? 69  ARG A N   1 
ATOM   494  C  CA  . ARG A 1 69  ? -0.343  21.236  10.872  1.00 22.32 ? 69  ARG A CA  1 
ATOM   495  C  C   . ARG A 1 69  ? 1.028   21.836  11.194  1.00 22.05 ? 69  ARG A C   1 
ATOM   496  O  O   . ARG A 1 69  ? 2.032   21.404  10.592  1.00 20.64 ? 69  ARG A O   1 
ATOM   497  C  CB  . ARG A 1 69  ? -0.912  20.553  12.114  1.00 24.22 ? 69  ARG A CB  1 
ATOM   498  C  CG  . ARG A 1 69  ? -2.281  19.924  11.901  1.00 26.17 ? 69  ARG A CG  1 
ATOM   499  C  CD  . ARG A 1 69  ? -3.404  20.942  12.004  1.00 28.06 ? 69  ARG A CD  1 
ATOM   500  N  NE  . ARG A 1 69  ? -4.691  20.284  11.842  0.50 28.81 ? 69  ARG A NE  1 
ATOM   501  C  CZ  . ARG A 1 69  ? -5.443  19.788  12.819  0.50 29.05 ? 69  ARG A CZ  1 
ATOM   502  N  NH1 . ARG A 1 69  ? -5.083  19.882  14.089  0.50 28.79 ? 69  ARG A NH1 1 
ATOM   503  N  NH2 . ARG A 1 69  ? -6.593  19.212  12.517  0.50 29.84 ? 69  ARG A NH2 1 
ATOM   504  N  N   . LYS A 1 70  ? 1.061   22.799  12.110  1.00 23.98 ? 70  LYS A N   1 
ATOM   505  C  CA  . LYS A 1 70  ? 2.327   23.374  12.628  1.00 23.69 ? 70  LYS A CA  1 
ATOM   506  C  C   . LYS A 1 70  ? 2.808   22.550  13.822  1.00 23.19 ? 70  LYS A C   1 
ATOM   507  O  O   . LYS A 1 70  ? 2.026   21.798  14.413  1.00 21.15 ? 70  LYS A O   1 
ATOM   508  C  CB  . LYS A 1 70  ? 2.154   24.853  12.984  1.00 27.56 ? 70  LYS A CB  1 
ATOM   509  C  CG  . LYS A 1 70  ? 1.987   25.749  11.767  1.00 30.17 ? 70  LYS A CG  1 
ATOM   510  C  CD  . LYS A 1 70  ? 2.014   27.234  12.073  1.00 33.80 ? 70  LYS A CD  1 
ATOM   511  C  CE  . LYS A 1 70  ? 1.640   28.062  10.862  1.00 35.26 ? 70  LYS A CE  1 
ATOM   512  N  NZ  . LYS A 1 70  ? 1.764   29.517  11.117  1.00 37.22 ? 70  LYS A NZ  1 
ATOM   513  N  N   . HIS A 1 71  ? 4.072   22.744  14.174  1.00 20.32 ? 71  HIS A N   1 
ATOM   514  C  CA  . HIS A 1 71  ? 4.736   22.082  15.315  1.00 19.86 ? 71  HIS A CA  1 
ATOM   515  C  C   . HIS A 1 71  ? 4.122   22.559  16.629  1.00 20.44 ? 71  HIS A C   1 
ATOM   516  O  O   . HIS A 1 71  ? 3.886   23.783  16.778  1.00 21.87 ? 71  HIS A O   1 
ATOM   517  C  CB  . HIS A 1 71  ? 6.242   22.334  15.263  1.00 18.81 ? 71  HIS A CB  1 
ATOM   518  C  CG  . HIS A 1 71  ? 6.945   21.650  16.367  1.00 18.98 ? 71  HIS A CG  1 
ATOM   519  N  ND1 . HIS A 1 71  ? 7.167   20.294  16.344  1.00 16.62 ? 71  HIS A ND1 1 
ATOM   520  C  CD2 . HIS A 1 71  ? 7.412   22.097  17.550  1.00 18.31 ? 71  HIS A CD2 1 
ATOM   521  C  CE1 . HIS A 1 71  ? 7.769   19.938  17.452  1.00 17.67 ? 71  HIS A CE1 1 
ATOM   522  N  NE2 . HIS A 1 71  ? 7.924   21.032  18.223  1.00 17.89 ? 71  HIS A NE2 1 
ATOM   523  N  N   . GLY A 1 72  ? 3.882   21.651  17.560  1.00 20.46 ? 72  GLY A N   1 
ATOM   524  C  CA  . GLY A 1 72  ? 3.475   21.977  18.931  1.00 21.07 ? 72  GLY A CA  1 
ATOM   525  C  C   . GLY A 1 72  ? 3.963   20.941  19.917  1.00 21.83 ? 72  GLY A C   1 
ATOM   526  O  O   . GLY A 1 72  ? 4.844   20.120  19.556  1.00 21.38 ? 72  GLY A O   1 
ATOM   527  N  N   . GLY A 1 73  ? 3.445   21.009  21.139  1.00 20.27 ? 73  GLY A N   1 
ATOM   528  C  CA  . GLY A 1 73  ? 3.650   20.025  22.204  1.00 20.24 ? 73  GLY A CA  1 
ATOM   529  C  C   . GLY A 1 73  ? 2.565   18.966  22.104  1.00 18.75 ? 73  GLY A C   1 
ATOM   530  O  O   . GLY A 1 73  ? 1.544   19.184  21.437  1.00 19.39 ? 73  GLY A O   1 
ATOM   531  N  N   . PRO A 1 74  ? 2.765   17.801  22.742  1.00 19.83 ? 74  PRO A N   1 
ATOM   532  C  CA  . PRO A 1 74  ? 1.807   16.704  22.650  1.00 20.83 ? 74  PRO A CA  1 
ATOM   533  C  C   . PRO A 1 74  ? 0.420   17.063  23.203  1.00 22.89 ? 74  PRO A C   1 
ATOM   534  O  O   . PRO A 1 74  ? -0.543  16.485  22.735  1.00 23.44 ? 74  PRO A O   1 
ATOM   535  C  CB  . PRO A 1 74  ? 2.453   15.567  23.446  1.00 21.54 ? 74  PRO A CB  1 
ATOM   536  C  CG  . PRO A 1 74  ? 3.456   16.242  24.349  1.00 21.20 ? 74  PRO A CG  1 
ATOM   537  C  CD  . PRO A 1 74  ? 3.929   17.453  23.574  1.00 19.63 ? 74  PRO A CD  1 
ATOM   538  N  N   . LYS A 1 75  ? 0.325   18.051  24.094  1.00 25.03 ? 75  LYS A N   1 
ATOM   539  C  CA  . LYS A 1 75  ? -0.969  18.446  24.710  1.00 28.22 ? 75  LYS A CA  1 
ATOM   540  C  C   . LYS A 1 75  ? -1.693  19.469  23.830  1.00 29.21 ? 75  LYS A C   1 
ATOM   541  O  O   . LYS A 1 75  ? -2.853  19.779  24.135  1.00 30.13 ? 75  LYS A O   1 
ATOM   542  C  CB  . LYS A 1 75  ? -0.735  19.058  26.090  1.00 29.06 ? 75  LYS A CB  1 
ATOM   543  C  CG  . LYS A 1 75  ? -0.096  18.136  27.112  1.00 32.80 ? 75  LYS A CG  1 
ATOM   544  C  CD  . LYS A 1 75  ? 0.118   18.831  28.452  1.00 34.11 ? 75  LYS A CD  1 
ATOM   545  C  CE  . LYS A 1 75  ? 0.483   17.891  29.584  1.00 37.06 ? 75  LYS A CE  1 
ATOM   546  N  NZ  . LYS A 1 75  ? 1.076   18.625  30.728  1.00 39.17 ? 75  LYS A NZ  1 
ATOM   547  N  N   . ASP A 1 76  ? -1.059  19.961  22.765  1.00 28.85 ? 76  ASP A N   1 
ATOM   548  C  CA  . ASP A 1 76  ? -1.651  21.006  21.892  1.00 29.09 ? 76  ASP A CA  1 
ATOM   549  C  C   . ASP A 1 76  ? -2.543  20.364  20.833  1.00 29.58 ? 76  ASP A C   1 
ATOM   550  O  O   . ASP A 1 76  ? -2.204  19.273  20.343  1.00 27.15 ? 76  ASP A O   1 
ATOM   551  C  CB  . ASP A 1 76  ? -0.578  21.861  21.226  1.00 29.68 ? 76  ASP A CB  1 
ATOM   552  C  CG  . ASP A 1 76  ? 0.248   22.658  22.221  1.00 31.56 ? 76  ASP A CG  1 
ATOM   553  O  OD1 . ASP A 1 76  ? -0.304  23.029  23.279  1.00 31.87 ? 76  ASP A OD1 1 
ATOM   554  O  OD2 . ASP A 1 76  ? 1.429   22.922  21.925  1.00 30.36 ? 76  ASP A OD2 1 
ATOM   555  N  N   . GLU A 1 77  ? -3.634  21.037  20.466  1.00 30.35 ? 77  GLU A N   1 
ATOM   556  C  CA  . GLU A 1 77  ? -4.461  20.648  19.295  1.00 30.45 ? 77  GLU A CA  1 
ATOM   557  C  C   . GLU A 1 77  ? -3.635  20.889  18.030  1.00 28.81 ? 77  GLU A C   1 
ATOM   558  O  O   . GLU A 1 77  ? -3.631  20.014  17.140  1.00 27.89 ? 77  GLU A O   1 
ATOM   559  C  CB  . GLU A 1 77  ? -5.767  21.443  19.272  1.00 34.40 ? 77  GLU A CB  1 
ATOM   560  C  CG  . GLU A 1 77  ? -6.848  20.799  18.433  1.00 36.79 ? 77  GLU A CG  1 
ATOM   561  C  CD  . GLU A 1 77  ? -6.749  21.039  16.938  1.00 39.09 ? 77  GLU A CD  1 
ATOM   562  O  OE1 . GLU A 1 77  ? -6.182  22.076  16.531  1.00 41.58 ? 77  GLU A OE1 1 
ATOM   563  O  OE2 . GLU A 1 77  ? -7.250  20.190  16.184  1.00 44.03 ? 77  GLU A OE2 1 
ATOM   564  N  N   . GLU A 1 78  ? -2.942  22.026  17.975  1.00 27.02 ? 78  GLU A N   1 
ATOM   565  C  CA  . GLU A 1 78  ? -2.067  22.378  16.833  1.00 25.97 ? 78  GLU A CA  1 
ATOM   566  C  C   . GLU A 1 78  ? -0.707  21.720  17.060  1.00 23.41 ? 78  GLU A C   1 
ATOM   567  O  O   . GLU A 1 78  ? 0.143   22.288  17.774  1.00 24.91 ? 78  GLU A O   1 
ATOM   568  C  CB  . GLU A 1 78  ? -1.936  23.888  16.656  1.00 27.40 ? 78  GLU A CB  1 
ATOM   569  C  CG  . GLU A 1 78  ? -1.325  24.271  15.318  1.00 29.14 ? 78  GLU A CG  1 
ATOM   570  C  CD  . GLU A 1 78  ? -2.158  23.975  14.075  1.00 33.69 ? 78  GLU A CD  1 
ATOM   571  O  OE1 . GLU A 1 78  ? -3.398  23.834  14.189  1.00 37.32 ? 78  GLU A OE1 1 
ATOM   572  O  OE2 . GLU A 1 78  ? -1.564  23.883  12.987  1.00 36.91 ? 78  GLU A OE2 1 
ATOM   573  N  N   . ARG A 1 79  ? -0.521  20.541  16.480  1.00 20.01 ? 79  ARG A N   1 
ATOM   574  C  CA  . ARG A 1 79  ? 0.751   19.784  16.574  1.00 18.96 ? 79  ARG A CA  1 
ATOM   575  C  C   . ARG A 1 79  ? 0.861   18.905  15.336  1.00 17.71 ? 79  ARG A C   1 
ATOM   576  O  O   . ARG A 1 79  ? -0.145  18.610  14.690  1.00 18.78 ? 79  ARG A O   1 
ATOM   577  C  CB  . ARG A 1 79  ? 0.809   18.923  17.836  1.00 18.80 ? 79  ARG A CB  1 
ATOM   578  C  CG  . ARG A 1 79  ? -0.340  17.934  17.939  1.00 17.56 ? 79  ARG A CG  1 
ATOM   579  C  CD  . ARG A 1 79  ? -0.158  17.003  19.098  1.00 18.09 ? 79  ARG A CD  1 
ATOM   580  N  NE  . ARG A 1 79  ? 0.601   15.819  18.715  1.00 17.02 ? 79  ARG A NE  1 
ATOM   581  C  CZ  . ARG A 1 79  ? 0.655   14.726  19.449  1.00 17.09 ? 79  ARG A CZ  1 
ATOM   582  N  NH1 . ARG A 1 79  ? 0.034   14.680  20.615  1.00 17.49 ? 79  ARG A NH1 1 
ATOM   583  N  NH2 . ARG A 1 79  ? 1.308   13.659  19.016  1.00 16.38 ? 79  ARG A NH2 1 
ATOM   584  N  N   . HIS A 1 80  ? 2.075   18.465  15.053  1.00 16.41 ? 80  HIS A N   1 
ATOM   585  C  CA  . HIS A 1 80  ? 2.326   17.349  14.118  1.00 16.12 ? 80  HIS A CA  1 
ATOM   586  C  C   . HIS A 1 80  ? 1.933   16.061  14.829  1.00 14.26 ? 80  HIS A C   1 
ATOM   587  O  O   . HIS A 1 80  ? 2.090   15.995  16.042  1.00 14.31 ? 80  HIS A O   1 
ATOM   588  C  CB  . HIS A 1 80  ? 3.803   17.284  13.746  1.00 16.41 ? 80  HIS A CB  1 
ATOM   589  C  CG  . HIS A 1 80  ? 4.316   18.521  13.106  1.00 17.62 ? 80  HIS A CG  1 
ATOM   590  N  ND1 . HIS A 1 80  ? 5.566   19.037  13.406  1.00 17.88 ? 80  HIS A ND1 1 
ATOM   591  C  CD2 . HIS A 1 80  ? 3.757   19.338  12.190  1.00 17.65 ? 80  HIS A CD2 1 
ATOM   592  C  CE1 . HIS A 1 80  ? 5.769   20.114  12.671  1.00 17.38 ? 80  HIS A CE1 1 
ATOM   593  N  NE2 . HIS A 1 80  ? 4.665   20.319  11.916  1.00 18.34 ? 80  HIS A NE2 1 
ATOM   594  N  N   . VAL A 1 81  ? 1.545   15.035  14.079  1.00 13.85 ? 81  VAL A N   1 
ATOM   595  C  CA  . VAL A 1 81  ? 1.311   13.718  14.725  1.00 13.42 ? 81  VAL A CA  1 
ATOM   596  C  C   . VAL A 1 81  ? 2.581   13.282  15.456  1.00 13.44 ? 81  VAL A C   1 
ATOM   597  O  O   . VAL A 1 81  ? 2.474   12.729  16.561  1.00 13.79 ? 81  VAL A O   1 
ATOM   598  C  CB  . VAL A 1 81  ? 0.817   12.682  13.708  1.00 14.74 ? 81  VAL A CB  1 
ATOM   599  C  CG1 . VAL A 1 81  ? 0.899   11.270  14.255  1.00 14.95 ? 81  VAL A CG1 1 
ATOM   600  C  CG2 . VAL A 1 81  ? -0.601  13.007  13.270  1.00 15.21 ? 81  VAL A CG2 1 
ATOM   601  N  N   . GLY A 1 82  ? 3.753   13.539  14.875  1.00 13.01 ? 82  GLY A N   1 
ATOM   602  C  CA  . GLY A 1 82  ? 5.016   13.059  15.466  1.00 13.50 ? 82  GLY A CA  1 
ATOM   603  C  C   . GLY A 1 82  ? 5.487   13.854  16.679  1.00 14.15 ? 82  GLY A C   1 
ATOM   604  O  O   . GLY A 1 82  ? 6.590   13.567  17.194  1.00 14.54 ? 82  GLY A O   1 
ATOM   605  N  N   . ASP A 1 83  ? 4.721   14.841  17.159  1.00 15.11 ? 83  ASP A N   1 
ATOM   606  C  CA  . ASP A 1 83  ? 5.207   15.757  18.222  1.00 15.09 ? 83  ASP A CA  1 
ATOM   607  C  C   . ASP A 1 83  ? 4.967   15.139  19.599  1.00 15.83 ? 83  ASP A C   1 
ATOM   608  O  O   . ASP A 1 83  ? 3.891   15.368  20.186  1.00 17.43 ? 83  ASP A O   1 
ATOM   609  C  CB  . ASP A 1 83  ? 4.527   17.112  18.091  1.00 15.87 ? 83  ASP A CB  1 
ATOM   610  C  CG  . ASP A 1 83  ? 5.024   17.904  16.910  1.00 16.87 ? 83  ASP A CG  1 
ATOM   611  O  OD1 . ASP A 1 83  ? 6.071   17.510  16.306  1.00 16.46 ? 83  ASP A OD1 1 
ATOM   612  O  OD2 . ASP A 1 83  ? 4.351   18.879  16.541  1.00 17.21 ? 83  ASP A OD2 1 
ATOM   613  N  N   . LEU A 1 84  ? 5.953   14.412  20.128  1.00 15.21 ? 84  LEU A N   1 
ATOM   614  C  CA  . LEU A 1 84  ? 5.824   13.743  21.451  1.00 17.09 ? 84  LEU A CA  1 
ATOM   615  C  C   . LEU A 1 84  ? 6.554   14.535  22.539  1.00 16.38 ? 84  LEU A C   1 
ATOM   616  O  O   . LEU A 1 84  ? 6.783   13.972  23.623  1.00 19.28 ? 84  LEU A O   1 
ATOM   617  C  CB  . LEU A 1 84  ? 6.341   12.314  21.356  1.00 16.47 ? 84  LEU A CB  1 
ATOM   618  C  CG  . LEU A 1 84  ? 5.500   11.400  20.465  1.00 18.01 ? 84  LEU A CG  1 
ATOM   619  C  CD1 . LEU A 1 84  ? 6.134   10.014  20.418  1.00 18.01 ? 84  LEU A CD1 1 
ATOM   620  C  CD2 . LEU A 1 84  ? 4.066   11.343  20.971  1.00 19.60 ? 84  LEU A CD2 1 
ATOM   621  N  N   . GLY A 1 85  ? 6.926   15.773  22.247  1.00 17.47 ? 85  GLY A N   1 
ATOM   622  C  CA  . GLY A 1 85  ? 7.420   16.700  23.283  1.00 18.20 ? 85  GLY A CA  1 
ATOM   623  C  C   . GLY A 1 85  ? 8.859   16.423  23.649  1.00 17.25 ? 85  GLY A C   1 
ATOM   624  O  O   . GLY A 1 85  ? 9.701   16.413  22.734  1.00 17.29 ? 85  GLY A O   1 
ATOM   625  N  N   . ASN A 1 86  ? 9.128   16.201  24.934  1.00 18.10 ? 86  ASN A N   1 
ATOM   626  C  CA  . ASN A 1 86  ? 10.490  15.970  25.465  1.00 17.95 ? 86  ASN A CA  1 
ATOM   627  C  C   . ASN A 1 86  ? 10.521  14.753  26.374  1.00 18.01 ? 86  ASN A C   1 
ATOM   628  O  O   . ASN A 1 86  ? 9.519   14.467  27.054  1.00 19.57 ? 86  ASN A O   1 
ATOM   629  C  CB  . ASN A 1 86  ? 11.025  17.154  26.269  1.00 19.62 ? 86  ASN A CB  1 
ATOM   630  C  CG  . ASN A 1 86  ? 11.232  18.367  25.404  1.00 19.96 ? 86  ASN A CG  1 
ATOM   631  O  OD1 . ASN A 1 86  ? 12.184  18.421  24.632  1.00 18.93 ? 86  ASN A OD1 1 
ATOM   632  N  ND2 . ASN A 1 86  ? 10.330  19.325  25.496  1.00 20.84 ? 86  ASN A ND2 1 
ATOM   633  N  N   . VAL A 1 87  ? 11.674  14.105  26.427  1.00 17.33 ? 87  VAL A N   1 
ATOM   634  C  CA  . VAL A 1 87  ? 12.033  13.146  27.494  1.00 18.68 ? 87  VAL A CA  1 
ATOM   635  C  C   . VAL A 1 87  ? 13.045  13.863  28.388  1.00 18.14 ? 87  VAL A C   1 
ATOM   636  O  O   . VAL A 1 87  ? 13.722  14.797  27.902  1.00 18.24 ? 87  VAL A O   1 
ATOM   637  C  CB  . VAL A 1 87  ? 12.574  11.831  26.913  1.00 20.00 ? 87  VAL A CB  1 
ATOM   638  C  CG1 . VAL A 1 87  ? 11.482  11.105  26.142  1.00 20.89 ? 87  VAL A CG1 1 
ATOM   639  C  CG2 . VAL A 1 87  ? 13.804  12.049  26.041  1.00 21.10 ? 87  VAL A CG2 1 
ATOM   640  N  N   . THR A 1 88  ? 13.124  13.442  29.639  1.00 19.05 ? 88  THR A N   1 
ATOM   641  C  CA  . THR A 1 88  ? 13.995  14.087  30.649  1.00 21.30 ? 88  THR A CA  1 
ATOM   642  C  C   . THR A 1 88  ? 15.018  13.082  31.136  1.00 20.46 ? 88  THR A C   1 
ATOM   643  O  O   . THR A 1 88  ? 14.639  12.014  31.644  1.00 21.39 ? 88  THR A O   1 
ATOM   644  C  CB  . THR A 1 88  ? 13.193  14.639  31.827  1.00 23.36 ? 88  THR A CB  1 
ATOM   645  O  OG1 . THR A 1 88  ? 12.309  15.635  31.325  1.00 26.28 ? 88  THR A OG1 1 
ATOM   646  C  CG2 . THR A 1 88  ? 14.099  15.235  32.882  1.00 24.22 ? 88  THR A CG2 1 
ATOM   647  N  N   . ALA A 1 89  ? 16.292  13.433  30.996  1.00 19.46 ? 89  ALA A N   1 
ATOM   648  C  CA  . ALA A 1 89  ? 17.416  12.659  31.544  1.00 19.79 ? 89  ALA A CA  1 
ATOM   649  C  C   . ALA A 1 89  ? 17.822  13.290  32.871  1.00 19.54 ? 89  ALA A C   1 
ATOM   650  O  O   . ALA A 1 89  ? 17.826  14.514  32.965  1.00 20.08 ? 89  ALA A O   1 
ATOM   651  C  CB  . ALA A 1 89  ? 18.564  12.629  30.570  1.00 20.72 ? 89  ALA A CB  1 
ATOM   652  N  N   . ASP A 1 90  ? 18.137  12.436  33.837  1.00 22.90 ? 90  ASP A N   1 
ATOM   653  C  CA  . ASP A 1 90  ? 18.600  12.869  35.177  1.00 23.23 ? 90  ASP A CA  1 
ATOM   654  C  C   . ASP A 1 90  ? 20.135  12.898  35.139  1.00 24.84 ? 90  ASP A C   1 
ATOM   655  O  O   . ASP A 1 90  ? 20.729  12.676  34.065  1.00 24.19 ? 90  ASP A O   1 
ATOM   656  C  CB  . ASP A 1 90  ? 17.991  11.966  36.252  1.00 25.29 ? 90  ASP A CB  1 
ATOM   657  C  CG  . ASP A 1 90  ? 16.482  12.103  36.427  0.60 25.76 ? 90  ASP A CG  1 
ATOM   658  O  OD1 . ASP A 1 90  ? 15.878  12.972  35.767  0.60 25.27 ? 90  ASP A OD1 1 
ATOM   659  O  OD2 . ASP A 1 90  ? 15.920  11.332  37.215  0.60 28.74 ? 90  ASP A OD2 1 
ATOM   660  N  N   . LYS A 1 91  ? 20.782  13.161  36.272  1.00 24.96 ? 91  LYS A N   1 
ATOM   661  C  CA  . LYS A 1 91  ? 22.269  13.201  36.360  1.00 26.93 ? 91  LYS A CA  1 
ATOM   662  C  C   . LYS A 1 91  ? 22.895  11.857  35.976  1.00 28.08 ? 91  LYS A C   1 
ATOM   663  O  O   . LYS A 1 91  ? 24.059  11.865  35.553  1.00 29.58 ? 91  LYS A O   1 
ATOM   664  C  CB  . LYS A 1 91  ? 22.702  13.613  37.771  1.00 28.46 ? 91  LYS A CB  1 
ATOM   665  C  CG  . LYS A 1 91  ? 22.764  15.115  37.988  1.00 28.62 ? 91  LYS A CG  1 
ATOM   666  C  CD  . LYS A 1 91  ? 23.749  15.797  37.068  1.00 29.26 ? 91  LYS A CD  1 
ATOM   667  C  CE  . LYS A 1 91  ? 24.476  16.973  37.682  1.00 33.05 ? 91  LYS A CE  1 
ATOM   668  N  NZ  . LYS A 1 91  ? 23.601  18.160  37.816  1.00 35.43 ? 91  LYS A NZ  1 
ATOM   669  N  N   . ASP A 1 92  ? 22.154  10.759  36.127  1.00 26.92 ? 92  ASP A N   1 
ATOM   670  C  CA  . ASP A 1 92  ? 22.587  9.374   35.800  1.00 27.69 ? 92  ASP A CA  1 
ATOM   671  C  C   . ASP A 1 92  ? 22.661  9.167   34.275  1.00 26.49 ? 92  ASP A C   1 
ATOM   672  O  O   . ASP A 1 92  ? 23.007  8.039   33.865  1.00 26.26 ? 92  ASP A O   1 
ATOM   673  C  CB  . ASP A 1 92  ? 21.634  8.359   36.435  1.00 30.33 ? 92  ASP A CB  1 
ATOM   674  C  CG  . ASP A 1 92  ? 20.170  8.541   36.053  1.00 32.67 ? 92  ASP A CG  1 
ATOM   675  O  OD1 . ASP A 1 92  ? 19.857  9.500   35.288  1.00 30.23 ? 92  ASP A OD1 1 
ATOM   676  O  OD2 . ASP A 1 92  ? 19.346  7.718   36.517  1.00 38.42 ? 92  ASP A OD2 1 
ATOM   677  N  N   . ALA A 1 93  ? 22.282  10.177  33.485  1.00 24.00 ? 93  ALA A N   1 
ATOM   678  C  CA  . ALA A 1 93  ? 22.312  10.189  31.996  1.00 24.21 ? 93  ALA A CA  1 
ATOM   679  C  C   . ALA A 1 93  ? 21.208  9.284   31.433  1.00 24.04 ? 93  ALA A C   1 
ATOM   680  O  O   . ALA A 1 93  ? 21.263  8.943   30.228  1.00 24.36 ? 93  ALA A O   1 
ATOM   681  C  CB  . ALA A 1 93  ? 23.680  9.787   31.492  1.00 24.46 ? 93  ALA A CB  1 
ATOM   682  N  N   . VAL A 1 94  ? 20.218  8.943   32.253  1.00 22.88 ? 94  VAL A N   1 
ATOM   683  C  CA  . VAL A 1 94  ? 19.099  8.040   31.859  1.00 22.78 ? 94  VAL A CA  1 
ATOM   684  C  C   . VAL A 1 94  ? 17.793  8.837   31.832  1.00 22.22 ? 94  VAL A C   1 
ATOM   685  O  O   . VAL A 1 94  ? 17.503  9.559   32.797  1.00 22.10 ? 94  VAL A O   1 
ATOM   686  C  CB  . VAL A 1 94  ? 19.011  6.813   32.782  1.00 24.12 ? 94  VAL A CB  1 
ATOM   687  C  CG1 . VAL A 1 94  ? 17.860  5.898   32.395  1.00 25.02 ? 94  VAL A CG1 1 
ATOM   688  C  CG2 . VAL A 1 94  ? 20.328  6.053   32.821  1.00 24.07 ? 94  VAL A CG2 1 
ATOM   689  N  N   . ALA A 1 95  ? 17.039  8.700   30.741  1.00 21.57 ? 95  ALA A N   1 
ATOM   690  C  CA  . ALA A 1 95  ? 15.636  9.143   30.601  1.00 22.06 ? 95  ALA A CA  1 
ATOM   691  C  C   . ALA A 1 95  ? 14.739  7.911   30.715  1.00 21.93 ? 95  ALA A C   1 
ATOM   692  O  O   . ALA A 1 95  ? 14.875  7.000   29.883  1.00 21.91 ? 95  ALA A O   1 
ATOM   693  C  CB  . ALA A 1 95  ? 15.429  9.856   29.291  1.00 22.49 ? 95  ALA A CB  1 
ATOM   694  N  N   . ASP A 1 96  ? 13.894  7.857   31.744  1.00 22.13 ? 96  ASP A N   1 
ATOM   695  C  CA  . ASP A 1 96  ? 12.822  6.844   31.877  1.00 24.67 ? 96  ASP A CA  1 
ATOM   696  C  C   . ASP A 1 96  ? 11.613  7.448   31.175  1.00 23.57 ? 96  ASP A C   1 
ATOM   697  O  O   . ASP A 1 96  ? 11.168  8.536   31.564  1.00 25.31 ? 96  ASP A O   1 
ATOM   698  C  CB  . ASP A 1 96  ? 12.594  6.445   33.338  1.00 27.01 ? 96  ASP A CB  1 
ATOM   699  C  CG  . ASP A 1 96  ? 13.726  5.588   33.892  1.00 29.48 ? 96  ASP A CG  1 
ATOM   700  O  OD1 . ASP A 1 96  ? 14.204  4.677   33.160  1.00 29.36 ? 96  ASP A OD1 1 
ATOM   701  O  OD2 . ASP A 1 96  ? 14.134  5.831   35.050  1.00 33.56 ? 96  ASP A OD2 1 
ATOM   702  N  N   . VAL A 1 97  ? 11.159  6.801   30.107  1.00 20.97 ? 97  VAL A N   1 
ATOM   703  C  CA  . VAL A 1 97  ? 10.107  7.361   29.226  1.00 22.05 ? 97  VAL A CA  1 
ATOM   704  C  C   . VAL A 1 97  ? 8.791   6.733   29.641  1.00 20.08 ? 97  VAL A C   1 
ATOM   705  O  O   . VAL A 1 97  ? 8.723   5.500   29.756  1.00 19.00 ? 97  VAL A O   1 
ATOM   706  C  CB  . VAL A 1 97  ? 10.418  7.120   27.747  1.00 21.46 ? 97  VAL A CB  1 
ATOM   707  C  CG1 . VAL A 1 97  ? 9.321   7.684   26.859  1.00 22.34 ? 97  VAL A CG1 1 
ATOM   708  C  CG2 . VAL A 1 97  ? 11.770  7.720   27.386  1.00 22.04 ? 97  VAL A CG2 1 
ATOM   709  N  N   . SER A 1 98  ? 7.801   7.581   29.874  1.00 23.33 ? 98  SER A N   1 
ATOM   710  C  CA  . SER A 1 98  ? 6.430   7.163   30.211  1.00 24.53 ? 98  SER A CA  1 
ATOM   711  C  C   . SER A 1 98  ? 5.491   8.219   29.643  1.00 24.42 ? 98  SER A C   1 
ATOM   712  O  O   . SER A 1 98  ? 5.417   9.343   30.184  1.00 25.78 ? 98  SER A O   1 
ATOM   713  C  CB  . SER A 1 98  ? 6.279   6.960   31.696  1.00 27.64 ? 98  SER A CB  1 
ATOM   714  O  OG  . SER A 1 98  ? 5.074   6.264   31.966  1.00 30.74 ? 98  SER A OG  1 
ATOM   715  N  N   . ILE A 1 99  ? 4.848   7.888   28.533  1.00 23.13 ? 99  ILE A N   1 
ATOM   716  C  CA  . ILE A 1 99  ? 3.992   8.823   27.759  1.00 21.98 ? 99  ILE A CA  1 
ATOM   717  C  C   . ILE A 1 99  ? 2.697   8.065   27.460  1.00 21.08 ? 99  ILE A C   1 
ATOM   718  O  O   . ILE A 1 99  ? 2.751   6.843   27.240  1.00 19.52 ? 99  ILE A O   1 
ATOM   719  C  CB  . ILE A 1 99  ? 4.736   9.289   26.482  1.00 21.51 ? 99  ILE A CB  1 
ATOM   720  C  CG1 . ILE A 1 99  ? 5.876   10.256  26.811  1.00 22.44 ? 99  ILE A CG1 1 
ATOM   721  C  CG2 . ILE A 1 99  ? 3.791   9.888   25.462  1.00 21.27 ? 99  ILE A CG2 1 
ATOM   722  C  CD1 . ILE A 1 99  ? 6.742   10.626  25.609  1.00 22.42 ? 99  ILE A CD1 1 
ATOM   723  N  N   . GLU A 1 100 ? 1.568   8.751   27.499  1.00 20.45 ? 100 GLU A N   1 
ATOM   724  C  CA  . GLU A 1 100 ? 0.330   8.285   26.838  1.00 20.91 ? 100 GLU A CA  1 
ATOM   725  C  C   . GLU A 1 100 ? -0.038  9.342   25.805  1.00 19.00 ? 100 GLU A C   1 
ATOM   726  O  O   . GLU A 1 100 ? -0.052  10.535  26.151  1.00 18.97 ? 100 GLU A O   1 
ATOM   727  C  CB  . GLU A 1 100 ? -0.798  8.054   27.843  1.00 23.86 ? 100 GLU A CB  1 
ATOM   728  C  CG  . GLU A 1 100 ? -1.891  7.172   27.285  1.00 29.25 ? 100 GLU A CG  1 
ATOM   729  C  CD  . GLU A 1 100 ? -2.138  5.918   28.103  1.00 35.13 ? 100 GLU A CD  1 
ATOM   730  O  OE1 . GLU A 1 100 ? -1.155  5.174   28.350  1.00 37.61 ? 100 GLU A OE1 1 
ATOM   731  O  OE2 . GLU A 1 100 ? -3.299  5.702   28.511  1.00 38.31 ? 100 GLU A OE2 1 
ATOM   732  N  N   . ASP A 1 101 ? -0.287  8.942   24.565  1.00 17.05 ? 101 ASP A N   1 
ATOM   733  C  CA  . ASP A 1 101 ? -0.621  9.924   23.511  1.00 17.10 ? 101 ASP A CA  1 
ATOM   734  C  C   . ASP A 1 101 ? -1.848  9.466   22.729  1.00 17.38 ? 101 ASP A C   1 
ATOM   735  O  O   . ASP A 1 101 ? -1.920  8.281   22.399  1.00 18.15 ? 101 ASP A O   1 
ATOM   736  C  CB  . ASP A 1 101 ? 0.581   10.184  22.610  1.00 17.35 ? 101 ASP A CB  1 
ATOM   737  C  CG  . ASP A 1 101 ? 0.399   11.428  21.774  1.00 18.00 ? 101 ASP A CG  1 
ATOM   738  O  OD1 . ASP A 1 101 ? 0.545   12.534  22.353  1.00 19.41 ? 101 ASP A OD1 1 
ATOM   739  O  OD2 . ASP A 1 101 ? 0.071   11.304  20.566  1.00 17.23 ? 101 ASP A OD2 1 
ATOM   740  N  N   . SER A 1 102 ? -2.746  10.395  22.416  1.00 18.36 ? 102 SER A N   1 
ATOM   741  C  CA  . SER A 1 102 ? -4.032  10.108  21.737  1.00 20.63 ? 102 SER A CA  1 
ATOM   742  C  C   . SER A 1 102 ? -3.956  10.457  20.250  1.00 19.14 ? 102 SER A C   1 
ATOM   743  O  O   . SER A 1 102 ? -4.952  10.226  19.544  1.00 21.16 ? 102 SER A O   1 
ATOM   744  C  CB  . SER A 1 102 ? -5.145  10.864  22.403  1.00 22.43 ? 102 SER A CB  1 
ATOM   745  O  OG  . SER A 1 102 ? -5.227  10.539  23.776  1.00 29.14 ? 102 SER A OG  1 
ATOM   746  N  N   . VAL A 1 103 ? -2.838  10.997  19.765  1.00 17.72 ? 103 VAL A N   1 
ATOM   747  C  CA  . VAL A 1 103 ? -2.745  11.489  18.369  1.00 17.22 ? 103 VAL A CA  1 
ATOM   748  C  C   . VAL A 1 103 ? -1.949  10.491  17.523  1.00 17.17 ? 103 VAL A C   1 
ATOM   749  O  O   . VAL A 1 103 ? -2.404  10.164  16.412  1.00 17.30 ? 103 VAL A O   1 
ATOM   750  C  CB  . VAL A 1 103 ? -2.142  12.896  18.328  1.00 17.69 ? 103 VAL A CB  1 
ATOM   751  C  CG1 . VAL A 1 103 ? -1.866  13.330  16.910  1.00 17.57 ? 103 VAL A CG1 1 
ATOM   752  C  CG2 . VAL A 1 103 ? -3.061  13.893  19.010  1.00 18.54 ? 103 VAL A CG2 1 
ATOM   753  N  N   . ILE A 1 104 ? -0.802  10.017  18.016  1.00 15.59 ? 104 ILE A N   1 
ATOM   754  C  CA  . ILE A 1 104 ? -0.115  8.887   17.334  1.00 15.04 ? 104 ILE A CA  1 
ATOM   755  C  C   . ILE A 1 104 ? -1.056  7.685   17.382  1.00 14.48 ? 104 ILE A C   1 
ATOM   756  O  O   . ILE A 1 104 ? -1.938  7.590   18.259  1.00 15.86 ? 104 ILE A O   1 
ATOM   757  C  CB  . ILE A 1 104 ? 1.252   8.557   17.956  1.00 14.51 ? 104 ILE A CB  1 
ATOM   758  C  CG1 . ILE A 1 104 ? 1.151   8.168   19.433  1.00 14.73 ? 104 ILE A CG1 1 
ATOM   759  C  CG2 . ILE A 1 104 ? 2.221   9.698   17.713  1.00 14.88 ? 104 ILE A CG2 1 
ATOM   760  C  CD1 . ILE A 1 104 ? 2.389   7.521   19.971  1.00 13.92 ? 104 ILE A CD1 1 
ATOM   761  N  N   . SER A 1 105 ? -0.826  6.733   16.496  1.00 14.48 ? 105 SER A N   1 
ATOM   762  C  CA  . SER A 1 105 ? -1.606  5.481   16.445  1.00 14.52 ? 105 SER A CA  1 
ATOM   763  C  C   . SER A 1 105 ? -0.701  4.373   15.941  1.00 13.49 ? 105 SER A C   1 
ATOM   764  O  O   . SER A 1 105 ? 0.362   4.678   15.363  1.00 12.91 ? 105 SER A O   1 
ATOM   765  C  CB  . SER A 1 105 ? -2.805  5.635   15.570  1.00 14.52 ? 105 SER A CB  1 
ATOM   766  O  OG  . SER A 1 105 ? -3.674  4.530   15.761  1.00 15.06 ? 105 SER A OG  1 
ATOM   767  N  N   . LEU A 1 106 ? -1.112  3.139   16.177  1.00 14.40 ? 106 LEU A N   1 
ATOM   768  C  CA  . LEU A 1 106 ? -0.515  1.943   15.534  1.00 14.40 ? 106 LEU A CA  1 
ATOM   769  C  C   . LEU A 1 106 ? -1.489  1.365   14.489  1.00 15.60 ? 106 LEU A C   1 
ATOM   770  O  O   . LEU A 1 106 ? -1.248  0.247   14.036  1.00 16.36 ? 106 LEU A O   1 
ATOM   771  C  CB  . LEU A 1 106 ? -0.121  0.925   16.615  1.00 13.58 ? 106 LEU A CB  1 
ATOM   772  C  CG  . LEU A 1 106 ? 0.807   1.452   17.709  1.00 13.82 ? 106 LEU A CG  1 
ATOM   773  C  CD1 . LEU A 1 106 ? 1.134   0.366   18.732  1.00 14.06 ? 106 LEU A CD1 1 
ATOM   774  C  CD2 . LEU A 1 106 ? 2.088   2.026   17.115  1.00 14.37 ? 106 LEU A CD2 1 
ATOM   775  N  N   . SER A 1 107 ? -2.441  2.159   13.995  1.00 18.42 ? 107 SER A N   1 
ATOM   776  C  CA  . SER A 1 107 ? -3.377  1.813   12.888  1.00 19.77 ? 107 SER A CA  1 
ATOM   777  C  C   . SER A 1 107 ? -3.727  3.069   12.088  1.00 20.03 ? 107 SER A C   1 
ATOM   778  O  O   . SER A 1 107 ? -3.701  4.165   12.671  1.00 18.33 ? 107 SER A O   1 
ATOM   779  C  CB  . SER A 1 107 ? -4.641  1.177   13.422  1.00 21.76 ? 107 SER A CB  1 
ATOM   780  O  OG  . SER A 1 107 ? -4.378  -0.081  14.003  1.00 26.49 ? 107 SER A OG  1 
ATOM   781  N  N   . GLY A 1 108 ? -4.075  2.918   10.806  1.00 19.94 ? 108 GLY A N   1 
ATOM   782  C  CA  . GLY A 1 108 ? -4.634  4.013   9.987   1.00 19.86 ? 108 GLY A CA  1 
ATOM   783  C  C   . GLY A 1 108 ? -3.579  5.028   9.568   1.00 19.08 ? 108 GLY A C   1 
ATOM   784  O  O   . GLY A 1 108 ? -2.381  4.777   9.747   1.00 18.14 ? 108 GLY A O   1 
ATOM   785  N  N   . ASP A 1 109 ? -3.994  6.185   9.052   1.00 19.35 ? 109 ASP A N   1 
ATOM   786  C  CA  . ASP A 1 109 ? -3.025  7.121   8.431   1.00 19.16 ? 109 ASP A CA  1 
ATOM   787  C  C   . ASP A 1 109 ? -2.283  7.939   9.497   1.00 18.66 ? 109 ASP A C   1 
ATOM   788  O  O   . ASP A 1 109 ? -1.369  8.686   9.093   1.00 20.32 ? 109 ASP A O   1 
ATOM   789  C  CB  . ASP A 1 109 ? -3.663  7.981   7.342   1.00 21.04 ? 109 ASP A CB  1 
ATOM   790  C  CG  . ASP A 1 109 ? -4.647  9.029   7.815   1.00 22.72 ? 109 ASP A CG  1 
ATOM   791  O  OD1 . ASP A 1 109 ? -4.945  9.087   9.024   1.00 25.23 ? 109 ASP A OD1 1 
ATOM   792  O  OD2 . ASP A 1 109 ? -5.139  9.765   6.942   1.00 23.53 ? 109 ASP A OD2 1 
ATOM   793  N  N   . HIS A 1 110 ? -2.614  7.809   10.785  1.00 16.97 ? 110 HIS A N   1 
ATOM   794  C  CA  . HIS A 1 110 ? -1.766  8.369   11.871  1.00 16.81 ? 110 HIS A CA  1 
ATOM   795  C  C   . HIS A 1 110 ? -0.783  7.310   12.356  1.00 15.75 ? 110 HIS A C   1 
ATOM   796  O  O   . HIS A 1 110 ? -0.124  7.557   13.369  1.00 15.09 ? 110 HIS A O   1 
ATOM   797  C  CB  . HIS A 1 110 ? -2.579  8.893   13.059  1.00 18.38 ? 110 HIS A CB  1 
ATOM   798  C  CG  . HIS A 1 110 ? -3.537  9.985   12.723  1.00 21.84 ? 110 HIS A CG  1 
ATOM   799  N  ND1 . HIS A 1 110 ? -3.900  10.958  13.627  1.00 24.62 ? 110 HIS A ND1 1 
ATOM   800  C  CD2 . HIS A 1 110 ? -4.214  10.250  11.590  1.00 24.43 ? 110 HIS A CD2 1 
ATOM   801  C  CE1 . HIS A 1 110 ? -4.774  11.766  13.064  1.00 24.76 ? 110 HIS A CE1 1 
ATOM   802  N  NE2 . HIS A 1 110 ? -4.974  11.362  11.813  1.00 25.12 ? 110 HIS A NE2 1 
ATOM   803  N  N   . CYS A 1 111 ? -0.695  6.163   11.700  1.00 14.40 ? 111 CYS A N   1 
ATOM   804  C  CA  . CYS A 1 111 ? 0.144   5.052   12.197  1.00 14.86 ? 111 CYS A CA  1 
ATOM   805  C  C   . CYS A 1 111 ? 1.618   5.433   12.105  1.00 13.71 ? 111 CYS A C   1 
ATOM   806  O  O   . CYS A 1 111 ? 2.043   5.983   11.094  1.00 14.11 ? 111 CYS A O   1 
ATOM   807  C  CB  . CYS A 1 111 ? -0.087  3.773   11.419  1.00 15.55 ? 111 CYS A CB  1 
ATOM   808  S  SG  . CYS A 1 111 ? 0.846   2.407   12.142  1.00 15.89 ? 111 CYS A SG  1 
ATOM   809  N  N   . ILE A 1 112 ? 2.381   5.113   13.141  1.00 12.38 ? 112 ILE A N   1 
ATOM   810  C  CA  . ILE A 1 112 ? 3.817   5.495   13.195  1.00 12.21 ? 112 ILE A CA  1 
ATOM   811  C  C   . ILE A 1 112 ? 4.718   4.301   12.875  1.00 12.15 ? 112 ILE A C   1 
ATOM   812  O  O   . ILE A 1 112 ? 5.937   4.483   12.870  1.00 11.64 ? 112 ILE A O   1 
ATOM   813  C  CB  . ILE A 1 112 ? 4.166   6.143   14.540  1.00 12.46 ? 112 ILE A CB  1 
ATOM   814  C  CG1 . ILE A 1 112 ? 3.907   5.202   15.716  1.00 12.44 ? 112 ILE A CG1 1 
ATOM   815  C  CG2 . ILE A 1 112 ? 3.408   7.455   14.694  1.00 12.76 ? 112 ILE A CG2 1 
ATOM   816  C  CD1 . ILE A 1 112 ? 4.411   5.751   17.043  1.00 12.43 ? 112 ILE A CD1 1 
ATOM   817  N  N   . ILE A 1 113 ? 4.159   3.123   12.633  1.00 12.42 ? 113 ILE A N   1 
ATOM   818  C  CA  . ILE A 1 113 ? 4.973   1.939   12.257  1.00 12.75 ? 113 ILE A CA  1 
ATOM   819  C  C   . ILE A 1 113 ? 5.677   2.252   10.934  1.00 12.53 ? 113 ILE A C   1 
ATOM   820  O  O   . ILE A 1 113 ? 5.061   2.805   10.015  1.00 12.77 ? 113 ILE A O   1 
ATOM   821  C  CB  . ILE A 1 113 ? 4.120   0.662   12.234  1.00 13.60 ? 113 ILE A CB  1 
ATOM   822  C  CG1 . ILE A 1 113 ? 3.680   0.335   13.664  1.00 14.76 ? 113 ILE A CG1 1 
ATOM   823  C  CG2 . ILE A 1 113 ? 4.839   -0.504  11.559  1.00 13.83 ? 113 ILE A CG2 1 
ATOM   824  C  CD1 . ILE A 1 113 ? 2.576   -0.698  13.749  1.00 15.09 ? 113 ILE A CD1 1 
ATOM   825  N  N   . GLY A 1 114 ? 6.966   1.934   10.872  1.00 11.40 ? 114 GLY A N   1 
ATOM   826  C  CA  . GLY A 1 114 ? 7.773   2.149   9.663   1.00 11.52 ? 114 GLY A CA  1 
ATOM   827  C  C   . GLY A 1 114 ? 8.298   3.563   9.570   1.00 11.83 ? 114 GLY A C   1 
ATOM   828  O  O   . GLY A 1 114 ? 8.972   3.867   8.593   1.00 11.82 ? 114 GLY A O   1 
ATOM   829  N  N   . ARG A 1 115 ? 8.067   4.388   10.583  1.00 11.34 ? 115 ARG A N   1 
ATOM   830  C  CA  . ARG A 1 115 ? 8.625   5.757   10.651  1.00 12.20 ? 115 ARG A CA  1 
ATOM   831  C  C   . ARG A 1 115 ? 9.790   5.722   11.628  1.00 11.80 ? 115 ARG A C   1 
ATOM   832  O  O   . ARG A 1 115 ? 10.109  4.650   12.150  1.00 13.14 ? 115 ARG A O   1 
ATOM   833  C  CB  . ARG A 1 115 ? 7.527   6.723   11.070  1.00 13.74 ? 115 ARG A CB  1 
ATOM   834  C  CG  . ARG A 1 115 ? 6.246   6.491   10.288  1.00 16.29 ? 115 ARG A CG  1 
ATOM   835  C  CD  . ARG A 1 115 ? 5.821   7.632   9.435   1.00 19.63 ? 115 ARG A CD  1 
ATOM   836  N  NE  . ARG A 1 115 ? 4.672   7.284   8.604   1.00 20.06 ? 115 ARG A NE  1 
ATOM   837  C  CZ  . ARG A 1 115 ? 4.531   7.668   7.341   1.00 19.52 ? 115 ARG A CZ  1 
ATOM   838  N  NH1 . ARG A 1 115 ? 5.479   8.361   6.746   1.00 18.94 ? 115 ARG A NH1 1 
ATOM   839  N  NH2 . ARG A 1 115 ? 3.438   7.356   6.671   1.00 20.90 ? 115 ARG A NH2 1 
ATOM   840  N  N   . THR A 1 116 ? 10.450  6.849   11.839  1.00 11.00 ? 116 THR A N   1 
ATOM   841  C  CA  . THR A 1 116 ? 11.653  6.902   12.696  1.00 11.22 ? 116 THR A CA  1 
ATOM   842  C  C   . THR A 1 116 ? 11.338  7.646   13.987  1.00 11.47 ? 116 THR A C   1 
ATOM   843  O  O   . THR A 1 116 ? 10.831  8.771   13.909  1.00 13.84 ? 116 THR A O   1 
ATOM   844  C  CB  . THR A 1 116 ? 12.821  7.562   11.965  1.00 12.11 ? 116 THR A CB  1 
ATOM   845  O  OG1 . THR A 1 116 ? 13.184  6.734   10.867  1.00 12.95 ? 116 THR A OG1 1 
ATOM   846  C  CG2 . THR A 1 116 ? 14.033  7.732   12.842  1.00 12.57 ? 116 THR A CG2 1 
ATOM   847  N  N   . LEU A 1 117 ? 11.721  7.069   15.116  1.00 11.63 ? 117 LEU A N   1 
ATOM   848  C  CA  . LEU A 1 117 ? 11.716  7.789   16.404  1.00 12.32 ? 117 LEU A CA  1 
ATOM   849  C  C   . LEU A 1 117 ? 13.084  8.430   16.587  1.00 12.81 ? 117 LEU A C   1 
ATOM   850  O  O   . LEU A 1 117 ? 14.085  7.740   16.355  1.00 13.26 ? 117 LEU A O   1 
ATOM   851  C  CB  . LEU A 1 117 ? 11.385  6.792   17.513  1.00 12.63 ? 117 LEU A CB  1 
ATOM   852  C  CG  . LEU A 1 117 ? 11.192  7.393   18.903  1.00 13.08 ? 117 LEU A CG  1 
ATOM   853  C  CD1 . LEU A 1 117 ? 9.973   8.318   18.942  1.00 13.68 ? 117 LEU A CD1 1 
ATOM   854  C  CD2 . LEU A 1 117 ? 11.077  6.302   19.952  1.00 13.65 ? 117 LEU A CD2 1 
ATOM   855  N  N   . VAL A 1 118 ? 13.113  9.703   16.960  1.00 12.55 ? 118 VAL A N   1 
ATOM   856  C  CA  . VAL A 1 118 ? 14.376  10.462  17.128  1.00 13.25 ? 118 VAL A CA  1 
ATOM   857  C  C   . VAL A 1 118 ? 14.382  11.100  18.511  1.00 13.70 ? 118 VAL A C   1 
ATOM   858  O  O   . VAL A 1 118 ? 13.400  11.733  18.891  1.00 13.52 ? 118 VAL A O   1 
ATOM   859  C  CB  . VAL A 1 118 ? 14.538  11.540  16.049  1.00 13.05 ? 118 VAL A CB  1 
ATOM   860  C  CG1 . VAL A 1 118 ? 15.828  12.325  16.222  1.00 13.79 ? 118 VAL A CG1 1 
ATOM   861  C  CG2 . VAL A 1 118 ? 14.463  10.937  14.656  1.00 13.07 ? 118 VAL A CG2 1 
ATOM   862  N  N   . VAL A 1 119 ? 15.504  10.985  19.206  1.00 13.14 ? 119 VAL A N   1 
ATOM   863  C  CA  . VAL A 1 119 ? 15.761  11.791  20.427  1.00 14.73 ? 119 VAL A CA  1 
ATOM   864  C  C   . VAL A 1 119 ? 16.823  12.839  20.085  1.00 15.07 ? 119 VAL A C   1 
ATOM   865  O  O   . VAL A 1 119 ? 17.805  12.516  19.418  1.00 14.97 ? 119 VAL A O   1 
ATOM   866  C  CB  . VAL A 1 119 ? 16.119  10.912  21.633  1.00 14.84 ? 119 VAL A CB  1 
ATOM   867  C  CG1 . VAL A 1 119 ? 17.392  10.116  21.439  1.00 15.50 ? 119 VAL A CG1 1 
ATOM   868  C  CG2 . VAL A 1 119 ? 16.182  11.754  22.895  1.00 15.61 ? 119 VAL A CG2 1 
ATOM   869  N  N   . HIS A 1 120 ? 16.584  14.074  20.495  1.00 15.38 ? 120 HIS A N   1 
ATOM   870  C  CA  . HIS A 1 120 ? 17.355  15.265  20.064  1.00 16.75 ? 120 HIS A CA  1 
ATOM   871  C  C   . HIS A 1 120 ? 18.321  15.751  21.147  1.00 16.94 ? 120 HIS A C   1 
ATOM   872  O  O   . HIS A 1 120 ? 18.201  15.376  22.312  1.00 16.82 ? 120 HIS A O   1 
ATOM   873  C  CB  . HIS A 1 120 ? 16.400  16.376  19.678  1.00 16.15 ? 120 HIS A CB  1 
ATOM   874  C  CG  . HIS A 1 120 ? 15.808  16.184  18.334  1.00 16.84 ? 120 HIS A CG  1 
ATOM   875  N  ND1 . HIS A 1 120 ? 16.408  16.716  17.201  1.00 17.61 ? 120 HIS A ND1 1 
ATOM   876  C  CD2 . HIS A 1 120 ? 14.717  15.511  17.912  1.00 16.38 ? 120 HIS A CD2 1 
ATOM   877  C  CE1 . HIS A 1 120 ? 15.690  16.398  16.159  1.00 18.12 ? 120 HIS A CE1 1 
ATOM   878  N  NE2 . HIS A 1 120 ? 14.644  15.679  16.549  1.00 17.60 ? 120 HIS A NE2 1 
ATOM   879  N  N   . GLU A 1 121 ? 19.260  16.575  20.709  1.00 19.13 ? 121 GLU A N   1 
ATOM   880  C  CA  . GLU A 1 121 ? 20.353  17.178  21.515  1.00 21.48 ? 121 GLU A CA  1 
ATOM   881  C  C   . GLU A 1 121 ? 19.769  18.080  22.608  1.00 20.98 ? 121 GLU A C   1 
ATOM   882  O  O   . GLU A 1 121 ? 20.262  18.028  23.753  1.00 19.61 ? 121 GLU A O   1 
ATOM   883  C  CB  . GLU A 1 121 ? 21.252  17.926  20.530  1.00 24.49 ? 121 GLU A CB  1 
ATOM   884  C  CG  . GLU A 1 121 ? 22.312  18.795  21.172  1.00 27.04 ? 121 GLU A CG  1 
ATOM   885  C  CD  . GLU A 1 121 ? 22.855  19.886  20.260  1.00 28.86 ? 121 GLU A CD  1 
ATOM   886  O  OE1 . GLU A 1 121 ? 23.803  20.581  20.688  1.00 34.76 ? 121 GLU A OE1 1 
ATOM   887  O  OE2 . GLU A 1 121 ? 22.338  20.052  19.133  1.00 29.85 ? 121 GLU A OE2 1 
ATOM   888  N  N   . LYS A 1 122 ? 18.760  18.876  22.243  1.00 20.95 ? 122 LYS A N   1 
ATOM   889  C  CA  . LYS A 1 122 ? 18.245  19.988  23.081  1.00 24.10 ? 122 LYS A CA  1 
ATOM   890  C  C   . LYS A 1 122 ? 16.753  19.795  23.339  1.00 23.94 ? 122 LYS A C   1 
ATOM   891  O  O   . LYS A 1 122 ? 16.127  18.872  22.766  1.00 22.03 ? 122 LYS A O   1 
ATOM   892  C  CB  . LYS A 1 122 ? 18.479  21.339  22.396  1.00 26.33 ? 122 LYS A CB  1 
ATOM   893  C  CG  . LYS A 1 122 ? 19.794  21.508  21.646  1.00 28.36 ? 122 LYS A CG  1 
ATOM   894  C  CD  . LYS A 1 122 ? 19.881  22.795  20.845  1.00 29.83 ? 122 LYS A CD  1 
ATOM   895  C  CE  . LYS A 1 122 ? 21.289  23.111  20.386  1.00 31.69 ? 122 LYS A CE  1 
ATOM   896  N  N   . ALA A 1 123 ? 16.184  20.678  24.147  1.00 20.96 ? 123 ALA A N   1 
ATOM   897  C  CA  . ALA A 1 123 ? 14.743  20.711  24.432  1.00 21.57 ? 123 ALA A CA  1 
ATOM   898  C  C   . ALA A 1 123 ? 13.976  21.123  23.167  1.00 20.44 ? 123 ALA A C   1 
ATOM   899  O  O   . ALA A 1 123 ? 14.407  22.006  22.415  1.00 20.86 ? 123 ALA A O   1 
ATOM   900  C  CB  . ALA A 1 123 ? 14.467  21.643  25.580  1.00 22.55 ? 123 ALA A CB  1 
ATOM   901  N  N   . ASP A 1 124 ? 12.862  20.449  22.921  1.00 19.87 ? 124 ASP A N   1 
ATOM   902  C  CA  . ASP A 1 124 ? 11.793  20.946  22.030  1.00 20.39 ? 124 ASP A CA  1 
ATOM   903  C  C   . ASP A 1 124 ? 11.055  22.060  22.777  1.00 20.48 ? 124 ASP A C   1 
ATOM   904  O  O   . ASP A 1 124 ? 10.592  21.811  23.902  1.00 22.26 ? 124 ASP A O   1 
ATOM   905  C  CB  . ASP A 1 124 ? 10.899  19.772  21.627  1.00 19.54 ? 124 ASP A CB  1 
ATOM   906  C  CG  . ASP A 1 124 ? 9.788   20.098  20.646  1.00 21.64 ? 124 ASP A CG  1 
ATOM   907  O  OD1 . ASP A 1 124 ? 9.385   21.276  20.533  1.00 20.27 ? 124 ASP A OD1 1 
ATOM   908  O  OD2 . ASP A 1 124 ? 9.325   19.153  19.984  1.00 20.46 ? 124 ASP A OD2 1 
ATOM   909  N  N   . ASP A 1 125 ? 10.973  23.245  22.187  1.00 22.19 ? 125 ASP A N   1 
ATOM   910  C  CA  . ASP A 1 125 ? 10.322  24.410  22.855  1.00 23.85 ? 125 ASP A CA  1 
ATOM   911  C  C   . ASP A 1 125 ? 8.799   24.323  22.701  1.00 25.48 ? 125 ASP A C   1 
ATOM   912  O  O   . ASP A 1 125 ? 8.113   25.273  23.102  1.00 26.86 ? 125 ASP A O   1 
ATOM   913  C  CB  . ASP A 1 125 ? 10.884  25.744  22.355  1.00 25.47 ? 125 ASP A CB  1 
ATOM   914  C  CG  . ASP A 1 125 ? 10.720  26.000  20.866  1.00 24.54 ? 125 ASP A CG  1 
ATOM   915  O  OD1 . ASP A 1 125 ? 9.769   25.450  20.243  1.00 25.98 ? 125 ASP A OD1 1 
ATOM   916  O  OD2 . ASP A 1 125 ? 11.534  26.772  20.330  1.00 27.78 ? 125 ASP A OD2 1 
ATOM   917  N  N   . LEU A 1 126 ? 8.296   23.231  22.118  1.00 24.77 ? 126 LEU A N   1 
ATOM   918  C  CA  . LEU A 1 126 ? 6.853   22.897  21.988  1.00 25.35 ? 126 LEU A CA  1 
ATOM   919  C  C   . LEU A 1 126 ? 6.137   23.992  21.195  1.00 25.26 ? 126 LEU A C   1 
ATOM   920  O  O   . LEU A 1 126 ? 4.917   24.165  21.405  1.00 28.45 ? 126 LEU A O   1 
ATOM   921  C  CB  . LEU A 1 126 ? 6.240   22.686  23.378  1.00 24.76 ? 126 LEU A CB  1 
ATOM   922  C  CG  . LEU A 1 126 ? 6.960   21.671  24.263  1.00 25.53 ? 126 LEU A CG  1 
ATOM   923  C  CD1 . LEU A 1 126 ? 6.146   21.314  25.499  1.00 25.28 ? 126 LEU A CD1 1 
ATOM   924  C  CD2 . LEU A 1 126 ? 7.273   20.407  23.476  1.00 25.04 ? 126 LEU A CD2 1 
ATOM   925  N  N   . GLY A 1 127 ? 6.848   24.659  20.283  1.00 26.90 ? 127 GLY A N   1 
ATOM   926  C  CA  . GLY A 1 127 ? 6.305   25.727  19.424  1.00 29.08 ? 127 GLY A CA  1 
ATOM   927  C  C   . GLY A 1 127 ? 6.126   27.046  20.169  1.00 31.98 ? 127 GLY A C   1 
ATOM   928  O  O   . GLY A 1 127 ? 5.483   27.942  19.603  1.00 33.72 ? 127 GLY A O   1 
ATOM   929  N  N   . LYS A 1 128 ? 6.640   27.166  21.399  1.00 34.01 ? 128 LYS A N   1 
ATOM   930  C  CA  . LYS A 1 128 ? 6.454   28.384  22.234  1.00 35.45 ? 128 LYS A CA  1 
ATOM   931  C  C   . LYS A 1 128 ? 7.771   29.162  22.286  1.00 37.69 ? 128 LYS A C   1 
ATOM   932  O  O   . LYS A 1 128 ? 7.883   30.036  23.159  1.00 35.72 ? 128 LYS A O   1 
ATOM   933  C  CB  . LYS A 1 128 ? 5.974   28.019  23.642  1.00 35.98 ? 128 LYS A CB  1 
ATOM   934  C  CG  . LYS A 1 128 ? 4.672   27.232  23.736  1.00 37.96 ? 128 LYS A CG  1 
ATOM   935  C  CD  . LYS A 1 128 ? 3.417   28.045  23.499  1.00 40.44 ? 128 LYS A CD  1 
ATOM   936  C  CE  . LYS A 1 128 ? 2.176   27.394  24.079  1.00 41.75 ? 128 LYS A CE  1 
ATOM   937  N  NZ  . LYS A 1 128 ? 1.820   26.132  23.386  1.00 42.61 ? 128 LYS A NZ  1 
ATOM   938  N  N   . GLY A 1 129 ? 8.692   28.920  21.345  1.00 40.20 ? 129 GLY A N   1 
ATOM   939  C  CA  . GLY A 1 129 ? 10.049  29.497  21.342  1.00 41.16 ? 129 GLY A CA  1 
ATOM   940  C  C   . GLY A 1 129 ? 10.074  30.902  20.755  1.00 42.35 ? 129 GLY A C   1 
ATOM   941  O  O   . GLY A 1 129 ? 10.992  31.661  21.086  1.00 41.44 ? 129 GLY A O   1 
ATOM   942  N  N   . GLY A 1 130 ? 9.122   31.228  19.878  1.00 45.08 ? 130 GLY A N   1 
ATOM   943  C  CA  . GLY A 1 130 ? 8.871   32.612  19.434  1.00 47.26 ? 130 GLY A CA  1 
ATOM   944  C  C   . GLY A 1 130 ? 9.700   33.016  18.230  1.00 48.21 ? 130 GLY A C   1 
ATOM   945  O  O   . GLY A 1 130 ? 9.473   34.134  17.741  1.00 49.89 ? 130 GLY A O   1 
ATOM   946  N  N   . ASN A 1 131 ? 10.637  32.177  17.771  1.00 47.24 ? 131 ASN A N   1 
ATOM   947  C  CA  . ASN A 1 131 ? 11.252  32.335  16.426  1.00 44.63 ? 131 ASN A CA  1 
ATOM   948  C  C   . ASN A 1 131 ? 10.482  31.446  15.440  1.00 44.28 ? 131 ASN A C   1 
ATOM   949  O  O   . ASN A 1 131 ? 9.594   30.681  15.886  1.00 44.06 ? 131 ASN A O   1 
ATOM   950  C  CB  . ASN A 1 131 ? 12.763  32.086  16.458  1.00 43.60 ? 131 ASN A CB  1 
ATOM   951  C  CG  . ASN A 1 131 ? 13.159  30.626  16.544  1.00 43.37 ? 131 ASN A CG  1 
ATOM   952  O  OD1 . ASN A 1 131 ? 12.312  29.742  16.689  1.00 40.17 ? 131 ASN A OD1 1 
ATOM   953  N  ND2 . ASN A 1 131 ? 14.451  30.368  16.435  1.00 42.84 ? 131 ASN A ND2 1 
ATOM   954  N  N   . GLU A 1 132 ? 10.821  31.495  14.162  1.00 41.75 ? 132 GLU A N   1 
ATOM   955  C  CA  . GLU A 1 132 ? 10.004  30.776  13.167  1.00 42.08 ? 132 GLU A CA  1 
ATOM   956  C  C   . GLU A 1 132 ? 10.239  29.277  13.309  1.00 39.13 ? 132 GLU A C   1 
ATOM   957  O  O   . GLU A 1 132 ? 9.266   28.508  13.246  1.00 39.79 ? 132 GLU A O   1 
ATOM   958  C  CB  . GLU A 1 132 ? 10.501  31.238  11.798  1.00 44.83 ? 132 GLU A CB  1 
ATOM   959  C  CG  . GLU A 1 132 ? 10.205  30.297  10.649  1.00 47.81 ? 132 GLU A CG  1 
ATOM   960  N  N   . GLU A 1 133 ? 11.489  28.908  13.500  1.00 35.15 ? 133 GLU A N   1 
ATOM   961  C  CA  . GLU A 1 133 ? 11.847  27.467  13.575  1.00 34.09 ? 133 GLU A CA  1 
ATOM   962  C  C   . GLU A 1 133 ? 11.007  26.783  14.661  1.00 33.63 ? 133 GLU A C   1 
ATOM   963  O  O   . GLU A 1 133 ? 10.734  25.577  14.515  1.00 30.55 ? 133 GLU A O   1 
ATOM   964  C  CB  . GLU A 1 133 ? 13.348  27.304  13.811  1.00 34.02 ? 133 GLU A CB  1 
ATOM   965  N  N   . SER A 1 134 ? 10.499  27.494  15.657  1.00 32.10 ? 134 SER A N   1 
ATOM   966  C  CA  . SER A 1 134 ? 9.737   26.862  16.763  1.00 32.24 ? 134 SER A CA  1 
ATOM   967  C  C   . SER A 1 134 ? 8.491   26.184  16.195  1.00 31.95 ? 134 SER A C   1 
ATOM   968  O  O   . SER A 1 134 ? 8.144   25.115  16.681  1.00 28.85 ? 134 SER A O   1 
ATOM   969  C  CB  . SER A 1 134 ? 9.311   27.932  17.712  1.00 32.39 ? 134 SER A CB  1 
ATOM   970  O  OG  . SER A 1 134 ? 8.855   27.415  18.929  1.00 34.02 ? 134 SER A OG  1 
ATOM   971  N  N   . THR A 1 135 ? 7.864   26.833  15.216  1.00 29.58 ? 135 THR A N   1 
ATOM   972  C  CA  . THR A 1 135 ? 6.590   26.344  14.615  1.00 30.98 ? 135 THR A CA  1 
ATOM   973  C  C   . THR A 1 135 ? 6.851   25.217  13.605  1.00 28.61 ? 135 THR A C   1 
ATOM   974  O  O   . THR A 1 135 ? 5.853   24.693  13.061  1.00 30.49 ? 135 THR A O   1 
ATOM   975  C  CB  . THR A 1 135 ? 5.765   27.459  13.940  1.00 30.77 ? 135 THR A CB  1 
ATOM   976  O  OG1 . THR A 1 135 ? 6.300   27.803  12.656  1.00 32.18 ? 135 THR A OG1 1 
ATOM   977  C  CG2 . THR A 1 135 ? 5.649   28.700  14.794  1.00 32.42 ? 135 THR A CG2 1 
ATOM   978  N  N   . LYS A 1 136 ? 8.110   24.834  13.360  1.00 29.35 ? 136 LYS A N   1 
ATOM   979  C  CA  . LYS A 1 136 ? 8.464   23.773  12.377  1.00 28.88 ? 136 LYS A CA  1 
ATOM   980  C  C   . LYS A 1 136 ? 9.156   22.604  13.084  1.00 26.83 ? 136 LYS A C   1 
ATOM   981  O  O   . LYS A 1 136 ? 8.692   21.466  12.916  1.00 27.54 ? 136 LYS A O   1 
ATOM   982  C  CB  . LYS A 1 136 ? 9.306   24.361  11.241  1.00 31.73 ? 136 LYS A CB  1 
ATOM   983  C  CG  . LYS A 1 136 ? 8.493   25.224  10.281  1.00 33.64 ? 136 LYS A CG  1 
ATOM   984  C  CD  . LYS A 1 136 ? 9.252   26.364  9.619   1.00 36.65 ? 136 LYS A CD  1 
ATOM   985  C  CE  . LYS A 1 136 ? 8.345   27.455  9.075   1.00 39.41 ? 136 LYS A CE  1 
ATOM   986  N  NZ  . LYS A 1 136 ? 8.210   27.393  7.599   1.00 42.11 ? 136 LYS A NZ  1 
ATOM   987  N  N   . THR A 1 137 ? 10.239  22.855  13.820  1.00 24.40 ? 137 THR A N   1 
ATOM   988  C  CA  . THR A 1 137 ? 11.062  21.790  14.451  1.00 22.54 ? 137 THR A CA  1 
ATOM   989  C  C   . THR A 1 137 ? 11.029  21.874  15.977  1.00 22.36 ? 137 THR A C   1 
ATOM   990  O  O   . THR A 1 137 ? 11.381  20.892  16.593  1.00 20.44 ? 137 THR A O   1 
ATOM   991  C  CB  . THR A 1 137 ? 12.517  21.832  13.971  1.00 23.13 ? 137 THR A CB  1 
ATOM   992  O  OG1 . THR A 1 137 ? 13.088  22.986  14.588  1.00 21.95 ? 137 THR A OG1 1 
ATOM   993  C  CG2 . THR A 1 137 ? 12.637  21.870  12.462  1.00 24.31 ? 137 THR A CG2 1 
ATOM   994  N  N   . GLY A 1 138 ? 10.703  23.024  16.564  1.00 20.04 ? 138 GLY A N   1 
ATOM   995  C  CA  . GLY A 1 138 ? 10.764  23.224  18.025  1.00 21.51 ? 138 GLY A CA  1 
ATOM   996  C  C   . GLY A 1 138 ? 12.188  23.463  18.509  1.00 20.60 ? 138 GLY A C   1 
ATOM   997  O  O   . GLY A 1 138 ? 12.408  23.432  19.725  1.00 22.05 ? 138 GLY A O   1 
ATOM   998  N  N   . ASN A 1 139 ? 13.139  23.639  17.587  1.00 22.67 ? 139 ASN A N   1 
ATOM   999  C  CA  . ASN A 1 139 ? 14.525  24.072  17.923  1.00 24.19 ? 139 ASN A CA  1 
ATOM   1000 C  C   . ASN A 1 139 ? 15.228  23.055  18.831  1.00 24.04 ? 139 ASN A C   1 
ATOM   1001 O  O   . ASN A 1 139 ? 16.006  23.470  19.698  1.00 23.61 ? 139 ASN A O   1 
ATOM   1002 C  CB  . ASN A 1 139 ? 14.527  25.433  18.628  1.00 26.12 ? 139 ASN A CB  1 
ATOM   1003 C  CG  . ASN A 1 139 ? 14.092  26.559  17.721  1.00 28.02 ? 139 ASN A CG  1 
ATOM   1004 O  OD1 . ASN A 1 139 ? 14.734  26.810  16.704  1.00 29.25 ? 139 ASN A OD1 1 
ATOM   1005 N  ND2 . ASN A 1 139 ? 12.998  27.221  18.061  1.00 29.68 ? 139 ASN A ND2 1 
ATOM   1006 N  N   . ALA A 1 140 ? 15.007  21.753  18.631  1.00 22.99 ? 140 ALA A N   1 
ATOM   1007 C  CA  . ALA A 1 140 ? 15.566  20.698  19.510  1.00 21.60 ? 140 ALA A CA  1 
ATOM   1008 C  C   . ALA A 1 140 ? 16.969  20.254  19.060  1.00 21.34 ? 140 ALA A C   1 
ATOM   1009 O  O   . ALA A 1 140 ? 17.552  19.393  19.715  1.00 21.88 ? 140 ALA A O   1 
ATOM   1010 C  CB  . ALA A 1 140 ? 14.601  19.541  19.594  1.00 21.84 ? 140 ALA A CB  1 
ATOM   1011 N  N   . GLY A 1 141 ? 17.546  20.870  18.033  1.00 22.83 ? 141 GLY A N   1 
ATOM   1012 C  CA  . GLY A 1 141 ? 18.964  20.660  17.692  1.00 23.60 ? 141 GLY A CA  1 
ATOM   1013 C  C   . GLY A 1 141 ? 19.203  19.301  17.060  1.00 22.70 ? 141 GLY A C   1 
ATOM   1014 O  O   . GLY A 1 141 ? 18.273  18.746  16.428  1.00 23.97 ? 141 GLY A O   1 
ATOM   1015 N  N   . SER A 1 142 ? 20.422  18.783  17.200  1.00 21.84 ? 142 SER A N   1 
ATOM   1016 C  CA  . SER A 1 142 ? 20.886  17.626  16.400  1.00 22.26 ? 142 SER A CA  1 
ATOM   1017 C  C   . SER A 1 142 ? 20.132  16.362  16.824  1.00 19.40 ? 142 SER A C   1 
ATOM   1018 O  O   . SER A 1 142 ? 19.560  16.307  17.944  1.00 20.20 ? 142 SER A O   1 
ATOM   1019 C  CB  . SER A 1 142 ? 22.375  17.454  16.500  1.00 22.95 ? 142 SER A CB  1 
ATOM   1020 O  OG  . SER A 1 142 ? 22.742  16.896  17.743  1.00 26.17 ? 142 SER A OG  1 
ATOM   1021 N  N   . ARG A 1 143 ? 20.165  15.365  15.948  1.00 17.15 ? 143 ARG A N   1 
ATOM   1022 C  CA  . ARG A 1 143 ? 19.531  14.052  16.188  1.00 16.32 ? 143 ARG A CA  1 
ATOM   1023 C  C   . ARG A 1 143 ? 20.557  13.153  16.868  1.00 15.69 ? 143 ARG A C   1 
ATOM   1024 O  O   . ARG A 1 143 ? 21.525  12.735  16.211  1.00 17.84 ? 143 ARG A O   1 
ATOM   1025 C  CB  . ARG A 1 143 ? 19.027  13.491  14.862  1.00 15.84 ? 143 ARG A CB  1 
ATOM   1026 C  CG  . ARG A 1 143 ? 18.099  14.463  14.161  1.00 16.67 ? 143 ARG A CG  1 
ATOM   1027 C  CD  . ARG A 1 143 ? 17.643  13.976  12.808  1.00 17.38 ? 143 ARG A CD  1 
ATOM   1028 N  NE  . ARG A 1 143 ? 16.811  15.006  12.223  1.00 17.69 ? 143 ARG A NE  1 
ATOM   1029 C  CZ  . ARG A 1 143 ? 16.046  14.889  11.150  1.00 17.71 ? 143 ARG A CZ  1 
ATOM   1030 N  NH1 . ARG A 1 143 ? 15.947  13.739  10.504  1.00 18.30 ? 143 ARG A NH1 1 
ATOM   1031 N  NH2 . ARG A 1 143 ? 15.339  15.931  10.755  1.00 17.97 ? 143 ARG A NH2 1 
ATOM   1032 N  N   . LEU A 1 144 ? 20.370  12.858  18.147  1.00 15.16 ? 144 LEU A N   1 
ATOM   1033 C  CA  . LEU A 1 144 ? 21.386  12.078  18.909  1.00 15.56 ? 144 LEU A CA  1 
ATOM   1034 C  C   . LEU A 1 144 ? 21.262  10.584  18.612  1.00 15.45 ? 144 LEU A C   1 
ATOM   1035 O  O   . LEU A 1 144 ? 22.271  9.884   18.592  1.00 15.41 ? 144 LEU A O   1 
ATOM   1036 C  CB  . LEU A 1 144 ? 21.222  12.322  20.405  1.00 17.65 ? 144 LEU A CB  1 
ATOM   1037 C  CG  . LEU A 1 144 ? 21.481  13.744  20.875  1.00 19.97 ? 144 LEU A CG  1 
ATOM   1038 C  CD1 . LEU A 1 144 ? 21.448  13.773  22.393  1.00 22.96 ? 144 LEU A CD1 1 
ATOM   1039 C  CD2 . LEU A 1 144 ? 22.803  14.278  20.338  1.00 21.22 ? 144 LEU A CD2 1 
ATOM   1040 N  N   . ALA A 1 145 ? 20.044  10.092  18.453  1.00 14.15 ? 145 ALA A N   1 
ATOM   1041 C  CA  . ALA A 1 145 ? 19.794  8.651   18.287  1.00 14.01 ? 145 ALA A CA  1 
ATOM   1042 C  C   . ALA A 1 145 ? 18.458  8.492   17.603  1.00 12.94 ? 145 ALA A C   1 
ATOM   1043 O  O   . ALA A 1 145 ? 17.583  9.345   17.756  1.00 13.29 ? 145 ALA A O   1 
ATOM   1044 C  CB  . ALA A 1 145 ? 19.838  7.920   19.609  1.00 14.43 ? 145 ALA A CB  1 
ATOM   1045 N  N   . CYS A 1 146 ? 18.316  7.424   16.858  1.00 12.61 ? 146 CYS A N   1 
ATOM   1046 C  CA  . CYS A 1 146 ? 17.055  7.141   16.158  1.00 12.93 ? 146 CYS A CA  1 
ATOM   1047 C  C   . CYS A 1 146 ? 16.951  5.648   15.899  1.00 11.90 ? 146 CYS A C   1 
ATOM   1048 O  O   . CYS A 1 146 ? 17.935  4.921   16.058  1.00 12.11 ? 146 CYS A O   1 
ATOM   1049 C  CB  . CYS A 1 146 ? 16.963  7.923   14.858  1.00 14.86 ? 146 CYS A CB  1 
ATOM   1050 S  SG  . CYS A 1 146 ? 18.289  7.548   13.680  1.00 18.67 ? 146 CYS A SG  1 
ATOM   1051 N  N   . GLY A 1 147 ? 15.757  5.239   15.505  1.00 11.53 ? 147 GLY A N   1 
ATOM   1052 C  CA  . GLY A 1 147 ? 15.521  3.873   15.043  1.00 10.96 ? 147 GLY A CA  1 
ATOM   1053 C  C   . GLY A 1 147 ? 14.200  3.811   14.332  1.00 10.98 ? 147 GLY A C   1 
ATOM   1054 O  O   . GLY A 1 147 ? 13.364  4.738   14.469  1.00 11.94 ? 147 GLY A O   1 
ATOM   1055 N  N   . VAL A 1 148 ? 14.012  2.776   13.536  1.00 11.50 ? 148 VAL A N   1 
ATOM   1056 C  CA  . VAL A 1 148 ? 12.752  2.578   12.794  1.00 11.84 ? 148 VAL A CA  1 
ATOM   1057 C  C   . VAL A 1 148 ? 11.780  1.890   13.758  1.00 11.73 ? 148 VAL A C   1 
ATOM   1058 O  O   . VAL A 1 148 ? 12.176  0.963   14.489  1.00 12.07 ? 148 VAL A O   1 
ATOM   1059 C  CB  . VAL A 1 148 ? 12.980  1.764   11.511  1.00 12.60 ? 148 VAL A CB  1 
ATOM   1060 C  CG1 . VAL A 1 148 ? 11.685  1.568   10.740  1.00 12.77 ? 148 VAL A CG1 1 
ATOM   1061 C  CG2 . VAL A 1 148 ? 14.025  2.429   10.632  1.00 13.06 ? 148 VAL A CG2 1 
ATOM   1062 N  N   . ILE A 1 149 ? 10.537  2.327   13.746  1.00 11.21 ? 149 ILE A N   1 
ATOM   1063 C  CA  . ILE A 1 149 ? 9.479   1.785   14.632  1.00 11.69 ? 149 ILE A CA  1 
ATOM   1064 C  C   . ILE A 1 149 ? 8.949   0.512   13.982  1.00 12.17 ? 149 ILE A C   1 
ATOM   1065 O  O   . ILE A 1 149 ? 8.417   0.582   12.855  1.00 12.29 ? 149 ILE A O   1 
ATOM   1066 C  CB  . ILE A 1 149 ? 8.394   2.844   14.896  1.00 11.48 ? 149 ILE A CB  1 
ATOM   1067 C  CG1 . ILE A 1 149 ? 8.991   4.073   15.584  1.00 12.35 ? 149 ILE A CG1 1 
ATOM   1068 C  CG2 . ILE A 1 149 ? 7.226   2.258   15.683  1.00 11.81 ? 149 ILE A CG2 1 
ATOM   1069 C  CD1 . ILE A 1 149 ? 8.065   5.247   15.590  1.00 13.69 ? 149 ILE A CD1 1 
ATOM   1070 N  N   . GLY A 1 150 ? 9.143   -0.624  14.639  1.00 11.21 ? 150 GLY A N   1 
ATOM   1071 C  CA  . GLY A 1 150 ? 8.769   -1.924  14.079  1.00 11.78 ? 150 GLY A CA  1 
ATOM   1072 C  C   . GLY A 1 150 ? 7.614   -2.578  14.801  1.00 11.47 ? 150 GLY A C   1 
ATOM   1073 O  O   . GLY A 1 150 ? 7.304   -2.231  15.942  1.00 12.21 ? 150 GLY A O   1 
ATOM   1074 N  N   . ILE A 1 151 ? 6.977   -3.514  14.120  1.00 11.80 ? 151 ILE A N   1 
ATOM   1075 C  CA  . ILE A 1 151 ? 5.883   -4.328  14.698  1.00 11.92 ? 151 ILE A CA  1 
ATOM   1076 C  C   . ILE A 1 151 ? 6.466   -5.258  15.752  1.00 12.09 ? 151 ILE A C   1 
ATOM   1077 O  O   . ILE A 1 151 ? 7.446   -5.949  15.467  1.00 12.39 ? 151 ILE A O   1 
ATOM   1078 C  CB  . ILE A 1 151 ? 5.176   -5.103  13.581  1.00 12.85 ? 151 ILE A CB  1 
ATOM   1079 C  CG1 . ILE A 1 151 ? 4.505   -4.148  12.590  1.00 14.05 ? 151 ILE A CG1 1 
ATOM   1080 C  CG2 . ILE A 1 151 ? 4.204   -6.119  14.167  1.00 14.19 ? 151 ILE A CG2 1 
ATOM   1081 C  CD1 . ILE A 1 151 ? 4.117   -4.820  11.295  1.00 14.30 ? 151 ILE A CD1 1 
ATOM   1082 N  N   . ALA A 1 152 ? 5.859   -5.305  16.931  1.00 12.62 ? 152 ALA A N   1 
ATOM   1083 C  CA  . ALA A 1 152 ? 6.314   -6.185  18.024  1.00 13.73 ? 152 ALA A CA  1 
ATOM   1084 C  C   . ALA A 1 152 ? 5.315   -7.317  18.260  1.00 15.04 ? 152 ALA A C   1 
ATOM   1085 O  O   . ALA A 1 152 ? 4.140   -7.246  17.823  1.00 15.02 ? 152 ALA A O   1 
ATOM   1086 C  CB  . ALA A 1 152 ? 6.547   -5.378  19.273  1.00 13.39 ? 152 ALA A CB  1 
ATOM   1087 N  N   . GLN A 1 153 ? 5.795   -8.341  18.946  1.00 16.11 ? 153 GLN A N   1 
ATOM   1088 C  CA  . GLN A 1 153 ? 5.011   -9.563  19.236  1.00 18.74 ? 153 GLN A CA  1 
ATOM   1089 C  C   . GLN A 1 153 ? 3.893   -9.222  20.218  1.00 19.90 ? 153 GLN A C   1 
ATOM   1090 O  O   . GLN A 1 153 ? 4.139   -8.485  21.169  1.00 23.29 ? 153 GLN A O   1 
ATOM   1091 C  CB  . GLN A 1 153 ? 5.957   -10.616 19.805  1.00 19.49 ? 153 GLN A CB  1 
ATOM   1092 C  CG  . GLN A 1 153 ? 5.287   -11.935 20.113  1.00 20.74 ? 153 GLN A CG  1 
ATOM   1093 C  CD  . GLN A 1 153 ? 6.319   -12.930 20.578  1.00 21.52 ? 153 GLN A CD  1 
ATOM   1094 O  OE1 . GLN A 1 153 ? 7.440   -12.981 20.054  1.00 22.27 ? 153 GLN A OE1 1 
ATOM   1095 N  NE2 . GLN A 1 153 ? 5.934   -13.734 21.559  1.00 22.07 ? 153 GLN A NE2 1 
ATOM   1096 O  OXT . GLN A 1 153 ? 2.756   -9.692  20.079  1.00 24.34 ? 153 GLN A OXT 1 
ATOM   1097 N  N   . ALA B 1 1   ? 2.824   5.464   -6.076  1.00 37.67 ? 1   ALA F N   1 
ATOM   1098 C  CA  . ALA B 1 1   ? 4.000   4.542   -5.913  1.00 35.91 ? 1   ALA F CA  1 
ATOM   1099 C  C   . ALA B 1 1   ? 4.457   4.568   -4.451  1.00 34.38 ? 1   ALA F C   1 
ATOM   1100 O  O   . ALA B 1 1   ? 4.425   5.661   -3.842  1.00 36.11 ? 1   ALA F O   1 
ATOM   1101 C  CB  . ALA B 1 1   ? 5.109   4.947   -6.855  1.00 38.11 ? 1   ALA F CB  1 
ATOM   1102 N  N   . THR B 1 2   ? 4.822   3.408   -3.900  1.00 27.63 ? 2   THR F N   1 
ATOM   1103 C  CA  . THR B 1 2   ? 5.238   3.240   -2.483  1.00 24.03 ? 2   THR F CA  1 
ATOM   1104 C  C   . THR B 1 2   ? 6.696   2.788   -2.481  1.00 19.20 ? 2   THR F C   1 
ATOM   1105 O  O   . THR B 1 2   ? 7.065   1.971   -3.336  1.00 17.82 ? 2   THR F O   1 
ATOM   1106 C  CB  . THR B 1 2   ? 4.336   2.257   -1.727  1.00 27.95 ? 2   THR F CB  1 
ATOM   1107 O  OG1 . THR B 1 2   ? 2.972   2.610   -1.987  1.00 32.58 ? 2   THR F OG1 1 
ATOM   1108 C  CG2 . THR B 1 2   ? 4.590   2.259   -0.236  1.00 29.54 ? 2   THR F CG2 1 
ATOM   1109 N  N   . LYS B 1 3   ? 7.505   3.346   -1.585  1.00 16.81 ? 3   LYS F N   1 
ATOM   1110 C  CA  . LYS B 1 3   ? 8.930   2.970   -1.460  1.00 16.52 ? 3   LYS F CA  1 
ATOM   1111 C  C   . LYS B 1 3   ? 9.242   2.668   -0.005  1.00 14.38 ? 3   LYS F C   1 
ATOM   1112 O  O   . LYS B 1 3   ? 8.650   3.289   0.886   1.00 14.57 ? 3   LYS F O   1 
ATOM   1113 C  CB  . LYS B 1 3   ? 9.837   4.086   -1.979  1.00 17.89 ? 3   LYS F CB  1 
ATOM   1114 C  CG  . LYS B 1 3   ? 9.712   4.367   -3.466  1.00 23.10 ? 3   LYS F CG  1 
ATOM   1115 C  CD  . LYS B 1 3   ? 10.573  5.510   -3.925  1.00 25.61 ? 3   LYS F CD  1 
ATOM   1116 C  CE  . LYS B 1 3   ? 9.948   6.274   -5.072  1.00 29.24 ? 3   LYS F CE  1 
ATOM   1117 N  NZ  . LYS B 1 3   ? 10.872  6.349   -6.225  1.00 33.08 ? 3   LYS F NZ  1 
ATOM   1118 N  N   . ALA B 1 4   ? 10.136  1.715   0.206   1.00 12.79 ? 4   ALA F N   1 
ATOM   1119 C  CA  . ALA B 1 4   ? 10.608  1.359   1.552   1.00 12.94 ? 4   ALA F CA  1 
ATOM   1120 C  C   . ALA B 1 4   ? 12.099  1.101   1.478   1.00 13.13 ? 4   ALA F C   1 
ATOM   1121 O  O   . ALA B 1 4   ? 12.658  0.959   0.355   1.00 13.10 ? 4   ALA F O   1 
ATOM   1122 C  CB  . ALA B 1 4   ? 9.844   0.171   2.085   1.00 13.31 ? 4   ALA F CB  1 
ATOM   1123 N  N   . VAL B 1 5   ? 12.741  1.050   2.633   1.00 13.53 ? 5   VAL F N   1 
ATOM   1124 C  CA  . VAL B 1 5   ? 14.213  0.925   2.688   1.00 14.03 ? 5   VAL F CA  1 
ATOM   1125 C  C   . VAL B 1 5   ? 14.566  0.198   3.974   1.00 13.35 ? 5   VAL F C   1 
ATOM   1126 O  O   . VAL B 1 5   ? 13.796  0.258   4.962   1.00 12.94 ? 5   VAL F O   1 
ATOM   1127 C  CB  . VAL B 1 5   ? 14.873  2.310   2.586   1.00 15.01 ? 5   VAL F CB  1 
ATOM   1128 C  CG1 . VAL B 1 5   ? 14.504  3.188   3.767   1.00 16.40 ? 5   VAL F CG1 1 
ATOM   1129 C  CG2 . VAL B 1 5   ? 16.373  2.213   2.421   1.00 15.99 ? 5   VAL F CG2 1 
ATOM   1130 N  N   . CYS B 1 6   ? 15.687  -0.480  3.937   1.00 13.23 ? 6   CYS F N   1 
ATOM   1131 C  CA  . CYS B 1 6   ? 16.175  -1.250  5.075   1.00 13.32 ? 6   CYS F CA  1 
ATOM   1132 C  C   . CYS B 1 6   ? 17.687  -1.170  5.121   1.00 13.22 ? 6   CYS F C   1 
ATOM   1133 O  O   . CYS B 1 6   ? 18.341  -1.468  4.101   1.00 13.81 ? 6   CYS F O   1 
ATOM   1134 C  CB  . CYS B 1 6   ? 15.745  -2.690  4.901   1.00 13.44 ? 6   CYS F CB  1 
ATOM   1135 S  SG  . CYS B 1 6   ? 16.163  -3.691  6.331   1.00 15.98 ? 6   CYS F SG  1 
ATOM   1136 N  N   . VAL B 1 7   ? 18.217  -0.758  6.258   1.00 13.24 ? 7   VAL F N   1 
ATOM   1137 C  CA  . VAL B 1 7   ? 19.669  -0.810  6.541   1.00 14.25 ? 7   VAL F CA  1 
ATOM   1138 C  C   . VAL B 1 7   ? 19.954  -2.117  7.276   1.00 14.06 ? 7   VAL F C   1 
ATOM   1139 O  O   . VAL B 1 7   ? 19.398  -2.309  8.351   1.00 14.78 ? 7   VAL F O   1 
ATOM   1140 C  CB  . VAL B 1 7   ? 20.098  0.414   7.363   1.00 16.05 ? 7   VAL F CB  1 
ATOM   1141 C  CG1 . VAL B 1 7   ? 21.578  0.337   7.695   1.00 17.00 ? 7   VAL F CG1 1 
ATOM   1142 C  CG2 . VAL B 1 7   ? 19.776  1.693   6.626   1.00 17.18 ? 7   VAL F CG2 1 
ATOM   1143 N  N   . LEU B 1 8   ? 20.749  -2.987  6.677   1.00 14.19 ? 8   LEU F N   1 
ATOM   1144 C  CA  . LEU B 1 8   ? 21.167  -4.265  7.299   1.00 14.75 ? 8   LEU F CA  1 
ATOM   1145 C  C   . LEU B 1 8   ? 22.439  -4.038  8.107   1.00 15.49 ? 8   LEU F C   1 
ATOM   1146 O  O   . LEU B 1 8   ? 23.430  -3.585  7.532   1.00 16.61 ? 8   LEU F O   1 
ATOM   1147 C  CB  . LEU B 1 8   ? 21.400  -5.309  6.206   1.00 15.00 ? 8   LEU F CB  1 
ATOM   1148 C  CG  . LEU B 1 8   ? 20.172  -5.676  5.374   1.00 16.29 ? 8   LEU F CG  1 
ATOM   1149 C  CD1 . LEU B 1 8   ? 20.577  -6.545  4.193   1.00 16.51 ? 8   LEU F CD1 1 
ATOM   1150 C  CD2 . LEU B 1 8   ? 19.141  -6.384  6.218   1.00 17.30 ? 8   LEU F CD2 1 
ATOM   1151 N  N   . LYS B 1 9   ? 22.419  -4.386  9.380   1.00 15.53 ? 9   LYS F N   1 
ATOM   1152 C  CA  . LYS B 1 9   ? 23.601  -4.330  10.274  1.00 16.91 ? 9   LYS F CA  1 
ATOM   1153 C  C   . LYS B 1 9   ? 23.533  -5.539  11.200  1.00 16.68 ? 9   LYS F C   1 
ATOM   1154 O  O   . LYS B 1 9   ? 22.425  -6.004  11.504  1.00 15.52 ? 9   LYS F O   1 
ATOM   1155 C  CB  . LYS B 1 9   ? 23.596  -3.032  11.088  1.00 19.50 ? 9   LYS F CB  1 
ATOM   1156 C  CG  . LYS B 1 9   ? 23.977  -1.783  10.308  1.00 22.88 ? 9   LYS F CG  1 
ATOM   1157 N  N   . GLY B 1 10  ? 24.675  -6.013  11.686  1.00 18.82 ? 10  GLY F N   1 
ATOM   1158 C  CA  . GLY B 1 10  ? 24.710  -7.087  12.690  1.00 20.03 ? 10  GLY F CA  1 
ATOM   1159 C  C   . GLY B 1 10  ? 25.931  -7.002  13.584  1.00 23.31 ? 10  GLY F C   1 
ATOM   1160 O  O   . GLY B 1 10  ? 26.532  -5.913  13.675  1.00 22.70 ? 10  GLY F O   1 
ATOM   1161 N  N   . ASP B 1 11  ? 26.274  -8.122  14.216  1.00 25.46 ? 11  ASP F N   1 
ATOM   1162 C  CA  . ASP B 1 11  ? 27.404  -8.215  15.174  1.00 28.30 ? 11  ASP F CA  1 
ATOM   1163 C  C   . ASP B 1 11  ? 28.728  -8.204  14.411  1.00 28.73 ? 11  ASP F C   1 
ATOM   1164 O  O   . ASP B 1 11  ? 29.720  -7.751  14.989  1.00 30.93 ? 11  ASP F O   1 
ATOM   1165 C  CB  . ASP B 1 11  ? 27.268  -9.443  16.071  1.00 31.40 ? 11  ASP F CB  1 
ATOM   1166 C  CG  . ASP B 1 11  ? 26.075  -9.381  17.005  1.00 34.77 ? 11  ASP F CG  1 
ATOM   1167 O  OD1 . ASP B 1 11  ? 25.570  -8.263  17.256  1.00 38.66 ? 11  ASP F OD1 1 
ATOM   1168 O  OD2 . ASP B 1 11  ? 25.665  -10.454 17.483  1.00 40.49 ? 11  ASP F OD2 1 
ATOM   1169 N  N   . GLY B 1 12  ? 28.760  -8.690  13.169  1.00 28.11 ? 12  GLY F N   1 
ATOM   1170 C  CA  . GLY B 1 12  ? 30.000  -8.822  12.386  1.00 27.06 ? 12  GLY F CA  1 
ATOM   1171 C  C   . GLY B 1 12  ? 30.127  -7.753  11.305  1.00 26.99 ? 12  GLY F C   1 
ATOM   1172 O  O   . GLY B 1 12  ? 29.540  -6.677  11.409  1.00 27.79 ? 12  GLY F O   1 
ATOM   1173 N  N   . PRO B 1 13  ? 30.895  -8.043  10.233  1.00 28.63 ? 13  PRO F N   1 
ATOM   1174 C  CA  . PRO B 1 13  ? 31.194  -7.066  9.187   1.00 28.11 ? 13  PRO F CA  1 
ATOM   1175 C  C   . PRO B 1 13  ? 30.143  -6.985  8.068   1.00 26.35 ? 13  PRO F C   1 
ATOM   1176 O  O   . PRO B 1 13  ? 30.326  -6.224  7.141   1.00 27.43 ? 13  PRO F O   1 
ATOM   1177 C  CB  . PRO B 1 13  ? 32.496  -7.638  8.610   1.00 30.08 ? 13  PRO F CB  1 
ATOM   1178 C  CG  . PRO B 1 13  ? 32.270  -9.127  8.675   1.00 30.39 ? 13  PRO F CG  1 
ATOM   1179 C  CD  . PRO B 1 13  ? 31.527  -9.345  9.976   1.00 29.73 ? 13  PRO F CD  1 
ATOM   1180 N  N   . VAL B 1 14  ? 29.070  -7.774  8.150   1.00 22.40 ? 14  VAL F N   1 
ATOM   1181 C  CA  . VAL B 1 14  ? 28.024  -7.795  7.087   1.00 20.13 ? 14  VAL F CA  1 
ATOM   1182 C  C   . VAL B 1 14  ? 27.152  -6.553  7.258   1.00 19.05 ? 14  VAL F C   1 
ATOM   1183 O  O   . VAL B 1 14  ? 26.627  -6.340  8.348   1.00 19.18 ? 14  VAL F O   1 
ATOM   1184 C  CB  . VAL B 1 14  ? 27.186  -9.084  7.088   1.00 19.43 ? 14  VAL F CB  1 
ATOM   1185 C  CG1 . VAL B 1 14  ? 26.047  -9.010  6.078   1.00 19.34 ? 14  VAL F CG1 1 
ATOM   1186 C  CG2 . VAL B 1 14  ? 28.054  -10.298 6.801   1.00 20.20 ? 14  VAL F CG2 1 
ATOM   1187 N  N   . GLN B 1 15  ? 27.082  -5.727  6.230   1.00 18.23 ? 15  GLN F N   1 
ATOM   1188 C  CA  . GLN B 1 15  ? 26.189  -4.553  6.231   1.00 19.56 ? 15  GLN F CA  1 
ATOM   1189 C  C   . GLN B 1 15  ? 25.675  -4.319  4.819   1.00 17.39 ? 15  GLN F C   1 
ATOM   1190 O  O   . GLN B 1 15  ? 26.310  -4.706  3.829   1.00 18.27 ? 15  GLN F O   1 
ATOM   1191 C  CB  . GLN B 1 15  ? 26.888  -3.320  6.801   1.00 23.56 ? 15  GLN F CB  1 
ATOM   1192 C  CG  . GLN B 1 15  ? 27.925  -2.718  5.879   1.00 27.01 ? 15  GLN F CG  1 
ATOM   1193 C  CD  . GLN B 1 15  ? 28.796  -1.727  6.612   1.00 30.72 ? 15  GLN F CD  1 
ATOM   1194 O  OE1 . GLN B 1 15  ? 29.613  -2.097  7.449   1.00 38.04 ? 15  GLN F OE1 1 
ATOM   1195 N  NE2 . GLN B 1 15  ? 28.639  -0.457  6.289   1.00 33.39 ? 15  GLN F NE2 1 
ATOM   1196 N  N   . GLY B 1 16  ? 24.503  -3.725  4.731   1.00 15.71 ? 16  GLY F N   1 
ATOM   1197 C  CA  . GLY B 1 16  ? 23.857  -3.544  3.427   1.00 15.13 ? 16  GLY F CA  1 
ATOM   1198 C  C   . GLY B 1 16  ? 22.763  -2.514  3.464   1.00 14.26 ? 16  GLY F C   1 
ATOM   1199 O  O   . GLY B 1 16  ? 22.352  -2.062  4.552   1.00 14.31 ? 16  GLY F O   1 
ATOM   1200 N  N   . ILE B 1 17  ? 22.327  -2.151  2.281   1.00 13.58 ? 17  ILE F N   1 
ATOM   1201 C  CA  . ILE B 1 17  ? 21.198  -1.214  2.043   1.00 14.91 ? 17  ILE F CA  1 
ATOM   1202 C  C   . ILE B 1 17  ? 20.298  -1.875  1.012   1.00 14.27 ? 17  ILE F C   1 
ATOM   1203 O  O   . ILE B 1 17  ? 20.786  -2.245  -0.077  1.00 14.51 ? 17  ILE F O   1 
ATOM   1204 C  CB  . ILE B 1 17  ? 21.685  0.156   1.538   1.00 17.96 ? 17  ILE F CB  1 
ATOM   1205 C  CG1 . ILE B 1 17  ? 22.689  0.813   2.487   1.00 21.18 ? 17  ILE F CG1 1 
ATOM   1206 C  CG2 . ILE B 1 17  ? 20.503  1.060   1.239   1.00 17.97 ? 17  ILE F CG2 1 
ATOM   1207 C  CD1 . ILE B 1 17  ? 23.705  1.661   1.784   1.00 23.76 ? 17  ILE F CD1 1 
ATOM   1208 N  N   . ILE B 1 18  ? 19.025  -2.030  1.346   1.00 12.83 ? 18  ILE F N   1 
ATOM   1209 C  CA  . ILE B 1 18  ? 18.044  -2.661  0.428   1.00 12.70 ? 18  ILE F CA  1 
ATOM   1210 C  C   . ILE B 1 18  ? 16.859  -1.725  0.250   1.00 12.51 ? 18  ILE F C   1 
ATOM   1211 O  O   . ILE B 1 18  ? 16.314  -1.224  1.263   1.00 12.52 ? 18  ILE F O   1 
ATOM   1212 C  CB  . ILE B 1 18  ? 17.611  -4.036  0.965   1.00 13.44 ? 18  ILE F CB  1 
ATOM   1213 C  CG1 . ILE B 1 18  ? 18.799  -4.989  1.130   1.00 14.40 ? 18  ILE F CG1 1 
ATOM   1214 C  CG2 . ILE B 1 18  ? 16.533  -4.636  0.085   1.00 14.32 ? 18  ILE F CG2 1 
ATOM   1215 C  CD1 . ILE B 1 18  ? 19.459  -5.407  -0.165  1.00 15.10 ? 18  ILE F CD1 1 
ATOM   1216 N  N   . ASN B 1 19  ? 16.499  -1.482  -1.002  1.00 13.29 ? 19  ASN F N   1 
ATOM   1217 C  CA  . ASN B 1 19  ? 15.384  -0.608  -1.411  1.00 12.89 ? 19  ASN F CA  1 
ATOM   1218 C  C   . ASN B 1 19  ? 14.235  -1.466  -1.928  1.00 12.86 ? 19  ASN F C   1 
ATOM   1219 O  O   . ASN B 1 19  ? 14.488  -2.504  -2.531  1.00 13.87 ? 19  ASN F O   1 
ATOM   1220 C  CB  . ASN B 1 19  ? 15.861  0.354   -2.501  1.00 13.99 ? 19  ASN F CB  1 
ATOM   1221 C  CG  . ASN B 1 19  ? 17.050  1.160   -2.041  1.00 15.22 ? 19  ASN F CG  1 
ATOM   1222 O  OD1 . ASN B 1 19  ? 16.866  2.114   -1.297  1.00 16.57 ? 19  ASN F OD1 1 
ATOM   1223 N  ND2 . ASN B 1 19  ? 18.253  0.765   -2.421  1.00 15.55 ? 19  ASN F ND2 1 
ATOM   1224 N  N   . PHE B 1 20  ? 13.019  -1.039  -1.665  1.00 12.58 ? 20  PHE F N   1 
ATOM   1225 C  CA  . PHE B 1 20  ? 11.777  -1.666  -2.153  1.00 12.62 ? 20  PHE F CA  1 
ATOM   1226 C  C   . PHE B 1 20  ? 10.969  -0.603  -2.875  1.00 13.45 ? 20  PHE F C   1 
ATOM   1227 O  O   . PHE B 1 20  ? 10.825  0.509   -2.358  1.00 14.30 ? 20  PHE F O   1 
ATOM   1228 C  CB  . PHE B 1 20  ? 10.956  -2.218  -0.991  1.00 12.84 ? 20  PHE F CB  1 
ATOM   1229 C  CG  . PHE B 1 20  ? 11.667  -3.201  -0.092  1.00 13.38 ? 20  PHE F CG  1 
ATOM   1230 C  CD1 . PHE B 1 20  ? 12.527  -2.782  0.917   1.00 14.13 ? 20  PHE F CD1 1 
ATOM   1231 C  CD2 . PHE B 1 20  ? 11.488  -4.561  -0.264  1.00 13.88 ? 20  PHE F CD2 1 
ATOM   1232 C  CE1 . PHE B 1 20  ? 13.175  -3.686  1.746   1.00 14.21 ? 20  PHE F CE1 1 
ATOM   1233 C  CE2 . PHE B 1 20  ? 12.139  -5.464  0.565   1.00 14.08 ? 20  PHE F CE2 1 
ATOM   1234 C  CZ  . PHE B 1 20  ? 12.968  -5.028  1.574   1.00 14.49 ? 20  PHE F CZ  1 
ATOM   1235 N  N   . GLU B 1 21  ? 10.405  -0.968  -4.013  1.00 14.88 ? 21  GLU F N   1 
ATOM   1236 C  CA  . GLU B 1 21  ? 9.518   -0.040  -4.744  1.00 15.83 ? 21  GLU F CA  1 
ATOM   1237 C  C   . GLU B 1 21  ? 8.332   -0.821  -5.278  1.00 15.13 ? 21  GLU F C   1 
ATOM   1238 O  O   . GLU B 1 21  ? 8.548   -1.912  -5.811  1.00 16.32 ? 21  GLU F O   1 
ATOM   1239 C  CB  . GLU B 1 21  ? 10.289  0.657   -5.859  1.00 19.25 ? 21  GLU F CB  1 
ATOM   1240 C  CG  . GLU B 1 21  ? 9.493   1.748   -6.539  1.00 23.47 ? 21  GLU F CG  1 
ATOM   1241 C  CD  . GLU B 1 21  ? 10.342  2.708   -7.358  1.00 27.79 ? 21  GLU F CD  1 
ATOM   1242 O  OE1 . GLU B 1 21  ? 9.895   3.860   -7.554  1.00 35.11 ? 21  GLU F OE1 1 
ATOM   1243 O  OE2 . GLU B 1 21  ? 11.449  2.305   -7.788  1.00 32.03 ? 21  GLU F OE2 1 
ATOM   1244 N  N   . GLN B 1 22  ? 7.136   -0.274  -5.126  1.00 15.98 ? 22  GLN F N   1 
ATOM   1245 C  CA  . GLN B 1 22  ? 5.893   -0.898  -5.629  1.00 17.21 ? 22  GLN F CA  1 
ATOM   1246 C  C   . GLN B 1 22  ? 5.072   0.184   -6.337  1.00 18.87 ? 22  GLN F C   1 
ATOM   1247 O  O   . GLN B 1 22  ? 4.693   1.159   -5.678  1.00 20.65 ? 22  GLN F O   1 
ATOM   1248 C  CB  . GLN B 1 22  ? 5.169   -1.539  -4.444  1.00 16.90 ? 22  GLN F CB  1 
ATOM   1249 C  CG  . GLN B 1 22  ? 3.983   -2.390  -4.852  1.00 17.64 ? 22  GLN F CG  1 
ATOM   1250 C  CD  . GLN B 1 22  ? 3.296   -3.001  -3.657  1.00 17.57 ? 22  GLN F CD  1 
ATOM   1251 O  OE1 . GLN B 1 22  ? 3.284   -2.437  -2.564  1.00 19.68 ? 22  GLN F OE1 1 
ATOM   1252 N  NE2 . GLN B 1 22  ? 2.692   -4.153  -3.866  1.00 19.31 ? 22  GLN F NE2 1 
ATOM   1253 N  N   . LYS B 1 23  ? 4.796   -0.002  -7.627  1.00 25.27 ? 23  LYS F N   1 
ATOM   1254 C  CA  . LYS B 1 23  ? 4.038   0.991   -8.439  1.00 28.84 ? 23  LYS F CA  1 
ATOM   1255 C  C   . LYS B 1 23  ? 2.570   1.034   -7.999  1.00 32.35 ? 23  LYS F C   1 
ATOM   1256 O  O   . LYS B 1 23  ? 1.993   2.140   -7.999  1.00 32.31 ? 23  LYS F O   1 
ATOM   1257 C  CB  . LYS B 1 23  ? 4.141   0.675   -9.934  1.00 31.56 ? 23  LYS F CB  1 
ATOM   1258 C  CG  . LYS B 1 23  ? 5.383   1.219   -10.622 1.00 32.94 ? 23  LYS F CG  1 
ATOM   1259 C  CD  . LYS B 1 23  ? 5.360   1.020   -12.128 1.00 34.64 ? 23  LYS F CD  1 
ATOM   1260 N  N   . GLU B 1 24  ? 1.973   -0.120  -7.685  1.00 35.21 ? 24  GLU F N   1 
ATOM   1261 C  CA  . GLU B 1 24  ? 0.537   -0.250  -7.303  1.00 38.51 ? 24  GLU F CA  1 
ATOM   1262 C  C   . GLU B 1 24  ? 0.395   -1.332  -6.227  1.00 37.79 ? 24  GLU F C   1 
ATOM   1263 O  O   . GLU B 1 24  ? 1.193   -2.281  -6.256  1.00 35.89 ? 24  GLU F O   1 
ATOM   1264 C  CB  . GLU B 1 24  ? -0.326  -0.630  -8.512  1.00 42.95 ? 24  GLU F CB  1 
ATOM   1265 C  CG  . GLU B 1 24  ? -0.013  0.111   -9.802  1.00 45.58 ? 24  GLU F CG  1 
ATOM   1266 C  CD  . GLU B 1 24  ? 0.537   -0.728  -10.946 1.00 50.16 ? 24  GLU F CD  1 
ATOM   1267 O  OE1 . GLU B 1 24  ? 0.069   -1.875  -11.133 1.00 54.92 ? 24  GLU F OE1 1 
ATOM   1268 O  OE2 . GLU B 1 24  ? 1.422   -0.227  -11.668 1.00 52.76 ? 24  GLU F OE2 1 
ATOM   1269 N  N   . SER B 1 25  ? -0.606  -1.211  -5.345  1.00 39.93 ? 25  SER F N   1 
ATOM   1270 C  CA  . SER B 1 25  ? -0.804  -2.099  -4.167  1.00 39.52 ? 25  SER F CA  1 
ATOM   1271 C  C   . SER B 1 25  ? -1.022  -3.551  -4.616  1.00 39.60 ? 25  SER F C   1 
ATOM   1272 O  O   . SER B 1 25  ? -0.684  -4.467  -3.839  1.00 40.18 ? 25  SER F O   1 
ATOM   1273 C  CB  . SER B 1 25  ? -1.932  -1.610  -3.278  1.00 40.73 ? 25  SER F CB  1 
ATOM   1274 O  OG  . SER B 1 25  ? -3.183  -1.684  -3.944  1.00 43.39 ? 25  SER F OG  1 
ATOM   1275 N  N   . ASN B 1 26  ? -1.544  -3.769  -5.825  1.00 38.29 ? 26  ASN F N   1 
ATOM   1276 C  CA  . ASN B 1 26  ? -1.800  -5.132  -6.365  1.00 38.56 ? 26  ASN F CA  1 
ATOM   1277 C  C   . ASN B 1 26  ? -0.609  -5.583  -7.220  1.00 35.36 ? 26  ASN F C   1 
ATOM   1278 O  O   . ASN B 1 26  ? -0.705  -6.667  -7.826  1.00 39.41 ? 26  ASN F O   1 
ATOM   1279 C  CB  . ASN B 1 26  ? -3.125  -5.201  -7.135  1.00 40.63 ? 26  ASN F CB  1 
ATOM   1280 C  CG  . ASN B 1 26  ? -3.231  -4.213  -8.278  1.00 43.47 ? 26  ASN F CG  1 
ATOM   1281 O  OD1 . ASN B 1 26  ? -2.490  -3.232  -8.343  1.00 47.41 ? 26  ASN F OD1 1 
ATOM   1282 N  ND2 . ASN B 1 26  ? -4.166  -4.454  -9.183  1.00 44.90 ? 26  ASN F ND2 1 
ATOM   1283 N  N   . GLY B 1 27  ? 0.488   -4.814  -7.245  1.00 30.94 ? 27  GLY F N   1 
ATOM   1284 C  CA  . GLY B 1 27  ? 1.591   -5.016  -8.203  1.00 26.99 ? 27  GLY F CA  1 
ATOM   1285 C  C   . GLY B 1 27  ? 2.837   -5.610  -7.546  1.00 24.28 ? 27  GLY F C   1 
ATOM   1286 O  O   . GLY B 1 27  ? 2.938   -5.671  -6.319  1.00 22.92 ? 27  GLY F O   1 
ATOM   1287 N  N   . PRO B 1 28  ? 3.812   -6.067  -8.354  1.00 22.64 ? 28  PRO F N   1 
ATOM   1288 C  CA  . PRO B 1 28  ? 5.061   -6.601  -7.833  1.00 20.84 ? 28  PRO F CA  1 
ATOM   1289 C  C   . PRO B 1 28  ? 5.905   -5.519  -7.153  1.00 18.54 ? 28  PRO F C   1 
ATOM   1290 O  O   . PRO B 1 28  ? 5.774   -4.325  -7.426  1.00 17.81 ? 28  PRO F O   1 
ATOM   1291 C  CB  . PRO B 1 28  ? 5.814   -7.158  -9.047  1.00 22.46 ? 28  PRO F CB  1 
ATOM   1292 C  CG  . PRO B 1 28  ? 5.206   -6.402  -10.216 1.00 24.02 ? 28  PRO F CG  1 
ATOM   1293 C  CD  . PRO B 1 28  ? 3.776   -6.089  -9.823  1.00 23.89 ? 28  PRO F CD  1 
ATOM   1294 N  N   . VAL B 1 29  ? 6.764   -5.983  -6.254  1.00 15.98 ? 29  VAL F N   1 
ATOM   1295 C  CA  . VAL B 1 29  ? 7.712   -5.143  -5.488  1.00 15.43 ? 29  VAL F CA  1 
ATOM   1296 C  C   . VAL B 1 29  ? 9.091   -5.410  -6.076  1.00 15.15 ? 29  VAL F C   1 
ATOM   1297 O  O   . VAL B 1 29  ? 9.501   -6.580  -6.142  1.00 16.31 ? 29  VAL F O   1 
ATOM   1298 C  CB  . VAL B 1 29  ? 7.676   -5.486  -3.989  1.00 14.44 ? 29  VAL F CB  1 
ATOM   1299 C  CG1 . VAL B 1 29  ? 8.669   -4.603  -3.235  1.00 13.65 ? 29  VAL F CG1 1 
ATOM   1300 C  CG2 . VAL B 1 29  ? 6.277   -5.363  -3.413  1.00 15.24 ? 29  VAL F CG2 1 
ATOM   1301 N  N   . LYS B 1 30  ? 9.762   -4.355  -6.519  1.00 15.35 ? 30  LYS F N   1 
ATOM   1302 C  CA  . LYS B 1 30  ? 11.178  -4.413  -6.942  1.00 16.84 ? 30  LYS F CA  1 
ATOM   1303 C  C   . LYS B 1 30  ? 12.033  -4.250  -5.688  1.00 15.93 ? 30  LYS F C   1 
ATOM   1304 O  O   . LYS B 1 30  ? 11.756  -3.338  -4.889  1.00 15.43 ? 30  LYS F O   1 
ATOM   1305 C  CB  . LYS B 1 30  ? 11.457  -3.333  -7.986  1.00 19.08 ? 30  LYS F CB  1 
ATOM   1306 C  CG  . LYS B 1 30  ? 10.754  -3.546  -9.320  1.00 23.10 ? 30  LYS F CG  1 
ATOM   1307 C  CD  . LYS B 1 30  ? 11.510  -2.987  -10.510 1.00 24.65 ? 30  LYS F CD  1 
ATOM   1308 N  N   . VAL B 1 31  ? 13.000  -5.127  -5.505  1.00 15.71 ? 31  VAL F N   1 
ATOM   1309 C  CA  . VAL B 1 31  ? 13.923  -5.133  -4.339  1.00 16.02 ? 31  VAL F CA  1 
ATOM   1310 C  C   . VAL B 1 31  ? 15.329  -4.981  -4.897  1.00 16.39 ? 31  VAL F C   1 
ATOM   1311 O  O   . VAL B 1 31  ? 15.724  -5.835  -5.683  1.00 17.61 ? 31  VAL F O   1 
ATOM   1312 C  CB  . VAL B 1 31  ? 13.782  -6.431  -3.516  1.00 16.09 ? 31  VAL F CB  1 
ATOM   1313 C  CG1 . VAL B 1 31  ? 14.624  -6.390  -2.251  1.00 17.14 ? 31  VAL F CG1 1 
ATOM   1314 C  CG2 . VAL B 1 31  ? 12.336  -6.725  -3.179  1.00 16.04 ? 31  VAL F CG2 1 
ATOM   1315 N  N   . TRP B 1 32  ? 16.051  -3.945  -4.496  1.00 16.31 ? 32  TRP F N   1 
ATOM   1316 C  CA  . TRP B 1 32  ? 17.399  -3.735  -5.059  1.00 15.82 ? 32  TRP F CA  1 
ATOM   1317 C  C   . TRP B 1 32  ? 18.326  -3.114  -4.012  1.00 14.86 ? 32  TRP F C   1 
ATOM   1318 O  O   . TRP B 1 32  ? 17.840  -2.409  -3.146  1.00 14.89 ? 32  TRP F O   1 
ATOM   1319 C  CB  . TRP B 1 32  ? 17.353  -2.876  -6.329  1.00 18.13 ? 32  TRP F CB  1 
ATOM   1320 C  CG  . TRP B 1 32  ? 16.922  -1.455  -6.145  1.00 19.02 ? 32  TRP F CG  1 
ATOM   1321 C  CD1 . TRP B 1 32  ? 15.649  -0.970  -6.210  1.00 18.75 ? 32  TRP F CD1 1 
ATOM   1322 C  CD2 . TRP B 1 32  ? 17.771  -0.320  -5.902  1.00 21.16 ? 32  TRP F CD2 1 
ATOM   1323 N  NE1 . TRP B 1 32  ? 15.648  0.384   -6.019  1.00 21.48 ? 32  TRP F NE1 1 
ATOM   1324 C  CE2 . TRP B 1 32  ? 16.934  0.808   -5.816  1.00 21.04 ? 32  TRP F CE2 1 
ATOM   1325 C  CE3 . TRP B 1 32  ? 19.148  -0.147  -5.729  1.00 21.42 ? 32  TRP F CE3 1 
ATOM   1326 C  CZ2 . TRP B 1 32  ? 17.432  2.085   -5.566  1.00 22.61 ? 32  TRP F CZ2 1 
ATOM   1327 C  CZ3 . TRP B 1 32  ? 19.640  1.114   -5.482  1.00 23.26 ? 32  TRP F CZ3 1 
ATOM   1328 C  CH2 . TRP B 1 32  ? 18.791  2.216   -5.407  1.00 23.37 ? 32  TRP F CH2 1 
ATOM   1329 N  N   . GLY B 1 33  ? 19.622  -3.362  -4.143  1.00 13.70 ? 33  GLY F N   1 
ATOM   1330 C  CA  . GLY B 1 33  ? 20.631  -2.745  -3.283  1.00 14.26 ? 33  GLY F CA  1 
ATOM   1331 C  C   . GLY B 1 33  ? 21.874  -3.585  -3.257  1.00 14.24 ? 33  GLY F C   1 
ATOM   1332 O  O   . GLY B 1 33  ? 22.149  -4.287  -4.233  1.00 14.68 ? 33  GLY F O   1 
ATOM   1333 N  N   . SER B 1 34  ? 22.616  -3.519  -2.179  1.00 15.01 ? 34  SER F N   1 
ATOM   1334 C  CA  A SER B 1 34  ? 23.957  -4.143  -2.089  0.50 16.06 ? 34  SER F CA  1 
ATOM   1335 C  CA  B SER B 1 34  ? 23.918  -4.212  -2.098  0.50 15.68 ? 34  SER F CA  1 
ATOM   1336 C  C   . SER B 1 34  ? 24.192  -4.600  -0.654  1.00 15.96 ? 34  SER F C   1 
ATOM   1337 O  O   . SER B 1 34  ? 23.705  -3.916  0.252   1.00 16.27 ? 34  SER F O   1 
ATOM   1338 C  CB  A SER B 1 34  ? 25.010  -3.173  -2.548  0.50 17.56 ? 34  SER F CB  1 
ATOM   1339 C  CB  B SER B 1 34  ? 25.000  -3.356  -2.657  0.50 16.68 ? 34  SER F CB  1 
ATOM   1340 O  OG  A SER B 1 34  ? 26.313  -3.722  -2.411  0.50 19.78 ? 34  SER F OG  1 
ATOM   1341 O  OG  B SER B 1 34  ? 25.144  -2.188  -1.877  0.50 17.52 ? 34  SER F OG  1 
ATOM   1342 N  N   . ILE B 1 35  ? 24.915  -5.696  -0.479  1.00 15.31 ? 35  ILE F N   1 
ATOM   1343 C  CA  . ILE B 1 35  ? 25.300  -6.196  0.863   1.00 15.53 ? 35  ILE F CA  1 
ATOM   1344 C  C   . ILE B 1 35  ? 26.782  -6.540  0.790   1.00 15.59 ? 35  ILE F C   1 
ATOM   1345 O  O   . ILE B 1 35  ? 27.172  -7.246  -0.152  1.00 17.44 ? 35  ILE F O   1 
ATOM   1346 C  CB  . ILE B 1 35  ? 24.462  -7.417  1.274   1.00 15.47 ? 35  ILE F CB  1 
ATOM   1347 C  CG1 . ILE B 1 35  ? 22.958  -7.157  1.133   1.00 15.53 ? 35  ILE F CG1 1 
ATOM   1348 C  CG2 . ILE B 1 35  ? 24.821  -7.836  2.689   1.00 16.03 ? 35  ILE F CG2 1 
ATOM   1349 C  CD1 . ILE B 1 35  ? 22.093  -8.380  1.358   1.00 16.55 ? 35  ILE F CD1 1 
ATOM   1350 N  N   . LYS B 1 36  ? 27.571  -6.063  1.743   1.00 17.02 ? 36  LYS F N   1 
ATOM   1351 C  CA  . LYS B 1 36  ? 29.029  -6.328  1.739   1.00 18.64 ? 36  LYS F CA  1 
ATOM   1352 C  C   . LYS B 1 36  ? 29.396  -7.215  2.929   1.00 17.71 ? 36  LYS F C   1 
ATOM   1353 O  O   . LYS B 1 36  ? 28.624  -7.313  3.903   1.00 17.99 ? 36  LYS F O   1 
ATOM   1354 C  CB  . LYS B 1 36  ? 29.802  -5.010  1.732   1.00 20.68 ? 36  LYS F CB  1 
ATOM   1355 C  CG  . LYS B 1 36  ? 29.739  -4.220  3.022   1.00 23.05 ? 36  LYS F CG  1 
ATOM   1356 N  N   . GLY B 1 37  ? 30.547  -7.876  2.837   1.00 18.06 ? 37  GLY F N   1 
ATOM   1357 C  CA  . GLY B 1 37  ? 31.126  -8.661  3.939   1.00 18.81 ? 37  GLY F CA  1 
ATOM   1358 C  C   . GLY B 1 37  ? 30.652  -10.102 3.943   1.00 18.81 ? 37  GLY F C   1 
ATOM   1359 O  O   . GLY B 1 37  ? 30.878  -10.774 4.968   1.00 21.54 ? 37  GLY F O   1 
ATOM   1360 N  N   . LEU B 1 38  ? 29.995  -10.545 2.871   1.00 18.30 ? 38  LEU F N   1 
ATOM   1361 C  CA  . LEU B 1 38  ? 29.440  -11.923 2.777   1.00 18.02 ? 38  LEU F CA  1 
ATOM   1362 C  C   . LEU B 1 38  ? 30.499  -12.887 2.230   1.00 18.85 ? 38  LEU F C   1 
ATOM   1363 O  O   . LEU B 1 38  ? 31.286  -12.489 1.360   1.00 20.53 ? 38  LEU F O   1 
ATOM   1364 C  CB  . LEU B 1 38  ? 28.220  -11.929 1.861   1.00 17.77 ? 38  LEU F CB  1 
ATOM   1365 C  CG  . LEU B 1 38  ? 26.988  -11.201 2.385   1.00 17.34 ? 38  LEU F CG  1 
ATOM   1366 C  CD1 . LEU B 1 38  ? 25.943  -11.089 1.292   1.00 17.70 ? 38  LEU F CD1 1 
ATOM   1367 C  CD2 . LEU B 1 38  ? 26.411  -11.893 3.619   1.00 17.01 ? 38  LEU F CD2 1 
ATOM   1368 N  N   . THR B 1 39  ? 30.488  -14.129 2.697   1.00 17.76 ? 39  THR F N   1 
ATOM   1369 C  CA  . THR B 1 39  ? 31.255  -15.232 2.063   1.00 18.42 ? 39  THR F CA  1 
ATOM   1370 C  C   . THR B 1 39  ? 30.680  -15.505 0.670   1.00 18.26 ? 39  THR F C   1 
ATOM   1371 O  O   . THR B 1 39  ? 29.459  -15.346 0.455   1.00 16.98 ? 39  THR F O   1 
ATOM   1372 C  CB  . THR B 1 39  ? 31.269  -16.476 2.953   1.00 19.19 ? 39  THR F CB  1 
ATOM   1373 O  OG1 . THR B 1 39  ? 29.917  -16.888 3.152   1.00 18.81 ? 39  THR F OG1 1 
ATOM   1374 C  CG2 . THR B 1 39  ? 31.955  -16.223 4.274   1.00 18.51 ? 39  THR F CG2 1 
ATOM   1375 N  N   . GLU B 1 40  ? 31.531  -15.915 -0.266  1.00 18.01 ? 40  GLU F N   1 
ATOM   1376 C  CA  . GLU B 1 40  ? 31.109  -16.293 -1.630  1.00 18.34 ? 40  GLU F CA  1 
ATOM   1377 C  C   . GLU B 1 40  ? 30.039  -17.381 -1.549  1.00 17.12 ? 40  GLU F C   1 
ATOM   1378 O  O   . GLU B 1 40  ? 30.216  -18.347 -0.791  1.00 18.68 ? 40  GLU F O   1 
ATOM   1379 C  CB  . GLU B 1 40  ? 32.295  -16.806 -2.444  1.00 18.37 ? 40  GLU F CB  1 
ATOM   1380 C  CG  . GLU B 1 40  ? 31.908  -17.256 -3.844  1.00 20.46 ? 40  GLU F CG  1 
ATOM   1381 C  CD  . GLU B 1 40  ? 33.016  -17.944 -4.614  1.00 22.28 ? 40  GLU F CD  1 
ATOM   1382 O  OE1 . GLU B 1 40  ? 33.885  -18.589 -3.974  1.00 25.67 ? 40  GLU F OE1 1 
ATOM   1383 O  OE2 . GLU B 1 40  ? 33.013  -17.827 -5.839  1.00 22.09 ? 40  GLU F OE2 1 
ATOM   1384 N  N   . GLY B 1 41  ? 28.946  -17.194 -2.283  1.00 16.78 ? 41  GLY F N   1 
ATOM   1385 C  CA  . GLY B 1 41  ? 27.879  -18.192 -2.403  1.00 15.96 ? 41  GLY F CA  1 
ATOM   1386 C  C   . GLY B 1 41  ? 26.538  -17.606 -2.038  1.00 15.46 ? 41  GLY F C   1 
ATOM   1387 O  O   . GLY B 1 41  ? 26.393  -16.379 -2.035  1.00 15.80 ? 41  GLY F O   1 
ATOM   1388 N  N   . LEU B 1 42  ? 25.596  -18.484 -1.743  1.00 15.15 ? 42  LEU F N   1 
ATOM   1389 C  CA  . LEU B 1 42  ? 24.178  -18.136 -1.511  1.00 16.27 ? 42  LEU F CA  1 
ATOM   1390 C  C   . LEU B 1 42  ? 24.006  -17.794 -0.032  1.00 14.41 ? 42  LEU F C   1 
ATOM   1391 O  O   . LEU B 1 42  ? 24.546  -18.491 0.840   1.00 14.25 ? 42  LEU F O   1 
ATOM   1392 C  CB  . LEU B 1 42  ? 23.292  -19.317 -1.910  1.00 17.88 ? 42  LEU F CB  1 
ATOM   1393 C  CG  . LEU B 1 42  ? 22.852  -19.345 -3.372  1.00 22.22 ? 42  LEU F CG  1 
ATOM   1394 C  CD1 . LEU B 1 42  ? 24.026  -19.629 -4.267  1.00 23.03 ? 42  LEU F CD1 1 
ATOM   1395 C  CD2 . LEU B 1 42  ? 21.767  -20.385 -3.594  1.00 22.81 ? 42  LEU F CD2 1 
ATOM   1396 N  N   . HIS B 1 43  ? 23.186  -16.795 0.239   1.00 13.86 ? 43  HIS F N   1 
ATOM   1397 C  CA  . HIS B 1 43  ? 22.816  -16.389 1.611   1.00 13.92 ? 43  HIS F CA  1 
ATOM   1398 C  C   . HIS B 1 43  ? 21.310  -16.229 1.693   1.00 12.83 ? 43  HIS F C   1 
ATOM   1399 O  O   . HIS B 1 43  ? 20.768  -15.424 0.913   1.00 12.95 ? 43  HIS F O   1 
ATOM   1400 C  CB  . HIS B 1 43  ? 23.517  -15.089 1.975   1.00 13.90 ? 43  HIS F CB  1 
ATOM   1401 C  CG  . HIS B 1 43  ? 24.982  -15.291 2.058   1.00 14.43 ? 43  HIS F CG  1 
ATOM   1402 N  ND1 . HIS B 1 43  ? 25.573  -15.703 3.226   1.00 15.69 ? 43  HIS F ND1 1 
ATOM   1403 C  CD2 . HIS B 1 43  ? 25.953  -15.226 1.117   1.00 15.41 ? 43  HIS F CD2 1 
ATOM   1404 C  CE1 . HIS B 1 43  ? 26.879  -15.846 3.008   1.00 16.04 ? 43  HIS F CE1 1 
ATOM   1405 N  NE2 . HIS B 1 43  ? 27.128  -15.557 1.730   1.00 16.40 ? 43  HIS F NE2 1 
ATOM   1406 N  N   . GLY B 1 44  ? 20.677  -16.961 2.609   1.00 13.71 ? 44  GLY F N   1 
ATOM   1407 C  CA  . GLY B 1 44  ? 19.223  -16.852 2.778   1.00 13.28 ? 44  GLY F CA  1 
ATOM   1408 C  C   . GLY B 1 44  ? 18.800  -15.406 3.019   1.00 12.39 ? 44  GLY F C   1 
ATOM   1409 O  O   . GLY B 1 44  ? 19.513  -14.644 3.697   1.00 13.27 ? 44  GLY F O   1 
ATOM   1410 N  N   . PHE B 1 45  ? 17.662  -15.032 2.457   1.00 11.88 ? 45  PHE F N   1 
ATOM   1411 C  CA  . PHE B 1 45  ? 17.201  -13.627 2.422   1.00 12.24 ? 45  PHE F CA  1 
ATOM   1412 C  C   . PHE B 1 45  ? 15.718  -13.630 2.740   1.00 11.67 ? 45  PHE F C   1 
ATOM   1413 O  O   . PHE B 1 45  ? 14.939  -14.066 1.911   1.00 12.54 ? 45  PHE F O   1 
ATOM   1414 C  CB  . PHE B 1 45  ? 17.510  -13.048 1.045   1.00 12.69 ? 45  PHE F CB  1 
ATOM   1415 C  CG  . PHE B 1 45  ? 17.411  -11.555 0.909   1.00 13.57 ? 45  PHE F CG  1 
ATOM   1416 C  CD1 . PHE B 1 45  ? 18.160  -10.714 1.711   1.00 15.06 ? 45  PHE F CD1 1 
ATOM   1417 C  CD2 . PHE B 1 45  ? 16.645  -11.007 -0.099  1.00 13.78 ? 45  PHE F CD2 1 
ATOM   1418 C  CE1 . PHE B 1 45  ? 18.107  -9.343  1.528   1.00 15.65 ? 45  PHE F CE1 1 
ATOM   1419 C  CE2 . PHE B 1 45  ? 16.600  -9.639  -0.279  1.00 15.17 ? 45  PHE F CE2 1 
ATOM   1420 C  CZ  . PHE B 1 45  ? 17.325  -8.819  0.533   1.00 15.20 ? 45  PHE F CZ  1 
ATOM   1421 N  N   . HIS B 1 46  ? 15.363  -13.183 3.932   1.00 11.58 ? 46  HIS F N   1 
ATOM   1422 C  CA  . HIS B 1 46  ? 13.992  -13.378 4.454   1.00 11.84 ? 46  HIS F CA  1 
ATOM   1423 C  C   . HIS B 1 46  ? 13.437  -12.129 5.097   1.00 11.67 ? 46  HIS F C   1 
ATOM   1424 O  O   . HIS B 1 46  ? 14.183  -11.385 5.752   1.00 11.75 ? 46  HIS F O   1 
ATOM   1425 C  CB  . HIS B 1 46  ? 13.932  -14.448 5.547   1.00 13.38 ? 46  HIS F CB  1 
ATOM   1426 C  CG  . HIS B 1 46  ? 14.533  -15.748 5.178   1.00 14.44 ? 46  HIS F CG  1 
ATOM   1427 N  ND1 . HIS B 1 46  ? 15.275  -16.496 6.081   1.00 16.91 ? 46  HIS F ND1 1 
ATOM   1428 C  CD2 . HIS B 1 46  ? 14.476  -16.460 4.026   1.00 16.19 ? 46  HIS F CD2 1 
ATOM   1429 C  CE1 . HIS B 1 46  ? 15.678  -17.601 5.478   1.00 17.33 ? 46  HIS F CE1 1 
ATOM   1430 N  NE2 . HIS B 1 46  ? 15.215  -17.596 4.229   1.00 16.89 ? 46  HIS F NE2 1 
ATOM   1431 N  N   . VAL B 1 47  ? 12.140  -11.958 4.966   1.00 11.20 ? 47  VAL F N   1 
ATOM   1432 C  CA  . VAL B 1 47  ? 11.389  -11.044 5.852   1.00 10.84 ? 47  VAL F CA  1 
ATOM   1433 C  C   . VAL B 1 47  ? 10.905  -11.864 7.042   1.00 11.02 ? 47  VAL F C   1 
ATOM   1434 O  O   . VAL B 1 47  ? 10.168  -12.857 6.857   1.00 11.45 ? 47  VAL F O   1 
ATOM   1435 C  CB  . VAL B 1 47  ? 10.226  -10.332 5.157   1.00 11.50 ? 47  VAL F CB  1 
ATOM   1436 C  CG1 . VAL B 1 47  ? 9.534   -9.371  6.113   1.00 11.99 ? 47  VAL F CG1 1 
ATOM   1437 C  CG2 . VAL B 1 47  ? 10.693  -9.628  3.908   1.00 12.06 ? 47  VAL F CG2 1 
ATOM   1438 N  N   . HIS B 1 48  ? 11.347  -11.467 8.219   1.00 11.76 ? 48  HIS F N   1 
ATOM   1439 C  CA  . HIS B 1 48  ? 10.938  -12.094 9.488   1.00 11.84 ? 48  HIS F CA  1 
ATOM   1440 C  C   . HIS B 1 48  ? 9.796   -11.271 10.082  1.00 12.51 ? 48  HIS F C   1 
ATOM   1441 O  O   . HIS B 1 48  ? 9.636   -10.089 9.751   1.00 12.91 ? 48  HIS F O   1 
ATOM   1442 C  CB  . HIS B 1 48  ? 12.156  -12.216 10.400  1.00 12.35 ? 48  HIS F CB  1 
ATOM   1443 C  CG  . HIS B 1 48  ? 13.085  -13.327 10.033  1.00 12.87 ? 48  HIS F CG  1 
ATOM   1444 N  ND1 . HIS B 1 48  ? 13.188  -14.422 10.831  1.00 13.52 ? 48  HIS F ND1 1 
ATOM   1445 C  CD2 . HIS B 1 48  ? 13.906  -13.559 8.978   1.00 14.67 ? 48  HIS F CD2 1 
ATOM   1446 C  CE1 . HIS B 1 48  ? 14.066  -15.258 10.336  1.00 14.48 ? 48  HIS F CE1 1 
ATOM   1447 N  NE2 . HIS B 1 48  ? 14.525  -14.769 9.219   1.00 14.54 ? 48  HIS F NE2 1 
ATOM   1448 N  N   . GLU B 1 49  ? 9.035   -11.869 10.979  1.00 12.20 ? 49  GLU F N   1 
ATOM   1449 C  CA  . GLU B 1 49  ? 7.715   -11.346 11.376  1.00 13.04 ? 49  GLU F CA  1 
ATOM   1450 C  C   . GLU B 1 49  ? 7.801   -10.018 12.130  1.00 12.27 ? 49  GLU F C   1 
ATOM   1451 O  O   . GLU B 1 49  ? 6.965   -9.146  11.858  1.00 13.71 ? 49  GLU F O   1 
ATOM   1452 C  CB  . GLU B 1 49  ? 7.028   -12.377 12.250  1.00 14.45 ? 49  GLU F CB  1 
ATOM   1453 C  CG  . GLU B 1 49  ? 5.630   -11.947 12.647  1.00 16.28 ? 49  GLU F CG  1 
ATOM   1454 C  CD  . GLU B 1 49  ? 4.927   -12.946 13.535  1.00 18.13 ? 49  GLU F CD  1 
ATOM   1455 O  OE1 . GLU B 1 49  ? 5.537   -13.985 13.853  1.00 20.12 ? 49  GLU F OE1 1 
ATOM   1456 O  OE2 . GLU B 1 49  ? 3.783   -12.643 13.929  1.00 20.52 ? 49  GLU F OE2 1 
ATOM   1457 N  N   . PHE B 1 50  ? 8.735   -9.867  13.050  1.00 11.86 ? 50  PHE F N   1 
ATOM   1458 C  CA  . PHE B 1 50  ? 8.728   -8.693  13.950  1.00 12.35 ? 50  PHE F CA  1 
ATOM   1459 C  C   . PHE B 1 50  ? 9.821   -7.712  13.560  1.00 11.82 ? 50  PHE F C   1 
ATOM   1460 O  O   . PHE B 1 50  ? 10.957  -8.139  13.261  1.00 12.89 ? 50  PHE F O   1 
ATOM   1461 C  CB  . PHE B 1 50  ? 8.939   -9.107  15.403  1.00 13.15 ? 50  PHE F CB  1 
ATOM   1462 C  CG  . PHE B 1 50  ? 8.002   -10.190 15.839  1.00 14.48 ? 50  PHE F CG  1 
ATOM   1463 C  CD1 . PHE B 1 50  ? 6.639   -10.005 15.724  1.00 15.05 ? 50  PHE F CD1 1 
ATOM   1464 C  CD2 . PHE B 1 50  ? 8.490   -11.390 16.341  1.00 16.25 ? 50  PHE F CD2 1 
ATOM   1465 C  CE1 . PHE B 1 50  ? 5.756   -11.000 16.117  1.00 16.11 ? 50  PHE F CE1 1 
ATOM   1466 C  CE2 . PHE B 1 50  ? 7.604   -12.381 16.746  1.00 15.71 ? 50  PHE F CE2 1 
ATOM   1467 C  CZ  . PHE B 1 50  ? 6.243   -12.190 16.611  1.00 16.86 ? 50  PHE F CZ  1 
ATOM   1468 N  N   . GLY B 1 51  ? 9.482   -6.430  13.606  1.00 12.20 ? 51  GLY F N   1 
ATOM   1469 C  CA  . GLY B 1 51  ? 10.456  -5.339  13.448  1.00 12.46 ? 51  GLY F CA  1 
ATOM   1470 C  C   . GLY B 1 51  ? 11.090  -5.022  14.782  1.00 13.30 ? 51  GLY F C   1 
ATOM   1471 O  O   . GLY B 1 51  ? 11.103  -3.848  15.179  1.00 13.63 ? 51  GLY F O   1 
ATOM   1472 N  N   . ASP B 1 52  ? 11.567  -6.054  15.467  1.00 14.17 ? 52  ASP F N   1 
ATOM   1473 C  CA  . ASP B 1 52  ? 12.068  -5.979  16.854  1.00 14.58 ? 52  ASP F CA  1 
ATOM   1474 C  C   . ASP B 1 52  ? 13.542  -6.344  16.798  1.00 15.00 ? 52  ASP F C   1 
ATOM   1475 O  O   . ASP B 1 52  ? 13.857  -7.509  16.526  1.00 15.73 ? 52  ASP F O   1 
ATOM   1476 C  CB  . ASP B 1 52  ? 11.257  -6.886  17.777  1.00 15.62 ? 52  ASP F CB  1 
ATOM   1477 C  CG  . ASP B 1 52  ? 11.632  -6.746  19.239  1.00 17.05 ? 52  ASP F CG  1 
ATOM   1478 O  OD1 . ASP B 1 52  ? 12.750  -6.298  19.516  1.00 18.72 ? 52  ASP F OD1 1 
ATOM   1479 O  OD2 . ASP B 1 52  ? 10.801  -7.101  20.090  1.00 19.51 ? 52  ASP F OD2 1 
ATOM   1480 N  N   . ASN B 1 53  ? 14.403  -5.368  17.031  1.00 15.28 ? 53  ASN F N   1 
ATOM   1481 C  CA  . ASN B 1 53  ? 15.871  -5.567  17.044  1.00 17.77 ? 53  ASN F CA  1 
ATOM   1482 C  C   . ASN B 1 53  ? 16.408  -5.384  18.467  1.00 18.38 ? 53  ASN F C   1 
ATOM   1483 O  O   . ASN B 1 53  ? 17.618  -5.124  18.595  1.00 19.72 ? 53  ASN F O   1 
ATOM   1484 C  CB  . ASN B 1 53  ? 16.540  -4.587  16.077  1.00 20.45 ? 53  ASN F CB  1 
ATOM   1485 C  CG  . ASN B 1 53  ? 17.963  -4.972  15.718  0.60 22.15 ? 53  ASN F CG  1 
ATOM   1486 O  OD1 . ASN B 1 53  ? 18.216  -6.106  15.314  0.60 23.29 ? 53  ASN F OD1 1 
ATOM   1487 N  ND2 . ASN B 1 53  ? 18.890  -4.028  15.802  0.60 23.26 ? 53  ASN F ND2 1 
ATOM   1488 N  N   . THR B 1 54  ? 15.565  -5.535  19.487  1.00 18.47 ? 54  THR F N   1 
ATOM   1489 C  CA  . THR B 1 54  ? 15.942  -5.258  20.904  1.00 20.82 ? 54  THR F CA  1 
ATOM   1490 C  C   . THR B 1 54  ? 17.167  -6.081  21.301  1.00 21.01 ? 54  THR F C   1 
ATOM   1491 O  O   . THR B 1 54  ? 18.063  -5.515  21.972  1.00 19.76 ? 54  THR F O   1 
ATOM   1492 C  CB  . THR B 1 54  ? 14.811  -5.538  21.891  1.00 22.70 ? 54  THR F CB  1 
ATOM   1493 O  OG1 . THR B 1 54  ? 14.340  -6.850  21.639  1.00 24.88 ? 54  THR F OG1 1 
ATOM   1494 C  CG2 . THR B 1 54  ? 13.657  -4.571  21.764  1.00 22.26 ? 54  THR F CG2 1 
ATOM   1495 N  N   . ALA B 1 55  ? 17.228  -7.332  20.881  1.00 22.24 ? 55  ALA F N   1 
ATOM   1496 C  CA  . ALA B 1 55  ? 18.415  -8.153  21.209  1.00 23.38 ? 55  ALA F CA  1 
ATOM   1497 C  C   . ALA B 1 55  ? 19.109  -8.580  19.936  1.00 24.36 ? 55  ALA F C   1 
ATOM   1498 O  O   . ALA B 1 55  ? 19.680  -9.663  19.889  1.00 28.04 ? 55  ALA F O   1 
ATOM   1499 C  CB  . ALA B 1 55  ? 18.010  -9.345  22.007  1.00 24.83 ? 55  ALA F CB  1 
ATOM   1500 N  N   . GLY B 1 56  ? 19.110  -7.695  18.974  1.00 21.35 ? 56  GLY F N   1 
ATOM   1501 C  CA  . GLY B 1 56  ? 19.690  -8.063  17.694  1.00 20.79 ? 56  GLY F CA  1 
ATOM   1502 C  C   . GLY B 1 56  ? 18.719  -8.810  16.811  1.00 19.56 ? 56  GLY F C   1 
ATOM   1503 O  O   . GLY B 1 56  ? 17.538  -8.826  17.115  1.00 19.34 ? 56  GLY F O   1 
ATOM   1504 N  N   . CYS B 1 57  ? 19.259  -9.500  15.822  1.00 17.91 ? 57  CYS F N   1 
ATOM   1505 C  CA  . CYS B 1 57  ? 18.442  -10.148 14.769  1.00 17.87 ? 57  CYS F CA  1 
ATOM   1506 C  C   . CYS B 1 57  ? 17.570  -11.285 15.325  1.00 16.93 ? 57  CYS F C   1 
ATOM   1507 O  O   . CYS B 1 57  ? 16.518  -11.573 14.716  1.00 16.32 ? 57  CYS F O   1 
ATOM   1508 C  CB  . CYS B 1 57  ? 19.338  -10.624 13.637  1.00 17.92 ? 57  CYS F CB  1 
ATOM   1509 S  SG  . CYS B 1 57  ? 20.259  -9.256  12.875  1.00 22.25 ? 57  CYS F SG  1 
ATOM   1510 N  N   . THR B 1 58  ? 17.918  -11.866 16.474  1.00 18.55 ? 58  THR F N   1 
ATOM   1511 C  CA  . THR B 1 58  ? 17.121  -12.960 17.080  1.00 19.04 ? 58  THR F CA  1 
ATOM   1512 C  C   . THR B 1 58  ? 15.704  -12.474 17.431  1.00 18.02 ? 58  THR F C   1 
ATOM   1513 O  O   . THR B 1 58  ? 14.741  -13.251 17.265  1.00 18.45 ? 58  THR F O   1 
ATOM   1514 C  CB  . THR B 1 58  ? 17.855  -13.579 18.276  1.00 21.78 ? 58  THR F CB  1 
ATOM   1515 O  OG1 . THR B 1 58  ? 18.086  -12.585 19.276  1.00 25.48 ? 58  THR F OG1 1 
ATOM   1516 C  CG2 . THR B 1 58  ? 19.162  -14.215 17.862  1.00 23.42 ? 58  THR F CG2 1 
ATOM   1517 N  N   A SER B 1 59  ? 15.536  -11.226 17.870  0.50 17.82 ? 59  SER F N   1 
ATOM   1518 N  N   B SER B 1 59  ? 15.576  -11.210 17.835  0.50 16.69 ? 59  SER F N   1 
ATOM   1519 C  CA  A SER B 1 59  ? 14.214  -10.719 18.324  0.50 17.77 ? 59  SER F CA  1 
ATOM   1520 C  CA  B SER B 1 59  ? 14.303  -10.609 18.297  0.50 16.04 ? 59  SER F CA  1 
ATOM   1521 C  C   A SER B 1 59  ? 13.244  -10.591 17.143  0.50 16.36 ? 59  SER F C   1 
ATOM   1522 C  C   B SER B 1 59  ? 13.280  -10.558 17.151  0.50 15.45 ? 59  SER F C   1 
ATOM   1523 O  O   A SER B 1 59  ? 12.046  -10.389 17.405  0.50 16.83 ? 59  SER F O   1 
ATOM   1524 O  O   B SER B 1 59  ? 12.095  -10.387 17.446  0.50 15.86 ? 59  SER F O   1 
ATOM   1525 C  CB  A SER B 1 59  ? 14.306  -9.427  19.100  0.50 18.75 ? 59  SER F CB  1 
ATOM   1526 C  CB  B SER B 1 59  ? 14.548  -9.247  18.912  0.50 15.89 ? 59  SER F CB  1 
ATOM   1527 O  OG  A SER B 1 59  ? 15.358  -8.598  18.645  0.50 20.89 ? 59  SER F OG  1 
ATOM   1528 O  OG  B SER B 1 59  ? 15.312  -9.368  20.108  0.50 15.45 ? 59  SER F OG  1 
ATOM   1529 N  N   . ALA B 1 60  ? 13.716  -10.750 15.901  1.00 15.35 ? 60  ALA F N   1 
ATOM   1530 C  CA  . ALA B 1 60  ? 12.853  -10.619 14.705  1.00 14.38 ? 60  ALA F CA  1 
ATOM   1531 C  C   . ALA B 1 60  ? 11.860  -11.783 14.593  1.00 14.17 ? 60  ALA F C   1 
ATOM   1532 O  O   . ALA B 1 60  ? 10.919  -11.676 13.806  1.00 13.90 ? 60  ALA F O   1 
ATOM   1533 C  CB  . ALA B 1 60  ? 13.693  -10.490 13.457  1.00 15.74 ? 60  ALA F CB  1 
ATOM   1534 N  N   . GLY B 1 61  ? 12.050  -12.873 15.321  1.00 13.36 ? 61  GLY F N   1 
ATOM   1535 C  CA  . GLY B 1 61  ? 11.094  -13.984 15.317  1.00 13.65 ? 61  GLY F CA  1 
ATOM   1536 C  C   . GLY B 1 61  ? 11.207  -14.819 14.047  1.00 13.90 ? 61  GLY F C   1 
ATOM   1537 O  O   . GLY B 1 61  ? 12.218  -14.812 13.347  1.00 13.24 ? 61  GLY F O   1 
ATOM   1538 N  N   . PRO B 1 62  ? 10.139  -15.573 13.736  1.00 14.01 ? 62  PRO F N   1 
ATOM   1539 C  CA  . PRO B 1 62  ? 10.159  -16.514 12.626  1.00 14.52 ? 62  PRO F CA  1 
ATOM   1540 C  C   . PRO B 1 62  ? 9.927   -15.804 11.289  1.00 13.87 ? 62  PRO F C   1 
ATOM   1541 O  O   . PRO B 1 62  ? 9.779   -14.598 11.252  1.00 13.39 ? 62  PRO F O   1 
ATOM   1542 C  CB  . PRO B 1 62  ? 9.010   -17.439 13.025  1.00 15.46 ? 62  PRO F CB  1 
ATOM   1543 C  CG  . PRO B 1 62  ? 8.018   -16.541 13.686  1.00 15.82 ? 62  PRO F CG  1 
ATOM   1544 C  CD  . PRO B 1 62  ? 8.858   -15.560 14.457  1.00 14.67 ? 62  PRO F CD  1 
ATOM   1545 N  N   . HIS B 1 63  ? 9.923   -16.566 10.200  1.00 14.86 ? 63  HIS F N   1 
ATOM   1546 C  CA  . HIS B 1 63  ? 9.650   -16.015 8.854   1.00 14.22 ? 63  HIS F CA  1 
ATOM   1547 C  C   . HIS B 1 63  ? 8.263   -15.398 8.869   1.00 13.19 ? 63  HIS F C   1 
ATOM   1548 O  O   . HIS B 1 63  ? 7.347   -15.934 9.530   1.00 13.21 ? 63  HIS F O   1 
ATOM   1549 C  CB  . HIS B 1 63  ? 9.697   -17.101 7.784   1.00 14.67 ? 63  HIS F CB  1 
ATOM   1550 C  CG  . HIS B 1 63  ? 11.058  -17.672 7.626   1.00 15.29 ? 63  HIS F CG  1 
ATOM   1551 N  ND1 . HIS B 1 63  ? 11.397  -18.487 6.574   1.00 15.04 ? 63  HIS F ND1 1 
ATOM   1552 C  CD2 . HIS B 1 63  ? 12.175  -17.550 8.378   1.00 17.83 ? 63  HIS F CD2 1 
ATOM   1553 C  CE1 . HIS B 1 63  ? 12.641  -18.877 6.685   1.00 17.08 ? 63  HIS F CE1 1 
ATOM   1554 N  NE2 . HIS B 1 63  ? 13.159  -18.297 7.775   1.00 18.73 ? 63  HIS F NE2 1 
ATOM   1555 N  N   . PHE B 1 64  ? 8.100   -14.289 8.177   1.00 12.46 ? 64  PHE F N   1 
ATOM   1556 C  CA  . PHE B 1 64  ? 6.768   -13.663 8.060   1.00 12.21 ? 64  PHE F CA  1 
ATOM   1557 C  C   . PHE B 1 64  ? 5.854   -14.606 7.277   1.00 12.48 ? 64  PHE F C   1 
ATOM   1558 O  O   . PHE B 1 64  ? 6.129   -14.912 6.111   1.00 12.66 ? 64  PHE F O   1 
ATOM   1559 C  CB  . PHE B 1 64  ? 6.906   -12.289 7.425   1.00 12.51 ? 64  PHE F CB  1 
ATOM   1560 C  CG  . PHE B 1 64  ? 5.597   -11.570 7.234   1.00 12.69 ? 64  PHE F CG  1 
ATOM   1561 C  CD1 . PHE B 1 64  ? 4.654   -11.496 8.248   1.00 13.69 ? 64  PHE F CD1 1 
ATOM   1562 C  CD2 . PHE B 1 64  ? 5.351   -10.909 6.049   1.00 13.55 ? 64  PHE F CD2 1 
ATOM   1563 C  CE1 . PHE B 1 64  ? 3.459   -10.826 8.036   1.00 14.12 ? 64  PHE F CE1 1 
ATOM   1564 C  CE2 . PHE B 1 64  ? 4.165   -10.224 5.856   1.00 13.95 ? 64  PHE F CE2 1 
ATOM   1565 C  CZ  . PHE B 1 64  ? 3.229   -10.181 6.852   1.00 14.14 ? 64  PHE F CZ  1 
ATOM   1566 N  N   . ASN B 1 65  ? 4.827   -15.136 7.936   1.00 13.01 ? 65  ASN F N   1 
ATOM   1567 C  CA  . ASN B 1 65  ? 4.015   -16.259 7.411   1.00 13.54 ? 65  ASN F CA  1 
ATOM   1568 C  C   . ASN B 1 65  ? 2.552   -16.044 7.762   1.00 15.17 ? 65  ASN F C   1 
ATOM   1569 O  O   . ASN B 1 65  ? 1.939   -16.885 8.426   1.00 16.01 ? 65  ASN F O   1 
ATOM   1570 C  CB  . ASN B 1 65  ? 4.526   -17.589 7.959   1.00 13.24 ? 65  ASN F CB  1 
ATOM   1571 C  CG  . ASN B 1 65  ? 3.826   -18.787 7.352   1.00 14.82 ? 65  ASN F CG  1 
ATOM   1572 O  OD1 . ASN B 1 65  ? 3.292   -18.698 6.260   1.00 14.68 ? 65  ASN F OD1 1 
ATOM   1573 N  ND2 . ASN B 1 65  ? 3.870   -19.919 8.029   1.00 15.22 ? 65  ASN F ND2 1 
ATOM   1574 N  N   . PRO B 1 66  ? 1.930   -14.947 7.299   1.00 15.91 ? 66  PRO F N   1 
ATOM   1575 C  CA  . PRO B 1 66  ? 0.550   -14.654 7.697   1.00 16.82 ? 66  PRO F CA  1 
ATOM   1576 C  C   . PRO B 1 66  ? -0.457  -15.684 7.166   1.00 18.15 ? 66  PRO F C   1 
ATOM   1577 O  O   . PRO B 1 66  ? -1.550  -15.775 7.738   1.00 20.10 ? 66  PRO F O   1 
ATOM   1578 C  CB  . PRO B 1 66  ? 0.296   -13.253 7.134   1.00 17.23 ? 66  PRO F CB  1 
ATOM   1579 C  CG  . PRO B 1 66  ? 1.269   -13.146 5.964   1.00 16.72 ? 66  PRO F CG  1 
ATOM   1580 C  CD  . PRO B 1 66  ? 2.488   -13.943 6.375   1.00 15.85 ? 66  PRO F CD  1 
ATOM   1581 N  N   . LEU B 1 67  ? -0.099  -16.454 6.137   1.00 17.44 ? 67  LEU F N   1 
ATOM   1582 C  CA  . LEU B 1 67  ? -1.025  -17.421 5.481   1.00 18.33 ? 67  LEU F CA  1 
ATOM   1583 C  C   . LEU B 1 67  ? -0.744  -18.854 5.942   1.00 18.74 ? 67  LEU F C   1 
ATOM   1584 O  O   . LEU B 1 67  ? -1.332  -19.783 5.371   1.00 18.90 ? 67  LEU F O   1 
ATOM   1585 C  CB  . LEU B 1 67  ? -0.916  -17.260 3.964   1.00 19.61 ? 67  LEU F CB  1 
ATOM   1586 C  CG  . LEU B 1 67  ? -1.339  -15.887 3.445   1.00 20.90 ? 67  LEU F CG  1 
ATOM   1587 C  CD1 . LEU B 1 67  ? -1.164  -15.791 1.944   1.00 21.25 ? 67  LEU F CD1 1 
ATOM   1588 C  CD2 . LEU B 1 67  ? -2.771  -15.547 3.836   1.00 22.39 ? 67  LEU F CD2 1 
ATOM   1589 N  N   . SER B 1 68  ? 0.107   -19.046 6.953   1.00 18.77 ? 68  SER F N   1 
ATOM   1590 C  CA  . SER B 1 68  ? 0.317   -20.368 7.601   1.00 19.82 ? 68  SER F CA  1 
ATOM   1591 C  C   . SER B 1 68  ? 0.706   -21.424 6.561   1.00 19.52 ? 68  SER F C   1 
ATOM   1592 O  O   . SER B 1 68  ? 0.090   -22.514 6.526   1.00 21.76 ? 68  SER F O   1 
ATOM   1593 C  CB  . SER B 1 68  ? -0.919  -20.797 8.366   1.00 20.49 ? 68  SER F CB  1 
ATOM   1594 O  OG  . SER B 1 68  ? -1.287  -19.828 9.330   1.00 22.12 ? 68  SER F OG  1 
ATOM   1595 N  N   . ARG B 1 69  ? 1.700   -21.129 5.729   1.00 17.69 ? 69  ARG F N   1 
ATOM   1596 C  CA  . ARG B 1 69  ? 2.220   -22.064 4.703   1.00 18.06 ? 69  ARG F CA  1 
ATOM   1597 C  C   . ARG B 1 69  ? 3.542   -22.641 5.193   1.00 17.39 ? 69  ARG F C   1 
ATOM   1598 O  O   . ARG B 1 69  ? 4.053   -22.176 6.237   1.00 18.27 ? 69  ARG F O   1 
ATOM   1599 C  CB  . ARG B 1 69  ? 2.416   -21.337 3.369   1.00 19.50 ? 69  ARG F CB  1 
ATOM   1600 C  CG  . ARG B 1 69  ? 1.200   -20.587 2.856   1.00 22.27 ? 69  ARG F CG  1 
ATOM   1601 C  CD  . ARG B 1 69  ? -0.047  -21.444 2.757   1.00 25.72 ? 69  ARG F CD  1 
ATOM   1602 N  NE  . ARG B 1 69  ? 0.144   -22.588 1.884   1.00 29.66 ? 69  ARG F NE  1 
ATOM   1603 C  CZ  . ARG B 1 69  ? 0.179   -22.546 0.548   1.00 32.54 ? 69  ARG F CZ  1 
ATOM   1604 N  NH1 . ARG B 1 69  ? 0.071   -21.397 -0.101  1.00 34.51 ? 69  ARG F NH1 1 
ATOM   1605 N  NH2 . ARG B 1 69  ? 0.350   -23.666 -0.131  1.00 32.38 ? 69  ARG F NH2 1 
ATOM   1606 N  N   . LYS B 1 70  ? 4.080   -23.588 4.433   1.00 18.88 ? 70  LYS F N   1 
ATOM   1607 C  CA  . LYS B 1 70  ? 5.437   -24.115 4.654   1.00 19.37 ? 70  LYS F CA  1 
ATOM   1608 C  C   . LYS B 1 70  ? 6.456   -23.224 3.943   1.00 18.10 ? 70  LYS F C   1 
ATOM   1609 O  O   . LYS B 1 70  ? 6.096   -22.422 3.052   1.00 16.89 ? 70  LYS F O   1 
ATOM   1610 C  CB  . LYS B 1 70  ? 5.547   -25.564 4.179   1.00 22.02 ? 70  LYS F CB  1 
ATOM   1611 C  CG  . LYS B 1 70  ? 4.707   -26.557 4.970   1.00 24.79 ? 70  LYS F CG  1 
ATOM   1612 C  CD  . LYS B 1 70  ? 4.988   -27.997 4.599   1.00 28.65 ? 70  LYS F CD  1 
ATOM   1613 C  CE  . LYS B 1 70  ? 4.270   -28.990 5.485   1.00 32.29 ? 70  LYS F CE  1 
ATOM   1614 N  NZ  . LYS B 1 70  ? 2.801   -28.857 5.355   1.00 35.44 ? 70  LYS F NZ  1 
ATOM   1615 N  N   . HIS B 1 71  ? 7.700   -23.368 4.356   1.00 16.15 ? 71  HIS F N   1 
ATOM   1616 C  CA  . HIS B 1 71  ? 8.844   -22.621 3.792   1.00 14.97 ? 71  HIS F CA  1 
ATOM   1617 C  C   . HIS B 1 71  ? 9.077   -23.059 2.350   1.00 15.78 ? 71  HIS F C   1 
ATOM   1618 O  O   . HIS B 1 71  ? 9.051   -24.293 2.071   1.00 16.72 ? 71  HIS F O   1 
ATOM   1619 C  CB  . HIS B 1 71  ? 10.081  -22.854 4.645   1.00 14.39 ? 71  HIS F CB  1 
ATOM   1620 C  CG  . HIS B 1 71  ? 11.234  -22.080 4.121   1.00 14.01 ? 71  HIS F CG  1 
ATOM   1621 N  ND1 . HIS B 1 71  ? 11.333  -20.696 4.244   1.00 13.92 ? 71  HIS F ND1 1 
ATOM   1622 C  CD2 . HIS B 1 71  ? 12.284  -22.484 3.389   1.00 13.97 ? 71  HIS F CD2 1 
ATOM   1623 C  CE1 . HIS B 1 71  ? 12.430  -20.312 3.646   1.00 14.37 ? 71  HIS F CE1 1 
ATOM   1624 N  NE2 . HIS B 1 71  ? 13.012  -21.372 3.089   1.00 14.46 ? 71  HIS F NE2 1 
ATOM   1625 N  N   . GLY B 1 72  ? 9.332   -22.113 1.457   1.00 15.57 ? 72  GLY F N   1 
ATOM   1626 C  CA  . GLY B 1 72  ? 9.743   -22.444 0.090   1.00 15.14 ? 72  GLY F CA  1 
ATOM   1627 C  C   . GLY B 1 72  ? 10.601  -21.359 -0.498  1.00 15.86 ? 72  GLY F C   1 
ATOM   1628 O  O   . GLY B 1 72  ? 11.131  -20.535 0.278   1.00 15.45 ? 72  GLY F O   1 
ATOM   1629 N  N   . GLY B 1 73  ? 10.800  -21.421 -1.810  1.00 15.62 ? 73  GLY F N   1 
ATOM   1630 C  CA  . GLY B 1 73  ? 11.498  -20.379 -2.576  1.00 15.40 ? 73  GLY F CA  1 
ATOM   1631 C  C   . GLY B 1 73  ? 10.490  -19.365 -3.089  1.00 15.53 ? 73  GLY F C   1 
ATOM   1632 O  O   . GLY B 1 73  ? 9.290   -19.609 -3.085  1.00 16.53 ? 73  GLY F O   1 
ATOM   1633 N  N   . PRO B 1 74  ? 10.965  -18.182 -3.525  1.00 15.27 ? 74  PRO F N   1 
ATOM   1634 C  CA  . PRO B 1 74  ? 10.083  -17.110 -3.960  1.00 15.79 ? 74  PRO F CA  1 
ATOM   1635 C  C   . PRO B 1 74  ? 9.239   -17.470 -5.185  1.00 17.09 ? 74  PRO F C   1 
ATOM   1636 O  O   . PRO B 1 74  ? 8.191   -16.890 -5.341  1.00 18.64 ? 74  PRO F O   1 
ATOM   1637 C  CB  . PRO B 1 74  ? 11.053  -15.952 -4.262  1.00 16.42 ? 74  PRO F CB  1 
ATOM   1638 C  CG  . PRO B 1 74  ? 12.384  -16.599 -4.469  1.00 16.18 ? 74  PRO F CG  1 
ATOM   1639 C  CD  . PRO B 1 74  ? 12.389  -17.804 -3.563  1.00 15.15 ? 74  PRO F CD  1 
ATOM   1640 N  N   . LYS B 1 75  ? 9.673   -18.439 -5.983  1.00 19.08 ? 75  LYS F N   1 
ATOM   1641 C  CA  . LYS B 1 75  ? 8.932   -18.832 -7.212  1.00 22.03 ? 75  LYS F CA  1 
ATOM   1642 C  C   . LYS B 1 75  ? 7.971   -19.979 -6.898  1.00 21.05 ? 75  LYS F C   1 
ATOM   1643 O  O   . LYS B 1 75  ? 7.351   -20.495 -7.837  1.00 22.06 ? 75  LYS F O   1 
ATOM   1644 C  CB  . LYS B 1 75  ? 9.922   -19.197 -8.321  1.00 24.90 ? 75  LYS F CB  1 
ATOM   1645 C  CG  . LYS B 1 75  ? 10.889  -18.083 -8.703  1.00 28.56 ? 75  LYS F CG  1 
ATOM   1646 C  CD  . LYS B 1 75  ? 10.219  -16.726 -8.806  1.00 31.94 ? 75  LYS F CD  1 
ATOM   1647 C  CE  . LYS B 1 75  ? 11.121  -15.634 -9.348  1.00 35.09 ? 75  LYS F CE  1 
ATOM   1648 N  NZ  . LYS B 1 75  ? 10.505  -14.293 -9.185  1.00 36.53 ? 75  LYS F NZ  1 
ATOM   1649 N  N   . ASP B 1 76  ? 7.868   -20.412 -5.643  1.00 19.66 ? 76  ASP F N   1 
ATOM   1650 C  CA  . ASP B 1 76  ? 6.947   -21.513 -5.247  1.00 20.59 ? 76  ASP F CA  1 
ATOM   1651 C  C   . ASP B 1 76  ? 5.604   -20.945 -4.805  1.00 20.71 ? 76  ASP F C   1 
ATOM   1652 O  O   . ASP B 1 76  ? 5.576   -19.862 -4.208  1.00 19.95 ? 76  ASP F O   1 
ATOM   1653 C  CB  . ASP B 1 76  ? 7.524   -22.355 -4.112  1.00 20.23 ? 76  ASP F CB  1 
ATOM   1654 C  CG  . ASP B 1 76  ? 8.784   -23.097 -4.488  1.00 21.31 ? 76  ASP F CG  1 
ATOM   1655 O  OD1 . ASP B 1 76  ? 8.914   -23.449 -5.694  1.00 23.63 ? 76  ASP F OD1 1 
ATOM   1656 O  OD2 . ASP B 1 76  ? 9.609   -23.344 -3.576  1.00 21.84 ? 76  ASP F OD2 1 
ATOM   1657 N  N   . GLU B 1 77  ? 4.519   -21.683 -5.025  1.00 21.26 ? 77  GLU F N   1 
ATOM   1658 C  CA  A GLU B 1 77  ? 3.199   -21.342 -4.438  0.50 22.20 ? 77  GLU F CA  1 
ATOM   1659 C  CA  B GLU B 1 77  ? 3.191   -21.372 -4.445  0.50 22.21 ? 77  GLU F CA  1 
ATOM   1660 C  C   . GLU B 1 77  ? 3.266   -21.604 -2.933  1.00 20.38 ? 77  GLU F C   1 
ATOM   1661 O  O   . GLU B 1 77  ? 2.755   -20.759 -2.157  1.00 20.92 ? 77  GLU F O   1 
ATOM   1662 C  CB  A GLU B 1 77  ? 2.049   -22.137 -5.058  0.50 24.01 ? 77  GLU F CB  1 
ATOM   1663 C  CB  B GLU B 1 77  ? 2.135   -22.259 -5.106  0.50 24.07 ? 77  GLU F CB  1 
ATOM   1664 C  CG  A GLU B 1 77  ? 0.737   -21.396 -4.921  0.50 26.63 ? 77  GLU F CG  1 
ATOM   1665 C  CG  B GLU B 1 77  ? 0.720   -21.869 -4.764  0.50 26.51 ? 77  GLU F CG  1 
ATOM   1666 C  CD  A GLU B 1 77  ? -0.402  -22.164 -4.287  0.50 28.62 ? 77  GLU F CD  1 
ATOM   1667 C  CD  B GLU B 1 77  ? 0.152   -22.604 -3.568  0.50 27.71 ? 77  GLU F CD  1 
ATOM   1668 O  OE1 A GLU B 1 77  ? -0.933  -23.066 -4.958  0.50 27.62 ? 77  GLU F OE1 1 
ATOM   1669 O  OE1 B GLU B 1 77  ? 0.675   -23.697 -3.243  0.50 28.37 ? 77  GLU F OE1 1 
ATOM   1670 O  OE2 A GLU B 1 77  ? -0.742  -21.854 -3.118  0.50 32.30 ? 77  GLU F OE2 1 
ATOM   1671 O  OE2 B GLU B 1 77  ? -0.811  -22.085 -2.968  0.50 32.27 ? 77  GLU F OE2 1 
ATOM   1672 N  N   . GLU B 1 78  ? 3.867   -22.731 -2.555  1.00 19.38 ? 78  GLU F N   1 
ATOM   1673 C  CA  A GLU B 1 78  ? 4.051   -23.107 -1.131  0.50 18.63 ? 78  GLU F CA  1 
ATOM   1674 C  CA  B GLU B 1 78  ? 4.058   -23.116 -1.134  0.50 19.15 ? 78  GLU F CA  1 
ATOM   1675 C  C   . GLU B 1 78  ? 5.283   -22.363 -0.607  1.00 17.32 ? 78  GLU F C   1 
ATOM   1676 O  O   . GLU B 1 78  ? 6.400   -22.861 -0.776  1.00 17.57 ? 78  GLU F O   1 
ATOM   1677 C  CB  A GLU B 1 78  ? 4.189   -24.621 -0.983  0.50 19.13 ? 78  GLU F CB  1 
ATOM   1678 C  CB  B GLU B 1 78  ? 4.214   -24.631 -0.985  0.50 20.41 ? 78  GLU F CB  1 
ATOM   1679 C  CG  A GLU B 1 78  ? 4.155   -25.077 0.464   0.50 20.30 ? 78  GLU F CG  1 
ATOM   1680 C  CG  B GLU B 1 78  ? 4.127   -25.096 0.461   0.50 22.37 ? 78  GLU F CG  1 
ATOM   1681 C  CD  A GLU B 1 78  ? 2.756   -25.142 1.038   0.50 21.85 ? 78  GLU F CD  1 
ATOM   1682 C  CD  B GLU B 1 78  ? 4.371   -26.576 0.713   0.50 24.86 ? 78  GLU F CD  1 
ATOM   1683 O  OE1 A GLU B 1 78  ? 1.916   -25.865 0.447   0.50 23.76 ? 78  GLU F OE1 1 
ATOM   1684 O  OE1 B GLU B 1 78  ? 3.508   -27.203 1.361   0.50 28.54 ? 78  GLU F OE1 1 
ATOM   1685 O  OE2 A GLU B 1 78  ? 2.498   -24.485 2.064   0.50 22.25 ? 78  GLU F OE2 1 
ATOM   1686 O  OE2 B GLU B 1 78  ? 5.438   -27.093 0.311   0.50 26.36 ? 78  GLU F OE2 1 
ATOM   1687 N  N   . ARG B 1 79  ? 5.052   -21.199 -0.018  1.00 16.15 ? 79  ARG F N   1 
ATOM   1688 C  CA  . ARG B 1 79  ? 6.128   -20.363 0.561   1.00 14.41 ? 79  ARG F CA  1 
ATOM   1689 C  C   . ARG B 1 79  ? 5.509   -19.502 1.650   1.00 13.81 ? 79  ARG F C   1 
ATOM   1690 O  O   . ARG B 1 79  ? 4.295   -19.255 1.647   1.00 13.72 ? 79  ARG F O   1 
ATOM   1691 C  CB  . ARG B 1 79  ? 6.783   -19.447 -0.479  1.00 14.17 ? 79  ARG F CB  1 
ATOM   1692 C  CG  . ARG B 1 79  ? 5.804   -18.519 -1.183  1.00 14.07 ? 79  ARG F CG  1 
ATOM   1693 C  CD  . ARG B 1 79  ? 6.518   -17.509 -2.068  1.00 14.45 ? 79  ARG F CD  1 
ATOM   1694 N  NE  . ARG B 1 79  ? 6.919   -16.319 -1.325  1.00 14.91 ? 79  ARG F NE  1 
ATOM   1695 C  CZ  . ARG B 1 79  ? 7.342   -15.204 -1.899  1.00 14.99 ? 79  ARG F CZ  1 
ATOM   1696 N  NH1 . ARG B 1 79  ? 7.451   -15.147 -3.212  1.00 14.33 ? 79  ARG F NH1 1 
ATOM   1697 N  NH2 . ARG B 1 79  ? 7.628   -14.141 -1.166  1.00 14.73 ? 79  ARG F NH2 1 
ATOM   1698 N  N   . HIS B 1 80  ? 6.350   -19.030 2.551   1.00 13.43 ? 80  HIS F N   1 
ATOM   1699 C  CA  . HIS B 1 80  ? 6.000   -17.932 3.469   1.00 13.26 ? 80  HIS F CA  1 
ATOM   1700 C  C   . HIS B 1 80  ? 5.980   -16.631 2.671   1.00 12.21 ? 80  HIS F C   1 
ATOM   1701 O  O   . HIS B 1 80  ? 6.759   -16.523 1.731   1.00 12.44 ? 80  HIS F O   1 
ATOM   1702 C  CB  . HIS B 1 80  ? 7.042   -17.844 4.587   1.00 12.64 ? 80  HIS F CB  1 
ATOM   1703 C  CG  . HIS B 1 80  ? 7.187   -19.108 5.365   1.00 13.60 ? 80  HIS F CG  1 
ATOM   1704 N  ND1 . HIS B 1 80  ? 8.400   -19.578 5.826   1.00 13.84 ? 80  HIS F ND1 1 
ATOM   1705 C  CD2 . HIS B 1 80  ? 6.251   -19.985 5.791   1.00 14.91 ? 80  HIS F CD2 1 
ATOM   1706 C  CE1 . HIS B 1 80  ? 8.191   -20.674 6.533   1.00 14.63 ? 80  HIS F CE1 1 
ATOM   1707 N  NE2 . HIS B 1 80  ? 6.893   -20.943 6.512   1.00 15.48 ? 80  HIS F NE2 1 
ATOM   1708 N  N   . VAL B 1 81  ? 5.204   -15.645 3.083   1.00 12.32 ? 81  VAL F N   1 
ATOM   1709 C  CA  . VAL B 1 81  ? 5.284   -14.311 2.437   1.00 12.44 ? 81  VAL F CA  1 
ATOM   1710 C  C   . VAL B 1 81  ? 6.729   -13.814 2.505   1.00 12.72 ? 81  VAL F C   1 
ATOM   1711 O  O   . VAL B 1 81  ? 7.180   -13.221 1.526   1.00 12.77 ? 81  VAL F O   1 
ATOM   1712 C  CB  . VAL B 1 81  ? 4.281   -13.309 3.038   1.00 13.54 ? 81  VAL F CB  1 
ATOM   1713 C  CG1 . VAL B 1 81  ? 4.579   -11.886 2.582   1.00 13.01 ? 81  VAL F CG1 1 
ATOM   1714 C  CG2 . VAL B 1 81  ? 2.862   -13.697 2.655   1.00 14.41 ? 81  VAL F CG2 1 
ATOM   1715 N  N   . GLY B 1 82  ? 7.426   -14.034 3.613   1.00 13.22 ? 82  GLY F N   1 
ATOM   1716 C  CA  . GLY B 1 82  ? 8.788   -13.497 3.787   1.00 12.78 ? 82  GLY F CA  1 
ATOM   1717 C  C   . GLY B 1 82  ? 9.864   -14.259 3.027   1.00 13.23 ? 82  GLY F C   1 
ATOM   1718 O  O   . GLY B 1 82  ? 11.054  -13.920 3.197   1.00 12.77 ? 82  GLY F O   1 
ATOM   1719 N  N   . ASP B 1 83  ? 9.537   -15.270 2.230   1.00 12.89 ? 83  ASP F N   1 
ATOM   1720 C  CA  . ASP B 1 83  ? 10.557  -16.133 1.580   1.00 13.33 ? 83  ASP F CA  1 
ATOM   1721 C  C   . ASP B 1 83  ? 11.074  -15.503 0.287   1.00 13.68 ? 83  ASP F C   1 
ATOM   1722 O  O   . ASP B 1 83  ? 10.486  -15.750 -0.779  1.00 15.56 ? 83  ASP F O   1 
ATOM   1723 C  CB  . ASP B 1 83  ? 9.986   -17.526 1.316   1.00 13.17 ? 83  ASP F CB  1 
ATOM   1724 C  CG  . ASP B 1 83  ? 9.795   -18.321 2.591   1.00 12.72 ? 83  ASP F CG  1 
ATOM   1725 O  OD1 . ASP B 1 83  ? 10.355  -17.914 3.644   1.00 12.60 ? 83  ASP F OD1 1 
ATOM   1726 O  OD2 . ASP B 1 83  ? 9.080   -19.343 2.545   1.00 13.03 ? 83  ASP F OD2 1 
ATOM   1727 N  N   . LEU B 1 84  ? 12.160  -14.743 0.378   1.00 13.37 ? 84  LEU F N   1 
ATOM   1728 C  CA  . LEU B 1 84  ? 12.765  -14.066 -0.792  1.00 13.81 ? 84  LEU F CA  1 
ATOM   1729 C  C   . LEU B 1 84  ? 13.985  -14.837 -1.298  1.00 14.02 ? 84  LEU F C   1 
ATOM   1730 O  O   . LEU B 1 84  ? 14.729  -14.270 -2.120  1.00 16.57 ? 84  LEU F O   1 
ATOM   1731 C  CB  . LEU B 1 84  ? 13.120  -12.627 -0.432  1.00 13.91 ? 84  LEU F CB  1 
ATOM   1732 C  CG  . LEU B 1 84  ? 11.919  -11.743 -0.124  1.00 15.25 ? 84  LEU F CG  1 
ATOM   1733 C  CD1 . LEU B 1 84  ? 12.393  -10.346 0.241   1.00 15.32 ? 84  LEU F CD1 1 
ATOM   1734 C  CD2 . LEU B 1 84  ? 10.960  -11.692 -1.295  1.00 16.64 ? 84  LEU F CD2 1 
ATOM   1735 N  N   . GLY B 1 85  ? 14.190  -16.067 -0.848  1.00 13.58 ? 85  GLY F N   1 
ATOM   1736 C  CA  . GLY B 1 85  ? 15.177  -16.967 -1.460  1.00 14.18 ? 85  GLY F CA  1 
ATOM   1737 C  C   . GLY B 1 85  ? 16.572  -16.659 -0.970  1.00 14.04 ? 85  GLY F C   1 
ATOM   1738 O  O   . GLY B 1 85  ? 16.788  -16.652 0.253   1.00 14.27 ? 85  GLY F O   1 
ATOM   1739 N  N   . ASN B 1 86  ? 17.495  -16.459 -1.907  1.00 14.35 ? 86  ASN F N   1 
ATOM   1740 C  CA  . ASN B 1 86  ? 18.915  -16.187 -1.597  1.00 14.62 ? 86  ASN F CA  1 
ATOM   1741 C  C   . ASN B 1 86  ? 19.401  -14.957 -2.341  1.00 14.63 ? 86  ASN F C   1 
ATOM   1742 O  O   . ASN B 1 86  ? 18.953  -14.696 -3.457  1.00 16.68 ? 86  ASN F O   1 
ATOM   1743 C  CB  . ASN B 1 86  ? 19.801  -17.367 -1.979  1.00 14.64 ? 86  ASN F CB  1 
ATOM   1744 C  CG  . ASN B 1 86  ? 19.517  -18.579 -1.126  1.00 15.24 ? 86  ASN F CG  1 
ATOM   1745 O  OD1 . ASN B 1 86  ? 19.926  -18.649 0.026   1.00 14.83 ? 86  ASN F OD1 1 
ATOM   1746 N  ND2 . ASN B 1 86  ? 18.823  -19.555 -1.689  1.00 17.39 ? 86  ASN F ND2 1 
ATOM   1747 N  N   . VAL B 1 87  ? 20.366  -14.288 -1.727  1.00 14.50 ? 87  VAL F N   1 
ATOM   1748 C  CA  . VAL B 1 87  ? 21.262  -13.342 -2.432  1.00 15.01 ? 87  VAL F CA  1 
ATOM   1749 C  C   . VAL B 1 87  ? 22.591  -14.062 -2.650  1.00 15.39 ? 87  VAL F C   1 
ATOM   1750 O  O   . VAL B 1 87  ? 22.912  -14.997 -1.892  1.00 14.40 ? 87  VAL F O   1 
ATOM   1751 C  CB  . VAL B 1 87  ? 21.415  -12.036 -1.638  1.00 16.01 ? 87  VAL F CB  1 
ATOM   1752 C  CG1 . VAL B 1 87  ? 20.086  -11.307 -1.569  1.00 17.57 ? 87  VAL F CG1 1 
ATOM   1753 C  CG2 . VAL B 1 87  ? 21.978  -12.263 -0.253  1.00 17.42 ? 87  VAL F CG2 1 
ATOM   1754 N  N   . THR B 1 88  ? 23.332  -13.634 -3.657  1.00 16.16 ? 88  THR F N   1 
ATOM   1755 C  CA  . THR B 1 88  ? 24.586  -14.296 -4.085  1.00 18.09 ? 88  THR F CA  1 
ATOM   1756 C  C   . THR B 1 88  ? 25.731  -13.310 -3.933  1.00 17.63 ? 88  THR F C   1 
ATOM   1757 O  O   . THR B 1 88  ? 25.685  -12.226 -4.533  1.00 17.21 ? 88  THR F O   1 
ATOM   1758 C  CB  . THR B 1 88  ? 24.516  -14.801 -5.524  1.00 19.23 ? 88  THR F CB  1 
ATOM   1759 O  OG1 . THR B 1 88  ? 23.454  -15.750 -5.600  1.00 21.29 ? 88  THR F OG1 1 
ATOM   1760 C  CG2 . THR B 1 88  ? 25.830  -15.415 -5.963  1.00 20.87 ? 88  THR F CG2 1 
ATOM   1761 N  N   . ALA B 1 89  ? 26.735  -13.698 -3.168  1.00 17.48 ? 89  ALA F N   1 
ATOM   1762 C  CA  . ALA B 1 89  ? 27.988  -12.938 -3.024  1.00 18.82 ? 89  ALA F CA  1 
ATOM   1763 C  C   . ALA B 1 89  ? 29.026  -13.610 -3.925  1.00 19.47 ? 89  ALA F C   1 
ATOM   1764 O  O   . ALA B 1 89  ? 29.066  -14.864 -3.978  1.00 18.96 ? 89  ALA F O   1 
ATOM   1765 C  CB  . ALA B 1 89  ? 28.432  -12.909 -1.589  1.00 19.44 ? 89  ALA F CB  1 
ATOM   1766 N  N   . ASP B 1 90  ? 29.840  -12.798 -4.584  1.00 21.79 ? 90  ASP F N   1 
ATOM   1767 C  CA  . ASP B 1 90  ? 31.002  -13.282 -5.371  1.00 24.57 ? 90  ASP F CA  1 
ATOM   1768 C  C   . ASP B 1 90  ? 32.233  -13.298 -4.457  1.00 23.35 ? 90  ASP F C   1 
ATOM   1769 O  O   . ASP B 1 90  ? 32.105  -13.054 -3.246  1.00 21.43 ? 90  ASP F O   1 
ATOM   1770 C  CB  . ASP B 1 90  ? 31.140  -12.436 -6.639  1.00 28.91 ? 90  ASP F CB  1 
ATOM   1771 C  CG  . ASP B 1 90  ? 30.135  -12.805 -7.720  1.00 33.07 ? 90  ASP F CG  1 
ATOM   1772 O  OD1 . ASP B 1 90  ? 29.215  -13.605 -7.429  1.00 33.71 ? 90  ASP F OD1 1 
ATOM   1773 O  OD2 . ASP B 1 90  ? 30.285  -12.299 -8.856  1.00 36.76 ? 90  ASP F OD2 1 
ATOM   1774 N  N   . LYS B 1 91  ? 33.404  -13.575 -5.018  1.00 22.86 ? 91  LYS F N   1 
ATOM   1775 C  CA  . LYS B 1 91  ? 34.670  -13.634 -4.236  1.00 23.84 ? 91  LYS F CA  1 
ATOM   1776 C  C   . LYS B 1 91  ? 34.981  -12.273 -3.596  1.00 24.33 ? 91  LYS F C   1 
ATOM   1777 O  O   . LYS B 1 91  ? 35.678  -12.279 -2.571  1.00 26.26 ? 91  LYS F O   1 
ATOM   1778 C  CB  . LYS B 1 91  ? 35.822  -14.100 -5.126  1.00 24.47 ? 91  LYS F CB  1 
ATOM   1779 C  CG  . LYS B 1 91  ? 35.949  -15.611 -5.261  1.00 26.38 ? 91  LYS F CG  1 
ATOM   1780 C  CD  . LYS B 1 91  ? 36.183  -16.318 -3.950  1.00 28.02 ? 91  LYS F CD  1 
ATOM   1781 C  CE  . LYS B 1 91  ? 37.111  -17.509 -4.080  1.00 28.95 ? 91  LYS F CE  1 
ATOM   1782 N  NZ  . LYS B 1 91  ? 36.568  -18.501 -5.034  1.00 28.07 ? 91  LYS F NZ  1 
ATOM   1783 N  N   . ASP B 1 92  ? 34.464  -11.183 -4.171  1.00 24.43 ? 92  ASP F N   1 
ATOM   1784 C  CA  . ASP B 1 92  ? 34.621  -9.784  -3.691  1.00 26.02 ? 92  ASP F CA  1 
ATOM   1785 C  C   . ASP B 1 92  ? 33.845  -9.540  -2.388  1.00 25.27 ? 92  ASP F C   1 
ATOM   1786 O  O   . ASP B 1 92  ? 33.941  -8.408  -1.874  1.00 24.59 ? 92  ASP F O   1 
ATOM   1787 C  CB  . ASP B 1 92  ? 34.153  -8.794  -4.765  1.00 28.69 ? 92  ASP F CB  1 
ATOM   1788 C  CG  . ASP B 1 92  ? 32.724  -8.995  -5.252  1.00 30.51 ? 92  ASP F CG  1 
ATOM   1789 O  OD1 . ASP B 1 92  ? 32.028  -9.899  -4.727  1.00 29.28 ? 92  ASP F OD1 1 
ATOM   1790 O  OD2 . ASP B 1 92  ? 32.326  -8.296  -6.215  1.00 35.52 ? 92  ASP F OD2 1 
ATOM   1791 N  N   . ALA B 1 93  ? 33.078  -10.524 -1.904  1.00 21.79 ? 93  ALA F N   1 
ATOM   1792 C  CA  . ALA B 1 93  ? 32.304  -10.486 -0.636  1.00 21.42 ? 93  ALA F CA  1 
ATOM   1793 C  C   . ALA B 1 93  ? 31.084  -9.567  -0.768  1.00 20.78 ? 93  ALA F C   1 
ATOM   1794 O  O   . ALA B 1 93  ? 30.471  -9.215  0.274   1.00 19.96 ? 93  ALA F O   1 
ATOM   1795 C  CB  . ALA B 1 93  ? 33.167  -10.066 0.536   1.00 22.06 ? 93  ALA F CB  1 
ATOM   1796 N  N   . VAL B 1 94  ? 30.704  -9.227  -1.990  1.00 20.47 ? 94  VAL F N   1 
ATOM   1797 C  CA  . VAL B 1 94  ? 29.568  -8.303  -2.263  1.00 20.48 ? 94  VAL F CA  1 
ATOM   1798 C  C   . VAL B 1 94  ? 28.451  -9.078  -2.968  1.00 20.29 ? 94  VAL F C   1 
ATOM   1799 O  O   . VAL B 1 94  ? 28.738  -9.811  -3.944  1.00 21.38 ? 94  VAL F O   1 
ATOM   1800 C  CB  . VAL B 1 94  ? 30.028  -7.089  -3.086  1.00 21.06 ? 94  VAL F CB  1 
ATOM   1801 C  CG1 . VAL B 1 94  ? 28.873  -6.145  -3.361  1.00 21.89 ? 94  VAL F CG1 1 
ATOM   1802 C  CG2 . VAL B 1 94  ? 31.177  -6.353  -2.407  1.00 19.89 ? 94  VAL F CG2 1 
ATOM   1803 N  N   . ALA B 1 95  ? 27.221  -8.927  -2.471  1.00 19.88 ? 95  ALA F N   1 
ATOM   1804 C  CA  . ALA B 1 95  ? 25.978  -9.324  -3.158  1.00 19.14 ? 95  ALA F CA  1 
ATOM   1805 C  C   . ALA B 1 95  ? 25.315  -8.070  -3.747  1.00 19.33 ? 95  ALA F C   1 
ATOM   1806 O  O   . ALA B 1 95  ? 24.995  -7.117  -2.992  1.00 17.50 ? 95  ALA F O   1 
ATOM   1807 C  CB  . ALA B 1 95  ? 25.075  -10.052 -2.200  1.00 18.79 ? 95  ALA F CB  1 
ATOM   1808 N  N   . ASP B 1 96  ? 25.149  -8.035  -5.068  1.00 19.59 ? 96  ASP F N   1 
ATOM   1809 C  CA  . ASP B 1 96  ? 24.308  -7.031  -5.770  1.00 20.28 ? 96  ASP F CA  1 
ATOM   1810 C  C   . ASP B 1 96  ? 22.905  -7.629  -5.828  1.00 20.04 ? 96  ASP F C   1 
ATOM   1811 O  O   . ASP B 1 96  ? 22.755  -8.707  -6.413  1.00 22.03 ? 96  ASP F O   1 
ATOM   1812 C  CB  . ASP B 1 96  ? 24.886  -6.701  -7.148  1.00 21.85 ? 96  ASP F CB  1 
ATOM   1813 C  CG  . ASP B 1 96  ? 26.151  -5.858  -7.070  0.70 23.47 ? 96  ASP F CG  1 
ATOM   1814 O  OD1 . ASP B 1 96  ? 26.192  -4.929  -6.230  0.60 23.08 ? 96  ASP F OD1 1 
ATOM   1815 O  OD2 . ASP B 1 96  ? 27.094  -6.142  -7.841  0.60 27.26 ? 96  ASP F OD2 1 
ATOM   1816 N  N   . VAL B 1 97  ? 21.932  -7.004  -5.176  1.00 16.80 ? 97  VAL F N   1 
ATOM   1817 C  CA  . VAL B 1 97  ? 20.581  -7.593  -4.990  1.00 16.87 ? 97  VAL F CA  1 
ATOM   1818 C  C   . VAL B 1 97  ? 19.671  -6.979  -6.036  1.00 16.34 ? 97  VAL F C   1 
ATOM   1819 O  O   . VAL B 1 97  ? 19.641  -5.749  -6.165  1.00 15.99 ? 97  VAL F O   1 
ATOM   1820 C  CB  . VAL B 1 97  ? 20.062  -7.354  -3.567  1.00 16.81 ? 97  VAL F CB  1 
ATOM   1821 C  CG1 . VAL B 1 97  ? 18.661  -7.918  -3.381  1.00 17.31 ? 97  VAL F CG1 1 
ATOM   1822 C  CG2 . VAL B 1 97  ? 21.028  -7.928  -2.535  1.00 17.53 ? 97  VAL F CG2 1 
ATOM   1823 N  N   . SER B 1 98  ? 18.981  -7.835  -6.769  1.00 17.52 ? 98  SER F N   1 
ATOM   1824 C  CA  . SER B 1 98  ? 17.992  -7.427  -7.782  1.00 19.02 ? 98  SER F CA  1 
ATOM   1825 C  C   . SER B 1 98  ? 16.923  -8.511  -7.824  1.00 19.37 ? 98  SER F C   1 
ATOM   1826 O  O   . SER B 1 98  ? 17.187  -9.621  -8.336  1.00 21.85 ? 98  SER F O   1 
ATOM   1827 C  CB  . SER B 1 98  ? 18.636  -7.175  -9.120  1.00 21.48 ? 98  SER F CB  1 
ATOM   1828 O  OG  . SER B 1 98  ? 17.714  -6.514  -9.982  1.00 24.71 ? 98  SER F OG  1 
ATOM   1829 N  N   . ILE B 1 99  ? 15.770  -8.220  -7.240  1.00 18.63 ? 99  ILE F N   1 
ATOM   1830 C  CA  . ILE B 1 99  ? 14.655  -9.191  -7.065  1.00 18.29 ? 99  ILE F CA  1 
ATOM   1831 C  C   . ILE B 1 99  ? 13.376  -8.490  -7.518  1.00 18.17 ? 99  ILE F C   1 
ATOM   1832 O  O   . ILE B 1 99  ? 13.263  -7.262  -7.322  1.00 17.49 ? 99  ILE F O   1 
ATOM   1833 C  CB  . ILE B 1 99  ? 14.611  -9.657  -5.587  1.00 18.89 ? 99  ILE F CB  1 
ATOM   1834 C  CG1 . ILE B 1 99  ? 15.785  -10.582 -5.249  1.00 20.26 ? 99  ILE F CG1 1 
ATOM   1835 C  CG2 . ILE B 1 99  ? 13.267  -10.279 -5.226  1.00 19.81 ? 99  ILE F CG2 1 
ATOM   1836 C  CD1 . ILE B 1 99  ? 15.879  -10.950 -3.787  1.00 22.61 ? 99  ILE F CD1 1 
ATOM   1837 N  N   . GLU B 1 100 ? 12.467  -9.215  -8.164  1.00 17.40 ? 100 GLU F N   1 
ATOM   1838 C  CA  . GLU B 1 100 ? 11.056  -8.781  -8.299  1.00 17.64 ? 100 GLU F CA  1 
ATOM   1839 C  C   . GLU B 1 100 ? 10.199  -9.848  -7.625  1.00 15.74 ? 100 GLU F C   1 
ATOM   1840 O  O   . GLU B 1 100 ? 10.419  -11.027 -7.873  1.00 17.00 ? 100 GLU F O   1 
ATOM   1841 C  CB  . GLU B 1 100 ? 10.672  -8.567  -9.763  1.00 20.95 ? 100 GLU F CB  1 
ATOM   1842 C  CG  . GLU B 1 100 ? 9.404   -7.753  -9.926  1.00 26.15 ? 100 GLU F CG  1 
ATOM   1843 C  CD  . GLU B 1 100 ? 9.161   -7.178  -11.314 1.00 28.76 ? 100 GLU F CD  1 
ATOM   1844 O  OE1 . GLU B 1 100 ? 9.467   -7.859  -12.312 0.70 33.90 ? 100 GLU F OE1 1 
ATOM   1845 O  OE2 . GLU B 1 100 ? 8.629   -6.049  -11.391 0.70 33.47 ? 100 GLU F OE2 1 
ATOM   1846 N  N   . ASP B 1 101 ? 9.295   -9.438  -6.745  1.00 14.77 ? 101 ASP F N   1 
ATOM   1847 C  CA  . ASP B 1 101 ? 8.445   -10.413 -6.021  1.00 15.08 ? 101 ASP F CA  1 
ATOM   1848 C  C   . ASP B 1 101 ? 6.994   -9.959  -6.052  1.00 15.53 ? 101 ASP F C   1 
ATOM   1849 O  O   . ASP B 1 101 ? 6.720   -8.776  -5.842  1.00 15.52 ? 101 ASP F O   1 
ATOM   1850 C  CB  . ASP B 1 101 ? 8.936   -10.620 -4.593  1.00 14.84 ? 101 ASP F CB  1 
ATOM   1851 C  CG  . ASP B 1 101 ? 8.340   -11.875 -3.976  1.00 15.33 ? 101 ASP F CG  1 
ATOM   1852 O  OD1 . ASP B 1 101 ? 8.780   -12.969 -4.372  1.00 16.77 ? 101 ASP F OD1 1 
ATOM   1853 O  OD2 . ASP B 1 101 ? 7.415   -11.750 -3.152  1.00 15.36 ? 101 ASP F OD2 1 
ATOM   1854 N  N   . SER B 1 102 ? 6.076   -10.904 -6.277  1.00 16.95 ? 102 SER F N   1 
ATOM   1855 C  CA  . SER B 1 102 ? 4.624   -10.631 -6.397  1.00 18.49 ? 102 SER F CA  1 
ATOM   1856 C  C   . SER B 1 102 ? 3.873   -10.987 -5.108  1.00 17.46 ? 102 SER F C   1 
ATOM   1857 O  O   . SER B 1 102 ? 2.663   -10.756 -5.064  1.00 18.09 ? 102 SER F O   1 
ATOM   1858 C  CB  . SER B 1 102 ? 4.073   -11.379 -7.582  1.00 21.28 ? 102 SER F CB  1 
ATOM   1859 O  OG  . SER B 1 102 ? 4.824   -11.073 -8.755  1.00 24.41 ? 102 SER F OG  1 
ATOM   1860 N  N   . VAL B 1 103 ? 4.544   -11.528 -4.090  1.00 15.58 ? 103 VAL F N   1 
ATOM   1861 C  CA  . VAL B 1 103 ? 3.857   -12.013 -2.859  1.00 15.80 ? 103 VAL F CA  1 
ATOM   1862 C  C   . VAL B 1 103 ? 4.031   -11.003 -1.722  1.00 14.59 ? 103 VAL F C   1 
ATOM   1863 O  O   . VAL B 1 103 ? 3.046   -10.715 -1.045  1.00 16.61 ? 103 VAL F O   1 
ATOM   1864 C  CB  . VAL B 1 103 ? 4.366   -13.406 -2.471  1.00 15.76 ? 103 VAL F CB  1 
ATOM   1865 C  CG1 . VAL B 1 103 ? 3.844   -13.851 -1.114  1.00 15.74 ? 103 VAL F CG1 1 
ATOM   1866 C  CG2 . VAL B 1 103 ? 3.981   -14.413 -3.541  1.00 15.71 ? 103 VAL F CG2 1 
ATOM   1867 N  N   . ILE B 1 104 ? 5.234   -10.487 -1.512  1.00 14.46 ? 104 ILE F N   1 
ATOM   1868 C  CA  . ILE B 1 104 ? 5.420   -9.355  -0.563  1.00 13.90 ? 104 ILE F CA  1 
ATOM   1869 C  C   . ILE B 1 104 ? 4.640   -8.156  -1.098  1.00 14.33 ? 104 ILE F C   1 
ATOM   1870 O  O   . ILE B 1 104 ? 4.374   -8.072  -2.317  1.00 16.09 ? 104 ILE F O   1 
ATOM   1871 C  CB  . ILE B 1 104 ? 6.902   -9.015  -0.314  1.00 13.88 ? 104 ILE F CB  1 
ATOM   1872 C  CG1 . ILE B 1 104 ? 7.622   -8.608  -1.605  1.00 13.43 ? 104 ILE F CG1 1 
ATOM   1873 C  CG2 . ILE B 1 104 ? 7.576   -10.158 0.434   1.00 13.93 ? 104 ILE F CG2 1 
ATOM   1874 C  CD1 . ILE B 1 104 ? 8.968   -7.948  -1.377  1.00 13.97 ? 104 ILE F CD1 1 
ATOM   1875 N  N   . SER B 1 105 ? 4.308   -7.241  -0.199  1.00 13.92 ? 105 SER F N   1 
ATOM   1876 C  CA  . SER B 1 105 ? 3.662   -5.969  -0.576  1.00 14.38 ? 105 SER F CA  1 
ATOM   1877 C  C   . SER B 1 105 ? 4.145   -4.868  0.349   1.00 14.52 ? 105 SER F C   1 
ATOM   1878 O  O   . SER B 1 105 ? 4.604   -5.177  1.456   1.00 14.47 ? 105 SER F O   1 
ATOM   1879 C  CB  . SER B 1 105 ? 2.169   -6.070  -0.518  1.00 16.25 ? 105 SER F CB  1 
ATOM   1880 O  OG  . SER B 1 105 ? 1.589   -4.940  -1.140  1.00 17.17 ? 105 SER F OG  1 
ATOM   1881 N  N   A LEU B 1 106 ? 4.029   -3.633  -0.114  1.00 15.28 ? 106 LEU F N   1 
ATOM   1882 C  CA  A LEU B 1 106 ? 4.280   -2.449  0.746   1.00 16.15 ? 106 LEU F CA  1 
ATOM   1883 C  C   A LEU B 1 106 ? 2.967   -1.767  1.114   1.00 17.88 ? 106 LEU F C   1 
ATOM   1884 O  O   A LEU B 1 106 ? 3.010   -0.828  1.901   1.00 20.54 ? 106 LEU F O   1 
ATOM   1885 C  CB  A LEU B 1 106 ? 5.185   -1.454  0.030   1.00 15.33 ? 106 LEU F CB  1 
ATOM   1886 C  CG  A LEU B 1 106 ? 6.498   -1.994  -0.504  1.00 14.64 ? 106 LEU F CG  1 
ATOM   1887 C  CD1 A LEU B 1 106 ? 7.257   -0.843  -1.165  1.00 14.59 ? 106 LEU F CD1 1 
ATOM   1888 C  CD2 A LEU B 1 106 ? 7.326   -2.649  0.600   1.00 15.56 ? 106 LEU F CD2 1 
ATOM   1889 N  N   . SER B 1 107 ? 1.842   -2.217  0.575   1.00 21.40 ? 107 SER F N   1 
ATOM   1890 C  CA  A SER B 1 107 ? 0.512   -1.635  0.903   0.50 23.08 ? 107 SER F CA  1 
ATOM   1891 C  CA  B SER B 1 107 ? 0.517   -1.637  0.908   0.50 24.89 ? 107 SER F CA  1 
ATOM   1892 C  C   . SER B 1 107 ? -0.580  -2.686  0.730   1.00 25.90 ? 107 SER F C   1 
ATOM   1893 O  O   . SER B 1 107 ? -0.300  -3.745  0.140   1.00 27.82 ? 107 SER F O   1 
ATOM   1894 C  CB  A SER B 1 107 ? 0.215   -0.394  0.087   0.50 23.82 ? 107 SER F CB  1 
ATOM   1895 C  CB  B SER B 1 107 ? 0.241   -0.409  0.081   0.50 26.31 ? 107 SER F CB  1 
ATOM   1896 O  OG  A SER B 1 107 ? 0.147   -0.695  -1.294  0.50 23.20 ? 107 SER F OG  1 
ATOM   1897 O  OG  B SER B 1 107 ? -1.027  0.137   0.408   0.50 28.58 ? 107 SER F OG  1 
ATOM   1898 N  N   . GLY B 1 108 ? -1.771  -2.372  1.233   1.00 28.34 ? 108 GLY F N   1 
ATOM   1899 C  CA  . GLY B 1 108 ? -2.948  -3.247  1.142   1.00 29.34 ? 108 GLY F CA  1 
ATOM   1900 C  C   . GLY B 1 108 ? -2.880  -4.302  2.219   1.00 30.00 ? 108 GLY F C   1 
ATOM   1901 O  O   . GLY B 1 108 ? -3.339  -4.017  3.330   1.00 32.94 ? 108 GLY F O   1 
ATOM   1902 N  N   . ASP B 1 109 ? -2.298  -5.458  1.893   1.00 29.28 ? 109 ASP F N   1 
ATOM   1903 C  CA  . ASP B 1 109 ? -2.263  -6.669  2.749   1.00 30.50 ? 109 ASP F CA  1 
ATOM   1904 C  C   . ASP B 1 109 ? -0.894  -7.332  2.575   1.00 28.01 ? 109 ASP F C   1 
ATOM   1905 O  O   . ASP B 1 109 ? -0.207  -7.028  1.586   1.00 26.90 ? 109 ASP F O   1 
ATOM   1906 C  CB  . ASP B 1 109 ? -3.424  -7.608  2.388   1.00 34.52 ? 109 ASP F CB  1 
ATOM   1907 C  CG  . ASP B 1 109 ? -4.789  -7.025  2.739   1.00 36.95 ? 109 ASP F CG  1 
ATOM   1908 O  OD1 . ASP B 1 109 ? -4.891  -6.436  3.828   1.00 42.75 ? 109 ASP F OD1 1 
ATOM   1909 O  OD2 . ASP B 1 109 ? -5.725  -7.130  1.915   1.00 42.16 ? 109 ASP F OD2 1 
ATOM   1910 N  N   . HIS B 1 110 ? -0.494  -8.180  3.518   1.00 26.48 ? 110 HIS F N   1 
ATOM   1911 C  CA  . HIS B 1 110 ? 0.799   -8.913  3.461   1.00 26.80 ? 110 HIS F CA  1 
ATOM   1912 C  C   . HIS B 1 110 ? 1.956   -7.913  3.431   1.00 20.50 ? 110 HIS F C   1 
ATOM   1913 O  O   . HIS B 1 110 ? 2.947   -8.108  2.708   1.00 20.87 ? 110 HIS F O   1 
ATOM   1914 C  CB  . HIS B 1 110 ? 0.860   -9.849  2.245   1.00 32.51 ? 110 HIS F CB  1 
ATOM   1915 C  CG  . HIS B 1 110 ? -0.251  -10.840 2.161   1.00 37.62 ? 110 HIS F CG  1 
ATOM   1916 N  ND1 . HIS B 1 110 ? -0.249  -11.847 1.220   1.00 39.75 ? 110 HIS F ND1 1 
ATOM   1917 C  CD2 . HIS B 1 110 ? -1.385  -10.989 2.885   1.00 40.36 ? 110 HIS F CD2 1 
ATOM   1918 C  CE1 . HIS B 1 110 ? -1.342  -12.567 1.356   1.00 42.50 ? 110 HIS F CE1 1 
ATOM   1919 N  NE2 . HIS B 1 110 ? -2.057  -12.065 2.376   1.00 41.63 ? 110 HIS F NE2 1 
ATOM   1920 N  N   . CYS B 1 111 ? 1.889   -6.869  4.271   1.00 18.05 ? 111 CYS F N   1 
ATOM   1921 C  CA  A CYS B 1 111 ? 2.760   -5.725  4.064   0.50 16.58 ? 111 CYS F CA  1 
ATOM   1922 C  CA  B CYS B 1 111 ? 2.707   -5.678  4.102   0.50 17.05 ? 111 CYS F CA  1 
ATOM   1923 C  C   . CYS B 1 111 ? 3.945   -5.986  4.949   1.00 14.74 ? 111 CYS F C   1 
ATOM   1924 O  O   . CYS B 1 111 ? 3.820   -6.511  6.044   1.00 15.10 ? 111 CYS F O   1 
ATOM   1925 C  CB  A CYS B 1 111 ? 2.203   -4.382  4.452   0.50 16.73 ? 111 CYS F CB  1 
ATOM   1926 C  CB  B CYS B 1 111 ? 2.040   -4.379  4.565   0.50 17.68 ? 111 CYS F CB  1 
ATOM   1927 S  SG  A CYS B 1 111 ? 0.770   -3.882  3.486   0.50 17.10 ? 111 CYS F SG  1 
ATOM   1928 S  SG  B CYS B 1 111 ? 3.027   -2.839  4.461   0.50 20.07 ? 111 CYS F SG  1 
ATOM   1929 N  N   . ILE B 1 112 ? 5.123   -5.635  4.423   1.00 12.85 ? 112 ILE F N   1 
ATOM   1930 C  CA  . ILE B 1 112 ? 6.366   -5.943  5.104   1.00 12.27 ? 112 ILE F CA  1 
ATOM   1931 C  C   . ILE B 1 112 ? 6.923   -4.712  5.811   1.00 11.36 ? 112 ILE F C   1 
ATOM   1932 O  O   . ILE B 1 112 ? 7.961   -4.856  6.446   1.00 11.66 ? 112 ILE F O   1 
ATOM   1933 C  CB  . ILE B 1 112 ? 7.401   -6.552  4.142   1.00 12.27 ? 112 ILE F CB  1 
ATOM   1934 C  CG1 . ILE B 1 112 ? 7.821   -5.594  3.019   1.00 12.12 ? 112 ILE F CG1 1 
ATOM   1935 C  CG2 . ILE B 1 112 ? 6.875   -7.880  3.606   1.00 12.03 ? 112 ILE F CG2 1 
ATOM   1936 C  CD1 . ILE B 1 112 ? 8.954   -6.096  2.135   1.00 12.59 ? 112 ILE F CD1 1 
ATOM   1937 N  N   A ILE B 1 113 ? 6.275   -3.554  5.676   1.00 11.71 ? 113 ILE F N   1 
ATOM   1938 C  CA  A ILE B 1 113 ? 6.691   -2.329  6.414   1.00 13.00 ? 113 ILE F CA  1 
ATOM   1939 C  C   A ILE B 1 113 ? 6.635   -2.657  7.904   1.00 12.64 ? 113 ILE F C   1 
ATOM   1940 O  O   A ILE B 1 113 ? 5.635   -3.222  8.363   1.00 12.23 ? 113 ILE F O   1 
ATOM   1941 C  CB  A ILE B 1 113 ? 5.761   -1.145  6.082   1.00 14.27 ? 113 ILE F CB  1 
ATOM   1942 C  CG1 A ILE B 1 113 ? 5.723   -0.818  4.593   1.00 17.77 ? 113 ILE F CG1 1 
ATOM   1943 C  CG2 A ILE B 1 113 ? 6.111   0.078   6.927   1.00 14.11 ? 113 ILE F CG2 1 
ATOM   1944 C  CD1 A ILE B 1 113 ? 7.053   -0.591  4.008   1.00 17.78 ? 113 ILE F CD1 1 
ATOM   1945 N  N   . GLY B 1 114 ? 7.682   -2.309  8.651   1.00 11.87 ? 114 GLY F N   1 
ATOM   1946 C  CA  . GLY B 1 114 ? 7.731   -2.520  10.109  1.00 11.85 ? 114 GLY F CA  1 
ATOM   1947 C  C   . GLY B 1 114 ? 8.140   -3.927  10.469  1.00 11.75 ? 114 GLY F C   1 
ATOM   1948 O  O   . GLY B 1 114 ? 8.183   -4.234  11.645  1.00 12.28 ? 114 GLY F O   1 
ATOM   1949 N  N   . ARG B 1 115 ? 8.493   -4.750  9.490   1.00 11.22 ? 115 ARG F N   1 
ATOM   1950 C  CA  . ARG B 1 115 ? 9.025   -6.117  9.730   1.00 11.70 ? 115 ARG F CA  1 
ATOM   1951 C  C   . ARG B 1 115 ? 10.523  -6.075  9.515   1.00 12.16 ? 115 ARG F C   1 
ATOM   1952 O  O   . ARG B 1 115 ? 11.062  -4.994  9.247   1.00 12.72 ? 115 ARG F O   1 
ATOM   1953 C  CB  . ARG B 1 115 ? 8.282   -7.121  8.854   1.00 12.58 ? 115 ARG F CB  1 
ATOM   1954 C  CG  . ARG B 1 115 ? 6.780   -6.930  8.991   1.00 14.48 ? 115 ARG F CG  1 
ATOM   1955 C  CD  . ARG B 1 115 ? 5.951   -8.133  8.655   1.00 15.34 ? 115 ARG F CD  1 
ATOM   1956 N  NE  . ARG B 1 115 ? 4.532   -7.873  8.864   1.00 15.47 ? 115 ARG F NE  1 
ATOM   1957 C  CZ  . ARG B 1 115 ? 3.823   -8.190  9.950   1.00 16.16 ? 115 ARG F CZ  1 
ATOM   1958 N  NH1 . ARG B 1 115 ? 4.379   -8.762  11.001  1.00 15.76 ? 115 ARG F NH1 1 
ATOM   1959 N  NH2 . ARG B 1 115 ? 2.531   -7.915  9.972   1.00 17.14 ? 115 ARG F NH2 1 
ATOM   1960 N  N   . THR B 1 116 ? 11.205  -7.190  9.687   1.00 11.64 ? 116 THR F N   1 
ATOM   1961 C  CA  . THR B 1 116 ? 12.682  -7.215  9.659   1.00 12.01 ? 116 THR F CA  1 
ATOM   1962 C  C   . THR B 1 116 ? 13.162  -7.988  8.439   1.00 11.96 ? 116 THR F C   1 
ATOM   1963 O  O   . THR B 1 116 ? 12.728  -9.120  8.233   1.00 14.05 ? 116 THR F O   1 
ATOM   1964 C  CB  . THR B 1 116 ? 13.277  -7.834  10.919  1.00 12.43 ? 116 THR F CB  1 
ATOM   1965 O  OG1 . THR B 1 116 ? 12.955  -6.984  12.023  1.00 13.81 ? 116 THR F OG1 1 
ATOM   1966 C  CG2 . THR B 1 116 ? 14.777  -7.999  10.859  1.00 12.50 ? 116 THR F CG2 1 
ATOM   1967 N  N   . LEU B 1 117 ? 14.063  -7.397  7.675   1.00 11.11 ? 117 LEU F N   1 
ATOM   1968 C  CA  . LEU B 1 117 ? 14.784  -8.114  6.609   1.00 11.28 ? 117 LEU F CA  1 
ATOM   1969 C  C   . LEU B 1 117 ? 16.060  -8.699  7.196   1.00 11.04 ? 117 LEU F C   1 
ATOM   1970 O  O   . LEU B 1 117 ? 16.753  -8.004  7.913   1.00 12.56 ? 117 LEU F O   1 
ATOM   1971 C  CB  . LEU B 1 117 ? 15.088  -7.109  5.504   1.00 11.15 ? 117 LEU F CB  1 
ATOM   1972 C  CG  . LEU B 1 117 ? 15.704  -7.707  4.241   1.00 12.40 ? 117 LEU F CG  1 
ATOM   1973 C  CD1 . LEU B 1 117 ? 14.741  -8.635  3.521   1.00 12.43 ? 117 LEU F CD1 1 
ATOM   1974 C  CD2 . LEU B 1 117 ? 16.179  -6.594  3.320   1.00 12.55 ? 117 LEU F CD2 1 
ATOM   1975 N  N   . VAL B 1 118 ? 16.327  -9.973  6.922   1.00 11.48 ? 118 VAL F N   1 
ATOM   1976 C  CA  . VAL B 1 118 ? 17.506  -10.692 7.470   1.00 11.80 ? 118 VAL F CA  1 
ATOM   1977 C  C   . VAL B 1 118 ? 18.281  -11.329 6.324   1.00 12.05 ? 118 VAL F C   1 
ATOM   1978 O  O   . VAL B 1 118 ? 17.673  -11.995 5.480   1.00 12.42 ? 118 VAL F O   1 
ATOM   1979 C  CB  . VAL B 1 118 ? 17.080  -11.768 8.477   1.00 11.92 ? 118 VAL F CB  1 
ATOM   1980 C  CG1 . VAL B 1 118 ? 18.281  -12.518 9.042   1.00 12.84 ? 118 VAL F CG1 1 
ATOM   1981 C  CG2 . VAL B 1 118 ? 16.213  -11.187 9.583   1.00 11.91 ? 118 VAL F CG2 1 
ATOM   1982 N  N   . VAL B 1 119 ? 19.598  -11.187 6.359   1.00 11.46 ? 119 VAL F N   1 
ATOM   1983 C  CA  . VAL B 1 119 ? 20.497  -11.976 5.482   1.00 11.99 ? 119 VAL F CA  1 
ATOM   1984 C  C   . VAL B 1 119 ? 21.236  -12.992 6.358   1.00 12.36 ? 119 VAL F C   1 
ATOM   1985 O  O   . VAL B 1 119 ? 21.680  -12.661 7.457   1.00 12.53 ? 119 VAL F O   1 
ATOM   1986 C  CB  . VAL B 1 119 ? 21.437  -11.081 4.655   1.00 12.24 ? 119 VAL F CB  1 
ATOM   1987 C  CG1 . VAL B 1 119 ? 22.390  -10.256 5.510   1.00 12.66 ? 119 VAL F CG1 1 
ATOM   1988 C  CG2 . VAL B 1 119 ? 22.193  -11.924 3.650   1.00 12.76 ? 119 VAL F CG2 1 
ATOM   1989 N  N   . HIS B 1 120 ? 21.281  -14.229 5.884   1.00 13.13 ? 120 HIS F N   1 
ATOM   1990 C  CA  . HIS B 1 120 ? 21.723  -15.411 6.659   1.00 14.02 ? 120 HIS F CA  1 
ATOM   1991 C  C   . HIS B 1 120 ? 23.135  -15.864 6.283   1.00 15.06 ? 120 HIS F C   1 
ATOM   1992 O  O   . HIS B 1 120 ? 23.640  -15.510 5.228   1.00 14.99 ? 120 HIS F O   1 
ATOM   1993 C  CB  . HIS B 1 120 ? 20.729  -16.552 6.460   1.00 14.22 ? 120 HIS F CB  1 
ATOM   1994 C  CG  . HIS B 1 120 ? 19.491  -16.373 7.261   1.00 14.26 ? 120 HIS F CG  1 
ATOM   1995 N  ND1 . HIS B 1 120 ? 19.378  -16.890 8.537   1.00 16.09 ? 120 HIS F ND1 1 
ATOM   1996 C  CD2 . HIS B 1 120 ? 18.336  -15.722 7.011   1.00 13.92 ? 120 HIS F CD2 1 
ATOM   1997 C  CE1 . HIS B 1 120 ? 18.206  -16.571 9.016   1.00 14.50 ? 120 HIS F CE1 1 
ATOM   1998 N  NE2 . HIS B 1 120 ? 17.522  -15.878 8.114   1.00 14.91 ? 120 HIS F NE2 1 
ATOM   1999 N  N   . GLU B 1 121 ? 23.695  -16.663 7.184   1.00 16.90 ? 121 GLU F N   1 
ATOM   2000 C  CA  . GLU B 1 121 ? 25.050  -17.256 7.109   1.00 18.28 ? 121 GLU F CA  1 
ATOM   2001 C  C   . GLU B 1 121 ? 25.168  -18.186 5.892   1.00 17.56 ? 121 GLU F C   1 
ATOM   2002 O  O   . GLU B 1 121 ? 26.206  -18.140 5.201   1.00 17.85 ? 121 GLU F O   1 
ATOM   2003 C  CB  . GLU B 1 121 ? 25.283  -17.988 8.426   1.00 20.60 ? 121 GLU F CB  1 
ATOM   2004 C  CG  . GLU B 1 121 ? 26.534  -18.834 8.480   1.00 21.97 ? 121 GLU F CG  1 
ATOM   2005 C  CD  . GLU B 1 121 ? 26.466  -19.923 9.541   0.70 23.16 ? 121 GLU F CD  1 
ATOM   2006 O  OE1 . GLU B 1 121 ? 25.351  -20.225 10.033  0.70 24.06 ? 121 GLU F OE1 1 
ATOM   2007 O  OE2 . GLU B 1 121 ? 27.525  -20.483 9.856   0.60 26.06 ? 121 GLU F OE2 1 
ATOM   2008 N  N   . LYS B 1 122 ? 24.143  -19.001 5.650   1.00 18.29 ? 122 LYS F N   1 
ATOM   2009 C  CA  . LYS B 1 122 ? 24.196  -20.113 4.671   1.00 18.50 ? 122 LYS F CA  1 
ATOM   2010 C  C   . LYS B 1 122 ? 23.082  -19.966 3.638   1.00 18.04 ? 122 LYS F C   1 
ATOM   2011 O  O   . LYS B 1 122 ? 22.228  -19.065 3.758   1.00 16.17 ? 122 LYS F O   1 
ATOM   2012 C  CB  . LYS B 1 122 ? 24.052  -21.470 5.372   1.00 20.50 ? 122 LYS F CB  1 
ATOM   2013 C  CG  . LYS B 1 122 ? 24.744  -21.625 6.721   1.00 22.46 ? 122 LYS F CG  1 
ATOM   2014 C  CD  . LYS B 1 122 ? 24.854  -23.080 7.165   1.00 24.23 ? 122 LYS F CD  1 
ATOM   2015 C  CE  . LYS B 1 122 ? 23.813  -23.460 8.193   0.70 25.23 ? 122 LYS F CE  1 
ATOM   2016 N  NZ  . LYS B 1 122 ? 23.536  -24.917 8.222   0.60 26.73 ? 122 LYS F NZ  1 
ATOM   2017 N  N   . ALA B 1 123 ? 23.076  -20.858 2.658   1.00 15.96 ? 123 ALA F N   1 
ATOM   2018 C  CA  . ALA B 1 123 ? 22.051  -20.919 1.601   1.00 15.98 ? 123 ALA F CA  1 
ATOM   2019 C  C   . ALA B 1 123 ? 20.734  -21.351 2.232   1.00 16.25 ? 123 ALA F C   1 
ATOM   2020 O  O   . ALA B 1 123 ? 20.713  -22.233 3.108   1.00 18.01 ? 123 ALA F O   1 
ATOM   2021 C  CB  . ALA B 1 123 ? 22.488  -21.851 0.503   1.00 16.33 ? 123 ALA F CB  1 
ATOM   2022 N  N   . ASP B 1 124 ? 19.661  -20.700 1.824   1.00 16.23 ? 124 ASP F N   1 
ATOM   2023 C  CA  . ASP B 1 124 ? 18.290  -21.202 2.019   1.00 15.44 ? 124 ASP F CA  1 
ATOM   2024 C  C   . ASP B 1 124 ? 18.102  -22.314 0.981   1.00 15.69 ? 124 ASP F C   1 
ATOM   2025 O  O   . ASP B 1 124 ? 18.289  -22.058 -0.214  1.00 16.48 ? 124 ASP F O   1 
ATOM   2026 C  CB  . ASP B 1 124 ? 17.307  -20.038 1.888   1.00 14.80 ? 124 ASP F CB  1 
ATOM   2027 C  CG  . ASP B 1 124 ? 15.855  -20.385 2.082   1.00 16.14 ? 124 ASP F CG  1 
ATOM   2028 O  OD1 . ASP B 1 124 ? 15.499  -21.594 1.999   1.00 16.06 ? 124 ASP F OD1 1 
ATOM   2029 O  OD2 . ASP B 1 124 ? 15.074  -19.445 2.297   1.00 16.69 ? 124 ASP F OD2 1 
ATOM   2030 N  N   . ASP B 1 125 ? 17.735  -23.511 1.425   1.00 15.25 ? 125 ASP F N   1 
ATOM   2031 C  CA  . ASP B 1 125 ? 17.580  -24.672 0.505   1.00 16.68 ? 125 ASP F CA  1 
ATOM   2032 C  C   . ASP B 1 125 ? 16.200  -24.629 -0.149  1.00 17.12 ? 125 ASP F C   1 
ATOM   2033 O  O   . ASP B 1 125 ? 15.888  -25.559 -0.903  1.00 18.62 ? 125 ASP F O   1 
ATOM   2034 C  CB  . ASP B 1 125 ? 17.844  -26.006 1.210   1.00 17.10 ? 125 ASP F CB  1 
ATOM   2035 C  CG  . ASP B 1 125 ? 16.938  -26.313 2.393   1.00 17.50 ? 125 ASP F CG  1 
ATOM   2036 O  OD1 . ASP B 1 125 ? 15.790  -25.825 2.410   1.00 15.86 ? 125 ASP F OD1 1 
ATOM   2037 O  OD2 . ASP B 1 125 ? 17.393  -27.047 3.301   1.00 18.23 ? 125 ASP F OD2 1 
ATOM   2038 N  N   . LEU B 1 126 ? 15.411  -23.574 0.092   1.00 17.30 ? 126 LEU F N   1 
ATOM   2039 C  CA  . LEU B 1 126 ? 14.107  -23.308 -0.567  1.00 17.49 ? 126 LEU F CA  1 
ATOM   2040 C  C   . LEU B 1 126 ? 13.121  -24.454 -0.297  1.00 17.68 ? 126 LEU F C   1 
ATOM   2041 O  O   . LEU B 1 126 ? 12.198  -24.646 -1.109  1.00 18.31 ? 126 LEU F O   1 
ATOM   2042 C  CB  . LEU B 1 126 ? 14.325  -23.059 -2.065  1.00 19.10 ? 126 LEU F CB  1 
ATOM   2043 C  CG  . LEU B 1 126 ? 15.383  -22.014 -2.424  1.00 20.06 ? 126 LEU F CG  1 
ATOM   2044 C  CD1 . LEU B 1 126 ? 15.327  -21.671 -3.906  1.00 21.46 ? 126 LEU F CD1 1 
ATOM   2045 C  CD2 . LEU B 1 126 ? 15.209  -20.741 -1.608  1.00 19.77 ? 126 LEU F CD2 1 
ATOM   2046 N  N   . GLY B 1 127 ? 13.283  -25.154 0.824   1.00 17.31 ? 127 GLY F N   1 
ATOM   2047 C  CA  . GLY B 1 127 ? 12.439  -26.303 1.212   1.00 17.75 ? 127 GLY F CA  1 
ATOM   2048 C  C   . GLY B 1 127 ? 12.816  -27.595 0.509   1.00 20.03 ? 127 GLY F C   1 
ATOM   2049 O  O   . GLY B 1 127 ? 12.026  -28.559 0.589   1.00 22.73 ? 127 GLY F O   1 
ATOM   2050 N  N   . LYS B 1 128 ? 13.986  -27.658 -0.125  1.00 19.80 ? 128 LYS F N   1 
ATOM   2051 C  CA  . LYS B 1 128 ? 14.435  -28.849 -0.912  1.00 22.35 ? 128 LYS F CA  1 
ATOM   2052 C  C   . LYS B 1 128 ? 15.732  -29.373 -0.277  1.00 22.90 ? 128 LYS F C   1 
ATOM   2053 O  O   . LYS B 1 128 ? 16.714  -29.691 -1.007  1.00 24.07 ? 128 LYS F O   1 
ATOM   2054 C  CB  . LYS B 1 128 ? 14.606  -28.465 -2.390  1.00 25.22 ? 128 LYS F CB  1 
ATOM   2055 C  CG  . LYS B 1 128 ? 13.368  -27.855 -3.045  1.00 27.71 ? 128 LYS F CG  1 
ATOM   2056 C  CD  . LYS B 1 128 ? 12.314  -28.867 -3.462  1.00 31.49 ? 128 LYS F CD  1 
ATOM   2057 C  CE  . LYS B 1 128 ? 10.916  -28.281 -3.560  1.00 33.68 ? 128 LYS F CE  1 
ATOM   2058 N  NZ  . LYS B 1 128 ? 10.790  -27.301 -4.666  1.00 34.80 ? 128 LYS F NZ  1 
ATOM   2059 N  N   . GLY B 1 129 ? 15.773  -29.427 1.050   1.00 21.16 ? 129 GLY F N   1 
ATOM   2060 C  CA  . GLY B 1 129 ? 16.991  -29.820 1.785   1.00 20.81 ? 129 GLY F CA  1 
ATOM   2061 C  C   . GLY B 1 129 ? 16.986  -31.278 2.200   1.00 20.64 ? 129 GLY F C   1 
ATOM   2062 O  O   . GLY B 1 129 ? 18.064  -31.804 2.505   1.00 22.34 ? 129 GLY F O   1 
ATOM   2063 N  N   . GLY B 1 130 ? 15.812  -31.876 2.307   1.00 17.94 ? 130 GLY F N   1 
ATOM   2064 C  CA  . GLY B 1 130 ? 15.655  -33.302 2.654   1.00 19.50 ? 130 GLY F CA  1 
ATOM   2065 C  C   . GLY B 1 130 ? 15.558  -33.549 4.147   1.00 20.26 ? 130 GLY F C   1 
ATOM   2066 O  O   . GLY B 1 130 ? 15.762  -34.699 4.556   1.00 20.94 ? 130 GLY F O   1 
ATOM   2067 N  N   . ASN B 1 131 ? 15.211  -32.542 4.950   1.00 20.19 ? 131 ASN F N   1 
ATOM   2068 C  CA  . ASN B 1 131 ? 14.952  -32.723 6.405   1.00 20.05 ? 131 ASN F CA  1 
ATOM   2069 C  C   . ASN B 1 131 ? 13.767  -31.843 6.806   1.00 19.56 ? 131 ASN F C   1 
ATOM   2070 O  O   . ASN B 1 131 ? 13.277  -31.072 5.973   1.00 19.69 ? 131 ASN F O   1 
ATOM   2071 C  CB  . ASN B 1 131 ? 16.198  -32.496 7.272   1.00 20.72 ? 131 ASN F CB  1 
ATOM   2072 C  CG  . ASN B 1 131 ? 16.686  -31.060 7.308   1.00 21.82 ? 131 ASN F CG  1 
ATOM   2073 O  OD1 . ASN B 1 131 ? 16.063  -30.162 6.764   1.00 20.75 ? 131 ASN F OD1 1 
ATOM   2074 N  ND2 . ASN B 1 131 ? 17.844  -30.836 7.909   1.00 24.53 ? 131 ASN F ND2 1 
ATOM   2075 N  N   . GLU B 1 132 ? 13.302  -31.984 8.044   1.00 21.13 ? 132 GLU F N   1 
ATOM   2076 C  CA  . GLU B 1 132 ? 12.111  -31.262 8.565   1.00 21.78 ? 132 GLU F CA  1 
ATOM   2077 C  C   . GLU B 1 132 ? 12.392  -29.757 8.556   1.00 21.06 ? 132 GLU F C   1 
ATOM   2078 O  O   . GLU B 1 132 ? 11.515  -28.979 8.130   1.00 21.03 ? 132 GLU F O   1 
ATOM   2079 C  CB  . GLU B 1 132 ? 11.793  -31.750 9.977   1.00 22.00 ? 132 GLU F CB  1 
ATOM   2080 N  N   . GLU B 1 133 ? 13.593  -29.361 8.975   1.00 20.04 ? 133 GLU F N   1 
ATOM   2081 C  CA  . GLU B 1 133 ? 13.949  -27.923 9.117   1.00 21.20 ? 133 GLU F CA  1 
ATOM   2082 C  C   . GLU B 1 133 ? 13.853  -27.236 7.745   1.00 19.49 ? 133 GLU F C   1 
ATOM   2083 O  O   . GLU B 1 133 ? 13.556  -26.036 7.689   1.00 19.41 ? 133 GLU F O   1 
ATOM   2084 C  CB  . GLU B 1 133 ? 15.339  -27.785 9.737   1.00 23.71 ? 133 GLU F CB  1 
ATOM   2085 C  CG  . GLU B 1 133 ? 15.682  -26.370 10.160  1.00 26.43 ? 133 GLU F CG  1 
ATOM   2086 C  CD  . GLU B 1 133 ? 17.034  -26.212 10.835  1.00 30.35 ? 133 GLU F CD  1 
ATOM   2087 O  OE1 . GLU B 1 133 ? 17.583  -27.235 11.288  1.00 30.47 ? 133 GLU F OE1 1 
ATOM   2088 O  OE2 . GLU B 1 133 ? 17.533  -25.059 10.909  1.00 32.67 ? 133 GLU F OE2 1 
ATOM   2089 N  N   . SER B 1 134 ? 14.057  -27.969 6.655   1.00 19.10 ? 134 SER F N   1 
ATOM   2090 C  CA  . SER B 1 134 ? 14.006  -27.407 5.285   1.00 17.91 ? 134 SER F CA  1 
ATOM   2091 C  C   . SER B 1 134 ? 12.659  -26.732 5.051   1.00 19.36 ? 134 SER F C   1 
ATOM   2092 O  O   . SER B 1 134 ? 12.635  -25.637 4.452   1.00 18.03 ? 134 SER F O   1 
ATOM   2093 C  CB  . SER B 1 134 ? 14.278  -28.478 4.263   1.00 17.43 ? 134 SER F CB  1 
ATOM   2094 O  OG  . SER B 1 134 ? 14.328  -27.906 2.974   1.00 17.61 ? 134 SER F OG  1 
ATOM   2095 N  N   . THR B 1 135 ? 11.568  -27.364 5.501   1.00 20.19 ? 135 THR F N   1 
ATOM   2096 C  CA  . THR B 1 135 ? 10.162  -26.932 5.275   1.00 22.44 ? 135 THR F CA  1 
ATOM   2097 C  C   . THR B 1 135 ? 9.772   -25.828 6.273   1.00 20.76 ? 135 THR F C   1 
ATOM   2098 O  O   . THR B 1 135 ? 8.637   -25.369 6.199   1.00 20.77 ? 135 THR F O   1 
ATOM   2099 C  CB  . THR B 1 135 ? 9.201   -28.130 5.418   1.00 26.07 ? 135 THR F CB  1 
ATOM   2100 O  OG1 . THR B 1 135 ? 9.175   -28.507 6.797   1.00 32.67 ? 135 THR F OG1 1 
ATOM   2101 C  CG2 . THR B 1 135 ? 9.615   -29.335 4.607   1.00 27.90 ? 135 THR F CG2 1 
ATOM   2102 N  N   . LYS B 1 136 ? 10.672  -25.430 7.183   1.00 21.05 ? 136 LYS F N   1 
ATOM   2103 C  CA  . LYS B 1 136 ? 10.393  -24.401 8.224   1.00 21.61 ? 136 LYS F CA  1 
ATOM   2104 C  C   . LYS B 1 136 ? 11.290  -23.174 8.016   1.00 20.24 ? 136 LYS F C   1 
ATOM   2105 O  O   . LYS B 1 136 ? 10.748  -22.065 7.928   1.00 20.42 ? 136 LYS F O   1 
ATOM   2106 C  CB  . LYS B 1 136 ? 10.549  -25.005 9.622   1.00 23.56 ? 136 LYS F CB  1 
ATOM   2107 C  CG  . LYS B 1 136 ? 9.582   -26.143 9.924   1.00 25.64 ? 136 LYS F CG  1 
ATOM   2108 C  CD  . LYS B 1 136 ? 9.530   -26.528 11.385  1.00 26.35 ? 136 LYS F CD  1 
ATOM   2109 N  N   . THR B 1 137 ? 12.610  -23.342 7.945   1.00 19.41 ? 137 THR F N   1 
ATOM   2110 C  CA  . THR B 1 137 ? 13.581  -22.215 7.911   1.00 19.13 ? 137 THR F CA  1 
ATOM   2111 C  C   . THR B 1 137 ? 14.408  -22.256 6.632   1.00 17.58 ? 137 THR F C   1 
ATOM   2112 O  O   . THR B 1 137 ? 15.024  -21.225 6.311   1.00 19.16 ? 137 THR F O   1 
ATOM   2113 C  CB  . THR B 1 137 ? 14.525  -22.237 9.119   1.00 20.59 ? 137 THR F CB  1 
ATOM   2114 O  OG1 . THR B 1 137 ? 15.410  -23.338 8.930   1.00 19.16 ? 137 THR F OG1 1 
ATOM   2115 C  CG2 . THR B 1 137 ? 13.798  -22.379 10.438  1.00 21.32 ? 137 THR F CG2 1 
ATOM   2116 N  N   . GLY B 1 138 ? 14.499  -23.411 5.967   1.00 15.72 ? 138 GLY F N   1 
ATOM   2117 C  CA  . GLY B 1 138 ? 15.356  -23.573 4.784   1.00 17.11 ? 138 GLY F CA  1 
ATOM   2118 C  C   . GLY B 1 138 ? 16.806  -23.790 5.171   1.00 16.01 ? 138 GLY F C   1 
ATOM   2119 O  O   . GLY B 1 138 ? 17.654  -23.745 4.272   1.00 16.27 ? 138 GLY F O   1 
ATOM   2120 N  N   . ASN B 1 139 ? 17.098  -23.979 6.459   1.00 17.17 ? 139 ASN F N   1 
ATOM   2121 C  CA  . ASN B 1 139 ? 18.454  -24.362 6.942   1.00 18.45 ? 139 ASN F CA  1 
ATOM   2122 C  C   . ASN B 1 139 ? 19.493  -23.297 6.564   1.00 17.93 ? 139 ASN F C   1 
ATOM   2123 O  O   . ASN B 1 139 ? 20.634  -23.653 6.295   1.00 16.95 ? 139 ASN F O   1 
ATOM   2124 C  CB  . ASN B 1 139 ? 18.903  -25.705 6.355   1.00 18.76 ? 139 ASN F CB  1 
ATOM   2125 C  CG  . ASN B 1 139 ? 18.093  -26.875 6.874   1.00 20.51 ? 139 ASN F CG  1 
ATOM   2126 O  OD1 . ASN B 1 139 ? 18.102  -27.148 8.066   1.00 22.60 ? 139 ASN F OD1 1 
ATOM   2127 N  ND2 . ASN B 1 139 ? 17.385  -27.556 5.996   1.00 20.68 ? 139 ASN F ND2 1 
ATOM   2128 N  N   . ALA B 1 140 ? 19.138  -22.011 6.598   1.00 18.25 ? 140 ALA F N   1 
ATOM   2129 C  CA  . ALA B 1 140 ? 20.044  -20.914 6.180   1.00 17.55 ? 140 ALA F CA  1 
ATOM   2130 C  C   . ALA B 1 140 ? 20.941  -20.441 7.338   1.00 18.03 ? 140 ALA F C   1 
ATOM   2131 O  O   . ALA B 1 140 ? 21.770  -19.545 7.108   1.00 18.03 ? 140 ALA F O   1 
ATOM   2132 C  CB  . ALA B 1 140 ? 19.255  -19.776 5.574   1.00 17.77 ? 140 ALA F CB  1 
ATOM   2133 N  N   . GLY B 1 141 ? 20.861  -21.043 8.525   1.00 18.56 ? 141 GLY F N   1 
ATOM   2134 C  CA  . GLY B 1 141 ? 21.852  -20.781 9.588   1.00 19.35 ? 141 GLY F CA  1 
ATOM   2135 C  C   . GLY B 1 141 ? 21.685  -19.409 10.213  1.00 18.99 ? 141 GLY F C   1 
ATOM   2136 O  O   . GLY B 1 141 ? 20.558  -18.883 10.225  1.00 20.98 ? 141 GLY F O   1 
ATOM   2137 N  N   . SER B 1 142 ? 22.771  -18.866 10.754  1.00 20.10 ? 142 SER F N   1 
ATOM   2138 C  CA  . SER B 1 142 ? 22.713  -17.704 11.672  1.00 18.99 ? 142 SER F CA  1 
ATOM   2139 C  C   . SER B 1 142 ? 22.276  -16.454 10.901  1.00 17.45 ? 142 SER F C   1 
ATOM   2140 O  O   . SER B 1 142 ? 22.400  -16.400 9.648   1.00 17.15 ? 142 SER F O   1 
ATOM   2141 C  CB  . SER B 1 142 ? 24.017  -17.488 12.390  1.00 21.08 ? 142 SER F CB  1 
ATOM   2142 O  OG  . SER B 1 142 ? 24.973  -16.898 11.541  1.00 25.28 ? 142 SER F OG  1 
ATOM   2143 N  N   . ARG B 1 143 ? 21.793  -15.475 11.651  1.00 15.55 ? 143 ARG F N   1 
ATOM   2144 C  CA  . ARG B 1 143 ? 21.363  -14.171 11.103  1.00 14.92 ? 143 ARG F CA  1 
ATOM   2145 C  C   . ARG B 1 143 ? 22.571  -13.241 11.108  1.00 15.83 ? 143 ARG F C   1 
ATOM   2146 O  O   . ARG B 1 143 ? 22.985  -12.791 12.196  1.00 18.14 ? 143 ARG F O   1 
ATOM   2147 C  CB  . ARG B 1 143 ? 20.196  -13.642 11.932  1.00 14.91 ? 143 ARG F CB  1 
ATOM   2148 C  CG  . ARG B 1 143 ? 19.063  -14.647 12.028  1.00 14.71 ? 143 ARG F CG  1 
ATOM   2149 C  CD  . ARG B 1 143 ? 17.954  -14.197 12.924  1.00 15.30 ? 143 ARG F CD  1 
ATOM   2150 N  NE  . ARG B 1 143 ? 16.952  -15.238 12.938  1.00 16.04 ? 143 ARG F NE  1 
ATOM   2151 C  CZ  . ARG B 1 143 ? 15.712  -15.123 13.395  1.00 15.99 ? 143 ARG F CZ  1 
ATOM   2152 N  NH1 . ARG B 1 143 ? 15.246  -13.972 13.848  1.00 16.62 ? 143 ARG F NH1 1 
ATOM   2153 N  NH2 . ARG B 1 143 ? 14.923  -16.175 13.346  1.00 15.19 ? 143 ARG F NH2 1 
ATOM   2154 N  N   . LEU B 1 144 ? 23.126  -12.932 9.944   1.00 14.56 ? 144 LEU F N   1 
ATOM   2155 C  CA  . LEU B 1 144 ? 24.380  -12.136 9.886   1.00 15.04 ? 144 LEU F CA  1 
ATOM   2156 C  C   . LEU B 1 144 ? 24.064  -10.652 10.061  1.00 15.47 ? 144 LEU F C   1 
ATOM   2157 O  O   . LEU B 1 144 ? 24.867  -9.925  10.682  1.00 16.40 ? 144 LEU F O   1 
ATOM   2158 C  CB  . LEU B 1 144 ? 25.081  -12.362 8.549   1.00 15.63 ? 144 LEU F CB  1 
ATOM   2159 C  CG  . LEU B 1 144 ? 25.564  -13.778 8.256   1.00 16.96 ? 144 LEU F CG  1 
ATOM   2160 C  CD1 . LEU B 1 144 ? 26.360  -13.807 6.961   1.00 18.00 ? 144 LEU F CD1 1 
ATOM   2161 C  CD2 . LEU B 1 144 ? 26.403  -14.301 9.398   1.00 18.52 ? 144 LEU F CD2 1 
ATOM   2162 N  N   . ALA B 1 145 ? 22.967  -10.181 9.480   1.00 14.37 ? 145 ALA F N   1 
ATOM   2163 C  CA  . ALA B 1 145 ? 22.637  -8.747  9.511   1.00 13.84 ? 145 ALA F CA  1 
ATOM   2164 C  C   . ALA B 1 145 ? 21.145  -8.610  9.285   1.00 14.08 ? 145 ALA F C   1 
ATOM   2165 O  O   . ALA B 1 145 ? 20.539  -9.470  8.630   1.00 13.80 ? 145 ALA F O   1 
ATOM   2166 C  CB  . ALA B 1 145 ? 23.424  -8.001  8.477   1.00 13.34 ? 145 ALA F CB  1 
ATOM   2167 N  N   . CYS B 1 146 ? 20.567  -7.572  9.838   1.00 13.31 ? 146 CYS F N   1 
ATOM   2168 C  CA  . CYS B 1 146 ? 19.121  -7.344  9.710   1.00 13.91 ? 146 CYS F CA  1 
ATOM   2169 C  C   . CYS B 1 146 ? 18.808  -5.870  9.890   1.00 12.94 ? 146 CYS F C   1 
ATOM   2170 O  O   . CYS B 1 146 ? 19.673  -5.107  10.358  1.00 12.59 ? 146 CYS F O   1 
ATOM   2171 C  CB  . CYS B 1 146 ? 18.355  -8.177  10.725  1.00 15.16 ? 146 CYS F CB  1 
ATOM   2172 S  SG  . CYS B 1 146 ? 18.760  -7.781  12.442  1.00 18.44 ? 146 CYS F SG  1 
ATOM   2173 N  N   . GLY B 1 147 ? 17.596  -5.501  9.526   1.00 12.40 ? 147 GLY F N   1 
ATOM   2174 C  CA  . GLY B 1 147 ? 17.106  -4.147  9.783   1.00 11.97 ? 147 GLY F CA  1 
ATOM   2175 C  C   . GLY B 1 147 ? 15.609  -4.102  9.682   1.00 11.22 ? 147 GLY F C   1 
ATOM   2176 O  O   . GLY B 1 147 ? 15.013  -5.018  9.101   1.00 12.16 ? 147 GLY F O   1 
ATOM   2177 N  N   . VAL B 1 148 ? 15.007  -3.080  10.250  1.00 10.98 ? 148 VAL F N   1 
ATOM   2178 C  CA  . VAL B 1 148 ? 13.545  -2.874  10.164  1.00 11.40 ? 148 VAL F CA  1 
ATOM   2179 C  C   . VAL B 1 148 ? 13.265  -2.194  8.826   1.00 12.10 ? 148 VAL F C   1 
ATOM   2180 O  O   . VAL B 1 148 ? 14.008  -1.277  8.430   1.00 13.34 ? 148 VAL F O   1 
ATOM   2181 C  CB  . VAL B 1 148 ? 13.037  -2.053  11.353  1.00 12.81 ? 148 VAL F CB  1 
ATOM   2182 C  CG1 . VAL B 1 148 ? 11.541  -1.845  11.286  1.00 13.18 ? 148 VAL F CG1 1 
ATOM   2183 C  CG2 . VAL B 1 148 ? 13.423  -2.725  12.665  1.00 13.21 ? 148 VAL F CG2 1 
ATOM   2184 N  N   . ILE B 1 149 ? 12.237  -2.646  8.141   1.00 11.75 ? 149 ILE F N   1 
ATOM   2185 C  CA  . ILE B 1 149 ? 11.830  -2.105  6.821   1.00 11.94 ? 149 ILE F CA  1 
ATOM   2186 C  C   . ILE B 1 149 ? 11.010  -0.846  7.089   1.00 12.79 ? 149 ILE F C   1 
ATOM   2187 O  O   . ILE B 1 149 ? 9.930   -0.925  7.714   1.00 12.90 ? 149 ILE F O   1 
ATOM   2188 C  CB  . ILE B 1 149 ? 11.090  -3.179  6.012   1.00 12.04 ? 149 ILE F CB  1 
ATOM   2189 C  CG1 . ILE B 1 149 ? 11.989  -4.395  5.782   1.00 11.90 ? 149 ILE F CG1 1 
ATOM   2190 C  CG2 . ILE B 1 149 ? 10.574  -2.596  4.714   1.00 11.68 ? 149 ILE F CG2 1 
ATOM   2191 C  CD1 . ILE B 1 149 ? 11.226  -5.613  5.341   1.00 12.36 ? 149 ILE F CD1 1 
ATOM   2192 N  N   . GLY B 1 150 ? 11.531  0.297   6.654   1.00 12.06 ? 150 GLY F N   1 
ATOM   2193 C  CA  . GLY B 1 150 ? 10.922  1.601   6.934   1.00 11.97 ? 150 GLY F CA  1 
ATOM   2194 C  C   . GLY B 1 150 ? 10.350  2.228   5.683   1.00 11.74 ? 150 GLY F C   1 
ATOM   2195 O  O   . GLY B 1 150 ? 10.792  1.906   4.563   1.00 12.14 ? 150 GLY F O   1 
ATOM   2196 N  N   . ILE B 1 151 ? 9.411   3.134   5.876   1.00 12.53 ? 151 ILE F N   1 
ATOM   2197 C  CA  . ILE B 1 151 ? 8.800   3.916   4.772   1.00 13.04 ? 151 ILE F CA  1 
ATOM   2198 C  C   . ILE B 1 151 ? 9.836   4.894   4.237   1.00 13.52 ? 151 ILE F C   1 
ATOM   2199 O  O   . ILE B 1 151 ? 10.426  5.615   5.024   1.00 12.95 ? 151 ILE F O   1 
ATOM   2200 C  CB  . ILE B 1 151 ? 7.550   4.641   5.282   1.00 14.38 ? 151 ILE F CB  1 
ATOM   2201 C  CG1 . ILE B 1 151 ? 6.468   3.641   5.684   1.00 15.82 ? 151 ILE F CG1 1 
ATOM   2202 C  CG2 . ILE B 1 151 ? 7.035   5.632   4.238   1.00 15.37 ? 151 ILE F CG2 1 
ATOM   2203 C  CD1 . ILE B 1 151 ? 5.434   4.223   6.588   1.00 16.50 ? 151 ILE F CD1 1 
ATOM   2204 N  N   . ALA B 1 152 ? 9.991   4.945   2.924   1.00 12.87 ? 152 ALA F N   1 
ATOM   2205 C  CA  . ALA B 1 152 ? 10.953  5.848   2.270   1.00 14.26 ? 152 ALA F CA  1 
ATOM   2206 C  C   . ALA B 1 152 ? 10.215  6.947   1.508   1.00 15.31 ? 152 ALA F C   1 
ATOM   2207 O  O   . ALA B 1 152 ? 9.030   6.816   1.192   1.00 15.35 ? 152 ALA F O   1 
ATOM   2208 C  CB  . ALA B 1 152 ? 11.878  5.063   1.368   1.00 14.24 ? 152 ALA F CB  1 
ATOM   2209 N  N   . GLN B 1 153 ? 10.967  7.981   1.174   1.00 16.57 ? 153 GLN F N   1 
ATOM   2210 C  CA  . GLN B 1 153 ? 10.448  9.166   0.465   1.00 18.47 ? 153 GLN F CA  1 
ATOM   2211 C  C   . GLN B 1 153 ? 10.092  8.785   -0.973  1.00 19.43 ? 153 GLN F C   1 
ATOM   2212 O  O   . GLN B 1 153 ? 10.852  8.046   -1.615  1.00 24.21 ? 153 GLN F O   1 
ATOM   2213 C  CB  . GLN B 1 153 ? 11.511  10.252  0.522   1.00 18.57 ? 153 GLN F CB  1 
ATOM   2214 C  CG  . GLN B 1 153 ? 11.103  11.537  -0.164  1.00 19.44 ? 153 GLN F CG  1 
ATOM   2215 C  CD  . GLN B 1 153 ? 12.169  12.578  0.057   1.00 19.19 ? 153 GLN F CD  1 
ATOM   2216 O  OE1 . GLN B 1 153 ? 12.758  12.668  1.132   1.00 20.13 ? 153 GLN F OE1 1 
ATOM   2217 N  NE2 . GLN B 1 153 ? 12.382  13.399  -0.954  1.00 19.99 ? 153 GLN F NE2 1 
ATOM   2218 O  OXT . GLN B 1 153 ? 9.066   9.215   -1.505  1.00 24.45 ? 153 GLN F OXT 1 
HETATM 2219 ZN ZN  . ZN  C 2 .   ? 6.723   18.794  15.027  1.00 15.79 ? 201 ZN  A ZN  1 
HETATM 2220 N  N1  A Q8H D 3 .   ? 0.863   -4.001  13.276  1.00 31.16 ? 202 Q8H A N1  1 
HETATM 2221 C  C2  A Q8H D 3 .   ? 2.636   1.393   7.954   1.00 23.56 ? 202 Q8H A C2  1 
HETATM 2222 C  C4  A Q8H D 3 .   ? 1.075   0.480   9.537   1.00 21.17 ? 202 Q8H A C4  1 
HETATM 2223 C  C5  A Q8H D 3 .   ? 1.092   -0.744  8.844   1.00 22.54 ? 202 Q8H A C5  1 
HETATM 2224 C  C6  A Q8H D 3 .   ? 0.224   -1.872  9.303   1.00 24.07 ? 202 Q8H A C6  1 
HETATM 2225 O  O   A Q8H D 3 .   ? -0.845  -1.631  9.865   1.00 24.40 ? 202 Q8H A O   1 
HETATM 2226 C  C3  A Q8H D 3 .   ? 1.853   1.533   9.077   1.00 20.85 ? 202 Q8H A C3  1 
HETATM 2227 C  C1  A Q8H D 3 .   ? 2.650   0.197   7.264   1.00 23.25 ? 202 Q8H A C1  1 
HETATM 2228 C  C   A Q8H D 3 .   ? 1.889   -0.862  7.701   1.00 23.97 ? 202 Q8H A C   1 
HETATM 2229 N  N   A Q8H D 3 .   ? 0.657   -3.117  9.109   1.00 24.90 ? 202 Q8H A N   1 
HETATM 2230 C  C7  A Q8H D 3 .   ? -0.089  -4.274  9.604   1.00 26.14 ? 202 Q8H A C7  1 
HETATM 2231 C  C12 A Q8H D 3 .   ? 0.258   -6.266  12.813  1.00 29.50 ? 202 Q8H A C12 1 
HETATM 2232 C  C11 A Q8H D 3 .   ? 0.687   -5.274  13.667  1.00 31.15 ? 202 Q8H A C11 1 
HETATM 2233 C  C10 A Q8H D 3 .   ? 0.612   -3.718  11.983  1.00 29.37 ? 202 Q8H A C10 1 
HETATM 2234 C  C9  A Q8H D 3 .   ? 0.006   -5.946  11.501  1.00 30.29 ? 202 Q8H A C9  1 
HETATM 2235 C  C8  A Q8H D 3 .   ? 0.197   -4.655  11.043  1.00 27.23 ? 202 Q8H A C8  1 
HETATM 2236 SE SE  A Q8H D 3 .   ? -0.032  0.629   11.110  1.00 19.52 ? 202 Q8H A SE  1 
HETATM 2237 ZN ZN  . ZN  E 2 .   ? 13.156  15.850  15.495  0.60 14.61 ? 203 ZN  A ZN  1 
HETATM 2238 C  C   . ACT F 4 .   ? 14.630  33.107  9.705   1.00 50.39 ? 204 ACT A C   1 
HETATM 2239 O  O   . ACT F 4 .   ? 13.968  32.681  8.736   1.00 51.84 ? 204 ACT A O   1 
HETATM 2240 O  OXT . ACT F 4 .   ? 14.171  33.872  10.570  1.00 50.88 ? 204 ACT A OXT 1 
HETATM 2241 C  CH3 . ACT F 4 .   ? 16.093  32.681  9.829   1.00 49.97 ? 204 ACT A CH3 1 
HETATM 2242 S  S   . SO4 G 5 .   ? 14.311  18.247  13.627  0.60 18.33 ? 205 SO4 A S   1 
HETATM 2243 O  O1  . SO4 G 5 .   ? 13.582  18.606  12.450  0.60 20.84 ? 205 SO4 A O1  1 
HETATM 2244 O  O2  . SO4 G 5 .   ? 15.376  17.363  13.260  0.60 17.75 ? 205 SO4 A O2  1 
HETATM 2245 O  O3  . SO4 G 5 .   ? 13.416  17.607  14.563  0.60 17.82 ? 205 SO4 A O3  1 
HETATM 2246 O  O4  . SO4 G 5 .   ? 14.886  19.430  14.244  0.60 20.42 ? 205 SO4 A O4  1 
HETATM 2247 N  N1  A Q8H H 3 .   ? -2.820  4.784   5.450   1.00 30.09 ? 201 Q8H F N1  1 
HETATM 2248 C  C2  A Q8H H 3 .   ? -2.476  -4.396  6.674   1.00 28.57 ? 201 Q8H F C2  1 
HETATM 2249 C  C4  A Q8H H 3 .   ? -1.201  -2.578  5.751   1.00 27.11 ? 201 Q8H F C4  1 
HETATM 2250 C  C5  A Q8H H 3 .   ? -1.905  -1.679  6.573   1.00 27.16 ? 201 Q8H F C5  1 
HETATM 2251 C  C6  A Q8H H 3 .   ? -1.605  -0.213  6.519   1.00 26.97 ? 201 Q8H F C6  1 
HETATM 2252 O  O   A Q8H H 3 .   ? -1.024  0.265   5.543   1.00 26.58 ? 201 Q8H F O   1 
HETATM 2253 C  C3  A Q8H H 3 .   ? -1.501  -3.930  5.818   1.00 28.01 ? 201 Q8H F C3  1 
HETATM 2254 C  C1  A Q8H H 3 .   ? -3.173  -3.524  7.483   1.00 28.25 ? 201 Q8H F C1  1 
HETATM 2255 C  C   A Q8H H 3 .   ? -2.902  -2.179  7.428   1.00 28.68 ? 201 Q8H F C   1 
HETATM 2256 N  N   A Q8H H 3 .   ? -1.976  0.522   7.570   1.00 26.19 ? 201 Q8H F N   1 
HETATM 2257 C  C7  A Q8H H 3 .   ? -1.660  1.944   7.664   1.00 26.82 ? 201 Q8H F C7  1 
HETATM 2258 C  C12 A Q8H H 3 .   ? -4.587  3.190   5.605   1.00 30.87 ? 201 Q8H F C12 1 
HETATM 2259 C  C11 A Q8H H 3 .   ? -4.054  4.367   5.143   1.00 30.75 ? 201 Q8H F C11 1 
HETATM 2260 C  C10 A Q8H H 3 .   ? -2.090  3.992   6.261   1.00 28.11 ? 201 Q8H F C10 1 
HETATM 2261 C  C9  A Q8H H 3 .   ? -3.817  2.393   6.421   1.00 29.95 ? 201 Q8H F C9  1 
HETATM 2262 C  C8  A Q8H H 3 .   ? -2.536  2.786   6.768   1.00 28.15 ? 201 Q8H F C8  1 
HETATM 2263 SE SE  A Q8H H 3 .   ? 0.175   -1.985  4.542   1.00 25.87 ? 201 Q8H F SE  1 
HETATM 2264 ZN ZN  . ZN  I 2 .   ? 10.216  -19.204 5.093   1.00 13.34 ? 202 ZN  F ZN  1 
HETATM 2265 ZN ZN  . ZN  J 2 .   ? 15.662  -16.138 8.221   0.60 14.02 ? 203 ZN  F ZN  1 
HETATM 2266 SE SE  B SE  K 6 .   ? 2.140   -1.103  4.611   0.40 28.15 ? 204 SE  F SE  1 
HETATM 2267 S  S   . SO4 L 5 .   ? 15.778  -18.560 10.355  0.50 15.46 ? 205 SO4 F S   1 
HETATM 2268 O  O1  . SO4 L 5 .   ? 16.812  -19.526 10.038  0.50 16.47 ? 205 SO4 F O1  1 
HETATM 2269 O  O2  . SO4 L 5 .   ? 15.407  -17.875 9.142   0.50 15.39 ? 205 SO4 F O2  1 
HETATM 2270 O  O3  . SO4 L 5 .   ? 14.634  -19.239 10.887  0.50 18.87 ? 205 SO4 F O3  1 
HETATM 2271 O  O4  . SO4 L 5 .   ? 16.290  -17.640 11.327  0.50 15.69 ? 205 SO4 F O4  1 
HETATM 2272 O  O   . HOH M 7 .   ? 31.338  9.017   23.699  1.00 36.53 ? 301 HOH A O   1 
HETATM 2273 O  O   . HOH M 7 .   ? 13.684  20.066  16.909  1.00 28.55 ? 302 HOH A O   1 
HETATM 2274 O  O   . HOH M 7 .   ? 12.884  33.526  12.672  1.00 43.23 ? 303 HOH A O   1 
HETATM 2275 O  O   . HOH M 7 .   ? 18.285  2.688   12.442  1.00 27.69 ? 304 HOH A O   1 
HETATM 2276 O  O   . HOH M 7 .   ? 20.787  18.436  28.176  1.00 40.24 ? 305 HOH A O   1 
HETATM 2277 O  O   . HOH M 7 .   ? 24.592  11.128  19.574  1.00 27.51 ? 306 HOH A O   1 
HETATM 2278 O  O   . HOH M 7 .   ? 4.914   3.729   31.776  1.00 36.19 ? 307 HOH A O   1 
HETATM 2279 O  O   . HOH M 7 .   ? 23.958  14.745  17.092  1.00 39.10 ? 308 HOH A O   1 
HETATM 2280 O  O   . HOH M 7 .   ? -3.137  -2.383  10.721  1.00 38.41 ? 309 HOH A O   1 
HETATM 2281 O  O   . HOH M 7 .   ? 23.871  12.051  7.735   1.00 34.13 ? 310 HOH A O   1 
HETATM 2282 O  O   . HOH M 7 .   ? 20.621  8.201   2.538   1.00 28.13 ? 311 HOH A O   1 
HETATM 2283 O  O   . HOH M 7 .   ? -3.005  -3.022  25.305  1.00 41.88 ? 312 HOH A O   1 
HETATM 2284 O  O   . HOH M 7 .   ? 18.230  1.188   15.742  1.00 25.20 ? 313 HOH A O   1 
HETATM 2285 O  O   . HOH M 7 .   ? 1.031   12.738  24.885  1.00 25.70 ? 314 HOH A O   1 
HETATM 2286 O  O   . HOH M 7 .   ? 1.283   24.580  18.188  1.00 32.60 ? 315 HOH A O   1 
HETATM 2287 O  O   . HOH M 7 .   ? -2.327  -1.835  12.906  1.00 36.72 ? 316 HOH A O   1 
HETATM 2288 O  O   . HOH M 7 .   ? 18.308  15.993  37.903  1.00 21.94 ? 317 HOH A O   1 
HETATM 2289 O  O   . HOH M 7 .   ? -5.483  -2.344  14.743  1.00 43.77 ? 318 HOH A O   1 
HETATM 2290 O  O   . HOH M 7 .   ? 1.226   -9.678  22.214  1.00 49.29 ? 319 HOH A O   1 
HETATM 2291 O  O   . HOH M 7 .   ? 15.629  24.289  22.864  1.00 31.31 ? 320 HOH A O   1 
HETATM 2292 O  O   . HOH M 7 .   ? -0.151  8.553   6.749   1.00 36.36 ? 321 HOH A O   1 
HETATM 2293 O  O   . HOH M 7 .   ? 13.694  8.090   2.123   1.00 21.65 ? 322 HOH A O   1 
HETATM 2294 O  O   . HOH M 7 .   ? 25.043  9.325   16.103  1.00 31.74 ? 323 HOH A O   1 
HETATM 2295 O  O   . HOH M 7 .   ? 9.014   9.249   32.937  1.00 36.64 ? 324 HOH A O   1 
HETATM 2296 O  O   . HOH M 7 .   ? 17.356  15.604  7.976   1.00 27.77 ? 325 HOH A O   1 
HETATM 2297 O  O   . HOH M 7 .   ? 3.402   4.705   9.174   1.00 20.10 ? 326 HOH A O   1 
HETATM 2298 O  O   . HOH M 7 .   ? -4.041  -0.312  16.816  1.00 39.06 ? 327 HOH A O   1 
HETATM 2299 O  O   . HOH M 7 .   ? -3.491  9.975   25.711  1.00 29.03 ? 328 HOH A O   1 
HETATM 2300 O  O   . HOH M 7 .   ? -3.799  17.142  20.359  1.00 31.63 ? 329 HOH A O   1 
HETATM 2301 O  O   . HOH M 7 .   ? 20.357  19.372  38.461  1.00 19.58 ? 330 HOH A O   1 
HETATM 2302 O  O   . HOH M 7 .   ? 11.508  16.680  33.653  1.00 27.78 ? 331 HOH A O   1 
HETATM 2303 O  O   . HOH M 7 .   ? -4.473  7.091   18.991  1.00 29.26 ? 332 HOH A O   1 
HETATM 2304 O  O   . HOH M 7 .   ? -6.180  4.745   14.727  1.00 24.58 ? 333 HOH A O   1 
HETATM 2305 O  O   . HOH M 7 .   ? 12.135  5.329   36.782  1.00 36.33 ? 334 HOH A O   1 
HETATM 2306 O  O   . HOH M 7 .   ? 19.544  3.357   14.567  1.00 29.10 ? 335 HOH A O   1 
HETATM 2307 O  O   . HOH M 7 .   ? -1.559  16.647  13.504  1.00 22.33 ? 336 HOH A O   1 
HETATM 2308 O  O   . HOH M 7 .   ? -4.737  9.059   4.370   1.00 24.33 ? 337 HOH A O   1 
HETATM 2309 O  O   . HOH M 7 .   ? 14.156  -0.255  15.857  1.00 11.32 ? 338 HOH A O   1 
HETATM 2310 O  O   . HOH M 7 .   ? 5.824   13.804  26.141  1.00 25.56 ? 339 HOH A O   1 
HETATM 2311 O  O   . HOH M 7 .   ? -3.078  15.541  22.837  1.00 31.13 ? 340 HOH A O   1 
HETATM 2312 O  O   . HOH M 7 .   ? -2.529  16.683  5.009   1.00 20.85 ? 341 HOH A O   1 
HETATM 2313 O  O   . HOH M 7 .   ? 6.945   18.108  9.435   1.00 27.16 ? 342 HOH A O   1 
HETATM 2314 O  O   . HOH M 7 .   ? 0.104   15.911  11.380  1.00 17.56 ? 343 HOH A O   1 
HETATM 2315 O  O   . HOH M 7 .   ? 5.420   19.555  7.993   1.00 31.03 ? 344 HOH A O   1 
HETATM 2316 O  O   . HOH M 7 .   ? 18.002  17.766  12.656  1.00 34.22 ? 345 HOH A O   1 
HETATM 2317 O  O   . HOH M 7 .   ? 13.948  10.175  33.536  1.00 29.19 ? 346 HOH A O   1 
HETATM 2318 O  O   . HOH M 7 .   ? 7.679   12.825  28.220  1.00 26.89 ? 347 HOH A O   1 
HETATM 2319 O  O   . HOH M 7 .   ? 16.534  8.430   35.088  1.00 40.05 ? 348 HOH A O   1 
HETATM 2320 O  O   . HOH M 7 .   ? -5.571  2.045   23.382  1.00 22.87 ? 349 HOH A O   1 
HETATM 2321 O  O   . HOH M 7 .   ? 2.288   25.582  20.749  1.00 40.69 ? 350 HOH A O   1 
HETATM 2322 O  O   . HOH M 7 .   ? 20.232  12.299  5.013   1.00 26.16 ? 351 HOH A O   1 
HETATM 2323 O  O   . HOH M 7 .   ? -4.076  17.316  17.415  1.00 33.58 ? 352 HOH A O   1 
HETATM 2324 O  O   . HOH M 7 .   ? 24.892  12.564  24.916  1.00 34.48 ? 353 HOH A O   1 
HETATM 2325 O  O   . HOH M 7 .   ? 12.799  30.150  22.547  1.00 40.86 ? 354 HOH A O   1 
HETATM 2326 O  O   . HOH M 7 .   ? 9.756   3.983   31.837  1.00 34.54 ? 355 HOH A O   1 
HETATM 2327 O  O   . HOH M 7 .   ? -4.839  6.689   12.331  1.00 21.23 ? 356 HOH A O   1 
HETATM 2328 O  O   . HOH M 7 .   ? 23.762  5.624   35.041  1.00 40.93 ? 357 HOH A O   1 
HETATM 2329 O  O   . HOH M 7 .   ? 22.732  10.348  15.394  1.00 35.85 ? 358 HOH A O   1 
HETATM 2330 O  O   . HOH M 7 .   ? -6.737  6.189   8.471   1.00 35.00 ? 359 HOH A O   1 
HETATM 2331 O  O   . HOH M 7 .   ? 1.233   22.399  25.552  1.00 42.11 ? 360 HOH A O   1 
HETATM 2332 O  O   . HOH M 7 .   ? 6.748   18.140  20.499  1.00 20.34 ? 361 HOH A O   1 
HETATM 2333 O  O   . HOH M 7 .   ? 15.991  2.449   7.193   1.00 14.76 ? 362 HOH A O   1 
HETATM 2334 O  O   . HOH M 7 .   ? 11.346  -4.263  24.071  1.00 29.57 ? 363 HOH A O   1 
HETATM 2335 O  O   . HOH M 7 .   ? 22.679  16.769  24.491  1.00 25.82 ? 364 HOH A O   1 
HETATM 2336 O  O   . HOH M 7 .   ? -5.545  18.281  7.657   1.00 25.03 ? 365 HOH A O   1 
HETATM 2337 O  O   . HOH M 7 .   ? 26.649  9.485   25.487  1.00 35.56 ? 366 HOH A O   1 
HETATM 2338 O  O   . HOH M 7 .   ? 7.163   -3.355  22.490  1.00 24.91 ? 367 HOH A O   1 
HETATM 2339 O  O   . HOH M 7 .   ? 22.680  14.131  25.289  1.00 26.79 ? 368 HOH A O   1 
HETATM 2340 O  O   . HOH M 7 .   ? 9.930   14.902  29.856  1.00 31.82 ? 369 HOH A O   1 
HETATM 2341 O  O   . HOH M 7 .   ? 2.340   19.744  25.237  1.00 26.40 ? 370 HOH A O   1 
HETATM 2342 O  O   . HOH M 7 .   ? 19.622  10.645  2.768   1.00 23.32 ? 371 HOH A O   1 
HETATM 2343 O  O   . HOH M 7 .   ? 20.322  10.843  38.339  1.00 34.98 ? 372 HOH A O   1 
HETATM 2344 O  O   . HOH M 7 .   ? 1.445   -6.244  17.783  1.00 20.90 ? 373 HOH A O   1 
HETATM 2345 O  O   . HOH M 7 .   ? -8.699  -2.004  17.594  1.00 33.90 ? 374 HOH A O   1 
HETATM 2346 O  O   . HOH M 7 .   ? 0.536   -7.879  19.813  1.00 35.52 ? 375 HOH A O   1 
HETATM 2347 O  O   . HOH M 7 .   ? 20.864  20.067  25.694  1.00 32.72 ? 376 HOH A O   1 
HETATM 2348 O  O   . HOH M 7 .   ? -2.299  13.069  23.386  1.00 25.20 ? 377 HOH A O   1 
HETATM 2349 O  O   . HOH M 7 .   ? 13.644  18.562  9.568   1.00 24.94 ? 378 HOH A O   1 
HETATM 2350 O  O   . HOH M 7 .   ? 2.686   -9.019  16.073  1.00 22.40 ? 379 HOH A O   1 
HETATM 2351 O  O   . HOH M 7 .   ? 7.502   12.871  1.416   1.00 31.19 ? 380 HOH A O   1 
HETATM 2352 O  O   . HOH M 7 .   ? 24.524  18.130  34.234  1.00 35.88 ? 381 HOH A O   1 
HETATM 2353 O  O   . HOH M 7 .   ? 11.318  11.163  30.261  1.00 27.88 ? 382 HOH A O   1 
HETATM 2354 O  O   . HOH M 7 .   ? 16.141  0.754   13.427  1.00 18.60 ? 383 HOH A O   1 
HETATM 2355 O  O   . HOH M 7 .   ? 5.476   9.494   4.033   1.00 30.07 ? 384 HOH A O   1 
HETATM 2356 O  O   . HOH M 7 .   ? 21.566  15.698  13.377  1.00 26.25 ? 385 HOH A O   1 
HETATM 2357 O  O   . HOH M 7 .   ? 30.268  6.837   26.940  1.00 37.04 ? 386 HOH A O   1 
HETATM 2358 O  O   . HOH M 7 .   ? 0.804   6.508   8.463   1.00 27.41 ? 387 HOH A O   1 
HETATM 2359 O  O   . HOH M 7 .   ? 17.431  23.183  25.106  1.00 33.96 ? 388 HOH A O   1 
HETATM 2360 O  O   . HOH M 7 .   ? -4.184  0.148   9.769   1.00 26.77 ? 389 HOH A O   1 
HETATM 2361 O  O   . HOH M 7 .   ? 5.085   -2.884  23.303  1.00 28.31 ? 390 HOH A O   1 
HETATM 2362 O  O   . HOH M 7 .   ? 24.795  16.060  31.873  1.00 30.83 ? 391 HOH A O   1 
HETATM 2363 O  O   . HOH M 7 .   ? 14.675  10.783  2.983   1.00 22.89 ? 392 HOH A O   1 
HETATM 2364 O  O   . HOH M 7 .   ? 19.000  16.333  10.692  1.00 45.30 ? 393 HOH A O   1 
HETATM 2365 O  O   . HOH M 7 .   ? 15.354  36.611  10.591  1.00 26.95 ? 394 HOH A O   1 
HETATM 2366 O  O   . HOH M 7 .   ? -3.170  24.571  19.518  1.00 37.80 ? 395 HOH A O   1 
HETATM 2367 O  O   . HOH M 7 .   ? -7.067  -1.031  13.109  1.00 42.62 ? 396 HOH A O   1 
HETATM 2368 O  O   . HOH M 7 .   ? -9.005  -4.322  20.413  1.00 44.11 ? 397 HOH A O   1 
HETATM 2369 O  O   . HOH M 7 .   ? -5.050  -1.727  18.729  1.00 27.34 ? 398 HOH A O   1 
HETATM 2370 O  O   . HOH M 7 .   ? -2.484  12.321  26.259  1.00 32.21 ? 399 HOH A O   1 
HETATM 2371 O  O   . HOH M 7 .   ? 0.057   21.057  3.232   1.00 37.31 ? 400 HOH A O   1 
HETATM 2372 O  O   . HOH M 7 .   ? 23.082  9.617   12.612  1.00 37.94 ? 401 HOH A O   1 
HETATM 2373 O  O   . HOH M 7 .   ? -7.354  8.410   20.186  1.00 35.44 ? 402 HOH A O   1 
HETATM 2374 O  O   . HOH M 7 .   ? 26.163  12.101  22.514  1.00 36.01 ? 403 HOH A O   1 
HETATM 2375 O  O   . HOH M 7 .   ? 9.500   19.238  10.752  1.00 25.07 ? 404 HOH A O   1 
HETATM 2376 O  O   . HOH M 7 .   ? 14.107  30.463  12.905  1.00 30.28 ? 405 HOH A O   1 
HETATM 2377 O  O   . HOH M 7 .   ? -4.465  23.549  22.103  1.00 41.13 ? 406 HOH A O   1 
HETATM 2378 O  O   . HOH M 7 .   ? -9.930  -1.910  15.798  1.00 44.47 ? 407 HOH A O   1 
HETATM 2379 O  O   . HOH M 7 .   ? -0.750  12.427  28.553  1.00 33.24 ? 408 HOH A O   1 
HETATM 2380 O  O   . HOH M 7 .   ? 20.446  0.554   21.416  1.00 48.50 ? 409 HOH A O   1 
HETATM 2381 O  O   . HOH M 7 .   ? 22.645  21.126  38.277  1.00 35.09 ? 410 HOH A O   1 
HETATM 2382 O  O   . HOH M 7 .   ? -2.922  1.329   25.125  1.00 40.78 ? 411 HOH A O   1 
HETATM 2383 O  O   . HOH M 7 .   ? 8.191   18.655  27.713  1.00 32.17 ? 412 HOH A O   1 
HETATM 2384 O  O   . HOH M 7 .   ? -0.655  -0.956  27.240  1.00 39.72 ? 413 HOH A O   1 
HETATM 2385 O  O   . HOH M 7 .   ? 2.123   11.725  28.421  1.00 25.71 ? 414 HOH A O   1 
HETATM 2386 O  O   . HOH M 7 .   ? 17.435  23.011  15.703  1.00 38.99 ? 415 HOH A O   1 
HETATM 2387 O  O   . HOH M 7 .   ? 8.575   10.618  29.378  1.00 20.23 ? 416 HOH A O   1 
HETATM 2388 O  O   . HOH M 7 .   ? 1.779   -11.164 17.412  1.00 34.70 ? 417 HOH A O   1 
HETATM 2389 O  O   . HOH M 7 .   ? -9.816  4.523   15.029  1.00 42.40 ? 418 HOH A O   1 
HETATM 2390 O  O   . HOH M 7 .   ? -0.598  -7.337  21.977  1.00 36.59 ? 419 HOH A O   1 
HETATM 2391 O  O   . HOH M 7 .   ? 11.979  2.466   32.316  1.00 33.77 ? 420 HOH A O   1 
HETATM 2392 O  O   . HOH M 7 .   ? 25.759  9.703   6.234   1.00 37.45 ? 421 HOH A O   1 
HETATM 2393 O  O   . HOH M 7 .   ? 6.481   16.943  26.718  1.00 23.39 ? 422 HOH A O   1 
HETATM 2394 O  O   . HOH M 7 .   ? -0.142  19.100  1.884   1.00 32.39 ? 423 HOH A O   1 
HETATM 2395 O  O   . HOH M 7 .   ? 29.771  10.685  20.468  1.00 44.64 ? 424 HOH A O   1 
HETATM 2396 O  O   . HOH M 7 .   ? 17.061  9.801   2.049   1.00 33.24 ? 425 HOH A O   1 
HETATM 2397 O  O   . HOH M 7 .   ? 18.231  4.467   35.959  1.00 42.48 ? 426 HOH A O   1 
HETATM 2398 O  O   . HOH M 7 .   ? 5.086   8.418   34.706  1.00 43.64 ? 427 HOH A O   1 
HETATM 2399 O  O   . HOH M 7 .   ? 8.708   16.797  29.538  1.00 41.91 ? 428 HOH A O   1 
HETATM 2400 O  O   . HOH M 7 .   ? 9.411   13.665  31.759  1.00 36.66 ? 429 HOH A O   1 
HETATM 2401 O  O   . HOH M 7 .   ? -7.250  3.430   12.362  1.00 42.84 ? 430 HOH A O   1 
HETATM 2402 O  O   . HOH M 7 .   ? -6.401  13.316  20.616  1.00 44.65 ? 431 HOH A O   1 
HETATM 2403 O  O   . HOH M 7 .   ? -4.596  8.996   27.812  1.00 38.16 ? 432 HOH A O   1 
HETATM 2404 O  O   . HOH M 7 .   ? -7.317  6.856   10.677  1.00 43.04 ? 433 HOH A O   1 
HETATM 2405 O  O   . HOH M 7 .   ? -5.389  13.982  15.177  1.00 33.90 ? 434 HOH A O   1 
HETATM 2406 O  O   . HOH M 7 .   ? 1.672   4.823   31.064  1.00 41.34 ? 435 HOH A O   1 
HETATM 2407 O  O   . HOH M 7 .   ? 15.023  29.584  10.989  1.00 42.19 ? 436 HOH A O   1 
HETATM 2408 O  O   . HOH M 7 .   ? 24.434  6.651   11.659  1.00 43.70 ? 437 HOH A O   1 
HETATM 2409 O  O   . HOH M 7 .   ? -5.922  7.695   14.698  1.00 29.18 ? 438 HOH A O   1 
HETATM 2410 O  O   . HOH M 7 .   ? 24.155  14.979  6.386   1.00 33.90 ? 439 HOH A O   1 
HETATM 2411 O  O   . HOH M 7 .   ? -9.091  11.782  23.274  1.00 41.13 ? 440 HOH A O   1 
HETATM 2412 O  O   . HOH M 7 .   ? 7.116   2.532   32.170  1.00 37.93 ? 441 HOH A O   1 
HETATM 2413 O  O   . HOH M 7 .   ? 0.152   2.151   31.982  1.00 43.06 ? 442 HOH A O   1 
HETATM 2414 O  O   . HOH M 7 .   ? -5.740  -10.030 20.254  1.00 44.90 ? 443 HOH A O   1 
HETATM 2415 O  O   . HOH M 7 .   ? 25.104  12.730  13.985  1.00 43.94 ? 444 HOH A O   1 
HETATM 2416 O  O   . HOH M 7 .   ? 25.884  12.497  17.838  1.00 40.95 ? 445 HOH A O   1 
HETATM 2417 O  O   . HOH M 7 .   ? 22.279  20.739  13.892  1.00 36.73 ? 446 HOH A O   1 
HETATM 2418 O  O   . HOH M 7 .   ? 13.920  1.864   36.630  1.00 37.11 ? 447 HOH A O   1 
HETATM 2419 O  O   . HOH M 7 .   ? 3.963   18.555  27.525  1.00 37.06 ? 448 HOH A O   1 
HETATM 2420 O  O   . HOH M 7 .   ? 27.132  13.475  26.163  1.00 41.49 ? 449 HOH A O   1 
HETATM 2421 O  O   . HOH M 7 .   ? -3.589  15.885  14.986  1.00 30.51 ? 450 HOH A O   1 
HETATM 2422 O  O   . HOH M 7 .   ? 3.115   13.497  26.611  1.00 24.61 ? 451 HOH A O   1 
HETATM 2423 O  O   . HOH M 7 .   ? -3.347  15.799  26.043  1.00 37.17 ? 452 HOH A O   1 
HETATM 2424 O  O   . HOH M 7 .   ? -7.920  2.210   24.911  1.00 32.38 ? 453 HOH A O   1 
HETATM 2425 O  O   . HOH M 7 .   ? 2.159   15.723  27.612  1.00 37.02 ? 454 HOH A O   1 
HETATM 2426 O  O   . HOH M 7 .   ? 30.765  4.337   27.003  1.00 42.43 ? 455 HOH A O   1 
HETATM 2427 O  O   . HOH M 7 .   ? -3.261  -10.817 19.519  1.00 40.99 ? 456 HOH A O   1 
HETATM 2428 O  O   . HOH M 7 .   ? -4.824  3.081   32.160  1.00 47.90 ? 457 HOH A O   1 
HETATM 2429 O  O   . HOH M 7 .   ? 4.762   -4.852  30.128  1.00 35.55 ? 458 HOH A O   1 
HETATM 2430 O  O   . HOH M 7 .   ? -1.512  0.330   30.423  1.00 44.78 ? 459 HOH A O   1 
HETATM 2431 O  O   . HOH M 7 .   ? -0.887  -0.758  32.573  1.00 42.92 ? 460 HOH A O   1 
HETATM 2432 O  O   . HOH M 7 .   ? 20.978  2.782   32.260  1.00 44.47 ? 461 HOH A O   1 
HETATM 2433 O  O   . HOH M 7 .   ? 5.517   16.036  29.978  1.00 36.76 ? 462 HOH A O   1 
HETATM 2434 O  O   . HOH M 7 .   ? -2.702  -7.165  8.641   1.00 31.64 ? 463 HOH A O   1 
HETATM 2435 O  O   . HOH M 7 .   ? 22.670  18.023  11.680  1.00 46.37 ? 464 HOH A O   1 
HETATM 2436 O  O   . HOH M 7 .   ? -0.556  4.349   33.901  1.00 41.47 ? 465 HOH A O   1 
HETATM 2437 O  O   . HOH M 7 .   ? -0.920  12.416  32.451  1.00 39.25 ? 466 HOH A O   1 
HETATM 2438 O  O   . HOH N 7 .   ? -2.743  -17.986 8.764   1.00 27.80 ? 301 HOH F O   1 
HETATM 2439 O  O   . HOH N 7 .   ? 13.900  -15.469 16.728  1.00 31.44 ? 302 HOH F O   1 
HETATM 2440 O  O   . HOH N 7 .   ? 17.060  -20.356 7.459   1.00 25.02 ? 303 HOH F O   1 
HETATM 2441 O  O   . HOH N 7 .   ? -2.614  -24.892 -4.613  1.00 35.04 ? 304 HOH F O   1 
HETATM 2442 O  O   . HOH N 7 .   ? 5.319   -28.540 -1.739  1.00 35.35 ? 305 HOH F O   1 
HETATM 2443 O  O   . HOH N 7 .   ? 2.318   -0.017  -2.407  1.00 35.42 ? 306 HOH F O   1 
HETATM 2444 O  O   . HOH N 7 .   ? 12.246  -18.715 11.593  1.00 33.32 ? 307 HOH F O   1 
HETATM 2445 O  O   . HOH N 7 .   ? 17.299  -22.423 10.375  1.00 40.05 ? 308 HOH F O   1 
HETATM 2446 O  O   . HOH N 7 .   ? 11.634  -24.877 -3.866  1.00 33.94 ? 309 HOH F O   1 
HETATM 2447 O  O   . HOH N 7 .   ? 18.055  -18.052 13.138  1.00 31.34 ? 310 HOH F O   1 
HETATM 2448 O  O   . HOH N 7 .   ? 21.250  -4.254  -7.523  1.00 31.97 ? 311 HOH F O   1 
HETATM 2449 O  O   . HOH N 7 .   ? 2.859   -7.742  -4.382  1.00 30.98 ? 312 HOH F O   1 
HETATM 2450 O  O   . HOH N 7 .   ? 1.906   -18.331 -2.475  1.00 26.24 ? 313 HOH F O   1 
HETATM 2451 O  O   . HOH N 7 .   ? -0.828  2.376   -0.886  1.00 48.40 ? 314 HOH F O   1 
HETATM 2452 O  O   . HOH N 7 .   ? 28.340  -21.492 12.111  1.00 38.57 ? 315 HOH F O   1 
HETATM 2453 O  O   . HOH N 7 .   ? 27.247  -13.583 -9.139  1.00 39.47 ? 316 HOH F O   1 
HETATM 2454 O  O   . HOH N 7 .   ? 19.541  -1.589  10.858  1.00 23.71 ? 317 HOH F O   1 
HETATM 2455 O  O   . HOH N 7 .   ? 30.792  -12.855 6.549   1.00 29.42 ? 318 HOH F O   1 
HETATM 2456 O  O   . HOH N 7 .   ? -4.103  -7.688  5.992   1.00 44.46 ? 319 HOH F O   1 
HETATM 2457 O  O   . HOH N 7 .   ? 7.308   -10.474 -9.360  1.00 32.87 ? 320 HOH F O   1 
HETATM 2458 O  O   . HOH N 7 .   ? 2.459   1.518   2.945   1.00 35.70 ? 321 HOH F O   1 
HETATM 2459 O  O   . HOH N 7 .   ? 7.360   7.387   -2.320  1.00 40.26 ? 322 HOH F O   1 
HETATM 2460 O  O   . HOH N 7 .   ? 15.400  -14.280 -4.668  1.00 23.48 ? 323 HOH F O   1 
HETATM 2461 O  O   . HOH N 7 .   ? 19.821  -3.564  18.224  1.00 41.19 ? 324 HOH F O   1 
HETATM 2462 O  O   . HOH N 7 .   ? 17.907  -13.206 -5.370  1.00 26.15 ? 325 HOH F O   1 
HETATM 2463 O  O   . HOH N 7 .   ? 27.114  -5.162  10.665  1.00 25.89 ? 326 HOH F O   1 
HETATM 2464 O  O   . HOH N 7 .   ? 0.721   2.174   4.991   1.00 35.51 ? 327 HOH F O   1 
HETATM 2465 O  O   . HOH N 7 .   ? 10.725  -13.136 -6.304  1.00 20.43 ? 328 HOH F O   1 
HETATM 2466 O  O   . HOH N 7 .   ? 8.579   -8.364  19.374  1.00 22.35 ? 329 HOH F O   1 
HETATM 2467 O  O   . HOH N 7 .   ? -2.391  -8.702  -8.125  1.00 37.22 ? 330 HOH F O   1 
HETATM 2468 O  O   . HOH N 7 .   ? -0.587  -18.916 0.606   1.00 41.05 ? 331 HOH F O   1 
HETATM 2469 O  O   . HOH N 7 .   ? 2.911   -13.582 16.264  1.00 31.59 ? 332 HOH F O   1 
HETATM 2470 O  O   . HOH N 7 .   ? -2.225  -0.207  3.206   1.00 30.78 ? 333 HOH F O   1 
HETATM 2471 O  O   . HOH N 7 .   ? 7.651   -21.467 -10.306 1.00 35.87 ? 334 HOH F O   1 
HETATM 2472 O  O   . HOH N 7 .   ? -2.104  -21.193 11.483  1.00 36.39 ? 335 HOH F O   1 
HETATM 2473 O  O   . HOH N 7 .   ? 16.387  -0.039  8.420   1.00 13.07 ? 336 HOH F O   1 
HETATM 2474 O  O   . HOH N 7 .   ? 23.818  -17.199 -7.835  1.00 27.73 ? 337 HOH F O   1 
HETATM 2475 O  O   . HOH N 7 .   ? 21.715  -24.675 3.630   1.00 29.94 ? 338 HOH F O   1 
HETATM 2476 O  O   . HOH N 7 .   ? 3.117   -4.093  7.936   1.00 24.68 ? 339 HOH F O   1 
HETATM 2477 O  O   . HOH N 7 .   ? 27.460  -9.165  10.547  1.00 40.51 ? 340 HOH F O   1 
HETATM 2478 O  O   . HOH N 7 .   ? 5.236   -17.438 -5.379  1.00 22.19 ? 341 HOH F O   1 
HETATM 2479 O  O   . HOH N 7 .   ? 2.523   -16.737 4.549   1.00 15.45 ? 342 HOH F O   1 
HETATM 2480 O  O   . HOH N 7 .   ? 4.087   -2.572  -8.629  1.00 26.77 ? 343 HOH F O   1 
HETATM 2481 O  O   . HOH N 7 .   ? 7.670   -25.307 -0.034  1.00 27.58 ? 344 HOH F O   1 
HETATM 2482 O  O   . HOH N 7 .   ? 14.388  3.192   -1.009  1.00 25.69 ? 345 HOH F O   1 
HETATM 2483 O  O   . HOH N 7 .   ? 18.389  -28.200 13.702  1.00 46.78 ? 346 HOH F O   1 
HETATM 2484 O  O   . HOH N 7 .   ? 19.132  -1.301  15.744  1.00 36.05 ? 347 HOH F O   1 
HETATM 2485 O  O   . HOH N 7 .   ? 28.589  -16.963 5.881   1.00 23.84 ? 348 HOH F O   1 
HETATM 2486 O  O   . HOH N 7 .   ? 33.880  -20.019 -7.267  1.00 20.35 ? 349 HOH F O   1 
HETATM 2487 O  O   . HOH N 7 .   ? 20.081  -27.662 3.373   1.00 27.03 ? 350 HOH F O   1 
HETATM 2488 O  O   . HOH N 7 .   ? 9.580   -28.817 -0.662  1.00 33.55 ? 351 HOH F O   1 
HETATM 2489 O  O   . HOH N 7 .   ? 33.858  -8.819  -8.450  1.00 37.42 ? 352 HOH F O   1 
HETATM 2490 O  O   . HOH N 7 .   ? 20.084  -3.665  12.677  1.00 27.62 ? 353 HOH F O   1 
HETATM 2491 O  O   . HOH N 7 .   ? 6.826   5.754   -0.100  1.00 20.72 ? 354 HOH F O   1 
HETATM 2492 O  O   . HOH N 7 .   ? 12.987  -30.947 1.618   1.00 26.38 ? 355 HOH F O   1 
HETATM 2493 O  O   . HOH N 7 .   ? 20.766  -15.082 -5.769  1.00 26.61 ? 356 HOH F O   1 
HETATM 2494 O  O   . HOH N 7 .   ? 2.331   -17.316 1.961   1.00 18.69 ? 357 HOH F O   1 
HETATM 2495 O  O   . HOH N 7 .   ? 11.095  -22.558 -7.176  1.00 30.62 ? 358 HOH F O   1 
HETATM 2496 O  O   . HOH N 7 .   ? -0.796  -6.964  6.006   1.00 29.91 ? 359 HOH F O   1 
HETATM 2497 O  O   . HOH N 7 .   ? 6.759   -23.322 7.974   1.00 26.67 ? 360 HOH F O   1 
HETATM 2498 O  O   . HOH N 7 .   ? 5.391   -20.261 10.350  1.00 27.97 ? 361 HOH F O   1 
HETATM 2499 O  O   . HOH N 7 .   ? 7.148   10.589  -0.001  1.00 34.25 ? 362 HOH F O   1 
HETATM 2500 O  O   . HOH N 7 .   ? 10.041  -10.806 19.335  1.00 32.98 ? 363 HOH F O   1 
HETATM 2501 O  O   . HOH N 7 .   ? 13.066  -18.422 0.610   1.00 15.38 ? 364 HOH F O   1 
HETATM 2502 O  O   . HOH N 7 .   ? 14.855  -36.748 6.271   1.00 28.61 ? 365 HOH F O   1 
HETATM 2503 O  O   . HOH N 7 .   ? 21.783  -9.502  -8.948  1.00 33.97 ? 366 HOH F O   1 
HETATM 2504 O  O   . HOH N 7 .   ? 18.597  3.971   -0.045  1.00 30.80 ? 367 HOH F O   1 
HETATM 2505 O  O   . HOH N 7 .   ? 2.364   -25.876 -3.887  1.00 31.82 ? 368 HOH F O   1 
HETATM 2506 O  O   . HOH N 7 .   ? 15.965  -7.606  14.477  1.00 29.14 ? 369 HOH F O   1 
HETATM 2507 O  O   . HOH N 7 .   ? 15.745  -12.497 20.871  1.00 29.04 ? 370 HOH F O   1 
HETATM 2508 O  O   . HOH N 7 .   ? 26.176  -10.389 -6.648  1.00 32.67 ? 371 HOH F O   1 
HETATM 2509 O  O   . HOH N 7 .   ? 1.099   -6.806  7.778   1.00 18.72 ? 372 HOH F O   1 
HETATM 2510 O  O   . HOH N 7 .   ? 28.947  -14.317 5.083   1.00 20.08 ? 373 HOH F O   1 
HETATM 2511 O  O   . HOH N 7 .   ? -1.581  -5.905  -1.536  1.00 37.10 ? 374 HOH F O   1 
HETATM 2512 O  O   . HOH N 7 .   ? 25.888  -3.158  14.094  1.00 30.71 ? 375 HOH F O   1 
HETATM 2513 O  O   . HOH N 7 .   ? 13.217  -2.761  16.778  1.00 14.27 ? 376 HOH F O   1 
HETATM 2514 O  O   . HOH N 7 .   ? 34.274  -16.094 0.551   1.00 27.73 ? 377 HOH F O   1 
HETATM 2515 O  O   . HOH N 7 .   ? -4.392  -1.372  3.701   1.00 38.81 ? 378 HOH F O   1 
HETATM 2516 O  O   . HOH N 7 .   ? 36.242  -14.650 -1.028  1.00 37.49 ? 379 HOH F O   1 
HETATM 2517 O  O   . HOH N 7 .   ? 7.168   -2.138  -8.710  1.00 31.49 ? 380 HOH F O   1 
HETATM 2518 O  O   . HOH N 7 .   ? 12.828  2.551   -2.811  1.00 28.38 ? 381 HOH F O   1 
HETATM 2519 O  O   . HOH N 7 .   ? 11.969  -20.204 -5.889  1.00 24.85 ? 382 HOH F O   1 
HETATM 2520 O  O   . HOH N 7 .   ? 29.135  -8.915  -6.680  1.00 34.95 ? 383 HOH F O   1 
HETATM 2521 O  O   . HOH N 7 .   ? 6.768   8.460   1.993   1.00 26.49 ? 384 HOH F O   1 
HETATM 2522 O  O   . HOH N 7 .   ? 2.992   -2.628  -11.150 1.00 41.38 ? 385 HOH F O   1 
HETATM 2523 O  O   . HOH N 7 .   ? 7.220   -13.540 -6.798  1.00 20.97 ? 386 HOH F O   1 
HETATM 2524 O  O   . HOH N 7 .   ? 2.959   -9.877  13.416  1.00 22.69 ? 387 HOH F O   1 
HETATM 2525 O  O   . HOH N 7 .   ? 19.712  -23.326 9.985   1.00 24.80 ? 388 HOH F O   1 
HETATM 2526 O  O   . HOH N 7 .   ? 13.421  -11.954 -8.637  1.00 24.61 ? 389 HOH F O   1 
HETATM 2527 O  O   . HOH N 7 .   ? 10.322  8.000   -8.596  1.00 36.77 ? 390 HOH F O   1 
HETATM 2528 O  O   . HOH N 7 .   ? -4.702  -13.222 1.737   1.00 29.33 ? 391 HOH F O   1 
HETATM 2529 O  O   . HOH N 7 .   ? 16.756  -0.878  11.201  1.00 18.11 ? 392 HOH F O   1 
HETATM 2530 O  O   . HOH N 7 .   ? 22.162  -11.410 -5.245  1.00 22.52 ? 393 HOH F O   1 
HETATM 2531 O  O   . HOH N 7 .   ? 25.917  -10.952 13.273  1.00 42.52 ? 394 HOH F O   1 
HETATM 2532 O  O   . HOH N 7 .   ? 24.626  -0.646  5.887   1.00 30.52 ? 395 HOH F O   1 
HETATM 2533 O  O   . HOH N 7 .   ? 14.030  -10.805 22.416  1.00 29.33 ? 396 HOH F O   1 
HETATM 2534 O  O   . HOH N 7 .   ? 27.837  -20.129 3.633   1.00 31.57 ? 397 HOH F O   1 
HETATM 2535 O  O   . HOH N 7 .   ? 1.240   -25.286 6.200   1.00 43.65 ? 398 HOH F O   1 
HETATM 2536 O  O   . HOH N 7 .   ? -2.677  -22.513 5.290   1.00 41.26 ? 399 HOH F O   1 
HETATM 2537 O  O   . HOH N 7 .   ? 22.189  -8.817  15.448  1.00 30.79 ? 400 HOH F O   1 
HETATM 2538 O  O   . HOH N 7 .   ? 18.464  -19.124 -4.674  1.00 30.82 ? 401 HOH F O   1 
HETATM 2539 O  O   . HOH N 7 .   ? 9.112   -5.865  22.292  1.00 35.37 ? 402 HOH F O   1 
HETATM 2540 O  O   . HOH N 7 .   ? 0.736   -9.524  11.860  1.00 31.20 ? 403 HOH F O   1 
HETATM 2541 O  O   . HOH N 7 .   ? -0.320  -10.752 -4.279  1.00 47.06 ? 404 HOH F O   1 
HETATM 2542 O  O   . HOH N 7 .   ? 13.814  7.812   -0.762  1.00 31.36 ? 405 HOH F O   1 
HETATM 2543 O  O   . HOH N 7 .   ? 33.189  -11.605 -9.659  1.00 27.44 ? 406 HOH F O   1 
HETATM 2544 O  O   . HOH N 7 .   ? 24.649  -23.525 2.583   1.00 23.22 ? 407 HOH F O   1 
HETATM 2545 O  O   . HOH N 7 .   ? 16.645  -22.880 12.927  1.00 37.58 ? 408 HOH F O   1 
HETATM 2546 O  O   . HOH N 7 .   ? 1.497   -8.738  -7.131  1.00 33.47 ? 409 HOH F O   1 
HETATM 2547 O  O   . HOH N 7 .   ? 21.235  -6.181  14.562  1.00 39.65 ? 410 HOH F O   1 
HETATM 2548 O  O   . HOH N 7 .   ? 10.238  -19.614 10.811  1.00 37.57 ? 411 HOH F O   1 
HETATM 2549 O  O   . HOH N 7 .   ? 14.829  -4.992  -8.852  1.00 32.64 ? 412 HOH F O   1 
HETATM 2550 O  O   . HOH N 7 .   ? 17.871  -30.374 11.095  1.00 32.96 ? 413 HOH F O   1 
HETATM 2551 O  O   . HOH N 7 .   ? 23.908  -10.318 13.965  1.00 37.27 ? 414 HOH F O   1 
HETATM 2552 O  O   . HOH N 7 .   ? 19.513  -10.858 -5.889  1.00 18.32 ? 415 HOH F O   1 
HETATM 2553 O  O   . HOH N 7 .   ? 17.079  -3.305  13.273  1.00 26.95 ? 416 HOH F O   1 
HETATM 2554 O  O   . HOH N 7 .   ? 15.621  -5.468  12.940  1.00 33.28 ? 417 HOH F O   1 
HETATM 2555 O  O   . HOH N 7 .   ? 21.380  -15.958 14.804  1.00 30.38 ? 418 HOH F O   1 
HETATM 2556 O  O   . HOH N 7 .   ? 2.257   -22.636 8.923   1.00 31.32 ? 419 HOH F O   1 
HETATM 2557 O  O   . HOH N 7 .   ? 1.198   3.016   -4.716  1.00 53.24 ? 420 HOH F O   1 
HETATM 2558 O  O   . HOH N 7 .   ? -4.368  -18.680 5.012   1.00 34.86 ? 421 HOH F O   1 
HETATM 2559 O  O   . HOH N 7 .   ? 16.269  -17.343 -4.791  1.00 25.77 ? 422 HOH F O   1 
HETATM 2560 O  O   . HOH N 7 .   ? 17.622  -16.910 15.666  1.00 38.60 ? 423 HOH F O   1 
HETATM 2561 O  O   . HOH N 7 .   ? 1.230   3.117   0.766   1.00 44.62 ? 424 HOH F O   1 
HETATM 2562 O  O   . HOH N 7 .   ? 6.977   -3.211  -11.773 1.00 42.19 ? 425 HOH F O   1 
HETATM 2563 O  O   . HOH N 7 .   ? 11.466  -10.051 21.494  1.00 34.46 ? 426 HOH F O   1 
HETATM 2564 O  O   . HOH N 7 .   ? 19.295  -33.752 9.067   1.00 38.40 ? 427 HOH F O   1 
HETATM 2565 O  O   . HOH N 7 .   ? 8.859   -0.271  -8.994  1.00 39.25 ? 428 HOH F O   1 
HETATM 2566 O  O   . HOH N 7 .   ? -5.324  -4.582  -4.126  1.00 35.35 ? 429 HOH F O   1 
HETATM 2567 O  O   . HOH N 7 .   ? 26.020  -0.810  3.157   1.00 39.16 ? 430 HOH F O   1 
HETATM 2568 O  O   . HOH N 7 .   ? 19.692  -17.390 -5.962  1.00 36.17 ? 431 HOH F O   1 
HETATM 2569 O  O   . HOH N 7 .   ? 6.376   -26.761 -3.364  1.00 35.76 ? 432 HOH F O   1 
HETATM 2570 O  O   . HOH N 7 .   ? 13.363  -13.970 -6.665  1.00 20.83 ? 433 HOH F O   1 
HETATM 2571 O  O   . HOH N 7 .   ? 6.111   8.574   -5.670  1.00 32.12 ? 434 HOH F O   1 
HETATM 2572 O  O   . HOH N 7 .   ? 16.644  -1.002  15.067  1.00 25.76 ? 435 HOH F O   1 
HETATM 2573 O  O   . HOH N 7 .   ? 21.206  -28.297 5.959   1.00 34.36 ? 436 HOH F O   1 
HETATM 2574 O  O   . HOH N 7 .   ? 14.120  -30.143 12.792  1.00 32.38 ? 437 HOH F O   1 
HETATM 2575 O  O   . HOH N 7 .   ? 28.558  -11.297 9.858   1.00 48.47 ? 438 HOH F O   1 
HETATM 2576 O  O   . HOH N 7 .   ? 21.558  -23.140 11.892  1.00 47.97 ? 439 HOH F O   1 
HETATM 2577 O  O   . HOH N 7 .   ? 13.659  -5.757  -11.055 1.00 38.14 ? 440 HOH F O   1 
HETATM 2578 O  O   . HOH N 7 .   ? 25.575  -8.880  -10.467 1.00 27.27 ? 441 HOH F O   1 
HETATM 2579 O  O   . HOH N 7 .   ? 0.255   -11.354 10.016  1.00 30.20 ? 442 HOH F O   1 
HETATM 2580 O  O   . HOH N 7 .   ? -0.380  -10.188 7.271   1.00 26.87 ? 443 HOH F O   1 
HETATM 2581 O  O   . HOH N 7 .   ? 21.966  -5.722  -9.770  1.00 38.88 ? 444 HOH F O   1 
HETATM 2582 O  O   . HOH N 7 .   ? 34.271  -18.272 2.111   1.00 38.44 ? 445 HOH F O   1 
HETATM 2583 O  O   . HOH N 7 .   ? 15.603  -28.884 14.827  1.00 36.49 ? 446 HOH F O   1 
HETATM 2584 O  O   . HOH N 7 .   ? 2.034   -29.272 9.724   1.00 38.07 ? 447 HOH F O   1 
HETATM 2585 O  O   . HOH N 7 .   ? 30.210  -2.884  -4.441  1.00 40.34 ? 448 HOH F O   1 
HETATM 2586 O  O   . HOH N 7 .   ? 15.003  5.239   -4.812  1.00 34.90 ? 449 HOH F O   1 
HETATM 2587 O  O   . HOH N 7 .   ? 20.371  1.131   11.140  1.00 26.02 ? 450 HOH F O   1 
HETATM 2588 O  O   . HOH N 7 .   ? 0.925   -16.911 -0.368  1.00 24.45 ? 451 HOH F O   1 
HETATM 2589 O  O   . HOH N 7 .   ? 25.764  -11.078 -9.062  1.00 28.69 ? 452 HOH F O   1 
HETATM 2590 O  O   . HOH N 7 .   ? 17.503  -16.341 -7.573  1.00 34.66 ? 453 HOH F O   1 
HETATM 2591 O  O   . HOH N 7 .   ? 4.401   5.747   1.579   1.00 34.58 ? 454 HOH F O   1 
HETATM 2592 O  O   . HOH N 7 .   ? 30.212  -13.081 9.104   1.00 32.32 ? 455 HOH F O   1 
HETATM 2593 O  O   . HOH N 7 .   ? 3.437   3.816   3.212   1.00 41.44 ? 456 HOH F O   1 
HETATM 2594 O  O   . HOH N 7 .   ? 29.610  -15.113 11.538  1.00 41.49 ? 457 HOH F O   1 
HETATM 2595 O  O   . HOH N 7 .   ? 29.760  -16.086 9.027   1.00 37.55 ? 458 HOH F O   1 
HETATM 2596 O  O   . HOH N 7 .   ? 32.955  -12.822 10.499  1.00 44.33 ? 459 HOH F O   1 
HETATM 2597 O  O   . HOH N 7 .   ? 24.517  -25.775 13.504  1.00 46.09 ? 460 HOH F O   1 
HETATM 2598 O  O   . HOH N 7 .   ? 15.251  3.756   -11.831 1.00 42.60 ? 461 HOH F O   1 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   ALA 1   1   1   ALA ALA A . n 
A 1 2   THR 2   2   2   THR THR A . n 
A 1 3   LYS 3   3   3   LYS LYS A . n 
A 1 4   ALA 4   4   4   ALA ALA A . n 
A 1 5   VAL 5   5   5   VAL VAL A . n 
A 1 6   CYS 6   6   6   CYS CYS A . n 
A 1 7   VAL 7   7   7   VAL VAL A . n 
A 1 8   LEU 8   8   8   LEU LEU A . n 
A 1 9   LYS 9   9   9   LYS LYS A . n 
A 1 10  GLY 10  10  10  GLY GLY A . n 
A 1 11  ASP 11  11  11  ASP ASP A . n 
A 1 12  GLY 12  12  12  GLY GLY A . n 
A 1 13  PRO 13  13  13  PRO PRO A . n 
A 1 14  VAL 14  14  14  VAL VAL A . n 
A 1 15  GLN 15  15  15  GLN GLN A . n 
A 1 16  GLY 16  16  16  GLY GLY A . n 
A 1 17  ILE 17  17  17  ILE ILE A . n 
A 1 18  ILE 18  18  18  ILE ILE A . n 
A 1 19  ASN 19  19  19  ASN ASN A . n 
A 1 20  PHE 20  20  20  PHE PHE A . n 
A 1 21  GLU 21  21  21  GLU GLU A . n 
A 1 22  GLN 22  22  22  GLN GLN A . n 
A 1 23  LYS 23  23  23  LYS LYS A . n 
A 1 24  GLU 24  24  24  GLU GLU A . n 
A 1 25  SER 25  25  25  SER SER A . n 
A 1 26  ASN 26  26  26  ASN ASN A . n 
A 1 27  GLY 27  27  27  GLY GLY A . n 
A 1 28  PRO 28  28  28  PRO PRO A . n 
A 1 29  VAL 29  29  29  VAL VAL A . n 
A 1 30  LYS 30  30  30  LYS LYS A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  TRP 32  32  32  TRP TRP A . n 
A 1 33  GLY 33  33  33  GLY GLY A . n 
A 1 34  SER 34  34  34  SER SER A . n 
A 1 35  ILE 35  35  35  ILE ILE A . n 
A 1 36  LYS 36  36  36  LYS LYS A . n 
A 1 37  GLY 37  37  37  GLY GLY A . n 
A 1 38  LEU 38  38  38  LEU LEU A . n 
A 1 39  THR 39  39  39  THR THR A . n 
A 1 40  GLU 40  40  40  GLU GLU A . n 
A 1 41  GLY 41  41  41  GLY GLY A . n 
A 1 42  LEU 42  42  42  LEU LEU A . n 
A 1 43  HIS 43  43  43  HIS HIS A . n 
A 1 44  GLY 44  44  44  GLY GLY A . n 
A 1 45  PHE 45  45  45  PHE PHE A . n 
A 1 46  HIS 46  46  46  HIS HIS A . n 
A 1 47  VAL 47  47  47  VAL VAL A . n 
A 1 48  HIS 48  48  48  HIS HIS A . n 
A 1 49  GLU 49  49  49  GLU GLU A . n 
A 1 50  PHE 50  50  50  PHE PHE A . n 
A 1 51  GLY 51  51  51  GLY GLY A . n 
A 1 52  ASP 52  52  52  ASP ASP A . n 
A 1 53  ASN 53  53  53  ASN ASN A . n 
A 1 54  THR 54  54  54  THR THR A . n 
A 1 55  ALA 55  55  55  ALA ALA A . n 
A 1 56  GLY 56  56  56  GLY GLY A . n 
A 1 57  CYS 57  57  57  CYS CYS A . n 
A 1 58  THR 58  58  58  THR THR A . n 
A 1 59  SER 59  59  59  SER SER A . n 
A 1 60  ALA 60  60  60  ALA ALA A . n 
A 1 61  GLY 61  61  61  GLY GLY A . n 
A 1 62  PRO 62  62  62  PRO PRO A . n 
A 1 63  HIS 63  63  63  HIS HIS A . n 
A 1 64  PHE 64  64  64  PHE PHE A . n 
A 1 65  ASN 65  65  65  ASN ASN A . n 
A 1 66  PRO 66  66  66  PRO PRO A . n 
A 1 67  LEU 67  67  67  LEU LEU A . n 
A 1 68  SER 68  68  68  SER SER A . n 
A 1 69  ARG 69  69  69  ARG ARG A . n 
A 1 70  LYS 70  70  70  LYS LYS A . n 
A 1 71  HIS 71  71  71  HIS HIS A . n 
A 1 72  GLY 72  72  72  GLY GLY A . n 
A 1 73  GLY 73  73  73  GLY GLY A . n 
A 1 74  PRO 74  74  74  PRO PRO A . n 
A 1 75  LYS 75  75  75  LYS LYS A . n 
A 1 76  ASP 76  76  76  ASP ASP A . n 
A 1 77  GLU 77  77  77  GLU GLU A . n 
A 1 78  GLU 78  78  78  GLU GLU A . n 
A 1 79  ARG 79  79  79  ARG ARG A . n 
A 1 80  HIS 80  80  80  HIS HIS A . n 
A 1 81  VAL 81  81  81  VAL VAL A . n 
A 1 82  GLY 82  82  82  GLY GLY A . n 
A 1 83  ASP 83  83  83  ASP ASP A . n 
A 1 84  LEU 84  84  84  LEU LEU A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  ASN 86  86  86  ASN ASN A . n 
A 1 87  VAL 87  87  87  VAL VAL A . n 
A 1 88  THR 88  88  88  THR THR A . n 
A 1 89  ALA 89  89  89  ALA ALA A . n 
A 1 90  ASP 90  90  90  ASP ASP A . n 
A 1 91  LYS 91  91  91  LYS LYS A . n 
A 1 92  ASP 92  92  92  ASP ASP A . n 
A 1 93  ALA 93  93  93  ALA ALA A . n 
A 1 94  VAL 94  94  94  VAL VAL A . n 
A 1 95  ALA 95  95  95  ALA ALA A . n 
A 1 96  ASP 96  96  96  ASP ASP A . n 
A 1 97  VAL 97  97  97  VAL VAL A . n 
A 1 98  SER 98  98  98  SER SER A . n 
A 1 99  ILE 99  99  99  ILE ILE A . n 
A 1 100 GLU 100 100 100 GLU GLU A . n 
A 1 101 ASP 101 101 101 ASP ASP A . n 
A 1 102 SER 102 102 102 SER SER A . n 
A 1 103 VAL 103 103 103 VAL VAL A . n 
A 1 104 ILE 104 104 104 ILE ILE A . n 
A 1 105 SER 105 105 105 SER SER A . n 
A 1 106 LEU 106 106 106 LEU LEU A . n 
A 1 107 SER 107 107 107 SER SER A . n 
A 1 108 GLY 108 108 108 GLY GLY A . n 
A 1 109 ASP 109 109 109 ASP ASP A . n 
A 1 110 HIS 110 110 110 HIS HIS A . n 
A 1 111 CYS 111 111 111 CYS CYS A . n 
A 1 112 ILE 112 112 112 ILE ILE A . n 
A 1 113 ILE 113 113 113 ILE ILE A . n 
A 1 114 GLY 114 114 114 GLY GLY A . n 
A 1 115 ARG 115 115 115 ARG ARG A . n 
A 1 116 THR 116 116 116 THR THR A . n 
A 1 117 LEU 117 117 117 LEU LEU A . n 
A 1 118 VAL 118 118 118 VAL VAL A . n 
A 1 119 VAL 119 119 119 VAL VAL A . n 
A 1 120 HIS 120 120 120 HIS HIS A . n 
A 1 121 GLU 121 121 121 GLU GLU A . n 
A 1 122 LYS 122 122 122 LYS LYS A . n 
A 1 123 ALA 123 123 123 ALA ALA A . n 
A 1 124 ASP 124 124 124 ASP ASP A . n 
A 1 125 ASP 125 125 125 ASP ASP A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 GLY 127 127 127 GLY GLY A . n 
A 1 128 LYS 128 128 128 LYS LYS A . n 
A 1 129 GLY 129 129 129 GLY GLY A . n 
A 1 130 GLY 130 130 130 GLY GLY A . n 
A 1 131 ASN 131 131 131 ASN ASN A . n 
A 1 132 GLU 132 132 132 GLU GLU A . n 
A 1 133 GLU 133 133 133 GLU GLU A . n 
A 1 134 SER 134 134 134 SER SER A . n 
A 1 135 THR 135 135 135 THR THR A . n 
A 1 136 LYS 136 136 136 LYS LYS A . n 
A 1 137 THR 137 137 137 THR THR A . n 
A 1 138 GLY 138 138 138 GLY GLY A . n 
A 1 139 ASN 139 139 139 ASN ASN A . n 
A 1 140 ALA 140 140 140 ALA ALA A . n 
A 1 141 GLY 141 141 141 GLY GLY A . n 
A 1 142 SER 142 142 142 SER SER A . n 
A 1 143 ARG 143 143 143 ARG ARG A . n 
A 1 144 LEU 144 144 144 LEU LEU A . n 
A 1 145 ALA 145 145 145 ALA ALA A . n 
A 1 146 CYS 146 146 146 CYS CYS A . n 
A 1 147 GLY 147 147 147 GLY GLY A . n 
A 1 148 VAL 148 148 148 VAL VAL A . n 
A 1 149 ILE 149 149 149 ILE ILE A . n 
A 1 150 GLY 150 150 150 GLY GLY A . n 
A 1 151 ILE 151 151 151 ILE ILE A . n 
A 1 152 ALA 152 152 152 ALA ALA A . n 
A 1 153 GLN 153 153 153 GLN GLN A . n 
B 1 1   ALA 1   1   1   ALA ALA F . n 
B 1 2   THR 2   2   2   THR THR F . n 
B 1 3   LYS 3   3   3   LYS LYS F . n 
B 1 4   ALA 4   4   4   ALA ALA F . n 
B 1 5   VAL 5   5   5   VAL VAL F . n 
B 1 6   CYS 6   6   6   CYS CYS F . n 
B 1 7   VAL 7   7   7   VAL VAL F . n 
B 1 8   LEU 8   8   8   LEU LEU F . n 
B 1 9   LYS 9   9   9   LYS LYS F . n 
B 1 10  GLY 10  10  10  GLY GLY F . n 
B 1 11  ASP 11  11  11  ASP ASP F . n 
B 1 12  GLY 12  12  12  GLY GLY F . n 
B 1 13  PRO 13  13  13  PRO PRO F . n 
B 1 14  VAL 14  14  14  VAL VAL F . n 
B 1 15  GLN 15  15  15  GLN GLN F . n 
B 1 16  GLY 16  16  16  GLY GLY F . n 
B 1 17  ILE 17  17  17  ILE ILE F . n 
B 1 18  ILE 18  18  18  ILE ILE F . n 
B 1 19  ASN 19  19  19  ASN ASN F . n 
B 1 20  PHE 20  20  20  PHE PHE F . n 
B 1 21  GLU 21  21  21  GLU GLU F . n 
B 1 22  GLN 22  22  22  GLN GLN F . n 
B 1 23  LYS 23  23  23  LYS LYS F . n 
B 1 24  GLU 24  24  24  GLU GLU F . n 
B 1 25  SER 25  25  25  SER SER F . n 
B 1 26  ASN 26  26  26  ASN ASN F . n 
B 1 27  GLY 27  27  27  GLY GLY F . n 
B 1 28  PRO 28  28  28  PRO PRO F . n 
B 1 29  VAL 29  29  29  VAL VAL F . n 
B 1 30  LYS 30  30  30  LYS LYS F . n 
B 1 31  VAL 31  31  31  VAL VAL F . n 
B 1 32  TRP 32  32  32  TRP TRP F . n 
B 1 33  GLY 33  33  33  GLY GLY F . n 
B 1 34  SER 34  34  34  SER SER F . n 
B 1 35  ILE 35  35  35  ILE ILE F . n 
B 1 36  LYS 36  36  36  LYS LYS F . n 
B 1 37  GLY 37  37  37  GLY GLY F . n 
B 1 38  LEU 38  38  38  LEU LEU F . n 
B 1 39  THR 39  39  39  THR THR F . n 
B 1 40  GLU 40  40  40  GLU GLU F . n 
B 1 41  GLY 41  41  41  GLY GLY F . n 
B 1 42  LEU 42  42  42  LEU LEU F . n 
B 1 43  HIS 43  43  43  HIS HIS F . n 
B 1 44  GLY 44  44  44  GLY GLY F . n 
B 1 45  PHE 45  45  45  PHE PHE F . n 
B 1 46  HIS 46  46  46  HIS HIS F . n 
B 1 47  VAL 47  47  47  VAL VAL F . n 
B 1 48  HIS 48  48  48  HIS HIS F . n 
B 1 49  GLU 49  49  49  GLU GLU F . n 
B 1 50  PHE 50  50  50  PHE PHE F . n 
B 1 51  GLY 51  51  51  GLY GLY F . n 
B 1 52  ASP 52  52  52  ASP ASP F . n 
B 1 53  ASN 53  53  53  ASN ASN F . n 
B 1 54  THR 54  54  54  THR THR F . n 
B 1 55  ALA 55  55  55  ALA ALA F . n 
B 1 56  GLY 56  56  56  GLY GLY F . n 
B 1 57  CYS 57  57  57  CYS CYS F . n 
B 1 58  THR 58  58  58  THR THR F . n 
B 1 59  SER 59  59  59  SER SER F . n 
B 1 60  ALA 60  60  60  ALA ALA F . n 
B 1 61  GLY 61  61  61  GLY GLY F . n 
B 1 62  PRO 62  62  62  PRO PRO F . n 
B 1 63  HIS 63  63  63  HIS HIS F . n 
B 1 64  PHE 64  64  64  PHE PHE F . n 
B 1 65  ASN 65  65  65  ASN ASN F . n 
B 1 66  PRO 66  66  66  PRO PRO F . n 
B 1 67  LEU 67  67  67  LEU LEU F . n 
B 1 68  SER 68  68  68  SER SER F . n 
B 1 69  ARG 69  69  69  ARG ARG F . n 
B 1 70  LYS 70  70  70  LYS LYS F . n 
B 1 71  HIS 71  71  71  HIS HIS F . n 
B 1 72  GLY 72  72  72  GLY GLY F . n 
B 1 73  GLY 73  73  73  GLY GLY F . n 
B 1 74  PRO 74  74  74  PRO PRO F . n 
B 1 75  LYS 75  75  75  LYS LYS F . n 
B 1 76  ASP 76  76  76  ASP ASP F . n 
B 1 77  GLU 77  77  77  GLU GLU F . n 
B 1 78  GLU 78  78  78  GLU GLU F . n 
B 1 79  ARG 79  79  79  ARG ARG F . n 
B 1 80  HIS 80  80  80  HIS HIS F . n 
B 1 81  VAL 81  81  81  VAL VAL F . n 
B 1 82  GLY 82  82  82  GLY GLY F . n 
B 1 83  ASP 83  83  83  ASP ASP F . n 
B 1 84  LEU 84  84  84  LEU LEU F . n 
B 1 85  GLY 85  85  85  GLY GLY F . n 
B 1 86  ASN 86  86  86  ASN ASN F . n 
B 1 87  VAL 87  87  87  VAL VAL F . n 
B 1 88  THR 88  88  88  THR THR F . n 
B 1 89  ALA 89  89  89  ALA ALA F . n 
B 1 90  ASP 90  90  90  ASP ASP F . n 
B 1 91  LYS 91  91  91  LYS LYS F . n 
B 1 92  ASP 92  92  92  ASP ASP F . n 
B 1 93  ALA 93  93  93  ALA ALA F . n 
B 1 94  VAL 94  94  94  VAL VAL F . n 
B 1 95  ALA 95  95  95  ALA ALA F . n 
B 1 96  ASP 96  96  96  ASP ASP F . n 
B 1 97  VAL 97  97  97  VAL VAL F . n 
B 1 98  SER 98  98  98  SER SER F . n 
B 1 99  ILE 99  99  99  ILE ILE F . n 
B 1 100 GLU 100 100 100 GLU GLU F . n 
B 1 101 ASP 101 101 101 ASP ASP F . n 
B 1 102 SER 102 102 102 SER SER F . n 
B 1 103 VAL 103 103 103 VAL VAL F . n 
B 1 104 ILE 104 104 104 ILE ILE F . n 
B 1 105 SER 105 105 105 SER SER F . n 
B 1 106 LEU 106 106 106 LEU LEU F . n 
B 1 107 SER 107 107 107 SER SER F . n 
B 1 108 GLY 108 108 108 GLY GLY F . n 
B 1 109 ASP 109 109 109 ASP ASP F . n 
B 1 110 HIS 110 110 110 HIS HIS F . n 
B 1 111 CYS 111 111 111 CYS CSO F . n 
B 1 112 ILE 112 112 112 ILE ILE F . n 
B 1 113 ILE 113 113 113 ILE ILE F . n 
B 1 114 GLY 114 114 114 GLY GLY F . n 
B 1 115 ARG 115 115 115 ARG ARG F . n 
B 1 116 THR 116 116 116 THR THR F . n 
B 1 117 LEU 117 117 117 LEU LEU F . n 
B 1 118 VAL 118 118 118 VAL VAL F . n 
B 1 119 VAL 119 119 119 VAL VAL F . n 
B 1 120 HIS 120 120 120 HIS HIS F . n 
B 1 121 GLU 121 121 121 GLU GLU F . n 
B 1 122 LYS 122 122 122 LYS LYS F . n 
B 1 123 ALA 123 123 123 ALA ALA F . n 
B 1 124 ASP 124 124 124 ASP ASP F . n 
B 1 125 ASP 125 125 125 ASP ASP F . n 
B 1 126 LEU 126 126 126 LEU LEU F . n 
B 1 127 GLY 127 127 127 GLY GLY F . n 
B 1 128 LYS 128 128 128 LYS LYS F . n 
B 1 129 GLY 129 129 129 GLY GLY F . n 
B 1 130 GLY 130 130 130 GLY GLY F . n 
B 1 131 ASN 131 131 131 ASN ASN F . n 
B 1 132 GLU 132 132 132 GLU GLU F . n 
B 1 133 GLU 133 133 133 GLU GLU F . n 
B 1 134 SER 134 134 134 SER SER F . n 
B 1 135 THR 135 135 135 THR THR F . n 
B 1 136 LYS 136 136 136 LYS LYS F . n 
B 1 137 THR 137 137 137 THR THR F . n 
B 1 138 GLY 138 138 138 GLY GLY F . n 
B 1 139 ASN 139 139 139 ASN ASN F . n 
B 1 140 ALA 140 140 140 ALA ALA F . n 
B 1 141 GLY 141 141 141 GLY GLY F . n 
B 1 142 SER 142 142 142 SER SER F . n 
B 1 143 ARG 143 143 143 ARG ARG F . n 
B 1 144 LEU 144 144 144 LEU LEU F . n 
B 1 145 ALA 145 145 145 ALA ALA F . n 
B 1 146 CYS 146 146 146 CYS CYS F . n 
B 1 147 GLY 147 147 147 GLY GLY F . n 
B 1 148 VAL 148 148 148 VAL VAL F . n 
B 1 149 ILE 149 149 149 ILE ILE F . n 
B 1 150 GLY 150 150 150 GLY GLY F . n 
B 1 151 ILE 151 151 151 ILE ILE F . n 
B 1 152 ALA 152 152 152 ALA ALA F . n 
B 1 153 GLN 153 153 153 GLN GLN F . n 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              S.S.Hasnain@liverpool.ac.uk 
_pdbx_contact_author.name_first         Samar 
_pdbx_contact_author.name_last          Hasnain 
_pdbx_contact_author.name_mi            S. 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-2854-4718 
# 
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   201 155 ZN  ZN  A . 
D 3 Q8H 1   202 157 Q8H 682 A . 
E 2 ZN  1   203 1   ZN  ZN  A . 
F 4 ACT 1   204 290 ACT ACT A . 
G 5 SO4 1   205 1   SO4 SO4 A . 
H 3 Q8H 1   201 158 Q8H 682 F . 
I 2 ZN  1   202 155 ZN  ZN  F . 
J 2 ZN  1   203 2   ZN  ZN  F . 
K 6 SE  1   204 1   SE  SE  F . 
L 5 SO4 1   205 2   SO4 SO4 F . 
M 7 HOH 1   301 278 HOH HOH A . 
M 7 HOH 2   302 198 HOH HOH A . 
M 7 HOH 3   303 200 HOH HOH A . 
M 7 HOH 4   304 144 HOH HOH A . 
M 7 HOH 5   305 267 HOH HOH A . 
M 7 HOH 6   306 67  HOH HOH A . 
M 7 HOH 7   307 260 HOH HOH A . 
M 7 HOH 8   308 269 HOH HOH A . 
M 7 HOH 9   309 253 HOH HOH A . 
M 7 HOH 10  310 60  HOH HOH A . 
M 7 HOH 11  311 33  HOH HOH A . 
M 7 HOH 12  312 123 HOH HOH A . 
M 7 HOH 13  313 142 HOH HOH A . 
M 7 HOH 14  314 83  HOH HOH A . 
M 7 HOH 15  315 134 HOH HOH A . 
M 7 HOH 16  316 252 HOH HOH A . 
M 7 HOH 17  317 129 HOH HOH A . 
M 7 HOH 18  318 139 HOH HOH A . 
M 7 HOH 19  319 188 HOH HOH A . 
M 7 HOH 20  320 47  HOH HOH A . 
M 7 HOH 21  321 19  HOH HOH A . 
M 7 HOH 22  322 47  HOH HOH A . 
M 7 HOH 23  323 68  HOH HOH A . 
M 7 HOH 24  324 114 HOH HOH A . 
M 7 HOH 25  325 284 HOH HOH A . 
M 7 HOH 26  326 20  HOH HOH A . 
M 7 HOH 27  327 254 HOH HOH A . 
M 7 HOH 28  328 91  HOH HOH A . 
M 7 HOH 29  329 80  HOH HOH A . 
M 7 HOH 30  330 130 HOH HOH A . 
M 7 HOH 31  331 162 HOH HOH A . 
M 7 HOH 32  332 98  HOH HOH A . 
M 7 HOH 33  333 15  HOH HOH A . 
M 7 HOH 34  334 263 HOH HOH A . 
M 7 HOH 35  335 143 HOH HOH A . 
M 7 HOH 36  336 76  HOH HOH A . 
M 7 HOH 37  337 2   HOH HOH A . 
M 7 HOH 38  338 28  HOH HOH A . 
M 7 HOH 39  339 85  HOH HOH A . 
M 7 HOH 40  340 81  HOH HOH A . 
M 7 HOH 41  341 172 HOH HOH A . 
M 7 HOH 42  342 74  HOH HOH A . 
M 7 HOH 43  343 75  HOH HOH A . 
M 7 HOH 44  344 42  HOH HOH A . 
M 7 HOH 45  345 283 HOH HOH A . 
M 7 HOH 46  346 273 HOH HOH A . 
M 7 HOH 47  347 111 HOH HOH A . 
M 7 HOH 48  348 127 HOH HOH A . 
M 7 HOH 49  349 97  HOH HOH A . 
M 7 HOH 50  350 287 HOH HOH A . 
M 7 HOH 51  351 54  HOH HOH A . 
M 7 HOH 52  352 79  HOH HOH A . 
M 7 HOH 53  353 191 HOH HOH A . 
M 7 HOH 54  354 140 HOH HOH A . 
M 7 HOH 55  355 261 HOH HOH A . 
M 7 HOH 56  356 16  HOH HOH A . 
M 7 HOH 57  357 266 HOH HOH A . 
M 7 HOH 58  358 69  HOH HOH A . 
M 7 HOH 59  359 257 HOH HOH A . 
M 7 HOH 60  360 135 HOH HOH A . 
M 7 HOH 61  361 141 HOH HOH A . 
M 7 HOH 62  362 184 HOH HOH A . 
M 7 HOH 63  363 232 HOH HOH A . 
M 7 HOH 64  364 194 HOH HOH A . 
M 7 HOH 65  365 174 HOH HOH A . 
M 7 HOH 66  366 190 HOH HOH A . 
M 7 HOH 67  367 24  HOH HOH A . 
M 7 HOH 68  368 193 HOH HOH A . 
M 7 HOH 69  369 108 HOH HOH A . 
M 7 HOH 70  370 103 HOH HOH A . 
M 7 HOH 71  371 53  HOH HOH A . 
M 7 HOH 72  372 265 HOH HOH A . 
M 7 HOH 73  373 8   HOH HOH A . 
M 7 HOH 74  374 13  HOH HOH A . 
M 7 HOH 75  375 233 HOH HOH A . 
M 7 HOH 76  376 268 HOH HOH A . 
M 7 HOH 77  377 82  HOH HOH A . 
M 7 HOH 78  378 72  HOH HOH A . 
M 7 HOH 79  379 9   HOH HOH A . 
M 7 HOH 80  380 23  HOH HOH A . 
M 7 HOH 81  381 279 HOH HOH A . 
M 7 HOH 82  382 113 HOH HOH A . 
M 7 HOH 83  383 29  HOH HOH A . 
M 7 HOH 84  384 22  HOH HOH A . 
M 7 HOH 85  385 64  HOH HOH A . 
M 7 HOH 86  386 95  HOH HOH A . 
M 7 HOH 87  387 18  HOH HOH A . 
M 7 HOH 88  388 187 HOH HOH A . 
M 7 HOH 89  389 3   HOH HOH A . 
M 7 HOH 90  390 25  HOH HOH A . 
M 7 HOH 91  391 197 HOH HOH A . 
M 7 HOH 92  392 48  HOH HOH A . 
M 7 HOH 93  393 282 HOH HOH A . 
M 7 HOH 94  394 226 HOH HOH A . 
M 7 HOH 95  395 133 HOH HOH A . 
M 7 HOH 96  396 48  HOH HOH A . 
M 7 HOH 97  397 136 HOH HOH A . 
M 7 HOH 98  398 12  HOH HOH A . 
M 7 HOH 99  399 90  HOH HOH A . 
M 7 HOH 100 400 243 HOH HOH A . 
M 7 HOH 101 401 44  HOH HOH A . 
M 7 HOH 102 402 99  HOH HOH A . 
M 7 HOH 103 403 270 HOH HOH A . 
M 7 HOH 104 404 73  HOH HOH A . 
M 7 HOH 105 405 201 HOH HOH A . 
M 7 HOH 106 406 288 HOH HOH A . 
M 7 HOH 107 407 14  HOH HOH A . 
M 7 HOH 108 408 88  HOH HOH A . 
M 7 HOH 109 409 126 HOH HOH A . 
M 7 HOH 110 410 235 HOH HOH A . 
M 7 HOH 111 411 259 HOH HOH A . 
M 7 HOH 112 412 106 HOH HOH A . 
M 7 HOH 113 413 122 HOH HOH A . 
M 7 HOH 114 414 89  HOH HOH A . 
M 7 HOH 115 415 70  HOH HOH A . 
M 7 HOH 116 416 112 HOH HOH A . 
M 7 HOH 117 417 189 HOH HOH A . 
M 7 HOH 118 418 195 HOH HOH A . 
M 7 HOH 119 419 43  HOH HOH A . 
M 7 HOH 120 420 262 HOH HOH A . 
M 7 HOH 121 421 62  HOH HOH A . 
M 7 HOH 122 422 105 HOH HOH A . 
M 7 HOH 123 423 244 HOH HOH A . 
M 7 HOH 124 424 100 HOH HOH A . 
M 7 HOH 125 425 49  HOH HOH A . 
M 7 HOH 126 426 131 HOH HOH A . 
M 7 HOH 127 427 117 HOH HOH A . 
M 7 HOH 128 428 107 HOH HOH A . 
M 7 HOH 129 429 109 HOH HOH A . 
M 7 HOH 130 430 255 HOH HOH A . 
M 7 HOH 131 431 102 HOH HOH A . 
M 7 HOH 132 432 92  HOH HOH A . 
M 7 HOH 133 433 256 HOH HOH A . 
M 7 HOH 134 434 78  HOH HOH A . 
M 7 HOH 135 435 118 HOH HOH A . 
M 7 HOH 136 436 202 HOH HOH A . 
M 7 HOH 137 437 281 HOH HOH A . 
M 7 HOH 138 438 17  HOH HOH A . 
M 7 HOH 139 439 58  HOH HOH A . 
M 7 HOH 140 440 101 HOH HOH A . 
M 7 HOH 141 441 196 HOH HOH A . 
M 7 HOH 142 442 36  HOH HOH A . 
M 7 HOH 143 443 274 HOH HOH A . 
M 7 HOH 144 444 65  HOH HOH A . 
M 7 HOH 145 445 66  HOH HOH A . 
M 7 HOH 146 446 34  HOH HOH A . 
M 7 HOH 147 447 272 HOH HOH A . 
M 7 HOH 148 448 104 HOH HOH A . 
M 7 HOH 149 449 192 HOH HOH A . 
M 7 HOH 150 450 77  HOH HOH A . 
M 7 HOH 151 451 84  HOH HOH A . 
M 7 HOH 152 452 87  HOH HOH A . 
M 7 HOH 153 453 96  HOH HOH A . 
M 7 HOH 154 454 86  HOH HOH A . 
M 7 HOH 155 455 17  HOH HOH A . 
M 7 HOH 156 456 137 HOH HOH A . 
M 7 HOH 157 457 125 HOH HOH A . 
M 7 HOH 158 458 124 HOH HOH A . 
M 7 HOH 159 459 37  HOH HOH A . 
M 7 HOH 160 460 121 HOH HOH A . 
M 7 HOH 161 461 264 HOH HOH A . 
M 7 HOH 162 462 110 HOH HOH A . 
M 7 HOH 163 463 238 HOH HOH A . 
M 7 HOH 164 464 271 HOH HOH A . 
M 7 HOH 165 465 275 HOH HOH A . 
M 7 HOH 166 466 277 HOH HOH A . 
N 7 HOH 1   301 223 HOH HOH F . 
N 7 HOH 2   302 21  HOH HOH F . 
N 7 HOH 3   303 160 HOH HOH F . 
N 7 HOH 4   304 21  HOH HOH F . 
N 7 HOH 5   305 219 HOH HOH F . 
N 7 HOH 6   306 228 HOH HOH F . 
N 7 HOH 7   307 161 HOH HOH F . 
N 7 HOH 8   308 31  HOH HOH F . 
N 7 HOH 9   309 63  HOH HOH F . 
N 7 HOH 10  310 29  HOH HOH F . 
N 7 HOH 11  311 213 HOH HOH F . 
N 7 HOH 12  312 176 HOH HOH F . 
N 7 HOH 13  313 171 HOH HOH F . 
N 7 HOH 14  314 19  HOH HOH F . 
N 7 HOH 15  315 46  HOH HOH F . 
N 7 HOH 16  316 250 HOH HOH F . 
N 7 HOH 17  317 32  HOH HOH F . 
N 7 HOH 18  318 151 HOH HOH F . 
N 7 HOH 19  319 239 HOH HOH F . 
N 7 HOH 20  320 205 HOH HOH F . 
N 7 HOH 21  321 39  HOH HOH F . 
N 7 HOH 22  322 2   HOH HOH F . 
N 7 HOH 23  323 208 HOH HOH F . 
N 7 HOH 24  324 40  HOH HOH F . 
N 7 HOH 25  325 209 HOH HOH F . 
N 7 HOH 26  326 147 HOH HOH F . 
N 7 HOH 27  327 258 HOH HOH F . 
N 7 HOH 28  328 206 HOH HOH F . 
N 7 HOH 29  329 26  HOH HOH F . 
N 7 HOH 30  330 286 HOH HOH F . 
N 7 HOH 31  331 218 HOH HOH F . 
N 7 HOH 32  332 234 HOH HOH F . 
N 7 HOH 33  333 5   HOH HOH F . 
N 7 HOH 34  334 289 HOH HOH F . 
N 7 HOH 35  335 38  HOH HOH F . 
N 7 HOH 36  336 185 HOH HOH F . 
N 7 HOH 37  337 199 HOH HOH F . 
N 7 HOH 38  338 51  HOH HOH F . 
N 7 HOH 39  339 6   HOH HOH F . 
N 7 HOH 40  340 8   HOH HOH F . 
N 7 HOH 41  341 173 HOH HOH F . 
N 7 HOH 42  342 168 HOH HOH F . 
N 7 HOH 43  343 179 HOH HOH F . 
N 7 HOH 44  344 164 HOH HOH F . 
N 7 HOH 45  345 44  HOH HOH F . 
N 7 HOH 46  346 120 HOH HOH F . 
N 7 HOH 47  347 50  HOH HOH F . 
N 7 HOH 48  348 153 HOH HOH F . 
N 7 HOH 49  349 43  HOH HOH F . 
N 7 HOH 50  350 13  HOH HOH F . 
N 7 HOH 51  351 221 HOH HOH F . 
N 7 HOH 52  352 37  HOH HOH F . 
N 7 HOH 53  353 33  HOH HOH F . 
N 7 HOH 54  354 40  HOH HOH F . 
N 7 HOH 55  355 222 HOH HOH F . 
N 7 HOH 56  356 210 HOH HOH F . 
N 7 HOH 57  357 169 HOH HOH F . 
N 7 HOH 58  358 61  HOH HOH F . 
N 7 HOH 59  359 23  HOH HOH F . 
N 7 HOH 60  360 132 HOH HOH F . 
N 7 HOH 61  361 128 HOH HOH F . 
N 7 HOH 62  362 42  HOH HOH F . 
N 7 HOH 63  363 186 HOH HOH F . 
N 7 HOH 64  364 163 HOH HOH F . 
N 7 HOH 65  365 214 HOH HOH F . 
N 7 HOH 66  366 28  HOH HOH F . 
N 7 HOH 67  367 280 HOH HOH F . 
N 7 HOH 68  368 1   HOH HOH F . 
N 7 HOH 69  369 35  HOH HOH F . 
N 7 HOH 70  370 22  HOH HOH F . 
N 7 HOH 71  371 249 HOH HOH F . 
N 7 HOH 72  372 16  HOH HOH F . 
N 7 HOH 73  373 152 HOH HOH F . 
N 7 HOH 74  374 240 HOH HOH F . 
N 7 HOH 75  375 138 HOH HOH F . 
N 7 HOH 76  376 27  HOH HOH F . 
N 7 HOH 77  377 166 HOH HOH F . 
N 7 HOH 78  378 4   HOH HOH F . 
N 7 HOH 79  379 217 HOH HOH F . 
N 7 HOH 80  380 245 HOH HOH F . 
N 7 HOH 81  381 32  HOH HOH F . 
N 7 HOH 82  382 59  HOH HOH F . 
N 7 HOH 83  383 248 HOH HOH F . 
N 7 HOH 84  384 41  HOH HOH F . 
N 7 HOH 85  385 178 HOH HOH F . 
N 7 HOH 86  386 175 HOH HOH F . 
N 7 HOH 87  387 10  HOH HOH F . 
N 7 HOH 88  388 158 HOH HOH F . 
N 7 HOH 89  389 215 HOH HOH F . 
N 7 HOH 90  390 183 HOH HOH F . 
N 7 HOH 91  391 225 HOH HOH F . 
N 7 HOH 92  392 31  HOH HOH F . 
N 7 HOH 93  393 212 HOH HOH F . 
N 7 HOH 94  394 7   HOH HOH F . 
N 7 HOH 95  395 146 HOH HOH F . 
N 7 HOH 96  396 36  HOH HOH F . 
N 7 HOH 97  397 4   HOH HOH F . 
N 7 HOH 98  398 14  HOH HOH F . 
N 7 HOH 99  399 15  HOH HOH F . 
N 7 HOH 100 400 148 HOH HOH F . 
N 7 HOH 101 401 55  HOH HOH F . 
N 7 HOH 102 402 231 HOH HOH F . 
N 7 HOH 103 403 11  HOH HOH F . 
N 7 HOH 104 404 242 HOH HOH F . 
N 7 HOH 105 405 50  HOH HOH F . 
N 7 HOH 106 406 38  HOH HOH F . 
N 7 HOH 107 407 46  HOH HOH F . 
N 7 HOH 108 408 30  HOH HOH F . 
N 7 HOH 109 409 241 HOH HOH F . 
N 7 HOH 110 410 39  HOH HOH F . 
N 7 HOH 111 411 10  HOH HOH F . 
N 7 HOH 112 412 182 HOH HOH F . 
N 7 HOH 113 413 227 HOH HOH F . 
N 7 HOH 114 414 149 HOH HOH F . 
N 7 HOH 115 415 211 HOH HOH F . 
N 7 HOH 116 416 229 HOH HOH F . 
N 7 HOH 117 417 34  HOH HOH F . 
N 7 HOH 118 418 154 HOH HOH F . 
N 7 HOH 119 419 224 HOH HOH F . 
N 7 HOH 120 420 204 HOH HOH F . 
N 7 HOH 121 421 216 HOH HOH F . 
N 7 HOH 122 422 57  HOH HOH F . 
N 7 HOH 123 423 9   HOH HOH F . 
N 7 HOH 124 424 18  HOH HOH F . 
N 7 HOH 125 425 177 HOH HOH F . 
N 7 HOH 126 426 230 HOH HOH F . 
N 7 HOH 127 427 247 HOH HOH F . 
N 7 HOH 128 428 35  HOH HOH F . 
N 7 HOH 129 429 180 HOH HOH F . 
N 7 HOH 130 430 11  HOH HOH F . 
N 7 HOH 131 431 56  HOH HOH F . 
N 7 HOH 132 432 220 HOH HOH F . 
N 7 HOH 133 433 207 HOH HOH F . 
N 7 HOH 134 434 3   HOH HOH F . 
N 7 HOH 135 435 30  HOH HOH F . 
N 7 HOH 136 436 52  HOH HOH F . 
N 7 HOH 137 437 116 HOH HOH F . 
N 7 HOH 138 438 150 HOH HOH F . 
N 7 HOH 139 439 12  HOH HOH F . 
N 7 HOH 140 440 246 HOH HOH F . 
N 7 HOH 141 441 1   HOH HOH F . 
N 7 HOH 142 442 236 HOH HOH F . 
N 7 HOH 143 443 237 HOH HOH F . 
N 7 HOH 144 444 203 HOH HOH F . 
N 7 HOH 145 445 167 HOH HOH F . 
N 7 HOH 146 446 115 HOH HOH F . 
N 7 HOH 147 447 41  HOH HOH F . 
N 7 HOH 148 448 181 HOH HOH F . 
N 7 HOH 149 449 45  HOH HOH F . 
N 7 HOH 150 450 145 HOH HOH F . 
N 7 HOH 151 451 170 HOH HOH F . 
N 7 HOH 152 452 71  HOH HOH F . 
N 7 HOH 153 453 251 HOH HOH F . 
N 7 HOH 154 454 20  HOH HOH F . 
N 7 HOH 155 455 6   HOH HOH F . 
N 7 HOH 156 456 49  HOH HOH F . 
N 7 HOH 157 457 5   HOH HOH F . 
N 7 HOH 158 458 45  HOH HOH F . 
N 7 HOH 159 459 165 HOH HOH F . 
N 7 HOH 160 460 276 HOH HOH F . 
N 7 HOH 161 461 119 HOH HOH F . 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N 
# 
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)' 2740  ? 
1 MORE         -139  ? 
1 'SSA (A^2)'  13350 ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  ND1 ? A HIS 46  ? A HIS 46  ? 1_555 ZN ? E ZN . ? A ZN 203 ? 1_555 NE2 ? A HIS 48  ? A HIS 48  ? 1_555 118.4 ? 
2  ND1 ? A HIS 46  ? A HIS 46  ? 1_555 ZN ? E ZN . ? A ZN 203 ? 1_555 NE2 ? A HIS 120 ? A HIS 120 ? 1_555 100.2 ? 
3  NE2 ? A HIS 48  ? A HIS 48  ? 1_555 ZN ? E ZN . ? A ZN 203 ? 1_555 NE2 ? A HIS 120 ? A HIS 120 ? 1_555 120.5 ? 
4  ND1 ? A HIS 46  ? A HIS 46  ? 1_555 ZN ? E ZN . ? A ZN 203 ? 1_555 O3  ? G SO4 .   ? A SO4 205 ? 1_555 105.7 ? 
5  NE2 ? A HIS 48  ? A HIS 48  ? 1_555 ZN ? E ZN . ? A ZN 203 ? 1_555 O3  ? G SO4 .   ? A SO4 205 ? 1_555 106.3 ? 
6  NE2 ? A HIS 120 ? A HIS 120 ? 1_555 ZN ? E ZN . ? A ZN 203 ? 1_555 O3  ? G SO4 .   ? A SO4 205 ? 1_555 104.1 ? 
7  ND1 ? A HIS 63  ? A HIS 63  ? 1_555 ZN ? C ZN . ? A ZN 201 ? 1_555 ND1 ? A HIS 71  ? A HIS 71  ? 1_555 104.0 ? 
8  ND1 ? A HIS 63  ? A HIS 63  ? 1_555 ZN ? C ZN . ? A ZN 201 ? 1_555 ND1 ? A HIS 80  ? A HIS 80  ? 1_555 109.0 ? 
9  ND1 ? A HIS 71  ? A HIS 71  ? 1_555 ZN ? C ZN . ? A ZN 201 ? 1_555 ND1 ? A HIS 80  ? A HIS 80  ? 1_555 123.8 ? 
10 ND1 ? A HIS 63  ? A HIS 63  ? 1_555 ZN ? C ZN . ? A ZN 201 ? 1_555 OD1 ? A ASP 83  ? A ASP 83  ? 1_555 105.3 ? 
11 ND1 ? A HIS 71  ? A HIS 71  ? 1_555 ZN ? C ZN . ? A ZN 201 ? 1_555 OD1 ? A ASP 83  ? A ASP 83  ? 1_555 97.7  ? 
12 ND1 ? A HIS 80  ? A HIS 80  ? 1_555 ZN ? C ZN . ? A ZN 201 ? 1_555 OD1 ? A ASP 83  ? A ASP 83  ? 1_555 115.0 ? 
13 ND1 ? B HIS 46  ? F HIS 46  ? 1_555 ZN ? J ZN . ? F ZN 203 ? 1_555 NE2 ? B HIS 48  ? F HIS 48  ? 1_555 119.1 ? 
14 ND1 ? B HIS 46  ? F HIS 46  ? 1_555 ZN ? J ZN . ? F ZN 203 ? 1_555 NE2 ? B HIS 120 ? F HIS 120 ? 1_555 98.1  ? 
15 NE2 ? B HIS 48  ? F HIS 48  ? 1_555 ZN ? J ZN . ? F ZN 203 ? 1_555 NE2 ? B HIS 120 ? F HIS 120 ? 1_555 119.1 ? 
16 ND1 ? B HIS 46  ? F HIS 46  ? 1_555 ZN ? J ZN . ? F ZN 203 ? 1_555 O2  ? L SO4 .   ? F SO4 205 ? 1_555 106.6 ? 
17 NE2 ? B HIS 48  ? F HIS 48  ? 1_555 ZN ? J ZN . ? F ZN 203 ? 1_555 O2  ? L SO4 .   ? F SO4 205 ? 1_555 106.8 ? 
18 NE2 ? B HIS 120 ? F HIS 120 ? 1_555 ZN ? J ZN . ? F ZN 203 ? 1_555 O2  ? L SO4 .   ? F SO4 205 ? 1_555 105.9 ? 
19 ND1 ? B HIS 63  ? F HIS 63  ? 1_555 ZN ? I ZN . ? F ZN 202 ? 1_555 ND1 ? B HIS 71  ? F HIS 71  ? 1_555 104.1 ? 
20 ND1 ? B HIS 63  ? F HIS 63  ? 1_555 ZN ? I ZN . ? F ZN 202 ? 1_555 ND1 ? B HIS 80  ? F HIS 80  ? 1_555 109.2 ? 
21 ND1 ? B HIS 71  ? F HIS 71  ? 1_555 ZN ? I ZN . ? F ZN 202 ? 1_555 ND1 ? B HIS 80  ? F HIS 80  ? 1_555 120.8 ? 
22 ND1 ? B HIS 63  ? F HIS 63  ? 1_555 ZN ? I ZN . ? F ZN 202 ? 1_555 OD1 ? B ASP 83  ? F ASP 83  ? 1_555 105.6 ? 
23 ND1 ? B HIS 71  ? F HIS 71  ? 1_555 ZN ? I ZN . ? F ZN 202 ? 1_555 OD1 ? B ASP 83  ? F ASP 83  ? 1_555 97.8  ? 
24 ND1 ? B HIS 80  ? F HIS 80  ? 1_555 ZN ? I ZN . ? F ZN 202 ? 1_555 OD1 ? B ASP 83  ? F ASP 83  ? 1_555 117.6 ? 
# 
_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       2023-01-25 
# 
_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 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? Aimless     ? ? ? 0.7.4    1 
? refinement        ? ? ? ? ? ? ? ? ? ? ? REFMAC      ? ? ? 5.8.0267 2 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.27     3 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? iMOSFLM     ? ? ? .        4 
? phasing           ? ? ? ? ? ? ? ? ? ? ? MOLREP      ? ? ? .        5 
# 
_pdbx_entry_details.entry_id                 7T8G 
_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         ? 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   HOH 
_pdbx_validate_close_contact.auth_seq_id_1    374 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    407 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.18 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       466 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   6.63 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
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 A GLN 15  ? CD  ? A GLN 15  CD  
2  1 Y 1 A GLN 15  ? OE1 ? A GLN 15  OE1 
3  1 Y 1 A GLN 15  ? NE2 ? A GLN 15  NE2 
4  1 Y 1 A LYS 23  ? CG  ? A LYS 23  CG  
5  1 Y 1 A LYS 23  ? CD  ? A LYS 23  CD  
6  1 Y 1 A LYS 23  ? CE  ? A LYS 23  CE  
7  1 Y 1 A LYS 23  ? NZ  ? A LYS 23  NZ  
8  1 Y 1 A GLU 24  ? CD  ? A GLU 24  CD  
9  1 Y 1 A GLU 24  ? OE1 ? A GLU 24  OE1 
10 1 Y 1 A GLU 24  ? OE2 ? A GLU 24  OE2 
11 1 Y 1 A LYS 36  ? CD  ? A LYS 36  CD  
12 1 Y 1 A LYS 36  ? CE  ? A LYS 36  CE  
13 1 Y 1 A LYS 36  ? NZ  ? A LYS 36  NZ  
14 1 Y 1 A LYS 122 ? NZ  ? A LYS 122 NZ  
15 1 Y 1 A GLU 132 ? CD  ? A GLU 132 CD  
16 1 Y 1 A GLU 132 ? OE1 ? A GLU 132 OE1 
17 1 Y 1 A GLU 132 ? OE2 ? A GLU 132 OE2 
18 1 Y 1 A GLU 133 ? CG  ? A GLU 133 CG  
19 1 Y 1 A GLU 133 ? CD  ? A GLU 133 CD  
20 1 Y 1 A GLU 133 ? OE1 ? A GLU 133 OE1 
21 1 Y 1 A GLU 133 ? OE2 ? A GLU 133 OE2 
22 1 Y 1 F LYS 9   ? CD  ? B LYS 9   CD  
23 1 Y 1 F LYS 9   ? CE  ? B LYS 9   CE  
24 1 Y 1 F LYS 9   ? NZ  ? B LYS 9   NZ  
25 1 Y 1 F LYS 23  ? CE  ? B LYS 23  CE  
26 1 Y 1 F LYS 23  ? NZ  ? B LYS 23  NZ  
27 1 Y 1 F LYS 30  ? CE  ? B LYS 30  CE  
28 1 Y 1 F LYS 30  ? NZ  ? B LYS 30  NZ  
29 1 Y 1 F LYS 36  ? CD  ? B LYS 36  CD  
30 1 Y 1 F LYS 36  ? CE  ? B LYS 36  CE  
31 1 Y 1 F LYS 36  ? NZ  ? B LYS 36  NZ  
32 1 Y 1 F GLU 132 ? CG  ? B GLU 132 CG  
33 1 Y 1 F GLU 132 ? CD  ? B GLU 132 CD  
34 1 Y 1 F GLU 132 ? OE1 ? B GLU 132 OE1 
35 1 Y 1 F GLU 132 ? OE2 ? B GLU 132 OE2 
36 1 Y 1 F LYS 136 ? CE  ? B LYS 136 CE  
37 1 Y 1 F LYS 136 ? NZ  ? B LYS 136 NZ  
# 
_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        Q8H 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   Q8H 
_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 '~{N}-(pyridin-3-ylmethyl)-2-selanyl-benzamide' Q8H 
4 'ACETATE ION'                                   ACT 
5 'SULFATE ION'                                   SO4 
6 'SELENIUM ATOM'                                 SE  
7 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                ? 
# 
