data_4FF9
# 
_entry.id   4FF9 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.281 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   4FF9         
RCSB  RCSB072827   
WWPDB D_1000072827 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        4FF9 
_pdbx_database_status.recvd_initial_deposition_date   2012-05-31 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Auclair, J.R.'  1 
'Brodkin, H.R.'  2 
;D'Aquino, J.A.
;
3 
'Ringe, D.'      4 
'Petsko, G.A.'   5 
'Agar, J.N.'     6 
# 
_citation.id                        primary 
_citation.title                     'Structural consequences of cysteinylation of cu/zn-superoxide dismutase.' 
_citation.journal_abbrev            Biochemistry 
_citation.journal_volume            52 
_citation.page_first                6145 
_citation.page_last                 6150 
_citation.year                      2013 
_citation.journal_id_ASTM           BICHAW 
_citation.country                   US 
_citation.journal_id_ISSN           0006-2960 
_citation.journal_id_CSD            0033 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   23919400 
_citation.pdbx_database_id_DOI      10.1021/bi400613h 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Auclair, J.R.'  1 
primary 'Brodkin, H.R.'  2 
primary 
;D'Aquino, J.A.
;
3 
primary 'Petsko, G.A.'   4 
primary 'Ringe, D.'      5 
primary 'Agar, J.N.'     6 
# 
_cell.entry_id           4FF9 
_cell.length_a           113.050 
_cell.length_b           113.050 
_cell.length_c           70.590 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        120.00 
_cell.Z_PDB              12 
_cell.pdbx_unique_axis   ? 
_cell.length_a_esd       ? 
_cell.length_b_esd       ? 
_cell.length_c_esd       ? 
_cell.angle_alpha_esd    ? 
_cell.angle_beta_esd     ? 
_cell.angle_gamma_esd    ? 
# 
_symmetry.entry_id                         4FF9 
_symmetry.space_group_name_H-M             'P 63' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                173 
_symmetry.space_group_name_Hall            ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Superoxide dismutase [Cu-Zn]' 15827.561 2  1.15.1.1 ? ? ? 
2 non-polymer syn CYSTEINE                       121.158   1  ?        ? ? ? 
3 non-polymer syn 'ZINC ION'                     65.409    2  ?        ? ? ? 
4 non-polymer syn 'COPPER (II) ION'              63.546    2  ?        ? ? ? 
5 water       nat water                          18.015    24 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Superoxide dismutase 1, hSod1' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ALA n 
1 2   THR n 
1 3   LYS n 
1 4   ALA n 
1 5   VAL n 
1 6   CYS n 
1 7   VAL n 
1 8   LEU n 
1 9   LYS n 
1 10  GLY n 
1 11  ASP n 
1 12  GLY n 
1 13  PRO n 
1 14  VAL n 
1 15  GLN n 
1 16  GLY n 
1 17  ILE n 
1 18  ILE n 
1 19  ASN n 
1 20  PHE n 
1 21  GLU n 
1 22  GLN n 
1 23  LYS n 
1 24  GLU n 
1 25  SER n 
1 26  ASN n 
1 27  GLY n 
1 28  PRO n 
1 29  VAL n 
1 30  LYS n 
1 31  VAL n 
1 32  TRP n 
1 33  GLY n 
1 34  SER n 
1 35  ILE n 
1 36  LYS n 
1 37  GLY n 
1 38  LEU n 
1 39  THR n 
1 40  GLU n 
1 41  GLY n 
1 42  LEU n 
1 43  HIS n 
1 44  GLY n 
1 45  PHE n 
1 46  HIS n 
1 47  VAL n 
1 48  HIS n 
1 49  GLU n 
1 50  PHE n 
1 51  GLY n 
1 52  ASP n 
1 53  ASN n 
1 54  THR n 
1 55  ALA n 
1 56  GLY n 
1 57  CYS n 
1 58  THR n 
1 59  SER n 
1 60  ALA n 
1 61  GLY n 
1 62  PRO n 
1 63  HIS n 
1 64  PHE n 
1 65  ASN n 
1 66  PRO n 
1 67  LEU n 
1 68  SER n 
1 69  ARG n 
1 70  LYS n 
1 71  HIS n 
1 72  GLY n 
1 73  GLY n 
1 74  PRO n 
1 75  LYS n 
1 76  ASP n 
1 77  GLU n 
1 78  GLU n 
1 79  ARG n 
1 80  HIS n 
1 81  VAL n 
1 82  GLY n 
1 83  ASP n 
1 84  LEU n 
1 85  GLY n 
1 86  ASN n 
1 87  VAL n 
1 88  THR n 
1 89  ALA n 
1 90  ASP n 
1 91  LYS n 
1 92  ASP n 
1 93  GLY n 
1 94  VAL n 
1 95  ALA n 
1 96  ASP n 
1 97  VAL n 
1 98  SER n 
1 99  ILE n 
1 100 GLU n 
1 101 ASP n 
1 102 SER n 
1 103 VAL n 
1 104 ILE n 
1 105 SER n 
1 106 LEU n 
1 107 SER n 
1 108 GLY n 
1 109 ASP n 
1 110 HIS n 
1 111 CYS n 
1 112 ILE n 
1 113 ILE n 
1 114 GLY n 
1 115 ARG n 
1 116 THR n 
1 117 LEU n 
1 118 VAL n 
1 119 VAL n 
1 120 HIS n 
1 121 GLU n 
1 122 LYS n 
1 123 ALA n 
1 124 ASP n 
1 125 ASP n 
1 126 LEU n 
1 127 GLY n 
1 128 LYS n 
1 129 GLY n 
1 130 GLY n 
1 131 ASN n 
1 132 GLU n 
1 133 GLU n 
1 134 SER n 
1 135 THR n 
1 136 LYS n 
1 137 THR n 
1 138 GLY n 
1 139 ASN n 
1 140 ALA n 
1 141 GLY n 
1 142 SER n 
1 143 ARG n 
1 144 LEU n 
1 145 ALA n 
1 146 CYS n 
1 147 GLY n 
1 148 VAL n 
1 149 ILE n 
1 150 GLY n 
1 151 ILE n 
1 152 ALA n 
1 153 GLN n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_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      'Saccharomyces cerevisiae' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     4932 
_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               'EGy118(delta SOD1)' 
_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          PLASMID 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       YEp-351 
_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.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_struct_ref.pdbx_align_begin           2 
_struct_ref.pdbx_db_isoform            ? 
# 
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 4FF9 A 1 ? 153 ? P00441 2 ? 154 ? 1 153 
2 1 4FF9 B 1 ? 153 ? P00441 2 ? 154 ? 1 153 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
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 
CU  non-polymer         . 'COPPER (II) ION' ? 'Cu 2'           63.546  
CYS 'L-peptide linking' y CYSTEINE          ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE         ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'   ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE           ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE         ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER             ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE        ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE           ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE            ? 'C6 H15 N2 O2 1' 147.195 
PHE 'L-peptide linking' y PHENYLALANINE     ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE           ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE            ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE         ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN        ? 'C11 H12 N2 O2'  204.225 
VAL 'L-peptide linking' y VALINE            ? 'C5 H11 N O2'    117.146 
ZN  non-polymer         . 'ZINC ION'        ? 'Zn 2'           65.409  
# 
_exptl.entry_id          4FF9 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      4.11 
_exptl_crystal.density_percent_sol   70.10 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.temp            298 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              6.25 
_exptl_crystal_grow.pdbx_details    '0.1M MES, pH 6.25, 20% PEG3350, VAPOR DIFFUSION, HANGING DROP, temperature 298K' 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               CCD 
_diffrn_detector.type                   'MARMOSAIC 300 mm CCD' 
_diffrn_detector.pdbx_collection_date   2011-10-26 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    'Double crystal cryo-cooled Si(111)' 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.95 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'APS BEAMLINE 23-ID-B' 
_diffrn_source.pdbx_synchrotron_site       APS 
_diffrn_source.pdbx_synchrotron_beamline   23-ID-B 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        0.95 
# 
_reflns.entry_id                     4FF9 
_reflns.observed_criterion_sigma_I   2.0 
_reflns.observed_criterion_sigma_F   0.11 
_reflns.d_resolution_low             27.154 
_reflns.d_resolution_high            2.480 
_reflns.number_obs                   16978 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         94.75 
_reflns.pdbx_Rmerge_I_obs            ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        ? 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              ? 
_reflns.R_free_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.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_chi_squared             ? 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_ordinal                 1 
_reflns.pdbx_diffrn_id               1 
# 
_reflns_shell.d_res_high             2.48 
_reflns_shell.d_res_low              2.57 
_reflns_shell.percent_possible_all   100.0 
_reflns_shell.Rmerge_I_obs           0.560 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.meanI_over_sigI_obs    4.8 
_reflns_shell.pdbx_redundancy        10.7 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      1831 
_reflns_shell.number_measured_all    ? 
_reflns_shell.number_measured_obs    ? 
_reflns_shell.number_unique_obs      ? 
_reflns_shell.pdbx_chi_squared       ? 
_reflns_shell.pdbx_ordinal           1 
_reflns_shell.pdbx_diffrn_id         1 
# 
_refine.entry_id                                 4FF9 
_refine.ls_number_reflns_obs                     16978 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.11 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             27.154 
_refine.ls_d_res_high                            2.5003 
_refine.ls_percent_reflns_obs                    94.75 
_refine.ls_R_factor_obs                          0.2822 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.2762 
_refine.ls_R_factor_R_free                       0.3351 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 9.94 
_refine.ls_number_reflns_R_free                  1688 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.B_iso_mean                               ? 
_refine.aniso_B[1][1]                            -1.5434 
_refine.aniso_B[2][2]                            -1.5434 
_refine.aniso_B[3][3]                            3.0868 
_refine.aniso_B[1][2]                            0.0000 
_refine.aniso_B[1][3]                            0.0000 
_refine.aniso_B[2][3]                            -0.0000 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_ksol                 0.304 
_refine.solvent_model_param_bsol                 29.883 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.95 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.details                                  ? 
_refine.pdbx_starting_model                      'PDB ENTRY 1SPD' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            1.04 
_refine.pdbx_overall_phase_error                 37.70 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_refine.overall_SU_R_free                        ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        2170 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         10 
_refine_hist.number_atoms_solvent             24 
_refine_hist.number_atoms_total               2204 
_refine_hist.d_res_high                       2.5003 
_refine_hist.d_res_low                        27.154 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_restraint_function 
_refine_ls_restr.pdbx_refine_id 
f_bond_d           0.009  ? ? 2233 ? 'X-RAY DIFFRACTION' 
f_angle_d          1.254  ? ? 3020 ? 'X-RAY DIFFRACTION' 
f_dihedral_angle_d 16.260 ? ? 784  ? 'X-RAY DIFFRACTION' 
f_chiral_restr     0.085  ? ? 337  ? 'X-RAY DIFFRACTION' 
f_plane_restr      0.004  ? ? 412  ? 'X-RAY DIFFRACTION' 
# 
loop_
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.pdbx_refine_id 
. 2.5003 2.5738  1056 0.3441 79.00  0.3771 . . 115 . . . . 'X-RAY DIFFRACTION' 
. 2.5738 2.6568  1205 0.3216 90.00  0.3759 . . 138 . . . . 'X-RAY DIFFRACTION' 
. 2.6568 2.7517  1197 0.3221 91.00  0.4454 . . 140 . . . . 'X-RAY DIFFRACTION' 
. 2.7517 2.8617  1236 0.3242 93.00  0.4036 . . 139 . . . . 'X-RAY DIFFRACTION' 
. 2.8617 2.9918  1268 0.3077 95.00  0.3695 . . 142 . . . . 'X-RAY DIFFRACTION' 
. 2.9918 3.1493  1301 0.2779 97.00  0.3357 . . 146 . . . . 'X-RAY DIFFRACTION' 
. 3.1493 3.3463  1334 0.2849 98.00  0.3882 . . 142 . . . . 'X-RAY DIFFRACTION' 
. 3.3463 3.6041  1312 0.2893 98.00  0.3087 . . 145 . . . . 'X-RAY DIFFRACTION' 
. 3.6041 3.9658  1323 0.2666 99.00  0.3572 . . 139 . . . . 'X-RAY DIFFRACTION' 
. 3.9658 4.5374  1351 0.2495 99.00  0.3036 . . 147 . . . . 'X-RAY DIFFRACTION' 
. 4.5374 5.7079  1353 0.2454 100.00 0.2906 . . 142 . . . . 'X-RAY DIFFRACTION' 
. 5.7079 27.1553 1354 0.2667 98.00  0.3063 . . 153 . . . . 'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  4FF9 
_struct.title                     'Crystal Structure of cysteinylated WT SOD1.' 
_struct.pdbx_descriptor           'Superoxide dismutase [Cu-Zn] (E.C.1.15.1.1)' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        4FF9 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
_struct_keywords.text            'superoxide dismutase, zinc binding, cysteinylation, OXIDOREDUCTASE' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 3 ? 
G N N 4 ? 
H N N 5 ? 
I N N 5 ? 
# 
_struct_biol.id        1 
_struct_biol.details   ? 
# 
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 1 ALA A 55  ? GLY A 61  ? ALA A 55  GLY A 61  5 ? 7 
HELX_P HELX_P2 2 GLU A 132 ? LYS A 136 ? GLU A 132 LYS A 136 5 ? 5 
HELX_P HELX_P3 3 ALA B 55  ? GLY B 61  ? ALA B 55  GLY B 61  5 ? 7 
HELX_P HELX_P4 4 GLU B 132 ? THR B 137 ? GLU B 132 THR B 137 1 ? 6 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
disulf1  disulf ? ? A CYS 57  SG  ? ? ? 1_555 A CYS 146 SG ? ? A CYS 57  A CYS 146 1_555 ? ? ? ? ? ? ? 2.050 ? 
disulf2  disulf ? ? B CYS 57  SG  ? ? ? 1_555 B CYS 146 SG ? ? B CYS 57  B CYS 146 1_555 ? ? ? ? ? ? ? 2.040 ? 
metalc1  metalc ? ? B HIS 80  ND1 ? ? ? 1_555 F ZN  .   ZN ? ? B HIS 80  B ZN  201 1_555 ? ? ? ? ? ? ? 2.024 ? 
metalc2  metalc ? ? A HIS 63  ND1 ? ? ? 1_555 D ZN  .   ZN ? ? A HIS 63  A ZN  202 1_555 ? ? ? ? ? ? ? 2.036 ? 
metalc3  metalc ? ? A ASP 83  OD2 ? ? ? 1_555 D ZN  .   ZN ? ? A ASP 83  A ZN  202 1_555 ? ? ? ? ? ? ? 2.047 ? 
metalc4  metalc ? ? A HIS 80  ND1 ? ? ? 1_555 D ZN  .   ZN ? ? A HIS 80  A ZN  202 1_555 ? ? ? ? ? ? ? 2.087 ? 
metalc5  metalc ? ? B HIS 63  ND1 ? ? ? 1_555 F ZN  .   ZN ? ? B HIS 63  B ZN  201 1_555 ? ? ? ? ? ? ? 2.150 ? 
metalc6  metalc ? ? A HIS 120 NE2 ? ? ? 1_555 E CU  .   CU ? ? A HIS 120 A CU  203 1_555 ? ? ? ? ? ? ? 2.163 ? 
metalc7  metalc ? ? A HIS 46  ND1 ? ? ? 1_555 E CU  .   CU ? ? A HIS 46  A CU  203 1_555 ? ? ? ? ? ? ? 2.179 ? 
metalc8  metalc ? ? B HIS 120 NE2 ? ? ? 1_555 G CU  .   CU ? ? B HIS 120 B CU  202 1_555 ? ? ? ? ? ? ? 2.189 ? 
metalc9  metalc ? ? B ASP 83  OD1 ? ? ? 1_555 F ZN  .   ZN ? ? B ASP 83  B ZN  201 1_555 ? ? ? ? ? ? ? 2.213 ? 
metalc10 metalc ? ? A HIS 71  ND1 ? ? ? 1_555 D ZN  .   ZN ? ? A HIS 71  A ZN  202 1_555 ? ? ? ? ? ? ? 2.236 ? 
metalc11 metalc ? ? B HIS 71  ND1 ? ? ? 1_555 F ZN  .   ZN ? ? B HIS 71  B ZN  201 1_555 ? ? ? ? ? ? ? 2.289 ? 
metalc12 metalc ? ? A HIS 48  NE2 ? ? ? 1_555 E CU  .   CU ? ? A HIS 48  A CU  203 1_555 ? ? ? ? ? ? ? 2.407 ? 
metalc13 metalc ? ? B HIS 46  NE2 ? ? ? 1_555 G CU  .   CU ? ? B HIS 46  B CU  202 1_555 ? ? ? ? ? ? ? 2.473 ? 
metalc14 metalc ? ? B HIS 48  NE2 ? ? ? 1_555 G CU  .   CU ? ? B HIS 48  B CU  202 1_555 ? ? ? ? ? ? ? 2.498 ? 
covale1  covale ? ? B CYS 111 SG  ? ? ? 1_555 C CYS .   SG ? ? B CYS 111 A CYS 201 1_555 ? ? ? ? ? ? ? 2.036 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
covale ? ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 8 ? 
B ? 6 ? 
C ? 5 ? 
D ? 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 
A 1 2 ? anti-parallel 
A 2 3 ? anti-parallel 
A 3 4 ? anti-parallel 
A 4 5 ? anti-parallel 
A 5 6 ? anti-parallel 
A 6 7 ? anti-parallel 
A 7 8 ? anti-parallel 
B 1 2 ? anti-parallel 
B 2 3 ? anti-parallel 
B 3 4 ? anti-parallel 
B 4 5 ? anti-parallel 
B 5 6 ? anti-parallel 
C 1 2 ? anti-parallel 
C 2 3 ? anti-parallel 
C 3 4 ? anti-parallel 
C 4 5 ? anti-parallel 
D 1 2 ? anti-parallel 
D 2 3 ? anti-parallel 
D 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 
A 1 ASP A 83  ? ALA A 89  ? ASP A 83  ALA A 89  
A 2 GLY A 41  ? HIS A 48  ? GLY A 41  HIS A 48  
A 3 THR A 116 ? HIS A 120 ? THR A 116 HIS A 120 
A 4 ARG A 143 ? VAL A 148 ? ARG A 143 VAL A 148 
A 5 ALA A 4   ? GLY A 10  ? ALA A 4   GLY A 10  
A 6 GLY A 16  ? GLU A 21  ? GLY A 16  GLU A 21  
A 7 VAL A 29  ? ILE A 35  ? VAL A 29  ILE A 35  
A 8 ALA A 95  ? ASP A 101 ? ALA A 95  ASP A 101 
B 1 ASP A 83  ? ALA A 89  ? ASP A 83  ALA A 89  
B 2 GLY A 41  ? HIS A 48  ? GLY A 41  HIS A 48  
B 3 THR A 116 ? HIS A 120 ? THR A 116 HIS A 120 
B 4 ARG A 143 ? VAL A 148 ? ARG A 143 VAL A 148 
B 5 ALA A 4   ? GLY A 10  ? ALA A 4   GLY A 10  
B 6 GLY A 150 ? ILE A 151 ? GLY A 150 ILE A 151 
C 1 ALA B 95  ? ASP B 101 ? ALA B 95  ASP B 101 
C 2 VAL B 29  ? ILE B 35  ? VAL B 29  ILE B 35  
C 3 GLY B 16  ? GLN B 22  ? GLY B 16  GLN B 22  
C 4 LYS B 3   ? LEU B 8   ? LYS B 3   LEU B 8   
C 5 GLY B 150 ? ILE B 151 ? GLY B 150 ILE B 151 
D 1 ASP B 83  ? ALA B 89  ? ASP B 83  ALA B 89  
D 2 GLY B 41  ? HIS B 48  ? GLY B 41  HIS B 48  
D 3 THR B 116 ? HIS B 120 ? THR B 116 HIS B 120 
D 4 ARG B 143 ? VAL B 148 ? ARG B 143 VAL B 148 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
A 1 2 O ALA A 89  ? O ALA A 89  N GLY A 41  ? N GLY A 41  
A 2 3 N HIS A 48  ? N HIS A 48  O THR A 116 ? O THR A 116 
A 3 4 N LEU A 117 ? N LEU A 117 O GLY A 147 ? O GLY A 147 
A 4 5 O CYS A 146 ? O CYS A 146 N LYS A 9   ? N LYS A 9   
A 5 6 N LEU A 8   ? N LEU A 8   O GLY A 16  ? O GLY A 16  
A 6 7 N ASN A 19  ? N ASN A 19  O TRP A 32  ? O TRP A 32  
A 7 8 N VAL A 31  ? N VAL A 31  O ILE A 99  ? O ILE A 99  
B 1 2 O ALA A 89  ? O ALA A 89  N GLY A 41  ? N GLY A 41  
B 2 3 N HIS A 48  ? N HIS A 48  O THR A 116 ? O THR A 116 
B 3 4 N LEU A 117 ? N LEU A 117 O GLY A 147 ? O GLY A 147 
B 4 5 O CYS A 146 ? O CYS A 146 N LYS A 9   ? N LYS A 9   
B 5 6 N VAL A 5   ? N VAL A 5   O GLY A 150 ? O GLY A 150 
C 1 2 O VAL B 97  ? O VAL B 97  N GLY B 33  ? N GLY B 33  
C 2 3 O TRP B 32  ? O TRP B 32  N ASN B 19  ? N ASN B 19  
C 3 4 O PHE B 20  ? O PHE B 20  N ALA B 4   ? N ALA B 4   
C 4 5 N VAL B 5   ? N VAL B 5   O GLY B 150 ? O GLY B 150 
D 1 2 O VAL B 87  ? O VAL B 87  N HIS B 43  ? N HIS B 43  
D 2 3 N GLY B 44  ? N GLY B 44  O HIS B 120 ? O HIS B 120 
D 3 4 N LEU B 117 ? N LEU B 117 O GLY B 147 ? O GLY B 147 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE CYS A 201' 
AC2 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN A 202'  
AC3 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE CU A 203'  
AC4 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE ZN B 201'  
AC5 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE CU B 202'  
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 5 SER A 107 ? SER A 107 . ? 1_555 ? 
2  AC1 5 GLY A 108 ? GLY A 108 . ? 1_555 ? 
3  AC1 5 CYS A 111 ? CYS A 111 . ? 1_555 ? 
4  AC1 5 ILE A 113 ? ILE A 113 . ? 1_555 ? 
5  AC1 5 CYS B 111 ? CYS B 111 . ? 1_555 ? 
6  AC2 4 HIS A 63  ? HIS A 63  . ? 1_555 ? 
7  AC2 4 HIS A 71  ? HIS A 71  . ? 1_555 ? 
8  AC2 4 HIS A 80  ? HIS A 80  . ? 1_555 ? 
9  AC2 4 ASP A 83  ? ASP A 83  . ? 1_555 ? 
10 AC3 4 HIS A 46  ? HIS A 46  . ? 1_555 ? 
11 AC3 4 HIS A 48  ? HIS A 48  . ? 1_555 ? 
12 AC3 4 HIS A 63  ? HIS A 63  . ? 1_555 ? 
13 AC3 4 HIS A 120 ? HIS A 120 . ? 1_555 ? 
14 AC4 5 HIS B 63  ? HIS B 63  . ? 1_555 ? 
15 AC4 5 HIS B 71  ? HIS B 71  . ? 1_555 ? 
16 AC4 5 HIS B 80  ? HIS B 80  . ? 1_555 ? 
17 AC4 5 ASP B 83  ? ASP B 83  . ? 1_555 ? 
18 AC4 5 LYS B 136 ? LYS B 136 . ? 1_555 ? 
19 AC5 4 HIS B 46  ? HIS B 46  . ? 1_555 ? 
20 AC5 4 HIS B 48  ? HIS B 48  . ? 1_555 ? 
21 AC5 4 HIS B 63  ? HIS B 63  . ? 1_555 ? 
22 AC5 4 HIS B 120 ? HIS B 120 . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          4FF9 
_database_PDB_matrix.origx[1][1]       1.000000 
_database_PDB_matrix.origx[1][2]       0.000000 
_database_PDB_matrix.origx[1][3]       0.000000 
_database_PDB_matrix.origx[2][1]       0.000000 
_database_PDB_matrix.origx[2][2]       1.000000 
_database_PDB_matrix.origx[2][3]       0.000000 
_database_PDB_matrix.origx[3][1]       0.000000 
_database_PDB_matrix.origx[3][2]       0.000000 
_database_PDB_matrix.origx[3][3]       1.000000 
_database_PDB_matrix.origx_vector[1]   0.00000 
_database_PDB_matrix.origx_vector[2]   0.00000 
_database_PDB_matrix.origx_vector[3]   0.00000 
# 
_atom_sites.entry_id                    4FF9 
_atom_sites.fract_transf_matrix[1][1]   0.008846 
_atom_sites.fract_transf_matrix[1][2]   0.005107 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.010214 
_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]   0.014166 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
CU 
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . ALA A 1 1   ? -22.654 20.561  -23.531 1.00 96.40  ? 1   ALA A N   1 
ATOM   2    C  CA  . ALA A 1 1   ? -21.228 20.731  -23.259 1.00 93.74  ? 1   ALA A CA  1 
ATOM   3    C  C   . ALA A 1 1   ? -20.977 21.568  -22.007 1.00 89.59  ? 1   ALA A C   1 
ATOM   4    O  O   . ALA A 1 1   ? -21.777 21.558  -21.073 1.00 90.08  ? 1   ALA A O   1 
ATOM   5    C  CB  . ALA A 1 1   ? -20.508 21.341  -24.467 1.00 95.63  ? 1   ALA A CB  1 
ATOM   6    N  N   . THR A 1 2   ? -19.862 22.296  -22.032 1.00 83.68  ? 2   THR A N   1 
ATOM   7    C  CA  . THR A 1 2   ? -19.293 23.059  -20.906 1.00 76.59  ? 2   THR A CA  1 
ATOM   8    C  C   . THR A 1 2   ? -19.926 23.072  -19.496 1.00 64.18  ? 2   THR A C   1 
ATOM   9    O  O   . THR A 1 2   ? -21.069 22.690  -19.278 1.00 68.47  ? 2   THR A O   1 
ATOM   10   C  CB  . THR A 1 2   ? -18.993 24.519  -21.320 1.00 84.83  ? 2   THR A CB  1 
ATOM   11   O  OG1 . THR A 1 2   ? -18.899 25.330  -20.142 1.00 89.91  ? 2   THR A OG1 1 
ATOM   12   C  CG2 . THR A 1 2   ? -20.088 25.066  -22.227 1.00 85.38  ? 2   THR A CG2 1 
ATOM   13   N  N   . LYS A 1 3   ? -19.119 23.537  -18.550 1.00 51.39  ? 3   LYS A N   1 
ATOM   14   C  CA  . LYS A 1 3   ? -19.451 23.691  -17.119 1.00 50.73  ? 3   LYS A CA  1 
ATOM   15   C  C   . LYS A 1 3   ? -20.513 22.805  -16.380 1.00 47.22  ? 3   LYS A C   1 
ATOM   16   O  O   . LYS A 1 3   ? -21.722 22.901  -16.604 1.00 46.45  ? 3   LYS A O   1 
ATOM   17   C  CB  . LYS A 1 3   ? -19.649 25.161  -16.790 1.00 52.35  ? 3   LYS A CB  1 
ATOM   18   N  N   . ALA A 1 4   ? -20.022 21.971  -15.465 1.00 42.64  ? 4   ALA A N   1 
ATOM   19   C  CA  . ALA A 1 4   ? -20.879 21.232  -14.533 1.00 43.65  ? 4   ALA A CA  1 
ATOM   20   C  C   . ALA A 1 4   ? -20.413 21.386  -13.084 1.00 41.60  ? 4   ALA A C   1 
ATOM   21   O  O   . ALA A 1 4   ? -19.355 21.955  -12.812 1.00 38.63  ? 4   ALA A O   1 
ATOM   22   C  CB  . ALA A 1 4   ? -20.953 19.757  -14.905 1.00 43.38  ? 4   ALA A CB  1 
ATOM   23   N  N   . VAL A 1 5   ? -21.219 20.891  -12.155 1.00 37.94  ? 5   VAL A N   1 
ATOM   24   C  CA  . VAL A 1 5   ? -20.820 20.883  -10.746 1.00 43.69  ? 5   VAL A CA  1 
ATOM   25   C  C   . VAL A 1 5   ? -21.513 19.764  -9.962  1.00 39.71  ? 5   VAL A C   1 
ATOM   26   O  O   . VAL A 1 5   ? -22.614 19.353  -10.286 1.00 36.43  ? 5   VAL A O   1 
ATOM   27   C  CB  . VAL A 1 5   ? -21.057 22.244  -10.055 1.00 46.91  ? 5   VAL A CB  1 
ATOM   28   C  CG1 . VAL A 1 5   ? -22.507 22.396  -9.667  1.00 45.80  ? 5   VAL A CG1 1 
ATOM   29   C  CG2 . VAL A 1 5   ? -20.195 22.348  -8.820  1.00 51.96  ? 5   VAL A CG2 1 
ATOM   30   N  N   . CYS A 1 6   ? -20.843 19.265  -8.937  1.00 37.27  ? 6   CYS A N   1 
ATOM   31   C  CA  . CYS A 1 6   ? -21.404 18.206  -8.141  1.00 36.44  ? 6   CYS A CA  1 
ATOM   32   C  C   . CYS A 1 6   ? -20.977 18.347  -6.675  1.00 39.37  ? 6   CYS A C   1 
ATOM   33   O  O   . CYS A 1 6   ? -19.813 18.160  -6.334  1.00 42.89  ? 6   CYS A O   1 
ATOM   34   C  CB  . CYS A 1 6   ? -20.996 16.845  -8.737  1.00 33.62  ? 6   CYS A CB  1 
ATOM   35   S  SG  . CYS A 1 6   ? -21.447 15.359  -7.759  1.00 41.45  ? 6   CYS A SG  1 
ATOM   36   N  N   . VAL A 1 7   ? -21.921 18.693  -5.812  1.00 39.23  ? 7   VAL A N   1 
ATOM   37   C  CA  . VAL A 1 7   ? -21.653 18.697  -4.377  1.00 43.38  ? 7   VAL A CA  1 
ATOM   38   C  C   . VAL A 1 7   ? -21.720 17.276  -3.832  1.00 48.61  ? 7   VAL A C   1 
ATOM   39   O  O   . VAL A 1 7   ? -22.777 16.640  -3.862  1.00 55.51  ? 7   VAL A O   1 
ATOM   40   C  CB  . VAL A 1 7   ? -22.673 19.529  -3.610  1.00 34.69  ? 7   VAL A CB  1 
ATOM   41   C  CG1 . VAL A 1 7   ? -22.358 19.504  -2.150  1.00 36.32  ? 7   VAL A CG1 1 
ATOM   42   C  CG2 . VAL A 1 7   ? -22.660 20.940  -4.108  1.00 38.26  ? 7   VAL A CG2 1 
ATOM   43   N  N   . LEU A 1 8   ? -20.594 16.778  -3.334  1.00 43.54  ? 8   LEU A N   1 
ATOM   44   C  CA  . LEU A 1 8   ? -20.561 15.461  -2.743  1.00 38.30  ? 8   LEU A CA  1 
ATOM   45   C  C   . LEU A 1 8   ? -20.830 15.543  -1.253  1.00 40.95  ? 8   LEU A C   1 
ATOM   46   O  O   . LEU A 1 8   ? -20.089 16.189  -0.507  1.00 38.06  ? 8   LEU A O   1 
ATOM   47   C  CB  . LEU A 1 8   ? -19.213 14.798  -2.996  1.00 36.93  ? 8   LEU A CB  1 
ATOM   48   C  CG  . LEU A 1 8   ? -19.092 14.109  -4.341  1.00 37.26  ? 8   LEU A CG  1 
ATOM   49   C  CD1 . LEU A 1 8   ? -18.893 15.141  -5.413  1.00 45.85  ? 8   LEU A CD1 1 
ATOM   50   C  CD2 . LEU A 1 8   ? -17.929 13.203  -4.317  1.00 39.23  ? 8   LEU A CD2 1 
ATOM   51   N  N   . LYS A 1 9   ? -21.911 14.885  -0.844  1.00 46.01  ? 9   LYS A N   1 
ATOM   52   C  CA  . LYS A 1 9   ? -22.339 14.797  0.551   1.00 46.82  ? 9   LYS A CA  1 
ATOM   53   C  C   . LYS A 1 9   ? -22.505 13.305  0.919   1.00 43.46  ? 9   LYS A C   1 
ATOM   54   O  O   . LYS A 1 9   ? -22.677 12.454  0.041   1.00 39.63  ? 9   LYS A O   1 
ATOM   55   C  CB  . LYS A 1 9   ? -23.656 15.569  0.724   1.00 50.84  ? 9   LYS A CB  1 
ATOM   56   C  CG  . LYS A 1 9   ? -24.081 15.851  2.157   1.00 55.05  ? 9   LYS A CG  1 
ATOM   57   C  CD  . LYS A 1 9   ? -23.019 16.631  2.937   0.00 59.16  ? 9   LYS A CD  1 
ATOM   58   C  CE  . LYS A 1 9   ? -23.459 16.904  4.381   1.00 63.06  ? 9   LYS A CE  1 
ATOM   59   N  NZ  . LYS A 1 9   ? -22.392 17.552  5.215   1.00 64.40  ? 9   LYS A NZ  1 
ATOM   60   N  N   . GLY A 1 10  ? -22.436 12.987  2.207   1.00 45.10  ? 10  GLY A N   1 
ATOM   61   C  CA  . GLY A 1 10  ? -22.614 11.617  2.668   1.00 45.65  ? 10  GLY A CA  1 
ATOM   62   C  C   . GLY A 1 10  ? -23.213 11.547  4.063   1.00 51.07  ? 10  GLY A C   1 
ATOM   63   O  O   . GLY A 1 10  ? -23.938 12.461  4.462   1.00 55.33  ? 10  GLY A O   1 
ATOM   64   N  N   . ASP A 1 11  ? -22.921 10.465  4.793   1.00 52.72  ? 11  ASP A N   1 
ATOM   65   C  CA  . ASP A 1 11  ? -23.405 10.272  6.171   1.00 54.76  ? 11  ASP A CA  1 
ATOM   66   C  C   . ASP A 1 11  ? -22.258 10.410  7.170   1.00 55.66  ? 11  ASP A C   1 
ATOM   67   O  O   . ASP A 1 11  ? -22.473 10.458  8.387   1.00 57.22  ? 11  ASP A O   1 
ATOM   68   C  CB  . ASP A 1 11  ? -24.032 8.886   6.362   1.00 56.73  ? 11  ASP A CB  1 
ATOM   69   C  CG  . ASP A 1 11  ? -25.096 8.567   5.335   1.00 61.30  ? 11  ASP A CG  1 
ATOM   70   O  OD1 . ASP A 1 11  ? -25.799 9.496   4.878   1.00 64.18  ? 11  ASP A OD1 1 
ATOM   71   O  OD2 . ASP A 1 11  ? -25.232 7.374   4.988   1.00 61.22  ? 11  ASP A OD2 1 
ATOM   72   N  N   . GLY A 1 12  ? -21.034 10.437  6.653   1.00 50.75  ? 12  GLY A N   1 
ATOM   73   C  CA  . GLY A 1 12  ? -19.869 10.630  7.488   1.00 42.63  ? 12  GLY A CA  1 
ATOM   74   C  C   . GLY A 1 12  ? -19.263 11.993  7.240   1.00 39.68  ? 12  GLY A C   1 
ATOM   75   O  O   . GLY A 1 12  ? -19.948 12.931  6.835   1.00 45.81  ? 12  GLY A O   1 
ATOM   76   N  N   . PRO A 1 13  ? -17.961 12.114  7.477   1.00 33.20  ? 13  PRO A N   1 
ATOM   77   C  CA  . PRO A 1 13  ? -17.254 13.388  7.301   1.00 34.44  ? 13  PRO A CA  1 
ATOM   78   C  C   . PRO A 1 13  ? -17.010 13.839  5.839   1.00 42.29  ? 13  PRO A C   1 
ATOM   79   O  O   . PRO A 1 13  ? -16.938 15.046  5.606   1.00 45.03  ? 13  PRO A O   1 
ATOM   80   C  CB  . PRO A 1 13  ? -15.914 13.142  7.993   1.00 36.62  ? 13  PRO A CB  1 
ATOM   81   C  CG  . PRO A 1 13  ? -15.732 11.609  7.979   1.00 37.55  ? 13  PRO A CG  1 
ATOM   82   C  CD  . PRO A 1 13  ? -17.115 11.042  8.044   1.00 33.22  ? 13  PRO A CD  1 
ATOM   83   N  N   . VAL A 1 14  ? -16.878 12.929  4.877   1.00 41.82  ? 14  VAL A N   1 
ATOM   84   C  CA  . VAL A 1 14  ? -16.340 13.376  3.588   1.00 46.35  ? 14  VAL A CA  1 
ATOM   85   C  C   . VAL A 1 14  ? -17.324 14.201  2.790   1.00 48.37  ? 14  VAL A C   1 
ATOM   86   O  O   . VAL A 1 14  ? -18.479 13.822  2.613   1.00 49.54  ? 14  VAL A O   1 
ATOM   87   C  CB  . VAL A 1 14  ? -15.662 12.256  2.699   1.00 36.66  ? 14  VAL A CB  1 
ATOM   88   C  CG1 . VAL A 1 14  ? -15.176 11.073  3.546   1.00 36.70  ? 14  VAL A CG1 1 
ATOM   89   C  CG2 . VAL A 1 14  ? -16.566 11.809  1.602   1.00 35.78  ? 14  VAL A CG2 1 
ATOM   90   N  N   . GLN A 1 15  ? -16.844 15.346  2.324   1.00 50.27  ? 15  GLN A N   1 
ATOM   91   C  CA  . GLN A 1 15  ? -17.651 16.264  1.543   1.00 51.82  ? 15  GLN A CA  1 
ATOM   92   C  C   . GLN A 1 15  ? -16.717 17.039  0.629   1.00 50.88  ? 15  GLN A C   1 
ATOM   93   O  O   . GLN A 1 15  ? -15.540 17.210  0.948   1.00 50.02  ? 15  GLN A O   1 
ATOM   94   C  CB  . GLN A 1 15  ? -18.390 17.211  2.480   1.00 54.53  ? 15  GLN A CB  1 
ATOM   95   C  CG  . GLN A 1 15  ? -17.660 17.417  3.795   1.00 60.53  ? 15  GLN A CG  1 
ATOM   96   C  CD  . GLN A 1 15  ? -17.980 18.749  4.467   1.00 67.15  ? 15  GLN A CD  1 
ATOM   97   O  OE1 . GLN A 1 15  ? -18.179 19.769  3.796   1.00 66.76  ? 15  GLN A OE1 1 
ATOM   98   N  NE2 . GLN A 1 15  ? -18.013 18.747  5.805   1.00 68.15  ? 15  GLN A NE2 1 
ATOM   99   N  N   . GLY A 1 16  ? -17.237 17.510  -0.499  1.00 40.53  ? 16  GLY A N   1 
ATOM   100  C  CA  . GLY A 1 16  ? -16.432 18.269  -1.433  1.00 40.73  ? 16  GLY A CA  1 
ATOM   101  C  C   . GLY A 1 16  ? -17.177 18.680  -2.684  1.00 42.99  ? 16  GLY A C   1 
ATOM   102  O  O   . GLY A 1 16  ? -18.160 18.038  -3.054  1.00 48.02  ? 16  GLY A O   1 
ATOM   103  N  N   . ILE A 1 17  ? -16.717 19.756  -3.325  1.00 38.88  ? 17  ILE A N   1 
ATOM   104  C  CA  . ILE A 1 17  ? -17.302 20.227  -4.577  1.00 37.82  ? 17  ILE A CA  1 
ATOM   105  C  C   . ILE A 1 17  ? -16.406 19.788  -5.720  1.00 33.02  ? 17  ILE A C   1 
ATOM   106  O  O   . ILE A 1 17  ? -15.183 19.945  -5.662  1.00 32.10  ? 17  ILE A O   1 
ATOM   107  C  CB  . ILE A 1 17  ? -17.416 21.795  -4.653  1.00 39.87  ? 17  ILE A CB  1 
ATOM   108  C  CG1 . ILE A 1 17  ? -18.340 22.370  -3.579  1.00 42.63  ? 17  ILE A CG1 1 
ATOM   109  C  CG2 . ILE A 1 17  ? -17.929 22.233  -6.017  1.00 36.88  ? 17  ILE A CG2 1 
ATOM   110  C  CD1 . ILE A 1 17  ? -17.761 22.384  -2.192  1.00 41.71  ? 17  ILE A CD1 1 
ATOM   111  N  N   . ILE A 1 18  ? -17.000 19.260  -6.775  1.00 28.70  ? 18  ILE A N   1 
ATOM   112  C  CA  . ILE A 1 18  ? -16.210 18.928  -7.948  1.00 31.56  ? 18  ILE A CA  1 
ATOM   113  C  C   . ILE A 1 18  ? -16.768 19.605  -9.170  1.00 35.70  ? 18  ILE A C   1 
ATOM   114  O  O   . ILE A 1 18  ? -17.909 19.367  -9.574  1.00 36.97  ? 18  ILE A O   1 
ATOM   115  C  CB  . ILE A 1 18  ? -16.137 17.411  -8.229  1.00 31.79  ? 18  ILE A CB  1 
ATOM   116  C  CG1 . ILE A 1 18  ? -15.632 16.644  -7.009  1.00 34.42  ? 18  ILE A CG1 1 
ATOM   117  C  CG2 . ILE A 1 18  ? -15.258 17.141  -9.453  1.00 28.99  ? 18  ILE A CG2 1 
ATOM   118  C  CD1 . ILE A 1 18  ? -14.165 16.876  -6.713  1.00 39.52  ? 18  ILE A CD1 1 
ATOM   119  N  N   . ASN A 1 19  ? -15.944 20.445  -9.770  1.00 37.60  ? 19  ASN A N   1 
ATOM   120  C  CA  . ASN A 1 19  ? -16.335 21.151  -10.971 1.00 41.78  ? 19  ASN A CA  1 
ATOM   121  C  C   . ASN A 1 19  ? -15.873 20.374  -12.191 1.00 41.18  ? 19  ASN A C   1 
ATOM   122  O  O   . ASN A 1 19  ? -14.906 19.616  -12.116 1.00 42.43  ? 19  ASN A O   1 
ATOM   123  C  CB  . ASN A 1 19  ? -15.730 22.544  -10.950 1.00 44.77  ? 19  ASN A CB  1 
ATOM   124  C  CG  . ASN A 1 19  ? -15.758 23.165  -9.560  1.00 46.01  ? 19  ASN A CG  1 
ATOM   125  O  OD1 . ASN A 1 19  ? -16.726 23.826  -9.184  1.00 54.84  ? 19  ASN A OD1 1 
ATOM   126  N  ND2 . ASN A 1 19  ? -14.699 22.958  -8.796  1.00 40.93  ? 19  ASN A ND2 1 
ATOM   127  N  N   . PHE A 1 20  ? -16.580 20.544  -13.303 1.00 36.73  ? 20  PHE A N   1 
ATOM   128  C  CA  . PHE A 1 20  ? -16.216 19.917  -14.568 1.00 35.39  ? 20  PHE A CA  1 
ATOM   129  C  C   . PHE A 1 20  ? -16.221 20.980  -15.651 1.00 39.16  ? 20  PHE A C   1 
ATOM   130  O  O   . PHE A 1 20  ? -17.212 21.673  -15.851 1.00 39.86  ? 20  PHE A O   1 
ATOM   131  C  CB  . PHE A 1 20  ? -17.254 18.866  -14.975 1.00 39.45  ? 20  PHE A CB  1 
ATOM   132  C  CG  . PHE A 1 20  ? -17.448 17.746  -13.980 1.00 38.92  ? 20  PHE A CG  1 
ATOM   133  C  CD1 . PHE A 1 20  ? -17.119 16.440  -14.322 1.00 35.85  ? 20  PHE A CD1 1 
ATOM   134  C  CD2 . PHE A 1 20  ? -18.006 17.985  -12.724 1.00 43.98  ? 20  PHE A CD2 1 
ATOM   135  C  CE1 . PHE A 1 20  ? -17.303 15.401  -13.424 1.00 37.25  ? 20  PHE A CE1 1 
ATOM   136  C  CE2 . PHE A 1 20  ? -18.213 16.931  -11.813 1.00 43.25  ? 20  PHE A CE2 1 
ATOM   137  C  CZ  . PHE A 1 20  ? -17.854 15.643  -12.163 1.00 39.60  ? 20  PHE A CZ  1 
ATOM   138  N  N   . GLU A 1 21  ? -15.131 21.118  -16.380 1.00 45.10  ? 21  GLU A N   1 
ATOM   139  C  CA  . GLU A 1 21  ? -15.157 21.992  -17.539 1.00 47.23  ? 21  GLU A CA  1 
ATOM   140  C  C   . GLU A 1 21  ? -14.984 21.133  -18.784 1.00 45.95  ? 21  GLU A C   1 
ATOM   141  O  O   . GLU A 1 21  ? -14.359 20.086  -18.708 1.00 47.52  ? 21  GLU A O   1 
ATOM   142  C  CB  . GLU A 1 21  ? -14.055 23.049  -17.418 1.00 49.65  ? 21  GLU A CB  1 
ATOM   143  C  CG  . GLU A 1 21  ? -14.124 24.161  -18.455 0.00 54.74  ? 21  GLU A CG  1 
ATOM   144  C  CD  . GLU A 1 21  ? -13.839 25.532  -17.861 1.00 58.87  ? 21  GLU A CD  1 
ATOM   145  O  OE1 . GLU A 1 21  ? -12.646 25.903  -17.739 1.00 60.14  ? 21  GLU A OE1 1 
ATOM   146  O  OE2 . GLU A 1 21  ? -14.815 26.236  -17.514 1.00 59.36  ? 21  GLU A OE2 1 
ATOM   147  N  N   . GLN A 1 22  ? -15.559 21.552  -19.911 1.00 44.29  ? 22  GLN A N   1 
ATOM   148  C  CA  . GLN A 1 22  ? -15.287 20.913  -21.200 1.00 45.38  ? 22  GLN A CA  1 
ATOM   149  C  C   . GLN A 1 22  ? -15.286 21.950  -22.333 1.00 55.45  ? 22  GLN A C   1 
ATOM   150  O  O   . GLN A 1 22  ? -16.325 22.226  -22.931 1.00 57.93  ? 22  GLN A O   1 
ATOM   151  C  CB  . GLN A 1 22  ? -16.306 19.812  -21.495 1.00 40.71  ? 22  GLN A CB  1 
ATOM   152  C  CG  . GLN A 1 22  ? -15.989 18.940  -22.720 1.00 40.31  ? 22  GLN A CG  1 
ATOM   153  C  CD  . GLN A 1 22  ? -17.123 17.983  -23.088 1.00 42.43  ? 22  GLN A CD  1 
ATOM   154  O  OE1 . GLN A 1 22  ? -18.293 18.238  -22.787 1.00 45.51  ? 22  GLN A OE1 1 
ATOM   155  N  NE2 . GLN A 1 22  ? -16.780 16.880  -23.742 1.00 39.46  ? 22  GLN A NE2 1 
ATOM   156  N  N   . LYS A 1 23  ? -14.110 22.512  -22.622 1.00 60.08  ? 23  LYS A N   1 
ATOM   157  C  CA  . LYS A 1 23  ? -13.953 23.603  -23.593 1.00 63.29  ? 23  LYS A CA  1 
ATOM   158  C  C   . LYS A 1 23  ? -14.557 23.297  -24.967 1.00 69.39  ? 23  LYS A C   1 
ATOM   159  O  O   . LYS A 1 23  ? -15.532 23.936  -25.391 1.00 67.59  ? 23  LYS A O   1 
ATOM   160  C  CB  . LYS A 1 23  ? -12.479 23.986  -23.730 1.00 58.39  ? 23  LYS A CB  1 
ATOM   161  N  N   . GLU A 1 24  ? -13.967 22.329  -25.664 1.00 73.73  ? 24  GLU A N   1 
ATOM   162  C  CA  . GLU A 1 24  ? -14.530 21.853  -26.920 1.00 76.43  ? 24  GLU A CA  1 
ATOM   163  C  C   . GLU A 1 24  ? -15.832 21.120  -26.616 1.00 76.58  ? 24  GLU A C   1 
ATOM   164  O  O   . GLU A 1 24  ? -16.401 21.293  -25.534 1.00 78.48  ? 24  GLU A O   1 
ATOM   165  C  CB  . GLU A 1 24  ? -13.547 20.942  -27.643 1.00 77.73  ? 24  GLU A CB  1 
ATOM   166  N  N   . SER A 1 25  ? -16.308 20.305  -27.555 1.00 75.25  ? 25  SER A N   1 
ATOM   167  C  CA  . SER A 1 25  ? -17.599 19.644  -27.380 1.00 75.40  ? 25  SER A CA  1 
ATOM   168  C  C   . SER A 1 25  ? -17.526 18.115  -27.386 1.00 76.67  ? 25  SER A C   1 
ATOM   169  O  O   . SER A 1 25  ? -18.244 17.449  -26.630 1.00 75.03  ? 25  SER A O   1 
ATOM   170  C  CB  . SER A 1 25  ? -18.607 20.136  -28.422 1.00 75.55  ? 25  SER A CB  1 
ATOM   171  O  OG  . SER A 1 25  ? -18.137 19.898  -29.738 0.00 76.82  ? 25  SER A OG  1 
ATOM   172  N  N   . ASN A 1 26  ? -16.666 17.557  -28.231 1.00 78.54  ? 26  ASN A N   1 
ATOM   173  C  CA  . ASN A 1 26  ? -16.537 16.106  -28.305 1.00 80.28  ? 26  ASN A CA  1 
ATOM   174  C  C   . ASN A 1 26  ? -15.243 15.567  -27.679 1.00 79.00  ? 26  ASN A C   1 
ATOM   175  O  O   . ASN A 1 26  ? -14.833 14.438  -27.962 1.00 80.18  ? 26  ASN A O   1 
ATOM   176  C  CB  . ASN A 1 26  ? -16.665 15.631  -29.760 1.00 81.92  ? 26  ASN A CB  1 
ATOM   177  C  CG  . ASN A 1 26  ? -15.571 16.183  -30.657 1.00 82.49  ? 26  ASN A CG  1 
ATOM   178  O  OD1 . ASN A 1 26  ? -15.097 17.302  -30.463 0.00 83.13  ? 26  ASN A OD1 1 
ATOM   179  N  ND2 . ASN A 1 26  ? -15.165 15.396  -31.647 0.00 83.38  ? 26  ASN A ND2 1 
ATOM   180  N  N   . GLY A 1 27  ? -14.605 16.364  -26.825 1.00 73.46  ? 27  GLY A N   1 
ATOM   181  C  CA  . GLY A 1 27  ? -13.273 16.023  -26.362 1.00 67.53  ? 27  GLY A CA  1 
ATOM   182  C  C   . GLY A 1 27  ? -13.072 15.749  -24.880 1.00 62.18  ? 27  GLY A C   1 
ATOM   183  O  O   . GLY A 1 27  ? -13.750 14.908  -24.273 1.00 61.43  ? 27  GLY A O   1 
ATOM   184  N  N   . PRO A 1 28  ? -12.103 16.453  -24.293 1.00 57.82  ? 28  PRO A N   1 
ATOM   185  C  CA  . PRO A 1 28  ? -11.608 16.215  -22.941 1.00 52.47  ? 28  PRO A CA  1 
ATOM   186  C  C   . PRO A 1 28  ? -12.251 17.088  -21.869 1.00 49.10  ? 28  PRO A C   1 
ATOM   187  O  O   . PRO A 1 28  ? -12.477 18.287  -22.069 1.00 50.44  ? 28  PRO A O   1 
ATOM   188  C  CB  . PRO A 1 28  ? -10.122 16.548  -23.067 1.00 54.72  ? 28  PRO A CB  1 
ATOM   189  C  CG  . PRO A 1 28  ? -10.079 17.625  -24.084 1.00 56.54  ? 28  PRO A CG  1 
ATOM   190  C  CD  . PRO A 1 28  ? -11.223 17.367  -25.045 1.00 59.08  ? 28  PRO A CD  1 
ATOM   191  N  N   . VAL A 1 29  ? -12.526 16.463  -20.725 1.00 32.08  ? 29  VAL A N   1 
ATOM   192  C  CA  . VAL A 1 29  ? -13.147 17.133  -19.603 1.00 34.66  ? 29  VAL A CA  1 
ATOM   193  C  C   . VAL A 1 29  ? -12.113 17.263  -18.478 1.00 31.75  ? 29  VAL A C   1 
ATOM   194  O  O   . VAL A 1 29  ? -11.553 16.280  -18.009 1.00 32.60  ? 29  VAL A O   1 
ATOM   195  C  CB  . VAL A 1 29  ? -14.420 16.344  -19.111 1.00 40.05  ? 29  VAL A CB  1 
ATOM   196  C  CG1 . VAL A 1 29  ? -14.924 16.849  -17.768 1.00 38.68  ? 29  VAL A CG1 1 
ATOM   197  C  CG2 . VAL A 1 29  ? -15.522 16.387  -20.148 1.00 35.73  ? 29  VAL A CG2 1 
ATOM   198  N  N   . LYS A 1 30  ? -11.845 18.486  -18.066 1.00 31.25  ? 30  LYS A N   1 
ATOM   199  C  CA  . LYS A 1 30  ? -11.012 18.691  -16.907 1.00 37.16  ? 30  LYS A CA  1 
ATOM   200  C  C   . LYS A 1 30  ? -11.900 18.553  -15.673 1.00 35.94  ? 30  LYS A C   1 
ATOM   201  O  O   . LYS A 1 30  ? -12.896 19.231  -15.529 1.00 35.88  ? 30  LYS A O   1 
ATOM   202  C  CB  . LYS A 1 30  ? -10.318 20.049  -16.961 1.00 37.56  ? 30  LYS A CB  1 
ATOM   203  C  CG  . LYS A 1 30  ? -9.278  20.138  -18.055 0.00 41.26  ? 30  LYS A CG  1 
ATOM   204  C  CD  . LYS A 1 30  ? -8.324  21.292  -17.839 0.00 44.57  ? 30  LYS A CD  1 
ATOM   205  C  CE  . LYS A 1 30  ? -7.001  20.985  -18.510 1.00 47.90  ? 30  LYS A CE  1 
ATOM   206  N  NZ  . LYS A 1 30  ? -6.078  22.160  -18.581 1.00 52.51  ? 30  LYS A NZ  1 
ATOM   207  N  N   . VAL A 1 31  ? -11.551 17.640  -14.793 1.00 36.15  ? 31  VAL A N   1 
ATOM   208  C  CA  . VAL A 1 31  ? -12.313 17.492  -13.579 1.00 37.99  ? 31  VAL A CA  1 
ATOM   209  C  C   . VAL A 1 31  ? -11.467 18.030  -12.447 1.00 36.04  ? 31  VAL A C   1 
ATOM   210  O  O   . VAL A 1 31  ? -10.323 17.615  -12.286 1.00 38.38  ? 31  VAL A O   1 
ATOM   211  C  CB  . VAL A 1 31  ? -12.636 16.008  -13.327 1.00 36.75  ? 31  VAL A CB  1 
ATOM   212  C  CG1 . VAL A 1 31  ? -13.406 15.842  -12.034 1.00 20.37  ? 31  VAL A CG1 1 
ATOM   213  C  CG2 . VAL A 1 31  ? -13.393 15.426  -14.520 1.00 30.98  ? 31  VAL A CG2 1 
ATOM   214  N  N   . TRP A 1 32  ? -11.991 18.958  -11.659 1.00 34.74  ? 32  TRP A N   1 
ATOM   215  C  CA  . TRP A 1 32  ? -11.179 19.437  -10.543 1.00 33.99  ? 32  TRP A CA  1 
ATOM   216  C  C   . TRP A 1 32  ? -11.977 19.903  -9.345  1.00 30.11  ? 32  TRP A C   1 
ATOM   217  O  O   . TRP A 1 32  ? -13.129 20.306  -9.475  1.00 29.99  ? 32  TRP A O   1 
ATOM   218  C  CB  . TRP A 1 32  ? -10.263 20.567  -11.000 1.00 37.05  ? 32  TRP A CB  1 
ATOM   219  C  CG  . TRP A 1 32  ? -10.910 21.913  -10.886 1.00 42.65  ? 32  TRP A CG  1 
ATOM   220  C  CD1 . TRP A 1 32  ? -10.878 22.752  -9.805  1.00 43.57  ? 32  TRP A CD1 1 
ATOM   221  C  CD2 . TRP A 1 32  ? -11.685 22.580  -11.888 1.00 41.37  ? 32  TRP A CD2 1 
ATOM   222  N  NE1 . TRP A 1 32  ? -11.577 23.896  -10.078 1.00 43.65  ? 32  TRP A NE1 1 
ATOM   223  C  CE2 . TRP A 1 32  ? -12.082 23.817  -11.345 1.00 40.23  ? 32  TRP A CE2 1 
ATOM   224  C  CE3 . TRP A 1 32  ? -12.075 22.250  -13.185 1.00 43.30  ? 32  TRP A CE3 1 
ATOM   225  C  CZ2 . TRP A 1 32  ? -12.859 24.726  -12.059 1.00 39.61  ? 32  TRP A CZ2 1 
ATOM   226  C  CZ3 . TRP A 1 32  ? -12.849 23.157  -13.894 1.00 45.11  ? 32  TRP A CZ3 1 
ATOM   227  C  CH2 . TRP A 1 32  ? -13.227 24.382  -13.331 1.00 42.69  ? 32  TRP A CH2 1 
ATOM   228  N  N   . GLY A 1 33  ? -11.342 19.876  -8.179  1.00 26.94  ? 33  GLY A N   1 
ATOM   229  C  CA  . GLY A 1 33  ? -11.993 20.343  -6.986  1.00 26.53  ? 33  GLY A CA  1 
ATOM   230  C  C   . GLY A 1 33  ? -11.416 19.703  -5.755  1.00 36.22  ? 33  GLY A C   1 
ATOM   231  O  O   . GLY A 1 33  ? -10.359 19.081  -5.807  1.00 44.20  ? 33  GLY A O   1 
ATOM   232  N  N   . SER A 1 34  ? -12.133 19.837  -4.648  1.00 34.27  ? 34  SER A N   1 
ATOM   233  C  CA  . SER A 1 34  ? -11.607 19.446  -3.356  1.00 37.77  ? 34  SER A CA  1 
ATOM   234  C  C   . SER A 1 34  ? -12.598 18.646  -2.500  1.00 39.38  ? 34  SER A C   1 
ATOM   235  O  O   . SER A 1 34  ? -13.773 18.999  -2.411  1.00 42.13  ? 34  SER A O   1 
ATOM   236  C  CB  . SER A 1 34  ? -11.156 20.687  -2.600  1.00 35.02  ? 34  SER A CB  1 
ATOM   237  O  OG  . SER A 1 34  ? -11.093 20.413  -1.220  1.00 36.80  ? 34  SER A OG  1 
ATOM   238  N  N   . ILE A 1 35  ? -12.096 17.587  -1.865  1.00 33.56  ? 35  ILE A N   1 
ATOM   239  C  CA  . ILE A 1 35  ? -12.881 16.713  -1.014  1.00 31.40  ? 35  ILE A CA  1 
ATOM   240  C  C   . ILE A 1 35  ? -12.180 16.498  0.326   1.00 32.53  ? 35  ILE A C   1 
ATOM   241  O  O   . ILE A 1 35  ? -10.979 16.226  0.377   1.00 41.69  ? 35  ILE A O   1 
ATOM   242  C  CB  . ILE A 1 35  ? -13.012 15.340  -1.655  1.00 32.04  ? 35  ILE A CB  1 
ATOM   243  C  CG1 . ILE A 1 35  ? -13.672 15.436  -3.035  1.00 36.44  ? 35  ILE A CG1 1 
ATOM   244  C  CG2 . ILE A 1 35  ? -13.724 14.400  -0.726  1.00 18.54  ? 35  ILE A CG2 1 
ATOM   245  C  CD1 . ILE A 1 35  ? -13.461 14.183  -3.906  1.00 16.05  ? 35  ILE A CD1 1 
ATOM   246  N  N   . LYS A 1 36  ? -12.938 16.585  1.409   1.00 28.98  ? 36  LYS A N   1 
ATOM   247  C  CA  . LYS A 1 36  ? -12.373 16.576  2.757   1.00 29.63  ? 36  LYS A CA  1 
ATOM   248  C  C   . LYS A 1 36  ? -12.743 15.304  3.458   1.00 34.29  ? 36  LYS A C   1 
ATOM   249  O  O   . LYS A 1 36  ? -13.456 14.475  2.888   1.00 34.89  ? 36  LYS A O   1 
ATOM   250  C  CB  . LYS A 1 36  ? -12.885 17.771  3.562   1.00 31.13  ? 36  LYS A CB  1 
ATOM   251  N  N   . GLY A 1 37  ? -12.247 15.148  4.688   1.00 34.28  ? 37  GLY A N   1 
ATOM   252  C  CA  . GLY A 1 37  ? -12.683 14.079  5.578   1.00 33.32  ? 37  GLY A CA  1 
ATOM   253  C  C   . GLY A 1 37  ? -12.227 12.664  5.258   1.00 35.92  ? 37  GLY A C   1 
ATOM   254  O  O   . GLY A 1 37  ? -12.568 11.729  5.970   1.00 40.89  ? 37  GLY A O   1 
ATOM   255  N  N   . LEU A 1 38  ? -11.467 12.499  4.184   1.00 34.54  ? 38  LEU A N   1 
ATOM   256  C  CA  . LEU A 1 38  ? -11.023 11.184  3.750   1.00 31.56  ? 38  LEU A CA  1 
ATOM   257  C  C   . LEU A 1 38  ? -9.804  10.685  4.527   1.00 36.71  ? 38  LEU A C   1 
ATOM   258  O  O   . LEU A 1 38  ? -9.069  11.469  5.130   1.00 41.35  ? 38  LEU A O   1 
ATOM   259  C  CB  . LEU A 1 38  ? -10.654 11.242  2.273   1.00 26.67  ? 38  LEU A CB  1 
ATOM   260  C  CG  . LEU A 1 38  ? -11.728 11.537  1.231   1.00 25.78  ? 38  LEU A CG  1 
ATOM   261  C  CD1 . LEU A 1 38  ? -11.071 12.149  -0.012  1.00 31.60  ? 38  LEU A CD1 1 
ATOM   262  C  CD2 . LEU A 1 38  ? -12.501 10.281  0.860   1.00 21.37  ? 38  LEU A CD2 1 
ATOM   263  N  N   . THR A 1 39  ? -9.567  9.378   4.487   1.00 32.44  ? 39  THR A N   1 
ATOM   264  C  CA  . THR A 1 39  ? -8.285  8.855   4.941   1.00 29.66  ? 39  THR A CA  1 
ATOM   265  C  C   . THR A 1 39  ? -7.210  9.056   3.875   1.00 38.08  ? 39  THR A C   1 
ATOM   266  O  O   . THR A 1 39  ? -7.479  8.974   2.645   1.00 37.44  ? 39  THR A O   1 
ATOM   267  C  CB  . THR A 1 39  ? -8.348  7.366   5.233   1.00 26.73  ? 39  THR A CB  1 
ATOM   268  O  OG1 . THR A 1 39  ? -8.927  6.719   4.095   1.00 30.66  ? 39  THR A OG1 1 
ATOM   269  C  CG2 . THR A 1 39  ? -9.173  7.074   6.506   1.00 24.93  ? 39  THR A CG2 1 
ATOM   270  N  N   . GLU A 1 40  ? -5.992  9.305   4.355   1.00 36.48  ? 40  GLU A N   1 
ATOM   271  C  CA  . GLU A 1 40  ? -4.850  9.493   3.483   1.00 34.57  ? 40  GLU A CA  1 
ATOM   272  C  C   . GLU A 1 40  ? -4.737  8.323   2.521   1.00 33.55  ? 40  GLU A C   1 
ATOM   273  O  O   . GLU A 1 40  ? -4.983  7.171   2.875   1.00 35.08  ? 40  GLU A O   1 
ATOM   274  C  CB  . GLU A 1 40  ? -3.556  9.631   4.294   1.00 39.22  ? 40  GLU A CB  1 
ATOM   275  C  CG  . GLU A 1 40  ? -2.522  10.553  3.658   1.00 42.00  ? 40  GLU A CG  1 
ATOM   276  C  CD  . GLU A 1 40  ? -1.104  10.324  4.167   1.00 45.06  ? 40  GLU A CD  1 
ATOM   277  O  OE1 . GLU A 1 40  ? -0.937  9.853   5.316   1.00 44.32  ? 40  GLU A OE1 1 
ATOM   278  O  OE2 . GLU A 1 40  ? -0.150  10.630  3.410   1.00 44.54  ? 40  GLU A OE2 1 
ATOM   279  N  N   . GLY A 1 41  ? -4.379  8.616   1.284   1.00 36.79  ? 41  GLY A N   1 
ATOM   280  C  CA  . GLY A 1 41  ? -4.172  7.554   0.326   1.00 38.66  ? 41  GLY A CA  1 
ATOM   281  C  C   . GLY A 1 41  ? -5.162  7.609   -0.804  1.00 41.40  ? 41  GLY A C   1 
ATOM   282  O  O   . GLY A 1 41  ? -5.778  8.648   -1.066  1.00 43.16  ? 41  GLY A O   1 
ATOM   283  N  N   . LEU A 1 42  ? -5.311  6.477   -1.479  1.00 42.40  ? 42  LEU A N   1 
ATOM   284  C  CA  . LEU A 1 42  ? -6.074  6.418   -2.719  1.00 37.75  ? 42  LEU A CA  1 
ATOM   285  C  C   . LEU A 1 42  ? -7.545  6.151   -2.458  1.00 34.44  ? 42  LEU A C   1 
ATOM   286  O  O   . LEU A 1 42  ? -7.894  5.447   -1.500  1.00 32.40  ? 42  LEU A O   1 
ATOM   287  C  CB  . LEU A 1 42  ? -5.514  5.322   -3.611  1.00 33.93  ? 42  LEU A CB  1 
ATOM   288  C  CG  . LEU A 1 42  ? -4.149  5.545   -4.243  1.00 25.47  ? 42  LEU A CG  1 
ATOM   289  C  CD1 . LEU A 1 42  ? -3.757  4.275   -4.916  1.00 20.77  ? 42  LEU A CD1 1 
ATOM   290  C  CD2 . LEU A 1 42  ? -4.205  6.662   -5.240  1.00 24.82  ? 42  LEU A CD2 1 
ATOM   291  N  N   . HIS A 1 43  ? -8.392  6.722   -3.313  1.00 28.85  ? 43  HIS A N   1 
ATOM   292  C  CA  . HIS A 1 43  ? -9.840  6.548   -3.226  1.00 21.33  ? 43  HIS A CA  1 
ATOM   293  C  C   . HIS A 1 43  ? -10.503 6.461   -4.590  1.00 24.54  ? 43  HIS A C   1 
ATOM   294  O  O   . HIS A 1 43  ? -10.233 7.264   -5.479  1.00 31.84  ? 43  HIS A O   1 
ATOM   295  C  CB  . HIS A 1 43  ? -10.469 7.647   -2.394  1.00 15.68  ? 43  HIS A CB  1 
ATOM   296  C  CG  . HIS A 1 43  ? -10.157 7.528   -0.938  1.00 28.56  ? 43  HIS A CG  1 
ATOM   297  N  ND1 . HIS A 1 43  ? -11.027 6.958   -0.035  1.00 27.96  ? 43  HIS A ND1 1 
ATOM   298  C  CD2 . HIS A 1 43  ? -9.060  7.887   -0.233  1.00 34.10  ? 43  HIS A CD2 1 
ATOM   299  C  CE1 . HIS A 1 43  ? -10.483 6.983   1.167   1.00 30.31  ? 43  HIS A CE1 1 
ATOM   300  N  NE2 . HIS A 1 43  ? -9.294  7.545   1.077   1.00 32.52  ? 43  HIS A NE2 1 
ATOM   301  N  N   . GLY A 1 44  ? -11.372 5.469   -4.742  1.00 21.79  ? 44  GLY A N   1 
ATOM   302  C  CA  . GLY A 1 44  ? -12.056 5.253   -5.994  1.00 21.60  ? 44  GLY A CA  1 
ATOM   303  C  C   . GLY A 1 44  ? -12.942 6.447   -6.272  1.00 24.75  ? 44  GLY A C   1 
ATOM   304  O  O   . GLY A 1 44  ? -13.487 7.080   -5.342  1.00 16.25  ? 44  GLY A O   1 
ATOM   305  N  N   . PHE A 1 45  ? -13.099 6.727   -7.566  1.00 23.45  ? 45  PHE A N   1 
ATOM   306  C  CA  . PHE A 1 45  ? -13.747 7.913   -8.024  1.00 16.60  ? 45  PHE A CA  1 
ATOM   307  C  C   . PHE A 1 45  ? -14.382 7.619   -9.393  1.00 31.26  ? 45  PHE A C   1 
ATOM   308  O  O   . PHE A 1 45  ? -13.685 7.472   -10.391 1.00 24.00  ? 45  PHE A O   1 
ATOM   309  C  CB  . PHE A 1 45  ? -12.674 8.977   -8.102  1.00 19.46  ? 45  PHE A CB  1 
ATOM   310  C  CG  . PHE A 1 45  ? -13.191 10.381  -8.229  1.00 27.00  ? 45  PHE A CG  1 
ATOM   311  C  CD1 . PHE A 1 45  ? -13.744 11.021  -7.143  1.00 20.32  ? 45  PHE A CD1 1 
ATOM   312  C  CD2 . PHE A 1 45  ? -13.100 11.064  -9.443  1.00 31.36  ? 45  PHE A CD2 1 
ATOM   313  C  CE1 . PHE A 1 45  ? -14.206 12.299  -7.245  1.00 22.29  ? 45  PHE A CE1 1 
ATOM   314  C  CE2 . PHE A 1 45  ? -13.565 12.346  -9.556  1.00 26.64  ? 45  PHE A CE2 1 
ATOM   315  C  CZ  . PHE A 1 45  ? -14.116 12.972  -8.454  1.00 28.50  ? 45  PHE A CZ  1 
ATOM   316  N  N   . HIS A 1 46  ? -15.715 7.509   -9.427  1.00 30.75  ? 46  HIS A N   1 
ATOM   317  C  CA  . HIS A 1 46  ? -16.400 7.160   -10.659 1.00 27.69  ? 46  HIS A CA  1 
ATOM   318  C  C   . HIS A 1 46  ? -17.730 7.857   -10.825 1.00 26.61  ? 46  HIS A C   1 
ATOM   319  O  O   . HIS A 1 46  ? -18.332 8.339   -9.870  1.00 19.83  ? 46  HIS A O   1 
ATOM   320  C  CB  . HIS A 1 46  ? -16.665 5.650   -10.754 1.00 30.10  ? 46  HIS A CB  1 
ATOM   321  C  CG  . HIS A 1 46  ? -15.627 4.802   -10.084 1.00 32.16  ? 46  HIS A CG  1 
ATOM   322  N  ND1 . HIS A 1 46  ? -15.786 4.304   -8.810  1.00 26.76  ? 46  HIS A ND1 1 
ATOM   323  C  CD2 . HIS A 1 46  ? -14.415 4.373   -10.509 1.00 29.47  ? 46  HIS A CD2 1 
ATOM   324  C  CE1 . HIS A 1 46  ? -14.722 3.597   -8.480  1.00 24.18  ? 46  HIS A CE1 1 
ATOM   325  N  NE2 . HIS A 1 46  ? -13.876 3.622   -9.493  1.00 24.50  ? 46  HIS A NE2 1 
ATOM   326  N  N   . VAL A 1 47  ? -18.194 7.886   -12.068 1.00 28.11  ? 47  VAL A N   1 
ATOM   327  C  CA  . VAL A 1 47  ? -19.573 8.221   -12.314 1.00 31.99  ? 47  VAL A CA  1 
ATOM   328  C  C   . VAL A 1 47  ? -20.386 6.932   -12.350 1.00 30.76  ? 47  VAL A C   1 
ATOM   329  O  O   . VAL A 1 47  ? -20.068 5.996   -13.071 1.00 20.52  ? 47  VAL A O   1 
ATOM   330  C  CB  . VAL A 1 47  ? -19.752 8.992   -13.634 1.00 36.07  ? 47  VAL A CB  1 
ATOM   331  C  CG1 . VAL A 1 47  ? -21.210 9.423   -13.790 1.00 38.22  ? 47  VAL A CG1 1 
ATOM   332  C  CG2 . VAL A 1 47  ? -18.809 10.187  -13.686 1.00 27.63  ? 47  VAL A CG2 1 
ATOM   333  N  N   . HIS A 1 48  ? -21.427 6.882   -11.536 1.00 39.42  ? 48  HIS A N   1 
ATOM   334  C  CA  . HIS A 1 48  ? -22.392 5.790   -11.582 1.00 36.95  ? 48  HIS A CA  1 
ATOM   335  C  C   . HIS A 1 48  ? -23.510 6.102   -12.569 1.00 40.25  ? 48  HIS A C   1 
ATOM   336  O  O   . HIS A 1 48  ? -23.581 7.210   -13.103 1.00 40.74  ? 48  HIS A O   1 
ATOM   337  C  CB  . HIS A 1 48  ? -22.899 5.505   -10.171 1.00 31.56  ? 48  HIS A CB  1 
ATOM   338  C  CG  . HIS A 1 48  ? -21.892 4.766   -9.352  1.00 31.87  ? 48  HIS A CG  1 
ATOM   339  N  ND1 . HIS A 1 48  ? -22.173 3.582   -8.697  1.00 29.57  ? 48  HIS A ND1 1 
ATOM   340  C  CD2 . HIS A 1 48  ? -20.567 4.985   -9.181  1.00 23.78  ? 48  HIS A CD2 1 
ATOM   341  C  CE1 . HIS A 1 48  ? -21.074 3.130   -8.125  1.00 22.29  ? 48  HIS A CE1 1 
ATOM   342  N  NE2 . HIS A 1 48  ? -20.089 3.968   -8.394  1.00 17.73  ? 48  HIS A NE2 1 
ATOM   343  N  N   . GLU A 1 49  ? -24.372 5.126   -12.821 1.00 44.34  ? 49  GLU A N   1 
ATOM   344  C  CA  . GLU A 1 49  ? -25.316 5.226   -13.925 1.00 46.25  ? 49  GLU A CA  1 
ATOM   345  C  C   . GLU A 1 49  ? -26.483 6.172   -13.650 1.00 42.73  ? 49  GLU A C   1 
ATOM   346  O  O   . GLU A 1 49  ? -26.944 6.862   -14.566 1.00 37.20  ? 49  GLU A O   1 
ATOM   347  C  CB  . GLU A 1 49  ? -25.837 3.836   -14.294 1.00 46.97  ? 49  GLU A CB  1 
ATOM   348  C  CG  . GLU A 1 49  ? -26.471 3.715   -15.677 1.00 46.54  ? 49  GLU A CG  1 
ATOM   349  C  CD  . GLU A 1 49  ? -26.890 2.280   -15.982 1.00 53.85  ? 49  GLU A CD  1 
ATOM   350  O  OE1 . GLU A 1 49  ? -26.653 1.396   -15.123 1.00 56.92  ? 49  GLU A OE1 1 
ATOM   351  O  OE2 . GLU A 1 49  ? -27.458 2.028   -17.067 1.00 56.57  ? 49  GLU A OE2 1 
ATOM   352  N  N   . PHE A 1 50  ? -26.950 6.199   -12.401 1.00 38.57  ? 50  PHE A N   1 
ATOM   353  C  CA  . PHE A 1 50  ? -28.186 6.900   -12.066 1.00 38.56  ? 50  PHE A CA  1 
ATOM   354  C  C   . PHE A 1 50  ? -28.007 8.047   -11.094 1.00 40.61  ? 50  PHE A C   1 
ATOM   355  O  O   . PHE A 1 50  ? -27.439 7.870   -10.014 1.00 44.59  ? 50  PHE A O   1 
ATOM   356  C  CB  . PHE A 1 50  ? -29.225 5.947   -11.464 1.00 41.78  ? 50  PHE A CB  1 
ATOM   357  C  CG  . PHE A 1 50  ? -29.370 4.642   -12.199 1.00 46.67  ? 50  PHE A CG  1 
ATOM   358  C  CD1 . PHE A 1 50  ? -29.825 4.612   -13.516 1.00 48.36  ? 50  PHE A CD1 1 
ATOM   359  C  CD2 . PHE A 1 50  ? -29.085 3.441   -11.563 1.00 41.83  ? 50  PHE A CD2 1 
ATOM   360  C  CE1 . PHE A 1 50  ? -29.967 3.408   -14.184 1.00 44.27  ? 50  PHE A CE1 1 
ATOM   361  C  CE2 . PHE A 1 50  ? -29.221 2.244   -12.225 1.00 40.04  ? 50  PHE A CE2 1 
ATOM   362  C  CZ  . PHE A 1 50  ? -29.666 2.222   -13.534 1.00 42.27  ? 50  PHE A CZ  1 
ATOM   363  N  N   . GLY A 1 51  ? -28.560 9.203   -11.453 1.00 41.46  ? 51  GLY A N   1 
ATOM   364  C  CA  . GLY A 1 51  ? -28.597 10.356  -10.570 1.00 42.71  ? 51  GLY A CA  1 
ATOM   365  C  C   . GLY A 1 51  ? -29.741 10.234  -9.585  1.00 45.20  ? 51  GLY A C   1 
ATOM   366  O  O   . GLY A 1 51  ? -30.568 11.148  -9.411  1.00 45.79  ? 51  GLY A O   1 
ATOM   367  N  N   . ASP A 1 52  ? -29.747 9.078   -8.931  1.00 43.16  ? 52  ASP A N   1 
ATOM   368  C  CA  . ASP A 1 52  ? -30.801 8.620   -8.042  1.00 41.03  ? 52  ASP A CA  1 
ATOM   369  C  C   . ASP A 1 52  ? -30.227 8.532   -6.622  1.00 39.93  ? 52  ASP A C   1 
ATOM   370  O  O   . ASP A 1 52  ? -29.368 7.685   -6.331  1.00 45.66  ? 52  ASP A O   1 
ATOM   371  C  CB  . ASP A 1 52  ? -31.267 7.242   -8.528  1.00 37.93  ? 52  ASP A CB  1 
ATOM   372  C  CG  . ASP A 1 52  ? -32.601 6.816   -7.942  1.00 40.85  ? 52  ASP A CG  1 
ATOM   373  O  OD1 . ASP A 1 52  ? -32.924 7.212   -6.794  1.00 40.96  ? 52  ASP A OD1 1 
ATOM   374  O  OD2 . ASP A 1 52  ? -33.319 6.063   -8.648  1.00 37.06  ? 52  ASP A OD2 1 
ATOM   375  N  N   A ASN A 1 53  ? -30.708 9.417   -5.746  0.50 35.97  ? 53  ASN A N   1 
ATOM   376  N  N   B ASN A 1 53  ? -30.666 9.416   -5.742  0.50 35.88  ? 53  ASN A N   1 
ATOM   377  C  CA  A ASN A 1 53  ? -30.228 9.520   -4.366  0.50 34.94  ? 53  ASN A CA  1 
ATOM   378  C  CA  B ASN A 1 53  ? -30.177 9.374   -4.377  0.50 34.82  ? 53  ASN A CA  1 
ATOM   379  C  C   A ASN A 1 53  ? -31.295 9.112   -3.350  0.50 36.70  ? 53  ASN A C   1 
ATOM   380  C  C   B ASN A 1 53  ? -31.299 9.137   -3.362  0.50 36.71  ? 53  ASN A C   1 
ATOM   381  O  O   A ASN A 1 53  ? -31.114 9.267   -2.142  0.50 36.75  ? 53  ASN A O   1 
ATOM   382  O  O   B ASN A 1 53  ? -31.156 9.422   -2.174  0.50 36.85  ? 53  ASN A O   1 
ATOM   383  C  CB  A ASN A 1 53  ? -29.750 10.953  -4.074  0.50 34.80  ? 53  ASN A CB  1 
ATOM   384  C  CB  B ASN A 1 53  ? -29.325 10.618  -4.061  0.50 34.74  ? 53  ASN A CB  1 
ATOM   385  C  CG  A ASN A 1 53  ? -29.010 11.079  -2.739  0.50 34.21  ? 53  ASN A CG  1 
ATOM   386  C  CG  B ASN A 1 53  ? -27.955 10.598  -4.773  0.50 32.24  ? 53  ASN A CG  1 
ATOM   387  O  OD1 A ASN A 1 53  ? -29.453 11.783  -1.840  0.50 28.85  ? 53  ASN A OD1 1 
ATOM   388  O  OD1 B ASN A 1 53  ? -27.472 9.543   -5.186  0.50 26.50  ? 53  ASN A OD1 1 
ATOM   389  N  ND2 A ASN A 1 53  ? -27.877 10.398  -2.616  0.50 26.95  ? 53  ASN A ND2 1 
ATOM   390  N  ND2 B ASN A 1 53  ? -27.332 11.772  -4.906  0.50 30.42  ? 53  ASN A ND2 1 
ATOM   391  N  N   . THR A 1 54  ? -32.408 8.583   -3.844  1.00 38.06  ? 54  THR A N   1 
ATOM   392  C  CA  . THR A 1 54  ? -33.502 8.195   -2.967  1.00 46.75  ? 54  THR A CA  1 
ATOM   393  C  C   . THR A 1 54  ? -33.017 7.332   -1.795  1.00 49.29  ? 54  THR A C   1 
ATOM   394  O  O   . THR A 1 54  ? -33.237 7.674   -0.629  1.00 50.35  ? 54  THR A O   1 
ATOM   395  C  CB  . THR A 1 54  ? -34.651 7.513   -3.736  1.00 52.70  ? 54  THR A CB  1 
ATOM   396  O  OG1 . THR A 1 54  ? -34.122 6.498   -4.589  1.00 55.82  ? 54  THR A OG1 1 
ATOM   397  C  CG2 . THR A 1 54  ? -35.369 8.535   -4.599  1.00 54.49  ? 54  THR A CG2 1 
ATOM   398  N  N   . ALA A 1 55  ? -32.336 6.231   -2.102  1.00 49.30  ? 55  ALA A N   1 
ATOM   399  C  CA  . ALA A 1 55  ? -31.798 5.345   -1.071  1.00 45.66  ? 55  ALA A CA  1 
ATOM   400  C  C   . ALA A 1 55  ? -30.320 5.620   -0.883  1.00 47.13  ? 55  ALA A C   1 
ATOM   401  O  O   . ALA A 1 55  ? -29.506 4.694   -0.821  1.00 50.52  ? 55  ALA A O   1 
ATOM   402  C  CB  . ALA A 1 55  ? -32.026 3.884   -1.438  1.00 40.46  ? 55  ALA A CB  1 
ATOM   403  N  N   . GLY A 1 56  ? -29.979 6.902   -0.809  1.00 45.63  ? 56  GLY A N   1 
ATOM   404  C  CA  . GLY A 1 56  ? -28.604 7.320   -0.612  1.00 48.51  ? 56  GLY A CA  1 
ATOM   405  C  C   . GLY A 1 56  ? -27.721 7.013   -1.805  1.00 51.50  ? 56  GLY A C   1 
ATOM   406  O  O   . GLY A 1 56  ? -28.195 6.934   -2.937  1.00 54.88  ? 56  GLY A O   1 
ATOM   407  N  N   . CYS A 1 57  ? -26.430 6.828   -1.543  1.00 49.57  ? 57  CYS A N   1 
ATOM   408  C  CA  . CYS A 1 57  ? -25.453 6.561   -2.598  1.00 39.88  ? 57  CYS A CA  1 
ATOM   409  C  C   . CYS A 1 57  ? -25.682 5.197   -3.247  1.00 37.45  ? 57  CYS A C   1 
ATOM   410  O  O   . CYS A 1 57  ? -25.243 4.950   -4.364  1.00 38.40  ? 57  CYS A O   1 
ATOM   411  C  CB  . CYS A 1 57  ? -24.017 6.705   -2.060  1.00 33.12  ? 57  CYS A CB  1 
ATOM   412  S  SG  . CYS A 1 57  ? -23.506 8.435   -1.660  1.00 36.58  ? 57  CYS A SG  1 
ATOM   413  N  N   . THR A 1 58  ? -26.407 4.324   -2.564  1.00 40.33  ? 58  THR A N   1 
ATOM   414  C  CA  . THR A 1 58  ? -26.713 2.995   -3.106  1.00 39.31  ? 58  THR A CA  1 
ATOM   415  C  C   . THR A 1 58  ? -27.538 3.049   -4.402  1.00 37.54  ? 58  THR A C   1 
ATOM   416  O  O   . THR A 1 58  ? -27.411 2.191   -5.287  1.00 34.96  ? 58  THR A O   1 
ATOM   417  C  CB  . THR A 1 58  ? -27.432 2.136   -2.046  1.00 36.52  ? 58  THR A CB  1 
ATOM   418  O  OG1 . THR A 1 58  ? -26.546 1.920   -0.953  0.80 34.97  ? 58  THR A OG1 1 
ATOM   419  C  CG2 . THR A 1 58  ? -27.838 0.782   -2.605  1.00 39.54  ? 58  THR A CG2 1 
ATOM   420  N  N   . SER A 1 59  ? -28.360 4.082   -4.509  1.00 37.70  ? 59  SER A N   1 
ATOM   421  C  CA  . SER A 1 59  ? -29.336 4.188   -5.582  1.00 40.16  ? 59  SER A CA  1 
ATOM   422  C  C   . SER A 1 59  ? -28.726 4.640   -6.894  1.00 45.12  ? 59  SER A C   1 
ATOM   423  O  O   . SER A 1 59  ? -29.394 4.619   -7.934  1.00 49.62  ? 59  SER A O   1 
ATOM   424  C  CB  . SER A 1 59  ? -30.445 5.136   -5.164  1.00 40.32  ? 59  SER A CB  1 
ATOM   425  O  OG  . SER A 1 59  ? -30.983 4.716   -3.922  1.00 41.86  ? 59  SER A OG  1 
ATOM   426  N  N   . ALA A 1 60  ? -27.452 5.033   -6.843  1.00 41.22  ? 60  ALA A N   1 
ATOM   427  C  CA  . ALA A 1 60  ? -26.747 5.530   -8.020  1.00 39.10  ? 60  ALA A CA  1 
ATOM   428  C  C   . ALA A 1 60  ? -26.526 4.386   -8.987  1.00 35.93  ? 60  ALA A C   1 
ATOM   429  O  O   . ALA A 1 60  ? -26.345 4.582   -10.194 1.00 37.44  ? 60  ALA A O   1 
ATOM   430  C  CB  . ALA A 1 60  ? -25.422 6.164   -7.612  1.00 39.15  ? 60  ALA A CB  1 
ATOM   431  N  N   . GLY A 1 61  ? -26.546 3.181   -8.430  1.00 33.89  ? 61  GLY A N   1 
ATOM   432  C  CA  . GLY A 1 61  ? -26.359 1.973   -9.199  1.00 33.08  ? 61  GLY A CA  1 
ATOM   433  C  C   . GLY A 1 61  ? -24.895 1.688   -9.496  1.00 33.48  ? 61  GLY A C   1 
ATOM   434  O  O   . GLY A 1 61  ? -23.986 2.175   -8.807  1.00 22.62  ? 61  GLY A O   1 
ATOM   435  N  N   . PRO A 1 62  ? -24.670 0.859   -10.518 1.00 35.35  ? 62  PRO A N   1 
ATOM   436  C  CA  . PRO A 1 62  ? -23.350 0.487   -11.025 1.00 31.11  ? 62  PRO A CA  1 
ATOM   437  C  C   . PRO A 1 62  ? -22.646 1.701   -11.624 1.00 25.64  ? 62  PRO A C   1 
ATOM   438  O  O   . PRO A 1 62  ? -23.237 2.766   -11.654 1.00 24.61  ? 62  PRO A O   1 
ATOM   439  C  CB  . PRO A 1 62  ? -23.664 -0.558  -12.108 1.00 29.87  ? 62  PRO A CB  1 
ATOM   440  C  CG  . PRO A 1 62  ? -25.124 -0.359  -12.434 1.00 35.11  ? 62  PRO A CG  1 
ATOM   441  C  CD  . PRO A 1 62  ? -25.750 0.090   -11.163 1.00 35.44  ? 62  PRO A CD  1 
ATOM   442  N  N   . HIS A 1 63  ? -21.394 1.539   -12.029 1.00 21.23  ? 63  HIS A N   1 
ATOM   443  C  CA  . HIS A 1 63  ? -20.660 2.576   -12.735 1.00 29.12  ? 63  HIS A CA  1 
ATOM   444  C  C   . HIS A 1 63  ? -21.321 2.832   -14.093 1.00 29.00  ? 63  HIS A C   1 
ATOM   445  O  O   . HIS A 1 63  ? -21.797 1.903   -14.765 1.00 23.15  ? 63  HIS A O   1 
ATOM   446  C  CB  . HIS A 1 63  ? -19.186 2.156   -12.940 1.00 29.39  ? 63  HIS A CB  1 
ATOM   447  C  CG  . HIS A 1 63  ? -18.445 1.877   -11.662 1.00 33.37  ? 63  HIS A CG  1 
ATOM   448  N  ND1 . HIS A 1 63  ? -17.173 1.350   -11.639 1.00 35.40  ? 63  HIS A ND1 1 
ATOM   449  C  CD2 . HIS A 1 63  ? -18.790 2.069   -10.369 1.00 33.35  ? 63  HIS A CD2 1 
ATOM   450  C  CE1 . HIS A 1 63  ? -16.761 1.227   -10.391 1.00 27.14  ? 63  HIS A CE1 1 
ATOM   451  N  NE2 . HIS A 1 63  ? -17.725 1.658   -9.599  1.00 33.96  ? 63  HIS A NE2 1 
ATOM   452  N  N   . PHE A 1 64  ? -21.367 4.101   -14.477 1.00 34.17  ? 64  PHE A N   1 
ATOM   453  C  CA  . PHE A 1 64  ? -21.865 4.476   -15.798 1.00 37.74  ? 64  PHE A CA  1 
ATOM   454  C  C   . PHE A 1 64  ? -21.156 3.638   -16.855 1.00 36.66  ? 64  PHE A C   1 
ATOM   455  O  O   . PHE A 1 64  ? -19.951 3.782   -17.065 1.00 38.35  ? 64  PHE A O   1 
ATOM   456  C  CB  . PHE A 1 64  ? -21.667 5.973   -16.052 1.00 35.82  ? 64  PHE A CB  1 
ATOM   457  C  CG  . PHE A 1 64  ? -22.328 6.476   -17.316 1.00 34.66  ? 64  PHE A CG  1 
ATOM   458  C  CD1 . PHE A 1 64  ? -23.568 6.011   -17.702 1.00 35.14  ? 64  PHE A CD1 1 
ATOM   459  C  CD2 . PHE A 1 64  ? -21.707 7.442   -18.103 1.00 36.11  ? 64  PHE A CD2 1 
ATOM   460  C  CE1 . PHE A 1 64  ? -24.181 6.485   -18.866 1.00 36.52  ? 64  PHE A CE1 1 
ATOM   461  C  CE2 . PHE A 1 64  ? -22.307 7.926   -19.267 1.00 41.01  ? 64  PHE A CE2 1 
ATOM   462  C  CZ  . PHE A 1 64  ? -23.558 7.447   -19.645 1.00 38.82  ? 64  PHE A CZ  1 
ATOM   463  N  N   . ASN A 1 65  ? -21.907 2.759   -17.512 1.00 38.39  ? 65  ASN A N   1 
ATOM   464  C  CA  . ASN A 1 65  ? -21.318 1.785   -18.426 1.00 44.04  ? 65  ASN A CA  1 
ATOM   465  C  C   . ASN A 1 65  ? -21.993 1.673   -19.814 1.00 48.44  ? 65  ASN A C   1 
ATOM   466  O  O   . ASN A 1 65  ? -22.377 0.590   -20.244 1.00 48.46  ? 65  ASN A O   1 
ATOM   467  C  CB  . ASN A 1 65  ? -21.280 0.418   -17.747 1.00 37.70  ? 65  ASN A CB  1 
ATOM   468  C  CG  . ASN A 1 65  ? -20.367 -0.544  -18.457 1.00 36.34  ? 65  ASN A CG  1 
ATOM   469  O  OD1 . ASN A 1 65  ? -19.568 -0.136  -19.304 1.00 41.31  ? 65  ASN A OD1 1 
ATOM   470  N  ND2 . ASN A 1 65  ? -20.475 -1.825  -18.127 1.00 29.50  ? 65  ASN A ND2 1 
ATOM   471  N  N   . PRO A 1 66  ? -22.091 2.790   -20.537 1.00 53.40  ? 66  PRO A N   1 
ATOM   472  C  CA  . PRO A 1 66  ? -22.871 2.900   -21.783 1.00 55.89  ? 66  PRO A CA  1 
ATOM   473  C  C   . PRO A 1 66  ? -22.445 1.911   -22.849 1.00 53.04  ? 66  PRO A C   1 
ATOM   474  O  O   . PRO A 1 66  ? -23.209 1.624   -23.760 1.00 56.82  ? 66  PRO A O   1 
ATOM   475  C  CB  . PRO A 1 66  ? -22.559 4.319   -22.275 1.00 58.54  ? 66  PRO A CB  1 
ATOM   476  C  CG  . PRO A 1 66  ? -22.078 5.041   -21.070 1.00 58.99  ? 66  PRO A CG  1 
ATOM   477  C  CD  . PRO A 1 66  ? -21.353 4.025   -20.241 1.00 55.05  ? 66  PRO A CD  1 
ATOM   478  N  N   . LEU A 1 67  ? -21.226 1.408   -22.740 1.00 49.91  ? 67  LEU A N   1 
ATOM   479  C  CA  . LEU A 1 67  ? -20.681 0.477   -23.717 1.00 46.37  ? 67  LEU A CA  1 
ATOM   480  C  C   . LEU A 1 67  ? -20.694 -0.945  -23.181 1.00 47.25  ? 67  LEU A C   1 
ATOM   481  O  O   . LEU A 1 67  ? -20.276 -1.881  -23.868 1.00 30.29  ? 67  LEU A O   1 
ATOM   482  C  CB  . LEU A 1 67  ? -19.261 0.900   -24.089 1.00 40.86  ? 67  LEU A CB  1 
ATOM   483  C  CG  . LEU A 1 67  ? -19.299 2.306   -24.669 1.00 43.52  ? 67  LEU A CG  1 
ATOM   484  C  CD1 . LEU A 1 67  ? -17.924 2.786   -25.084 1.00 46.68  ? 67  LEU A CD1 1 
ATOM   485  C  CD2 . LEU A 1 67  ? -20.274 2.317   -25.854 1.00 45.24  ? 67  LEU A CD2 1 
ATOM   486  N  N   . SER A 1 68  ? -21.172 -1.085  -21.942 1.00 47.53  ? 68  SER A N   1 
ATOM   487  C  CA  . SER A 1 68  ? -21.216 -2.365  -21.249 1.00 43.94  ? 68  SER A CA  1 
ATOM   488  C  C   . SER A 1 68  ? -19.938 -3.167  -21.510 1.00 46.30  ? 68  SER A C   1 
ATOM   489  O  O   . SER A 1 68  ? -19.932 -4.163  -22.233 1.00 46.06  ? 68  SER A O   1 
ATOM   490  C  CB  . SER A 1 68  ? -22.474 -3.151  -21.640 1.00 45.99  ? 68  SER A CB  1 
ATOM   491  O  OG  . SER A 1 68  ? -22.942 -2.768  -22.927 1.00 45.31  ? 68  SER A OG  1 
ATOM   492  N  N   . ARG A 1 69  ? -18.847 -2.680  -20.936 1.00 49.93  ? 69  ARG A N   1 
ATOM   493  C  CA  . ARG A 1 69  ? -17.566 -3.363  -20.938 1.00 50.67  ? 69  ARG A CA  1 
ATOM   494  C  C   . ARG A 1 69  ? -17.228 -3.642  -19.479 1.00 48.64  ? 69  ARG A C   1 
ATOM   495  O  O   . ARG A 1 69  ? -18.053 -3.404  -18.586 1.00 42.27  ? 69  ARG A O   1 
ATOM   496  C  CB  . ARG A 1 69  ? -16.483 -2.472  -21.556 1.00 55.49  ? 69  ARG A CB  1 
ATOM   497  C  CG  . ARG A 1 69  ? -16.557 -2.308  -23.075 1.00 59.44  ? 69  ARG A CG  1 
ATOM   498  C  CD  . ARG A 1 69  ? -15.552 -1.262  -23.575 1.00 61.62  ? 69  ARG A CD  1 
ATOM   499  N  NE  . ARG A 1 69  ? -15.623 -1.076  -25.022 1.00 68.28  ? 69  ARG A NE  1 
ATOM   500  C  CZ  . ARG A 1 69  ? -14.966 -0.136  -25.697 1.00 72.94  ? 69  ARG A CZ  1 
ATOM   501  N  NH1 . ARG A 1 69  ? -14.182 0.727   -25.059 1.00 72.81  ? 69  ARG A NH1 1 
ATOM   502  N  NH2 . ARG A 1 69  ? -15.094 -0.054  -27.015 1.00 75.46  ? 69  ARG A NH2 1 
ATOM   503  N  N   . LYS A 1 70  ? -16.012 -4.129  -19.242 1.00 50.19  ? 70  LYS A N   1 
ATOM   504  C  CA  . LYS A 1 70  ? -15.559 -4.487  -17.901 1.00 44.24  ? 70  LYS A CA  1 
ATOM   505  C  C   . LYS A 1 70  ? -14.856 -3.317  -17.214 1.00 39.90  ? 70  LYS A C   1 
ATOM   506  O  O   . LYS A 1 70  ? -14.387 -2.388  -17.886 1.00 38.23  ? 70  LYS A O   1 
ATOM   507  C  CB  . LYS A 1 70  ? -14.630 -5.690  -17.964 1.00 44.86  ? 70  LYS A CB  1 
ATOM   508  C  CG  . LYS A 1 70  ? -15.354 -6.984  -18.257 1.00 46.71  ? 70  LYS A CG  1 
ATOM   509  C  CD  . LYS A 1 70  ? -14.744 -8.139  -17.484 1.00 48.36  ? 70  LYS A CD  1 
ATOM   510  C  CE  . LYS A 1 70  ? -15.746 -9.285  -17.345 1.00 54.07  ? 70  LYS A CE  1 
ATOM   511  N  NZ  . LYS A 1 70  ? -16.960 -8.904  -16.565 1.00 56.54  ? 70  LYS A NZ  1 
ATOM   512  N  N   . HIS A 1 71  ? -14.796 -3.366  -15.881 1.00 29.97  ? 71  HIS A N   1 
ATOM   513  C  CA  . HIS A 1 71  ? -14.198 -2.294  -15.101 1.00 20.88  ? 71  HIS A CA  1 
ATOM   514  C  C   . HIS A 1 71  ? -12.713 -2.203  -15.372 1.00 19.68  ? 71  HIS A C   1 
ATOM   515  O  O   . HIS A 1 71  ? -12.036 -3.217  -15.502 1.00 20.49  ? 71  HIS A O   1 
ATOM   516  C  CB  . HIS A 1 71  ? -14.407 -2.489  -13.586 1.00 28.06  ? 71  HIS A CB  1 
ATOM   517  C  CG  . HIS A 1 71  ? -13.705 -1.449  -12.764 1.00 25.82  ? 71  HIS A CG  1 
ATOM   518  N  ND1 . HIS A 1 71  ? -14.226 -0.190  -12.558 1.00 19.79  ? 71  HIS A ND1 1 
ATOM   519  C  CD2 . HIS A 1 71  ? -12.478 -1.449  -12.191 1.00 22.03  ? 71  HIS A CD2 1 
ATOM   520  C  CE1 . HIS A 1 71  ? -13.374 0.525   -11.847 1.00 17.87  ? 71  HIS A CE1 1 
ATOM   521  N  NE2 . HIS A 1 71  ? -12.304 -0.210  -11.619 1.00 21.33  ? 71  HIS A NE2 1 
ATOM   522  N  N   . GLY A 1 72  ? -12.194 -0.986  -15.449 1.00 13.99  ? 72  GLY A N   1 
ATOM   523  C  CA  . GLY A 1 72  ? -10.773 -0.806  -15.667 1.00 13.61  ? 72  GLY A CA  1 
ATOM   524  C  C   . GLY A 1 72  ? -10.333 0.556   -15.185 1.00 12.80  ? 72  GLY A C   1 
ATOM   525  O  O   . GLY A 1 72  ? -11.130 1.329   -14.677 1.00 20.75  ? 72  GLY A O   1 
ATOM   526  N  N   . GLY A 1 73  ? -9.062  0.873   -15.346 1.00 17.69  ? 73  GLY A N   1 
ATOM   527  C  CA  . GLY A 1 73  ? -8.612  2.212   -15.009 1.00 20.22  ? 73  GLY A CA  1 
ATOM   528  C  C   . GLY A 1 73  ? -8.816  3.151   -16.179 1.00 28.20  ? 73  GLY A C   1 
ATOM   529  O  O   . GLY A 1 73  ? -9.063  2.706   -17.312 1.00 32.79  ? 73  GLY A O   1 
ATOM   530  N  N   . PRO A 1 74  ? -8.682  4.456   -15.926 1.00 23.81  ? 74  PRO A N   1 
ATOM   531  C  CA  . PRO A 1 74  ? -8.952  5.497   -16.927 1.00 24.41  ? 74  PRO A CA  1 
ATOM   532  C  C   . PRO A 1 74  ? -8.145  5.357   -18.205 1.00 28.11  ? 74  PRO A C   1 
ATOM   533  O  O   . PRO A 1 74  ? -8.627  5.787   -19.227 1.00 29.26  ? 74  PRO A O   1 
ATOM   534  C  CB  . PRO A 1 74  ? -8.593  6.797   -16.199 1.00 27.51  ? 74  PRO A CB  1 
ATOM   535  C  CG  . PRO A 1 74  ? -7.689  6.377   -15.083 1.00 25.54  ? 74  PRO A CG  1 
ATOM   536  C  CD  . PRO A 1 74  ? -8.177  5.013   -14.663 1.00 22.19  ? 74  PRO A CD  1 
ATOM   537  N  N   . LYS A 1 75  ? -6.961  4.750   -18.157 1.00 35.99  ? 75  LYS A N   1 
ATOM   538  C  CA  . LYS A 1 75  ? -6.111  4.619   -19.350 1.00 39.70  ? 75  LYS A CA  1 
ATOM   539  C  C   . LYS A 1 75  ? -6.331  3.333   -20.165 1.00 40.14  ? 75  LYS A C   1 
ATOM   540  O  O   . LYS A 1 75  ? -5.835  3.212   -21.280 1.00 48.05  ? 75  LYS A O   1 
ATOM   541  C  CB  . LYS A 1 75  ? -4.625  4.751   -18.978 1.00 39.56  ? 75  LYS A CB  1 
ATOM   542  C  CG  . LYS A 1 75  ? -4.241  6.111   -18.372 1.00 42.58  ? 75  LYS A CG  1 
ATOM   543  C  CD  . LYS A 1 75  ? -4.046  7.205   -19.437 1.00 46.10  ? 75  LYS A CD  1 
ATOM   544  C  CE  . LYS A 1 75  ? -4.321  8.616   -18.899 1.00 45.48  ? 75  LYS A CE  1 
ATOM   545  N  NZ  . LYS A 1 75  ? -5.785  8.964   -18.913 1.00 43.51  ? 75  LYS A NZ  1 
ATOM   546  N  N   . ASP A 1 76  ? -7.059  2.373   -19.612 1.00 38.69  ? 76  ASP A N   1 
ATOM   547  C  CA  . ASP A 1 76  ? -7.264  1.099   -20.282 1.00 38.41  ? 76  ASP A CA  1 
ATOM   548  C  C   . ASP A 1 76  ? -8.438  1.194   -21.241 1.00 40.54  ? 76  ASP A C   1 
ATOM   549  O  O   . ASP A 1 76  ? -9.464  1.753   -20.864 1.00 42.12  ? 76  ASP A O   1 
ATOM   550  C  CB  . ASP A 1 76  ? -7.547  0.011   -19.250 1.00 40.11  ? 76  ASP A CB  1 
ATOM   551  C  CG  . ASP A 1 76  ? -6.501  -0.048  -18.165 1.00 47.12  ? 76  ASP A CG  1 
ATOM   552  O  OD1 . ASP A 1 76  ? -5.306  0.040   -18.502 1.00 51.34  ? 76  ASP A OD1 1 
ATOM   553  O  OD2 . ASP A 1 76  ? -6.868  -0.180  -16.972 1.00 50.11  ? 76  ASP A OD2 1 
ATOM   554  N  N   . GLU A 1 77  ? -8.291  0.653   -22.462 1.00 39.85  ? 77  GLU A N   1 
ATOM   555  C  CA  . GLU A 1 77  ? -9.386  0.614   -23.440 1.00 40.92  ? 77  GLU A CA  1 
ATOM   556  C  C   . GLU A 1 77  ? -10.622 -0.095  -22.887 1.00 41.93  ? 77  GLU A C   1 
ATOM   557  O  O   . GLU A 1 77  ? -11.742 0.425   -22.944 1.00 43.67  ? 77  GLU A O   1 
ATOM   558  C  CB  . GLU A 1 77  ? -8.959  -0.059  -24.753 1.00 44.80  ? 77  GLU A CB  1 
ATOM   559  C  CG  . GLU A 1 77  ? -10.091 -0.182  -25.795 1.00 45.38  ? 77  GLU A CG  1 
ATOM   560  C  CD  . GLU A 1 77  ? -9.577  -0.492  -27.203 1.00 48.11  ? 77  GLU A CD  1 
ATOM   561  O  OE1 . GLU A 1 77  ? -8.363  -0.774  -27.334 1.00 49.15  ? 77  GLU A OE1 1 
ATOM   562  O  OE2 . GLU A 1 77  ? -10.381 -0.452  -28.174 1.00 42.72  ? 77  GLU A OE2 1 
ATOM   563  N  N   . GLU A 1 78  ? -10.414 -1.293  -22.363 1.00 41.98  ? 78  GLU A N   1 
ATOM   564  C  CA  . GLU A 1 78  ? -11.443 -1.962  -21.582 1.00 39.81  ? 78  GLU A CA  1 
ATOM   565  C  C   . GLU A 1 78  ? -11.651 -1.234  -20.222 1.00 39.08  ? 78  GLU A C   1 
ATOM   566  O  O   . GLU A 1 78  ? -11.081 -1.591  -19.189 1.00 36.83  ? 78  GLU A O   1 
ATOM   567  C  CB  . GLU A 1 78  ? -11.088 -3.445  -21.407 1.00 39.15  ? 78  GLU A CB  1 
ATOM   568  C  CG  . GLU A 1 78  ? -12.208 -4.302  -20.844 1.00 41.33  ? 78  GLU A CG  1 
ATOM   569  C  CD  . GLU A 1 78  ? -13.358 -4.478  -21.810 1.00 44.08  ? 78  GLU A CD  1 
ATOM   570  O  OE1 . GLU A 1 78  ? -13.126 -4.381  -23.037 1.00 51.49  ? 78  GLU A OE1 1 
ATOM   571  O  OE2 . GLU A 1 78  ? -14.494 -4.714  -21.345 1.00 38.66  ? 78  GLU A OE2 1 
ATOM   572  N  N   . ARG A 1 79  ? -12.465 -0.189  -20.251 1.00 40.40  ? 79  ARG A N   1 
ATOM   573  C  CA  . ARG A 1 79  ? -12.891 0.490   -19.042 1.00 41.74  ? 79  ARG A CA  1 
ATOM   574  C  C   . ARG A 1 79  ? -14.385 0.788   -19.088 1.00 46.94  ? 79  ARG A C   1 
ATOM   575  O  O   . ARG A 1 79  ? -15.046 0.635   -20.113 1.00 53.30  ? 79  ARG A O   1 
ATOM   576  C  CB  . ARG A 1 79  ? -12.134 1.806   -18.881 1.00 42.06  ? 79  ARG A CB  1 
ATOM   577  C  CG  . ARG A 1 79  ? -12.148 2.699   -20.134 1.00 36.62  ? 79  ARG A CG  1 
ATOM   578  C  CD  . ARG A 1 79  ? -11.623 4.110   -19.848 1.00 35.16  ? 79  ARG A CD  1 
ATOM   579  N  NE  . ARG A 1 79  ? -12.639 4.963   -19.224 1.00 37.21  ? 79  ARG A NE  1 
ATOM   580  C  CZ  . ARG A 1 79  ? -12.468 6.243   -18.898 1.00 37.40  ? 79  ARG A CZ  1 
ATOM   581  N  NH1 . ARG A 1 79  ? -11.311 6.853   -19.125 1.00 19.46  ? 79  ARG A NH1 1 
ATOM   582  N  NH2 . ARG A 1 79  ? -13.463 6.912   -18.344 1.00 18.06  ? 79  ARG A NH2 1 
ATOM   583  N  N   . HIS A 1 80  ? -14.905 1.202   -17.948 1.00 48.39  ? 80  HIS A N   1 
ATOM   584  C  CA  . HIS A 1 80  ? -16.243 1.742   -17.844 1.00 45.29  ? 80  HIS A CA  1 
ATOM   585  C  C   . HIS A 1 80  ? -16.133 3.227   -18.237 1.00 48.25  ? 80  HIS A C   1 
ATOM   586  O  O   . HIS A 1 80  ? -15.050 3.825   -18.144 1.00 48.17  ? 80  HIS A O   1 
ATOM   587  C  CB  . HIS A 1 80  ? -16.741 1.590   -16.389 1.00 30.99  ? 80  HIS A CB  1 
ATOM   588  C  CG  . HIS A 1 80  ? -17.093 0.181   -16.002 1.00 34.21  ? 80  HIS A CG  1 
ATOM   589  N  ND1 . HIS A 1 80  ? -17.044 -0.271  -14.697 1.00 39.62  ? 80  HIS A ND1 1 
ATOM   590  C  CD2 . HIS A 1 80  ? -17.516 -0.871  -16.743 1.00 36.01  ? 80  HIS A CD2 1 
ATOM   591  C  CE1 . HIS A 1 80  ? -17.412 -1.538  -14.652 1.00 38.76  ? 80  HIS A CE1 1 
ATOM   592  N  NE2 . HIS A 1 80  ? -17.702 -1.927  -15.881 1.00 40.33  ? 80  HIS A NE2 1 
ATOM   593  N  N   . VAL A 1 81  ? -17.227 3.830   -18.687 1.00 44.04  ? 81  VAL A N   1 
ATOM   594  C  CA  . VAL A 1 81  ? -17.177 5.256   -18.969 1.00 41.00  ? 81  VAL A CA  1 
ATOM   595  C  C   . VAL A 1 81  ? -17.026 6.014   -17.659 1.00 39.04  ? 81  VAL A C   1 
ATOM   596  O  O   . VAL A 1 81  ? -16.292 6.987   -17.581 1.00 39.11  ? 81  VAL A O   1 
ATOM   597  C  CB  . VAL A 1 81  ? -18.404 5.763   -19.780 1.00 42.56  ? 81  VAL A CB  1 
ATOM   598  C  CG1 . VAL A 1 81  ? -18.616 7.249   -19.559 1.00 43.18  ? 81  VAL A CG1 1 
ATOM   599  C  CG2 . VAL A 1 81  ? -18.224 5.470   -21.274 1.00 39.27  ? 81  VAL A CG2 1 
ATOM   600  N  N   . GLY A 1 82  ? -17.701 5.558   -16.614 1.00 36.50  ? 82  GLY A N   1 
ATOM   601  C  CA  . GLY A 1 82  ? -17.581 6.220   -15.331 1.00 31.27  ? 82  GLY A CA  1 
ATOM   602  C  C   . GLY A 1 82  ? -16.215 6.103   -14.687 1.00 28.71  ? 82  GLY A C   1 
ATOM   603  O  O   . GLY A 1 82  ? -15.949 6.756   -13.678 1.00 32.86  ? 82  GLY A O   1 
ATOM   604  N  N   . ASP A 1 83  ? -15.347 5.279   -15.269 1.00 27.92  ? 83  ASP A N   1 
ATOM   605  C  CA  . ASP A 1 83  ? -14.073 4.919   -14.639 1.00 25.20  ? 83  ASP A CA  1 
ATOM   606  C  C   . ASP A 1 83  ? -13.020 6.012   -14.637 1.00 21.89  ? 83  ASP A C   1 
ATOM   607  O  O   . ASP A 1 83  ? -12.211 6.103   -15.562 1.00 23.12  ? 83  ASP A O   1 
ATOM   608  C  CB  . ASP A 1 83  ? -13.481 3.646   -15.260 1.00 30.60  ? 83  ASP A CB  1 
ATOM   609  C  CG  . ASP A 1 83  ? -14.145 2.392   -14.759 1.00 36.83  ? 83  ASP A CG  1 
ATOM   610  O  OD1 . ASP A 1 83  ? -13.982 1.326   -15.396 1.00 34.92  ? 83  ASP A OD1 1 
ATOM   611  O  OD2 . ASP A 1 83  ? -14.846 2.479   -13.725 1.00 40.77  ? 83  ASP A OD2 1 
ATOM   612  N  N   . LEU A 1 84  ? -13.018 6.825   -13.581 1.00 16.58  ? 84  LEU A N   1 
ATOM   613  C  CA  . LEU A 1 84  ? -12.019 7.872   -13.459 1.00 16.40  ? 84  LEU A CA  1 
ATOM   614  C  C   . LEU A 1 84  ? -10.881 7.435   -12.546 1.00 24.97  ? 84  LEU A C   1 
ATOM   615  O  O   . LEU A 1 84  ? -10.046 8.254   -12.155 1.00 27.08  ? 84  LEU A O   1 
ATOM   616  C  CB  . LEU A 1 84  ? -12.643 9.182   -12.989 1.00 12.37  ? 84  LEU A CB  1 
ATOM   617  C  CG  . LEU A 1 84  ? -13.838 9.634   -13.812 1.00 22.51  ? 84  LEU A CG  1 
ATOM   618  C  CD1 . LEU A 1 84  ? -14.561 10.795  -13.152 1.00 14.31  ? 84  LEU A CD1 1 
ATOM   619  C  CD2 . LEU A 1 84  ? -13.389 9.979   -15.281 1.00 40.86  ? 84  LEU A CD2 1 
ATOM   620  N  N   . GLY A 1 85  ? -10.831 6.140   -12.224 1.00 24.11  ? 85  GLY A N   1 
ATOM   621  C  CA  . GLY A 1 85  ? -9.759  5.615   -11.394 1.00 29.80  ? 85  GLY A CA  1 
ATOM   622  C  C   . GLY A 1 85  ? -9.755  6.132   -9.953  1.00 29.65  ? 85  GLY A C   1 
ATOM   623  O  O   . GLY A 1 85  ? -10.726 5.932   -9.232  1.00 27.41  ? 85  GLY A O   1 
ATOM   624  N  N   . ASN A 1 86  ? -8.665  6.791   -9.543  1.00 28.09  ? 86  ASN A N   1 
ATOM   625  C  CA  . ASN A 1 86  ? -8.489  7.269   -8.171  1.00 28.13  ? 86  ASN A CA  1 
ATOM   626  C  C   . ASN A 1 86  ? -8.224  8.764   -8.023  1.00 30.14  ? 86  ASN A C   1 
ATOM   627  O  O   . ASN A 1 86  ? -7.787  9.444   -8.945  1.00 31.71  ? 86  ASN A O   1 
ATOM   628  C  CB  . ASN A 1 86  ? -7.339  6.537   -7.485  1.00 29.91  ? 86  ASN A CB  1 
ATOM   629  C  CG  . ASN A 1 86  ? -7.621  5.060   -7.273  1.00 33.78  ? 86  ASN A CG  1 
ATOM   630  O  OD1 . ASN A 1 86  ? -8.440  4.686   -6.434  1.00 39.28  ? 86  ASN A OD1 1 
ATOM   631  N  ND2 . ASN A 1 86  ? -6.918  4.211   -8.013  1.00 26.78  ? 86  ASN A ND2 1 
ATOM   632  N  N   . VAL A 1 87  ? -8.494  9.258   -6.828  1.00 26.87  ? 87  VAL A N   1 
ATOM   633  C  CA  . VAL A 1 87  ? -8.054  10.571  -6.425  1.00 29.84  ? 87  VAL A CA  1 
ATOM   634  C  C   . VAL A 1 87  ? -7.223  10.319  -5.168  1.00 34.39  ? 87  VAL A C   1 
ATOM   635  O  O   . VAL A 1 87  ? -7.225  9.212   -4.619  1.00 33.46  ? 87  VAL A O   1 
ATOM   636  C  CB  . VAL A 1 87  ? -9.240  11.542  -6.093  1.00 27.92  ? 87  VAL A CB  1 
ATOM   637  C  CG1 . VAL A 1 87  ? -10.193 11.705  -7.293  1.00 21.76  ? 87  VAL A CG1 1 
ATOM   638  C  CG2 . VAL A 1 87  ? -9.990  11.091  -4.813  1.00 18.60  ? 87  VAL A CG2 1 
ATOM   639  N  N   . THR A 1 88  ? -6.517  11.337  -4.703  1.00 31.12  ? 88  THR A N   1 
ATOM   640  C  CA  . THR A 1 88  ? -5.568  11.124  -3.642  1.00 25.28  ? 88  THR A CA  1 
ATOM   641  C  C   . THR A 1 88  ? -5.707  12.112  -2.493  1.00 24.27  ? 88  THR A C   1 
ATOM   642  O  O   . THR A 1 88  ? -5.623  13.314  -2.704  1.00 21.02  ? 88  THR A O   1 
ATOM   643  C  CB  . THR A 1 88  ? -4.140  11.147  -4.177  1.00 25.18  ? 88  THR A CB  1 
ATOM   644  O  OG1 . THR A 1 88  ? -3.911  9.955   -4.934  1.00 30.63  ? 88  THR A OG1 1 
ATOM   645  C  CG2 . THR A 1 88  ? -3.141  11.200  -3.013  1.00 25.23  ? 88  THR A CG2 1 
ATOM   646  N  N   . ALA A 1 89  ? -5.918  11.593  -1.282  1.00 23.39  ? 89  ALA A N   1 
ATOM   647  C  CA  . ALA A 1 89  ? -6.037  12.457  -0.104  1.00 24.90  ? 89  ALA A CA  1 
ATOM   648  C  C   . ALA A 1 89  ? -4.701  12.620  0.601   1.00 24.77  ? 89  ALA A C   1 
ATOM   649  O  O   . ALA A 1 89  ? -4.013  11.632  0.880   1.00 23.24  ? 89  ALA A O   1 
ATOM   650  C  CB  . ALA A 1 89  ? -7.067  11.921  0.855   1.00 25.53  ? 89  ALA A CB  1 
ATOM   651  N  N   . ASP A 1 90  ? -4.323  13.858  0.880   1.00 18.59  ? 90  ASP A N   1 
ATOM   652  C  CA  . ASP A 1 90  ? -3.169  14.068  1.732   1.00 29.12  ? 90  ASP A CA  1 
ATOM   653  C  C   . ASP A 1 90  ? -3.531  13.712  3.166   1.00 35.18  ? 90  ASP A C   1 
ATOM   654  O  O   . ASP A 1 90  ? -4.599  13.155  3.447   1.00 29.99  ? 90  ASP A O   1 
ATOM   655  C  CB  . ASP A 1 90  ? -2.639  15.514  1.663   1.00 30.94  ? 90  ASP A CB  1 
ATOM   656  C  CG  . ASP A 1 90  ? -3.661  16.561  2.127   1.00 35.87  ? 90  ASP A CG  1 
ATOM   657  O  OD1 . ASP A 1 90  ? -4.617  16.227  2.864   1.00 38.17  ? 90  ASP A OD1 1 
ATOM   658  O  OD2 . ASP A 1 90  ? -3.498  17.747  1.759   1.00 36.48  ? 90  ASP A OD2 1 
ATOM   659  N  N   . LYS A 1 91  ? -2.628  14.012  4.083   1.00 47.29  ? 91  LYS A N   1 
ATOM   660  C  CA  . LYS A 1 91  ? -3.043  14.022  5.468   1.00 52.63  ? 91  LYS A CA  1 
ATOM   661  C  C   . LYS A 1 91  ? -3.780  15.336  5.691   1.00 54.63  ? 91  LYS A C   1 
ATOM   662  O  O   . LYS A 1 91  ? -3.564  16.301  4.966   1.00 57.23  ? 91  LYS A O   1 
ATOM   663  C  CB  . LYS A 1 91  ? -1.887  13.806  6.432   1.00 54.85  ? 91  LYS A CB  1 
ATOM   664  C  CG  . LYS A 1 91  ? -2.341  13.052  7.686   1.00 61.93  ? 91  LYS A CG  1 
ATOM   665  C  CD  . LYS A 1 91  ? -3.219  11.821  7.341   1.00 104.40 ? 91  LYS A CD  1 
ATOM   666  C  CE  . LYS A 1 91  ? -4.697  12.178  7.019   1.00 52.44  ? 91  LYS A CE  1 
ATOM   667  N  NZ  . LYS A 1 91  ? -5.591  10.977  6.825   1.00 50.11  ? 91  LYS A NZ  1 
ATOM   668  N  N   . ASP A 1 92  ? -4.652  15.364  6.683   1.00 54.94  ? 92  ASP A N   1 
ATOM   669  C  CA  . ASP A 1 92  ? -5.713  16.363  6.758   1.00 49.01  ? 92  ASP A CA  1 
ATOM   670  C  C   . ASP A 1 92  ? -6.910  15.775  6.000   1.00 38.09  ? 92  ASP A C   1 
ATOM   671  O  O   . ASP A 1 92  ? -7.995  16.350  5.937   1.00 37.47  ? 92  ASP A O   1 
ATOM   672  C  CB  . ASP A 1 92  ? -5.256  17.710  6.190   1.00 51.50  ? 92  ASP A CB  1 
ATOM   673  C  CG  . ASP A 1 92  ? -4.050  18.289  6.945   1.00 57.25  ? 92  ASP A CG  1 
ATOM   674  O  OD1 . ASP A 1 92  ? -3.101  17.532  7.233   1.00 57.77  ? 92  ASP A OD1 1 
ATOM   675  O  OD2 . ASP A 1 92  ? -4.052  19.503  7.256   1.00 60.26  ? 92  ASP A OD2 1 
ATOM   676  N  N   . GLY A 1 93  ? -6.701  14.586  5.460   1.00 33.68  ? 93  GLY A N   1 
ATOM   677  C  CA  . GLY A 1 93  ? -7.725  13.912  4.691   1.00 39.43  ? 93  GLY A CA  1 
ATOM   678  C  C   . GLY A 1 93  ? -8.278  14.734  3.540   1.00 35.76  ? 93  GLY A C   1 
ATOM   679  O  O   . GLY A 1 93  ? -9.450  14.601  3.201   1.00 40.99  ? 93  GLY A O   1 
ATOM   680  N  N   . VAL A 1 94  ? -7.452  15.582  2.939   1.00 22.50  ? 94  VAL A N   1 
ATOM   681  C  CA  . VAL A 1 94  ? -7.953  16.444  1.882   1.00 34.03  ? 94  VAL A CA  1 
ATOM   682  C  C   . VAL A 1 94  ? -7.483  16.003  0.501   1.00 36.77  ? 94  VAL A C   1 
ATOM   683  O  O   . VAL A 1 94  ? -6.301  15.764  0.264   1.00 37.53  ? 94  VAL A O   1 
ATOM   684  C  CB  . VAL A 1 94  ? -7.596  17.924  2.132   1.00 35.49  ? 94  VAL A CB  1 
ATOM   685  C  CG1 . VAL A 1 94  ? -8.117  18.802  0.977   1.00 27.83  ? 94  VAL A CG1 1 
ATOM   686  C  CG2 . VAL A 1 94  ? -8.167  18.382  3.488   1.00 29.96  ? 94  VAL A CG2 1 
ATOM   687  N  N   . ALA A 1 95  ? -8.415  15.874  -0.415  1.00 36.28  ? 95  ALA A N   1 
ATOM   688  C  CA  . ALA A 1 95  ? -8.035  15.471  -1.760  1.00 38.12  ? 95  ALA A CA  1 
ATOM   689  C  C   . ALA A 1 95  ? -8.348  16.555  -2.773  1.00 39.67  ? 95  ALA A C   1 
ATOM   690  O  O   . ALA A 1 95  ? -9.480  16.665  -3.256  1.00 43.54  ? 95  ALA A O   1 
ATOM   691  C  CB  . ALA A 1 95  ? -8.721  14.192  -2.135  1.00 36.90  ? 95  ALA A CB  1 
ATOM   692  N  N   . ASP A 1 96  ? -7.339  17.357  -3.080  1.00 36.76  ? 96  ASP A N   1 
ATOM   693  C  CA  . ASP A 1 96  ? -7.422  18.296  -4.189  1.00 40.22  ? 96  ASP A CA  1 
ATOM   694  C  C   . ASP A 1 96  ? -7.466  17.490  -5.481  1.00 33.81  ? 96  ASP A C   1 
ATOM   695  O  O   . ASP A 1 96  ? -6.457  16.982  -5.928  1.00 34.69  ? 96  ASP A O   1 
ATOM   696  C  CB  . ASP A 1 96  ? -6.214  19.252  -4.178  1.00 47.83  ? 96  ASP A CB  1 
ATOM   697  C  CG  . ASP A 1 96  ? -6.211  20.212  -5.364  1.00 57.85  ? 96  ASP A CG  1 
ATOM   698  O  OD1 . ASP A 1 96  ? -7.308  20.627  -5.807  0.50 58.98  ? 96  ASP A OD1 1 
ATOM   699  O  OD2 . ASP A 1 96  ? -5.110  20.554  -5.855  0.50 58.86  ? 96  ASP A OD2 1 
ATOM   700  N  N   . VAL A 1 97  ? -8.640  17.345  -6.070  1.00 35.50  ? 97  VAL A N   1 
ATOM   701  C  CA  . VAL A 1 97  ? -8.749  16.564  -7.297  1.00 40.21  ? 97  VAL A CA  1 
ATOM   702  C  C   . VAL A 1 97  ? -8.268  17.371  -8.502  1.00 39.25  ? 97  VAL A C   1 
ATOM   703  O  O   . VAL A 1 97  ? -8.549  18.566  -8.594  1.00 38.25  ? 97  VAL A O   1 
ATOM   704  C  CB  . VAL A 1 97  ? -10.211 16.129  -7.577  1.00 27.09  ? 97  VAL A CB  1 
ATOM   705  C  CG1 . VAL A 1 97  ? -10.304 15.402  -8.910  1.00 28.12  ? 97  VAL A CG1 1 
ATOM   706  C  CG2 . VAL A 1 97  ? -10.752 15.293  -6.453  1.00 19.45  ? 97  VAL A CG2 1 
ATOM   707  N  N   . SER A 1 98  ? -7.559  16.716  -9.421  1.00 36.09  ? 98  SER A N   1 
ATOM   708  C  CA  . SER A 1 98  ? -7.272  17.309  -10.727 1.00 37.12  ? 98  SER A CA  1 
ATOM   709  C  C   . SER A 1 98  ? -7.133  16.229  -11.793 1.00 36.54  ? 98  SER A C   1 
ATOM   710  O  O   . SER A 1 98  ? -6.100  15.576  -11.907 1.00 41.31  ? 98  SER A O   1 
ATOM   711  C  CB  . SER A 1 98  ? -6.010  18.182  -10.674 1.00 39.27  ? 98  SER A CB  1 
ATOM   712  O  OG  . SER A 1 98  ? -5.743  18.792  -11.928 1.00 40.52  ? 98  SER A OG  1 
ATOM   713  N  N   . ILE A 1 99  ? -8.176  16.046  -12.583 1.00 36.69  ? 99  ILE A N   1 
ATOM   714  C  CA  . ILE A 1 99  ? -8.196  14.975  -13.572 1.00 39.20  ? 99  ILE A CA  1 
ATOM   715  C  C   . ILE A 1 99  ? -8.515  15.497  -14.952 1.00 33.50  ? 99  ILE A C   1 
ATOM   716  O  O   . ILE A 1 99  ? -9.235  16.496  -15.116 1.00 32.76  ? 99  ILE A O   1 
ATOM   717  C  CB  . ILE A 1 99  ? -9.253  13.909  -13.211 1.00 46.94  ? 99  ILE A CB  1 
ATOM   718  C  CG1 . ILE A 1 99  ? -8.812  13.115  -11.977 1.00 46.64  ? 99  ILE A CG1 1 
ATOM   719  C  CG2 . ILE A 1 99  ? -9.527  12.987  -14.404 1.00 46.65  ? 99  ILE A CG2 1 
ATOM   720  C  CD1 . ILE A 1 99  ? -9.880  12.166  -11.462 1.00 45.49  ? 99  ILE A CD1 1 
ATOM   721  N  N   . GLU A 1 100 ? -7.987  14.828  -15.959 1.00 33.44  ? 100 GLU A N   1 
ATOM   722  C  CA  . GLU A 1 100 ? -8.434  15.123  -17.320 1.00 35.07  ? 100 GLU A CA  1 
ATOM   723  C  C   . GLU A 1 100 ? -8.797  13.842  -18.009 1.00 33.99  ? 100 GLU A C   1 
ATOM   724  O  O   . GLU A 1 100 ? -7.961  12.940  -18.154 1.00 32.00  ? 100 GLU A O   1 
ATOM   725  C  CB  . GLU A 1 100 ? -7.367  15.840  -18.110 1.00 36.72  ? 100 GLU A CB  1 
ATOM   726  C  CG  . GLU A 1 100 ? -7.926  17.001  -18.861 1.00 47.15  ? 100 GLU A CG  1 
ATOM   727  C  CD  . GLU A 1 100 ? -7.328  17.146  -20.244 1.00 50.87  ? 100 GLU A CD  1 
ATOM   728  O  OE1 . GLU A 1 100 ? -7.136  18.310  -20.643 1.00 50.81  ? 100 GLU A OE1 1 
ATOM   729  O  OE2 . GLU A 1 100 ? -7.071  16.113  -20.923 1.00 48.52  ? 100 GLU A OE2 1 
ATOM   730  N  N   . ASP A 1 101 ? -10.060 13.738  -18.396 1.00 31.72  ? 101 ASP A N   1 
ATOM   731  C  CA  . ASP A 1 101 ? -10.529 12.529  -19.047 1.00 34.35  ? 101 ASP A CA  1 
ATOM   732  C  C   . ASP A 1 101 ? -11.149 12.845  -20.392 1.00 37.59  ? 101 ASP A C   1 
ATOM   733  O  O   . ASP A 1 101 ? -11.820 13.882  -20.559 1.00 37.67  ? 101 ASP A O   1 
ATOM   734  C  CB  . ASP A 1 101 ? -11.550 11.820  -18.167 1.00 25.18  ? 101 ASP A CB  1 
ATOM   735  C  CG  . ASP A 1 101 ? -11.735 10.365  -18.543 1.00 30.32  ? 101 ASP A CG  1 
ATOM   736  O  OD1 . ASP A 1 101 ? -12.891 9.989   -18.794 1.00 31.51  ? 101 ASP A OD1 1 
ATOM   737  O  OD2 . ASP A 1 101 ? -10.742 9.590   -18.584 1.00 26.44  ? 101 ASP A OD2 1 
ATOM   738  N  N   . SER A 1 102 ? -10.946 11.947  -21.350 1.00 41.49  ? 102 SER A N   1 
ATOM   739  C  CA  . SER A 1 102 ? -11.523 12.146  -22.691 1.00 45.67  ? 102 SER A CA  1 
ATOM   740  C  C   . SER A 1 102 ? -12.499 11.038  -23.081 1.00 48.59  ? 102 SER A C   1 
ATOM   741  O  O   . SER A 1 102 ? -12.801 10.866  -24.278 1.00 49.93  ? 102 SER A O   1 
ATOM   742  C  CB  . SER A 1 102 ? -10.434 12.287  -23.765 1.00 40.58  ? 102 SER A CB  1 
ATOM   743  O  OG  . SER A 1 102 ? -9.736  11.067  -23.960 1.00 40.24  ? 102 SER A OG  1 
ATOM   744  N  N   . VAL A 1 103 ? -12.979 10.282  -22.083 1.00 39.25  ? 103 VAL A N   1 
ATOM   745  C  CA  . VAL A 1 103 ? -14.051 9.319   -22.335 1.00 37.73  ? 103 VAL A CA  1 
ATOM   746  C  C   . VAL A 1 103 ? -15.389 9.871   -21.817 1.00 40.09  ? 103 VAL A C   1 
ATOM   747  O  O   . VAL A 1 103 ? -16.345 9.988   -22.581 1.00 42.76  ? 103 VAL A O   1 
ATOM   748  C  CB  . VAL A 1 103 ? -13.732 7.884   -21.795 1.00 48.74  ? 103 VAL A CB  1 
ATOM   749  C  CG1 . VAL A 1 103 ? -14.917 6.942   -21.993 1.00 28.64  ? 103 VAL A CG1 1 
ATOM   750  C  CG2 . VAL A 1 103 ? -12.506 7.307   -22.474 1.00 28.18  ? 103 VAL A CG2 1 
ATOM   751  N  N   . ILE A 1 104 ? -15.448 10.207  -20.525 1.00 36.95  ? 104 ILE A N   1 
ATOM   752  C  CA  . ILE A 1 104 ? -16.581 10.933  -19.964 1.00 36.31  ? 104 ILE A CA  1 
ATOM   753  C  C   . ILE A 1 104 ? -16.819 12.234  -20.728 1.00 40.89  ? 104 ILE A C   1 
ATOM   754  O  O   . ILE A 1 104 ? -15.903 12.786  -21.333 1.00 43.62  ? 104 ILE A O   1 
ATOM   755  C  CB  . ILE A 1 104 ? -16.346 11.347  -18.501 1.00 34.15  ? 104 ILE A CB  1 
ATOM   756  C  CG1 . ILE A 1 104 ? -15.253 12.422  -18.442 1.00 35.78  ? 104 ILE A CG1 1 
ATOM   757  C  CG2 . ILE A 1 104 ? -16.042 10.138  -17.636 1.00 30.04  ? 104 ILE A CG2 1 
ATOM   758  C  CD1 . ILE A 1 104 ? -15.394 13.389  -17.304 1.00 37.24  ? 104 ILE A CD1 1 
ATOM   759  N  N   . SER A 1 105 ? -18.042 12.749  -20.658 1.00 40.19  ? 105 SER A N   1 
ATOM   760  C  CA  . SER A 1 105 ? -18.416 13.915  -21.445 1.00 38.29  ? 105 SER A CA  1 
ATOM   761  C  C   . SER A 1 105 ? -19.550 14.702  -20.772 1.00 40.80  ? 105 SER A C   1 
ATOM   762  O  O   . SER A 1 105 ? -20.292 14.157  -19.955 1.00 37.79  ? 105 SER A O   1 
ATOM   763  C  CB  . SER A 1 105 ? -18.839 13.471  -22.844 1.00 36.96  ? 105 SER A CB  1 
ATOM   764  O  OG  . SER A 1 105 ? -19.179 14.592  -23.635 1.00 42.04  ? 105 SER A OG  1 
ATOM   765  N  N   . LEU A 1 106 ? -19.672 15.986  -21.105 1.00 42.05  ? 106 LEU A N   1 
ATOM   766  C  CA  . LEU A 1 106 ? -20.808 16.777  -20.647 1.00 41.02  ? 106 LEU A CA  1 
ATOM   767  C  C   . LEU A 1 106 ? -21.877 16.927  -21.738 1.00 47.81  ? 106 LEU A C   1 
ATOM   768  O  O   . LEU A 1 106 ? -22.976 17.427  -21.482 1.00 45.52  ? 106 LEU A O   1 
ATOM   769  C  CB  . LEU A 1 106 ? -20.353 18.159  -20.180 1.00 37.01  ? 106 LEU A CB  1 
ATOM   770  C  CG  . LEU A 1 106 ? -19.263 18.274  -19.114 1.00 38.76  ? 106 LEU A CG  1 
ATOM   771  C  CD1 . LEU A 1 106 ? -19.194 19.734  -18.683 1.00 40.10  ? 106 LEU A CD1 1 
ATOM   772  C  CD2 . LEU A 1 106 ? -19.503 17.368  -17.894 1.00 30.88  ? 106 LEU A CD2 1 
ATOM   773  N  N   . SER A 1 107 ? -21.561 16.488  -22.952 1.00 56.68  ? 107 SER A N   1 
ATOM   774  C  CA  . SER A 1 107 ? -22.450 16.730  -24.085 1.00 66.41  ? 107 SER A CA  1 
ATOM   775  C  C   . SER A 1 107 ? -23.493 15.628  -24.218 1.00 74.59  ? 107 SER A C   1 
ATOM   776  O  O   . SER A 1 107 ? -24.529 15.681  -23.564 1.00 80.10  ? 107 SER A O   1 
ATOM   777  C  CB  . SER A 1 107 ? -21.657 16.904  -25.391 1.00 66.44  ? 107 SER A CB  1 
ATOM   778  O  OG  . SER A 1 107 ? -22.491 17.368  -26.438 1.00 65.33  ? 107 SER A OG  1 
ATOM   779  N  N   . GLY A 1 108 ? -23.225 14.627  -25.052 1.00 77.20  ? 108 GLY A N   1 
ATOM   780  C  CA  . GLY A 1 108 ? -24.216 13.597  -25.320 1.00 79.74  ? 108 GLY A CA  1 
ATOM   781  C  C   . GLY A 1 108 ? -23.685 12.174  -25.293 1.00 81.13  ? 108 GLY A C   1 
ATOM   782  O  O   . GLY A 1 108 ? -22.469 11.955  -25.311 1.00 83.33  ? 108 GLY A O   1 
ATOM   783  N  N   . ASP A 1 109 ? -24.605 11.210  -25.240 1.00 79.12  ? 109 ASP A N   1 
ATOM   784  C  CA  . ASP A 1 109 ? -24.265 9.786   -25.263 1.00 77.36  ? 109 ASP A CA  1 
ATOM   785  C  C   . ASP A 1 109 ? -23.450 9.390   -24.032 1.00 69.61  ? 109 ASP A C   1 
ATOM   786  O  O   . ASP A 1 109 ? -23.962 8.758   -23.109 1.00 68.26  ? 109 ASP A O   1 
ATOM   787  C  CB  . ASP A 1 109 ? -23.499 9.435   -26.545 1.00 84.55  ? 109 ASP A CB  1 
ATOM   788  C  CG  . ASP A 1 109 ? -24.243 8.437   -27.422 1.00 90.17  ? 109 ASP A CG  1 
ATOM   789  O  OD1 . ASP A 1 109 ? -25.493 8.479   -27.456 1.00 92.83  ? 109 ASP A OD1 1 
ATOM   790  O  OD2 . ASP A 1 109 ? -23.572 7.609   -28.077 1.00 90.70  ? 109 ASP A OD2 1 
ATOM   791  N  N   . HIS A 1 110 ? -22.177 9.765   -24.022 1.00 62.76  ? 110 HIS A N   1 
ATOM   792  C  CA  . HIS A 1 110 ? -21.337 9.529   -22.858 1.00 58.23  ? 110 HIS A CA  1 
ATOM   793  C  C   . HIS A 1 110 ? -21.565 10.621  -21.822 1.00 58.32  ? 110 HIS A C   1 
ATOM   794  O  O   . HIS A 1 110 ? -20.872 10.679  -20.805 1.00 59.07  ? 110 HIS A O   1 
ATOM   795  C  CB  . HIS A 1 110 ? -19.860 9.440   -23.259 1.00 54.92  ? 110 HIS A CB  1 
ATOM   796  C  CG  . HIS A 1 110 ? -19.532 8.229   -24.082 1.00 50.95  ? 110 HIS A CG  1 
ATOM   797  N  ND1 . HIS A 1 110 ? -20.502 7.385   -24.588 1.00 51.61  ? 110 HIS A ND1 1 
ATOM   798  C  CD2 . HIS A 1 110 ? -18.347 7.716   -24.482 1.00 46.73  ? 110 HIS A CD2 1 
ATOM   799  C  CE1 . HIS A 1 110 ? -19.924 6.407   -25.260 1.00 50.23  ? 110 HIS A CE1 1 
ATOM   800  N  NE2 . HIS A 1 110 ? -18.615 6.582   -25.206 1.00 47.94  ? 110 HIS A NE2 1 
ATOM   801  N  N   . CYS A 1 111 ? -22.554 11.474  -22.086 1.00 55.20  ? 111 CYS A N   1 
ATOM   802  C  CA  . CYS A 1 111 ? -22.932 12.546  -21.165 1.00 49.70  ? 111 CYS A CA  1 
ATOM   803  C  C   . CYS A 1 111 ? -23.242 12.010  -19.761 1.00 43.23  ? 111 CYS A C   1 
ATOM   804  O  O   . CYS A 1 111 ? -24.125 11.186  -19.585 1.00 45.32  ? 111 CYS A O   1 
ATOM   805  C  CB  . CYS A 1 111 ? -24.115 13.344  -21.711 1.00 35.51  ? 111 CYS A CB  1 
ATOM   806  S  SG  . CYS A 1 111 ? -24.764 14.594  -20.569 1.00 61.31  ? 111 CYS A SG  1 
ATOM   807  N  N   . ILE A 1 112 ? -22.501 12.507  -18.780 1.00 39.82  ? 112 ILE A N   1 
ATOM   808  C  CA  . ILE A 1 112 ? -22.578 12.060  -17.397 1.00 42.51  ? 112 ILE A CA  1 
ATOM   809  C  C   . ILE A 1 112 ? -23.440 13.001  -16.558 1.00 45.93  ? 112 ILE A C   1 
ATOM   810  O  O   . ILE A 1 112 ? -23.420 12.950  -15.322 1.00 42.38  ? 112 ILE A O   1 
ATOM   811  C  CB  . ILE A 1 112 ? -21.153 11.940  -16.768 1.00 38.68  ? 112 ILE A CB  1 
ATOM   812  C  CG1 . ILE A 1 112 ? -20.323 13.190  -17.048 1.00 39.42  ? 112 ILE A CG1 1 
ATOM   813  C  CG2 . ILE A 1 112 ? -20.403 10.735  -17.330 1.00 34.79  ? 112 ILE A CG2 1 
ATOM   814  C  CD1 . ILE A 1 112 ? -20.411 14.234  -15.986 1.00 41.67  ? 112 ILE A CD1 1 
ATOM   815  N  N   . ILE A 1 113 ? -24.207 13.856  -17.231 1.00 50.93  ? 113 ILE A N   1 
ATOM   816  C  CA  . ILE A 1 113 ? -24.992 14.859  -16.525 1.00 50.45  ? 113 ILE A CA  1 
ATOM   817  C  C   . ILE A 1 113 ? -26.289 14.260  -16.012 1.00 50.03  ? 113 ILE A C   1 
ATOM   818  O  O   . ILE A 1 113 ? -26.919 13.448  -16.689 1.00 52.11  ? 113 ILE A O   1 
ATOM   819  C  CB  . ILE A 1 113 ? -25.256 16.082  -17.383 1.00 56.74  ? 113 ILE A CB  1 
ATOM   820  C  CG1 . ILE A 1 113 ? -25.263 17.342  -16.513 1.00 53.09  ? 113 ILE A CG1 1 
ATOM   821  C  CG2 . ILE A 1 113 ? -26.520 15.894  -18.206 1.00 66.27  ? 113 ILE A CG2 1 
ATOM   822  C  CD1 . ILE A 1 113 ? -23.891 18.031  -16.437 1.00 48.84  ? 113 ILE A CD1 1 
ATOM   823  N  N   . GLY A 1 114 ? -26.657 14.638  -14.792 1.00 47.05  ? 114 GLY A N   1 
ATOM   824  C  CA  . GLY A 1 114 ? -27.768 14.011  -14.103 1.00 44.27  ? 114 GLY A CA  1 
ATOM   825  C  C   . GLY A 1 114 ? -27.386 12.619  -13.620 1.00 43.57  ? 114 GLY A C   1 
ATOM   826  O  O   . GLY A 1 114 ? -28.235 11.801  -13.273 1.00 43.73  ? 114 GLY A O   1 
ATOM   827  N  N   . ARG A 1 115 ? -26.088 12.354  -13.613 1.00 41.75  ? 115 ARG A N   1 
ATOM   828  C  CA  . ARG A 1 115 ? -25.565 11.079  -13.170 1.00 40.46  ? 115 ARG A CA  1 
ATOM   829  C  C   . ARG A 1 115 ? -24.917 11.291  -11.803 1.00 43.18  ? 115 ARG A C   1 
ATOM   830  O  O   . ARG A 1 115 ? -24.844 12.428  -11.335 1.00 46.20  ? 115 ARG A O   1 
ATOM   831  C  CB  . ARG A 1 115 ? -24.542 10.575  -14.185 1.00 39.75  ? 115 ARG A CB  1 
ATOM   832  C  CG  . ARG A 1 115 ? -24.919 9.290   -14.872 1.00 39.33  ? 115 ARG A CG  1 
ATOM   833  C  CD  . ARG A 1 115 ? -25.369 9.440   -16.308 1.00 43.63  ? 115 ARG A CD  1 
ATOM   834  N  NE  . ARG A 1 115 ? -26.144 8.252   -16.652 1.00 46.47  ? 115 ARG A NE  1 
ATOM   835  C  CZ  . ARG A 1 115 ? -26.642 7.956   -17.848 1.00 46.98  ? 115 ARG A CZ  1 
ATOM   836  N  NH1 . ARG A 1 115 ? -26.464 8.758   -18.893 1.00 42.35  ? 115 ARG A NH1 1 
ATOM   837  N  NH2 . ARG A 1 115 ? -27.322 6.823   -17.988 1.00 50.26  ? 115 ARG A NH2 1 
ATOM   838  N  N   . THR A 1 116 ? -24.472 10.215  -11.155 1.00 39.42  ? 116 THR A N   1 
ATOM   839  C  CA  . THR A 1 116 ? -23.852 10.340  -9.832  1.00 36.29  ? 116 THR A CA  1 
ATOM   840  C  C   . THR A 1 116 ? -22.340 10.083  -9.860  1.00 43.52  ? 116 THR A C   1 
ATOM   841  O  O   . THR A 1 116 ? -21.844 9.157   -10.498 1.00 47.80  ? 116 THR A O   1 
ATOM   842  C  CB  . THR A 1 116 ? -24.516 9.436   -8.788  1.00 38.21  ? 116 THR A CB  1 
ATOM   843  O  OG1 . THR A 1 116 ? -25.905 9.770   -8.699  1.00 44.59  ? 116 THR A OG1 1 
ATOM   844  C  CG2 . THR A 1 116 ? -23.850 9.588   -7.379  1.00 21.37  ? 116 THR A CG2 1 
ATOM   845  N  N   . LEU A 1 117 ? -21.615 10.950  -9.174  1.00 42.39  ? 117 LEU A N   1 
ATOM   846  C  CA  . LEU A 1 117 ? -20.188 10.836  -9.023  1.00 35.53  ? 117 LEU A CA  1 
ATOM   847  C  C   . LEU A 1 117 ? -19.970 10.335  -7.601  1.00 33.57  ? 117 LEU A C   1 
ATOM   848  O  O   . LEU A 1 117 ? -20.512 10.911  -6.654  1.00 33.45  ? 117 LEU A O   1 
ATOM   849  C  CB  . LEU A 1 117 ? -19.571 12.221  -9.197  1.00 37.10  ? 117 LEU A CB  1 
ATOM   850  C  CG  . LEU A 1 117 ? -18.121 12.475  -8.761  1.00 36.71  ? 117 LEU A CG  1 
ATOM   851  C  CD1 . LEU A 1 117 ? -17.119 11.731  -9.641  1.00 34.00  ? 117 LEU A CD1 1 
ATOM   852  C  CD2 . LEU A 1 117 ? -17.836 13.962  -8.766  1.00 35.73  ? 117 LEU A CD2 1 
ATOM   853  N  N   . VAL A 1 118 ? -19.182 9.271   -7.455  1.00 27.33  ? 118 VAL A N   1 
ATOM   854  C  CA  . VAL A 1 118 ? -18.880 8.691   -6.155  1.00 24.25  ? 118 VAL A CA  1 
ATOM   855  C  C   . VAL A 1 118 ? -17.381 8.715   -5.851  1.00 27.78  ? 118 VAL A C   1 
ATOM   856  O  O   . VAL A 1 118 ? -16.556 8.443   -6.740  1.00 29.60  ? 118 VAL A O   1 
ATOM   857  C  CB  . VAL A 1 118 ? -19.326 7.206   -6.108  1.00 33.44  ? 118 VAL A CB  1 
ATOM   858  C  CG1 . VAL A 1 118 ? -19.397 6.691   -4.661  1.00 34.49  ? 118 VAL A CG1 1 
ATOM   859  C  CG2 . VAL A 1 118 ? -20.650 7.022   -6.822  1.00 30.23  ? 118 VAL A CG2 1 
ATOM   860  N  N   . VAL A 1 119 ? -17.046 9.050   -4.601  1.00 25.15  ? 119 VAL A N   1 
ATOM   861  C  CA  . VAL A 1 119 ? -15.726 8.803   -4.028  1.00 26.92  ? 119 VAL A CA  1 
ATOM   862  C  C   . VAL A 1 119 ? -15.875 7.633   -3.035  1.00 30.40  ? 119 VAL A C   1 
ATOM   863  O  O   . VAL A 1 119 ? -16.882 7.552   -2.322  1.00 29.54  ? 119 VAL A O   1 
ATOM   864  C  CB  . VAL A 1 119 ? -15.103 10.061  -3.304  1.00 28.29  ? 119 VAL A CB  1 
ATOM   865  C  CG1 . VAL A 1 119 ? -16.041 10.651  -2.254  1.00 27.58  ? 119 VAL A CG1 1 
ATOM   866  C  CG2 . VAL A 1 119 ? -13.788 9.706   -2.601  1.00 24.91  ? 119 VAL A CG2 1 
ATOM   867  N  N   . HIS A 1 120 ? -14.867 6.756   -2.961  1.00 29.10  ? 120 HIS A N   1 
ATOM   868  C  CA  . HIS A 1 120 ? -15.017 5.491   -2.242  1.00 29.13  ? 120 HIS A CA  1 
ATOM   869  C  C   . HIS A 1 120 ? -14.210 5.335   -0.965  1.00 32.81  ? 120 HIS A C   1 
ATOM   870  O  O   . HIS A 1 120 ? -13.343 6.137   -0.653  1.00 37.00  ? 120 HIS A O   1 
ATOM   871  C  CB  . HIS A 1 120 ? -14.743 4.316   -3.173  1.00 29.83  ? 120 HIS A CB  1 
ATOM   872  C  CG  . HIS A 1 120 ? -15.861 4.044   -4.128  1.00 29.21  ? 120 HIS A CG  1 
ATOM   873  N  ND1 . HIS A 1 120 ? -16.850 3.117   -3.873  1.00 22.23  ? 120 HIS A ND1 1 
ATOM   874  C  CD2 . HIS A 1 120 ? -16.171 4.604   -5.318  1.00 28.31  ? 120 HIS A CD2 1 
ATOM   875  C  CE1 . HIS A 1 120 ? -17.704 3.103   -4.873  1.00 16.36  ? 120 HIS A CE1 1 
ATOM   876  N  NE2 . HIS A 1 120 ? -17.322 4.005   -5.757  1.00 26.50  ? 120 HIS A NE2 1 
ATOM   877  N  N   . GLU A 1 121 ? -14.526 4.272   -0.239  1.00 32.95  ? 121 GLU A N   1 
ATOM   878  C  CA  . GLU A 1 121 ? -13.877 3.921   1.010   1.00 33.12  ? 121 GLU A CA  1 
ATOM   879  C  C   . GLU A 1 121 ? -12.407 3.542   0.803   1.00 32.23  ? 121 GLU A C   1 
ATOM   880  O  O   . GLU A 1 121 ? -11.547 3.857   1.621   1.00 30.56  ? 121 GLU A O   1 
ATOM   881  C  CB  . GLU A 1 121 ? -14.631 2.740   1.616   1.00 38.32  ? 121 GLU A CB  1 
ATOM   882  C  CG  . GLU A 1 121 ? -13.971 2.058   2.793   1.00 39.92  ? 121 GLU A CG  1 
ATOM   883  C  CD  . GLU A 1 121 ? -14.527 0.643   3.016   1.00 41.92  ? 121 GLU A CD  1 
ATOM   884  O  OE1 . GLU A 1 121 ? -15.526 0.296   2.345   1.00 43.68  ? 121 GLU A OE1 1 
ATOM   885  O  OE2 . GLU A 1 121 ? -13.963 -0.114  3.844   1.00 38.42  ? 121 GLU A OE2 1 
ATOM   886  N  N   . LYS A 1 122 ? -12.121 2.870   -0.300  1.00 30.45  ? 122 LYS A N   1 
ATOM   887  C  CA  . LYS A 1 122 ? -10.780 2.339   -0.515  1.00 32.14  ? 122 LYS A CA  1 
ATOM   888  C  C   . LYS A 1 122 ? -10.245 2.619   -1.913  1.00 30.53  ? 122 LYS A C   1 
ATOM   889  O  O   . LYS A 1 122 ? -10.931 3.206   -2.775  1.00 30.46  ? 122 LYS A O   1 
ATOM   890  C  CB  . LYS A 1 122 ? -10.760 0.828   -0.260  1.00 33.57  ? 122 LYS A CB  1 
ATOM   891  C  CG  . LYS A 1 122 ? -11.257 0.431   1.125   1.00 35.39  ? 122 LYS A CG  1 
ATOM   892  C  CD  . LYS A 1 122 ? -11.259 -1.077  1.337   1.00 39.47  ? 122 LYS A CD  1 
ATOM   893  C  CE  . LYS A 1 122 ? -11.947 -1.786  0.184   1.00 45.41  ? 122 LYS A CE  1 
ATOM   894  N  NZ  . LYS A 1 122 ? -12.299 -3.195  0.508   1.00 47.09  ? 122 LYS A NZ  1 
ATOM   895  N  N   . ALA A 1 123 ? -9.017  2.171   -2.135  1.00 22.82  ? 123 ALA A N   1 
ATOM   896  C  CA  . ALA A 1 123 ? -8.387  2.338   -3.433  1.00 24.31  ? 123 ALA A CA  1 
ATOM   897  C  C   . ALA A 1 123 ? -9.099  1.526   -4.490  1.00 25.34  ? 123 ALA A C   1 
ATOM   898  O  O   . ALA A 1 123 ? -9.546  0.401   -4.247  1.00 27.59  ? 123 ALA A O   1 
ATOM   899  C  CB  . ALA A 1 123 ? -6.916  1.948   -3.372  1.00 19.98  ? 123 ALA A CB  1 
ATOM   900  N  N   . ASP A 1 124 ? -9.195  2.103   -5.675  1.00 28.30  ? 124 ASP A N   1 
ATOM   901  C  CA  . ASP A 1 124 ? -9.662  1.389   -6.855  1.00 20.48  ? 124 ASP A CA  1 
ATOM   902  C  C   . ASP A 1 124 ? -8.487  0.612   -7.432  1.00 15.56  ? 124 ASP A C   1 
ATOM   903  O  O   . ASP A 1 124 ? -7.500  1.222   -7.806  1.00 14.02  ? 124 ASP A O   1 
ATOM   904  C  CB  . ASP A 1 124 ? -10.096 2.430   -7.864  1.00 19.94  ? 124 ASP A CB  1 
ATOM   905  C  CG  . ASP A 1 124 ? -10.686 1.831   -9.124  1.00 21.74  ? 124 ASP A CG  1 
ATOM   906  O  OD1 . ASP A 1 124 ? -10.363 0.682   -9.501  1.00 24.21  ? 124 ASP A OD1 1 
ATOM   907  O  OD2 . ASP A 1 124 ? -11.500 2.532   -9.729  1.00 21.90  ? 124 ASP A OD2 1 
ATOM   908  N  N   . ASP A 1 125 ? -8.576  -0.719  -7.522  1.00 16.84  ? 125 ASP A N   1 
ATOM   909  C  CA  . ASP A 1 125 ? -7.468  -1.489  -8.122  1.00 13.77  ? 125 ASP A CA  1 
ATOM   910  C  C   . ASP A 1 125 ? -7.437  -1.515  -9.689  1.00 25.46  ? 125 ASP A C   1 
ATOM   911  O  O   . ASP A 1 125 ? -6.676  -2.253  -10.296 1.00 24.86  ? 125 ASP A O   1 
ATOM   912  C  CB  . ASP A 1 125 ? -7.294  -2.886  -7.491  1.00 13.18  ? 125 ASP A CB  1 
ATOM   913  C  CG  . ASP A 1 125 ? -8.454  -3.879  -7.801  1.00 32.87  ? 125 ASP A CG  1 
ATOM   914  O  OD1 . ASP A 1 125 ? -9.093  -3.822  -8.897  1.00 30.34  ? 125 ASP A OD1 1 
ATOM   915  O  OD2 . ASP A 1 125 ? -8.693  -4.761  -6.930  1.00 28.35  ? 125 ASP A OD2 1 
ATOM   916  N  N   . LEU A 1 126 ? -8.240  -0.690  -10.341 1.00 20.66  ? 126 LEU A N   1 
ATOM   917  C  CA  . LEU A 1 126 ? -8.094  -0.533  -11.785 1.00 26.10  ? 126 LEU A CA  1 
ATOM   918  C  C   . LEU A 1 126 ? -8.214  -1.854  -12.576 1.00 22.32  ? 126 LEU A C   1 
ATOM   919  O  O   . LEU A 1 126 ? -7.577  -2.012  -13.603 1.00 23.66  ? 126 LEU A O   1 
ATOM   920  C  CB  . LEU A 1 126 ? -6.743  0.117   -12.107 1.00 25.08  ? 126 LEU A CB  1 
ATOM   921  C  CG  . LEU A 1 126 ? -6.286  1.402   -11.395 1.00 26.14  ? 126 LEU A CG  1 
ATOM   922  C  CD1 . LEU A 1 126 ? -4.916  1.829   -11.871 1.00 16.13  ? 126 LEU A CD1 1 
ATOM   923  C  CD2 . LEU A 1 126 ? -7.283  2.545   -11.520 1.00 16.52  ? 126 LEU A CD2 1 
ATOM   924  N  N   . GLY A 1 127 ? -9.031  -2.790  -12.102 1.00 19.88  ? 127 GLY A N   1 
ATOM   925  C  CA  . GLY A 1 127 ? -9.211  -4.075  -12.767 1.00 18.21  ? 127 GLY A CA  1 
ATOM   926  C  C   . GLY A 1 127 ? -8.104  -5.102  -12.527 1.00 20.65  ? 127 GLY A C   1 
ATOM   927  O  O   . GLY A 1 127 ? -8.263  -6.260  -12.817 1.00 19.70  ? 127 GLY A O   1 
ATOM   928  N  N   . LYS A 1 128 ? -6.987  -4.680  -11.953 1.00 28.05  ? 128 LYS A N   1 
ATOM   929  C  CA  . LYS A 1 128 ? -5.838  -5.556  -11.725 1.00 31.94  ? 128 LYS A CA  1 
ATOM   930  C  C   . LYS A 1 128 ? -5.905  -6.399  -10.417 1.00 32.32  ? 128 LYS A C   1 
ATOM   931  O  O   . LYS A 1 128 ? -4.913  -7.029  -10.013 1.00 29.78  ? 128 LYS A O   1 
ATOM   932  C  CB  . LYS A 1 128 ? -4.540  -4.714  -11.776 1.00 33.58  ? 128 LYS A CB  1 
ATOM   933  C  CG  . LYS A 1 128 ? -4.424  -3.796  -13.007 1.00 37.36  ? 128 LYS A CG  1 
ATOM   934  C  CD  . LYS A 1 128 ? -2.958  -3.466  -13.356 0.70 42.28  ? 128 LYS A CD  1 
ATOM   935  C  CE  . LYS A 1 128 ? -2.255  -2.577  -12.323 0.70 45.64  ? 128 LYS A CE  1 
ATOM   936  N  NZ  . LYS A 1 128 ? -2.580  -1.107  -12.394 1.00 49.70  ? 128 LYS A NZ  1 
ATOM   937  N  N   . GLY A 1 129 ? -7.068  -6.428  -9.774  1.00 29.42  ? 129 GLY A N   1 
ATOM   938  C  CA  . GLY A 1 129 ? -7.239  -7.164  -8.527  1.00 32.50  ? 129 GLY A CA  1 
ATOM   939  C  C   . GLY A 1 129 ? -7.241  -8.696  -8.491  1.00 30.84  ? 129 GLY A C   1 
ATOM   940  O  O   . GLY A 1 129 ? -6.920  -9.269  -7.449  1.00 28.68  ? 129 GLY A O   1 
ATOM   941  N  N   . GLY A 1 130 ? -7.623  -9.365  -9.580  1.00 26.96  ? 130 GLY A N   1 
ATOM   942  C  CA  . GLY A 1 130 ? -7.567  -10.821 -9.632  1.00 13.53  ? 130 GLY A CA  1 
ATOM   943  C  C   . GLY A 1 130 ? -8.775  -11.525 -9.022  1.00 19.92  ? 130 GLY A C   1 
ATOM   944  O  O   . GLY A 1 130 ? -8.765  -12.729 -8.814  1.00 18.10  ? 130 GLY A O   1 
ATOM   945  N  N   . ASN A 1 131 ? -9.819  -10.769 -8.704  1.00 24.96  ? 131 ASN A N   1 
ATOM   946  C  CA  . ASN A 1 131 ? -11.105 -11.373 -8.338  1.00 29.81  ? 131 ASN A CA  1 
ATOM   947  C  C   . ASN A 1 131 ? -12.206 -10.828 -9.230  1.00 32.16  ? 131 ASN A C   1 
ATOM   948  O  O   . ASN A 1 131 ? -11.944 -9.974  -10.073 1.00 32.44  ? 131 ASN A O   1 
ATOM   949  C  CB  . ASN A 1 131 ? -11.462 -11.206 -6.841  1.00 28.95  ? 131 ASN A CB  1 
ATOM   950  C  CG  . ASN A 1 131 ? -11.403 -9.757  -6.366  1.00 30.39  ? 131 ASN A CG  1 
ATOM   951  O  OD1 . ASN A 1 131 ? -11.527 -8.824  -7.158  1.00 29.26  ? 131 ASN A OD1 1 
ATOM   952  N  ND2 . ASN A 1 131 ? -11.219 -9.567  -5.056  1.00 26.64  ? 131 ASN A ND2 1 
ATOM   953  N  N   . GLU A 1 132 ? -13.424 -11.335 -9.041  1.00 37.50  ? 132 GLU A N   1 
ATOM   954  C  CA  A GLU A 1 132 ? -14.529 -10.924 -9.895  0.50 33.63  ? 132 GLU A CA  1 
ATOM   955  C  CA  B GLU A 1 132 ? -14.607 -10.964 -9.818  0.50 33.24  ? 132 GLU A CA  1 
ATOM   956  C  C   . GLU A 1 132 ? -14.960 -9.500  -9.557  1.00 32.24  ? 132 GLU A C   1 
ATOM   957  O  O   . GLU A 1 132 ? -15.363 -8.755  -10.449 1.00 36.99  ? 132 GLU A O   1 
ATOM   958  C  CB  A GLU A 1 132 ? -15.693 -11.922 -9.842  0.50 32.42  ? 132 GLU A CB  1 
ATOM   959  C  CB  B GLU A 1 132 ? -15.766 -11.903 -9.425  0.50 32.04  ? 132 GLU A CB  1 
ATOM   960  C  CG  A GLU A 1 132 ? -16.940 -11.515 -10.627 0.50 33.75  ? 132 GLU A CG  1 
ATOM   961  C  CG  B GLU A 1 132 ? -17.152 -11.571 -9.968  0.50 33.10  ? 132 GLU A CG  1 
ATOM   962  C  CD  A GLU A 1 132 ? -16.736 -11.433 -12.147 0.50 33.79  ? 132 GLU A CD  1 
ATOM   963  C  CD  B GLU A 1 132 ? -18.236 -12.566 -9.523  0.50 35.41  ? 132 GLU A CD  1 
ATOM   964  O  OE1 A GLU A 1 132 ? -15.626 -11.752 -12.626 0.50 29.46  ? 132 GLU A OE1 1 
ATOM   965  O  OE1 B GLU A 1 132 ? -17.908 -13.589 -8.887  0.50 37.36  ? 132 GLU A OE1 1 
ATOM   966  O  OE2 A GLU A 1 132 ? -17.706 -11.047 -12.857 0.50 33.47  ? 132 GLU A OE2 1 
ATOM   967  O  OE2 B GLU A 1 132 ? -19.427 -12.334 -9.813  0.50 36.88  ? 132 GLU A OE2 1 
ATOM   968  N  N   . GLU A 1 133 ? -14.809 -9.105  -8.302  1.00 29.65  ? 133 GLU A N   1 
ATOM   969  C  CA  . GLU A 1 133 ? -15.181 -7.775  -7.863  1.00 28.40  ? 133 GLU A CA  1 
ATOM   970  C  C   . GLU A 1 133 ? -14.330 -6.722  -8.558  1.00 27.55  ? 133 GLU A C   1 
ATOM   971  O  O   . GLU A 1 133 ? -14.803 -5.635  -8.899  1.00 26.94  ? 133 GLU A O   1 
ATOM   972  C  CB  . GLU A 1 133 ? -15.013 -7.672  -6.343  1.00 28.08  ? 133 GLU A CB  1 
ATOM   973  C  CG  . GLU A 1 133 ? -15.734 -6.480  -5.717  1.00 29.46  ? 133 GLU A CG  1 
ATOM   974  C  CD  . GLU A 1 133 ? -17.235 -6.508  -5.979  1.00 38.41  ? 133 GLU A CD  1 
ATOM   975  O  OE1 . GLU A 1 133 ? -17.882 -7.523  -5.631  1.00 44.88  ? 133 GLU A OE1 1 
ATOM   976  O  OE2 . GLU A 1 133 ? -17.768 -5.531  -6.548  1.00 40.55  ? 133 GLU A OE2 1 
ATOM   977  N  N   . SER A 1 134 ? -13.064 -7.063  -8.768  1.00 23.28  ? 134 SER A N   1 
ATOM   978  C  CA  . SER A 1 134 ? -12.124 -6.159  -9.389  1.00 26.77  ? 134 SER A CA  1 
ATOM   979  C  C   . SER A 1 134 ? -12.585 -5.804  -10.798 1.00 30.88  ? 134 SER A C   1 
ATOM   980  O  O   . SER A 1 134 ? -12.284 -4.722  -11.290 1.00 32.98  ? 134 SER A O   1 
ATOM   981  C  CB  . SER A 1 134 ? -10.731 -6.782  -9.448  1.00 29.79  ? 134 SER A CB  1 
ATOM   982  O  OG  . SER A 1 134 ? -9.748  -5.818  -9.766  1.00 30.88  ? 134 SER A OG  1 
ATOM   983  N  N   . THR A 1 135 ? -13.320 -6.707  -11.441 1.00 31.81  ? 135 THR A N   1 
ATOM   984  C  CA  . THR A 1 135 ? -13.854 -6.411  -12.768 1.00 39.08  ? 135 THR A CA  1 
ATOM   985  C  C   . THR A 1 135 ? -15.188 -5.646  -12.744 1.00 36.56  ? 135 THR A C   1 
ATOM   986  O  O   . THR A 1 135 ? -15.680 -5.237  -13.795 1.00 38.43  ? 135 THR A O   1 
ATOM   987  C  CB  . THR A 1 135 ? -13.970 -7.675  -13.633 1.00 44.03  ? 135 THR A CB  1 
ATOM   988  O  OG1 . THR A 1 135 ? -14.708 -8.675  -12.918 1.00 46.14  ? 135 THR A OG1 1 
ATOM   989  C  CG2 . THR A 1 135 ? -12.582 -8.204  -13.959 1.00 42.13  ? 135 THR A CG2 1 
ATOM   990  N  N   . LYS A 1 136 ? -15.757 -5.443  -11.558 1.00 31.60  ? 136 LYS A N   1 
ATOM   991  C  CA  . LYS A 1 136 ? -16.992 -4.649  -11.440 1.00 33.95  ? 136 LYS A CA  1 
ATOM   992  C  C   . LYS A 1 136 ? -16.767 -3.261  -10.844 1.00 31.14  ? 136 LYS A C   1 
ATOM   993  O  O   . LYS A 1 136 ? -17.242 -2.255  -11.371 1.00 27.78  ? 136 LYS A O   1 
ATOM   994  C  CB  . LYS A 1 136 ? -18.048 -5.380  -10.609 1.00 35.81  ? 136 LYS A CB  1 
ATOM   995  C  CG  . LYS A 1 136 ? -18.519 -6.697  -11.201 1.00 40.85  ? 136 LYS A CG  1 
ATOM   996  C  CD  . LYS A 1 136 ? -19.402 -7.422  -10.209 1.00 47.15  ? 136 LYS A CD  1 
ATOM   997  C  CE  . LYS A 1 136 ? -19.123 -8.924  -10.214 1.00 50.41  ? 136 LYS A CE  1 
ATOM   998  N  NZ  . LYS A 1 136 ? -19.093 -9.464  -8.815  1.00 49.61  ? 136 LYS A NZ  1 
ATOM   999  N  N   . THR A 1 137 ? -16.037 -3.213  -9.734  1.00 32.97  ? 137 THR A N   1 
ATOM   1000 C  CA  . THR A 1 137 ? -15.893 -1.977  -8.982  1.00 29.76  ? 137 THR A CA  1 
ATOM   1001 C  C   . THR A 1 137 ? -14.450 -1.671  -8.682  1.00 30.56  ? 137 THR A C   1 
ATOM   1002 O  O   . THR A 1 137 ? -14.154 -0.693  -8.013  1.00 32.44  ? 137 THR A O   1 
ATOM   1003 C  CB  . THR A 1 137 ? -16.647 -2.055  -7.660  1.00 28.52  ? 137 THR A CB  1 
ATOM   1004 O  OG1 . THR A 1 137 ? -16.079 -3.091  -6.848  1.00 30.21  ? 137 THR A OG1 1 
ATOM   1005 C  CG2 . THR A 1 137 ? -18.107 -2.362  -7.908  1.00 28.43  ? 137 THR A CG2 1 
ATOM   1006 N  N   . GLY A 1 138 ? -13.556 -2.515  -9.178  1.00 32.48  ? 138 GLY A N   1 
ATOM   1007 C  CA  . GLY A 1 138 ? -12.152 -2.400  -8.859  1.00 31.85  ? 138 GLY A CA  1 
ATOM   1008 C  C   . GLY A 1 138 ? -11.890 -2.492  -7.360  1.00 31.20  ? 138 GLY A C   1 
ATOM   1009 O  O   . GLY A 1 138 ? -10.860 -2.001  -6.875  1.00 38.23  ? 138 GLY A O   1 
ATOM   1010 N  N   . ASN A 1 139 ? -12.820 -3.101  -6.625  1.00 22.13  ? 139 ASN A N   1 
ATOM   1011 C  CA  . ASN A 1 139 ? -12.645 -3.333  -5.185  1.00 20.79  ? 139 ASN A CA  1 
ATOM   1012 C  C   . ASN A 1 139 ? -12.595 -2.061  -4.370  1.00 22.33  ? 139 ASN A C   1 
ATOM   1013 O  O   . ASN A 1 139 ? -12.021 -2.055  -3.290  1.00 23.44  ? 139 ASN A O   1 
ATOM   1014 C  CB  . ASN A 1 139 ? -11.398 -4.191  -4.871  1.00 21.01  ? 139 ASN A CB  1 
ATOM   1015 C  CG  . ASN A 1 139 ? -11.549 -5.640  -5.329  1.00 29.60  ? 139 ASN A CG  1 
ATOM   1016 O  OD1 . ASN A 1 139 ? -12.354 -6.380  -4.777  1.00 34.48  ? 139 ASN A OD1 1 
ATOM   1017 N  ND2 . ASN A 1 139 ? -10.783 -6.042  -6.356  1.00 27.43  ? 139 ASN A ND2 1 
ATOM   1018 N  N   . ALA A 1 140 ? -13.219 -0.994  -4.873  1.00 26.95  ? 140 ALA A N   1 
ATOM   1019 C  CA  . ALA A 1 140 ? -13.146 0.310   -4.213  1.00 27.35  ? 140 ALA A CA  1 
ATOM   1020 C  C   . ALA A 1 140 ? -13.936 0.446   -2.892  1.00 31.01  ? 140 ALA A C   1 
ATOM   1021 O  O   . ALA A 1 140 ? -13.722 1.397   -2.142  1.00 33.16  ? 140 ALA A O   1 
ATOM   1022 C  CB  . ALA A 1 140 ? -13.513 1.404   -5.169  1.00 23.91  ? 140 ALA A CB  1 
ATOM   1023 N  N   . GLY A 1 141 ? -14.828 -0.498  -2.600  1.00 30.21  ? 141 GLY A N   1 
ATOM   1024 C  CA  . GLY A 1 141 ? -15.519 -0.509  -1.315  1.00 32.16  ? 141 GLY A CA  1 
ATOM   1025 C  C   . GLY A 1 141 ? -16.774 0.346   -1.197  1.00 36.63  ? 141 GLY A C   1 
ATOM   1026 O  O   . GLY A 1 141 ? -17.500 0.579   -2.180  1.00 38.33  ? 141 GLY A O   1 
ATOM   1027 N  N   . SER A 1 142 ? -17.048 0.828   0.011   1.00 33.96  ? 142 SER A N   1 
ATOM   1028 C  CA  A SER A 1 142 ? -18.267 1.600   0.255   0.50 30.24  ? 142 SER A CA  1 
ATOM   1029 C  CA  B SER A 1 142 ? -18.276 1.580   0.248   0.50 30.23  ? 142 SER A CA  1 
ATOM   1030 C  C   . SER A 1 142 ? -18.277 2.879   -0.562  1.00 34.61  ? 142 SER A C   1 
ATOM   1031 O  O   . SER A 1 142 ? -17.291 3.213   -1.230  1.00 33.13  ? 142 SER A O   1 
ATOM   1032 C  CB  A SER A 1 142 ? -18.397 1.962   1.736   0.50 25.35  ? 142 SER A CB  1 
ATOM   1033 C  CB  B SER A 1 142 ? -18.489 1.851   1.750   0.50 25.17  ? 142 SER A CB  1 
ATOM   1034 O  OG  A SER A 1 142 ? -18.062 0.867   2.549   0.50 22.76  ? 142 SER A OG  1 
ATOM   1035 O  OG  B SER A 1 142 ? -17.685 2.917   2.226   0.50 21.12  ? 142 SER A OG  1 
ATOM   1036 N  N   . ARG A 1 143 ? -19.399 3.595   -0.499  1.00 37.79  ? 143 ARG A N   1 
ATOM   1037 C  CA  . ARG A 1 143 ? -19.542 4.896   -1.126  1.00 32.39  ? 143 ARG A CA  1 
ATOM   1038 C  C   . ARG A 1 143 ? -19.604 5.862   0.025   1.00 27.94  ? 143 ARG A C   1 
ATOM   1039 O  O   . ARG A 1 143 ? -20.562 5.856   0.770   1.00 32.28  ? 143 ARG A O   1 
ATOM   1040 C  CB  . ARG A 1 143 ? -20.828 4.940   -1.957  1.00 32.97  ? 143 ARG A CB  1 
ATOM   1041 C  CG  . ARG A 1 143 ? -21.077 3.651   -2.735  1.00 24.30  ? 143 ARG A CG  1 
ATOM   1042 C  CD  . ARG A 1 143 ? -22.129 3.777   -3.818  1.00 30.26  ? 143 ARG A CD  1 
ATOM   1043 N  NE  . ARG A 1 143 ? -22.129 2.577   -4.658  1.00 33.09  ? 143 ARG A NE  1 
ATOM   1044 C  CZ  . ARG A 1 143 ? -23.018 2.308   -5.606  1.00 26.24  ? 143 ARG A CZ  1 
ATOM   1045 N  NH1 . ARG A 1 143 ? -23.998 3.150   -5.863  1.00 27.46  ? 143 ARG A NH1 1 
ATOM   1046 N  NH2 . ARG A 1 143 ? -22.932 1.190   -6.295  1.00 22.61  ? 143 ARG A NH2 1 
ATOM   1047 N  N   . LEU A 1 144 ? -18.553 6.653   0.204   1.00 28.35  ? 144 LEU A N   1 
ATOM   1048 C  CA  . LEU A 1 144 ? -18.450 7.585   1.329   1.00 30.15  ? 144 LEU A CA  1 
ATOM   1049 C  C   . LEU A 1 144 ? -19.318 8.853   1.171   1.00 35.77  ? 144 LEU A C   1 
ATOM   1050 O  O   . LEU A 1 144 ? -19.843 9.393   2.158   1.00 36.99  ? 144 LEU A O   1 
ATOM   1051 C  CB  . LEU A 1 144 ? -16.976 7.975   1.558   1.00 29.64  ? 144 LEU A CB  1 
ATOM   1052 C  CG  . LEU A 1 144 ? -16.011 6.829   1.875   1.00 34.18  ? 144 LEU A CG  1 
ATOM   1053 C  CD1 . LEU A 1 144 ? -14.698 7.346   2.481   1.00 33.14  ? 144 LEU A CD1 1 
ATOM   1054 C  CD2 . LEU A 1 144 ? -16.686 5.791   2.807   1.00 25.31  ? 144 LEU A CD2 1 
ATOM   1055 N  N   . ALA A 1 145 ? -19.435 9.328   -0.070  1.00 34.47  ? 145 ALA A N   1 
ATOM   1056 C  CA  . ALA A 1 145 ? -20.224 10.500  -0.397  1.00 34.77  ? 145 ALA A CA  1 
ATOM   1057 C  C   . ALA A 1 145 ? -20.405 10.593  -1.906  1.00 35.65  ? 145 ALA A C   1 
ATOM   1058 O  O   . ALA A 1 145 ? -19.540 10.143  -2.670  1.00 38.56  ? 145 ALA A O   1 
ATOM   1059 C  CB  . ALA A 1 145 ? -19.552 11.748  0.113   1.00 40.60  ? 145 ALA A CB  1 
ATOM   1060 N  N   . CYS A 1 146 ? -21.518 11.199  -2.323  1.00 26.59  ? 146 CYS A N   1 
ATOM   1061 C  CA  . CYS A 1 146 ? -21.930 11.216  -3.710  1.00 26.16  ? 146 CYS A CA  1 
ATOM   1062 C  C   . CYS A 1 146 ? -22.758 12.472  -3.984  1.00 31.31  ? 146 CYS A C   1 
ATOM   1063 O  O   . CYS A 1 146 ? -23.165 13.158  -3.052  1.00 28.52  ? 146 CYS A O   1 
ATOM   1064 C  CB  . CYS A 1 146 ? -22.775 9.971   -4.019  1.00 28.23  ? 146 CYS A CB  1 
ATOM   1065 S  SG  . CYS A 1 146 ? -24.274 9.783   -3.000  1.00 47.28  ? 146 CYS A SG  1 
ATOM   1066 N  N   . GLY A 1 147 ? -23.001 12.773  -5.258  1.00 29.28  ? 147 GLY A N   1 
ATOM   1067 C  CA  . GLY A 1 147 ? -23.908 13.845  -5.621  1.00 26.19  ? 147 GLY A CA  1 
ATOM   1068 C  C   . GLY A 1 147 ? -24.317 13.748  -7.073  1.00 35.88  ? 147 GLY A C   1 
ATOM   1069 O  O   . GLY A 1 147 ? -23.659 13.103  -7.881  1.00 36.62  ? 147 GLY A O   1 
ATOM   1070 N  N   . VAL A 1 148 ? -25.420 14.387  -7.417  1.00 37.29  ? 148 VAL A N   1 
ATOM   1071 C  CA  . VAL A 1 148 ? -25.843 14.425  -8.807  1.00 39.31  ? 148 VAL A CA  1 
ATOM   1072 C  C   . VAL A 1 148 ? -25.113 15.534  -9.605  1.00 40.37  ? 148 VAL A C   1 
ATOM   1073 O  O   . VAL A 1 148 ? -25.021 16.698  -9.178  1.00 32.51  ? 148 VAL A O   1 
ATOM   1074 C  CB  . VAL A 1 148 ? -27.359 14.551  -8.922  1.00 37.33  ? 148 VAL A CB  1 
ATOM   1075 C  CG1 . VAL A 1 148 ? -27.795 14.335  -10.363 1.00 37.55  ? 148 VAL A CG1 1 
ATOM   1076 C  CG2 . VAL A 1 148 ? -28.028 13.534  -8.004  1.00 29.04  ? 148 VAL A CG2 1 
ATOM   1077 N  N   . ILE A 1 149 ? -24.572 15.141  -10.754 1.00 41.65  ? 149 ILE A N   1 
ATOM   1078 C  CA  . ILE A 1 149 ? -23.798 16.046  -11.583 1.00 44.41  ? 149 ILE A CA  1 
ATOM   1079 C  C   . ILE A 1 149 ? -24.747 16.946  -12.362 1.00 45.41  ? 149 ILE A C   1 
ATOM   1080 O  O   . ILE A 1 149 ? -25.428 16.507  -13.293 1.00 41.86  ? 149 ILE A O   1 
ATOM   1081 C  CB  . ILE A 1 149 ? -22.855 15.294  -12.560 1.00 47.16  ? 149 ILE A CB  1 
ATOM   1082 C  CG1 . ILE A 1 149 ? -22.071 14.190  -11.838 1.00 43.51  ? 149 ILE A CG1 1 
ATOM   1083 C  CG2 . ILE A 1 149 ? -21.908 16.280  -13.248 1.00 46.36  ? 149 ILE A CG2 1 
ATOM   1084 C  CD1 . ILE A 1 149 ? -21.222 13.332  -12.780 1.00 41.83  ? 149 ILE A CD1 1 
ATOM   1085 N  N   . GLY A 1 150 ? -24.779 18.211  -11.959 1.00 49.23  ? 150 GLY A N   1 
ATOM   1086 C  CA  . GLY A 1 150 ? -25.711 19.187  -12.497 1.00 51.20  ? 150 GLY A CA  1 
ATOM   1087 C  C   . GLY A 1 150 ? -25.071 20.340  -13.241 1.00 51.99  ? 150 GLY A C   1 
ATOM   1088 O  O   . GLY A 1 150 ? -23.871 20.603  -13.128 1.00 48.13  ? 150 GLY A O   1 
ATOM   1089 N  N   . ILE A 1 151 ? -25.895 21.031  -14.016 1.00 58.67  ? 151 ILE A N   1 
ATOM   1090 C  CA  . ILE A 1 151 ? -25.438 22.134  -14.847 1.00 59.77  ? 151 ILE A CA  1 
ATOM   1091 C  C   . ILE A 1 151 ? -24.952 23.304  -13.991 1.00 60.19  ? 151 ILE A C   1 
ATOM   1092 O  O   . ILE A 1 151 ? -25.544 23.623  -12.952 1.00 60.76  ? 151 ILE A O   1 
ATOM   1093 C  CB  . ILE A 1 151 ? -26.550 22.584  -15.821 1.00 59.72  ? 151 ILE A CB  1 
ATOM   1094 C  CG1 . ILE A 1 151 ? -26.965 21.413  -16.727 1.00 61.33  ? 151 ILE A CG1 1 
ATOM   1095 C  CG2 . ILE A 1 151 ? -26.100 23.767  -16.654 1.00 58.08  ? 151 ILE A CG2 1 
ATOM   1096 C  CD1 . ILE A 1 151 ? -27.417 21.839  -18.121 1.00 62.98  ? 151 ILE A CD1 1 
ATOM   1097 N  N   . ALA A 1 152 ? -23.848 23.912  -14.421 1.00 59.50  ? 152 ALA A N   1 
ATOM   1098 C  CA  . ALA A 1 152 ? -23.341 25.136  -13.809 1.00 60.74  ? 152 ALA A CA  1 
ATOM   1099 C  C   . ALA A 1 152 ? -23.259 26.256  -14.866 1.00 59.72  ? 152 ALA A C   1 
ATOM   1100 O  O   . ALA A 1 152 ? -23.208 25.972  -16.063 1.00 55.44  ? 152 ALA A O   1 
ATOM   1101 C  CB  . ALA A 1 152 ? -21.978 24.877  -13.159 1.00 59.83  ? 152 ALA A CB  1 
ATOM   1102 N  N   . GLN A 1 153 ? -23.249 27.509  -14.406 1.00 65.97  ? 153 GLN A N   1 
ATOM   1103 C  CA  . GLN A 1 153 ? -23.284 28.735  -15.250 1.00 75.04  ? 153 GLN A CA  1 
ATOM   1104 C  C   . GLN A 1 153 ? -23.283 28.603  -16.790 1.00 81.06  ? 153 GLN A C   1 
ATOM   1105 O  O   . GLN A 1 153 ? -22.754 29.490  -17.479 1.00 82.91  ? 153 GLN A O   1 
ATOM   1106 C  CB  . GLN A 1 153 ? -22.173 29.717  -14.842 1.00 74.19  ? 153 GLN A CB  1 
ATOM   1107 C  CG  . GLN A 1 153 ? -22.170 30.107  -13.372 1.00 73.33  ? 153 GLN A CG  1 
ATOM   1108 C  CD  . GLN A 1 153 ? -23.431 30.839  -12.926 1.00 73.14  ? 153 GLN A CD  1 
ATOM   1109 O  OE1 . GLN A 1 153 ? -24.032 30.488  -11.908 1.00 75.34  ? 153 GLN A OE1 1 
ATOM   1110 N  NE2 . GLN A 1 153 ? -23.823 31.868  -13.669 1.00 72.42  ? 153 GLN A NE2 1 
ATOM   1111 O  OXT . GLN A 1 153 ? -23.796 27.656  -17.399 1.00 80.26  ? 153 GLN A OXT 1 
ATOM   1112 N  N   . ALA B 1 1   ? -33.212 8.782   -21.427 1.00 87.14  ? 1   ALA B N   1 
ATOM   1113 C  CA  . ALA B 1 1   ? -33.800 10.021  -20.920 1.00 86.04  ? 1   ALA B CA  1 
ATOM   1114 C  C   . ALA B 1 1   ? -35.321 9.921   -20.767 1.00 83.53  ? 1   ALA B C   1 
ATOM   1115 O  O   . ALA B 1 1   ? -36.038 10.898  -20.981 1.00 84.55  ? 1   ALA B O   1 
ATOM   1116 C  CB  . ALA B 1 1   ? -33.425 11.203  -21.813 1.00 85.39  ? 1   ALA B CB  1 
ATOM   1117 N  N   . THR B 1 2   ? -35.802 8.741   -20.383 1.00 79.77  ? 2   THR B N   1 
ATOM   1118 C  CA  . THR B 1 2   ? -37.234 8.517   -20.188 1.00 76.27  ? 2   THR B CA  1 
ATOM   1119 C  C   . THR B 1 2   ? -37.682 8.667   -18.730 1.00 74.41  ? 2   THR B C   1 
ATOM   1120 O  O   . THR B 1 2   ? -38.789 9.131   -18.459 1.00 75.75  ? 2   THR B O   1 
ATOM   1121 C  CB  . THR B 1 2   ? -37.670 7.139   -20.724 1.00 72.23  ? 2   THR B CB  1 
ATOM   1122 O  OG1 . THR B 1 2   ? -38.334 7.306   -21.986 1.00 71.30  ? 2   THR B OG1 1 
ATOM   1123 C  CG2 . THR B 1 2   ? -38.619 6.462   -19.736 1.00 69.99  ? 2   THR B CG2 1 
ATOM   1124 N  N   . LYS B 1 3   ? -36.828 8.275   -17.791 1.00 70.17  ? 3   LYS B N   1 
ATOM   1125 C  CA  . LYS B 1 3   ? -37.178 8.394   -16.382 1.00 65.61  ? 3   LYS B CA  1 
ATOM   1126 C  C   . LYS B 1 3   ? -36.215 9.313   -15.645 1.00 62.20  ? 3   LYS B C   1 
ATOM   1127 O  O   . LYS B 1 3   ? -35.015 9.343   -15.928 1.00 61.45  ? 3   LYS B O   1 
ATOM   1128 C  CB  . LYS B 1 3   ? -37.209 7.024   -15.709 1.00 64.87  ? 3   LYS B CB  1 
ATOM   1129 C  CG  . LYS B 1 3   ? -38.197 6.042   -16.317 1.00 65.99  ? 3   LYS B CG  1 
ATOM   1130 C  CD  . LYS B 1 3   ? -38.297 4.784   -15.466 1.00 66.63  ? 3   LYS B CD  1 
ATOM   1131 C  CE  . LYS B 1 3   ? -38.904 3.614   -16.247 1.00 67.46  ? 3   LYS B CE  1 
ATOM   1132 N  NZ  . LYS B 1 3   ? -38.337 2.281   -15.812 1.00 66.06  ? 3   LYS B NZ  1 
ATOM   1133 N  N   . ALA B 1 4   ? -36.747 10.073  -14.699 1.00 59.27  ? 4   ALA B N   1 
ATOM   1134 C  CA  . ALA B 1 4   ? -35.900 10.892  -13.850 1.00 58.86  ? 4   ALA B CA  1 
ATOM   1135 C  C   . ALA B 1 4   ? -36.482 10.947  -12.454 1.00 54.51  ? 4   ALA B C   1 
ATOM   1136 O  O   . ALA B 1 4   ? -37.571 10.442  -12.216 1.00 57.87  ? 4   ALA B O   1 
ATOM   1137 C  CB  . ALA B 1 4   ? -35.748 12.278  -14.424 1.00 59.80  ? 4   ALA B CB  1 
ATOM   1138 N  N   . VAL B 1 5   ? -35.736 11.542  -11.532 1.00 47.63  ? 5   VAL B N   1 
ATOM   1139 C  CA  . VAL B 1 5   ? -36.185 11.692  -10.155 1.00 47.43  ? 5   VAL B CA  1 
ATOM   1140 C  C   . VAL B 1 5   ? -35.309 12.723  -9.458  1.00 48.86  ? 5   VAL B C   1 
ATOM   1141 O  O   . VAL B 1 5   ? -34.208 13.016  -9.911  1.00 54.84  ? 5   VAL B O   1 
ATOM   1142 C  CB  . VAL B 1 5   ? -36.167 10.345  -9.384  1.00 44.54  ? 5   VAL B CB  1 
ATOM   1143 C  CG1 . VAL B 1 5   ? -34.788 9.689   -9.455  1.00 44.82  ? 5   VAL B CG1 1 
ATOM   1144 C  CG2 . VAL B 1 5   ? -36.571 10.547  -7.941  1.00 43.48  ? 5   VAL B CG2 1 
ATOM   1145 N  N   . CYS B 1 6   ? -35.797 13.269  -8.355  1.00 45.43  ? 6   CYS B N   1 
ATOM   1146 C  CA  . CYS B 1 6   ? -35.096 14.312  -7.646  1.00 37.99  ? 6   CYS B CA  1 
ATOM   1147 C  C   . CYS B 1 6   ? -35.392 14.153  -6.178  1.00 40.61  ? 6   CYS B C   1 
ATOM   1148 O  O   . CYS B 1 6   ? -36.542 14.006  -5.804  1.00 45.00  ? 6   CYS B O   1 
ATOM   1149 C  CB  . CYS B 1 6   ? -35.602 15.678  -8.143  1.00 48.84  ? 6   CYS B CB  1 
ATOM   1150 S  SG  . CYS B 1 6   ? -35.049 17.144  -7.202  1.00 52.27  ? 6   CYS B SG  1 
ATOM   1151 N  N   . VAL B 1 7   ? -34.370 14.166  -5.336  1.00 41.95  ? 7   VAL B N   1 
ATOM   1152 C  CA  . VAL B 1 7   ? -34.599 14.162  -3.899  1.00 43.60  ? 7   VAL B CA  1 
ATOM   1153 C  C   . VAL B 1 7   ? -34.584 15.590  -3.416  1.00 51.81  ? 7   VAL B C   1 
ATOM   1154 O  O   . VAL B 1 7   ? -33.524 16.178  -3.216  1.00 55.63  ? 7   VAL B O   1 
ATOM   1155 C  CB  . VAL B 1 7   ? -33.522 13.387  -3.121  1.00 44.11  ? 7   VAL B CB  1 
ATOM   1156 C  CG1 . VAL B 1 7   ? -33.690 13.597  -1.612  1.00 36.41  ? 7   VAL B CG1 1 
ATOM   1157 C  CG2 . VAL B 1 7   ? -33.557 11.908  -3.477  1.00 42.44  ? 7   VAL B CG2 1 
ATOM   1158 N  N   . LEU B 1 8   ? -35.765 16.166  -3.251  1.00 57.88  ? 8   LEU B N   1 
ATOM   1159 C  CA  . LEU B 1 8   ? -35.849 17.502  -2.699  1.00 61.28  ? 8   LEU B CA  1 
ATOM   1160 C  C   . LEU B 1 8   ? -35.392 17.422  -1.260  1.00 63.26  ? 8   LEU B C   1 
ATOM   1161 O  O   . LEU B 1 8   ? -36.034 16.777  -0.433  1.00 66.02  ? 8   LEU B O   1 
ATOM   1162 C  CB  . LEU B 1 8   ? -37.271 18.049  -2.783  1.00 61.80  ? 8   LEU B CB  1 
ATOM   1163 C  CG  . LEU B 1 8   ? -37.769 18.317  -4.202  1.00 64.36  ? 8   LEU B CG  1 
ATOM   1164 C  CD1 . LEU B 1 8   ? -39.138 18.944  -4.157  1.00 66.26  ? 8   LEU B CD1 1 
ATOM   1165 C  CD2 . LEU B 1 8   ? -36.804 19.216  -4.952  1.00 67.04  ? 8   LEU B CD2 1 
ATOM   1166 N  N   . LYS B 1 9   ? -34.261 18.053  -0.975  1.00 62.75  ? 9   LYS B N   1 
ATOM   1167 C  CA  . LYS B 1 9   ? -33.764 18.141  0.385   1.00 63.85  ? 9   LYS B CA  1 
ATOM   1168 C  C   . LYS B 1 9   ? -33.568 19.607  0.730   1.00 70.59  ? 9   LYS B C   1 
ATOM   1169 O  O   . LYS B 1 9   ? -33.274 20.432  -0.137  1.00 71.25  ? 9   LYS B O   1 
ATOM   1170 C  CB  . LYS B 1 9   ? -32.453 17.365  0.538   1.00 63.28  ? 9   LYS B CB  1 
ATOM   1171 C  CG  . LYS B 1 9   ? -32.514 16.239  1.558   1.00 62.10  ? 9   LYS B CG  1 
ATOM   1172 C  CD  . LYS B 1 9   ? -31.261 15.386  1.535   0.00 60.40  ? 9   LYS B CD  1 
ATOM   1173 C  CE  . LYS B 1 9   ? -31.280 14.372  2.667   0.00 58.89  ? 9   LYS B CE  1 
ATOM   1174 N  NZ  . LYS B 1 9   ? -32.534 13.566  2.677   0.00 58.06  ? 9   LYS B NZ  1 
ATOM   1175 N  N   . GLY B 1 10  ? -33.753 19.934  2.000   1.00 75.69  ? 10  GLY B N   1 
ATOM   1176 C  CA  . GLY B 1 10  ? -33.562 21.294  2.457   1.00 80.93  ? 10  GLY B CA  1 
ATOM   1177 C  C   . GLY B 1 10  ? -33.018 21.285  3.868   1.00 86.18  ? 10  GLY B C   1 
ATOM   1178 O  O   . GLY B 1 10  ? -33.258 20.341  4.624   1.00 87.86  ? 10  GLY B O   1 
ATOM   1179 N  N   . ASP B 1 11  ? -32.291 22.340  4.223   1.00 87.41  ? 11  ASP B N   1 
ATOM   1180 C  CA  . ASP B 1 11  ? -31.691 22.469  5.547   1.00 88.39  ? 11  ASP B CA  1 
ATOM   1181 C  C   . ASP B 1 11  ? -32.710 22.733  6.663   1.00 88.37  ? 11  ASP B C   1 
ATOM   1182 O  O   . ASP B 1 11  ? -32.345 23.173  7.754   1.00 90.05  ? 11  ASP B O   1 
ATOM   1183 C  CB  . ASP B 1 11  ? -30.640 23.578  5.520   1.00 89.94  ? 11  ASP B CB  1 
ATOM   1184 C  CG  . ASP B 1 11  ? -30.992 24.683  4.538   1.00 90.38  ? 11  ASP B CG  1 
ATOM   1185 O  OD1 . ASP B 1 11  ? -32.199 24.991  4.389   1.00 87.88  ? 11  ASP B OD1 1 
ATOM   1186 O  OD2 . ASP B 1 11  ? -30.062 25.231  3.906   1.00 91.75  ? 11  ASP B OD2 1 
ATOM   1187 N  N   . GLY B 1 12  ? -33.984 22.461  6.387   1.00 85.45  ? 12  GLY B N   1 
ATOM   1188 C  CA  . GLY B 1 12  ? -35.035 22.593  7.381   1.00 81.00  ? 12  GLY B CA  1 
ATOM   1189 C  C   . GLY B 1 12  ? -35.790 21.297  7.607   1.00 75.20  ? 12  GLY B C   1 
ATOM   1190 O  O   . GLY B 1 12  ? -35.183 20.238  7.700   1.00 74.53  ? 12  GLY B O   1 
ATOM   1191 N  N   . PRO B 1 13  ? -37.121 21.378  7.716   1.00 74.41  ? 13  PRO B N   1 
ATOM   1192 C  CA  . PRO B 1 13  ? -37.981 20.206  7.893   1.00 73.56  ? 13  PRO B CA  1 
ATOM   1193 C  C   . PRO B 1 13  ? -38.592 19.720  6.576   1.00 73.24  ? 13  PRO B C   1 
ATOM   1194 O  O   . PRO B 1 13  ? -39.104 18.595  6.510   1.00 74.31  ? 13  PRO B O   1 
ATOM   1195 C  CB  . PRO B 1 13  ? -39.088 20.749  8.790   1.00 74.23  ? 13  PRO B CB  1 
ATOM   1196 C  CG  . PRO B 1 13  ? -39.244 22.160  8.332   1.00 75.09  ? 13  PRO B CG  1 
ATOM   1197 C  CD  . PRO B 1 13  ? -37.864 22.634  7.927   1.00 75.30  ? 13  PRO B CD  1 
ATOM   1198 N  N   . VAL B 1 14  ? -38.535 20.561  5.545   1.00 70.40  ? 14  VAL B N   1 
ATOM   1199 C  CA  . VAL B 1 14  ? -39.183 20.285  4.265   1.00 67.65  ? 14  VAL B CA  1 
ATOM   1200 C  C   . VAL B 1 14  ? -38.375 19.333  3.398   1.00 69.49  ? 14  VAL B C   1 
ATOM   1201 O  O   . VAL B 1 14  ? -37.204 19.590  3.126   1.00 72.33  ? 14  VAL B O   1 
ATOM   1202 C  CB  . VAL B 1 14  ? -39.383 21.578  3.471   1.00 66.73  ? 14  VAL B CB  1 
ATOM   1203 C  CG1 . VAL B 1 14  ? -40.052 21.279  2.133   1.00 65.71  ? 14  VAL B CG1 1 
ATOM   1204 C  CG2 . VAL B 1 14  ? -40.193 22.576  4.280   1.00 66.82  ? 14  VAL B CG2 1 
ATOM   1205 N  N   . GLN B 1 15  ? -39.002 18.245  2.949   1.00 66.87  ? 15  GLN B N   1 
ATOM   1206 C  CA  . GLN B 1 15  ? -38.288 17.222  2.184   1.00 61.37  ? 15  GLN B CA  1 
ATOM   1207 C  C   . GLN B 1 15  ? -39.233 16.253  1.481   1.00 59.56  ? 15  GLN B C   1 
ATOM   1208 O  O   . GLN B 1 15  ? -40.328 15.964  1.979   1.00 59.99  ? 15  GLN B O   1 
ATOM   1209 C  CB  . GLN B 1 15  ? -37.392 16.423  3.114   1.00 57.31  ? 15  GLN B CB  1 
ATOM   1210 C  CG  . GLN B 1 15  ? -38.179 15.473  3.999   1.00 58.12  ? 15  GLN B CG  1 
ATOM   1211 C  CD  . GLN B 1 15  ? -37.331 14.849  5.083   1.00 60.89  ? 15  GLN B CD  1 
ATOM   1212 O  OE1 . GLN B 1 15  ? -36.941 13.681  4.993   1.00 59.52  ? 15  GLN B OE1 1 
ATOM   1213 N  NE2 . GLN B 1 15  ? -37.028 15.630  6.117   1.00 62.87  ? 15  GLN B NE2 1 
ATOM   1214 N  N   . GLY B 1 16  ? -38.797 15.732  0.336   1.00 57.53  ? 16  GLY B N   1 
ATOM   1215 C  CA  . GLY B 1 16  ? -39.591 14.760  -0.397  1.00 60.04  ? 16  GLY B CA  1 
ATOM   1216 C  C   . GLY B 1 16  ? -38.976 14.318  -1.710  1.00 60.24  ? 16  GLY B C   1 
ATOM   1217 O  O   . GLY B 1 16  ? -38.024 14.938  -2.185  1.00 62.94  ? 16  GLY B O   1 
ATOM   1218 N  N   . ILE B 1 17  ? -39.523 13.252  -2.295  1.00 54.63  ? 17  ILE B N   1 
ATOM   1219 C  CA  . ILE B 1 17  ? -39.034 12.722  -3.569  1.00 51.34  ? 17  ILE B CA  1 
ATOM   1220 C  C   . ILE B 1 17  ? -40.027 12.999  -4.690  1.00 46.72  ? 17  ILE B C   1 
ATOM   1221 O  O   . ILE B 1 17  ? -41.237 12.947  -4.486  1.00 45.43  ? 17  ILE B O   1 
ATOM   1222 C  CB  . ILE B 1 17  ? -38.752 11.191  -3.497  1.00 53.75  ? 17  ILE B CB  1 
ATOM   1223 C  CG1 . ILE B 1 17  ? -37.722 10.874  -2.420  1.00 53.59  ? 17  ILE B CG1 1 
ATOM   1224 C  CG2 . ILE B 1 17  ? -38.266 10.663  -4.833  1.00 53.32  ? 17  ILE B CG2 1 
ATOM   1225 C  CD1 . ILE B 1 17  ? -38.231 11.053  -1.001  1.00 56.63  ? 17  ILE B CD1 1 
ATOM   1226 N  N   . ILE B 1 18  ? -39.516 13.287  -5.876  1.00 37.49  ? 18  ILE B N   1 
ATOM   1227 C  CA  . ILE B 1 18  ? -40.369 13.633  -7.007  1.00 39.33  ? 18  ILE B CA  1 
ATOM   1228 C  C   . ILE B 1 18  ? -39.929 12.839  -8.226  1.00 39.69  ? 18  ILE B C   1 
ATOM   1229 O  O   . ILE B 1 18  ? -38.746 12.767  -8.512  1.00 41.28  ? 18  ILE B O   1 
ATOM   1230 C  CB  . ILE B 1 18  ? -40.291 15.166  -7.341  1.00 45.07  ? 18  ILE B CB  1 
ATOM   1231 C  CG1 . ILE B 1 18  ? -40.655 16.034  -6.127  1.00 44.28  ? 18  ILE B CG1 1 
ATOM   1232 C  CG2 . ILE B 1 18  ? -41.174 15.520  -8.536  1.00 43.91  ? 18  ILE B CG2 1 
ATOM   1233 C  CD1 . ILE B 1 18  ? -42.129 15.949  -5.712  1.00 44.42  ? 18  ILE B CD1 1 
ATOM   1234 N  N   . ASN B 1 19  ? -40.870 12.260  -8.962  1.00 37.70  ? 19  ASN B N   1 
ATOM   1235 C  CA  . ASN B 1 19  ? -40.504 11.477  -10.137 1.00 42.67  ? 19  ASN B CA  1 
ATOM   1236 C  C   . ASN B 1 19  ? -40.887 12.133  -11.458 1.00 44.78  ? 19  ASN B C   1 
ATOM   1237 O  O   . ASN B 1 19  ? -41.703 13.049  -11.482 1.00 39.04  ? 19  ASN B O   1 
ATOM   1238 C  CB  . ASN B 1 19  ? -41.094 10.071  -10.035 1.00 43.69  ? 19  ASN B CB  1 
ATOM   1239 C  CG  . ASN B 1 19  ? -40.561 9.314   -8.839  1.00 45.66  ? 19  ASN B CG  1 
ATOM   1240 O  OD1 . ASN B 1 19  ? -39.398 8.891   -8.827  1.00 48.53  ? 19  ASN B OD1 1 
ATOM   1241 N  ND2 . ASN B 1 19  ? -41.403 9.134   -7.827  1.00 41.05  ? 19  ASN B ND2 1 
ATOM   1242 N  N   . PHE B 1 20  ? -40.280 11.664  -12.548 1.00 46.18  ? 20  PHE B N   1 
ATOM   1243 C  CA  . PHE B 1 20  ? -40.552 12.192  -13.887 1.00 51.29  ? 20  PHE B CA  1 
ATOM   1244 C  C   . PHE B 1 20  ? -40.555 11.068  -14.916 1.00 58.05  ? 20  PHE B C   1 
ATOM   1245 O  O   . PHE B 1 20  ? -39.594 10.313  -15.007 1.00 63.21  ? 20  PHE B O   1 
ATOM   1246 C  CB  . PHE B 1 20  ? -39.490 13.212  -14.327 1.00 49.23  ? 20  PHE B CB  1 
ATOM   1247 C  CG  . PHE B 1 20  ? -39.236 14.309  -13.340 1.00 50.32  ? 20  PHE B CG  1 
ATOM   1248 C  CD1 . PHE B 1 20  ? -38.515 14.065  -12.178 1.00 50.66  ? 20  PHE B CD1 1 
ATOM   1249 C  CD2 . PHE B 1 20  ? -39.681 15.598  -13.587 1.00 53.94  ? 20  PHE B CD2 1 
ATOM   1250 C  CE1 . PHE B 1 20  ? -38.267 15.081  -11.262 1.00 50.91  ? 20  PHE B CE1 1 
ATOM   1251 C  CE2 . PHE B 1 20  ? -39.436 16.624  -12.678 1.00 55.40  ? 20  PHE B CE2 1 
ATOM   1252 C  CZ  . PHE B 1 20  ? -38.723 16.363  -11.511 1.00 53.31  ? 20  PHE B CZ  1 
ATOM   1253 N  N   . GLU B 1 21  ? -41.619 10.976  -15.706 1.00 61.01  ? 21  GLU B N   1 
ATOM   1254 C  CA  . GLU B 1 21  ? -41.661 10.042  -16.825 1.00 64.23  ? 21  GLU B CA  1 
ATOM   1255 C  C   . GLU B 1 21  ? -41.913 10.773  -18.139 1.00 63.79  ? 21  GLU B C   1 
ATOM   1256 O  O   . GLU B 1 21  ? -42.683 11.736  -18.193 1.00 64.16  ? 21  GLU B O   1 
ATOM   1257 C  CB  . GLU B 1 21  ? -42.737 8.975   -16.620 1.00 70.07  ? 21  GLU B CB  1 
ATOM   1258 C  CG  . GLU B 1 21  ? -42.369 7.855   -15.665 1.00 74.97  ? 21  GLU B CG  1 
ATOM   1259 C  CD  . GLU B 1 21  ? -43.141 6.569   -15.962 1.00 82.04  ? 21  GLU B CD  1 
ATOM   1260 O  OE1 . GLU B 1 21  ? -44.258 6.394   -15.420 1.00 83.31  ? 21  GLU B OE1 1 
ATOM   1261 O  OE2 . GLU B 1 21  ? -42.630 5.734   -16.746 1.00 84.05  ? 21  GLU B OE2 1 
ATOM   1262 N  N   . GLN B 1 22  ? -41.257 10.300  -19.194 1.00 70.27  ? 22  GLN B N   1 
ATOM   1263 C  CA  . GLN B 1 22  ? -41.414 10.852  -20.534 1.00 74.08  ? 22  GLN B CA  1 
ATOM   1264 C  C   . GLN B 1 22  ? -41.350 9.740   -21.580 1.00 78.93  ? 22  GLN B C   1 
ATOM   1265 O  O   . GLN B 1 22  ? -40.563 8.802   -21.445 1.00 81.94  ? 22  GLN B O   1 
ATOM   1266 C  CB  . GLN B 1 22  ? -40.332 11.896  -20.815 0.00 72.59  ? 22  GLN B CB  1 
ATOM   1267 C  CG  . GLN B 1 22  ? -40.492 12.599  -22.152 1.00 72.47  ? 22  GLN B CG  1 
ATOM   1268 C  CD  . GLN B 1 22  ? -39.368 13.579  -22.448 1.00 71.81  ? 22  GLN B CD  1 
ATOM   1269 O  OE1 . GLN B 1 22  ? -39.617 14.751  -22.754 1.00 74.69  ? 22  GLN B OE1 1 
ATOM   1270 N  NE2 . GLN B 1 22  ? -38.125 13.103  -22.373 1.00 66.46  ? 22  GLN B NE2 1 
ATOM   1271 N  N   . LYS B 1 23  ? -42.175 9.848   -22.621 1.00 81.21  ? 23  LYS B N   1 
ATOM   1272 C  CA  . LYS B 1 23  ? -42.208 8.847   -23.692 1.00 79.64  ? 23  LYS B CA  1 
ATOM   1273 C  C   . LYS B 1 23  ? -42.469 9.492   -25.063 1.00 76.69  ? 23  LYS B C   1 
ATOM   1274 O  O   . LYS B 1 23  ? -42.014 10.610  -25.344 1.00 72.04  ? 23  LYS B O   1 
ATOM   1275 C  CB  . LYS B 1 23  ? -43.266 7.780   -23.382 1.00 78.98  ? 23  LYS B CB  1 
ATOM   1276 C  CG  . LYS B 1 23  ? -42.989 6.395   -23.961 1.00 79.43  ? 23  LYS B CG  1 
ATOM   1277 C  CD  . LYS B 1 23  ? -44.099 5.408   -23.589 1.00 78.74  ? 23  LYS B CD  1 
ATOM   1278 C  CE  . LYS B 1 23  ? -43.777 3.993   -24.037 0.00 79.47  ? 23  LYS B CE  1 
ATOM   1279 N  NZ  . LYS B 1 23  ? -44.836 3.034   -23.617 0.00 79.67  ? 23  LYS B NZ  1 
ATOM   1280 N  N   . ASN B 1 26  ? -40.750 13.477  -28.239 1.00 81.97  ? 26  ASN B N   1 
ATOM   1281 C  CA  . ASN B 1 26  ? -40.745 14.717  -27.466 1.00 82.63  ? 26  ASN B CA  1 
ATOM   1282 C  C   . ASN B 1 26  ? -42.110 15.065  -26.875 1.00 79.43  ? 26  ASN B C   1 
ATOM   1283 O  O   . ASN B 1 26  ? -42.649 16.149  -27.113 1.00 75.03  ? 26  ASN B O   1 
ATOM   1284 C  CB  . ASN B 1 26  ? -40.183 15.891  -28.282 1.00 85.82  ? 26  ASN B CB  1 
ATOM   1285 C  CG  . ASN B 1 26  ? -40.580 15.837  -29.756 1.00 89.76  ? 26  ASN B CG  1 
ATOM   1286 O  OD1 . ASN B 1 26  ? -39.898 15.208  -30.570 1.00 91.73  ? 26  ASN B OD1 1 
ATOM   1287 N  ND2 . ASN B 1 26  ? -41.677 16.510  -30.106 1.00 90.03  ? 26  ASN B ND2 1 
ATOM   1288 N  N   . GLY B 1 27  ? -42.650 14.135  -26.089 1.00 80.97  ? 27  GLY B N   1 
ATOM   1289 C  CA  . GLY B 1 27  ? -43.979 14.271  -25.509 1.00 80.34  ? 27  GLY B CA  1 
ATOM   1290 C  C   . GLY B 1 27  ? -43.995 14.996  -24.177 1.00 78.27  ? 27  GLY B C   1 
ATOM   1291 O  O   . GLY B 1 27  ? -43.081 15.767  -23.883 1.00 79.35  ? 27  GLY B O   1 
ATOM   1292 N  N   . PRO B 1 28  ? -45.041 14.759  -23.370 1.00 76.42  ? 28  PRO B N   1 
ATOM   1293 C  CA  . PRO B 1 28  ? -45.260 15.435  -22.086 1.00 74.51  ? 28  PRO B CA  1 
ATOM   1294 C  C   . PRO B 1 28  ? -44.534 14.735  -20.949 1.00 73.43  ? 28  PRO B C   1 
ATOM   1295 O  O   . PRO B 1 28  ? -44.069 13.611  -21.125 1.00 74.70  ? 28  PRO B O   1 
ATOM   1296 C  CB  . PRO B 1 28  ? -46.765 15.297  -21.887 1.00 73.59  ? 28  PRO B CB  1 
ATOM   1297 C  CG  . PRO B 1 28  ? -47.080 13.984  -22.514 0.00 75.09  ? 28  PRO B CG  1 
ATOM   1298 C  CD  . PRO B 1 28  ? -46.153 13.851  -23.704 0.00 76.55  ? 28  PRO B CD  1 
ATOM   1299 N  N   . VAL B 1 29  ? -44.454 15.391  -19.796 1.00 72.41  ? 29  VAL B N   1 
ATOM   1300 C  CA  . VAL B 1 29  ? -43.756 14.834  -18.640 1.00 71.29  ? 29  VAL B CA  1 
ATOM   1301 C  C   . VAL B 1 29  ? -44.715 14.705  -17.477 1.00 64.78  ? 29  VAL B C   1 
ATOM   1302 O  O   . VAL B 1 29  ? -45.396 15.666  -17.139 1.00 64.24  ? 29  VAL B O   1 
ATOM   1303 C  CB  . VAL B 1 29  ? -42.555 15.723  -18.204 1.00 63.75  ? 29  VAL B CB  1 
ATOM   1304 C  CG1 . VAL B 1 29  ? -42.196 15.481  -16.730 1.00 60.51  ? 29  VAL B CG1 1 
ATOM   1305 C  CG2 . VAL B 1 29  ? -41.364 15.484  -19.101 1.00 63.54  ? 29  VAL B CG2 1 
ATOM   1306 N  N   . LYS B 1 30  ? -44.775 13.518  -16.880 1.00 59.30  ? 30  LYS B N   1 
ATOM   1307 C  CA  . LYS B 1 30  ? -45.545 13.328  -15.658 1.00 55.34  ? 30  LYS B CA  1 
ATOM   1308 C  C   . LYS B 1 30  ? -44.634 13.572  -14.468 1.00 54.32  ? 30  LYS B C   1 
ATOM   1309 O  O   . LYS B 1 30  ? -43.605 12.928  -14.316 1.00 56.02  ? 30  LYS B O   1 
ATOM   1310 C  CB  . LYS B 1 30  ? -46.156 11.929  -15.595 1.00 53.78  ? 30  LYS B CB  1 
ATOM   1311 N  N   . VAL B 1 31  ? -45.004 14.527  -13.634 1.00 53.50  ? 31  VAL B N   1 
ATOM   1312 C  CA  . VAL B 1 31  ? -44.228 14.821  -12.445 1.00 51.91  ? 31  VAL B CA  1 
ATOM   1313 C  C   . VAL B 1 31  ? -45.044 14.451  -11.205 1.00 50.31  ? 31  VAL B C   1 
ATOM   1314 O  O   . VAL B 1 31  ? -46.062 15.078  -10.911 1.00 49.49  ? 31  VAL B O   1 
ATOM   1315 C  CB  . VAL B 1 31  ? -43.841 16.305  -12.403 1.00 48.02  ? 31  VAL B CB  1 
ATOM   1316 C  CG1 . VAL B 1 31  ? -42.999 16.595  -11.187 1.00 43.19  ? 31  VAL B CG1 1 
ATOM   1317 C  CG2 . VAL B 1 31  ? -43.124 16.692  -13.678 1.00 40.28  ? 31  VAL B CG2 1 
ATOM   1318 N  N   . TRP B 1 32  ? -44.608 13.420  -10.491 1.00 48.80  ? 32  TRP B N   1 
ATOM   1319 C  CA  . TRP B 1 32  ? -45.340 12.975  -9.315  1.00 49.40  ? 32  TRP B CA  1 
ATOM   1320 C  C   . TRP B 1 32  ? -44.416 12.645  -8.151  1.00 47.98  ? 32  TRP B C   1 
ATOM   1321 O  O   . TRP B 1 32  ? -43.224 12.383  -8.337  1.00 49.36  ? 32  TRP B O   1 
ATOM   1322 C  CB  . TRP B 1 32  ? -46.237 11.776  -9.651  1.00 48.75  ? 32  TRP B CB  1 
ATOM   1323 C  CG  . TRP B 1 32  ? -45.527 10.477  -9.624  1.00 53.06  ? 32  TRP B CG  1 
ATOM   1324 C  CD1 . TRP B 1 32  ? -45.335 9.665   -8.539  1.00 54.85  ? 32  TRP B CD1 1 
ATOM   1325 C  CD2 . TRP B 1 32  ? -44.901 9.819   -10.732 1.00 60.65  ? 32  TRP B CD2 1 
ATOM   1326 N  NE1 . TRP B 1 32  ? -44.624 8.548   -8.903  1.00 56.30  ? 32  TRP B NE1 1 
ATOM   1327 C  CE2 . TRP B 1 32  ? -44.348 8.618   -10.244 1.00 60.78  ? 32  TRP B CE2 1 
ATOM   1328 C  CE3 . TRP B 1 32  ? -44.754 10.131  -12.088 1.00 64.73  ? 32  TRP B CE3 1 
ATOM   1329 C  CZ2 . TRP B 1 32  ? -43.659 7.729   -11.067 1.00 66.39  ? 32  TRP B CZ2 1 
ATOM   1330 C  CZ3 . TRP B 1 32  ? -44.071 9.250   -12.903 1.00 66.40  ? 32  TRP B CZ3 1 
ATOM   1331 C  CH2 . TRP B 1 32  ? -43.531 8.061   -12.391 1.00 68.48  ? 32  TRP B CH2 1 
ATOM   1332 N  N   . GLY B 1 33  ? -44.983 12.650  -6.951  1.00 40.68  ? 33  GLY B N   1 
ATOM   1333 C  CA  . GLY B 1 33  ? -44.244 12.316  -5.755  1.00 40.23  ? 33  GLY B CA  1 
ATOM   1334 C  C   . GLY B 1 33  ? -44.896 13.005  -4.592  1.00 43.36  ? 33  GLY B C   1 
ATOM   1335 O  O   . GLY B 1 33  ? -45.974 13.544  -4.741  1.00 46.59  ? 33  GLY B O   1 
ATOM   1336 N  N   . SER B 1 34  ? -44.247 13.013  -3.437  1.00 50.37  ? 34  SER B N   1 
ATOM   1337 C  CA  . SER B 1 34  ? -44.810 13.710  -2.287  1.00 53.21  ? 34  SER B CA  1 
ATOM   1338 C  C   . SER B 1 34  ? -43.778 14.630  -1.636  1.00 55.59  ? 34  SER B C   1 
ATOM   1339 O  O   . SER B 1 34  ? -42.583 14.488  -1.867  1.00 55.52  ? 34  SER B O   1 
ATOM   1340 C  CB  . SER B 1 34  ? -45.348 12.715  -1.264  1.00 49.77  ? 34  SER B CB  1 
ATOM   1341 O  OG  . SER B 1 34  ? -44.303 12.203  -0.462  1.00 49.20  ? 34  SER B OG  1 
ATOM   1342 N  N   . ILE B 1 35  ? -44.255 15.567  -0.818  1.00 56.20  ? 35  ILE B N   1 
ATOM   1343 C  CA  . ILE B 1 35  ? -43.399 16.493  -0.081  1.00 54.44  ? 35  ILE B CA  1 
ATOM   1344 C  C   . ILE B 1 35  ? -43.971 16.669  1.322   1.00 56.29  ? 35  ILE B C   1 
ATOM   1345 O  O   . ILE B 1 35  ? -45.177 16.700  1.491   1.00 62.03  ? 35  ILE B O   1 
ATOM   1346 C  CB  . ILE B 1 35  ? -43.351 17.864  -0.784  1.00 52.60  ? 35  ILE B CB  1 
ATOM   1347 C  CG1 . ILE B 1 35  ? -43.065 17.682  -2.276  1.00 53.14  ? 35  ILE B CG1 1 
ATOM   1348 C  CG2 . ILE B 1 35  ? -42.326 18.785  -0.127  1.00 52.40  ? 35  ILE B CG2 1 
ATOM   1349 C  CD1 . ILE B 1 35  ? -42.769 18.969  -3.002  1.00 54.13  ? 35  ILE B CD1 1 
ATOM   1350 N  N   . LYS B 1 36  ? -43.121 16.787  2.330   1.00 56.10  ? 36  LYS B N   1 
ATOM   1351 C  CA  . LYS B 1 36  ? -43.609 16.868  3.705   1.00 58.97  ? 36  LYS B CA  1 
ATOM   1352 C  C   . LYS B 1 36  ? -42.868 17.923  4.532   1.00 61.74  ? 36  LYS B C   1 
ATOM   1353 O  O   . LYS B 1 36  ? -41.775 18.360  4.164   1.00 64.61  ? 36  LYS B O   1 
ATOM   1354 C  CB  . LYS B 1 36  ? -43.514 15.498  4.377   1.00 58.85  ? 36  LYS B CB  1 
ATOM   1355 N  N   . GLY B 1 37  ? -43.466 18.318  5.653   1.00 60.93  ? 37  GLY B N   1 
ATOM   1356 C  CA  . GLY B 1 37  ? -42.909 19.359  6.502   1.00 61.26  ? 37  GLY B CA  1 
ATOM   1357 C  C   . GLY B 1 37  ? -43.335 20.758  6.075   1.00 63.97  ? 37  GLY B C   1 
ATOM   1358 O  O   . GLY B 1 37  ? -42.855 21.770  6.606   1.00 63.91  ? 37  GLY B O   1 
ATOM   1359 N  N   . LEU B 1 38  ? -44.244 20.820  5.107   1.00 63.01  ? 38  LEU B N   1 
ATOM   1360 C  CA  . LEU B 1 38  ? -44.687 22.100  4.564   1.00 63.81  ? 38  LEU B CA  1 
ATOM   1361 C  C   . LEU B 1 38  ? -45.692 22.794  5.480   1.00 66.27  ? 38  LEU B C   1 
ATOM   1362 O  O   . LEU B 1 38  ? -46.244 22.178  6.389   1.00 67.97  ? 38  LEU B O   1 
ATOM   1363 C  CB  . LEU B 1 38  ? -45.292 21.896  3.173   1.00 59.23  ? 38  LEU B CB  1 
ATOM   1364 C  CG  . LEU B 1 38  ? -44.273 21.478  2.116   1.00 55.80  ? 38  LEU B CG  1 
ATOM   1365 C  CD1 . LEU B 1 38  ? -44.933 21.211  0.776   1.00 54.98  ? 38  LEU B CD1 1 
ATOM   1366 C  CD2 . LEU B 1 38  ? -43.219 22.557  1.987   1.00 54.05  ? 38  LEU B CD2 1 
ATOM   1367 N  N   . THR B 1 39  ? -45.920 24.081  5.241   1.00 67.54  ? 39  THR B N   1 
ATOM   1368 C  CA  . THR B 1 39  ? -46.999 24.797  5.910   1.00 70.05  ? 39  THR B CA  1 
ATOM   1369 C  C   . THR B 1 39  ? -48.241 24.746  5.027   1.00 72.58  ? 39  THR B C   1 
ATOM   1370 O  O   . THR B 1 39  ? -48.162 24.996  3.823   1.00 72.41  ? 39  THR B O   1 
ATOM   1371 C  CB  . THR B 1 39  ? -46.639 26.267  6.185   1.00 72.43  ? 39  THR B CB  1 
ATOM   1372 O  OG1 . THR B 1 39  ? -45.471 26.335  7.014   1.00 71.46  ? 39  THR B OG1 1 
ATOM   1373 C  CG2 . THR B 1 39  ? -47.790 26.964  6.894   1.00 74.59  ? 39  THR B CG2 1 
ATOM   1374 N  N   . GLU B 1 40  ? -49.385 24.421  5.622   1.00 73.77  ? 40  GLU B N   1 
ATOM   1375 C  CA  . GLU B 1 40  ? -50.595 24.202  4.839   1.00 75.21  ? 40  GLU B CA  1 
ATOM   1376 C  C   . GLU B 1 40  ? -50.854 25.353  3.872   1.00 75.88  ? 40  GLU B C   1 
ATOM   1377 O  O   . GLU B 1 40  ? -50.638 26.514  4.210   1.00 78.44  ? 40  GLU B O   1 
ATOM   1378 C  CB  . GLU B 1 40  ? -51.814 23.980  5.738   1.00 75.16  ? 40  GLU B CB  1 
ATOM   1379 C  CG  . GLU B 1 40  ? -53.027 23.443  4.968   1.00 74.98  ? 40  GLU B CG  1 
ATOM   1380 C  CD  . GLU B 1 40  ? -54.285 23.393  5.806   1.00 74.82  ? 40  GLU B CD  1 
ATOM   1381 O  OE1 . GLU B 1 40  ? -54.164 23.392  7.047   1.00 76.11  ? 40  GLU B OE1 1 
ATOM   1382 O  OE2 . GLU B 1 40  ? -55.393 23.364  5.225   1.00 74.36  ? 40  GLU B OE2 1 
ATOM   1383 N  N   . GLY B 1 41  ? -51.310 25.024  2.668   1.00 87.01  ? 41  GLY B N   1 
ATOM   1384 C  CA  . GLY B 1 41  ? -51.637 26.036  1.683   1.00 84.22  ? 41  GLY B CA  1 
ATOM   1385 C  C   . GLY B 1 41  ? -51.042 25.723  0.330   1.00 82.56  ? 41  GLY B C   1 
ATOM   1386 O  O   . GLY B 1 41  ? -50.795 24.561  0.016   1.00 86.14  ? 41  GLY B O   1 
ATOM   1387 N  N   . LEU B 1 42  ? -50.817 26.758  -0.474  1.00 77.83  ? 42  LEU B N   1 
ATOM   1388 C  CA  . LEU B 1 42  ? -50.161 26.593  -1.767  1.00 74.06  ? 42  LEU B CA  1 
ATOM   1389 C  C   . LEU B 1 42  ? -48.676 26.906  -1.651  1.00 72.62  ? 42  LEU B C   1 
ATOM   1390 O  O   . LEU B 1 42  ? -48.284 27.856  -0.972  1.00 72.49  ? 42  LEU B O   1 
ATOM   1391 C  CB  . LEU B 1 42  ? -50.787 27.508  -2.820  1.00 70.31  ? 42  LEU B CB  1 
ATOM   1392 C  CG  . LEU B 1 42  ? -52.226 27.256  -3.270  1.00 67.49  ? 42  LEU B CG  1 
ATOM   1393 C  CD1 . LEU B 1 42  ? -52.702 28.433  -4.125  1.00 66.41  ? 42  LEU B CD1 1 
ATOM   1394 C  CD2 . LEU B 1 42  ? -52.358 25.934  -4.022  1.00 63.72  ? 42  LEU B CD2 1 
ATOM   1395 N  N   . HIS B 1 43  ? -47.857 26.105  -2.322  1.00 69.41  ? 43  HIS B N   1 
ATOM   1396 C  CA  . HIS B 1 43  ? -46.410 26.299  -2.302  1.00 62.03  ? 43  HIS B CA  1 
ATOM   1397 C  C   . HIS B 1 43  ? -45.824 26.322  -3.697  1.00 60.12  ? 43  HIS B C   1 
ATOM   1398 O  O   . HIS B 1 43  ? -46.049 25.401  -4.486  1.00 59.55  ? 43  HIS B O   1 
ATOM   1399 C  CB  . HIS B 1 43  ? -45.732 25.211  -1.496  1.00 54.34  ? 43  HIS B CB  1 
ATOM   1400 C  CG  . HIS B 1 43  ? -45.917 25.358  -0.026  1.00 56.68  ? 43  HIS B CG  1 
ATOM   1401 N  ND1 . HIS B 1 43  ? -44.995 25.991  0.778   1.00 58.53  ? 43  HIS B ND1 1 
ATOM   1402 C  CD2 . HIS B 1 43  ? -46.916 24.953  0.791   1.00 60.63  ? 43  HIS B CD2 1 
ATOM   1403 C  CE1 . HIS B 1 43  ? -45.415 25.966  2.029   1.00 62.71  ? 43  HIS B CE1 1 
ATOM   1404 N  NE2 . HIS B 1 43  ? -46.580 25.344  2.064   1.00 65.11  ? 43  HIS B NE2 1 
ATOM   1405 N  N   . GLY B 1 44  ? -45.079 27.389  -3.980  1.00 57.19  ? 44  GLY B N   1 
ATOM   1406 C  CA  . GLY B 1 44  ? -44.378 27.552  -5.238  1.00 57.33  ? 44  GLY B CA  1 
ATOM   1407 C  C   . GLY B 1 44  ? -43.381 26.424  -5.427  1.00 58.10  ? 44  GLY B C   1 
ATOM   1408 O  O   . GLY B 1 44  ? -42.733 25.970  -4.484  1.00 56.03  ? 44  GLY B O   1 
ATOM   1409 N  N   . PHE B 1 45  ? -43.257 25.984  -6.668  1.00 54.06  ? 45  PHE B N   1 
ATOM   1410 C  CA  . PHE B 1 45  ? -42.623 24.736  -6.962  1.00 50.71  ? 45  PHE B CA  1 
ATOM   1411 C  C   . PHE B 1 45  ? -42.270 24.816  -8.419  1.00 52.11  ? 45  PHE B C   1 
ATOM   1412 O  O   . PHE B 1 45  ? -43.137 25.111  -9.234  1.00 45.51  ? 45  PHE B O   1 
ATOM   1413 C  CB  . PHE B 1 45  ? -43.622 23.601  -6.705  1.00 52.01  ? 45  PHE B CB  1 
ATOM   1414 C  CG  . PHE B 1 45  ? -43.212 22.258  -7.277  1.00 53.68  ? 45  PHE B CG  1 
ATOM   1415 C  CD1 . PHE B 1 45  ? -42.474 21.353  -6.513  1.00 52.77  ? 45  PHE B CD1 1 
ATOM   1416 C  CD2 . PHE B 1 45  ? -43.581 21.894  -8.568  1.00 52.04  ? 45  PHE B CD2 1 
ATOM   1417 C  CE1 . PHE B 1 45  ? -42.098 20.118  -7.024  1.00 50.31  ? 45  PHE B CE1 1 
ATOM   1418 C  CE2 . PHE B 1 45  ? -43.213 20.661  -9.087  1.00 52.28  ? 45  PHE B CE2 1 
ATOM   1419 C  CZ  . PHE B 1 45  ? -42.469 19.769  -8.307  1.00 51.68  ? 45  PHE B CZ  1 
ATOM   1420 N  N   . HIS B 1 46  ? -40.997 24.572  -8.740  1.00 57.60  ? 46  HIS B N   1 
ATOM   1421 C  CA  . HIS B 1 46  ? -40.564 24.530  -10.129 1.00 60.02  ? 46  HIS B CA  1 
ATOM   1422 C  C   . HIS B 1 46  ? -39.050 24.455  -10.340 1.00 56.34  ? 46  HIS B C   1 
ATOM   1423 O  O   . HIS B 1 46  ? -38.273 24.225  -9.404  1.00 53.61  ? 46  HIS B O   1 
ATOM   1424 C  CB  . HIS B 1 46  ? -41.093 25.744  -10.847 1.00 65.21  ? 46  HIS B CB  1 
ATOM   1425 C  CG  . HIS B 1 46  ? -40.701 27.017  -10.187 1.00 68.18  ? 46  HIS B CG  1 
ATOM   1426 N  ND1 . HIS B 1 46  ? -39.399 27.466  -10.175 1.00 65.56  ? 46  HIS B ND1 1 
ATOM   1427 C  CD2 . HIS B 1 46  ? -41.425 27.918  -9.484  1.00 70.14  ? 46  HIS B CD2 1 
ATOM   1428 C  CE1 . HIS B 1 46  ? -39.344 28.604  -9.515  1.00 70.51  ? 46  HIS B CE1 1 
ATOM   1429 N  NE2 . HIS B 1 46  ? -40.557 28.896  -9.075  1.00 73.80  ? 46  HIS B NE2 1 
ATOM   1430 N  N   . VAL B 1 47  ? -38.654 24.659  -11.593 1.00 50.28  ? 47  VAL B N   1 
ATOM   1431 C  CA  . VAL B 1 47  ? -37.283 24.446  -12.018 1.00 47.52  ? 47  VAL B CA  1 
ATOM   1432 C  C   . VAL B 1 47  ? -36.442 25.729  -12.120 1.00 50.03  ? 47  VAL B C   1 
ATOM   1433 O  O   . VAL B 1 47  ? -36.843 26.705  -12.738 1.00 44.78  ? 47  VAL B O   1 
ATOM   1434 C  CB  . VAL B 1 47  ? -37.232 23.692  -13.370 1.00 43.79  ? 47  VAL B CB  1 
ATOM   1435 C  CG1 . VAL B 1 47  ? -35.829 23.184  -13.621 1.00 44.27  ? 47  VAL B CG1 1 
ATOM   1436 C  CG2 . VAL B 1 47  ? -38.182 22.540  -13.358 1.00 37.49  ? 47  VAL B CG2 1 
ATOM   1437 N  N   . HIS B 1 48  ? -35.261 25.713  -11.513 1.00 59.64  ? 48  HIS B N   1 
ATOM   1438 C  CA  . HIS B 1 48  ? -34.301 26.801  -11.693 1.00 63.93  ? 48  HIS B CA  1 
ATOM   1439 C  C   . HIS B 1 48  ? -33.220 26.371  -12.669 1.00 66.96  ? 48  HIS B C   1 
ATOM   1440 O  O   . HIS B 1 48  ? -33.170 25.211  -13.075 1.00 66.19  ? 48  HIS B O   1 
ATOM   1441 C  CB  . HIS B 1 48  ? -33.675 27.231  -10.366 1.00 64.42  ? 48  HIS B CB  1 
ATOM   1442 C  CG  . HIS B 1 48  ? -34.608 27.987  -9.474  1.00 66.58  ? 48  HIS B CG  1 
ATOM   1443 N  ND1 . HIS B 1 48  ? -34.221 29.113  -8.777  1.00 67.24  ? 48  HIS B ND1 1 
ATOM   1444 C  CD2 . HIS B 1 48  ? -35.908 27.777  -9.159  1.00 65.95  ? 48  HIS B CD2 1 
ATOM   1445 C  CE1 . HIS B 1 48  ? -35.244 29.563  -8.076  1.00 67.10  ? 48  HIS B CE1 1 
ATOM   1446 N  NE2 . HIS B 1 48  ? -36.278 28.768  -8.286  1.00 65.48  ? 48  HIS B NE2 1 
ATOM   1447 N  N   . GLU B 1 49  ? -32.342 27.314  -13.008 1.00 68.35  ? 49  GLU B N   1 
ATOM   1448 C  CA  . GLU B 1 49  ? -31.387 27.172  -14.109 1.00 64.75  ? 49  GLU B CA  1 
ATOM   1449 C  C   . GLU B 1 49  ? -30.213 26.230  -13.846 1.00 59.17  ? 49  GLU B C   1 
ATOM   1450 O  O   . GLU B 1 49  ? -29.818 25.453  -14.730 1.00 53.60  ? 49  GLU B O   1 
ATOM   1451 C  CB  . GLU B 1 49  ? -30.850 28.554  -14.484 1.00 68.89  ? 49  GLU B CB  1 
ATOM   1452 C  CG  . GLU B 1 49  ? -30.169 28.640  -15.835 1.00 72.24  ? 49  GLU B CG  1 
ATOM   1453 C  CD  . GLU B 1 49  ? -30.010 30.079  -16.300 1.00 77.92  ? 49  GLU B CD  1 
ATOM   1454 O  OE1 . GLU B 1 49  ? -30.596 30.983  -15.658 1.00 80.72  ? 49  GLU B OE1 1 
ATOM   1455 O  OE2 . GLU B 1 49  ? -29.308 30.308  -17.308 1.00 79.55  ? 49  GLU B OE2 1 
ATOM   1456 N  N   . PHE B 1 50  ? -29.645 26.310  -12.646 1.00 58.90  ? 50  PHE B N   1 
ATOM   1457 C  CA  . PHE B 1 50  ? -28.377 25.626  -12.364 1.00 55.60  ? 50  PHE B CA  1 
ATOM   1458 C  C   . PHE B 1 50  ? -28.558 24.463  -11.408 1.00 53.34  ? 50  PHE B C   1 
ATOM   1459 O  O   . PHE B 1 50  ? -29.296 24.575  -10.427 1.00 49.32  ? 50  PHE B O   1 
ATOM   1460 C  CB  . PHE B 1 50  ? -27.340 26.616  -11.801 1.00 51.54  ? 50  PHE B CB  1 
ATOM   1461 C  CG  . PHE B 1 50  ? -27.183 27.864  -12.634 1.00 50.14  ? 50  PHE B CG  1 
ATOM   1462 C  CD1 . PHE B 1 50  ? -26.877 27.780  -13.988 1.00 46.98  ? 50  PHE B CD1 1 
ATOM   1463 C  CD2 . PHE B 1 50  ? -27.391 29.119  -12.078 1.00 53.01  ? 50  PHE B CD2 1 
ATOM   1464 C  CE1 . PHE B 1 50  ? -26.754 28.922  -14.766 1.00 43.01  ? 50  PHE B CE1 1 
ATOM   1465 C  CE2 . PHE B 1 50  ? -27.276 30.271  -12.855 1.00 50.18  ? 50  PHE B CE2 1 
ATOM   1466 C  CZ  . PHE B 1 50  ? -26.950 30.167  -14.197 1.00 44.65  ? 50  PHE B CZ  1 
ATOM   1467 N  N   . GLY B 1 51  ? -27.868 23.356  -11.694 1.00 53.97  ? 51  GLY B N   1 
ATOM   1468 C  CA  . GLY B 1 51  ? -27.847 22.209  -10.801 1.00 51.25  ? 51  GLY B CA  1 
ATOM   1469 C  C   . GLY B 1 51  ? -26.739 22.349  -9.782  1.00 49.45  ? 51  GLY B C   1 
ATOM   1470 O  O   . GLY B 1 51  ? -25.939 21.429  -9.572  1.00 52.69  ? 51  GLY B O   1 
ATOM   1471 N  N   . ASP B 1 52  ? -26.701 23.508  -9.136  1.00 48.56  ? 52  ASP B N   1 
ATOM   1472 C  CA  . ASP B 1 52  ? -25.584 23.888  -8.275  1.00 49.93  ? 52  ASP B CA  1 
ATOM   1473 C  C   . ASP B 1 52  ? -25.984 24.080  -6.807  1.00 50.49  ? 52  ASP B C   1 
ATOM   1474 O  O   . ASP B 1 52  ? -26.522 25.123  -6.429  1.00 57.82  ? 52  ASP B O   1 
ATOM   1475 C  CB  . ASP B 1 52  ? -24.937 25.160  -8.827  1.00 51.19  ? 52  ASP B CB  1 
ATOM   1476 C  CG  . ASP B 1 52  ? -23.701 25.576  -8.047  1.00 50.10  ? 52  ASP B CG  1 
ATOM   1477 O  OD1 . ASP B 1 52  ? -23.463 25.002  -6.958  0.70 49.57  ? 52  ASP B OD1 1 
ATOM   1478 O  OD2 . ASP B 1 52  ? -22.990 26.489  -8.517  0.70 42.43  ? 52  ASP B OD2 1 
ATOM   1479 N  N   . ASN B 1 53  ? -25.725 23.063  -5.996  1.00 43.90  ? 53  ASN B N   1 
ATOM   1480 C  CA  . ASN B 1 53  ? -26.058 23.070  -4.576  1.00 45.44  ? 53  ASN B CA  1 
ATOM   1481 C  C   . ASN B 1 53  ? -24.877 23.571  -3.740  1.00 48.03  ? 53  ASN B C   1 
ATOM   1482 O  O   . ASN B 1 53  ? -24.819 23.366  -2.532  1.00 39.70  ? 53  ASN B O   1 
ATOM   1483 C  CB  . ASN B 1 53  ? -26.474 21.652  -4.156  1.00 51.24  ? 53  ASN B CB  1 
ATOM   1484 C  CG  . ASN B 1 53  ? -26.666 21.491  -2.643  1.00 57.17  ? 53  ASN B CG  1 
ATOM   1485 O  OD1 . ASN B 1 53  ? -25.804 20.932  -1.955  1.00 59.57  ? 53  ASN B OD1 1 
ATOM   1486 N  ND2 . ASN B 1 53  ? -27.809 21.945  -2.130  1.00 55.01  ? 53  ASN B ND2 1 
ATOM   1487 N  N   . THR B 1 54  ? -23.936 24.248  -4.388  1.00 47.39  ? 54  THR B N   1 
ATOM   1488 C  CA  . THR B 1 54  ? -22.699 24.637  -3.713  1.00 51.96  ? 54  THR B CA  1 
ATOM   1489 C  C   . THR B 1 54  ? -22.936 25.483  -2.454  1.00 55.31  ? 54  THR B C   1 
ATOM   1490 O  O   . THR B 1 54  ? -22.350 25.215  -1.402  1.00 56.22  ? 54  THR B O   1 
ATOM   1491 C  CB  . THR B 1 54  ? -21.732 25.342  -4.682  1.00 54.92  ? 54  THR B CB  1 
ATOM   1492 O  OG1 . THR B 1 54  ? -22.493 25.972  -5.721  1.00 57.39  ? 54  THR B OG1 1 
ATOM   1493 C  CG2 . THR B 1 54  ? -20.787 24.336  -5.325  1.00 50.44  ? 54  THR B CG2 1 
ATOM   1494 N  N   . ALA B 1 55  ? -23.801 26.492  -2.561  1.00 55.83  ? 55  ALA B N   1 
ATOM   1495 C  CA  . ALA B 1 55  ? -24.172 27.320  -1.414  1.00 57.49  ? 55  ALA B CA  1 
ATOM   1496 C  C   . ALA B 1 55  ? -25.614 27.078  -0.976  1.00 59.60  ? 55  ALA B C   1 
ATOM   1497 O  O   . ALA B 1 55  ? -26.272 27.980  -0.464  1.00 61.56  ? 55  ALA B O   1 
ATOM   1498 C  CB  . ALA B 1 55  ? -23.972 28.790  -1.742  1.00 56.85  ? 55  ALA B CB  1 
ATOM   1499 N  N   . GLY B 1 56  ? -26.106 25.861  -1.182  1.00 62.57  ? 56  GLY B N   1 
ATOM   1500 C  CA  . GLY B 1 56  ? -27.494 25.542  -0.891  1.00 66.27  ? 56  GLY B CA  1 
ATOM   1501 C  C   . GLY B 1 56  ? -28.400 25.813  -2.080  1.00 66.18  ? 56  GLY B C   1 
ATOM   1502 O  O   . GLY B 1 56  ? -27.955 25.773  -3.225  1.00 65.89  ? 56  GLY B O   1 
ATOM   1503 N  N   . CYS B 1 57  ? -29.669 26.101  -1.804  1.00 63.52  ? 57  CYS B N   1 
ATOM   1504 C  CA  . CYS B 1 57  ? -30.662 26.333  -2.850  1.00 61.42  ? 57  CYS B CA  1 
ATOM   1505 C  C   . CYS B 1 57  ? -30.389 27.614  -3.628  1.00 57.72  ? 57  CYS B C   1 
ATOM   1506 O  O   . CYS B 1 57  ? -30.757 27.730  -4.801  1.00 55.47  ? 57  CYS B O   1 
ATOM   1507 C  CB  . CYS B 1 57  ? -32.062 26.381  -2.242  1.00 64.60  ? 57  CYS B CB  1 
ATOM   1508 S  SG  . CYS B 1 57  ? -32.669 24.775  -1.646  1.00 72.53  ? 57  CYS B SG  1 
ATOM   1509 N  N   . THR B 1 58  ? -29.723 28.556  -2.962  1.00 58.23  ? 58  THR B N   1 
ATOM   1510 C  CA  . THR B 1 58  ? -29.385 29.876  -3.506  1.00 54.00  ? 58  THR B CA  1 
ATOM   1511 C  C   . THR B 1 58  ? -28.648 29.818  -4.844  1.00 52.95  ? 58  THR B C   1 
ATOM   1512 O  O   . THR B 1 58  ? -28.909 30.617  -5.761  1.00 50.68  ? 58  THR B O   1 
ATOM   1513 C  CB  . THR B 1 58  ? -28.464 30.623  -2.519  1.00 54.53  ? 58  THR B CB  1 
ATOM   1514 O  OG1 . THR B 1 58  ? -29.036 30.611  -1.205  1.00 55.89  ? 58  THR B OG1 1 
ATOM   1515 C  CG2 . THR B 1 58  ? -28.220 32.053  -2.972  1.00 55.47  ? 58  THR B CG2 1 
ATOM   1516 N  N   . SER B 1 59  ? -27.716 28.871  -4.940  1.00 52.19  ? 59  SER B N   1 
ATOM   1517 C  CA  . SER B 1 59  ? -26.824 28.769  -6.091  1.00 51.78  ? 59  SER B CA  1 
ATOM   1518 C  C   . SER B 1 59  ? -27.487 28.109  -7.299  1.00 51.95  ? 59  SER B C   1 
ATOM   1519 O  O   . SER B 1 59  ? -26.861 27.906  -8.342  1.00 47.27  ? 59  SER B O   1 
ATOM   1520 C  CB  . SER B 1 59  ? -25.550 28.033  -5.696  1.00 51.19  ? 59  SER B CB  1 
ATOM   1521 O  OG  . SER B 1 59  ? -25.667 27.509  -4.387  1.00 50.10  ? 59  SER B OG  1 
ATOM   1522 N  N   . ALA B 1 60  ? -28.767 27.792  -7.143  1.00 51.65  ? 60  ALA B N   1 
ATOM   1523 C  CA  . ALA B 1 60  ? -29.574 27.282  -8.230  1.00 49.37  ? 60  ALA B CA  1 
ATOM   1524 C  C   . ALA B 1 60  ? -29.900 28.429  -9.172  1.00 56.04  ? 60  ALA B C   1 
ATOM   1525 O  O   . ALA B 1 60  ? -30.187 28.222  -10.356 1.00 59.24  ? 60  ALA B O   1 
ATOM   1526 C  CB  . ALA B 1 60  ? -30.831 26.691  -7.674  1.00 47.67  ? 60  ALA B CB  1 
ATOM   1527 N  N   . GLY B 1 61  ? -29.854 29.645  -8.626  1.00 55.72  ? 61  GLY B N   1 
ATOM   1528 C  CA  . GLY B 1 61  ? -30.133 30.856  -9.371  1.00 51.89  ? 61  GLY B CA  1 
ATOM   1529 C  C   . GLY B 1 61  ? -31.590 31.076  -9.751  1.00 53.40  ? 61  GLY B C   1 
ATOM   1530 O  O   . GLY B 1 61  ? -32.520 30.537  -9.127  1.00 45.58  ? 61  GLY B O   1 
ATOM   1531 N  N   . PRO B 1 62  ? -31.799 31.882  -10.802 1.00 57.77  ? 62  PRO B N   1 
ATOM   1532 C  CA  . PRO B 1 62  ? -33.140 32.226  -11.274 1.00 60.16  ? 62  PRO B CA  1 
ATOM   1533 C  C   . PRO B 1 62  ? -33.842 31.017  -11.876 1.00 61.51  ? 62  PRO B C   1 
ATOM   1534 O  O   . PRO B 1 62  ? -33.174 30.036  -12.223 1.00 58.66  ? 62  PRO B O   1 
ATOM   1535 C  CB  . PRO B 1 62  ? -32.869 33.277  -12.353 1.00 58.34  ? 62  PRO B CB  1 
ATOM   1536 C  CG  . PRO B 1 62  ? -31.491 32.963  -12.838 1.00 56.82  ? 62  PRO B CG  1 
ATOM   1537 C  CD  . PRO B 1 62  ? -30.746 32.494  -11.632 1.00 55.92  ? 62  PRO B CD  1 
ATOM   1538 N  N   . HIS B 1 63  ? -35.172 31.105  -11.974 1.00 61.60  ? 63  HIS B N   1 
ATOM   1539 C  CA  . HIS B 1 63  ? -36.011 30.081  -12.597 1.00 56.75  ? 63  HIS B CA  1 
ATOM   1540 C  C   . HIS B 1 63  ? -35.483 29.734  -13.994 1.00 48.00  ? 63  HIS B C   1 
ATOM   1541 O  O   . HIS B 1 63  ? -34.941 30.597  -14.682 1.00 46.91  ? 63  HIS B O   1 
ATOM   1542 C  CB  . HIS B 1 63  ? -37.474 30.564  -12.685 1.00 58.90  ? 63  HIS B CB  1 
ATOM   1543 C  CG  . HIS B 1 63  ? -38.110 30.858  -11.357 1.00 57.03  ? 63  HIS B CG  1 
ATOM   1544 N  ND1 . HIS B 1 63  ? -39.453 31.136  -11.221 1.00 55.95  ? 63  HIS B ND1 1 
ATOM   1545 C  CD2 . HIS B 1 63  ? -37.590 30.915  -10.108 1.00 56.79  ? 63  HIS B CD2 1 
ATOM   1546 C  CE1 . HIS B 1 63  ? -39.733 31.359  -9.950  1.00 54.12  ? 63  HIS B CE1 1 
ATOM   1547 N  NE2 . HIS B 1 63  ? -38.621 31.222  -9.251  1.00 54.48  ? 63  HIS B NE2 1 
ATOM   1548 N  N   . PHE B 1 64  ? -35.629 28.474  -14.398 1.00 44.29  ? 64  PHE B N   1 
ATOM   1549 C  CA  . PHE B 1 64  ? -35.136 28.022  -15.695 1.00 45.52  ? 64  PHE B CA  1 
ATOM   1550 C  C   . PHE B 1 64  ? -35.914 28.695  -16.794 1.00 48.72  ? 64  PHE B C   1 
ATOM   1551 O  O   . PHE B 1 64  ? -37.083 28.396  -17.016 1.00 51.25  ? 64  PHE B O   1 
ATOM   1552 C  CB  . PHE B 1 64  ? -35.239 26.497  -15.826 1.00 50.03  ? 64  PHE B CB  1 
ATOM   1553 C  CG  . PHE B 1 64  ? -34.843 25.964  -17.189 1.00 51.80  ? 64  PHE B CG  1 
ATOM   1554 C  CD1 . PHE B 1 64  ? -33.720 26.444  -17.845 1.00 46.95  ? 64  PHE B CD1 1 
ATOM   1555 C  CD2 . PHE B 1 64  ? -35.585 24.955  -17.796 1.00 53.63  ? 64  PHE B CD2 1 
ATOM   1556 C  CE1 . PHE B 1 64  ? -33.362 25.942  -19.086 1.00 45.62  ? 64  PHE B CE1 1 
ATOM   1557 C  CE2 . PHE B 1 64  ? -35.230 24.444  -19.030 1.00 44.17  ? 64  PHE B CE2 1 
ATOM   1558 C  CZ  . PHE B 1 64  ? -34.124 24.935  -19.680 1.00 43.40  ? 64  PHE B CZ  1 
ATOM   1559 N  N   . ASN B 1 65  ? -35.269 29.631  -17.470 1.00 51.32  ? 65  ASN B N   1 
ATOM   1560 C  CA  . ASN B 1 65  ? -35.953 30.401  -18.483 1.00 57.08  ? 65  ASN B CA  1 
ATOM   1561 C  C   . ASN B 1 65  ? -35.126 30.518  -19.749 1.00 60.69  ? 65  ASN B C   1 
ATOM   1562 O  O   . ASN B 1 65  ? -34.410 31.501  -19.942 1.00 56.80  ? 65  ASN B O   1 
ATOM   1563 C  CB  . ASN B 1 65  ? -36.326 31.777  -17.950 1.00 61.12  ? 65  ASN B CB  1 
ATOM   1564 C  CG  . ASN B 1 65  ? -36.908 32.676  -19.027 1.00 64.57  ? 65  ASN B CG  1 
ATOM   1565 O  OD1 . ASN B 1 65  ? -36.646 33.882  -19.054 1.00 64.72  ? 65  ASN B OD1 1 
ATOM   1566 N  ND2 . ASN B 1 65  ? -37.687 32.087  -19.934 1.00 63.84  ? 65  ASN B ND2 1 
ATOM   1567 N  N   . PRO B 1 66  ? -35.217 29.491  -20.607 1.00 64.02  ? 66  PRO B N   1 
ATOM   1568 C  CA  . PRO B 1 66  ? -34.541 29.381  -21.902 1.00 63.92  ? 66  PRO B CA  1 
ATOM   1569 C  C   . PRO B 1 66  ? -34.953 30.467  -22.892 1.00 65.04  ? 66  PRO B C   1 
ATOM   1570 O  O   . PRO B 1 66  ? -34.185 30.767  -23.808 1.00 62.74  ? 66  PRO B O   1 
ATOM   1571 C  CB  . PRO B 1 66  ? -35.009 28.023  -22.425 1.00 62.02  ? 66  PRO B CB  1 
ATOM   1572 C  CG  . PRO B 1 66  ? -35.387 27.263  -21.225 1.00 62.61  ? 66  PRO B CG  1 
ATOM   1573 C  CD  . PRO B 1 66  ? -35.912 28.246  -20.241 1.00 63.22  ? 66  PRO B CD  1 
ATOM   1574 N  N   . LEU B 1 67  ? -36.140 31.043  -22.722 1.00 67.26  ? 67  LEU B N   1 
ATOM   1575 C  CA  . LEU B 1 67  ? -36.673 31.972  -23.724 1.00 65.98  ? 67  LEU B CA  1 
ATOM   1576 C  C   . LEU B 1 67  ? -36.883 33.403  -23.214 1.00 66.75  ? 67  LEU B C   1 
ATOM   1577 O  O   . LEU B 1 67  ? -37.724 34.139  -23.745 1.00 64.55  ? 67  LEU B O   1 
ATOM   1578 C  CB  . LEU B 1 67  ? -37.977 31.425  -24.309 1.00 67.49  ? 67  LEU B CB  1 
ATOM   1579 C  CG  . LEU B 1 67  ? -37.977 30.223  -25.263 1.00 69.99  ? 67  LEU B CG  1 
ATOM   1580 C  CD1 . LEU B 1 67  ? -36.666 29.451  -25.272 1.00 71.98  ? 67  LEU B CD1 1 
ATOM   1581 C  CD2 . LEU B 1 67  ? -39.118 29.295  -24.895 1.00 71.68  ? 67  LEU B CD2 1 
ATOM   1582 N  N   . SER B 1 68  ? -36.117 33.785  -22.190 1.00 67.88  ? 68  SER B N   1 
ATOM   1583 C  CA  . SER B 1 68  ? -36.123 35.145  -21.631 1.00 65.96  ? 68  SER B CA  1 
ATOM   1584 C  C   . SER B 1 68  ? -37.514 35.795  -21.512 1.00 65.13  ? 68  SER B C   1 
ATOM   1585 O  O   . SER B 1 68  ? -37.836 36.735  -22.240 1.00 63.06  ? 68  SER B O   1 
ATOM   1586 C  CB  . SER B 1 68  ? -35.168 36.039  -22.422 1.00 66.64  ? 68  SER B CB  1 
ATOM   1587 O  OG  . SER B 1 68  ? -33.871 35.454  -22.472 1.00 68.38  ? 68  SER B OG  1 
ATOM   1588 N  N   . ARG B 1 69  ? -38.316 35.303  -20.569 1.00 65.78  ? 69  ARG B N   1 
ATOM   1589 C  CA  . ARG B 1 69  ? -39.707 35.738  -20.419 1.00 69.34  ? 69  ARG B CA  1 
ATOM   1590 C  C   . ARG B 1 69  ? -40.109 35.983  -18.959 1.00 67.56  ? 69  ARG B C   1 
ATOM   1591 O  O   . ARG B 1 69  ? -39.370 35.648  -18.028 1.00 64.31  ? 69  ARG B O   1 
ATOM   1592 C  CB  . ARG B 1 69  ? -40.665 34.719  -21.069 1.00 71.40  ? 69  ARG B CB  1 
ATOM   1593 C  CG  . ARG B 1 69  ? -40.684 34.783  -22.593 1.00 72.88  ? 69  ARG B CG  1 
ATOM   1594 C  CD  . ARG B 1 69  ? -40.906 33.421  -23.218 1.00 76.52  ? 69  ARG B CD  1 
ATOM   1595 N  NE  . ARG B 1 69  ? -41.230 33.526  -24.639 1.00 82.92  ? 69  ARG B NE  1 
ATOM   1596 C  CZ  . ARG B 1 69  ? -42.437 33.292  -25.154 1.00 90.02  ? 69  ARG B CZ  1 
ATOM   1597 N  NH1 . ARG B 1 69  ? -43.444 32.923  -24.366 1.00 91.86  ? 69  ARG B NH1 1 
ATOM   1598 N  NH2 . ARG B 1 69  ? -42.640 33.418  -26.463 1.00 91.76  ? 69  ARG B NH2 1 
ATOM   1599 N  N   . LYS B 1 70  ? -41.292 36.569  -18.780 1.00 66.89  ? 70  LYS B N   1 
ATOM   1600 C  CA  . LYS B 1 70  ? -41.805 36.911  -17.460 1.00 61.35  ? 70  LYS B CA  1 
ATOM   1601 C  C   . LYS B 1 70  ? -42.239 35.660  -16.758 1.00 60.69  ? 70  LYS B C   1 
ATOM   1602 O  O   . LYS B 1 70  ? -42.655 34.701  -17.398 1.00 64.31  ? 70  LYS B O   1 
ATOM   1603 C  CB  . LYS B 1 70  ? -42.979 37.872  -17.569 1.00 60.55  ? 70  LYS B CB  1 
ATOM   1604 N  N   . HIS B 1 71  ? -42.144 35.674  -15.435 1.00 57.75  ? 71  HIS B N   1 
ATOM   1605 C  CA  . HIS B 1 71  ? -42.606 34.565  -14.611 1.00 57.85  ? 71  HIS B CA  1 
ATOM   1606 C  C   . HIS B 1 71  ? -44.105 34.264  -14.793 1.00 61.94  ? 71  HIS B C   1 
ATOM   1607 O  O   . HIS B 1 71  ? -44.901 35.165  -15.078 1.00 62.59  ? 71  HIS B O   1 
ATOM   1608 C  CB  . HIS B 1 71  ? -42.305 34.881  -13.148 1.00 47.58  ? 71  HIS B CB  1 
ATOM   1609 C  CG  . HIS B 1 71  ? -42.927 33.923  -12.181 1.00 48.07  ? 71  HIS B CG  1 
ATOM   1610 N  ND1 . HIS B 1 71  ? -42.354 32.713  -11.864 1.00 47.72  ? 71  HIS B ND1 1 
ATOM   1611 C  CD2 . HIS B 1 71  ? -44.067 34.005  -11.456 1.00 48.87  ? 71  HIS B CD2 1 
ATOM   1612 C  CE1 . HIS B 1 71  ? -43.113 32.088  -10.983 1.00 54.30  ? 71  HIS B CE1 1 
ATOM   1613 N  NE2 . HIS B 1 71  ? -44.158 32.852  -10.719 1.00 54.89  ? 71  HIS B NE2 1 
ATOM   1614 N  N   . GLY B 1 72  ? -44.499 33.004  -14.613 1.00 64.72  ? 72  GLY B N   1 
ATOM   1615 C  CA  . GLY B 1 72  ? -45.903 32.656  -14.753 1.00 68.27  ? 72  GLY B CA  1 
ATOM   1616 C  C   . GLY B 1 72  ? -46.380 31.345  -14.140 1.00 73.11  ? 72  GLY B C   1 
ATOM   1617 O  O   . GLY B 1 72  ? -45.591 30.567  -13.600 1.00 72.41  ? 72  GLY B O   1 
ATOM   1618 N  N   . GLY B 1 73  ? -47.694 31.116  -14.221 1.00 75.17  ? 73  GLY B N   1 
ATOM   1619 C  CA  . GLY B 1 73  ? -48.299 29.850  -13.852 1.00 70.94  ? 73  GLY B CA  1 
ATOM   1620 C  C   . GLY B 1 73  ? -48.165 28.886  -15.013 1.00 68.75  ? 73  GLY B C   1 
ATOM   1621 O  O   . GLY B 1 73  ? -47.924 29.306  -16.142 1.00 68.19  ? 73  GLY B O   1 
ATOM   1622 N  N   . PRO B 1 74  ? -48.318 27.584  -14.748 1.00 70.32  ? 74  PRO B N   1 
ATOM   1623 C  CA  . PRO B 1 74  ? -48.018 26.582  -15.779 1.00 70.99  ? 74  PRO B CA  1 
ATOM   1624 C  C   . PRO B 1 74  ? -48.776 26.783  -17.082 1.00 73.21  ? 74  PRO B C   1 
ATOM   1625 O  O   . PRO B 1 74  ? -48.295 26.344  -18.124 1.00 70.77  ? 74  PRO B O   1 
ATOM   1626 C  CB  . PRO B 1 74  ? -48.405 25.248  -15.119 1.00 71.75  ? 74  PRO B CB  1 
ATOM   1627 C  CG  . PRO B 1 74  ? -49.135 25.597  -13.860 1.00 72.99  ? 74  PRO B CG  1 
ATOM   1628 C  CD  . PRO B 1 74  ? -48.688 26.972  -13.461 1.00 72.39  ? 74  PRO B CD  1 
ATOM   1629 N  N   . LYS B 1 75  ? -49.925 27.453  -17.029 1.00 78.47  ? 75  LYS B N   1 
ATOM   1630 C  CA  . LYS B 1 75  ? -50.800 27.551  -18.198 1.00 79.40  ? 75  LYS B CA  1 
ATOM   1631 C  C   . LYS B 1 75  ? -50.822 28.938  -18.871 1.00 80.68  ? 75  LYS B C   1 
ATOM   1632 O  O   . LYS B 1 75  ? -51.403 29.103  -19.944 1.00 81.15  ? 75  LYS B O   1 
ATOM   1633 C  CB  . LYS B 1 75  ? -52.205 27.069  -17.836 1.00 79.66  ? 75  LYS B CB  1 
ATOM   1634 C  CG  . LYS B 1 75  ? -52.212 25.720  -17.118 1.00 81.18  ? 75  LYS B CG  1 
ATOM   1635 C  CD  . LYS B 1 75  ? -52.642 24.572  -18.029 1.00 82.52  ? 75  LYS B CD  1 
ATOM   1636 C  CE  . LYS B 1 75  ? -51.766 24.469  -19.264 0.00 82.69  ? 75  LYS B CE  1 
ATOM   1637 N  NZ  . LYS B 1 75  ? -52.237 23.394  -20.179 0.00 83.57  ? 75  LYS B NZ  1 
ATOM   1638 N  N   . ASP B 1 76  ? -50.179 29.925  -18.249 1.00 79.55  ? 76  ASP B N   1 
ATOM   1639 C  CA  . ASP B 1 76  ? -49.925 31.205  -18.910 1.00 80.95  ? 76  ASP B CA  1 
ATOM   1640 C  C   . ASP B 1 76  ? -49.047 30.971  -20.131 1.00 83.83  ? 76  ASP B C   1 
ATOM   1641 O  O   . ASP B 1 76  ? -48.188 30.096  -20.111 1.00 85.61  ? 76  ASP B O   1 
ATOM   1642 C  CB  . ASP B 1 76  ? -49.206 32.165  -17.960 1.00 78.84  ? 76  ASP B CB  1 
ATOM   1643 C  CG  . ASP B 1 76  ? -50.071 32.590  -16.794 1.00 78.19  ? 76  ASP B CG  1 
ATOM   1644 O  OD1 . ASP B 1 76  ? -51.291 32.769  -17.004 1.00 82.05  ? 76  ASP B OD1 1 
ATOM   1645 O  OD2 . ASP B 1 76  ? -49.533 32.747  -15.673 1.00 73.43  ? 76  ASP B OD2 1 
ATOM   1646 N  N   . GLU B 1 77  ? -49.244 31.746  -21.191 1.00 87.23  ? 77  GLU B N   1 
ATOM   1647 C  CA  . GLU B 1 77  ? -48.371 31.626  -22.355 1.00 90.74  ? 77  GLU B CA  1 
ATOM   1648 C  C   . GLU B 1 77  ? -47.018 32.239  -22.035 1.00 88.34  ? 77  GLU B C   1 
ATOM   1649 O  O   . GLU B 1 77  ? -45.985 31.782  -22.531 1.00 88.93  ? 77  GLU B O   1 
ATOM   1650 C  CB  . GLU B 1 77  ? -48.979 32.299  -23.590 1.00 96.28  ? 77  GLU B CB  1 
ATOM   1651 C  CG  . GLU B 1 77  ? -48.035 32.354  -24.805 1.00 97.58  ? 77  GLU B CG  1 
ATOM   1652 C  CD  . GLU B 1 77  ? -47.747 30.984  -25.415 1.00 97.20  ? 77  GLU B CD  1 
ATOM   1653 O  OE1 . GLU B 1 77  ? -46.553 30.639  -25.549 1.00 95.93  ? 77  GLU B OE1 1 
ATOM   1654 O  OE2 . GLU B 1 77  ? -48.707 30.259  -25.768 1.00 97.19  ? 77  GLU B OE2 1 
ATOM   1655 N  N   . GLU B 1 78  ? -47.037 33.273  -21.195 0.00 85.02  ? 78  GLU B N   1 
ATOM   1656 C  CA  . GLU B 1 78  ? -45.823 33.937  -20.727 1.00 80.58  ? 78  GLU B CA  1 
ATOM   1657 C  C   . GLU B 1 78  ? -45.347 33.344  -19.400 1.00 74.28  ? 78  GLU B C   1 
ATOM   1658 O  O   . GLU B 1 78  ? -45.929 33.593  -18.343 1.00 72.86  ? 78  GLU B O   1 
ATOM   1659 C  CB  . GLU B 1 78  ? -46.050 35.442  -20.583 1.00 81.21  ? 78  GLU B CB  1 
ATOM   1660 C  CG  . GLU B 1 78  ? -45.518 36.272  -21.747 1.00 83.32  ? 78  GLU B CG  1 
ATOM   1661 C  CD  . GLU B 1 78  ? -44.064 36.693  -21.563 1.00 83.54  ? 78  GLU B CD  1 
ATOM   1662 O  OE1 . GLU B 1 78  ? -43.708 37.184  -20.468 1.00 82.21  ? 78  GLU B OE1 1 
ATOM   1663 O  OE2 . GLU B 1 78  ? -43.277 36.527  -22.517 1.00 84.61  ? 78  GLU B OE2 1 
ATOM   1664 N  N   . ARG B 1 79  ? -44.286 32.553  -19.462 1.00 69.25  ? 79  ARG B N   1 
ATOM   1665 C  CA  . ARG B 1 79  ? -43.759 31.949  -18.257 1.00 69.53  ? 79  ARG B CA  1 
ATOM   1666 C  C   . ARG B 1 79  ? -42.367 31.383  -18.455 1.00 70.30  ? 79  ARG B C   1 
ATOM   1667 O  O   . ARG B 1 79  ? -41.914 31.151  -19.578 1.00 71.88  ? 79  ARG B O   1 
ATOM   1668 C  CB  . ARG B 1 79  ? -44.703 30.863  -17.739 1.00 70.90  ? 79  ARG B CB  1 
ATOM   1669 C  CG  . ARG B 1 79  ? -44.206 29.444  -17.915 0.00 69.24  ? 79  ARG B CG  1 
ATOM   1670 C  CD  . ARG B 1 79  ? -45.310 28.560  -18.463 1.00 68.92  ? 79  ARG B CD  1 
ATOM   1671 N  NE  . ARG B 1 79  ? -45.361 27.254  -17.815 1.00 68.04  ? 79  ARG B NE  1 
ATOM   1672 C  CZ  . ARG B 1 79  ? -44.371 26.369  -17.838 1.00 67.07  ? 79  ARG B CZ  1 
ATOM   1673 N  NH1 . ARG B 1 79  ? -43.242 26.665  -18.464 1.00 68.04  ? 79  ARG B NH1 1 
ATOM   1674 N  NH2 . ARG B 1 79  ? -44.505 25.194  -17.232 1.00 64.12  ? 79  ARG B NH2 1 
ATOM   1675 N  N   . HIS B 1 80  ? -41.687 31.183  -17.337 1.00 66.37  ? 80  HIS B N   1 
ATOM   1676 C  CA  . HIS B 1 80  ? -40.394 30.565  -17.345 1.00 60.63  ? 80  HIS B CA  1 
ATOM   1677 C  C   . HIS B 1 80  ? -40.637 29.092  -17.615 1.00 62.73  ? 80  HIS B C   1 
ATOM   1678 O  O   . HIS B 1 80  ? -41.479 28.471  -16.966 1.00 64.42  ? 80  HIS B O   1 
ATOM   1679 C  CB  . HIS B 1 80  ? -39.730 30.802  -15.995 1.00 57.84  ? 80  HIS B CB  1 
ATOM   1680 C  CG  . HIS B 1 80  ? -39.601 32.253  -15.643 1.00 60.12  ? 80  HIS B CG  1 
ATOM   1681 N  ND1 . HIS B 1 80  ? -39.530 32.705  -14.345 1.00 59.95  ? 80  HIS B ND1 1 
ATOM   1682 C  CD2 . HIS B 1 80  ? -39.532 33.357  -16.427 1.00 63.84  ? 80  HIS B CD2 1 
ATOM   1683 C  CE1 . HIS B 1 80  ? -39.432 34.024  -14.340 1.00 63.32  ? 80  HIS B CE1 1 
ATOM   1684 N  NE2 . HIS B 1 80  ? -39.431 34.445  -15.592 1.00 65.11  ? 80  HIS B NE2 1 
ATOM   1685 N  N   . VAL B 1 81  ? -39.940 28.549  -18.611 1.00 59.92  ? 81  VAL B N   1 
ATOM   1686 C  CA  . VAL B 1 81  ? -40.073 27.141  -18.968 1.00 57.18  ? 81  VAL B CA  1 
ATOM   1687 C  C   . VAL B 1 81  ? -40.134 26.274  -17.721 1.00 51.58  ? 81  VAL B C   1 
ATOM   1688 O  O   . VAL B 1 81  ? -40.829 25.265  -17.680 1.00 47.60  ? 81  VAL B O   1 
ATOM   1689 C  CB  . VAL B 1 81  ? -38.905 26.667  -19.858 1.00 59.34  ? 81  VAL B CB  1 
ATOM   1690 C  CG1 . VAL B 1 81  ? -38.938 25.147  -20.033 1.00 57.93  ? 81  VAL B CG1 1 
ATOM   1691 C  CG2 . VAL B 1 81  ? -38.961 27.359  -21.203 1.00 62.69  ? 81  VAL B CG2 1 
ATOM   1692 N  N   . GLY B 1 82  ? -39.406 26.679  -16.694 1.00 52.23  ? 82  GLY B N   1 
ATOM   1693 C  CA  . GLY B 1 82  ? -39.391 25.922  -15.461 1.00 55.05  ? 82  GLY B CA  1 
ATOM   1694 C  C   . GLY B 1 82  ? -40.597 26.130  -14.563 1.00 56.97  ? 82  GLY B C   1 
ATOM   1695 O  O   . GLY B 1 82  ? -40.708 25.461  -13.540 1.00 57.97  ? 82  GLY B O   1 
ATOM   1696 N  N   . ASP B 1 83  ? -41.496 27.043  -14.935 1.00 59.21  ? 83  ASP B N   1 
ATOM   1697 C  CA  . ASP B 1 83  ? -42.615 27.421  -14.064 1.00 64.64  ? 83  ASP B CA  1 
ATOM   1698 C  C   . ASP B 1 83  ? -43.649 26.303  -13.916 1.00 67.22  ? 83  ASP B C   1 
ATOM   1699 O  O   . ASP B 1 83  ? -44.341 25.952  -14.871 1.00 69.14  ? 83  ASP B O   1 
ATOM   1700 C  CB  . ASP B 1 83  ? -43.320 28.695  -14.556 1.00 67.19  ? 83  ASP B CB  1 
ATOM   1701 C  CG  . ASP B 1 83  ? -42.390 29.907  -14.637 1.00 65.54  ? 83  ASP B CG  1 
ATOM   1702 O  OD1 . ASP B 1 83  ? -41.312 29.900  -13.999 1.00 65.17  ? 83  ASP B OD1 1 
ATOM   1703 O  OD2 . ASP B 1 83  ? -42.750 30.871  -15.346 1.00 62.68  ? 83  ASP B OD2 1 
ATOM   1704 N  N   . LEU B 1 84  ? -43.762 25.764  -12.707 1.00 65.08  ? 84  LEU B N   1 
ATOM   1705 C  CA  . LEU B 1 84  ? -44.739 24.723  -12.425 1.00 62.84  ? 84  LEU B CA  1 
ATOM   1706 C  C   . LEU B 1 84  ? -45.905 25.253  -11.599 1.00 60.42  ? 84  LEU B C   1 
ATOM   1707 O  O   . LEU B 1 84  ? -46.892 24.561  -11.355 1.00 60.56  ? 84  LEU B O   1 
ATOM   1708 C  CB  . LEU B 1 84  ? -44.057 23.559  -11.720 1.00 59.53  ? 84  LEU B CB  1 
ATOM   1709 C  CG  . LEU B 1 84  ? -43.086 22.909  -12.688 1.00 59.35  ? 84  LEU B CG  1 
ATOM   1710 C  CD1 . LEU B 1 84  ? -42.581 21.587  -12.131 1.00 62.98  ? 84  LEU B CD1 1 
ATOM   1711 C  CD2 . LEU B 1 84  ? -43.785 22.716  -14.031 1.00 56.36  ? 84  LEU B CD2 1 
ATOM   1712 N  N   . GLY B 1 85  ? -45.786 26.501  -11.180 1.00 59.18  ? 85  GLY B N   1 
ATOM   1713 C  CA  . GLY B 1 85  ? -46.787 27.085  -10.324 1.00 59.65  ? 85  GLY B CA  1 
ATOM   1714 C  C   . GLY B 1 85  ? -46.801 26.430  -8.961  1.00 61.07  ? 85  GLY B C   1 
ATOM   1715 O  O   . GLY B 1 85  ? -45.784 26.400  -8.253  1.00 47.48  ? 85  GLY B O   1 
ATOM   1716 N  N   . ASN B 1 86  ? -47.963 25.908  -8.589  1.00 61.13  ? 86  ASN B N   1 
ATOM   1717 C  CA  . ASN B 1 86  ? -48.159 25.452  -7.231  1.00 62.24  ? 86  ASN B CA  1 
ATOM   1718 C  C   . ASN B 1 86  ? -48.380 23.960  -7.092  1.00 62.25  ? 86  ASN B C   1 
ATOM   1719 O  O   . ASN B 1 86  ? -48.937 23.301  -7.978  1.00 61.25  ? 86  ASN B O   1 
ATOM   1720 C  CB  . ASN B 1 86  ? -49.321 26.200  -6.591  1.00 68.44  ? 86  ASN B CB  1 
ATOM   1721 C  CG  . ASN B 1 86  ? -48.909 27.547  -6.025  1.00 73.83  ? 86  ASN B CG  1 
ATOM   1722 O  OD1 . ASN B 1 86  ? -48.474 27.635  -4.873  1.00 79.50  ? 86  ASN B OD1 1 
ATOM   1723 N  ND2 . ASN B 1 86  ? -49.046 28.603  -6.826  1.00 68.31  ? 86  ASN B ND2 1 
ATOM   1724 N  N   . VAL B 1 87  ? -47.909 23.444  -5.966  1.00 61.38  ? 87  VAL B N   1 
ATOM   1725 C  CA  . VAL B 1 87  ? -48.343 22.160  -5.458  1.00 62.96  ? 87  VAL B CA  1 
ATOM   1726 C  C   . VAL B 1 87  ? -49.057 22.447  -4.146  1.00 64.83  ? 87  VAL B C   1 
ATOM   1727 O  O   . VAL B 1 87  ? -48.690 23.375  -3.421  1.00 66.69  ? 87  VAL B O   1 
ATOM   1728 C  CB  . VAL B 1 87  ? -47.163 21.188  -5.202  1.00 51.77  ? 87  VAL B CB  1 
ATOM   1729 C  CG1 . VAL B 1 87  ? -46.309 21.030  -6.457  1.00 50.03  ? 87  VAL B CG1 1 
ATOM   1730 C  CG2 . VAL B 1 87  ? -46.336 21.648  -4.012  1.00 51.76  ? 87  VAL B CG2 1 
ATOM   1731 N  N   . THR B 1 88  ? -50.084 21.665  -3.839  1.00 62.63  ? 88  THR B N   1 
ATOM   1732 C  CA  . THR B 1 88  ? -50.863 21.931  -2.648  1.00 63.05  ? 88  THR B CA  1 
ATOM   1733 C  C   . THR B 1 88  ? -50.501 21.001  -1.512  1.00 61.38  ? 88  THR B C   1 
ATOM   1734 O  O   . THR B 1 88  ? -50.684 19.783  -1.607  1.00 63.14  ? 88  THR B O   1 
ATOM   1735 C  CB  . THR B 1 88  ? -52.370 21.818  -2.911  1.00 69.34  ? 88  THR B CB  1 
ATOM   1736 O  OG1 . THR B 1 88  ? -52.679 22.373  -4.199  1.00 73.32  ? 88  THR B OG1 1 
ATOM   1737 C  CG2 . THR B 1 88  ? -53.142 22.555  -1.815  1.00 67.41  ? 88  THR B CG2 1 
ATOM   1738 N  N   . ALA B 1 89  ? -49.990 21.589  -0.437  1.00 58.93  ? 89  ALA B N   1 
ATOM   1739 C  CA  . ALA B 1 89  ? -49.709 20.853  0.781   1.00 58.91  ? 89  ALA B CA  1 
ATOM   1740 C  C   . ALA B 1 89  ? -50.988 20.733  1.573   1.00 63.82  ? 89  ALA B C   1 
ATOM   1741 O  O   . ALA B 1 89  ? -51.529 21.741  2.026   1.00 65.61  ? 89  ALA B O   1 
ATOM   1742 C  CB  . ALA B 1 89  ? -48.664 21.574  1.600   1.00 56.82  ? 89  ALA B CB  1 
ATOM   1743 N  N   . ASP B 1 90  ? -51.487 19.508  1.718   1.00 68.06  ? 90  ASP B N   1 
ATOM   1744 C  CA  . ASP B 1 90  ? -52.674 19.277  2.538   1.00 73.77  ? 90  ASP B CA  1 
ATOM   1745 C  C   . ASP B 1 90  ? -52.389 19.687  3.984   1.00 73.37  ? 90  ASP B C   1 
ATOM   1746 O  O   . ASP B 1 90  ? -51.260 20.068  4.321   1.00 72.49  ? 90  ASP B O   1 
ATOM   1747 C  CB  . ASP B 1 90  ? -53.163 17.818  2.455   1.00 77.60  ? 90  ASP B CB  1 
ATOM   1748 C  CG  . ASP B 1 90  ? -52.183 16.814  3.079   1.00 78.00  ? 90  ASP B CG  1 
ATOM   1749 O  OD1 . ASP B 1 90  ? -51.329 17.215  3.901   1.00 78.34  ? 90  ASP B OD1 1 
ATOM   1750 O  OD2 . ASP B 1 90  ? -52.283 15.612  2.748   1.00 76.49  ? 90  ASP B OD2 1 
ATOM   1751 N  N   . LYS B 1 91  ? -53.414 19.606  4.827   1.00 72.54  ? 91  LYS B N   1 
ATOM   1752 C  CA  . LYS B 1 91  ? -53.321 20.052  6.217   1.00 71.05  ? 91  LYS B CA  1 
ATOM   1753 C  C   . LYS B 1 91  ? -52.103 19.475  6.936   1.00 71.57  ? 91  LYS B C   1 
ATOM   1754 O  O   . LYS B 1 91  ? -51.601 20.059  7.896   1.00 70.24  ? 91  LYS B O   1 
ATOM   1755 C  CB  . LYS B 1 91  ? -54.599 19.693  6.979   1.00 66.84  ? 91  LYS B CB  1 
ATOM   1756 C  CG  . LYS B 1 91  ? -54.814 20.507  8.230   1.00 63.09  ? 91  LYS B CG  1 
ATOM   1757 C  CD  . LYS B 1 91  ? -55.899 19.904  9.117   0.00 62.79  ? 91  LYS B CD  1 
ATOM   1758 C  CE  . LYS B 1 91  ? -57.158 19.551  8.332   0.00 62.07  ? 91  LYS B CE  1 
ATOM   1759 N  NZ  . LYS B 1 91  ? -57.099 18.181  7.739   1.00 59.77  ? 91  LYS B NZ  1 
ATOM   1760 N  N   . ASP B 1 92  ? -51.629 18.331  6.456   1.00 73.64  ? 92  ASP B N   1 
ATOM   1761 C  CA  . ASP B 1 92  ? -50.521 17.638  7.089   1.00 76.91  ? 92  ASP B CA  1 
ATOM   1762 C  C   . ASP B 1 92  ? -49.188 17.946  6.439   1.00 77.16  ? 92  ASP B C   1 
ATOM   1763 O  O   . ASP B 1 92  ? -48.263 17.135  6.491   1.00 80.44  ? 92  ASP B O   1 
ATOM   1764 C  CB  . ASP B 1 92  ? -50.762 16.136  7.065   1.00 81.53  ? 92  ASP B CB  1 
ATOM   1765 C  CG  . ASP B 1 92  ? -51.532 15.665  8.271   1.00 85.77  ? 92  ASP B CG  1 
ATOM   1766 O  OD1 . ASP B 1 92  ? -51.379 16.296  9.343   1.00 86.70  ? 92  ASP B OD1 1 
ATOM   1767 O  OD2 . ASP B 1 92  ? -52.285 14.675  8.147   1.00 86.83  ? 92  ASP B OD2 1 
ATOM   1768 N  N   . GLY B 1 93  ? -49.093 19.117  5.824   1.00 74.62  ? 93  GLY B N   1 
ATOM   1769 C  CA  . GLY B 1 93  ? -47.874 19.527  5.153   1.00 70.78  ? 93  GLY B CA  1 
ATOM   1770 C  C   . GLY B 1 93  ? -47.453 18.579  4.047   1.00 67.66  ? 93  GLY B C   1 
ATOM   1771 O  O   . GLY B 1 93  ? -46.363 18.715  3.495   1.00 69.75  ? 93  GLY B O   1 
ATOM   1772 N  N   . VAL B 1 94  ? -48.311 17.619  3.715   1.00 63.06  ? 94  VAL B N   1 
ATOM   1773 C  CA  . VAL B 1 94  ? -47.970 16.624  2.702   1.00 61.12  ? 94  VAL B CA  1 
ATOM   1774 C  C   . VAL B 1 94  ? -48.568 16.951  1.352   1.00 67.77  ? 94  VAL B C   1 
ATOM   1775 O  O   . VAL B 1 94  ? -49.772 16.813  1.142   1.00 72.49  ? 94  VAL B O   1 
ATOM   1776 C  CB  . VAL B 1 94  ? -48.426 15.206  3.083   1.00 55.66  ? 94  VAL B CB  1 
ATOM   1777 C  CG1 . VAL B 1 94  ? -48.310 14.271  1.869   1.00 52.98  ? 94  VAL B CG1 1 
ATOM   1778 C  CG2 . VAL B 1 94  ? -47.638 14.686  4.279   1.00 51.60  ? 94  VAL B CG2 1 
ATOM   1779 N  N   . ALA B 1 95  ? -47.723 17.388  0.431   1.00 61.29  ? 95  ALA B N   1 
ATOM   1780 C  CA  . ALA B 1 95  ? -48.188 17.658  -0.917  1.00 62.21  ? 95  ALA B CA  1 
ATOM   1781 C  C   . ALA B 1 95  ? -48.131 16.398  -1.783  1.00 60.84  ? 95  ALA B C   1 
ATOM   1782 O  O   . ALA B 1 95  ? -47.067 15.823  -1.995  1.00 60.87  ? 95  ALA B O   1 
ATOM   1783 C  CB  . ALA B 1 95  ? -47.385 18.797  -1.545  1.00 59.51  ? 95  ALA B CB  1 
ATOM   1784 N  N   . ASP B 1 96  ? -49.290 15.963  -2.259  1.00 59.40  ? 96  ASP B N   1 
ATOM   1785 C  CA  . ASP B 1 96  ? -49.367 14.877  -3.221  1.00 63.62  ? 96  ASP B CA  1 
ATOM   1786 C  C   . ASP B 1 96  ? -49.164 15.486  -4.600  1.00 61.49  ? 96  ASP B C   1 
ATOM   1787 O  O   . ASP B 1 96  ? -50.050 16.157  -5.108  1.00 67.99  ? 96  ASP B O   1 
ATOM   1788 C  CB  . ASP B 1 96  ? -50.740 14.195  -3.122  1.00 71.08  ? 96  ASP B CB  1 
ATOM   1789 C  CG  . ASP B 1 96  ? -50.917 13.060  -4.123  1.00 77.45  ? 96  ASP B CG  1 
ATOM   1790 O  OD1 . ASP B 1 96  ? -50.480 13.207  -5.289  1.00 79.81  ? 96  ASP B OD1 1 
ATOM   1791 O  OD2 . ASP B 1 96  ? -51.506 12.023  -3.736  1.00 78.76  ? 96  ASP B OD2 1 
ATOM   1792 N  N   . VAL B 1 97  ? -48.003 15.282  -5.209  1.00 55.02  ? 97  VAL B N   1 
ATOM   1793 C  CA  . VAL B 1 97  ? -47.733 15.964  -6.468  1.00 53.27  ? 97  VAL B CA  1 
ATOM   1794 C  C   . VAL B 1 97  ? -48.065 15.131  -7.690  1.00 57.38  ? 97  VAL B C   1 
ATOM   1795 O  O   . VAL B 1 97  ? -47.572 14.018  -7.834  1.00 64.80  ? 97  VAL B O   1 
ATOM   1796 C  CB  . VAL B 1 97  ? -46.269 16.429  -6.588  1.00 48.16  ? 97  VAL B CB  1 
ATOM   1797 C  CG1 . VAL B 1 97  ? -46.045 17.043  -7.938  1.00 46.85  ? 97  VAL B CG1 1 
ATOM   1798 C  CG2 . VAL B 1 97  ? -45.937 17.434  -5.520  1.00 41.60  ? 97  VAL B CG2 1 
ATOM   1799 N  N   . SER B 1 98  ? -48.895 15.677  -8.572  1.00 55.17  ? 98  SER B N   1 
ATOM   1800 C  CA  . SER B 1 98  ? -49.098 15.088  -9.896  1.00 60.74  ? 98  SER B CA  1 
ATOM   1801 C  C   . SER B 1 98  ? -49.342 16.180  -10.935 1.00 60.57  ? 98  SER B C   1 
ATOM   1802 O  O   . SER B 1 98  ? -50.165 17.074  -10.734 1.00 60.28  ? 98  SER B O   1 
ATOM   1803 C  CB  . SER B 1 98  ? -50.247 14.075  -9.898  1.00 64.67  ? 98  SER B CB  1 
ATOM   1804 O  OG  . SER B 1 98  ? -50.423 13.516  -11.190 1.00 65.32  ? 98  SER B OG  1 
ATOM   1805 N  N   . ILE B 1 99  ? -48.614 16.099  -12.042 1.00 58.48  ? 99  ILE B N   1 
ATOM   1806 C  CA  . ILE B 1 99  ? -48.614 17.137  -13.059 1.00 59.30  ? 99  ILE B CA  1 
ATOM   1807 C  C   . ILE B 1 99  ? -48.242 16.493  -14.376 1.00 63.22  ? 99  ILE B C   1 
ATOM   1808 O  O   . ILE B 1 99  ? -47.502 15.513  -14.398 1.00 63.93  ? 99  ILE B O   1 
ATOM   1809 C  CB  . ILE B 1 99  ? -47.563 18.225  -12.752 1.00 60.79  ? 99  ILE B CB  1 
ATOM   1810 C  CG1 . ILE B 1 99  ? -47.938 19.020  -11.500 1.00 61.47  ? 99  ILE B CG1 1 
ATOM   1811 C  CG2 . ILE B 1 99  ? -47.381 19.158  -13.942 1.00 61.50  ? 99  ILE B CG2 1 
ATOM   1812 C  CD1 . ILE B 1 99  ? -46.821 19.920  -10.999 1.00 60.60  ? 99  ILE B CD1 1 
ATOM   1813 N  N   . GLU B 1 100 ? -48.762 17.030  -15.472 1.00 66.91  ? 100 GLU B N   1 
ATOM   1814 C  CA  . GLU B 1 100 ? -48.355 16.584  -16.795 1.00 70.93  ? 100 GLU B CA  1 
ATOM   1815 C  C   . GLU B 1 100 ? -48.054 17.808  -17.648 1.00 74.51  ? 100 GLU B C   1 
ATOM   1816 O  O   . GLU B 1 100 ? -48.756 18.086  -18.625 1.00 81.10  ? 100 GLU B O   1 
ATOM   1817 C  CB  . GLU B 1 100 ? -49.427 15.721  -17.435 1.00 70.74  ? 100 GLU B CB  1 
ATOM   1818 N  N   . ASP B 1 101 ? -47.019 18.547  -17.249 1.00 65.17  ? 101 ASP B N   1 
ATOM   1819 C  CA  . ASP B 1 101 ? -46.552 19.708  -17.987 1.00 59.83  ? 101 ASP B CA  1 
ATOM   1820 C  C   . ASP B 1 101 ? -45.923 19.257  -19.298 1.00 61.00  ? 101 ASP B C   1 
ATOM   1821 O  O   . ASP B 1 101 ? -45.130 18.331  -19.317 1.00 61.09  ? 101 ASP B O   1 
ATOM   1822 C  CB  . ASP B 1 101 ? -45.519 20.469  -17.143 1.00 55.61  ? 101 ASP B CB  1 
ATOM   1823 C  CG  . ASP B 1 101 ? -45.330 21.920  -17.590 1.00 53.50  ? 101 ASP B CG  1 
ATOM   1824 O  OD1 . ASP B 1 101 ? -44.186 22.300  -17.907 1.00 52.96  ? 101 ASP B OD1 1 
ATOM   1825 O  OD2 . ASP B 1 101 ? -46.316 22.692  -17.604 1.00 53.89  ? 101 ASP B OD2 1 
ATOM   1826 N  N   . SER B 1 102 ? -46.278 19.903  -20.400 1.00 68.52  ? 102 SER B N   1 
ATOM   1827 C  CA  . SER B 1 102 ? -45.603 19.626  -21.669 1.00 76.59  ? 102 SER B CA  1 
ATOM   1828 C  C   . SER B 1 102 ? -44.685 20.787  -22.055 1.00 79.33  ? 102 SER B C   1 
ATOM   1829 O  O   . SER B 1 102 ? -44.034 20.779  -23.108 1.00 77.84  ? 102 SER B O   1 
ATOM   1830 C  CB  . SER B 1 102 ? -46.615 19.323  -22.777 1.00 77.21  ? 102 SER B CB  1 
ATOM   1831 O  OG  . SER B 1 102 ? -46.544 17.959  -23.164 1.00 75.19  ? 102 SER B OG  1 
ATOM   1832 N  N   . VAL B 1 103 ? -44.640 21.780  -21.172 1.00 80.55  ? 103 VAL B N   1 
ATOM   1833 C  CA  . VAL B 1 103 ? -43.783 22.941  -21.339 1.00 78.92  ? 103 VAL B CA  1 
ATOM   1834 C  C   . VAL B 1 103 ? -42.375 22.600  -20.840 1.00 78.10  ? 103 VAL B C   1 
ATOM   1835 O  O   . VAL B 1 103 ? -41.413 23.317  -21.124 1.00 81.06  ? 103 VAL B O   1 
ATOM   1836 C  CB  . VAL B 1 103 ? -44.348 24.166  -20.571 1.00 58.16  ? 103 VAL B CB  1 
ATOM   1837 C  CG1 . VAL B 1 103 ? -43.678 25.443  -21.038 1.00 61.26  ? 103 VAL B CG1 1 
ATOM   1838 C  CG2 . VAL B 1 103 ? -45.867 24.265  -20.742 1.00 50.87  ? 103 VAL B CG2 1 
ATOM   1839 N  N   . ILE B 1 104 ? -42.263 21.504  -20.090 1.00 74.87  ? 104 ILE B N   1 
ATOM   1840 C  CA  . ILE B 1 104 ? -40.959 20.969  -19.680 1.00 71.30  ? 104 ILE B CA  1 
ATOM   1841 C  C   . ILE B 1 104 ? -40.759 19.531  -20.149 1.00 67.40  ? 104 ILE B C   1 
ATOM   1842 O  O   . ILE B 1 104 ? -41.726 18.811  -20.378 1.00 65.91  ? 104 ILE B O   1 
ATOM   1843 C  CB  . ILE B 1 104 ? -40.700 21.083  -18.148 1.00 53.59  ? 104 ILE B CB  1 
ATOM   1844 C  CG1 . ILE B 1 104 ? -41.829 20.462  -17.330 1.00 51.27  ? 104 ILE B CG1 1 
ATOM   1845 C  CG2 . ILE B 1 104 ? -40.552 22.531  -17.752 1.00 54.96  ? 104 ILE B CG2 1 
ATOM   1846 C  CD1 . ILE B 1 104 ? -41.668 19.021  -17.045 1.00 46.96  ? 104 ILE B CD1 1 
ATOM   1847 N  N   . SER B 1 105 ? -39.494 19.134  -20.302 1.00 79.43  ? 105 SER B N   1 
ATOM   1848 C  CA  . SER B 1 105 ? -39.131 17.797  -20.793 1.00 76.22  ? 105 SER B CA  1 
ATOM   1849 C  C   . SER B 1 105 ? -37.819 17.277  -20.201 1.00 75.37  ? 105 SER B C   1 
ATOM   1850 O  O   . SER B 1 105 ? -37.061 18.028  -19.586 1.00 76.41  ? 105 SER B O   1 
ATOM   1851 C  CB  . SER B 1 105 ? -39.043 17.787  -22.324 1.00 74.37  ? 105 SER B CB  1 
ATOM   1852 O  OG  . SER B 1 105 ? -38.380 18.946  -22.806 1.00 71.82  ? 105 SER B OG  1 
ATOM   1853 N  N   . LEU B 1 106 ? -37.562 15.984  -20.397 1.00 72.73  ? 106 LEU B N   1 
ATOM   1854 C  CA  . LEU B 1 106 ? -36.365 15.336  -19.871 1.00 68.42  ? 106 LEU B CA  1 
ATOM   1855 C  C   . LEU B 1 106 ? -35.297 15.223  -20.954 1.00 69.58  ? 106 LEU B C   1 
ATOM   1856 O  O   . LEU B 1 106 ? -34.177 14.753  -20.710 1.00 67.46  ? 106 LEU B O   1 
ATOM   1857 C  CB  . LEU B 1 106 ? -36.697 13.942  -19.337 1.00 65.03  ? 106 LEU B CB  1 
ATOM   1858 C  CG  . LEU B 1 106 ? -37.870 13.811  -18.370 1.00 61.41  ? 106 LEU B CG  1 
ATOM   1859 C  CD1 . LEU B 1 106 ? -37.966 12.373  -17.913 1.00 59.88  ? 106 LEU B CD1 1 
ATOM   1860 C  CD2 . LEU B 1 106 ? -37.721 14.740  -17.185 1.00 58.76  ? 106 LEU B CD2 1 
ATOM   1861 N  N   . SER B 1 107 ? -35.654 15.654  -22.154 1.00 72.10  ? 107 SER B N   1 
ATOM   1862 C  CA  . SER B 1 107 ? -34.747 15.599  -23.282 1.00 76.87  ? 107 SER B CA  1 
ATOM   1863 C  C   . SER B 1 107 ? -35.174 16.624  -24.308 1.00 82.62  ? 107 SER B C   1 
ATOM   1864 O  O   . SER B 1 107 ? -35.984 16.329  -25.192 1.00 85.71  ? 107 SER B O   1 
ATOM   1865 C  CB  . SER B 1 107 ? -34.757 14.207  -23.914 1.00 78.78  ? 107 SER B CB  1 
ATOM   1866 O  OG  . SER B 1 107 ? -34.784 14.303  -25.331 1.00 81.61  ? 107 SER B OG  1 
ATOM   1867 N  N   . GLY B 1 108 ? -34.638 17.830  -24.181 1.00 83.28  ? 108 GLY B N   1 
ATOM   1868 C  CA  . GLY B 1 108 ? -34.895 18.874  -25.152 1.00 88.65  ? 108 GLY B CA  1 
ATOM   1869 C  C   . GLY B 1 108 ? -33.891 19.995  -25.008 1.00 90.61  ? 108 GLY B C   1 
ATOM   1870 O  O   . GLY B 1 108 ? -32.862 19.837  -24.350 1.00 90.29  ? 108 GLY B O   1 
ATOM   1871 N  N   . ASP B 1 109 ? -34.177 21.128  -25.637 1.00 91.36  ? 109 ASP B N   1 
ATOM   1872 C  CA  . ASP B 1 109 ? -33.441 22.341  -25.336 1.00 89.58  ? 109 ASP B CA  1 
ATOM   1873 C  C   . ASP B 1 109 ? -34.035 22.869  -24.038 1.00 86.66  ? 109 ASP B C   1 
ATOM   1874 O  O   . ASP B 1 109 ? -33.541 23.825  -23.442 1.00 85.97  ? 109 ASP B O   1 
ATOM   1875 C  CB  . ASP B 1 109 ? -33.561 23.363  -26.469 1.00 92.63  ? 109 ASP B CB  1 
ATOM   1876 C  CG  . ASP B 1 109 ? -32.725 22.987  -27.687 1.00 92.77  ? 109 ASP B CG  1 
ATOM   1877 O  OD1 . ASP B 1 109 ? -31.479 23.017  -27.585 1.00 88.39  ? 109 ASP B OD1 1 
ATOM   1878 O  OD2 . ASP B 1 109 ? -33.315 22.675  -28.749 1.00 95.85  ? 109 ASP B OD2 1 
ATOM   1879 N  N   . HIS B 1 110 ? -35.110 22.217  -23.610 1.00 85.88  ? 110 HIS B N   1 
ATOM   1880 C  CA  . HIS B 1 110 ? -35.746 22.502  -22.331 1.00 83.14  ? 110 HIS B CA  1 
ATOM   1881 C  C   . HIS B 1 110 ? -35.493 21.355  -21.364 1.00 81.05  ? 110 HIS B C   1 
ATOM   1882 O  O   . HIS B 1 110 ? -36.250 21.160  -20.408 1.00 81.44  ? 110 HIS B O   1 
ATOM   1883 C  CB  . HIS B 1 110 ? -37.249 22.686  -22.519 0.00 84.00  ? 110 HIS B CB  1 
ATOM   1884 C  CG  . HIS B 1 110 ? -37.611 23.848  -23.380 1.00 85.06  ? 110 HIS B CG  1 
ATOM   1885 N  ND1 . HIS B 1 110 ? -36.663 24.709  -23.909 1.00 85.54  ? 110 HIS B ND1 1 
ATOM   1886 C  CD2 . HIS B 1 110 ? -38.807 24.313  -23.808 1.00 86.71  ? 110 HIS B CD2 1 
ATOM   1887 C  CE1 . HIS B 1 110 ? -37.261 25.640  -24.617 1.00 87.34  ? 110 HIS B CE1 1 
ATOM   1888 N  NE2 . HIS B 1 110 ? -38.569 25.425  -24.574 1.00 88.52  ? 110 HIS B NE2 1 
ATOM   1889 N  N   . CYS B 1 111 ? -34.442 20.584  -21.634 1.00 77.55  ? 111 CYS B N   1 
ATOM   1890 C  CA  . CYS B 1 111 ? -34.049 19.485  -20.764 1.00 72.28  ? 111 CYS B CA  1 
ATOM   1891 C  C   . CYS B 1 111 ? -34.011 19.976  -19.323 1.00 70.77  ? 111 CYS B C   1 
ATOM   1892 O  O   . CYS B 1 111 ? -33.203 20.839  -18.979 1.00 69.22  ? 111 CYS B O   1 
ATOM   1893 C  CB  . CYS B 1 111 ? -32.676 18.946  -21.178 1.00 70.20  ? 111 CYS B CB  1 
ATOM   1894 S  SG  . CYS B 1 111 ? -32.011 17.598  -20.139 1.00 98.48  ? 111 CYS B SG  1 
ATOM   1895 N  N   . ILE B 1 112 ? -34.900 19.439  -18.491 1.00 71.89  ? 112 ILE B N   1 
ATOM   1896 C  CA  . ILE B 1 112 ? -34.921 19.767  -17.066 1.00 70.31  ? 112 ILE B CA  1 
ATOM   1897 C  C   . ILE B 1 112 ? -33.862 18.973  -16.302 1.00 65.75  ? 112 ILE B C   1 
ATOM   1898 O  O   . ILE B 1 112 ? -33.703 19.147  -15.096 1.00 64.97  ? 112 ILE B O   1 
ATOM   1899 C  CB  . ILE B 1 112 ? -36.309 19.509  -16.471 1.00 70.24  ? 112 ILE B CB  1 
ATOM   1900 N  N   . ILE B 1 113 ? -33.141 18.103  -17.007 1.00 63.27  ? 113 ILE B N   1 
ATOM   1901 C  CA  . ILE B 1 113 ? -32.154 17.235  -16.365 1.00 62.06  ? 113 ILE B CA  1 
ATOM   1902 C  C   . ILE B 1 113 ? -30.858 17.973  -16.041 1.00 60.01  ? 113 ILE B C   1 
ATOM   1903 O  O   . ILE B 1 113 ? -30.341 18.746  -16.852 1.00 60.72  ? 113 ILE B O   1 
ATOM   1904 C  CB  . ILE B 1 113 ? -31.816 15.995  -17.217 1.00 57.57  ? 113 ILE B CB  1 
ATOM   1905 C  CG1 . ILE B 1 113 ? -33.089 15.255  -17.631 1.00 54.07  ? 113 ILE B CG1 1 
ATOM   1906 C  CG2 . ILE B 1 113 ? -30.890 15.086  -16.444 1.00 55.62  ? 113 ILE B CG2 1 
ATOM   1907 C  CD1 . ILE B 1 113 ? -33.188 13.866  -17.086 1.00 51.71  ? 113 ILE B CD1 1 
ATOM   1908 N  N   . GLY B 1 114 ? -30.342 17.728  -14.845 1.00 53.45  ? 114 GLY B N   1 
ATOM   1909 C  CA  . GLY B 1 114 ? -29.178 18.445  -14.372 1.00 51.88  ? 114 GLY B CA  1 
ATOM   1910 C  C   . GLY B 1 114 ? -29.496 19.783  -13.717 1.00 49.86  ? 114 GLY B C   1 
ATOM   1911 O  O   . GLY B 1 114 ? -28.578 20.519  -13.353 1.00 40.19  ? 114 GLY B O   1 
ATOM   1912 N  N   . ARG B 1 115 ? -30.788 20.088  -13.558 1.00 46.52  ? 115 ARG B N   1 
ATOM   1913 C  CA  . ARG B 1 115 ? -31.238 21.347  -12.949 1.00 45.64  ? 115 ARG B CA  1 
ATOM   1914 C  C   . ARG B 1 115 ? -31.737 21.140  -11.517 1.00 46.52  ? 115 ARG B C   1 
ATOM   1915 O  O   . ARG B 1 115 ? -31.754 20.012  -11.024 1.00 44.53  ? 115 ARG B O   1 
ATOM   1916 C  CB  . ARG B 1 115 ? -32.315 21.999  -13.808 1.00 47.53  ? 115 ARG B CB  1 
ATOM   1917 C  CG  . ARG B 1 115 ? -31.801 23.111  -14.707 1.00 52.91  ? 115 ARG B CG  1 
ATOM   1918 C  CD  . ARG B 1 115 ? -31.614 22.717  -16.168 1.00 52.51  ? 115 ARG B CD  1 
ATOM   1919 N  NE  . ARG B 1 115 ? -30.936 23.788  -16.901 1.00 52.76  ? 115 ARG B NE  1 
ATOM   1920 C  CZ  . ARG B 1 115 ? -30.704 23.776  -18.209 1.00 52.74  ? 115 ARG B CZ  1 
ATOM   1921 N  NH1 . ARG B 1 115 ? -31.120 22.759  -18.950 1.00 55.36  ? 115 ARG B NH1 1 
ATOM   1922 N  NH2 . ARG B 1 115 ? -30.062 24.784  -18.781 1.00 49.10  ? 115 ARG B NH2 1 
ATOM   1923 N  N   . THR B 1 116 ? -32.135 22.214  -10.845 1.00 40.58  ? 116 THR B N   1 
ATOM   1924 C  CA  . THR B 1 116 ? -32.610 22.096  -9.466  1.00 56.10  ? 116 THR B CA  1 
ATOM   1925 C  C   . THR B 1 116 ? -34.099 22.351  -9.307  1.00 55.06  ? 116 THR B C   1 
ATOM   1926 O  O   . THR B 1 116 ? -34.579 23.443  -9.560  1.00 54.74  ? 116 THR B O   1 
ATOM   1927 C  CB  . THR B 1 116 ? -31.882 23.046  -8.502  1.00 57.49  ? 116 THR B CB  1 
ATOM   1928 O  OG1 . THR B 1 116 ? -30.481 22.748  -8.493  1.00 56.97  ? 116 THR B OG1 1 
ATOM   1929 C  CG2 . THR B 1 116 ? -32.452 22.903  -7.076  1.00 37.48  ? 116 THR B CG2 1 
ATOM   1930 N  N   . LEU B 1 117 ? -34.828 21.336  -8.866  1.00 54.75  ? 117 LEU B N   1 
ATOM   1931 C  CA  . LEU B 1 117 ? -36.220 21.509  -8.517  1.00 49.55  ? 117 LEU B CA  1 
ATOM   1932 C  C   . LEU B 1 117 ? -36.261 22.240  -7.184  1.00 53.07  ? 117 LEU B C   1 
ATOM   1933 O  O   . LEU B 1 117 ? -35.476 21.934  -6.278  1.00 54.82  ? 117 LEU B O   1 
ATOM   1934 C  CB  . LEU B 1 117 ? -36.889 20.147  -8.395  1.00 46.67  ? 117 LEU B CB  1 
ATOM   1935 C  CG  . LEU B 1 117 ? -38.390 20.125  -8.130  1.00 44.68  ? 117 LEU B CG  1 
ATOM   1936 C  CD1 . LEU B 1 117 ? -39.081 21.103  -9.058  1.00 44.25  ? 117 LEU B CD1 1 
ATOM   1937 C  CD2 . LEU B 1 117 ? -38.908 18.706  -8.325  1.00 45.49  ? 117 LEU B CD2 1 
ATOM   1938 N  N   . VAL B 1 118 ? -37.173 23.202  -7.059  1.00 54.13  ? 118 VAL B N   1 
ATOM   1939 C  CA  . VAL B 1 118 ? -37.269 24.012  -5.849  1.00 51.21  ? 118 VAL B CA  1 
ATOM   1940 C  C   . VAL B 1 118 ? -38.703 24.105  -5.364  1.00 53.57  ? 118 VAL B C   1 
ATOM   1941 O  O   . VAL B 1 118 ? -39.628 24.232  -6.165  1.00 55.86  ? 118 VAL B O   1 
ATOM   1942 C  CB  . VAL B 1 118 ? -36.732 25.454  -6.081  1.00 47.48  ? 118 VAL B CB  1 
ATOM   1943 C  CG1 . VAL B 1 118 ? -36.952 26.331  -4.844  1.00 50.97  ? 118 VAL B CG1 1 
ATOM   1944 C  CG2 . VAL B 1 118 ? -35.270 25.435  -6.439  1.00 43.45  ? 118 VAL B CG2 1 
ATOM   1945 N  N   . VAL B 1 119 ? -38.887 24.042  -4.050  1.00 53.00  ? 119 VAL B N   1 
ATOM   1946 C  CA  . VAL B 1 119 ? -40.178 24.381  -3.458  1.00 54.60  ? 119 VAL B CA  1 
ATOM   1947 C  C   . VAL B 1 119 ? -40.050 25.504  -2.441  1.00 55.72  ? 119 VAL B C   1 
ATOM   1948 O  O   . VAL B 1 119 ? -39.118 25.522  -1.637  1.00 53.33  ? 119 VAL B O   1 
ATOM   1949 C  CB  . VAL B 1 119 ? -40.833 23.189  -2.779  1.00 55.62  ? 119 VAL B CB  1 
ATOM   1950 C  CG1 . VAL B 1 119 ? -41.395 22.256  -3.821  1.00 56.86  ? 119 VAL B CG1 1 
ATOM   1951 C  CG2 . VAL B 1 119 ? -39.824 22.485  -1.858  1.00 53.73  ? 119 VAL B CG2 1 
ATOM   1952 N  N   . HIS B 1 120 ? -41.030 26.409  -2.457  1.00 60.95  ? 120 HIS B N   1 
ATOM   1953 C  CA  . HIS B 1 120 ? -40.913 27.716  -1.810  1.00 59.30  ? 120 HIS B CA  1 
ATOM   1954 C  C   . HIS B 1 120 ? -41.743 27.977  -0.564  1.00 61.97  ? 120 HIS B C   1 
ATOM   1955 O  O   . HIS B 1 120 ? -42.638 27.216  -0.206  1.00 66.78  ? 120 HIS B O   1 
ATOM   1956 C  CB  . HIS B 1 120 ? -41.214 28.806  -2.826  1.00 57.11  ? 120 HIS B CB  1 
ATOM   1957 C  CG  . HIS B 1 120 ? -40.085 29.058  -3.767  1.00 57.34  ? 120 HIS B CG  1 
ATOM   1958 N  ND1 . HIS B 1 120 ? -39.106 29.994  -3.518  1.00 56.79  ? 120 HIS B ND1 1 
ATOM   1959 C  CD2 . HIS B 1 120 ? -39.762 28.478  -4.945  1.00 56.57  ? 120 HIS B CD2 1 
ATOM   1960 C  CE1 . HIS B 1 120 ? -38.234 29.986  -4.507  1.00 56.44  ? 120 HIS B CE1 1 
ATOM   1961 N  NE2 . HIS B 1 120 ? -38.609 29.075  -5.384  1.00 55.42  ? 120 HIS B NE2 1 
ATOM   1962 N  N   . GLU B 1 121 ? -41.413 29.090  0.076   1.00 66.26  ? 121 GLU B N   1 
ATOM   1963 C  CA  . GLU B 1 121 ? -42.092 29.582  1.255   1.00 63.70  ? 121 GLU B CA  1 
ATOM   1964 C  C   . GLU B 1 121 ? -43.581 29.717  0.971   1.00 62.50  ? 121 GLU B C   1 
ATOM   1965 O  O   . GLU B 1 121 ? -44.417 29.085  1.620   1.00 60.04  ? 121 GLU B O   1 
ATOM   1966 C  CB  . GLU B 1 121 ? -41.499 30.953  1.604   1.00 65.77  ? 121 GLU B CB  1 
ATOM   1967 C  CG  . GLU B 1 121 ? -41.778 31.482  3.005   1.00 68.78  ? 121 GLU B CG  1 
ATOM   1968 C  CD  . GLU B 1 121 ? -40.970 32.741  3.308   1.00 72.91  ? 121 GLU B CD  1 
ATOM   1969 O  OE1 . GLU B 1 121 ? -39.835 32.853  2.796   1.00 75.11  ? 121 GLU B OE1 1 
ATOM   1970 O  OE2 . GLU B 1 121 ? -41.467 33.626  4.042   1.00 73.28  ? 121 GLU B OE2 1 
ATOM   1971 N  N   . LYS B 1 122 ? -43.903 30.531  -0.027  1.00 64.39  ? 122 LYS B N   1 
ATOM   1972 C  CA  . LYS B 1 122 ? -45.278 30.961  -0.246  1.00 65.87  ? 122 LYS B CA  1 
ATOM   1973 C  C   . LYS B 1 122 ? -45.824 30.512  -1.594  1.00 63.93  ? 122 LYS B C   1 
ATOM   1974 O  O   . LYS B 1 122 ? -45.257 29.646  -2.261  1.00 60.95  ? 122 LYS B O   1 
ATOM   1975 C  CB  . LYS B 1 122 ? -45.377 32.493  -0.153  1.00 66.47  ? 122 LYS B CB  1 
ATOM   1976 C  CG  . LYS B 1 122 ? -44.946 33.092  1.183   1.00 65.84  ? 122 LYS B CG  1 
ATOM   1977 C  CD  . LYS B 1 122 ? -45.026 34.610  1.165   0.00 68.19  ? 122 LYS B CD  1 
ATOM   1978 C  CE  . LYS B 1 122 ? -44.007 35.201  0.206   0.00 69.03  ? 122 LYS B CE  1 
ATOM   1979 N  NZ  . LYS B 1 122 ? -44.060 36.688  0.178   0.00 71.03  ? 122 LYS B NZ  1 
ATOM   1980 N  N   . ALA B 1 123 ? -46.931 31.133  -1.984  1.00 63.74  ? 123 ALA B N   1 
ATOM   1981 C  CA  . ALA B 1 123 ? -47.590 30.857  -3.248  1.00 65.09  ? 123 ALA B CA  1 
ATOM   1982 C  C   . ALA B 1 123 ? -46.903 31.545  -4.421  1.00 68.48  ? 123 ALA B C   1 
ATOM   1983 O  O   . ALA B 1 123 ? -46.486 32.711  -4.333  1.00 69.62  ? 123 ALA B O   1 
ATOM   1984 C  CB  . ALA B 1 123 ? -49.042 31.295  -3.176  1.00 66.01  ? 123 ALA B CB  1 
ATOM   1985 N  N   . ASP B 1 124 ? -46.784 30.810  -5.520  1.00 65.25  ? 124 ASP B N   1 
ATOM   1986 C  CA  . ASP B 1 124 ? -46.386 31.398  -6.781  1.00 60.99  ? 124 ASP B CA  1 
ATOM   1987 C  C   . ASP B 1 124 ? -47.526 32.306  -7.203  1.00 63.46  ? 124 ASP B C   1 
ATOM   1988 O  O   . ASP B 1 124 ? -48.647 31.836  -7.440  1.00 61.98  ? 124 ASP B O   1 
ATOM   1989 C  CB  . ASP B 1 124 ? -46.175 30.301  -7.820  1.00 62.01  ? 124 ASP B CB  1 
ATOM   1990 C  CG  . ASP B 1 124 ? -45.538 30.811  -9.091  1.00 65.16  ? 124 ASP B CG  1 
ATOM   1991 O  OD1 . ASP B 1 124 ? -45.986 31.855  -9.606  1.00 71.61  ? 124 ASP B OD1 1 
ATOM   1992 O  OD2 . ASP B 1 124 ? -44.584 30.167  -9.575  1.00 61.56  ? 124 ASP B OD2 1 
ATOM   1993 N  N   . ASP B 1 125 ? -47.237 33.607  -7.270  1.00 67.20  ? 125 ASP B N   1 
ATOM   1994 C  CA  . ASP B 1 125 ? -48.204 34.636  -7.659  1.00 70.17  ? 125 ASP B CA  1 
ATOM   1995 C  C   . ASP B 1 125 ? -48.735 34.374  -9.058  1.00 70.76  ? 125 ASP B C   1 
ATOM   1996 O  O   . ASP B 1 125 ? -49.624 35.076  -9.546  1.00 70.64  ? 125 ASP B O   1 
ATOM   1997 C  CB  . ASP B 1 125 ? -47.528 36.016  -7.648  1.00 72.96  ? 125 ASP B CB  1 
ATOM   1998 C  CG  . ASP B 1 125 ? -48.272 37.024  -6.798  1.00 76.58  ? 125 ASP B CG  1 
ATOM   1999 O  OD1 . ASP B 1 125 ? -49.497 36.863  -6.616  1.00 81.34  ? 125 ASP B OD1 1 
ATOM   2000 O  OD2 . ASP B 1 125 ? -47.638 37.977  -6.310  1.00 74.23  ? 125 ASP B OD2 1 
ATOM   2001 N  N   . LEU B 1 126 ? -48.170 33.359  -9.701  1.00 71.17  ? 126 LEU B N   1 
ATOM   2002 C  CA  . LEU B 1 126 ? -48.425 33.086  -11.106 1.00 72.52  ? 126 LEU B CA  1 
ATOM   2003 C  C   . LEU B 1 126 ? -48.271 34.363  -11.936 1.00 77.43  ? 126 LEU B C   1 
ATOM   2004 O  O   . LEU B 1 126 ? -48.704 34.425  -13.086 1.00 79.41  ? 126 LEU B O   1 
ATOM   2005 C  CB  . LEU B 1 126 ? -49.791 32.435  -11.296 1.00 71.64  ? 126 LEU B CB  1 
ATOM   2006 C  CG  . LEU B 1 126 ? -50.076 31.259  -10.357 1.00 69.57  ? 126 LEU B CG  1 
ATOM   2007 C  CD1 . LEU B 1 126 ? -51.506 30.732  -10.554 1.00 70.16  ? 126 LEU B CD1 1 
ATOM   2008 C  CD2 . LEU B 1 126 ? -49.051 30.128  -10.512 1.00 67.39  ? 126 LEU B CD2 1 
ATOM   2009 N  N   . GLY B 1 127 ? -47.639 35.373  -11.336 1.00 79.27  ? 127 GLY B N   1 
ATOM   2010 C  CA  . GLY B 1 127 ? -47.213 36.556  -12.058 1.00 84.13  ? 127 GLY B CA  1 
ATOM   2011 C  C   . GLY B 1 127 ? -48.170 37.733  -12.017 1.00 90.84  ? 127 GLY B C   1 
ATOM   2012 O  O   . GLY B 1 127 ? -47.809 38.837  -12.405 1.00 94.33  ? 127 GLY B O   1 
ATOM   2013 N  N   . LYS B 1 128 ? -49.392 37.501  -11.551 1.00 91.19  ? 128 LYS B N   1 
ATOM   2014 C  CA  . LYS B 1 128 ? -50.402 38.545  -11.491 1.00 91.66  ? 128 LYS B CA  1 
ATOM   2015 C  C   . LYS B 1 128 ? -50.391 39.233  -10.122 1.00 90.70  ? 128 LYS B C   1 
ATOM   2016 O  O   . LYS B 1 128 ? -51.441 39.601  -9.592  1.00 92.24  ? 128 LYS B O   1 
ATOM   2017 C  CB  . LYS B 1 128 ? -51.783 37.940  -11.763 1.00 93.95  ? 128 LYS B CB  1 
ATOM   2018 C  CG  . LYS B 1 128 ? -51.795 36.849  -12.828 1.00 94.16  ? 128 LYS B CG  1 
ATOM   2019 C  CD  . LYS B 1 128 ? -51.329 37.381  -14.172 1.00 97.88  ? 128 LYS B CD  1 
ATOM   2020 C  CE  . LYS B 1 128 ? -51.368 36.295  -15.237 1.00 98.77  ? 128 LYS B CE  1 
ATOM   2021 N  NZ  . LYS B 1 128 ? -51.067 36.848  -16.586 1.00 100.93 ? 128 LYS B NZ  1 
ATOM   2022 N  N   . GLY B 1 129 ? -49.197 39.412  -9.560  1.00 88.44  ? 129 GLY B N   1 
ATOM   2023 C  CA  . GLY B 1 129 ? -49.036 39.924  -8.205  1.00 84.35  ? 129 GLY B CA  1 
ATOM   2024 C  C   . GLY B 1 129 ? -49.044 41.436  -8.032  1.00 81.10  ? 129 GLY B C   1 
ATOM   2025 O  O   . GLY B 1 129 ? -49.113 41.936  -6.908  1.00 78.15  ? 129 GLY B O   1 
ATOM   2026 N  N   . GLY B 1 130 ? -48.963 42.169  -9.134  1.00 80.57  ? 130 GLY B N   1 
ATOM   2027 C  CA  . GLY B 1 130 ? -49.047 43.613  -9.065  1.00 85.97  ? 130 GLY B CA  1 
ATOM   2028 C  C   . GLY B 1 130 ? -47.748 44.265  -8.632  1.00 88.32  ? 130 GLY B C   1 
ATOM   2029 O  O   . GLY B 1 130 ? -47.753 45.361  -8.072  1.00 89.17  ? 130 GLY B O   1 
ATOM   2030 N  N   . ASN B 1 131 ? -46.632 43.586  -8.879  1.00 87.56  ? 131 ASN B N   1 
ATOM   2031 C  CA  . ASN B 1 131 ? -45.318 44.192  -8.670  1.00 89.47  ? 131 ASN B CA  1 
ATOM   2032 C  C   . ASN B 1 131 ? -44.162 43.489  -9.381  1.00 85.85  ? 131 ASN B C   1 
ATOM   2033 O  O   . ASN B 1 131 ? -44.335 42.435  -9.993  1.00 82.89  ? 131 ASN B O   1 
ATOM   2034 C  CB  . ASN B 1 131 ? -45.014 44.413  -7.180  1.00 90.68  ? 131 ASN B CB  1 
ATOM   2035 C  CG  . ASN B 1 131 ? -44.867 43.122  -6.402  1.00 89.25  ? 131 ASN B CG  1 
ATOM   2036 O  OD1 . ASN B 1 131 ? -44.575 42.067  -6.964  1.00 89.01  ? 131 ASN B OD1 1 
ATOM   2037 N  ND2 . ASN B 1 131 ? -45.066 43.205  -5.092  1.00 88.36  ? 131 ASN B ND2 1 
ATOM   2038 N  N   . GLU B 1 132 ? -42.991 44.110  -9.305  1.00 86.12  ? 132 GLU B N   1 
ATOM   2039 C  CA  . GLU B 1 132 ? -41.796 43.638  -9.986  1.00 86.05  ? 132 GLU B CA  1 
ATOM   2040 C  C   . GLU B 1 132 ? -41.423 42.243  -9.550  1.00 87.59  ? 132 GLU B C   1 
ATOM   2041 O  O   . GLU B 1 132 ? -41.056 41.404  -10.372 1.00 89.44  ? 132 GLU B O   1 
ATOM   2042 C  CB  . GLU B 1 132 ? -40.626 44.570  -9.690  1.00 86.56  ? 132 GLU B CB  1 
ATOM   2043 C  CG  . GLU B 1 132 ? -39.290 44.057  -10.188 1.00 88.55  ? 132 GLU B CG  1 
ATOM   2044 C  CD  . GLU B 1 132 ? -39.210 44.001  -11.705 1.00 92.08  ? 132 GLU B CD  1 
ATOM   2045 O  OE1 . GLU B 1 132 ? -40.259 44.180  -12.368 1.00 93.71  ? 132 GLU B OE1 1 
ATOM   2046 O  OE2 . GLU B 1 132 ? -38.093 43.782  -12.232 1.00 91.52  ? 132 GLU B OE2 1 
ATOM   2047 N  N   . GLU B 1 133 ? -41.506 42.009  -8.244  1.00 87.63  ? 133 GLU B N   1 
ATOM   2048 C  CA  . GLU B 1 133 ? -41.119 40.732  -7.658  1.00 85.87  ? 133 GLU B CA  1 
ATOM   2049 C  C   . GLU B 1 133 ? -41.915 39.564  -8.270  1.00 85.32  ? 133 GLU B C   1 
ATOM   2050 O  O   . GLU B 1 133 ? -41.335 38.559  -8.693  1.00 82.88  ? 133 GLU B O   1 
ATOM   2051 C  CB  . GLU B 1 133 ? -41.283 40.797  -6.135  1.00 86.45  ? 133 GLU B CB  1 
ATOM   2052 C  CG  . GLU B 1 133 ? -40.828 39.563  -5.382  1.00 86.74  ? 133 GLU B CG  1 
ATOM   2053 C  CD  . GLU B 1 133 ? -39.342 39.319  -5.495  1.00 88.87  ? 133 GLU B CD  1 
ATOM   2054 O  OE1 . GLU B 1 133 ? -38.593 40.310  -5.622  1.00 88.48  ? 133 GLU B OE1 1 
ATOM   2055 O  OE2 . GLU B 1 133 ? -38.931 38.133  -5.459  1.00 90.52  ? 133 GLU B OE2 1 
ATOM   2056 N  N   . SER B 1 134 ? -43.238 39.707  -8.337  1.00 86.71  ? 134 SER B N   1 
ATOM   2057 C  CA  . SER B 1 134 ? -44.096 38.679  -8.933  1.00 87.59  ? 134 SER B CA  1 
ATOM   2058 C  C   . SER B 1 134 ? -43.892 38.552  -10.441 1.00 84.99  ? 134 SER B C   1 
ATOM   2059 O  O   . SER B 1 134 ? -44.527 37.723  -11.092 1.00 84.17  ? 134 SER B O   1 
ATOM   2060 C  CB  . SER B 1 134 ? -45.573 38.960  -8.639  1.00 93.39  ? 134 SER B CB  1 
ATOM   2061 O  OG  . SER B 1 134 ? -45.855 38.800  -7.260  1.00 95.93  ? 134 SER B OG  1 
ATOM   2062 N  N   . THR B 1 135 ? -43.021 39.391  -10.992 1.00 82.77  ? 135 THR B N   1 
ATOM   2063 C  CA  . THR B 1 135 ? -42.651 39.301  -12.398 1.00 80.68  ? 135 THR B CA  1 
ATOM   2064 C  C   . THR B 1 135 ? -41.538 38.271  -12.549 1.00 79.48  ? 135 THR B C   1 
ATOM   2065 O  O   . THR B 1 135 ? -41.433 37.597  -13.575 1.00 78.18  ? 135 THR B O   1 
ATOM   2066 C  CB  . THR B 1 135 ? -42.189 40.665  -12.937 1.00 81.86  ? 135 THR B CB  1 
ATOM   2067 O  OG1 . THR B 1 135 ? -43.335 41.488  -13.197 1.00 85.69  ? 135 THR B OG1 1 
ATOM   2068 C  CG2 . THR B 1 135 ? -41.389 40.501  -14.213 1.00 81.31  ? 135 THR B CG2 1 
ATOM   2069 N  N   . LYS B 1 136 ? -40.725 38.141  -11.504 1.00 79.05  ? 136 LYS B N   1 
ATOM   2070 C  CA  . LYS B 1 136 ? -39.606 37.205  -11.508 1.00 77.30  ? 136 LYS B CA  1 
ATOM   2071 C  C   . LYS B 1 136 ? -39.949 35.849  -10.854 1.00 70.75  ? 136 LYS B C   1 
ATOM   2072 O  O   . LYS B 1 136 ? -39.777 34.798  -11.466 1.00 70.03  ? 136 LYS B O   1 
ATOM   2073 C  CB  . LYS B 1 136 ? -38.379 37.825  -10.822 1.00 77.66  ? 136 LYS B CB  1 
ATOM   2074 C  CG  . LYS B 1 136 ? -38.400 39.346  -10.670 1.00 76.50  ? 136 LYS B CG  1 
ATOM   2075 C  CD  . LYS B 1 136 ? -37.004 39.847  -10.285 1.00 78.37  ? 136 LYS B CD  1 
ATOM   2076 C  CE  . LYS B 1 136 ? -37.021 41.271  -9.717  1.00 81.36  ? 136 LYS B CE  1 
ATOM   2077 N  NZ  . LYS B 1 136 ? -37.107 41.313  -8.224  1.00 79.52  ? 136 LYS B NZ  1 
ATOM   2078 N  N   . THR B 1 137 ? -40.460 35.892  -9.625  1.00 65.15  ? 137 THR B N   1 
ATOM   2079 C  CA  . THR B 1 137 ? -40.571 34.709  -8.776  1.00 60.09  ? 137 THR B CA  1 
ATOM   2080 C  C   . THR B 1 137 ? -42.018 34.315  -8.445  1.00 62.90  ? 137 THR B C   1 
ATOM   2081 O  O   . THR B 1 137 ? -42.303 33.172  -8.049  1.00 61.87  ? 137 THR B O   1 
ATOM   2082 C  CB  . THR B 1 137 ? -39.804 34.937  -7.447  1.00 66.12  ? 137 THR B CB  1 
ATOM   2083 O  OG1 . THR B 1 137 ? -40.508 35.883  -6.635  1.00 65.16  ? 137 THR B OG1 1 
ATOM   2084 C  CG2 . THR B 1 137 ? -38.403 35.476  -7.712  1.00 59.53  ? 137 THR B CG2 1 
ATOM   2085 N  N   . GLY B 1 138 ? -42.934 35.263  -8.606  1.00 64.66  ? 138 GLY B N   1 
ATOM   2086 C  CA  . GLY B 1 138 ? -44.302 35.064  -8.178  1.00 61.76  ? 138 GLY B CA  1 
ATOM   2087 C  C   . GLY B 1 138 ? -44.401 35.189  -6.670  1.00 61.75  ? 138 GLY B C   1 
ATOM   2088 O  O   . GLY B 1 138 ? -45.216 34.520  -6.041  1.00 63.88  ? 138 GLY B O   1 
ATOM   2089 N  N   . ASN B 1 139 ? -43.565 36.048  -6.093  1.00 61.56  ? 139 ASN B N   1 
ATOM   2090 C  CA  . ASN B 1 139 ? -43.545 36.281  -4.651  1.00 61.16  ? 139 ASN B CA  1 
ATOM   2091 C  C   . ASN B 1 139 ? -43.562 34.995  -3.859  1.00 62.15  ? 139 ASN B C   1 
ATOM   2092 O  O   . ASN B 1 139 ? -44.168 34.940  -2.793  1.00 59.09  ? 139 ASN B O   1 
ATOM   2093 C  CB  . ASN B 1 139 ? -44.716 37.172  -4.213  1.00 63.32  ? 139 ASN B CB  1 
ATOM   2094 C  CG  . ASN B 1 139 ? -44.534 38.627  -4.620  1.00 66.91  ? 139 ASN B CG  1 
ATOM   2095 O  OD1 . ASN B 1 139 ? -43.416 39.120  -4.716  1.00 64.69  ? 139 ASN B OD1 1 
ATOM   2096 N  ND2 . ASN B 1 139 ? -45.641 39.321  -4.852  1.00 72.30  ? 139 ASN B ND2 1 
ATOM   2097 N  N   . ALA B 1 140 ? -42.884 33.973  -4.390  1.00 66.49  ? 140 ALA B N   1 
ATOM   2098 C  CA  . ALA B 1 140 ? -42.853 32.623  -3.807  1.00 66.14  ? 140 ALA B CA  1 
ATOM   2099 C  C   . ALA B 1 140 ? -41.940 32.539  -2.593  1.00 68.95  ? 140 ALA B C   1 
ATOM   2100 O  O   . ALA B 1 140 ? -41.974 31.558  -1.846  1.00 68.81  ? 140 ALA B O   1 
ATOM   2101 C  CB  . ALA B 1 140 ? -42.444 31.586  -4.854  1.00 60.90  ? 140 ALA B CB  1 
ATOM   2102 N  N   . GLY B 1 141 ? -41.115 33.569  -2.415  1.00 71.81  ? 141 GLY B N   1 
ATOM   2103 C  CA  . GLY B 1 141 ? -40.285 33.696  -1.231  1.00 70.58  ? 141 GLY B CA  1 
ATOM   2104 C  C   . GLY B 1 141 ? -39.064 32.793  -1.188  1.00 68.17  ? 141 GLY B C   1 
ATOM   2105 O  O   . GLY B 1 141 ? -38.487 32.439  -2.224  1.00 66.48  ? 141 GLY B O   1 
ATOM   2106 N  N   . SER B 1 142 ? -38.680 32.419  0.031   1.00 64.06  ? 142 SER B N   1 
ATOM   2107 C  CA  . SER B 1 142 ? -37.452 31.683  0.274   1.00 61.17  ? 142 SER B CA  1 
ATOM   2108 C  C   . SER B 1 142 ? -37.500 30.265  -0.293  1.00 62.44  ? 142 SER B C   1 
ATOM   2109 O  O   . SER B 1 142 ? -38.575 29.712  -0.516  1.00 62.09  ? 142 SER B O   1 
ATOM   2110 C  CB  . SER B 1 142 ? -37.123 31.668  1.777   1.00 59.40  ? 142 SER B CB  1 
ATOM   2111 O  OG  . SER B 1 142 ? -37.592 30.500  2.423   1.00 55.27  ? 142 SER B OG  1 
ATOM   2112 N  N   . ARG B 1 143 ? -36.323 29.685  -0.523  1.00 63.51  ? 143 ARG B N   1 
ATOM   2113 C  CA  . ARG B 1 143 ? -36.209 28.350  -1.098  1.00 58.03  ? 143 ARG B CA  1 
ATOM   2114 C  C   . ARG B 1 143 ? -36.056 27.369  0.031   1.00 56.24  ? 143 ARG B C   1 
ATOM   2115 O  O   . ARG B 1 143 ? -34.992 27.277  0.632   1.00 58.47  ? 143 ARG B O   1 
ATOM   2116 C  CB  . ARG B 1 143 ? -35.006 28.299  -2.032  1.00 56.81  ? 143 ARG B CB  1 
ATOM   2117 C  CG  . ARG B 1 143 ? -34.913 29.541  -2.899  1.00 59.11  ? 143 ARG B CG  1 
ATOM   2118 C  CD  . ARG B 1 143 ? -33.648 29.586  -3.743  1.00 58.76  ? 143 ARG B CD  1 
ATOM   2119 N  NE  . ARG B 1 143 ? -33.837 30.487  -4.880  1.00 59.00  ? 143 ARG B NE  1 
ATOM   2120 C  CZ  . ARG B 1 143 ? -33.043 30.540  -5.943  1.00 55.67  ? 143 ARG B CZ  1 
ATOM   2121 N  NH1 . ARG B 1 143 ? -31.987 29.746  -6.025  1.00 57.57  ? 143 ARG B NH1 1 
ATOM   2122 N  NH2 . ARG B 1 143 ? -33.309 31.384  -6.925  1.00 52.95  ? 143 ARG B NH2 1 
ATOM   2123 N  N   . LEU B 1 144 ? -37.133 26.642  0.319   1.00 58.29  ? 144 LEU B N   1 
ATOM   2124 C  CA  . LEU B 1 144 ? -37.213 25.757  1.491   1.00 57.82  ? 144 LEU B CA  1 
ATOM   2125 C  C   . LEU B 1 144 ? -36.576 24.389  1.245   1.00 58.27  ? 144 LEU B C   1 
ATOM   2126 O  O   . LEU B 1 144 ? -36.116 23.734  2.175   1.00 56.17  ? 144 LEU B O   1 
ATOM   2127 C  CB  . LEU B 1 144 ? -38.667 25.560  1.928   1.00 54.60  ? 144 LEU B CB  1 
ATOM   2128 C  CG  . LEU B 1 144 ? -39.517 26.753  2.366   1.00 54.06  ? 144 LEU B CG  1 
ATOM   2129 C  CD1 . LEU B 1 144 ? -40.893 26.246  2.746   1.00 53.18  ? 144 LEU B CD1 1 
ATOM   2130 C  CD2 . LEU B 1 144 ? -38.896 27.499  3.534   1.00 53.93  ? 144 LEU B CD2 1 
ATOM   2131 N  N   . ALA B 1 145 ? -36.579 23.951  -0.007  1.00 59.38  ? 145 ALA B N   1 
ATOM   2132 C  CA  . ALA B 1 145 ? -35.893 22.722  -0.373  1.00 57.90  ? 145 ALA B CA  1 
ATOM   2133 C  C   . ALA B 1 145 ? -35.636 22.640  -1.881  1.00 61.15  ? 145 ALA B C   1 
ATOM   2134 O  O   . ALA B 1 145 ? -36.317 23.291  -2.677  1.00 66.17  ? 145 ALA B O   1 
ATOM   2135 C  CB  . ALA B 1 145 ? -36.660 21.494  0.130   1.00 52.01  ? 145 ALA B CB  1 
ATOM   2136 N  N   . CYS B 1 146 ? -34.646 21.834  -2.256  1.00 55.59  ? 146 CYS B N   1 
ATOM   2137 C  CA  . CYS B 1 146 ? -34.243 21.681  -3.642  1.00 53.24  ? 146 CYS B CA  1 
ATOM   2138 C  C   . CYS B 1 146 ? -33.439 20.381  -3.843  1.00 55.13  ? 146 CYS B C   1 
ATOM   2139 O  O   . CYS B 1 146 ? -32.971 19.770  -2.884  1.00 53.69  ? 146 CYS B O   1 
ATOM   2140 C  CB  . CYS B 1 146 ? -33.400 22.886  -4.048  1.00 53.02  ? 146 CYS B CB  1 
ATOM   2141 S  SG  . CYS B 1 146 ? -32.036 23.280  -2.882  1.00 58.76  ? 146 CYS B SG  1 
ATOM   2142 N  N   . GLY B 1 147 ? -33.287 19.966  -5.094  1.00 53.10  ? 147 GLY B N   1 
ATOM   2143 C  CA  . GLY B 1 147 ? -32.442 18.843  -5.431  1.00 50.22  ? 147 GLY B CA  1 
ATOM   2144 C  C   . GLY B 1 147 ? -32.146 18.876  -6.917  1.00 52.51  ? 147 GLY B C   1 
ATOM   2145 O  O   . GLY B 1 147 ? -32.913 19.464  -7.683  1.00 55.72  ? 147 GLY B O   1 
ATOM   2146 N  N   . VAL B 1 148 ? -31.038 18.263  -7.329  1.00 51.01  ? 148 VAL B N   1 
ATOM   2147 C  CA  . VAL B 1 148 ? -30.708 18.179  -8.749  1.00 49.13  ? 148 VAL B CA  1 
ATOM   2148 C  C   . VAL B 1 148 ? -31.529 17.093  -9.416  1.00 47.18  ? 148 VAL B C   1 
ATOM   2149 O  O   . VAL B 1 148 ? -31.715 15.993  -8.874  1.00 44.46  ? 148 VAL B O   1 
ATOM   2150 C  CB  . VAL B 1 148 ? -29.200 17.913  -9.022  1.00 58.12  ? 148 VAL B CB  1 
ATOM   2151 C  CG1 . VAL B 1 148 ? -28.936 17.847  -10.531 1.00 57.16  ? 148 VAL B CG1 1 
ATOM   2152 C  CG2 . VAL B 1 148 ? -28.325 18.994  -8.383  1.00 58.21  ? 148 VAL B CG2 1 
ATOM   2153 N  N   . ILE B 1 149 ? -32.020 17.409  -10.604 1.00 46.95  ? 149 ILE B N   1 
ATOM   2154 C  CA  . ILE B 1 149 ? -32.830 16.465  -11.339 1.00 47.07  ? 149 ILE B CA  1 
ATOM   2155 C  C   . ILE B 1 149 ? -31.900 15.504  -12.054 1.00 49.34  ? 149 ILE B C   1 
ATOM   2156 O  O   . ILE B 1 149 ? -31.022 15.912  -12.816 1.00 51.73  ? 149 ILE B O   1 
ATOM   2157 C  CB  . ILE B 1 149 ? -33.778 17.180  -12.303 1.00 46.34  ? 149 ILE B CB  1 
ATOM   2158 C  CG1 . ILE B 1 149 ? -34.870 17.905  -11.496 1.00 47.97  ? 149 ILE B CG1 1 
ATOM   2159 C  CG2 . ILE B 1 149 ? -34.373 16.180  -13.287 1.00 44.64  ? 149 ILE B CG2 1 
ATOM   2160 C  CD1 . ILE B 1 149 ? -35.490 19.117  -12.179 1.00 49.66  ? 149 ILE B CD1 1 
ATOM   2161 N  N   . GLY B 1 150 ? -32.076 14.221  -11.784 1.00 49.35  ? 150 GLY B N   1 
ATOM   2162 C  CA  . GLY B 1 150 ? -31.143 13.242  -12.297 1.00 50.48  ? 150 GLY B CA  1 
ATOM   2163 C  C   . GLY B 1 150 ? -31.774 11.986  -12.836 1.00 45.41  ? 150 GLY B C   1 
ATOM   2164 O  O   . GLY B 1 150 ? -32.816 11.554  -12.359 1.00 44.37  ? 150 GLY B O   1 
ATOM   2165 N  N   . ILE B 1 151 ? -31.111 11.397  -13.824 1.00 45.63  ? 151 ILE B N   1 
ATOM   2166 C  CA  . ILE B 1 151 ? -31.589 10.196  -14.499 1.00 48.92  ? 151 ILE B CA  1 
ATOM   2167 C  C   . ILE B 1 151 ? -31.883 9.037   -13.529 1.00 48.14  ? 151 ILE B C   1 
ATOM   2168 O  O   . ILE B 1 151 ? -31.012 8.613   -12.763 1.00 51.18  ? 151 ILE B O   1 
ATOM   2169 C  CB  . ILE B 1 151 ? -30.598 9.767   -15.605 1.00 45.58  ? 151 ILE B CB  1 
ATOM   2170 C  CG1 . ILE B 1 151 ? -30.234 10.982  -16.467 1.00 45.07  ? 151 ILE B CG1 1 
ATOM   2171 C  CG2 . ILE B 1 151 ? -31.182 8.657   -16.462 1.00 41.72  ? 151 ILE B CG2 1 
ATOM   2172 C  CD1 . ILE B 1 151 ? -29.068 10.758  -17.410 1.00 44.75  ? 151 ILE B CD1 1 
ATOM   2173 N  N   . ALA B 1 152 ? -33.125 8.550   -13.565 1.00 45.40  ? 152 ALA B N   1 
ATOM   2174 C  CA  . ALA B 1 152 ? -33.561 7.456   -12.700 1.00 46.24  ? 152 ALA B CA  1 
ATOM   2175 C  C   . ALA B 1 152 ? -33.670 6.148   -13.469 1.00 48.42  ? 152 ALA B C   1 
ATOM   2176 O  O   . ALA B 1 152 ? -33.896 6.154   -14.684 1.00 47.93  ? 152 ALA B O   1 
ATOM   2177 C  CB  . ALA B 1 152 ? -34.880 7.789   -12.040 1.00 42.87  ? 152 ALA B CB  1 
ATOM   2178 N  N   . GLN B 1 153 ? -33.503 5.041   -12.745 1.00 50.82  ? 153 GLN B N   1 
ATOM   2179 C  CA  . GLN B 1 153 ? -33.512 3.704   -13.335 1.00 59.48  ? 153 GLN B CA  1 
ATOM   2180 C  C   . GLN B 1 153 ? -34.853 3.339   -13.979 1.00 65.31  ? 153 GLN B C   1 
ATOM   2181 O  O   . GLN B 1 153 ? -35.916 3.338   -13.340 1.00 63.95  ? 153 GLN B O   1 
ATOM   2182 C  CB  . GLN B 1 153 ? -33.100 2.640   -12.296 1.00 61.82  ? 153 GLN B CB  1 
ATOM   2183 C  CG  . GLN B 1 153 ? -33.596 1.230   -12.618 1.00 63.95  ? 153 GLN B CG  1 
ATOM   2184 C  CD  . GLN B 1 153 ? -32.743 0.120   -12.005 1.00 64.10  ? 153 GLN B CD  1 
ATOM   2185 O  OE1 . GLN B 1 153 ? -32.730 -0.081  -10.784 1.00 65.31  ? 153 GLN B OE1 1 
ATOM   2186 N  NE2 . GLN B 1 153 ? -32.035 -0.615  -12.861 1.00 60.27  ? 153 GLN B NE2 1 
ATOM   2187 O  OXT . GLN B 1 153 ? -34.884 3.025   -15.173 1.00 67.72  ? 153 GLN B OXT 1 
HETATM 2188 N  N   . CYS C 2 .   ? -28.343 14.339  -20.589 1.00 111.77 ? 201 CYS A N   1 
HETATM 2189 C  CA  . CYS C 2 .   ? -28.478 15.007  -21.877 1.00 100.61 ? 201 CYS A CA  1 
HETATM 2190 C  C   . CYS C 2 .   ? -27.158 15.016  -22.651 1.00 93.61  ? 201 CYS A C   1 
HETATM 2191 O  O   . CYS C 2 .   ? -27.135 15.312  -23.850 1.00 82.40  ? 201 CYS A O   1 
HETATM 2192 C  CB  . CYS C 2 .   ? -29.008 16.436  -21.696 1.00 99.23  ? 201 CYS A CB  1 
HETATM 2193 S  SG  . CYS C 2 .   ? -30.795 16.541  -21.384 1.00 96.56  ? 201 CYS A SG  1 
HETATM 2194 ZN ZN  . ZN  D 3 .   ? -16.050 0.887   -13.273 1.00 31.00  ? 202 ZN  A ZN  1 
HETATM 2195 CU CU  . CU  E 4 .   ? -17.748 4.167   -7.871  1.00 36.75  ? 203 CU  A CU  1 
HETATM 2196 ZN ZN  . ZN  F 3 .   ? -40.602 31.712  -12.945 1.00 58.71  ? 201 ZN  B ZN  1 
HETATM 2197 CU CU  . CU  G 4 .   ? -38.652 28.613  -7.523  1.00 60.79  ? 202 CU  B CU  1 
HETATM 2198 O  O   . HOH H 5 .   ? -7.882  -8.976  -12.453 1.00 22.69  ? 301 HOH A O   1 
HETATM 2199 O  O   . HOH H 5 .   ? -13.274 8.884   6.068   1.00 29.79  ? 302 HOH A O   1 
HETATM 2200 O  O   . HOH H 5 .   ? -10.032 -3.818  -18.029 1.00 38.98  ? 303 HOH A O   1 
HETATM 2201 O  O   . HOH H 5 .   ? -6.323  13.785  -6.023  1.00 24.53  ? 304 HOH A O   1 
HETATM 2202 O  O   . HOH H 5 .   ? -27.910 11.291  -21.908 1.00 49.63  ? 305 HOH A O   1 
HETATM 2203 O  O   . HOH H 5 .   ? -11.593 21.008  1.460   1.00 39.62  ? 306 HOH A O   1 
HETATM 2204 O  O   . HOH H 5 .   ? -23.408 25.154  -19.116 1.00 37.12  ? 307 HOH A O   1 
HETATM 2205 O  O   . HOH H 5 .   ? -19.967 -1.532  -11.409 1.00 33.44  ? 308 HOH A O   1 
HETATM 2206 O  O   . HOH H 5 .   ? -24.284 17.404  -7.122  1.00 34.93  ? 309 HOH A O   1 
HETATM 2207 O  O   . HOH H 5 .   ? -18.081 -4.338  -15.649 1.00 47.74  ? 310 HOH A O   1 
HETATM 2208 O  O   . HOH H 5 .   ? -12.249 12.573  8.730   1.00 37.71  ? 311 HOH A O   1 
HETATM 2209 O  O   . HOH H 5 .   ? -8.130  8.825   -21.315 1.00 41.22  ? 312 HOH A O   1 
HETATM 2210 O  O   . HOH H 5 .   ? -2.168  9.259   8.331   1.00 41.69  ? 313 HOH A O   1 
HETATM 2211 O  O   . HOH H 5 .   ? -7.623  9.012   -11.231 1.00 32.22  ? 314 HOH A O   1 
HETATM 2212 O  O   . HOH H 5 .   ? -11.579 21.267  -21.139 1.00 26.78  ? 315 HOH A O   1 
HETATM 2213 O  O   . HOH H 5 .   ? -11.869 7.238   3.852   1.00 30.46  ? 316 HOH A O   1 
HETATM 2214 O  O   . HOH H 5 .   ? -18.375 2.192   -21.438 1.00 31.83  ? 317 HOH A O   1 
HETATM 2215 O  O   . HOH H 5 .   ? -11.532 3.325   -12.670 1.00 23.49  ? 318 HOH A O   1 
HETATM 2216 O  O   . HOH I 5 .   ? -41.867 18.250  -23.426 1.00 40.58  ? 301 HOH B O   1 
HETATM 2217 O  O   . HOH I 5 .   ? -45.177 29.017  -11.703 1.00 36.55  ? 302 HOH B O   1 
HETATM 2218 O  O   . HOH I 5 .   ? -37.389 0.823   -13.270 1.00 39.03  ? 303 HOH B O   1 
HETATM 2219 O  O   . HOH I 5 .   ? -42.146 8.072   -4.938  1.00 34.36  ? 304 HOH B O   1 
HETATM 2220 O  O   . HOH I 5 .   ? -31.127 12.799  5.397   1.00 37.66  ? 305 HOH B O   1 
HETATM 2221 O  O   . HOH I 5 .   ? -33.108 26.899  1.030   1.00 43.82  ? 306 HOH B O   1 
# 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   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 ALA 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 ALA A . n 
A 1 24  GLU 24  24  24  GLU ALA 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 ALA A . n 
A 1 37  GLY 37  37  37  GLY GLY A . n 
A 1 38  LEU 38  38  38  LEU LEU A . n 
A 1 39  THR 39  39  39  THR THR A . n 
A 1 40  GLU 40  40  40  GLU GLU A . n 
A 1 41  GLY 41  41  41  GLY GLY A . n 
A 1 42  LEU 42  42  42  LEU LEU A . n 
A 1 43  HIS 43  43  43  HIS HIS A . n 
A 1 44  GLY 44  44  44  GLY GLY A . n 
A 1 45  PHE 45  45  45  PHE PHE A . n 
A 1 46  HIS 46  46  46  HIS HIS A . n 
A 1 47  VAL 47  47  47  VAL VAL A . n 
A 1 48  HIS 48  48  48  HIS HIS A . n 
A 1 49  GLU 49  49  49  GLU GLU A . n 
A 1 50  PHE 50  50  50  PHE PHE A . n 
A 1 51  GLY 51  51  51  GLY GLY A . n 
A 1 52  ASP 52  52  52  ASP ASP A . n 
A 1 53  ASN 53  53  53  ASN ASN A . n 
A 1 54  THR 54  54  54  THR THR A . n 
A 1 55  ALA 55  55  55  ALA ALA A . n 
A 1 56  GLY 56  56  56  GLY GLY A . n 
A 1 57  CYS 57  57  57  CYS CYS A . n 
A 1 58  THR 58  58  58  THR THR A . n 
A 1 59  SER 59  59  59  SER SER A . n 
A 1 60  ALA 60  60  60  ALA ALA A . n 
A 1 61  GLY 61  61  61  GLY GLY A . n 
A 1 62  PRO 62  62  62  PRO PRO A . n 
A 1 63  HIS 63  63  63  HIS HIS A . n 
A 1 64  PHE 64  64  64  PHE PHE A . n 
A 1 65  ASN 65  65  65  ASN ASN A . n 
A 1 66  PRO 66  66  66  PRO PRO A . n 
A 1 67  LEU 67  67  67  LEU LEU A . n 
A 1 68  SER 68  68  68  SER SER A . n 
A 1 69  ARG 69  69  69  ARG ARG A . n 
A 1 70  LYS 70  70  70  LYS LYS A . n 
A 1 71  HIS 71  71  71  HIS HIS A . n 
A 1 72  GLY 72  72  72  GLY GLY A . n 
A 1 73  GLY 73  73  73  GLY GLY A . n 
A 1 74  PRO 74  74  74  PRO PRO A . n 
A 1 75  LYS 75  75  75  LYS LYS A . n 
A 1 76  ASP 76  76  76  ASP ASP A . n 
A 1 77  GLU 77  77  77  GLU GLU A . n 
A 1 78  GLU 78  78  78  GLU GLU A . n 
A 1 79  ARG 79  79  79  ARG ARG A . n 
A 1 80  HIS 80  80  80  HIS HIS A . n 
A 1 81  VAL 81  81  81  VAL VAL A . n 
A 1 82  GLY 82  82  82  GLY GLY A . n 
A 1 83  ASP 83  83  83  ASP ASP A . n 
A 1 84  LEU 84  84  84  LEU LEU A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  ASN 86  86  86  ASN ASN A . n 
A 1 87  VAL 87  87  87  VAL VAL A . n 
A 1 88  THR 88  88  88  THR THR A . n 
A 1 89  ALA 89  89  89  ALA ALA A . n 
A 1 90  ASP 90  90  90  ASP ASP A . n 
A 1 91  LYS 91  91  91  LYS LYS A . n 
A 1 92  ASP 92  92  92  ASP ASP A . n 
A 1 93  GLY 93  93  93  GLY GLY A . n 
A 1 94  VAL 94  94  94  VAL VAL A . n 
A 1 95  ALA 95  95  95  ALA ALA A . n 
A 1 96  ASP 96  96  96  ASP ASP A . n 
A 1 97  VAL 97  97  97  VAL VAL A . n 
A 1 98  SER 98  98  98  SER SER A . n 
A 1 99  ILE 99  99  99  ILE ILE A . n 
A 1 100 GLU 100 100 100 GLU GLU A . n 
A 1 101 ASP 101 101 101 ASP ASP A . n 
A 1 102 SER 102 102 102 SER SER A . n 
A 1 103 VAL 103 103 103 VAL VAL A . n 
A 1 104 ILE 104 104 104 ILE ILE A . n 
A 1 105 SER 105 105 105 SER SER A . n 
A 1 106 LEU 106 106 106 LEU LEU A . n 
A 1 107 SER 107 107 107 SER SER A . n 
A 1 108 GLY 108 108 108 GLY GLY A . n 
A 1 109 ASP 109 109 109 ASP ASP A . n 
A 1 110 HIS 110 110 110 HIS HIS A . n 
A 1 111 CYS 111 111 111 CYS CYS A . n 
A 1 112 ILE 112 112 112 ILE ILE A . n 
A 1 113 ILE 113 113 113 ILE ILE A . n 
A 1 114 GLY 114 114 114 GLY GLY A . n 
A 1 115 ARG 115 115 115 ARG ARG A . n 
A 1 116 THR 116 116 116 THR THR A . n 
A 1 117 LEU 117 117 117 LEU LEU A . n 
A 1 118 VAL 118 118 118 VAL VAL A . n 
A 1 119 VAL 119 119 119 VAL VAL A . n 
A 1 120 HIS 120 120 120 HIS HIS A . n 
A 1 121 GLU 121 121 121 GLU GLU A . n 
A 1 122 LYS 122 122 122 LYS LYS A . n 
A 1 123 ALA 123 123 123 ALA ALA A . n 
A 1 124 ASP 124 124 124 ASP ASP A . n 
A 1 125 ASP 125 125 125 ASP ASP A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 GLY 127 127 127 GLY GLY A . n 
A 1 128 LYS 128 128 128 LYS LYS A . n 
A 1 129 GLY 129 129 129 GLY GLY A . n 
A 1 130 GLY 130 130 130 GLY GLY A . n 
A 1 131 ASN 131 131 131 ASN ASN A . n 
A 1 132 GLU 132 132 132 GLU GLU A . n 
A 1 133 GLU 133 133 133 GLU GLU A . n 
A 1 134 SER 134 134 134 SER SER A . n 
A 1 135 THR 135 135 135 THR THR A . n 
A 1 136 LYS 136 136 136 LYS LYS A . n 
A 1 137 THR 137 137 137 THR THR A . n 
A 1 138 GLY 138 138 138 GLY GLY A . n 
A 1 139 ASN 139 139 139 ASN ASN A . n 
A 1 140 ALA 140 140 140 ALA ALA A . n 
A 1 141 GLY 141 141 141 GLY GLY A . n 
A 1 142 SER 142 142 142 SER SER A . n 
A 1 143 ARG 143 143 143 ARG ARG A . n 
A 1 144 LEU 144 144 144 LEU LEU A . n 
A 1 145 ALA 145 145 145 ALA ALA A . n 
A 1 146 CYS 146 146 146 CYS CYS A . n 
A 1 147 GLY 147 147 147 GLY GLY A . n 
A 1 148 VAL 148 148 148 VAL VAL A . n 
A 1 149 ILE 149 149 149 ILE ILE A . n 
A 1 150 GLY 150 150 150 GLY GLY A . n 
A 1 151 ILE 151 151 151 ILE ILE A . n 
A 1 152 ALA 152 152 152 ALA ALA A . n 
A 1 153 GLN 153 153 153 GLN GLN A . n 
B 1 1   ALA 1   1   1   ALA ALA B . n 
B 1 2   THR 2   2   2   THR THR B . n 
B 1 3   LYS 3   3   3   LYS LYS B . n 
B 1 4   ALA 4   4   4   ALA ALA B . n 
B 1 5   VAL 5   5   5   VAL VAL B . n 
B 1 6   CYS 6   6   6   CYS CYS B . n 
B 1 7   VAL 7   7   7   VAL VAL B . n 
B 1 8   LEU 8   8   8   LEU LEU B . n 
B 1 9   LYS 9   9   9   LYS LYS B . n 
B 1 10  GLY 10  10  10  GLY GLY B . n 
B 1 11  ASP 11  11  11  ASP ASP B . n 
B 1 12  GLY 12  12  12  GLY GLY B . n 
B 1 13  PRO 13  13  13  PRO PRO B . n 
B 1 14  VAL 14  14  14  VAL VAL B . n 
B 1 15  GLN 15  15  15  GLN GLN B . n 
B 1 16  GLY 16  16  16  GLY GLY B . n 
B 1 17  ILE 17  17  17  ILE ILE B . n 
B 1 18  ILE 18  18  18  ILE ILE B . n 
B 1 19  ASN 19  19  19  ASN ASN B . n 
B 1 20  PHE 20  20  20  PHE PHE B . n 
B 1 21  GLU 21  21  21  GLU GLU B . n 
B 1 22  GLN 22  22  22  GLN GLN B . n 
B 1 23  LYS 23  23  23  LYS LYS B . n 
B 1 24  GLU 24  24  ?   ?   ?   B . n 
B 1 25  SER 25  25  ?   ?   ?   B . n 
B 1 26  ASN 26  26  26  ASN ASN B . n 
B 1 27  GLY 27  27  27  GLY GLY B . n 
B 1 28  PRO 28  28  28  PRO PRO B . n 
B 1 29  VAL 29  29  29  VAL VAL B . n 
B 1 30  LYS 30  30  30  LYS ALA B . n 
B 1 31  VAL 31  31  31  VAL VAL B . n 
B 1 32  TRP 32  32  32  TRP TRP B . n 
B 1 33  GLY 33  33  33  GLY GLY B . n 
B 1 34  SER 34  34  34  SER SER B . n 
B 1 35  ILE 35  35  35  ILE ILE B . n 
B 1 36  LYS 36  36  36  LYS ALA B . n 
B 1 37  GLY 37  37  37  GLY GLY B . n 
B 1 38  LEU 38  38  38  LEU LEU B . n 
B 1 39  THR 39  39  39  THR THR B . n 
B 1 40  GLU 40  40  40  GLU GLU B . n 
B 1 41  GLY 41  41  41  GLY GLY B . n 
B 1 42  LEU 42  42  42  LEU LEU B . n 
B 1 43  HIS 43  43  43  HIS HIS B . n 
B 1 44  GLY 44  44  44  GLY GLY B . n 
B 1 45  PHE 45  45  45  PHE PHE B . n 
B 1 46  HIS 46  46  46  HIS HIS B . n 
B 1 47  VAL 47  47  47  VAL VAL B . n 
B 1 48  HIS 48  48  48  HIS HIS B . n 
B 1 49  GLU 49  49  49  GLU GLU B . n 
B 1 50  PHE 50  50  50  PHE PHE B . n 
B 1 51  GLY 51  51  51  GLY GLY B . n 
B 1 52  ASP 52  52  52  ASP ASP B . n 
B 1 53  ASN 53  53  53  ASN ASN B . n 
B 1 54  THR 54  54  54  THR THR B . n 
B 1 55  ALA 55  55  55  ALA ALA B . n 
B 1 56  GLY 56  56  56  GLY GLY B . n 
B 1 57  CYS 57  57  57  CYS CYS B . n 
B 1 58  THR 58  58  58  THR THR B . n 
B 1 59  SER 59  59  59  SER SER B . n 
B 1 60  ALA 60  60  60  ALA ALA B . n 
B 1 61  GLY 61  61  61  GLY GLY B . n 
B 1 62  PRO 62  62  62  PRO PRO B . n 
B 1 63  HIS 63  63  63  HIS HIS B . n 
B 1 64  PHE 64  64  64  PHE PHE B . n 
B 1 65  ASN 65  65  65  ASN ASN B . n 
B 1 66  PRO 66  66  66  PRO PRO B . n 
B 1 67  LEU 67  67  67  LEU LEU B . n 
B 1 68  SER 68  68  68  SER SER B . n 
B 1 69  ARG 69  69  69  ARG ARG B . n 
B 1 70  LYS 70  70  70  LYS ALA B . n 
B 1 71  HIS 71  71  71  HIS HIS B . n 
B 1 72  GLY 72  72  72  GLY GLY B . n 
B 1 73  GLY 73  73  73  GLY GLY B . n 
B 1 74  PRO 74  74  74  PRO PRO B . n 
B 1 75  LYS 75  75  75  LYS LYS B . n 
B 1 76  ASP 76  76  76  ASP ASP B . n 
B 1 77  GLU 77  77  77  GLU GLU B . n 
B 1 78  GLU 78  78  78  GLU GLU B . n 
B 1 79  ARG 79  79  79  ARG ARG B . n 
B 1 80  HIS 80  80  80  HIS HIS B . n 
B 1 81  VAL 81  81  81  VAL VAL B . n 
B 1 82  GLY 82  82  82  GLY GLY B . n 
B 1 83  ASP 83  83  83  ASP ASP B . n 
B 1 84  LEU 84  84  84  LEU LEU B . n 
B 1 85  GLY 85  85  85  GLY GLY B . n 
B 1 86  ASN 86  86  86  ASN ASN B . n 
B 1 87  VAL 87  87  87  VAL VAL B . n 
B 1 88  THR 88  88  88  THR THR B . n 
B 1 89  ALA 89  89  89  ALA ALA B . n 
B 1 90  ASP 90  90  90  ASP ASP B . n 
B 1 91  LYS 91  91  91  LYS LYS B . n 
B 1 92  ASP 92  92  92  ASP ASP B . n 
B 1 93  GLY 93  93  93  GLY GLY B . n 
B 1 94  VAL 94  94  94  VAL VAL B . n 
B 1 95  ALA 95  95  95  ALA ALA B . n 
B 1 96  ASP 96  96  96  ASP ASP B . n 
B 1 97  VAL 97  97  97  VAL VAL B . n 
B 1 98  SER 98  98  98  SER SER B . n 
B 1 99  ILE 99  99  99  ILE ILE B . n 
B 1 100 GLU 100 100 100 GLU ALA B . n 
B 1 101 ASP 101 101 101 ASP ASP B . n 
B 1 102 SER 102 102 102 SER SER B . n 
B 1 103 VAL 103 103 103 VAL VAL B . n 
B 1 104 ILE 104 104 104 ILE ILE B . n 
B 1 105 SER 105 105 105 SER SER B . n 
B 1 106 LEU 106 106 106 LEU LEU B . n 
B 1 107 SER 107 107 107 SER SER B . n 
B 1 108 GLY 108 108 108 GLY GLY B . n 
B 1 109 ASP 109 109 109 ASP ASP B . n 
B 1 110 HIS 110 110 110 HIS HIS B . n 
B 1 111 CYS 111 111 111 CYS CYS B . n 
B 1 112 ILE 112 112 112 ILE ALA B . n 
B 1 113 ILE 113 113 113 ILE ILE B . n 
B 1 114 GLY 114 114 114 GLY GLY B . n 
B 1 115 ARG 115 115 115 ARG ARG B . n 
B 1 116 THR 116 116 116 THR THR B . n 
B 1 117 LEU 117 117 117 LEU LEU B . n 
B 1 118 VAL 118 118 118 VAL VAL B . n 
B 1 119 VAL 119 119 119 VAL VAL B . n 
B 1 120 HIS 120 120 120 HIS HIS B . n 
B 1 121 GLU 121 121 121 GLU GLU B . n 
B 1 122 LYS 122 122 122 LYS LYS B . n 
B 1 123 ALA 123 123 123 ALA ALA B . n 
B 1 124 ASP 124 124 124 ASP ASP B . n 
B 1 125 ASP 125 125 125 ASP ASP B . n 
B 1 126 LEU 126 126 126 LEU LEU B . n 
B 1 127 GLY 127 127 127 GLY GLY B . n 
B 1 128 LYS 128 128 128 LYS LYS B . n 
B 1 129 GLY 129 129 129 GLY GLY B . n 
B 1 130 GLY 130 130 130 GLY GLY B . n 
B 1 131 ASN 131 131 131 ASN ASN B . n 
B 1 132 GLU 132 132 132 GLU GLU B . n 
B 1 133 GLU 133 133 133 GLU GLU B . n 
B 1 134 SER 134 134 134 SER SER B . n 
B 1 135 THR 135 135 135 THR THR B . n 
B 1 136 LYS 136 136 136 LYS LYS B . n 
B 1 137 THR 137 137 137 THR THR B . n 
B 1 138 GLY 138 138 138 GLY GLY B . n 
B 1 139 ASN 139 139 139 ASN ASN B . n 
B 1 140 ALA 140 140 140 ALA ALA B . n 
B 1 141 GLY 141 141 141 GLY GLY B . n 
B 1 142 SER 142 142 142 SER SER B . n 
B 1 143 ARG 143 143 143 ARG ARG B . n 
B 1 144 LEU 144 144 144 LEU LEU B . n 
B 1 145 ALA 145 145 145 ALA ALA B . n 
B 1 146 CYS 146 146 146 CYS CYS B . n 
B 1 147 GLY 147 147 147 GLY GLY B . n 
B 1 148 VAL 148 148 148 VAL VAL B . n 
B 1 149 ILE 149 149 149 ILE ILE B . n 
B 1 150 GLY 150 150 150 GLY GLY B . n 
B 1 151 ILE 151 151 151 ILE ILE B . n 
B 1 152 ALA 152 152 152 ALA ALA B . n 
B 1 153 GLN 153 153 153 GLN GLN B . n 
# 
_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 
# 
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)' 1520  ? 
1 MORE         -15   ? 
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 ? B HIS 80  ? B HIS 80  ? 1_555 ZN ? F ZN . ? B ZN 201 ? 1_555 ND1 ? B HIS 63 ? B HIS 63 ? 1_555 113.8 ? 
2  ND1 ? B HIS 80  ? B HIS 80  ? 1_555 ZN ? F ZN . ? B ZN 201 ? 1_555 OD1 ? B ASP 83 ? B ASP 83 ? 1_555 104.0 ? 
3  ND1 ? B HIS 63  ? B HIS 63  ? 1_555 ZN ? F ZN . ? B ZN 201 ? 1_555 OD1 ? B ASP 83 ? B ASP 83 ? 1_555 109.5 ? 
4  ND1 ? B HIS 80  ? B HIS 80  ? 1_555 ZN ? F ZN . ? B ZN 201 ? 1_555 ND1 ? B HIS 71 ? B HIS 71 ? 1_555 121.2 ? 
5  ND1 ? B HIS 63  ? B HIS 63  ? 1_555 ZN ? F ZN . ? B ZN 201 ? 1_555 ND1 ? B HIS 71 ? B HIS 71 ? 1_555 98.5  ? 
6  OD1 ? B ASP 83  ? B ASP 83  ? 1_555 ZN ? F ZN . ? B ZN 201 ? 1_555 ND1 ? B HIS 71 ? B HIS 71 ? 1_555 109.7 ? 
7  ND1 ? A HIS 63  ? A HIS 63  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 OD2 ? A ASP 83 ? A ASP 83 ? 1_555 109.0 ? 
8  ND1 ? A HIS 63  ? A HIS 63  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 80 ? A HIS 80 ? 1_555 114.3 ? 
9  OD2 ? A ASP 83  ? A ASP 83  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 80 ? A HIS 80 ? 1_555 124.1 ? 
10 ND1 ? A HIS 63  ? A HIS 63  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 71 ? A HIS 71 ? 1_555 107.6 ? 
11 OD2 ? A ASP 83  ? A ASP 83  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 71 ? A HIS 71 ? 1_555 88.0  ? 
12 ND1 ? A HIS 80  ? A HIS 80  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 71 ? A HIS 71 ? 1_555 109.8 ? 
13 NE2 ? A HIS 120 ? A HIS 120 ? 1_555 CU ? E CU . ? A CU 203 ? 1_555 ND1 ? A HIS 46 ? A HIS 46 ? 1_555 104.4 ? 
14 NE2 ? A HIS 120 ? A HIS 120 ? 1_555 CU ? E CU . ? A CU 203 ? 1_555 NE2 ? A HIS 48 ? A HIS 48 ? 1_555 113.4 ? 
15 ND1 ? A HIS 46  ? A HIS 46  ? 1_555 CU ? E CU . ? A CU 203 ? 1_555 NE2 ? A HIS 48 ? A HIS 48 ? 1_555 141.9 ? 
16 NE2 ? B HIS 120 ? B HIS 120 ? 1_555 CU ? G CU . ? B CU 202 ? 1_555 NE2 ? B HIS 46 ? B HIS 46 ? 1_555 127.2 ? 
17 NE2 ? B HIS 120 ? B HIS 120 ? 1_555 CU ? G CU . ? B CU 202 ? 1_555 NE2 ? B HIS 48 ? B HIS 48 ? 1_555 105.5 ? 
18 NE2 ? B HIS 46  ? B HIS 46  ? 1_555 CU ? G CU . ? B CU 202 ? 1_555 NE2 ? B HIS 48 ? B HIS 48 ? 1_555 122.2 ? 
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2013-09-04 
2 'Structure model' 1 1 2013-12-25 
# 
_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_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][3] 
'X-RAY DIFFRACTION' 1  ? refined -28.9003 15.6388 -21.9263 0.7779 1.6722 1.1081  0.2232  -0.1889 0.2778  5.3849 0.7737 3.8704 
-2.0374 -4.5650 1.7284  -2.8483 -5.9368 -1.0571 2.2285  2.4194  0.8418  1.1749  0.7378  0.4573  
'X-RAY DIFFRACTION' 2  ? refined -20.4217 16.7938 -3.9602  0.4624 0.4403 0.3034  0.0971  -0.1324 0.1657  0.1138 0.4126 0.0130 
-0.2169 -0.0397 0.0747  -0.4507 0.2979  0.7346  0.0216  0.3854  0.2451  -0.1184 0.0082  -0.0178 
'X-RAY DIFFRACTION' 3  ? refined -15.6438 19.6111 -17.7818 0.4950 0.4458 0.2470  -0.2532 0.0934  0.2837  0.3795 0.4425 0.2238 
-0.0542 -0.2891 0.0014  0.0726  0.3986  0.2172  -0.4679 0.0835  -0.0211 -0.2901 -0.1348 -0.0524 
'X-RAY DIFFRACTION' 4  ? refined -11.9545 12.2317 -5.9837  0.2712 0.1846 -0.0802 0.0065  0.0986  0.2375  1.0577 0.3713 0.3129 
-0.2075 -0.3410 0.3219  0.0590  0.1880  0.2523  -0.2104 0.1532  0.1207  -0.0161 0.1355  0.5112  
'X-RAY DIFFRACTION' 5  ? refined -26.7930 5.3209  -8.8757  0.2278 0.2523 0.4407  0.0019  -0.0539 0.2064  0.0026 1.4907 0.3037 
0.0418  -0.0055 0.2320  -0.3057 0.2921  0.1966  0.0677  0.1992  0.5925  -0.3066 -0.2422 -0.2963 
'X-RAY DIFFRACTION' 6  ? refined -14.4746 0.2822  -19.2058 0.3317 0.3633 -0.1222 0.0399  -0.1354 0.1062  0.7045 0.6170 0.2401 
-0.3702 -0.0859 0.3555  -0.1155 0.6904  0.1552  -0.8134 0.1623  0.3137  0.1195  -0.3349 -0.2709 
'X-RAY DIFFRACTION' 7  ? refined -12.8211 2.6676  -18.1469 0.2731 0.4300 -0.1280 -0.0655 0.0546  -0.0005 1.3058 0.4901 0.2320 
0.4380  0.5493  0.1672  -0.0619 0.5720  -0.0842 -0.5927 0.0870  -0.0597 0.3174  0.1832  0.2775  
'X-RAY DIFFRACTION' 8  ? refined -5.9192  13.0678 0.4037   0.3447 0.3107 -0.0106 0.0736  -0.0306 0.0177  0.5716 0.1538 0.0683 
-0.2997 0.2012  -0.1026 0.0715  -0.3953 0.0485  0.4310  -0.0827 -0.0638 -0.1182 0.2224  -0.1632 
'X-RAY DIFFRACTION' 9  ? refined -14.9195 8.1300  -12.8518 0.2290 0.2769 -0.3328 0.1554  -0.1186 0.4485  1.0090 0.6380 0.1735 
0.7938  -0.4104 -0.3305 0.0903  0.5543  0.4174  -0.2108 0.1730  0.3104  -0.0386 -0.1119 0.3344  
'X-RAY DIFFRACTION' 10 ? refined -18.8826 4.8319  -7.7563  0.2444 0.2694 0.3553  0.0234  -0.0746 0.2465  0.4928 0.1086 0.2812 
0.2358  0.0707  0.0333  0.0063  0.3909  0.2893  -0.3226 0.0898  0.4869  0.0245  0.1950  0.1762  
'X-RAY DIFFRACTION' 11 ? refined -37.2413 14.4416 -5.8260  0.1974 0.3055 0.9248  0.1240  -0.1279 0.2185  0.6787 0.2140 0.4072 
-0.0843 -0.2231 -0.1110 0.1738  0.1596  0.5899  -0.0422 -0.0330 0.0203  -0.1747 -0.1109 0.2583  
'X-RAY DIFFRACTION' 12 ? refined -44.4290 15.6755 -9.8663  0.2080 0.3742 0.8368  0.1712  -0.0188 -0.0961 0.7774 0.2122 0.6586 
-0.2542 -0.0993 0.0214  0.2324  0.5441  -0.1873 -0.2484 -0.2563 -0.0326 -0.0900 -0.2697 0.0190  
'X-RAY DIFFRACTION' 13 ? refined -35.0005 25.6814 -7.1835  0.1617 0.4238 0.8595  0.1662  0.1362  0.3269  1.4272 0.8325 0.1565 
-0.2698 -0.1750 -0.1390 -0.1006 -0.0933 0.1700  0.1723  0.2011  -0.0015 -0.0658 -0.0714 -0.4133 
'X-RAY DIFFRACTION' 14 ? refined -37.8843 30.4691 -14.8877 0.4228 0.3811 0.8870  -0.0335 -0.0718 0.3909  0.0681 0.2363 0.0028 
0.1277  0.0156  0.0282  0.0382  0.0982  0.1402  -0.0188 0.1873  0.5507  0.2670  -0.2590 0.0609  
'X-RAY DIFFRACTION' 15 ? refined -46.9491 25.3512 -9.0221  0.4038 0.5281 0.8797  0.2565  0.0319  0.2037  0.5078 0.8997 1.1982 
0.6137  0.2492  0.6980  -0.4515 0.2405  -0.4764 0.1885  0.1113  0.1777  -0.7709 -0.6286 0.0640  
'X-RAY DIFFRACTION' 16 ? refined -46.6620 18.1845 -13.3816 0.3455 0.4249 0.8910  0.0820  -0.0645 0.1411  0.1332 0.2512 0.1776 
0.1613  -0.0028 0.0943  0.2657  0.2208  -0.3354 -0.1527 0.1763  0.2642  0.0637  -0.1891 0.0054  
'X-RAY DIFFRACTION' 17 ? refined -35.2828 21.0906 -15.3401 0.5705 0.4399 0.7671  0.2786  -0.1137 0.1588  0.8540 0.5689 0.5371 
0.6915  0.2476  0.2566  0.5583  0.6288  0.3078  -0.5420 -0.2661 0.4352  -0.0892 -0.3916 0.0379  
'X-RAY DIFFRACTION' 18 ? refined -40.5863 29.9535 -7.1930  0.3872 0.3742 1.2508  -0.0467 -0.0162 0.2693  0.4308 1.3673 0.6960 
-0.1909 0.0234  0.9490  -0.0952 0.1811  0.7719  -0.2851 -0.1493 0.3841  -0.4943 -0.0680 -0.3045 
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
'X-RAY DIFFRACTION' 1  1  ? ? ? ? ? ? ? ? ? 
;chain 'A' and resseq 201
;
'X-RAY DIFFRACTION' 2  2  ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resseq 1:15)
;
'X-RAY DIFFRACTION' 3  3  ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resseq 16:28)
;
'X-RAY DIFFRACTION' 4  4  ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resseq 29:48)
;
'X-RAY DIFFRACTION' 5  5  ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resseq 49:65)
;
'X-RAY DIFFRACTION' 6  6  ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resseq 66:75)
;
'X-RAY DIFFRACTION' 7  7  ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resseq 76:85)
;
'X-RAY DIFFRACTION' 8  8  ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resseq 86:94)
;
'X-RAY DIFFRACTION' 9  9  ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resseq 95:131)
;
'X-RAY DIFFRACTION' 10 10 ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resseq 132:153)
;
'X-RAY DIFFRACTION' 11 11 ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resseq 1:21)
;
'X-RAY DIFFRACTION' 12 12 ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resseq 22:40)
;
'X-RAY DIFFRACTION' 13 13 ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resseq 41:56)
;
'X-RAY DIFFRACTION' 14 14 ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resseq 57:75)
;
'X-RAY DIFFRACTION' 15 15 ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resseq 76:94)
;
'X-RAY DIFFRACTION' 16 16 ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resseq 95:104)
;
'X-RAY DIFFRACTION' 17 17 ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resseq 105:120)
;
'X-RAY DIFFRACTION' 18 18 ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resseq 121:153)
;
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
'PROTEUM PLUS' 'data collection' PLUS                         ? 1 
PHASER         phasing           .                            ? 2 
PHENIX         refinement        '(phenix.refine: 1.7.1_743)' ? 3 
HKL-2000       'data reduction'  .                            ? 4 
HKL-2000       'data scaling'    .                            ? 5 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 OD1 B ASP 52  ? ? OG1 B THR 54  ? ? 1.85 
2 1 O   B ARG 143 ? ? O   B HOH 306 ? ? 1.96 
3 1 OD2 B ASP 125 ? ? OG  B SER 134 ? ? 2.18 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 THR A 2   ? ? 1.90    164.63  
2  1 LYS A 3   ? ? 27.44   111.95  
3  1 GLU A 24  ? ? -68.56  -161.99 
4  1 ALA A 55  ? ? -100.30 45.37   
5  1 GLU A 78  ? ? -69.67  83.86   
6  1 ASP A 92  ? ? 89.07   -1.53   
7  1 SER A 107 ? ? -87.87  -94.92  
8  1 ASP A 109 ? ? 63.82   -75.18  
9  1 HIS B 46  ? ? 171.01  -168.46 
10 1 SER B 68  ? ? 40.56   71.52   
11 1 LYS B 122 ? ? -118.12 -164.51 
12 1 ASP B 125 ? ? -59.54  -5.10   
13 1 LEU B 126 ? ? 48.85   15.63   
14 1 LYS B 128 ? ? -92.98  37.34   
# 
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 LYS 3   ? CG  ? A LYS 3   CG  
2  1 Y 1 A LYS 3   ? CD  ? A LYS 3   CD  
3  1 Y 1 A LYS 3   ? CE  ? A LYS 3   CE  
4  1 Y 1 A LYS 3   ? NZ  ? A LYS 3   NZ  
5  1 Y 0 A LYS 9   ? CD  ? A LYS 9   CD  
6  1 Y 0 A GLU 21  ? CG  ? A GLU 21  CG  
7  1 Y 1 A LYS 23  ? CG  ? A LYS 23  CG  
8  1 Y 1 A LYS 23  ? CD  ? A LYS 23  CD  
9  1 Y 1 A LYS 23  ? CE  ? A LYS 23  CE  
10 1 Y 1 A LYS 23  ? NZ  ? A LYS 23  NZ  
11 1 Y 1 A GLU 24  ? CG  ? A GLU 24  CG  
12 1 Y 1 A GLU 24  ? CD  ? A GLU 24  CD  
13 1 Y 1 A GLU 24  ? OE1 ? A GLU 24  OE1 
14 1 Y 1 A GLU 24  ? OE2 ? A GLU 24  OE2 
15 1 Y 0 A SER 25  ? OG  ? A SER 25  OG  
16 1 Y 0 A ASN 26  ? OD1 ? A ASN 26  OD1 
17 1 Y 0 A ASN 26  ? ND2 ? A ASN 26  ND2 
18 1 Y 0 A LYS 30  ? CG  ? A LYS 30  CG  
19 1 Y 0 A LYS 30  ? CD  ? A LYS 30  CD  
20 1 Y 1 A LYS 36  ? CG  ? A LYS 36  CG  
21 1 Y 1 A LYS 36  ? CD  ? A LYS 36  CD  
22 1 Y 1 A LYS 36  ? CE  ? A LYS 36  CE  
23 1 Y 1 A LYS 36  ? NZ  ? A LYS 36  NZ  
24 1 Y 0 B LYS 9   ? CD  ? B LYS 9   CD  
25 1 Y 0 B LYS 9   ? CE  ? B LYS 9   CE  
26 1 Y 0 B LYS 9   ? NZ  ? B LYS 9   NZ  
27 1 Y 0 B GLN 22  ? CB  ? B GLN 22  CB  
28 1 Y 0 B LYS 23  ? CE  ? B LYS 23  CE  
29 1 Y 0 B LYS 23  ? NZ  ? B LYS 23  NZ  
30 1 Y 0 B PRO 28  ? CG  ? B PRO 28  CG  
31 1 Y 0 B PRO 28  ? CD  ? B PRO 28  CD  
32 1 Y 1 B LYS 30  ? CG  ? B LYS 30  CG  
33 1 Y 1 B LYS 30  ? CD  ? B LYS 30  CD  
34 1 Y 1 B LYS 30  ? CE  ? B LYS 30  CE  
35 1 Y 1 B LYS 30  ? NZ  ? B LYS 30  NZ  
36 1 Y 1 B LYS 36  ? CG  ? B LYS 36  CG  
37 1 Y 1 B LYS 36  ? CD  ? B LYS 36  CD  
38 1 Y 1 B LYS 36  ? CE  ? B LYS 36  CE  
39 1 Y 1 B LYS 36  ? NZ  ? B LYS 36  NZ  
40 1 Y 1 B LYS 70  ? CG  ? B LYS 70  CG  
41 1 Y 1 B LYS 70  ? CD  ? B LYS 70  CD  
42 1 Y 1 B LYS 70  ? CE  ? B LYS 70  CE  
43 1 Y 1 B LYS 70  ? NZ  ? B LYS 70  NZ  
44 1 Y 0 B LYS 75  ? CE  ? B LYS 75  CE  
45 1 Y 0 B LYS 75  ? NZ  ? B LYS 75  NZ  
46 1 Y 0 B GLU 78  ? N   ? B GLU 78  N   
47 1 Y 0 B ARG 79  ? CG  ? B ARG 79  CG  
48 1 Y 0 B LYS 91  ? CD  ? B LYS 91  CD  
49 1 Y 0 B LYS 91  ? CE  ? B LYS 91  CE  
50 1 Y 1 B GLU 100 ? CG  ? B GLU 100 CG  
51 1 Y 1 B GLU 100 ? CD  ? B GLU 100 CD  
52 1 Y 1 B GLU 100 ? OE1 ? B GLU 100 OE1 
53 1 Y 1 B GLU 100 ? OE2 ? B GLU 100 OE2 
54 1 Y 0 B HIS 110 ? CB  ? B HIS 110 CB  
55 1 Y 1 B ILE 112 ? CG1 ? B ILE 112 CG1 
56 1 Y 1 B ILE 112 ? CG2 ? B ILE 112 CG2 
57 1 Y 1 B ILE 112 ? CD1 ? B ILE 112 CD1 
58 1 Y 0 B LYS 122 ? CD  ? B LYS 122 CD  
59 1 Y 0 B LYS 122 ? CE  ? B LYS 122 CE  
60 1 Y 0 B LYS 122 ? NZ  ? B LYS 122 NZ  
61 1 N 1 A CYS 201 ? OXT ? C CYS 1   OXT 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 B GLU 24 ? B GLU 24 
2 1 Y 1 B SER 25 ? B SER 25 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 CYSTEINE          CYS 
3 'ZINC ION'        ZN  
4 'COPPER (II) ION' CU  
5 water             HOH 
# 
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 CYS 1  201 146 CYS CYS A . 
D 3 ZN  1  202 1   ZN  ZN  A . 
E 4 CU  1  203 1   CU  CU  A . 
F 3 ZN  1  201 2   ZN  ZN  B . 
G 4 CU  1  202 2   CU  CU  B . 
H 5 HOH 1  301 1   HOH HOH A . 
H 5 HOH 2  302 4   HOH HOH A . 
H 5 HOH 3  303 5   HOH HOH A . 
H 5 HOH 4  304 11  HOH HOH A . 
H 5 HOH 5  305 17  HOH HOH A . 
H 5 HOH 6  306 18  HOH HOH A . 
H 5 HOH 7  307 23  HOH HOH A . 
H 5 HOH 8  308 24  HOH HOH A . 
H 5 HOH 9  309 25  HOH HOH A . 
H 5 HOH 10 310 29  HOH HOH A . 
H 5 HOH 11 311 36  HOH HOH A . 
H 5 HOH 12 312 41  HOH HOH A . 
H 5 HOH 13 313 56  HOH HOH A . 
H 5 HOH 14 314 69  HOH HOH A . 
H 5 HOH 15 315 70  HOH HOH A . 
H 5 HOH 16 316 71  HOH HOH A . 
H 5 HOH 17 317 72  HOH HOH A . 
H 5 HOH 18 318 76  HOH HOH A . 
I 5 HOH 1  301 9   HOH HOH B . 
I 5 HOH 2  302 12  HOH HOH B . 
I 5 HOH 3  303 22  HOH HOH B . 
I 5 HOH 4  304 33  HOH HOH B . 
I 5 HOH 5  305 55  HOH HOH B . 
I 5 HOH 6  306 77  HOH HOH B . 
# 
