data_1SPD
# 
_entry.id   1SPD 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.313 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   1SPD         
WWPDB D_1000176459 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        1SPD 
_pdbx_database_status.recvd_initial_deposition_date   1993-07-21 
_pdbx_database_status.deposit_site                    ? 
_pdbx_database_status.process_site                    BNL 
_pdbx_database_status.SG_entry                        . 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_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 
'Parge, H.E.'  1 
'Tainer, J.A.' 2 
# 
_citation.id                        primary 
_citation.title                     'Amyotrophic lateral sclerosis and structural defects in Cu,Zn superoxide dismutase.' 
_citation.journal_abbrev            Science 
_citation.journal_volume            261 
_citation.page_first                1047 
_citation.page_last                 1051 
_citation.year                      1993 
_citation.journal_id_ASTM           SCIEAS 
_citation.country                   US 
_citation.journal_id_ISSN           0036-8075 
_citation.journal_id_CSD            0038 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   8351519 
_citation.pdbx_database_id_DOI      ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Deng, H.X.'          1  ? 
primary 'Hentati, A.'         2  ? 
primary 'Tainer, J.A.'        3  ? 
primary 'Iqbal, Z.'           4  ? 
primary 'Cayabyab, A.'        5  ? 
primary 'Hung, W.Y.'          6  ? 
primary 'Getzoff, E.D.'       7  ? 
primary 'Hu, P.'              8  ? 
primary 'Herzfeldt, B.'       9  ? 
primary 'Roos, R.P.'          10 ? 
primary 'Warner, C.'          11 ? 
primary 'Deng, G.'            12 ? 
primary 'Soriano, E.'         13 ? 
primary 'Smyth, C.'           14 ? 
primary 'Parge, H.E.'         15 ? 
primary 'Ahmed, A.'           16 ? 
primary 'Roses, A.D.'         17 ? 
primary 'Hallewell, R.A.'     18 ? 
primary 'Pericak-Vance, M.A.' 19 ? 
primary 'Siddique, T.'        20 ? 
# 
_cell.entry_id           1SPD 
_cell.length_a           113.570 
_cell.length_b           113.570 
_cell.length_c           71.550 
_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                         1SPD 
_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' 15853.599 2 1.15.1.1 ? ? ? 
2 non-polymer syn 'COPPER (II) ION'      63.546    2 ?        ? ? ? 
3 non-polymer syn 'ZINC ION'             65.409    2 ?        ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   yes 
_entity_poly.pdbx_seq_one_letter_code       
;(ACE)ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPK
DEERHVGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;XATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEER
HVGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_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   ACE n 
1 2   ALA n 
1 3   THR n 
1 4   LYS n 
1 5   ALA n 
1 6   VAL n 
1 7   CYS n 
1 8   VAL n 
1 9   LEU n 
1 10  LYS n 
1 11  GLY n 
1 12  ASP n 
1 13  GLY n 
1 14  PRO n 
1 15  VAL n 
1 16  GLN n 
1 17  GLY n 
1 18  ILE n 
1 19  ILE n 
1 20  ASN n 
1 21  PHE n 
1 22  GLU n 
1 23  GLN n 
1 24  LYS n 
1 25  GLU n 
1 26  SER n 
1 27  ASN n 
1 28  GLY n 
1 29  PRO n 
1 30  VAL n 
1 31  LYS n 
1 32  VAL n 
1 33  TRP n 
1 34  GLY n 
1 35  SER n 
1 36  ILE n 
1 37  LYS n 
1 38  GLY n 
1 39  LEU n 
1 40  THR n 
1 41  GLU n 
1 42  GLY n 
1 43  LEU n 
1 44  HIS n 
1 45  GLY n 
1 46  PHE n 
1 47  HIS n 
1 48  VAL n 
1 49  HIS n 
1 50  GLU n 
1 51  PHE n 
1 52  GLY n 
1 53  ASP n 
1 54  ASN n 
1 55  THR n 
1 56  ALA n 
1 57  GLY n 
1 58  CYS n 
1 59  THR n 
1 60  SER n 
1 61  ALA n 
1 62  GLY n 
1 63  PRO n 
1 64  HIS n 
1 65  PHE n 
1 66  ASN n 
1 67  PRO n 
1 68  LEU n 
1 69  SER n 
1 70  ARG n 
1 71  LYS n 
1 72  HIS n 
1 73  GLY n 
1 74  GLY n 
1 75  PRO n 
1 76  LYS n 
1 77  ASP n 
1 78  GLU n 
1 79  GLU n 
1 80  ARG n 
1 81  HIS n 
1 82  VAL n 
1 83  GLY n 
1 84  ASP n 
1 85  LEU n 
1 86  GLY n 
1 87  ASN n 
1 88  VAL n 
1 89  THR n 
1 90  ALA n 
1 91  ASP n 
1 92  LYS n 
1 93  ASP n 
1 94  GLY n 
1 95  VAL n 
1 96  ALA n 
1 97  ASP n 
1 98  VAL n 
1 99  SER n 
1 100 ILE n 
1 101 GLU n 
1 102 ASP n 
1 103 SER n 
1 104 VAL n 
1 105 ILE n 
1 106 SER n 
1 107 LEU n 
1 108 SER n 
1 109 GLY n 
1 110 ASP n 
1 111 HIS n 
1 112 CYS n 
1 113 ILE n 
1 114 ILE n 
1 115 GLY n 
1 116 ARG n 
1 117 THR n 
1 118 LEU n 
1 119 VAL n 
1 120 VAL n 
1 121 HIS n 
1 122 GLU n 
1 123 LYS n 
1 124 ALA n 
1 125 ASP n 
1 126 ASP n 
1 127 LEU n 
1 128 GLY n 
1 129 LYS n 
1 130 GLY n 
1 131 GLY n 
1 132 ASN n 
1 133 GLU n 
1 134 GLU n 
1 135 SER n 
1 136 THR n 
1 137 LYS n 
1 138 THR n 
1 139 GLY n 
1 140 ASN n 
1 141 ALA n 
1 142 GLY n 
1 143 SER n 
1 144 ARG n 
1 145 LEU n 
1 146 ALA n 
1 147 CYS n 
1 148 GLY n 
1 149 VAL n 
1 150 ILE n 
1 151 GLY n 
1 152 ILE n 
1 153 ALA n 
1 154 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                     Homo 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_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      ? 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     ? 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    SODC_HUMAN 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_db_accession          P00441 
_struct_ref.pdbx_align_begin           1 
_struct_ref.pdbx_seq_one_letter_code   
;ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_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 1SPD A 2 ? 154 ? P00441 1 ? 153 ? 1 153 
2 1 1SPD B 2 ? 154 ? P00441 1 ? 153 ? 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 
ACE non-polymer         . 'ACETYL GROUP'    ? 'C2 H4 O'        44.053  
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 
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          1SPD 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   ? 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      4.20 
_exptl_crystal.density_percent_sol   70.71 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           ? 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   ? 
_diffrn_radiation.pdbx_diffrn_protocol             ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   . 
_diffrn_radiation_wavelength.wt           1.0 
# 
_refine.entry_id                                 1SPD 
_refine.ls_number_reflns_obs                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          5.0 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             5.0 
_refine.ls_d_res_high                            2.4 
_refine.ls_percent_reflns_obs                    ? 
_refine.ls_R_factor_obs                          0.224 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.224 
_refine.ls_R_factor_R_free                       ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_number_reflns_R_free                  ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.B_iso_mean                               ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_B                             ? 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_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_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        2226 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         4 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               2230 
_refine_hist.d_res_high                       2.4 
_refine_hist.d_res_low                        5.0 
# 
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_refine_id 
_refine_ls_restr.pdbx_restraint_function 
x_bond_d                0.04 ? ? ? 'X-RAY DIFFRACTION' ? 
x_bond_d_na             ?    ? ? ? 'X-RAY DIFFRACTION' ? 
x_bond_d_prot           ?    ? ? ? 'X-RAY DIFFRACTION' ? 
x_angle_d               ?    ? ? ? 'X-RAY DIFFRACTION' ? 
x_angle_d_na            ?    ? ? ? 'X-RAY DIFFRACTION' ? 
x_angle_d_prot          ?    ? ? ? 'X-RAY DIFFRACTION' ? 
x_angle_deg             3.5  ? ? ? 'X-RAY DIFFRACTION' ? 
x_angle_deg_na          ?    ? ? ? 'X-RAY DIFFRACTION' ? 
x_angle_deg_prot        ?    ? ? ? 'X-RAY DIFFRACTION' ? 
x_dihedral_angle_d      ?    ? ? ? 'X-RAY DIFFRACTION' ? 
x_dihedral_angle_d_na   ?    ? ? ? 'X-RAY DIFFRACTION' ? 
x_dihedral_angle_d_prot ?    ? ? ? 'X-RAY DIFFRACTION' ? 
x_improper_angle_d      ?    ? ? ? 'X-RAY DIFFRACTION' ? 
x_improper_angle_d_na   ?    ? ? ? 'X-RAY DIFFRACTION' ? 
x_improper_angle_d_prot ?    ? ? ? 'X-RAY DIFFRACTION' ? 
x_mcbond_it             ?    ? ? ? 'X-RAY DIFFRACTION' ? 
x_mcangle_it            ?    ? ? ? 'X-RAY DIFFRACTION' ? 
x_scbond_it             ?    ? ? ? 'X-RAY DIFFRACTION' ? 
x_scangle_it            ?    ? ? ? 'X-RAY DIFFRACTION' ? 
# 
_struct_ncs_oper.id             1 
_struct_ncs_oper.code           given 
_struct_ncs_oper.details        ? 
_struct_ncs_oper.matrix[1][1]   -0.998800 
_struct_ncs_oper.matrix[1][2]   0.009900 
_struct_ncs_oper.matrix[1][3]   -0.048600 
_struct_ncs_oper.matrix[2][1]   -0.005600 
_struct_ncs_oper.matrix[2][2]   -0.996200 
_struct_ncs_oper.matrix[2][3]   -0.087200 
_struct_ncs_oper.matrix[3][1]   -0.049300 
_struct_ncs_oper.matrix[3][2]   -0.086800 
_struct_ncs_oper.matrix[3][3]   0.995000 
_struct_ncs_oper.vector[1]      57.20400 
_struct_ncs_oper.vector[2]      -32.03400 
_struct_ncs_oper.vector[3]      0.28400 
# 
_struct.entry_id                  1SPD 
_struct.title                     'AMYOTROPHIC LATERAL SCLEROSIS AND STRUCTURAL DEFECTS IN CU,ZN SUPEROXIDE DISMUTASE' 
_struct.pdbx_descriptor           'SUPEROXIDE DISMUTASE (E.C.1.15.1.1)' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        1SPD 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
_struct_keywords.text            'OXIDOREDUCTASE, SUPEROXIDE ACCEPTOR' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 2 ? 
F N N 3 ? 
# 
_struct_biol.id                    1 
_struct_biol.details               
;THE TRANSFORMATION PRESENTED ON *MTRIX* RECORDS BELOW WILL
YIELD APPROXIMATE COORDINATES FOR CHAIN *A* WHEN APPLIED TO
CHAIN *B*.
;
_struct_biol.pdbx_parent_biol_id   ? 
# 
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 HA GLU A 134 ? THR A 138 ? GLU A 133 THR A 137 1 ? 5 
HELX_P HELX_P2 HB GLU B 134 ? THR B 138 ? GLU B 133 THR B 137 1 ? 5 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
disulf1  disulf ?    ? A CYS 58 SG  ? ? ? 1_555 A CYS 147 SG  ? ? A CYS 57  A CYS 146 1_555 ? ? ? ? ? ? ? 2.095 ? 
disulf2  disulf ?    ? B CYS 58 SG  ? ? ? 1_555 B CYS 147 SG  ? ? B CYS 57  B CYS 146 1_555 ? ? ? ? ? ? ? 2.055 ? 
covale1  covale one  ? A ACE 1  CH3 ? ? ? 1_555 A ALA 2   N   ? ? A ACE 0   A ALA 1   1_555 ? ? ? ? ? ? ? 1.493 ? 
covale2  covale one  ? B ACE 1  CH3 ? ? ? 1_555 B ALA 2   N   ? ? B ACE 0   B ALA 1   1_555 ? ? ? ? ? ? ? 1.579 ? 
covale3  covale both ? A ACE 1  C   ? ? ? 1_555 A ALA 2   N   ? ? A ACE 0   A ALA 1   1_555 ? ? ? ? ? ? ? 1.847 ? 
metalc1  metalc ?    ? C CU  .  CU  ? ? ? 1_555 A HIS 121 NE2 ? ? A CU  154 A HIS 120 1_555 ? ? ? ? ? ? ? 2.077 ? 
metalc2  metalc ?    ? C CU  .  CU  ? ? ? 1_555 A HIS 47  ND1 ? ? A CU  154 A HIS 46  1_555 ? ? ? ? ? ? ? 2.047 ? 
metalc3  metalc ?    ? C CU  .  CU  ? ? ? 1_555 A HIS 64  NE2 ? ? A CU  154 A HIS 63  1_555 ? ? ? ? ? ? ? 2.090 ? 
metalc4  metalc ?    ? C CU  .  CU  ? ? ? 1_555 A HIS 49  NE2 ? ? A CU  154 A HIS 48  1_555 ? ? ? ? ? ? ? 2.125 ? 
metalc5  metalc ?    ? D ZN  .  ZN  ? ? ? 1_555 A HIS 72  ND1 ? ? A ZN  155 A HIS 71  1_555 ? ? ? ? ? ? ? 2.130 ? 
metalc6  metalc ?    ? D ZN  .  ZN  ? ? ? 1_555 A HIS 64  ND1 ? ? A ZN  155 A HIS 63  1_555 ? ? ? ? ? ? ? 2.052 ? 
metalc7  metalc ?    ? D ZN  .  ZN  ? ? ? 1_555 A HIS 81  ND1 ? ? A ZN  155 A HIS 80  1_555 ? ? ? ? ? ? ? 2.080 ? 
metalc8  metalc ?    ? D ZN  .  ZN  ? ? ? 1_555 A ASP 84  OD2 ? ? A ZN  155 A ASP 83  1_555 ? ? ? ? ? ? ? 1.949 ? 
covale4  covale both ? B ACE 1  C   ? ? ? 1_555 B ALA 2   N   ? ? B ACE 0   B ALA 1   1_555 ? ? ? ? ? ? ? 1.802 ? 
metalc9  metalc ?    ? E CU  .  CU  ? ? ? 1_555 B HIS 121 NE2 ? ? B CU  154 B HIS 120 1_555 ? ? ? ? ? ? ? 2.022 ? 
metalc10 metalc ?    ? E CU  .  CU  ? ? ? 1_555 B HIS 64  NE2 ? ? B CU  154 B HIS 63  1_555 ? ? ? ? ? ? ? 2.150 ? 
metalc11 metalc ?    ? E CU  .  CU  ? ? ? 1_555 B HIS 47  ND1 ? ? B CU  154 B HIS 46  1_555 ? ? ? ? ? ? ? 2.151 ? 
metalc12 metalc ?    ? E CU  .  CU  ? ? ? 1_555 B HIS 49  NE2 ? ? B CU  154 B HIS 48  1_555 ? ? ? ? ? ? ? 2.126 ? 
metalc13 metalc ?    ? F ZN  .  ZN  ? ? ? 1_555 B HIS 64  ND1 ? ? B ZN  155 B HIS 63  1_555 ? ? ? ? ? ? ? 2.195 ? 
metalc14 metalc ?    ? F ZN  .  ZN  ? ? ? 1_555 B ASP 84  OD2 ? ? B ZN  155 B ASP 83  1_555 ? ? ? ? ? ? ? 2.002 ? 
metalc15 metalc ?    ? F ZN  .  ZN  ? ? ? 1_555 B HIS 81  ND1 ? ? B ZN  155 B HIS 80  1_555 ? ? ? ? ? ? ? 2.083 ? 
metalc16 metalc ?    ? F ZN  .  ZN  ? ? ? 1_555 B HIS 72  ND1 ? ? B ZN  155 B HIS 71  1_555 ? ? ? ? ? ? ? 2.162 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
metalc ? ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
SA ? 9 ? 
SB ? 9 ? 
# 
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 
SA 1 2 ? anti-parallel 
SA 2 3 ? parallel      
SA 3 4 ? anti-parallel 
SA 4 5 ? parallel      
SA 5 6 ? anti-parallel 
SA 6 7 ? parallel      
SA 7 8 ? anti-parallel 
SA 8 9 ? parallel      
SB 1 2 ? anti-parallel 
SB 2 3 ? parallel      
SB 3 4 ? anti-parallel 
SB 4 5 ? parallel      
SB 5 6 ? anti-parallel 
SB 6 7 ? parallel      
SB 7 8 ? anti-parallel 
SB 8 9 ? 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 
SA 1 ALA A 5   ? LYS A 10  ? ALA A 4   LYS A 9   
SA 2 GLN A 16  ? GLU A 22  ? GLN A 15  GLU A 21  
SA 3 VAL A 30  ? LYS A 31  ? VAL A 29  LYS A 30  
SA 4 VAL A 95  ? ASP A 102 ? VAL A 94  ASP A 101 
SA 5 GLY A 86  ? ALA A 90  ? GLY A 85  ALA A 89  
SA 6 GLY A 42  ? HIS A 49  ? GLY A 41  HIS A 48  
SA 7 ARG A 116 ? HIS A 121 ? ARG A 115 HIS A 120 
SA 8 CYS A 147 ? GLY A 151 ? CYS A 146 GLY A 150 
SA 9 ALA A 5   ? LYS A 10  ? ALA A 4   LYS A 9   
SB 1 ALA B 5   ? LYS B 10  ? ALA B 4   LYS B 9   
SB 2 GLN B 16  ? GLU B 22  ? GLN B 15  GLU B 21  
SB 3 VAL B 30  ? LYS B 31  ? VAL B 29  LYS B 30  
SB 4 VAL B 95  ? ASP B 102 ? VAL B 94  ASP B 101 
SB 5 GLY B 86  ? ALA B 90  ? GLY B 85  ALA B 89  
SB 6 GLY B 42  ? HIS B 49  ? GLY B 41  HIS B 48  
SB 7 ARG B 116 ? HIS B 121 ? ARG B 115 HIS B 120 
SB 8 CYS B 147 ? GLY B 151 ? CYS B 146 GLY B 150 
SB 9 ALA B 5   ? LYS B 10  ? ALA B 4   LYS B 9   
# 
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 
SA 1 2 O ALA A 5   ? O ALA A 4   N PHE A 21  ? N PHE A 20  
SA 2 3 O GLU A 22  ? O GLU A 21  N LYS A 31  ? N LYS A 30  
SA 5 6 O VAL A 88  ? O VAL A 87  N HIS A 44  ? N HIS A 43  
SA 6 7 O HIS A 47  ? O HIS A 46  N VAL A 119 ? N VAL A 118 
SA 7 8 O LEU A 118 ? O LEU A 117 N GLY A 148 ? N GLY A 147 
SA 8 9 O VAL A 149 ? O VAL A 148 N VAL A 8   ? N VAL A 7   
SB 1 2 O ALA B 5   ? O ALA B 4   N PHE B 21  ? N PHE B 20  
SB 2 3 O GLU B 22  ? O GLU B 21  N LYS B 31  ? N LYS B 30  
SB 5 6 O VAL B 88  ? O VAL B 87  N HIS B 44  ? N HIS B 43  
SB 6 7 O HIS B 47  ? O HIS B 46  N VAL B 119 ? N VAL B 118 
SB 7 8 O LEU B 118 ? O LEU B 117 N GLY B 148 ? N GLY B 147 
SB 8 9 O VAL B 149 ? O VAL B 148 N VAL B 8   ? N VAL B 7   
# 
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 
CUA Unknown  ? ? ? ? 4 ?                                   
ZNA Unknown  ? ? ? ? 4 ?                                   
CUB Unknown  ? ? ? ? 4 ?                                   
ZNB Unknown  ? ? ? ? 4 ?                                   
AC1 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE CU A 154' 
AC2 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN A 155' 
AC3 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE CU B 154' 
AC4 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN B 155' 
# 
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  CUA 4 HIS A 47  ? HIS A 46  . ? 1_555 ? 
2  CUA 4 HIS A 49  ? HIS A 48  . ? 1_555 ? 
3  CUA 4 HIS A 64  ? HIS A 63  . ? 1_555 ? 
4  CUA 4 HIS A 121 ? HIS A 120 . ? 1_555 ? 
5  ZNA 4 HIS A 64  ? HIS A 63  . ? 1_555 ? 
6  ZNA 4 HIS A 72  ? HIS A 71  . ? 1_555 ? 
7  ZNA 4 HIS A 81  ? HIS A 80  . ? 1_555 ? 
8  ZNA 4 ASP A 84  ? ASP A 83  . ? 1_555 ? 
9  CUB 4 HIS B 47  ? HIS B 46  . ? 1_555 ? 
10 CUB 4 HIS B 49  ? HIS B 48  . ? 1_555 ? 
11 CUB 4 HIS B 64  ? HIS B 63  . ? 1_555 ? 
12 CUB 4 HIS B 121 ? HIS B 120 . ? 1_555 ? 
13 ZNB 4 HIS B 64  ? HIS B 63  . ? 1_555 ? 
14 ZNB 4 HIS B 72  ? HIS B 71  . ? 1_555 ? 
15 ZNB 4 HIS B 81  ? HIS B 80  . ? 1_555 ? 
16 ZNB 4 ASP B 84  ? ASP B 83  . ? 1_555 ? 
17 AC1 4 HIS A 47  ? HIS A 46  . ? 1_555 ? 
18 AC1 4 HIS A 49  ? HIS A 48  . ? 1_555 ? 
19 AC1 4 HIS A 64  ? HIS A 63  . ? 1_555 ? 
20 AC1 4 HIS A 121 ? HIS A 120 . ? 1_555 ? 
21 AC2 4 HIS A 64  ? HIS A 63  . ? 1_555 ? 
22 AC2 4 HIS A 72  ? HIS A 71  . ? 1_555 ? 
23 AC2 4 HIS A 81  ? HIS A 80  . ? 1_555 ? 
24 AC2 4 ASP A 84  ? ASP A 83  . ? 1_555 ? 
25 AC3 4 HIS B 47  ? HIS B 46  . ? 1_555 ? 
26 AC3 4 HIS B 49  ? HIS B 48  . ? 1_555 ? 
27 AC3 4 HIS B 64  ? HIS B 63  . ? 1_555 ? 
28 AC3 4 HIS B 121 ? HIS B 120 . ? 1_555 ? 
29 AC4 4 HIS B 64  ? HIS B 63  . ? 1_555 ? 
30 AC4 4 HIS B 72  ? HIS B 71  . ? 1_555 ? 
31 AC4 4 HIS B 81  ? HIS B 80  . ? 1_555 ? 
32 AC4 4 ASP B 84  ? ASP B 83  . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          1SPD 
_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                    1SPD 
_atom_sites.fract_transf_matrix[1][1]   0.008805 
_atom_sites.fract_transf_matrix[1][2]   0.005084 
_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]   0.010167 
_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]   0.013976 
_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 
HETATM 1    C  C   . ACE A 1 1   ? 33.042 -11.070 24.499 1.00 8.74  ? 0   ACE A C   1 
HETATM 2    O  O   . ACE A 1 1   ? 33.828 -10.864 24.277 1.00 9.48  ? 0   ACE A O   1 
HETATM 3    C  CH3 . ACE A 1 1   ? 32.117 -11.386 24.809 1.00 8.49  ? 0   ACE A CH3 1 
ATOM   4    N  N   . ALA A 1 2   ? 31.457 -10.139 24.320 1.00 8.47  ? 1   ALA A N   1 
ATOM   5    C  CA  . ALA A 1 2   ? 31.502 -8.875  23.700 1.00 9.32  ? 1   ALA A CA  1 
ATOM   6    C  C   . ALA A 1 2   ? 31.926 -8.678  22.211 1.00 10.84 ? 1   ALA A C   1 
ATOM   7    O  O   . ALA A 1 2   ? 32.520 -9.312  21.343 1.00 7.49  ? 1   ALA A O   1 
ATOM   8    C  CB  . ALA A 1 2   ? 32.564 -8.031  24.414 1.00 8.06  ? 1   ALA A CB  1 
ATOM   9    N  N   . THR A 1 3   ? 31.431 -7.410  21.996 1.00 12.15 ? 2   THR A N   1 
ATOM   10   C  CA  . THR A 1 3   ? 31.513 -6.545  20.829 1.00 10.77 ? 2   THR A CA  1 
ATOM   11   C  C   . THR A 1 3   ? 30.857 -6.714  19.505 1.00 8.48  ? 2   THR A C   1 
ATOM   12   O  O   . THR A 1 3   ? 30.530 -7.779  19.072 1.00 6.92  ? 2   THR A O   1 
ATOM   13   C  CB  . THR A 1 3   ? 33.164 -6.595  20.746 1.00 10.15 ? 2   THR A CB  1 
ATOM   14   O  OG1 . THR A 1 3   ? 33.414 -5.765  22.035 1.00 8.67  ? 2   THR A OG1 1 
ATOM   15   C  CG2 . THR A 1 3   ? 33.716 -6.262  19.381 1.00 10.41 ? 2   THR A CG2 1 
ATOM   16   N  N   . LYS A 1 4   ? 30.749 -5.563  18.856 1.00 8.33  ? 3   LYS A N   1 
ATOM   17   C  CA  . LYS A 1 4   ? 30.170 -5.188  17.544 1.00 8.24  ? 3   LYS A CA  1 
ATOM   18   C  C   . LYS A 1 4   ? 30.090 -6.279  16.532 1.00 7.24  ? 3   LYS A C   1 
ATOM   19   O  O   . LYS A 1 4   ? 30.957 -6.775  15.833 1.00 6.72  ? 3   LYS A O   1 
ATOM   20   C  CB  . LYS A 1 4   ? 31.004 -4.051  16.912 1.00 8.52  ? 3   LYS A CB  1 
ATOM   21   C  CG  . LYS A 1 4   ? 30.481 -3.538  15.602 1.00 6.21  ? 3   LYS A CG  1 
ATOM   22   C  CD  . LYS A 1 4   ? 31.306 -2.698  14.704 1.00 6.46  ? 3   LYS A CD  1 
ATOM   23   C  CE  . LYS A 1 4   ? 31.601 -1.245  14.898 1.00 2.00  ? 3   LYS A CE  1 
ATOM   24   N  NZ  . LYS A 1 4   ? 32.460 -1.409  16.150 1.00 2.00  ? 3   LYS A NZ  1 
ATOM   25   N  N   . ALA A 1 5   ? 28.869 -6.714  16.413 1.00 8.85  ? 4   ALA A N   1 
ATOM   26   C  CA  . ALA A 1 5   ? 28.604 -7.823  15.475 1.00 10.76 ? 4   ALA A CA  1 
ATOM   27   C  C   . ALA A 1 5   ? 28.673 -7.422  13.973 1.00 9.83  ? 4   ALA A C   1 
ATOM   28   O  O   . ALA A 1 5   ? 28.880 -6.125  13.762 1.00 8.63  ? 4   ALA A O   1 
ATOM   29   C  CB  . ALA A 1 5   ? 27.202 -8.333  15.766 1.00 11.30 ? 4   ALA A CB  1 
ATOM   30   N  N   . VAL A 1 6   ? 28.457 -8.659  13.290 1.00 4.66  ? 5   VAL A N   1 
ATOM   31   C  CA  . VAL A 1 6   ? 28.458 -8.125  11.872 1.00 5.90  ? 5   VAL A CA  1 
ATOM   32   C  C   . VAL A 1 6   ? 27.477 -9.066  11.153 1.00 7.58  ? 5   VAL A C   1 
ATOM   33   O  O   . VAL A 1 6   ? 26.891 -10.069 11.742 1.00 7.01  ? 5   VAL A O   1 
ATOM   34   C  CB  . VAL A 1 6   ? 29.726 -8.033  11.053 1.00 6.61  ? 5   VAL A CB  1 
ATOM   35   C  CG1 . VAL A 1 6   ? 30.110 -9.424  10.449 1.00 5.87  ? 5   VAL A CG1 1 
ATOM   36   C  CG2 . VAL A 1 6   ? 29.698 -6.943  9.948  1.00 3.31  ? 5   VAL A CG2 1 
ATOM   37   N  N   . CYS A 1 7   ? 27.398 -8.589  9.827  1.00 9.96  ? 6   CYS A N   1 
ATOM   38   C  CA  . CYS A 1 7   ? 26.501 -9.519  9.027  1.00 10.46 ? 6   CYS A CA  1 
ATOM   39   C  C   . CYS A 1 7   ? 26.522 -8.757  7.709  1.00 9.32  ? 6   CYS A C   1 
ATOM   40   O  O   . CYS A 1 7   ? 26.387 -7.566  7.765  1.00 8.22  ? 6   CYS A O   1 
ATOM   41   C  CB  . CYS A 1 7   ? 25.116 -9.798  9.548  1.00 9.92  ? 6   CYS A CB  1 
ATOM   42   S  SG  . CYS A 1 7   ? 24.454 -11.461 9.141  1.00 8.05  ? 6   CYS A SG  1 
ATOM   43   N  N   . VAL A 1 8   ? 26.671 -9.566  6.744  1.00 8.80  ? 7   VAL A N   1 
ATOM   44   C  CA  . VAL A 1 8   ? 26.706 -9.019  5.371  1.00 6.03  ? 7   VAL A CA  1 
ATOM   45   C  C   . VAL A 1 8   ? 25.753 -10.002 4.666  1.00 6.87  ? 7   VAL A C   1 
ATOM   46   O  O   . VAL A 1 8   ? 26.087 -11.206 4.621  1.00 5.63  ? 7   VAL A O   1 
ATOM   47   C  CB  . VAL A 1 8   ? 28.164 -8.970  5.060  1.00 4.82  ? 7   VAL A CB  1 
ATOM   48   C  CG1 . VAL A 1 8   ? 29.003 -10.018 5.776  1.00 2.83  ? 7   VAL A CG1 1 
ATOM   49   C  CG2 . VAL A 1 8   ? 28.433 -9.186  3.583  1.00 5.63  ? 7   VAL A CG2 1 
ATOM   50   N  N   . LEU A 1 9   ? 24.655 -9.473  4.151  1.00 6.56  ? 8   LEU A N   1 
ATOM   51   C  CA  . LEU A 1 9   ? 23.645 -10.156 3.468  1.00 5.82  ? 8   LEU A CA  1 
ATOM   52   C  C   . LEU A 1 9   ? 23.925 -10.310 1.980  1.00 4.93  ? 8   LEU A C   1 
ATOM   53   O  O   . LEU A 1 9   ? 24.432 -9.295  1.557  1.00 2.00  ? 8   LEU A O   1 
ATOM   54   C  CB  . LEU A 1 9   ? 22.305 -9.384  3.484  1.00 5.36  ? 8   LEU A CB  1 
ATOM   55   C  CG  . LEU A 1 9   ? 21.380 -8.950  4.636  1.00 5.51  ? 8   LEU A CG  1 
ATOM   56   C  CD1 . LEU A 1 9   ? 20.932 -10.127 5.547  1.00 5.65  ? 8   LEU A CD1 1 
ATOM   57   C  CD2 . LEU A 1 9   ? 22.107 -7.934  5.426  1.00 5.20  ? 8   LEU A CD2 1 
ATOM   58   N  N   . LYS A 1 10  ? 23.541 -11.489 1.498  1.00 7.95  ? 9   LYS A N   1 
ATOM   59   C  CA  . LYS A 1 10  ? 23.679 -11.759 -0.025 1.00 8.80  ? 9   LYS A CA  1 
ATOM   60   C  C   . LYS A 1 10  ? 22.975 -13.095 -0.391 1.00 9.49  ? 9   LYS A C   1 
ATOM   61   O  O   . LYS A 1 10  ? 22.691 -13.882 0.551  1.00 12.63 ? 9   LYS A O   1 
ATOM   62   C  CB  . LYS A 1 10  ? 25.036 -11.702 -0.593 1.00 8.49  ? 9   LYS A CB  1 
ATOM   63   C  CG  . LYS A 1 10  ? 25.735 -10.482 -1.178 1.00 8.82  ? 9   LYS A CG  1 
ATOM   64   C  CD  . LYS A 1 10  ? 27.254 -10.720 -1.105 1.00 9.63  ? 9   LYS A CD  1 
ATOM   65   C  CE  . LYS A 1 10  ? 28.099 -10.120 -2.195 1.00 7.51  ? 9   LYS A CE  1 
ATOM   66   N  NZ  . LYS A 1 10  ? 28.494 -8.783  -1.737 1.00 10.30 ? 9   LYS A NZ  1 
ATOM   67   N  N   . GLY A 1 11  ? 22.604 -13.524 -1.547 1.00 12.92 ? 10  GLY A N   1 
ATOM   68   C  CA  . GLY A 1 11  ? 21.951 -14.831 -1.921 1.00 13.77 ? 10  GLY A CA  1 
ATOM   69   C  C   . GLY A 1 11  ? 21.606 -14.842 -3.419 1.00 16.09 ? 10  GLY A C   1 
ATOM   70   O  O   . GLY A 1 11  ? 22.179 -13.960 -4.073 1.00 16.77 ? 10  GLY A O   1 
ATOM   71   N  N   . ASP A 1 12  ? 20.742 -15.728 -4.016 1.00 15.74 ? 11  ASP A N   1 
ATOM   72   C  CA  . ASP A 1 12  ? 20.406 -15.676 -5.466 1.00 11.85 ? 11  ASP A CA  1 
ATOM   73   C  C   . ASP A 1 12  ? 19.690 -14.269 -5.657 1.00 12.16 ? 11  ASP A C   1 
ATOM   74   O  O   . ASP A 1 12  ? 19.674 -13.790 -6.842 1.00 12.34 ? 11  ASP A O   1 
ATOM   75   C  CB  . ASP A 1 12  ? 19.681 -16.855 -6.054 1.00 10.29 ? 11  ASP A CB  1 
ATOM   76   C  CG  . ASP A 1 12  ? 18.945 -17.879 -5.242 1.00 12.14 ? 11  ASP A CG  1 
ATOM   77   O  OD1 . ASP A 1 12  ? 17.927 -17.583 -4.556 1.00 12.32 ? 11  ASP A OD1 1 
ATOM   78   O  OD2 . ASP A 1 12  ? 19.331 -19.117 -5.207 1.00 10.09 ? 11  ASP A OD2 1 
ATOM   79   N  N   . GLY A 1 13  ? 19.161 -13.561 -4.684 1.00 9.40  ? 12  GLY A N   1 
ATOM   80   C  CA  . GLY A 1 13  ? 18.510 -12.183 -4.804 1.00 9.36  ? 12  GLY A CA  1 
ATOM   81   C  C   . GLY A 1 13  ? 19.662 -11.276 -5.388 1.00 7.88  ? 12  GLY A C   1 
ATOM   82   O  O   . GLY A 1 13  ? 20.825 -11.491 -5.032 1.00 8.94  ? 12  GLY A O   1 
ATOM   83   N  N   . PRO A 1 14  ? 19.448 -10.314 -6.262 1.00 6.48  ? 13  PRO A N   1 
ATOM   84   C  CA  . PRO A 1 14  ? 20.423 -9.465  -6.860 1.00 5.50  ? 13  PRO A CA  1 
ATOM   85   C  C   . PRO A 1 14  ? 20.637 -8.300  -5.949 1.00 5.24  ? 13  PRO A C   1 
ATOM   86   O  O   . PRO A 1 14  ? 20.964 -7.286  -6.420 1.00 2.08  ? 13  PRO A O   1 
ATOM   87   C  CB  . PRO A 1 14  ? 19.662 -9.061  -8.118 1.00 7.11  ? 13  PRO A CB  1 
ATOM   88   C  CG  . PRO A 1 14  ? 18.280 -8.595  -7.490 1.00 5.21  ? 13  PRO A CG  1 
ATOM   89   C  CD  . PRO A 1 14  ? 18.074 -9.888  -6.724 1.00 7.88  ? 13  PRO A CD  1 
ATOM   90   N  N   . VAL A 1 15  ? 20.410 -8.573  -4.682 1.00 7.45  ? 14  VAL A N   1 
ATOM   91   C  CA  . VAL A 1 15  ? 20.462 -7.610  -3.560 1.00 6.13  ? 14  VAL A CA  1 
ATOM   92   C  C   . VAL A 1 15  ? 21.419 -7.920  -2.499 1.00 6.68  ? 14  VAL A C   1 
ATOM   93   O  O   . VAL A 1 15  ? 21.819 -9.009  -2.403 1.00 5.49  ? 14  VAL A O   1 
ATOM   94   C  CB  . VAL A 1 15  ? 18.943 -7.541  -3.268 1.00 6.21  ? 14  VAL A CB  1 
ATOM   95   C  CG1 . VAL A 1 15  ? 18.573 -6.644  -4.467 1.00 6.55  ? 14  VAL A CG1 1 
ATOM   96   C  CG2 . VAL A 1 15  ? 18.017 -8.726  -3.278 1.00 4.27  ? 14  VAL A CG2 1 
ATOM   97   N  N   . GLN A 1 16  ? 21.719 -6.786  -1.784 1.00 9.52  ? 15  GLN A N   1 
ATOM   98   C  CA  . GLN A 1 16  ? 22.785 -7.246  -0.772 1.00 9.50  ? 15  GLN A CA  1 
ATOM   99   C  C   . GLN A 1 16  ? 22.950 -6.271  0.288  1.00 10.02 ? 15  GLN A C   1 
ATOM   100  O  O   . GLN A 1 16  ? 22.112 -5.293  0.323  1.00 11.62 ? 15  GLN A O   1 
ATOM   101  C  CB  . GLN A 1 16  ? 24.021 -7.473  -1.664 1.00 9.65  ? 15  GLN A CB  1 
ATOM   102  C  CG  . GLN A 1 16  ? 24.473 -6.759  -2.947 1.00 7.49  ? 15  GLN A CG  1 
ATOM   103  C  CD  . GLN A 1 16  ? 25.790 -7.382  -3.544 1.00 5.62  ? 15  GLN A CD  1 
ATOM   104  O  OE1 . GLN A 1 16  ? 26.917 -7.140  -3.090 1.00 2.00  ? 15  GLN A OE1 1 
ATOM   105  N  NE2 . GLN A 1 16  ? 25.667 -8.218  -4.591 1.00 2.28  ? 15  GLN A NE2 1 
ATOM   106  N  N   . GLY A 1 17  ? 23.965 -6.498  1.136  1.00 9.40  ? 16  GLY A N   1 
ATOM   107  C  CA  . GLY A 1 17  ? 24.111 -5.472  2.182  1.00 10.37 ? 16  GLY A CA  1 
ATOM   108  C  C   . GLY A 1 17  ? 25.003 -5.757  3.376  1.00 9.95  ? 16  GLY A C   1 
ATOM   109  O  O   . GLY A 1 17  ? 24.904 -6.727  4.093  1.00 8.65  ? 16  GLY A O   1 
ATOM   110  N  N   . ILE A 1 18  ? 25.876 -4.801  3.643  1.00 8.96  ? 17  ILE A N   1 
ATOM   111  C  CA  . ILE A 1 18  ? 26.819 -5.013  4.820  1.00 7.84  ? 17  ILE A CA  1 
ATOM   112  C  C   . ILE A 1 18  ? 25.897 -4.354  5.868  1.00 9.98  ? 17  ILE A C   1 
ATOM   113  O  O   . ILE A 1 18  ? 25.468 -3.117  5.667  1.00 10.93 ? 17  ILE A O   1 
ATOM   114  C  CB  . ILE A 1 18  ? 28.130 -4.402  4.417  1.00 8.18  ? 17  ILE A CB  1 
ATOM   115  C  CG1 . ILE A 1 18  ? 28.571 -5.145  3.082  1.00 10.43 ? 17  ILE A CG1 1 
ATOM   116  C  CG2 . ILE A 1 18  ? 29.274 -4.414  5.454  1.00 7.44  ? 17  ILE A CG2 1 
ATOM   117  C  CD1 . ILE A 1 18  ? 29.179 -4.114  2.041  1.00 9.55  ? 17  ILE A CD1 1 
ATOM   118  N  N   . ILE A 1 19  ? 25.503 -4.999  6.971  1.00 7.69  ? 18  ILE A N   1 
ATOM   119  C  CA  . ILE A 1 19  ? 24.640 -4.486  8.036  1.00 5.83  ? 18  ILE A CA  1 
ATOM   120  C  C   . ILE A 1 19  ? 25.422 -4.599  9.405  1.00 4.83  ? 18  ILE A C   1 
ATOM   121  O  O   . ILE A 1 19  ? 26.035 -5.757  9.644  1.00 2.80  ? 18  ILE A O   1 
ATOM   122  C  CB  . ILE A 1 19  ? 23.247 -5.214  7.964  1.00 4.80  ? 18  ILE A CB  1 
ATOM   123  C  CG1 . ILE A 1 19  ? 22.223 -4.484  8.833  1.00 2.20  ? 18  ILE A CG1 1 
ATOM   124  C  CG2 . ILE A 1 19  ? 23.414 -6.668  8.379  1.00 3.59  ? 18  ILE A CG2 1 
ATOM   125  C  CD1 . ILE A 1 19  ? 21.170 -5.222  9.601  1.00 2.00  ? 18  ILE A CD1 1 
ATOM   126  N  N   . ASN A 1 20  ? 25.350 -3.493  10.189 1.00 2.00  ? 19  ASN A N   1 
ATOM   127  C  CA  . ASN A 1 20  ? 26.103 -3.483  11.485 1.00 3.40  ? 19  ASN A CA  1 
ATOM   128  C  C   . ASN A 1 20  ? 25.352 -3.590  12.865 1.00 2.74  ? 19  ASN A C   1 
ATOM   129  O  O   . ASN A 1 20  ? 24.141 -3.281  12.867 1.00 2.00  ? 19  ASN A O   1 
ATOM   130  C  CB  . ASN A 1 20  ? 27.057 -2.234  11.385 1.00 2.00  ? 19  ASN A CB  1 
ATOM   131  C  CG  . ASN A 1 20  ? 28.006 -2.164  10.206 1.00 2.67  ? 19  ASN A CG  1 
ATOM   132  O  OD1 . ASN A 1 20  ? 27.879 -1.473  9.100  1.00 2.00  ? 19  ASN A OD1 1 
ATOM   133  N  ND2 . ASN A 1 20  ? 29.141 -2.931  10.333 1.00 2.00  ? 19  ASN A ND2 1 
ATOM   134  N  N   . PHE A 1 21  ? 26.258 -4.069  13.891 1.00 2.62  ? 20  PHE A N   1 
ATOM   135  C  CA  . PHE A 1 21  ? 25.400 -4.123  15.191 1.00 3.06  ? 20  PHE A CA  1 
ATOM   136  C  C   . PHE A 1 21  ? 26.284 -3.623  16.303 1.00 4.68  ? 20  PHE A C   1 
ATOM   137  O  O   . PHE A 1 21  ? 27.317 -4.370  16.412 1.00 2.80  ? 20  PHE A O   1 
ATOM   138  C  CB  . PHE A 1 21  ? 24.937 -5.535  15.341 1.00 4.61  ? 20  PHE A CB  1 
ATOM   139  C  CG  . PHE A 1 21  ? 24.037 -6.283  14.505 1.00 6.99  ? 20  PHE A CG  1 
ATOM   140  C  CD1 . PHE A 1 21  ? 24.458 -6.722  13.216 1.00 8.39  ? 20  PHE A CD1 1 
ATOM   141  C  CD2 . PHE A 1 21  ? 22.726 -6.595  14.918 1.00 8.87  ? 20  PHE A CD2 1 
ATOM   142  C  CE1 . PHE A 1 21  ? 23.595 -7.455  12.382 1.00 10.84 ? 20  PHE A CE1 1 
ATOM   143  C  CE2 . PHE A 1 21  ? 21.835 -7.326  14.121 1.00 7.02  ? 20  PHE A CE2 1 
ATOM   144  C  CZ  . PHE A 1 21  ? 22.273 -7.743  12.868 1.00 9.59  ? 20  PHE A CZ  1 
ATOM   145  N  N   . GLU A 1 22  ? 26.091 -2.579  17.077 1.00 4.58  ? 21  GLU A N   1 
ATOM   146  C  CA  . GLU A 1 22  ? 26.923 -2.059  18.138 1.00 3.79  ? 21  GLU A CA  1 
ATOM   147  C  C   . GLU A 1 22  ? 26.147 -2.031  19.473 1.00 7.23  ? 21  GLU A C   1 
ATOM   148  O  O   . GLU A 1 22  ? 25.098 -1.286  19.666 1.00 6.53  ? 21  GLU A O   1 
ATOM   149  C  CB  . GLU A 1 22  ? 27.474 -0.650  17.843 1.00 3.09  ? 21  GLU A CB  1 
ATOM   150  C  CG  . GLU A 1 22  ? 28.848 -0.515  17.176 1.00 4.03  ? 21  GLU A CG  1 
ATOM   151  C  CD  . GLU A 1 22  ? 29.845 0.582   17.296 1.00 5.30  ? 21  GLU A CD  1 
ATOM   152  O  OE1 . GLU A 1 22  ? 29.578 1.831   17.255 1.00 4.09  ? 21  GLU A OE1 1 
ATOM   153  O  OE2 . GLU A 1 22  ? 31.060 0.269   17.432 1.00 4.76  ? 21  GLU A OE2 1 
ATOM   154  N  N   . GLN A 1 23  ? 26.592 -2.868  20.481 1.00 8.61  ? 22  GLN A N   1 
ATOM   155  C  CA  . GLN A 1 23  ? 25.891 -2.883  21.773 1.00 10.09 ? 22  GLN A CA  1 
ATOM   156  C  C   . GLN A 1 23  ? 26.729 -2.928  23.071 1.00 10.76 ? 22  GLN A C   1 
ATOM   157  O  O   . GLN A 1 23  ? 27.391 -3.850  23.511 1.00 10.60 ? 22  GLN A O   1 
ATOM   158  C  CB  . GLN A 1 23  ? 24.882 -4.050  21.803 1.00 10.49 ? 22  GLN A CB  1 
ATOM   159  C  CG  . GLN A 1 23  ? 24.244 -4.177  23.214 1.00 12.73 ? 22  GLN A CG  1 
ATOM   160  C  CD  . GLN A 1 23  ? 24.700 -5.361  24.049 1.00 12.02 ? 22  GLN A CD  1 
ATOM   161  O  OE1 . GLN A 1 23  ? 25.214 -6.382  23.508 1.00 11.60 ? 22  GLN A OE1 1 
ATOM   162  N  NE2 . GLN A 1 23  ? 24.499 -5.218  25.361 1.00 11.45 ? 22  GLN A NE2 1 
ATOM   163  N  N   . LYS A 1 24  ? 26.650 -1.821  23.815 1.00 9.42  ? 23  LYS A N   1 
ATOM   164  C  CA  . LYS A 1 24  ? 27.304 -1.541  25.078 1.00 7.35  ? 23  LYS A CA  1 
ATOM   165  C  C   . LYS A 1 24  ? 26.548 -2.150  26.302 1.00 6.98  ? 23  LYS A C   1 
ATOM   166  O  O   . LYS A 1 24  ? 26.064 -3.351  26.140 1.00 5.57  ? 23  LYS A O   1 
ATOM   167  C  CB  . LYS A 1 24  ? 27.510 -0.028  25.096 1.00 5.26  ? 23  LYS A CB  1 
ATOM   168  C  CG  . LYS A 1 24  ? 28.414 0.489   24.021 1.00 4.38  ? 23  LYS A CG  1 
ATOM   169  C  CD  . LYS A 1 24  ? 29.717 1.288   24.423 1.00 3.50  ? 23  LYS A CD  1 
ATOM   170  C  CE  . LYS A 1 24  ? 29.436 2.377   25.425 1.00 3.96  ? 23  LYS A CE  1 
ATOM   171  N  NZ  . LYS A 1 24  ? 28.134 3.081   24.985 1.00 2.00  ? 23  LYS A NZ  1 
ATOM   172  N  N   . GLU A 1 25  ? 26.451 -1.517  27.472 1.00 4.50  ? 24  GLU A N   1 
ATOM   173  C  CA  . GLU A 1 25  ? 25.800 -1.970  28.706 1.00 5.07  ? 24  GLU A CA  1 
ATOM   174  C  C   . GLU A 1 25  ? 25.018 -3.342  28.729 1.00 5.78  ? 24  GLU A C   1 
ATOM   175  O  O   . GLU A 1 25  ? 24.000 -3.746  28.143 1.00 3.16  ? 24  GLU A O   1 
ATOM   176  C  CB  . GLU A 1 25  ? 24.764 -0.977  29.278 1.00 5.57  ? 24  GLU A CB  1 
ATOM   177  C  CG  . GLU A 1 25  ? 24.817 -0.951  30.870 1.00 9.43  ? 24  GLU A CG  1 
ATOM   178  C  CD  . GLU A 1 25  ? 26.285 -0.720  31.350 1.00 14.42 ? 24  GLU A CD  1 
ATOM   179  O  OE1 . GLU A 1 25  ? 27.139 -0.035  30.656 1.00 11.03 ? 24  GLU A OE1 1 
ATOM   180  O  OE2 . GLU A 1 25  ? 26.565 -1.282  32.515 1.00 12.66 ? 24  GLU A OE2 1 
ATOM   181  N  N   . SER A 1 26  ? 25.579 -4.205  29.534 1.00 4.70  ? 25  SER A N   1 
ATOM   182  C  CA  . SER A 1 26  ? 25.186 -5.545  29.853 1.00 7.29  ? 25  SER A CA  1 
ATOM   183  C  C   . SER A 1 26  ? 24.149 -6.154  28.901 1.00 9.15  ? 25  SER A C   1 
ATOM   184  O  O   . SER A 1 26  ? 24.499 -6.941  27.972 1.00 7.62  ? 25  SER A O   1 
ATOM   185  C  CB  . SER A 1 26  ? 24.686 -5.507  31.334 1.00 5.89  ? 25  SER A CB  1 
ATOM   186  O  OG  . SER A 1 26  ? 24.294 -6.786  31.788 1.00 3.57  ? 25  SER A OG  1 
ATOM   187  N  N   . ASN A 1 27  ? 22.851 -5.789  29.176 1.00 8.94  ? 26  ASN A N   1 
ATOM   188  C  CA  . ASN A 1 27  ? 21.825 -6.403  28.267 1.00 8.81  ? 26  ASN A CA  1 
ATOM   189  C  C   . ASN A 1 27  ? 20.950 -5.271  27.885 1.00 8.99  ? 26  ASN A C   1 
ATOM   190  O  O   . ASN A 1 27  ? 21.008 -4.191  28.493 1.00 8.08  ? 26  ASN A O   1 
ATOM   191  C  CB  . ASN A 1 27  ? 21.123 -7.588  28.890 1.00 8.04  ? 26  ASN A CB  1 
ATOM   192  C  CG  . ASN A 1 27  ? 20.360 -7.232  30.160 1.00 7.89  ? 26  ASN A CG  1 
ATOM   193  O  OD1 . ASN A 1 27  ? 19.128 -7.342  30.241 1.00 5.63  ? 26  ASN A OD1 1 
ATOM   194  N  ND2 . ASN A 1 27  ? 21.200 -6.824  31.124 1.00 8.57  ? 26  ASN A ND2 1 
ATOM   195  N  N   . GLY A 1 28  ? 20.122 -5.616  26.835 1.00 9.37  ? 27  GLY A N   1 
ATOM   196  C  CA  . GLY A 1 28  ? 19.481 -4.247  26.693 1.00 7.16  ? 27  GLY A CA  1 
ATOM   197  C  C   . GLY A 1 28  ? 19.924 -3.807  25.204 1.00 6.27  ? 27  GLY A C   1 
ATOM   198  O  O   . GLY A 1 28  ? 20.420 -4.641  24.391 1.00 2.12  ? 27  GLY A O   1 
ATOM   199  N  N   . PRO A 1 29  ? 19.805 -2.499  24.901 1.00 5.86  ? 28  PRO A N   1 
ATOM   200  C  CA  . PRO A 1 29  ? 19.900 -2.010  23.509 1.00 7.64  ? 28  PRO A CA  1 
ATOM   201  C  C   . PRO A 1 29  ? 20.908 -2.050  22.400 1.00 8.45  ? 28  PRO A C   1 
ATOM   202  O  O   . PRO A 1 29  ? 21.854 -1.424  22.090 1.00 5.47  ? 28  PRO A O   1 
ATOM   203  C  CB  . PRO A 1 29  ? 19.297 -0.560  23.783 1.00 6.79  ? 28  PRO A CB  1 
ATOM   204  C  CG  . PRO A 1 29  ? 19.913 -0.210  25.076 1.00 5.29  ? 28  PRO A CG  1 
ATOM   205  C  CD  . PRO A 1 29  ? 19.371 -1.509  25.815 1.00 6.70  ? 28  PRO A CD  1 
ATOM   206  N  N   . VAL A 1 30  ? 20.440 -3.189  21.629 1.00 8.19  ? 29  VAL A N   1 
ATOM   207  C  CA  . VAL A 1 30  ? 21.262 -3.455  20.455 1.00 10.42 ? 29  VAL A CA  1 
ATOM   208  C  C   . VAL A 1 30  ? 20.912 -2.193  19.497 1.00 9.63  ? 29  VAL A C   1 
ATOM   209  O  O   . VAL A 1 30  ? 19.691 -1.854  19.256 1.00 8.91  ? 29  VAL A O   1 
ATOM   210  C  CB  . VAL A 1 30  ? 21.118 -4.751  19.761 1.00 11.89 ? 29  VAL A CB  1 
ATOM   211  C  CG1 . VAL A 1 30  ? 21.629 -4.575  18.296 1.00 12.07 ? 29  VAL A CG1 1 
ATOM   212  C  CG2 . VAL A 1 30  ? 21.856 -5.984  20.348 1.00 12.05 ? 29  VAL A CG2 1 
ATOM   213  N  N   . LYS A 1 31  ? 22.149 -1.702  19.133 1.00 7.26  ? 30  LYS A N   1 
ATOM   214  C  CA  . LYS A 1 31  ? 22.012 -0.537  18.198 1.00 6.81  ? 30  LYS A CA  1 
ATOM   215  C  C   . LYS A 1 31  ? 22.300 -1.190  16.771 1.00 5.58  ? 30  LYS A C   1 
ATOM   216  O  O   . LYS A 1 31  ? 23.407 -1.726  16.552 1.00 4.09  ? 30  LYS A O   1 
ATOM   217  C  CB  . LYS A 1 31  ? 22.871 0.570   18.624 1.00 7.72  ? 30  LYS A CB  1 
ATOM   218  C  CG  . LYS A 1 31  ? 22.803 1.026   20.110 1.00 8.67  ? 30  LYS A CG  1 
ATOM   219  C  CD  . LYS A 1 31  ? 23.539 2.265   20.474 1.00 5.95  ? 30  LYS A CD  1 
ATOM   220  C  CE  . LYS A 1 31  ? 23.210 3.469   19.573 1.00 5.93  ? 30  LYS A CE  1 
ATOM   221  N  NZ  . LYS A 1 31  ? 21.848 3.975   19.756 1.00 4.86  ? 30  LYS A NZ  1 
ATOM   222  N  N   . VAL A 1 32  ? 21.279 -1.169  15.834 1.00 4.32  ? 31  VAL A N   1 
ATOM   223  C  CA  . VAL A 1 32  ? 21.607 -1.784  14.507 1.00 2.69  ? 31  VAL A CA  1 
ATOM   224  C  C   . VAL A 1 32  ? 21.311 -0.721  13.394 1.00 2.38  ? 31  VAL A C   1 
ATOM   225  O  O   . VAL A 1 32  ? 20.274 -0.125  13.215 1.00 2.00  ? 31  VAL A O   1 
ATOM   226  C  CB  . VAL A 1 32  ? 21.015 -3.179  14.269 1.00 2.00  ? 31  VAL A CB  1 
ATOM   227  C  CG1 . VAL A 1 32  ? 19.728 -3.384  15.000 1.00 3.56  ? 31  VAL A CG1 1 
ATOM   228  C  CG2 . VAL A 1 32  ? 20.830 -3.550  12.766 1.00 2.00  ? 31  VAL A CG2 1 
ATOM   229  N  N   . TRP A 1 33  ? 22.481 -0.651  12.713 1.00 2.00  ? 32  TRP A N   1 
ATOM   230  C  CA  . TRP A 1 33  ? 22.344 0.341   11.617 1.00 2.10  ? 32  TRP A CA  1 
ATOM   231  C  C   . TRP A 1 33  ? 23.174 -0.209  10.491 1.00 3.42  ? 32  TRP A C   1 
ATOM   232  O  O   . TRP A 1 33  ? 24.080 -0.984  10.894 1.00 3.27  ? 32  TRP A O   1 
ATOM   233  C  CB  . TRP A 1 33  ? 22.785 1.673   12.001 1.00 3.61  ? 32  TRP A CB  1 
ATOM   234  C  CG  . TRP A 1 33  ? 24.027 1.970   12.724 1.00 5.77  ? 32  TRP A CG  1 
ATOM   235  C  CD1 . TRP A 1 33  ? 25.280 1.454   12.711 1.00 5.06  ? 32  TRP A CD1 1 
ATOM   236  C  CD2 . TRP A 1 33  ? 24.064 3.066   13.675 1.00 8.09  ? 32  TRP A CD2 1 
ATOM   237  N  NE1 . TRP A 1 33  ? 26.156 2.090   13.574 1.00 2.71  ? 32  TRP A NE1 1 
ATOM   238  C  CE2 . TRP A 1 33  ? 25.413 3.098   14.178 1.00 8.11  ? 32  TRP A CE2 1 
ATOM   239  C  CE3 . TRP A 1 33  ? 23.096 3.949   14.120 1.00 8.14  ? 32  TRP A CE3 1 
ATOM   240  C  CZ2 . TRP A 1 33  ? 25.771 4.042   15.137 1.00 8.92  ? 32  TRP A CZ2 1 
ATOM   241  C  CZ3 . TRP A 1 33  ? 23.463 4.867   15.065 1.00 10.14 ? 32  TRP A CZ3 1 
ATOM   242  C  CH2 . TRP A 1 33  ? 24.782 4.902   15.555 1.00 11.49 ? 32  TRP A CH2 1 
ATOM   243  N  N   . GLY A 1 34  ? 22.786 0.239   9.296  1.00 4.32  ? 33  GLY A N   1 
ATOM   244  C  CA  . GLY A 1 34  ? 23.703 -0.340  8.200  1.00 6.65  ? 33  GLY A CA  1 
ATOM   245  C  C   . GLY A 1 34  ? 23.038 -0.187  6.845  1.00 6.23  ? 33  GLY A C   1 
ATOM   246  O  O   . GLY A 1 34  ? 22.010 0.535   6.942  1.00 8.36  ? 33  GLY A O   1 
ATOM   247  N  N   . SER A 1 35  ? 23.578 -0.782  5.778  1.00 2.00  ? 34  SER A N   1 
ATOM   248  C  CA  . SER A 1 35  ? 22.748 -0.507  4.616  1.00 3.36  ? 34  SER A CA  1 
ATOM   249  C  C   . SER A 1 35  ? 22.595 -1.792  3.756  1.00 5.32  ? 34  SER A C   1 
ATOM   250  O  O   . SER A 1 35  ? 23.344 -2.876  3.995  1.00 7.81  ? 34  SER A O   1 
ATOM   251  C  CB  . SER A 1 35  ? 23.349 0.663   3.995  1.00 2.21  ? 34  SER A CB  1 
ATOM   252  O  OG  . SER A 1 35  ? 23.455 1.602   5.036  1.00 4.48  ? 34  SER A OG  1 
ATOM   253  N  N   . ILE A 1 36  ? 21.573 -1.481  2.828  1.00 4.21  ? 35  ILE A N   1 
ATOM   254  C  CA  . ILE A 1 36  ? 21.398 -2.716  1.928  1.00 4.64  ? 35  ILE A CA  1 
ATOM   255  C  C   . ILE A 1 36  ? 20.798 -2.195  0.637  1.00 4.29  ? 35  ILE A C   1 
ATOM   256  O  O   . ILE A 1 36  ? 19.812 -1.485  0.712  1.00 4.11  ? 35  ILE A O   1 
ATOM   257  C  CB  . ILE A 1 36  ? 20.682 -3.768  2.764  1.00 5.16  ? 35  ILE A CB  1 
ATOM   258  C  CG1 . ILE A 1 36  ? 19.521 -4.413  2.015  1.00 6.09  ? 35  ILE A CG1 1 
ATOM   259  C  CG2 . ILE A 1 36  ? 20.047 -3.261  4.130  1.00 9.01  ? 35  ILE A CG2 1 
ATOM   260  C  CD1 . ILE A 1 36  ? 18.912 -5.569  2.915  1.00 6.48  ? 35  ILE A CD1 1 
ATOM   261  N  N   . LYS A 1 37  ? 21.429 -2.574  -0.452 1.00 2.00  ? 36  LYS A N   1 
ATOM   262  C  CA  . LYS A 1 37  ? 21.095 -2.181  -1.780 1.00 2.00  ? 36  LYS A CA  1 
ATOM   263  C  C   . LYS A 1 37  ? 20.308 -3.273  -2.559 1.00 2.06  ? 36  LYS A C   1 
ATOM   264  O  O   . LYS A 1 37  ? 19.831 -4.290  -2.091 1.00 2.00  ? 36  LYS A O   1 
ATOM   265  C  CB  . LYS A 1 37  ? 22.316 -1.719  -2.602 1.00 2.54  ? 36  LYS A CB  1 
ATOM   266  C  CG  . LYS A 1 37  ? 22.980 -0.318  -2.562 1.00 4.70  ? 36  LYS A CG  1 
ATOM   267  C  CD  . LYS A 1 37  ? 21.937 0.788   -3.092 1.00 7.35  ? 36  LYS A CD  1 
ATOM   268  C  CE  . LYS A 1 37  ? 22.729 1.702   -4.050 1.00 7.83  ? 36  LYS A CE  1 
ATOM   269  N  NZ  . LYS A 1 37  ? 21.989 2.880   -4.503 1.00 11.13 ? 36  LYS A NZ  1 
ATOM   270  N  N   . GLY A 1 38  ? 20.259 -2.842  -3.855 1.00 2.74  ? 37  GLY A N   1 
ATOM   271  C  CA  . GLY A 1 38  ? 19.627 -3.493  -4.946 1.00 2.00  ? 37  GLY A CA  1 
ATOM   272  C  C   . GLY A 1 38  ? 18.078 -3.512  -4.941 1.00 2.00  ? 37  GLY A C   1 
ATOM   273  O  O   . GLY A 1 38  ? 17.458 -3.224  -6.000 1.00 2.00  ? 37  GLY A O   1 
ATOM   274  N  N   . LEU A 1 39  ? 17.415 -3.811  -3.863 1.00 2.00  ? 38  LEU A N   1 
ATOM   275  C  CA  . LEU A 1 39  ? 15.955 -3.929  -3.839 1.00 2.37  ? 38  LEU A CA  1 
ATOM   276  C  C   . LEU A 1 39  ? 15.031 -2.729  -4.112 1.00 3.81  ? 38  LEU A C   1 
ATOM   277  O  O   . LEU A 1 39  ? 15.299 -1.552  -4.036 1.00 2.00  ? 38  LEU A O   1 
ATOM   278  C  CB  . LEU A 1 39  ? 15.671 -4.658  -2.499 1.00 2.00  ? 38  LEU A CB  1 
ATOM   279  C  CG  . LEU A 1 39  ? 15.718 -4.033  -1.156 1.00 2.00  ? 38  LEU A CG  1 
ATOM   280  C  CD1 . LEU A 1 39  ? 15.897 -5.074  -0.001 1.00 2.00  ? 38  LEU A CD1 1 
ATOM   281  C  CD2 . LEU A 1 39  ? 16.874 -3.060  -1.111 1.00 2.04  ? 38  LEU A CD2 1 
ATOM   282  N  N   . THR A 1 40  ? 13.888 -3.291  -4.511 1.00 3.83  ? 39  THR A N   1 
ATOM   283  C  CA  . THR A 1 40  ? 12.568 -3.058  -4.940 1.00 4.10  ? 39  THR A CA  1 
ATOM   284  C  C   . THR A 1 40  ? 12.102 -2.256  -3.711 1.00 3.35  ? 39  THR A C   1 
ATOM   285  O  O   . THR A 1 40  ? 12.252 -2.792  -2.594 1.00 3.59  ? 39  THR A O   1 
ATOM   286  C  CB  . THR A 1 40  ? 11.579 -4.291  -5.097 1.00 5.00  ? 39  THR A CB  1 
ATOM   287  O  OG1 . THR A 1 40  ? 12.226 -5.446  -5.791 1.00 5.41  ? 39  THR A OG1 1 
ATOM   288  C  CG2 . THR A 1 40  ? 10.313 -4.068  -5.896 1.00 5.43  ? 39  THR A CG2 1 
ATOM   289  N  N   . GLU A 1 41  ? 11.595 -1.106  -3.982 1.00 4.77  ? 40  GLU A N   1 
ATOM   290  C  CA  . GLU A 1 41  ? 11.120 -0.155  -2.927 1.00 6.87  ? 40  GLU A CA  1 
ATOM   291  C  C   . GLU A 1 41  ? 10.015 -0.759  -2.069 1.00 6.34  ? 40  GLU A C   1 
ATOM   292  O  O   . GLU A 1 41  ? 9.606  -1.906  -2.267 1.00 3.55  ? 40  GLU A O   1 
ATOM   293  C  CB  . GLU A 1 41  ? 10.695 1.184   -3.527 1.00 6.51  ? 40  GLU A CB  1 
ATOM   294  C  CG  . GLU A 1 41  ? 10.077 2.309   -2.783 1.00 6.38  ? 40  GLU A CG  1 
ATOM   295  C  CD  . GLU A 1 41  ? 9.968  3.675   -3.404 1.00 6.04  ? 40  GLU A CD  1 
ATOM   296  O  OE1 . GLU A 1 41  ? 11.031 4.320   -3.412 1.00 3.56  ? 40  GLU A OE1 1 
ATOM   297  O  OE2 . GLU A 1 41  ? 8.894  4.086   -3.873 1.00 5.62  ? 40  GLU A OE2 1 
ATOM   298  N  N   . GLY A 1 42  ? 9.605  0.081   -1.085 1.00 6.02  ? 41  GLY A N   1 
ATOM   299  C  CA  . GLY A 1 42  ? 8.544  -0.523  -0.235 1.00 10.11 ? 41  GLY A CA  1 
ATOM   300  C  C   . GLY A 1 42  ? 9.306  -1.153  1.048  1.00 11.62 ? 41  GLY A C   1 
ATOM   301  O  O   . GLY A 1 42  ? 10.564 -1.112  1.291  1.00 8.61  ? 41  GLY A O   1 
ATOM   302  N  N   . LEU A 1 43  ? 8.326  -1.691  1.793  1.00 8.56  ? 42  LEU A N   1 
ATOM   303  C  CA  . LEU A 1 43  ? 8.757  -2.290  3.038  1.00 10.59 ? 42  LEU A CA  1 
ATOM   304  C  C   . LEU A 1 43  ? 9.251  -3.677  2.723  1.00 10.62 ? 42  LEU A C   1 
ATOM   305  O  O   . LEU A 1 43  ? 8.802  -4.212  1.710  1.00 11.30 ? 42  LEU A O   1 
ATOM   306  C  CB  . LEU A 1 43  ? 7.633  -2.335  4.066  1.00 10.60 ? 42  LEU A CB  1 
ATOM   307  C  CG  . LEU A 1 43  ? 7.173  -1.215  4.989  1.00 8.90  ? 42  LEU A CG  1 
ATOM   308  C  CD1 . LEU A 1 43  ? 7.259  0.161   4.424  1.00 6.99  ? 42  LEU A CD1 1 
ATOM   309  C  CD2 . LEU A 1 43  ? 5.717  -1.657  5.280  1.00 7.66  ? 42  LEU A CD2 1 
ATOM   310  N  N   . HIS A 1 44  ? 10.134 -4.065  3.635  1.00 9.18  ? 43  HIS A N   1 
ATOM   311  C  CA  . HIS A 1 44  ? 10.732 -5.401  3.591  1.00 8.59  ? 43  HIS A CA  1 
ATOM   312  C  C   . HIS A 1 44  ? 10.787 -5.968  5.043  1.00 9.30  ? 43  HIS A C   1 
ATOM   313  O  O   . HIS A 1 44  ? 11.120 -5.280  6.014  1.00 6.07  ? 43  HIS A O   1 
ATOM   314  C  CB  . HIS A 1 44  ? 12.141 -5.493  2.942  1.00 5.01  ? 43  HIS A CB  1 
ATOM   315  C  CG  . HIS A 1 44  ? 11.850 -5.109  1.539  1.00 4.05  ? 43  HIS A CG  1 
ATOM   316  N  ND1 . HIS A 1 44  ? 11.498 -6.057  0.533  1.00 3.85  ? 43  HIS A ND1 1 
ATOM   317  C  CD2 . HIS A 1 44  ? 11.844 -3.905  0.995  1.00 2.31  ? 43  HIS A CD2 1 
ATOM   318  C  CE1 . HIS A 1 44  ? 11.305 -5.345  -0.546 1.00 3.32  ? 43  HIS A CE1 1 
ATOM   319  N  NE2 . HIS A 1 44  ? 11.510 -4.044  -0.320 1.00 2.00  ? 43  HIS A NE2 1 
ATOM   320  N  N   . GLY A 1 45  ? 10.481 -7.242  5.212  1.00 10.75 ? 44  GLY A N   1 
ATOM   321  C  CA  . GLY A 1 45  ? 10.541 -7.860  6.631  1.00 10.00 ? 44  GLY A CA  1 
ATOM   322  C  C   . GLY A 1 45  ? 12.076 -7.824  6.895  1.00 9.15  ? 44  GLY A C   1 
ATOM   323  O  O   . GLY A 1 45  ? 12.866 -7.752  5.957  1.00 9.66  ? 44  GLY A O   1 
ATOM   324  N  N   . PHE A 1 46  ? 12.476 -7.840  8.129  1.00 8.50  ? 45  PHE A N   1 
ATOM   325  C  CA  . PHE A 1 46  ? 13.853 -7.779  8.662  1.00 5.28  ? 45  PHE A CA  1 
ATOM   326  C  C   . PHE A 1 46  ? 13.926 -8.334  10.090 1.00 4.79  ? 45  PHE A C   1 
ATOM   327  O  O   . PHE A 1 46  ? 13.842 -7.774  11.189 1.00 2.00  ? 45  PHE A O   1 
ATOM   328  C  CB  . PHE A 1 46  ? 14.295 -6.334  8.657  1.00 4.76  ? 45  PHE A CB  1 
ATOM   329  C  CG  . PHE A 1 46  ? 15.787 -6.170  8.440  1.00 2.84  ? 45  PHE A CG  1 
ATOM   330  C  CD1 . PHE A 1 46  ? 16.261 -6.379  7.129  1.00 2.00  ? 45  PHE A CD1 1 
ATOM   331  C  CD2 . PHE A 1 46  ? 16.579 -5.824  9.468  1.00 3.01  ? 45  PHE A CD2 1 
ATOM   332  C  CE1 . PHE A 1 46  ? 17.647 -6.223  6.929  1.00 4.43  ? 45  PHE A CE1 1 
ATOM   333  C  CE2 . PHE A 1 46  ? 17.962 -5.665  9.277  1.00 4.66  ? 45  PHE A CE2 1 
ATOM   334  C  CZ  . PHE A 1 46  ? 18.506 -5.862  7.985  1.00 3.06  ? 45  PHE A CZ  1 
ATOM   335  N  N   . HIS A 1 47  ? 14.134 -9.582  9.862  1.00 6.01  ? 46  HIS A N   1 
ATOM   336  C  CA  . HIS A 1 47  ? 14.263 -10.668 10.825 1.00 7.14  ? 46  HIS A CA  1 
ATOM   337  C  C   . HIS A 1 47  ? 15.659 -11.235 11.059 1.00 5.67  ? 46  HIS A C   1 
ATOM   338  O  O   . HIS A 1 47  ? 16.670 -10.887 10.463 1.00 2.00  ? 46  HIS A O   1 
ATOM   339  C  CB  . HIS A 1 47  ? 13.401 -11.885 10.309 1.00 6.65  ? 46  HIS A CB  1 
ATOM   340  C  CG  . HIS A 1 47  ? 12.066 -11.249 9.954  1.00 9.21  ? 46  HIS A CG  1 
ATOM   341  N  ND1 . HIS A 1 47  ? 11.519 -11.568 8.749  1.00 9.92  ? 46  HIS A ND1 1 
ATOM   342  C  CD2 . HIS A 1 47  ? 11.236 -10.409 10.537 1.00 9.85  ? 46  HIS A CD2 1 
ATOM   343  C  CE1 . HIS A 1 47  ? 10.368 -10.920 8.628  1.00 11.86 ? 46  HIS A CE1 1 
ATOM   344  N  NE2 . HIS A 1 47  ? 10.192 -10.209 9.736  1.00 12.46 ? 46  HIS A NE2 1 
ATOM   345  N  N   . VAL A 1 48  ? 15.511 -12.154 12.013 1.00 5.53  ? 47  VAL A N   1 
ATOM   346  C  CA  . VAL A 1 48  ? 16.579 -13.012 12.543 1.00 4.60  ? 47  VAL A CA  1 
ATOM   347  C  C   . VAL A 1 48  ? 15.954 -14.423 12.298 1.00 4.32  ? 47  VAL A C   1 
ATOM   348  O  O   . VAL A 1 48  ? 14.733 -14.630 12.426 1.00 4.24  ? 47  VAL A O   1 
ATOM   349  C  CB  . VAL A 1 48  ? 17.071 -12.775 13.967 1.00 3.17  ? 47  VAL A CB  1 
ATOM   350  C  CG1 . VAL A 1 48  ? 17.761 -13.950 14.718 1.00 2.00  ? 47  VAL A CG1 1 
ATOM   351  C  CG2 . VAL A 1 48  ? 18.123 -11.641 14.015 1.00 2.00  ? 47  VAL A CG2 1 
ATOM   352  N  N   . HIS A 1 49  ? 16.623 -15.380 11.954 1.00 6.74  ? 48  HIS A N   1 
ATOM   353  C  CA  . HIS A 1 49  ? 16.254 -16.810 11.686 1.00 11.54 ? 48  HIS A CA  1 
ATOM   354  C  C   . HIS A 1 49  ? 17.378 -17.499 12.497 1.00 12.51 ? 48  HIS A C   1 
ATOM   355  O  O   . HIS A 1 49  ? 18.564 -17.253 12.259 1.00 12.42 ? 48  HIS A O   1 
ATOM   356  C  CB  . HIS A 1 49  ? 16.037 -17.074 10.200 1.00 11.85 ? 48  HIS A CB  1 
ATOM   357  C  CG  . HIS A 1 49  ? 14.794 -16.418 9.675  1.00 12.87 ? 48  HIS A CG  1 
ATOM   358  N  ND1 . HIS A 1 49  ? 13.639 -17.140 9.556  1.00 12.19 ? 48  HIS A ND1 1 
ATOM   359  C  CD2 . HIS A 1 49  ? 14.484 -15.135 9.238  1.00 13.20 ? 48  HIS A CD2 1 
ATOM   360  C  CE1 . HIS A 1 49  ? 12.697 -16.335 9.078  1.00 12.67 ? 48  HIS A CE1 1 
ATOM   361  N  NE2 . HIS A 1 49  ? 13.185 -15.110 8.862  1.00 11.95 ? 48  HIS A NE2 1 
ATOM   362  N  N   . GLU A 1 50  ? 16.962 -18.340 13.459 1.00 12.17 ? 49  GLU A N   1 
ATOM   363  C  CA  . GLU A 1 50  ? 17.670 -19.104 14.453 1.00 7.14  ? 49  GLU A CA  1 
ATOM   364  C  C   . GLU A 1 50  ? 18.894 -19.912 14.211 1.00 6.61  ? 49  GLU A C   1 
ATOM   365  O  O   . GLU A 1 50  ? 19.856 -19.945 15.063 1.00 6.93  ? 49  GLU A O   1 
ATOM   366  C  CB  . GLU A 1 50  ? 16.636 -20.130 15.136 1.00 6.25  ? 49  GLU A CB  1 
ATOM   367  C  CG  . GLU A 1 50  ? 17.060 -20.676 16.583 1.00 4.86  ? 49  GLU A CG  1 
ATOM   368  C  CD  . GLU A 1 50  ? 15.978 -21.210 17.523 1.00 2.43  ? 49  GLU A CD  1 
ATOM   369  O  OE1 . GLU A 1 50  ? 15.421 -22.304 17.536 1.00 2.00  ? 49  GLU A OE1 1 
ATOM   370  O  OE2 . GLU A 1 50  ? 15.586 -20.408 18.417 1.00 3.42  ? 49  GLU A OE2 1 
ATOM   371  N  N   . PHE A 1 51  ? 18.835 -20.540 13.092 1.00 6.65  ? 50  PHE A N   1 
ATOM   372  C  CA  . PHE A 1 51  ? 19.921 -21.440 12.636 1.00 5.20  ? 50  PHE A CA  1 
ATOM   373  C  C   . PHE A 1 51  ? 20.835 -20.751 11.668 1.00 4.00  ? 50  PHE A C   1 
ATOM   374  O  O   . PHE A 1 51  ? 20.195 -20.393 10.717 1.00 4.29  ? 50  PHE A O   1 
ATOM   375  C  CB  . PHE A 1 51  ? 19.406 -22.761 11.975 1.00 3.93  ? 50  PHE A CB  1 
ATOM   376  C  CG  . PHE A 1 51  ? 18.579 -23.445 13.069 1.00 3.32  ? 50  PHE A CG  1 
ATOM   377  C  CD1 . PHE A 1 51  ? 18.849 -23.213 14.429 1.00 2.00  ? 50  PHE A CD1 1 
ATOM   378  C  CD2 . PHE A 1 51  ? 17.541 -24.302 12.638 1.00 3.39  ? 50  PHE A CD2 1 
ATOM   379  C  CE1 . PHE A 1 51  ? 18.057 -23.850 15.322 1.00 3.10  ? 50  PHE A CE1 1 
ATOM   380  C  CE2 . PHE A 1 51  ? 16.770 -24.943 13.588 1.00 2.00  ? 50  PHE A CE2 1 
ATOM   381  C  CZ  . PHE A 1 51  ? 16.998 -24.740 14.930 1.00 2.00  ? 50  PHE A CZ  1 
ATOM   382  N  N   . GLY A 1 52  ? 22.074 -20.688 12.061 1.00 3.17  ? 51  GLY A N   1 
ATOM   383  C  CA  . GLY A 1 52  ? 23.047 -20.033 11.214 1.00 4.23  ? 51  GLY A CA  1 
ATOM   384  C  C   . GLY A 1 52  ? 23.653 -21.066 10.267 1.00 4.74  ? 51  GLY A C   1 
ATOM   385  O  O   . GLY A 1 52  ? 24.916 -21.228 10.131 1.00 4.21  ? 51  GLY A O   1 
ATOM   386  N  N   . ASP A 1 53  ? 22.738 -21.750 9.630  1.00 4.37  ? 52  ASP A N   1 
ATOM   387  C  CA  . ASP A 1 53  ? 23.152 -22.778 8.663  1.00 6.28  ? 52  ASP A CA  1 
ATOM   388  C  C   . ASP A 1 53  ? 23.073 -22.041 7.297  1.00 6.71  ? 52  ASP A C   1 
ATOM   389  O  O   . ASP A 1 53  ? 21.973 -22.103 6.774  1.00 3.66  ? 52  ASP A O   1 
ATOM   390  C  CB  . ASP A 1 53  ? 22.365 -24.019 8.745  1.00 6.72  ? 52  ASP A CB  1 
ATOM   391  C  CG  . ASP A 1 53  ? 22.784 -25.363 9.284  1.00 9.06  ? 52  ASP A CG  1 
ATOM   392  O  OD1 . ASP A 1 53  ? 23.906 -25.745 8.900  1.00 9.57  ? 52  ASP A OD1 1 
ATOM   393  O  OD2 . ASP A 1 53  ? 22.094 -26.152 10.051 1.00 7.16  ? 52  ASP A OD2 1 
ATOM   394  N  N   . ASN A 1 54  ? 24.114 -21.392 6.754  1.00 5.56  ? 53  ASN A N   1 
ATOM   395  C  CA  . ASN A 1 54  ? 23.734 -20.789 5.356  1.00 8.20  ? 53  ASN A CA  1 
ATOM   396  C  C   . ASN A 1 54  ? 23.906 -21.959 4.314  1.00 7.00  ? 53  ASN A C   1 
ATOM   397  O  O   . ASN A 1 54  ? 24.130 -21.940 3.109  1.00 3.73  ? 53  ASN A O   1 
ATOM   398  C  CB  . ASN A 1 54  ? 24.482 -19.557 4.957  1.00 5.82  ? 53  ASN A CB  1 
ATOM   399  C  CG  . ASN A 1 54  ? 23.971 -18.152 5.271  1.00 8.65  ? 53  ASN A CG  1 
ATOM   400  O  OD1 . ASN A 1 54  ? 24.677 -17.117 5.620  1.00 6.08  ? 53  ASN A OD1 1 
ATOM   401  N  ND2 . ASN A 1 54  ? 22.641 -18.116 5.121  1.00 6.76  ? 53  ASN A ND2 1 
ATOM   402  N  N   . THR A 1 55  ? 23.795 -23.158 4.908  1.00 8.63  ? 54  THR A N   1 
ATOM   403  C  CA  . THR A 1 55  ? 23.948 -24.468 4.294  1.00 9.13  ? 54  THR A CA  1 
ATOM   404  C  C   . THR A 1 55  ? 23.573 -24.813 2.861  1.00 9.31  ? 54  THR A C   1 
ATOM   405  O  O   . THR A 1 55  ? 24.379 -25.480 2.215  1.00 8.06  ? 54  THR A O   1 
ATOM   406  C  CB  . THR A 1 55  ? 23.204 -25.556 5.269  1.00 6.54  ? 54  THR A CB  1 
ATOM   407  O  OG1 . THR A 1 55  ? 22.349 -24.812 6.156  1.00 3.58  ? 54  THR A OG1 1 
ATOM   408  C  CG2 . THR A 1 55  ? 24.216 -26.364 6.017  1.00 6.97  ? 54  THR A CG2 1 
ATOM   409  N  N   . ALA A 1 56  ? 22.420 -24.384 2.478  1.00 11.26 ? 55  ALA A N   1 
ATOM   410  C  CA  . ALA A 1 56  ? 21.664 -24.505 1.271  1.00 12.16 ? 55  ALA A CA  1 
ATOM   411  C  C   . ALA A 1 56  ? 20.698 -23.290 1.219  1.00 13.78 ? 55  ALA A C   1 
ATOM   412  O  O   . ALA A 1 56  ? 19.503 -23.397 1.568  1.00 13.35 ? 55  ALA A O   1 
ATOM   413  C  CB  . ALA A 1 56  ? 20.933 -25.820 1.394  1.00 11.48 ? 55  ALA A CB  1 
ATOM   414  N  N   . GLY A 1 57  ? 21.288 -22.162 0.795  1.00 12.94 ? 56  GLY A N   1 
ATOM   415  C  CA  . GLY A 1 57  ? 20.655 -20.882 0.682  1.00 11.77 ? 56  GLY A CA  1 
ATOM   416  C  C   . GLY A 1 57  ? 20.412 -20.330 2.191  1.00 11.32 ? 56  GLY A C   1 
ATOM   417  O  O   . GLY A 1 57  ? 21.165 -20.440 3.170  1.00 8.52  ? 56  GLY A O   1 
ATOM   418  N  N   . CYS A 1 58  ? 19.251 -19.736 2.181  1.00 8.40  ? 57  CYS A N   1 
ATOM   419  C  CA  . CYS A 1 58  ? 18.345 -19.051 2.967  1.00 6.38  ? 57  CYS A CA  1 
ATOM   420  C  C   . CYS A 1 58  ? 17.135 -19.885 3.413  1.00 6.19  ? 57  CYS A C   1 
ATOM   421  O  O   . CYS A 1 58  ? 16.180 -19.357 3.942  1.00 6.04  ? 57  CYS A O   1 
ATOM   422  C  CB  . CYS A 1 58  ? 17.761 -17.769 2.231  1.00 4.93  ? 57  CYS A CB  1 
ATOM   423  S  SG  . CYS A 1 58  ? 18.937 -16.538 1.885  1.00 5.28  ? 57  CYS A SG  1 
ATOM   424  N  N   . THR A 1 59  ? 17.050 -21.130 3.258  1.00 6.47  ? 58  THR A N   1 
ATOM   425  C  CA  . THR A 1 59  ? 16.064 -22.118 3.607  1.00 5.65  ? 58  THR A CA  1 
ATOM   426  C  C   . THR A 1 59  ? 16.424 -22.505 5.032  1.00 5.89  ? 58  THR A C   1 
ATOM   427  O  O   . THR A 1 59  ? 15.595 -22.464 5.901  1.00 7.58  ? 58  THR A O   1 
ATOM   428  C  CB  . THR A 1 59  ? 16.054 -23.382 2.639  1.00 5.70  ? 58  THR A CB  1 
ATOM   429  O  OG1 . THR A 1 59  ? 15.745 -22.827 1.334  1.00 3.31  ? 58  THR A OG1 1 
ATOM   430  C  CG2 . THR A 1 59  ? 15.130 -24.508 3.078  1.00 6.15  ? 58  THR A CG2 1 
ATOM   431  N  N   . SER A 1 60  ? 17.680 -22.850 5.235  1.00 7.21  ? 59  SER A N   1 
ATOM   432  C  CA  . SER A 1 60  ? 18.242 -23.279 6.526  1.00 7.91  ? 59  SER A CA  1 
ATOM   433  C  C   . SER A 1 60  ? 18.284 -22.464 7.790  1.00 8.00  ? 59  SER A C   1 
ATOM   434  O  O   . SER A 1 60  ? 18.481 -22.956 8.924  1.00 7.91  ? 59  SER A O   1 
ATOM   435  C  CB  . SER A 1 60  ? 19.699 -23.562 6.096  1.00 5.97  ? 59  SER A CB  1 
ATOM   436  O  OG  . SER A 1 60  ? 19.508 -24.671 5.214  1.00 6.77  ? 59  SER A OG  1 
ATOM   437  N  N   . ALA A 1 61  ? 18.084 -21.192 7.609  1.00 8.52  ? 60  ALA A N   1 
ATOM   438  C  CA  . ALA A 1 61  ? 18.095 -20.156 8.645  1.00 8.21  ? 60  ALA A CA  1 
ATOM   439  C  C   . ALA A 1 61  ? 17.136 -20.343 9.849  1.00 7.91  ? 60  ALA A C   1 
ATOM   440  O  O   . ALA A 1 61  ? 17.366 -19.766 10.963 1.00 2.00  ? 60  ALA A O   1 
ATOM   441  C  CB  . ALA A 1 61  ? 17.888 -18.947 7.739  1.00 7.02  ? 60  ALA A CB  1 
ATOM   442  N  N   . GLY A 1 62  ? 16.092 -21.157 9.480  1.00 8.62  ? 61  GLY A N   1 
ATOM   443  C  CA  . GLY A 1 62  ? 14.951 -21.583 10.320 1.00 5.51  ? 61  GLY A CA  1 
ATOM   444  C  C   . GLY A 1 62  ? 13.834 -20.557 10.252 1.00 5.33  ? 61  GLY A C   1 
ATOM   445  O  O   . GLY A 1 62  ? 13.958 -19.598 9.493  1.00 2.07  ? 61  GLY A O   1 
ATOM   446  N  N   . PRO A 1 63  ? 12.770 -20.712 10.987 1.00 5.89  ? 62  PRO A N   1 
ATOM   447  C  CA  . PRO A 1 63  ? 11.660 -19.829 11.156 1.00 7.62  ? 62  PRO A CA  1 
ATOM   448  C  C   . PRO A 1 63  ? 12.243 -18.626 12.047 1.00 8.32  ? 62  PRO A C   1 
ATOM   449  O  O   . PRO A 1 63  ? 13.515 -18.421 12.157 1.00 10.86 ? 62  PRO A O   1 
ATOM   450  C  CB  . PRO A 1 63  ? 10.572 -20.530 11.886 1.00 7.64  ? 62  PRO A CB  1 
ATOM   451  C  CG  . PRO A 1 63  ? 10.953 -21.958 11.591 1.00 8.52  ? 62  PRO A CG  1 
ATOM   452  C  CD  . PRO A 1 63  ? 12.505 -21.914 11.836 1.00 8.49  ? 62  PRO A CD  1 
ATOM   453  N  N   . HIS A 1 64  ? 11.505 -17.727 12.717 1.00 6.07  ? 63  HIS A N   1 
ATOM   454  C  CA  . HIS A 1 64  ? 12.038 -16.643 13.535 1.00 5.19  ? 63  HIS A CA  1 
ATOM   455  C  C   . HIS A 1 64  ? 12.439 -17.084 14.948 1.00 5.11  ? 63  HIS A C   1 
ATOM   456  O  O   . HIS A 1 64  ? 11.641 -17.819 15.590 1.00 4.25  ? 63  HIS A O   1 
ATOM   457  C  CB  . HIS A 1 64  ? 11.041 -15.498 13.760 1.00 6.81  ? 63  HIS A CB  1 
ATOM   458  C  CG  . HIS A 1 64  ? 10.792 -14.748 12.468 1.00 6.34  ? 63  HIS A CG  1 
ATOM   459  N  ND1 . HIS A 1 64  ? 9.603  -14.297 12.030 1.00 8.01  ? 63  HIS A ND1 1 
ATOM   460  C  CD2 . HIS A 1 64  ? 11.662 -14.395 11.570 1.00 6.72  ? 63  HIS A CD2 1 
ATOM   461  C  CE1 . HIS A 1 64  ? 9.744  -13.678 10.877 1.00 8.55  ? 63  HIS A CE1 1 
ATOM   462  N  NE2 . HIS A 1 64  ? 10.975 -13.745 10.609 1.00 8.89  ? 63  HIS A NE2 1 
ATOM   463  N  N   . PHE A 1 65  ? 13.559 -16.679 15.405 1.00 5.69  ? 64  PHE A N   1 
ATOM   464  C  CA  . PHE A 1 65  ? 14.156 -16.919 16.694 1.00 8.91  ? 64  PHE A CA  1 
ATOM   465  C  C   . PHE A 1 65  ? 13.121 -16.849 17.870 1.00 8.76  ? 64  PHE A C   1 
ATOM   466  O  O   . PHE A 1 65  ? 12.654 -15.838 18.348 1.00 7.52  ? 64  PHE A O   1 
ATOM   467  C  CB  . PHE A 1 65  ? 15.207 -15.879 17.068 1.00 8.35  ? 64  PHE A CB  1 
ATOM   468  C  CG  . PHE A 1 65  ? 16.100 -15.995 18.263 1.00 8.96  ? 64  PHE A CG  1 
ATOM   469  C  CD1 . PHE A 1 65  ? 16.603 -17.249 18.727 1.00 7.06  ? 64  PHE A CD1 1 
ATOM   470  C  CD2 . PHE A 1 65  ? 16.472 -14.801 18.948 1.00 7.03  ? 64  PHE A CD2 1 
ATOM   471  C  CE1 . PHE A 1 65  ? 17.451 -17.267 19.835 1.00 5.21  ? 64  PHE A CE1 1 
ATOM   472  C  CE2 . PHE A 1 65  ? 17.312 -14.838 20.045 1.00 5.40  ? 64  PHE A CE2 1 
ATOM   473  C  CZ  . PHE A 1 65  ? 17.794 -16.069 20.473 1.00 5.78  ? 64  PHE A CZ  1 
ATOM   474  N  N   . ASN A 1 66  ? 12.805 -18.053 18.340 1.00 9.63  ? 65  ASN A N   1 
ATOM   475  C  CA  . ASN A 1 66  ? 11.849 -18.184 19.432 1.00 9.18  ? 65  ASN A CA  1 
ATOM   476  C  C   . ASN A 1 66  ? 12.102 -18.638 20.862 1.00 7.97  ? 65  ASN A C   1 
ATOM   477  O  O   . ASN A 1 66  ? 11.045 -19.009 21.282 1.00 5.42  ? 65  ASN A O   1 
ATOM   478  C  CB  . ASN A 1 66  ? 10.656 -19.083 18.800 1.00 9.43  ? 65  ASN A CB  1 
ATOM   479  C  CG  . ASN A 1 66  ? 9.395  -18.232 18.650 1.00 9.87  ? 65  ASN A CG  1 
ATOM   480  O  OD1 . ASN A 1 66  ? 9.566  -17.060 18.274 1.00 8.80  ? 65  ASN A OD1 1 
ATOM   481  N  ND2 . ASN A 1 66  ? 8.172  -18.746 18.933 1.00 6.69  ? 65  ASN A ND2 1 
ATOM   482  N  N   . PRO A 1 67  ? 13.117 -18.657 21.675 1.00 10.29 ? 66  PRO A N   1 
ATOM   483  C  CA  . PRO A 1 67  ? 13.278 -19.030 23.117 1.00 8.56  ? 66  PRO A CA  1 
ATOM   484  C  C   . PRO A 1 67  ? 12.109 -19.611 23.787 1.00 7.78  ? 66  PRO A C   1 
ATOM   485  O  O   . PRO A 1 67  ? 12.436 -20.626 24.450 1.00 9.87  ? 66  PRO A O   1 
ATOM   486  C  CB  . PRO A 1 67  ? 13.729 -17.602 23.555 1.00 8.11  ? 66  PRO A CB  1 
ATOM   487  C  CG  . PRO A 1 67  ? 14.880 -17.310 22.564 1.00 7.74  ? 66  PRO A CG  1 
ATOM   488  C  CD  . PRO A 1 67  ? 14.514 -18.148 21.263 1.00 10.29 ? 66  PRO A CD  1 
ATOM   489  N  N   . LEU A 1 68  ? 10.860 -19.243 23.783 1.00 7.10  ? 67  LEU A N   1 
ATOM   490  C  CA  . LEU A 1 68  ? 9.652  -19.937 24.430 1.00 7.99  ? 67  LEU A CA  1 
ATOM   491  C  C   . LEU A 1 68  ? 8.655  -19.508 23.289 1.00 7.34  ? 67  LEU A C   1 
ATOM   492  O  O   . LEU A 1 68  ? 8.413  -18.333 23.188 1.00 6.07  ? 67  LEU A O   1 
ATOM   493  C  CB  . LEU A 1 68  ? 9.138  -19.699 25.840 1.00 10.37 ? 67  LEU A CB  1 
ATOM   494  C  CG  . LEU A 1 68  ? 8.815  -20.984 26.650 1.00 10.25 ? 67  LEU A CG  1 
ATOM   495  C  CD1 . LEU A 1 68  ? 8.414  -20.599 28.064 1.00 10.14 ? 67  LEU A CD1 1 
ATOM   496  C  CD2 . LEU A 1 68  ? 7.673  -21.774 26.053 1.00 10.66 ? 67  LEU A CD2 1 
ATOM   497  N  N   . SER A 1 69  ? 8.162  -20.408 22.519 1.00 5.94  ? 68  SER A N   1 
ATOM   498  C  CA  . SER A 1 69  ? 7.344  -20.046 21.383 1.00 7.51  ? 68  SER A CA  1 
ATOM   499  C  C   . SER A 1 69  ? 6.102  -19.210 21.251 1.00 8.95  ? 68  SER A C   1 
ATOM   500  O  O   . SER A 1 69  ? 4.854  -19.440 21.377 1.00 4.72  ? 68  SER A O   1 
ATOM   501  C  CB  . SER A 1 69  ? 7.108  -21.474 20.692 1.00 9.93  ? 68  SER A CB  1 
ATOM   502  O  OG  . SER A 1 69  ? 8.464  -21.818 20.254 1.00 13.39 ? 68  SER A OG  1 
ATOM   503  N  N   . ARG A 1 70  ? 6.684  -17.972 20.839 1.00 7.90  ? 69  ARG A N   1 
ATOM   504  C  CA  . ARG A 1 70  ? 5.700  -16.914 20.593 1.00 8.10  ? 69  ARG A CA  1 
ATOM   505  C  C   . ARG A 1 70  ? 5.251  -16.814 19.151 1.00 10.72 ? 69  ARG A C   1 
ATOM   506  O  O   . ARG A 1 70  ? 5.846  -17.352 18.177 1.00 10.19 ? 69  ARG A O   1 
ATOM   507  C  CB  . ARG A 1 70  ? 6.154  -15.439 20.969 1.00 6.15  ? 69  ARG A CB  1 
ATOM   508  C  CG  . ARG A 1 70  ? 5.357  -15.102 22.175 1.00 4.14  ? 69  ARG A CG  1 
ATOM   509  C  CD  . ARG A 1 70  ? 6.121  -15.775 23.394 1.00 4.43  ? 69  ARG A CD  1 
ATOM   510  N  NE  . ARG A 1 70  ? 6.610  -14.573 24.099 1.00 5.76  ? 69  ARG A NE  1 
ATOM   511  C  CZ  . ARG A 1 70  ? 6.529  -14.392 25.433 1.00 7.25  ? 69  ARG A CZ  1 
ATOM   512  N  NH1 . ARG A 1 70  ? 6.120  -15.510 26.088 1.00 6.99  ? 69  ARG A NH1 1 
ATOM   513  N  NH2 . ARG A 1 70  ? 6.883  -13.145 25.913 1.00 6.93  ? 69  ARG A NH2 1 
ATOM   514  N  N   . LYS A 1 71  ? 4.130  -16.051 19.059 1.00 11.21 ? 70  LYS A N   1 
ATOM   515  C  CA  . LYS A 1 71  ? 3.642  -15.836 17.681 1.00 8.60  ? 70  LYS A CA  1 
ATOM   516  C  C   . LYS A 1 71  ? 4.404  -14.540 17.339 1.00 8.03  ? 70  LYS A C   1 
ATOM   517  O  O   . LYS A 1 71  ? 5.189  -13.944 18.106 1.00 5.19  ? 70  LYS A O   1 
ATOM   518  C  CB  . LYS A 1 71  ? 2.195  -15.605 17.619 1.00 9.56  ? 70  LYS A CB  1 
ATOM   519  C  CG  . LYS A 1 71  ? 1.416  -16.189 18.838 1.00 11.24 ? 70  LYS A CG  1 
ATOM   520  C  CD  . LYS A 1 71  ? 1.112  -15.105 19.856 1.00 12.78 ? 70  LYS A CD  1 
ATOM   521  C  CE  . LYS A 1 71  ? 0.006  -14.192 19.318 1.00 14.68 ? 70  LYS A CE  1 
ATOM   522  N  NZ  . LYS A 1 71  ? -0.519 -13.159 20.218 1.00 13.60 ? 70  LYS A NZ  1 
ATOM   523  N  N   . HIS A 1 72  ? 4.145  -14.056 16.116 1.00 7.53  ? 71  HIS A N   1 
ATOM   524  C  CA  . HIS A 1 72  ? 4.726  -12.865 15.611 1.00 5.74  ? 71  HIS A CA  1 
ATOM   525  C  C   . HIS A 1 72  ? 4.277  -11.645 16.401 1.00 5.80  ? 71  HIS A C   1 
ATOM   526  O  O   . HIS A 1 72  ? 3.432  -11.811 17.268 1.00 3.92  ? 71  HIS A O   1 
ATOM   527  C  CB  . HIS A 1 72  ? 4.299  -12.545 14.139 1.00 6.37  ? 71  HIS A CB  1 
ATOM   528  C  CG  . HIS A 1 72  ? 5.427  -11.877 13.375 1.00 8.90  ? 71  HIS A CG  1 
ATOM   529  N  ND1 . HIS A 1 72  ? 6.795  -11.874 13.460 1.00 8.99  ? 71  HIS A ND1 1 
ATOM   530  C  CD2 . HIS A 1 72  ? 5.136  -11.110 12.317 1.00 10.95 ? 71  HIS A CD2 1 
ATOM   531  C  CE1 . HIS A 1 72  ? 7.312  -11.094 12.476 1.00 9.99  ? 71  HIS A CE1 1 
ATOM   532  N  NE2 . HIS A 1 72  ? 6.333  -10.639 11.794 1.00 12.25 ? 71  HIS A NE2 1 
ATOM   533  N  N   . GLY A 1 73  ? 4.849  -10.483 16.026 1.00 5.02  ? 72  GLY A N   1 
ATOM   534  C  CA  . GLY A 1 73  ? 4.712  -9.176  16.381 1.00 3.28  ? 72  GLY A CA  1 
ATOM   535  C  C   . GLY A 1 73  ? 5.576  -8.181  15.521 1.00 4.52  ? 72  GLY A C   1 
ATOM   536  O  O   . GLY A 1 73  ? 6.307  -8.549  14.612 1.00 2.00  ? 72  GLY A O   1 
ATOM   537  N  N   . GLY A 1 74  ? 5.435  -6.844  15.865 1.00 3.27  ? 73  GLY A N   1 
ATOM   538  C  CA  . GLY A 1 74  ? 6.292  -5.810  15.129 1.00 3.56  ? 73  GLY A CA  1 
ATOM   539  C  C   . GLY A 1 74  ? 7.419  -5.651  16.150 1.00 2.00  ? 73  GLY A C   1 
ATOM   540  O  O   . GLY A 1 74  ? 7.615  -6.649  16.904 1.00 2.00  ? 73  GLY A O   1 
ATOM   541  N  N   . PRO A 1 75  ? 8.138  -4.623  16.283 1.00 2.00  ? 74  PRO A N   1 
ATOM   542  C  CA  . PRO A 1 75  ? 9.211  -4.549  17.376 1.00 2.00  ? 74  PRO A CA  1 
ATOM   543  C  C   . PRO A 1 75  ? 8.476  -4.029  18.639 1.00 2.43  ? 74  PRO A C   1 
ATOM   544  O  O   . PRO A 1 75  ? 8.503  -4.477  19.758 1.00 2.00  ? 74  PRO A O   1 
ATOM   545  C  CB  . PRO A 1 75  ? 10.272 -3.755  16.786 1.00 2.13  ? 74  PRO A CB  1 
ATOM   546  C  CG  . PRO A 1 75  ? 9.773  -3.574  15.352 1.00 2.00  ? 74  PRO A CG  1 
ATOM   547  C  CD  . PRO A 1 75  ? 8.218  -3.400  15.565 1.00 2.00  ? 74  PRO A CD  1 
ATOM   548  N  N   . LYS A 1 76  ? 7.681  -2.959  18.476 1.00 3.84  ? 75  LYS A N   1 
ATOM   549  C  CA  . LYS A 1 76  ? 6.824  -2.184  19.434 1.00 2.00  ? 75  LYS A CA  1 
ATOM   550  C  C   . LYS A 1 76  ? 5.975  -3.096  20.326 1.00 2.77  ? 75  LYS A C   1 
ATOM   551  O  O   . LYS A 1 76  ? 5.592  -2.634  21.488 1.00 2.23  ? 75  LYS A O   1 
ATOM   552  C  CB  . LYS A 1 76  ? 6.139  -1.223  18.549 1.00 2.00  ? 75  LYS A CB  1 
ATOM   553  C  CG  . LYS A 1 76  ? 5.529  0.099   18.862 1.00 2.00  ? 75  LYS A CG  1 
ATOM   554  C  CD  . LYS A 1 76  ? 6.296  1.233   19.393 1.00 2.77  ? 75  LYS A CD  1 
ATOM   555  C  CE  . LYS A 1 76  ? 5.588  2.265   20.282 1.00 4.21  ? 75  LYS A CE  1 
ATOM   556  N  NZ  . LYS A 1 76  ? 6.388  3.497   20.611 1.00 2.00  ? 75  LYS A NZ  1 
ATOM   557  N  N   . ASP A 1 77  ? 5.701  -4.383  19.939 1.00 2.95  ? 76  ASP A N   1 
ATOM   558  C  CA  . ASP A 1 77  ? 4.815  -5.188  20.941 1.00 3.84  ? 76  ASP A CA  1 
ATOM   559  C  C   . ASP A 1 77  ? 5.326  -6.068  22.027 1.00 2.56  ? 76  ASP A C   1 
ATOM   560  O  O   . ASP A 1 77  ? 6.528  -5.959  22.553 1.00 5.00  ? 76  ASP A O   1 
ATOM   561  C  CB  . ASP A 1 77  ? 4.003  -5.976  19.850 1.00 2.00  ? 76  ASP A CB  1 
ATOM   562  C  CG  . ASP A 1 77  ? 2.539  -6.006  20.266 1.00 4.68  ? 76  ASP A CG  1 
ATOM   563  O  OD1 . ASP A 1 77  ? 1.782  -5.053  20.019 1.00 2.73  ? 76  ASP A OD1 1 
ATOM   564  O  OD2 . ASP A 1 77  ? 1.997  -7.046  20.874 1.00 6.53  ? 76  ASP A OD2 1 
ATOM   565  N  N   . GLU A 1 78  ? 4.637  -6.989  22.594 1.00 2.68  ? 77  GLU A N   1 
ATOM   566  C  CA  . GLU A 1 78  ? 5.183  -7.921  23.644 1.00 3.99  ? 77  GLU A CA  1 
ATOM   567  C  C   . GLU A 1 78  ? 4.637  -9.221  22.972 1.00 5.87  ? 77  GLU A C   1 
ATOM   568  O  O   . GLU A 1 78  ? 4.822  -10.403 23.320 1.00 7.95  ? 77  GLU A O   1 
ATOM   569  C  CB  . GLU A 1 78  ? 4.983  -7.706  25.123 1.00 5.15  ? 77  GLU A CB  1 
ATOM   570  C  CG  . GLU A 1 78  ? 6.061  -6.981  25.983 1.00 4.27  ? 77  GLU A CG  1 
ATOM   571  C  CD  . GLU A 1 78  ? 7.471  -7.488  26.243 1.00 5.93  ? 77  GLU A CD  1 
ATOM   572  O  OE1 . GLU A 1 78  ? 7.901  -8.621  26.491 1.00 3.56  ? 77  GLU A OE1 1 
ATOM   573  O  OE2 . GLU A 1 78  ? 8.457  -6.656  26.251 1.00 3.96  ? 77  GLU A OE2 1 
ATOM   574  N  N   . GLU A 1 79  ? 3.878  -9.014  21.846 1.00 3.63  ? 78  GLU A N   1 
ATOM   575  C  CA  . GLU A 1 79  ? 3.449  -10.255 21.195 1.00 6.66  ? 78  GLU A CA  1 
ATOM   576  C  C   . GLU A 1 79  ? 4.569  -10.033 20.091 1.00 2.76  ? 78  GLU A C   1 
ATOM   577  O  O   . GLU A 1 79  ? 4.370  -9.075  19.368 1.00 2.00  ? 78  GLU A O   1 
ATOM   578  C  CB  . GLU A 1 79  ? 2.130  -10.656 20.563 1.00 6.32  ? 78  GLU A CB  1 
ATOM   579  C  CG  . GLU A 1 79  ? 1.543  -10.261 19.201 1.00 6.36  ? 78  GLU A CG  1 
ATOM   580  C  CD  . GLU A 1 79  ? 0.051  -10.351 19.218 1.00 6.83  ? 78  GLU A CD  1 
ATOM   581  O  OE1 . GLU A 1 79  ? -0.445 -9.683  20.139 1.00 7.61  ? 78  GLU A OE1 1 
ATOM   582  O  OE2 . GLU A 1 79  ? -0.657 -11.006 18.458 1.00 9.33  ? 78  GLU A OE2 1 
ATOM   583  N  N   . ARG A 1 80  ? 5.570  -10.846 20.138 1.00 2.00  ? 79  ARG A N   1 
ATOM   584  C  CA  . ARG A 1 80  ? 6.661  -10.803 19.129 1.00 4.45  ? 79  ARG A CA  1 
ATOM   585  C  C   . ARG A 1 80  ? 7.621  -11.975 19.515 1.00 7.22  ? 79  ARG A C   1 
ATOM   586  O  O   . ARG A 1 80  ? 7.664  -12.464 20.656 1.00 7.53  ? 79  ARG A O   1 
ATOM   587  C  CB  . ARG A 1 80  ? 7.411  -9.546  18.899 1.00 2.00  ? 79  ARG A CB  1 
ATOM   588  C  CG  . ARG A 1 80  ? 8.168  -9.132  20.116 1.00 2.14  ? 79  ARG A CG  1 
ATOM   589  C  CD  . ARG A 1 80  ? 8.423  -7.620  20.121 1.00 2.86  ? 79  ARG A CD  1 
ATOM   590  N  NE  . ARG A 1 80  ? 9.816  -7.269  20.093 1.00 2.00  ? 79  ARG A NE  1 
ATOM   591  C  CZ  . ARG A 1 80  ? 10.609 -7.801  19.174 1.00 2.00  ? 79  ARG A CZ  1 
ATOM   592  N  NH1 . ARG A 1 80  ? 10.055 -8.531  18.220 1.00 2.00  ? 79  ARG A NH1 1 
ATOM   593  N  NH2 . ARG A 1 80  ? 11.948 -7.595  19.170 1.00 2.00  ? 79  ARG A NH2 1 
ATOM   594  N  N   . HIS A 1 81  ? 8.385  -12.427 18.525 1.00 8.62  ? 80  HIS A N   1 
ATOM   595  C  CA  . HIS A 1 81  ? 9.351  -13.514 18.738 1.00 7.42  ? 80  HIS A CA  1 
ATOM   596  C  C   . HIS A 1 81  ? 10.573 -12.806 19.215 1.00 8.70  ? 80  HIS A C   1 
ATOM   597  O  O   . HIS A 1 81  ? 10.638 -11.592 18.899 1.00 5.53  ? 80  HIS A O   1 
ATOM   598  C  CB  . HIS A 1 81  ? 9.695  -14.241 17.453 1.00 6.57  ? 80  HIS A CB  1 
ATOM   599  C  CG  . HIS A 1 81  ? 8.722  -14.639 16.388 1.00 12.19 ? 80  HIS A CG  1 
ATOM   600  N  ND1 . HIS A 1 81  ? 8.503  -14.498 15.048 1.00 11.10 ? 80  HIS A ND1 1 
ATOM   601  C  CD2 . HIS A 1 81  ? 7.635  -15.459 16.861 1.00 14.33 ? 80  HIS A CD2 1 
ATOM   602  C  CE1 . HIS A 1 81  ? 7.357  -15.220 14.784 1.00 12.10 ? 80  HIS A CE1 1 
ATOM   603  N  NE2 . HIS A 1 81  ? 6.828  -15.765 15.744 1.00 13.94 ? 80  HIS A NE2 1 
ATOM   604  N  N   . VAL A 1 82  ? 11.558 -13.312 19.877 1.00 9.21  ? 81  VAL A N   1 
ATOM   605  C  CA  . VAL A 1 82  ? 12.778 -12.641 20.287 1.00 9.96  ? 81  VAL A CA  1 
ATOM   606  C  C   . VAL A 1 82  ? 13.702 -12.557 19.023 1.00 9.88  ? 81  VAL A C   1 
ATOM   607  O  O   . VAL A 1 82  ? 14.906 -12.105 19.109 1.00 10.08 ? 81  VAL A O   1 
ATOM   608  C  CB  . VAL A 1 82  ? 13.463 -13.327 21.466 1.00 11.87 ? 81  VAL A CB  1 
ATOM   609  C  CG1 . VAL A 1 82  ? 14.098 -14.667 21.014 1.00 13.56 ? 81  VAL A CG1 1 
ATOM   610  C  CG2 . VAL A 1 82  ? 14.567 -12.571 22.244 1.00 13.18 ? 81  VAL A CG2 1 
ATOM   611  N  N   . GLY A 1 83  ? 13.247 -12.969 17.845 1.00 8.82  ? 82  GLY A N   1 
ATOM   612  C  CA  . GLY A 1 83  ? 14.091 -12.844 16.637 1.00 8.12  ? 82  GLY A CA  1 
ATOM   613  C  C   . GLY A 1 83  ? 13.547 -11.655 15.770 1.00 6.84  ? 82  GLY A C   1 
ATOM   614  O  O   . GLY A 1 83  ? 14.292 -10.809 15.315 1.00 4.27  ? 82  GLY A O   1 
ATOM   615  N  N   . ASP A 1 84  ? 12.241 -11.544 15.527 1.00 9.40  ? 83  ASP A N   1 
ATOM   616  C  CA  . ASP A 1 84  ? 11.726 -10.450 14.652 1.00 11.28 ? 83  ASP A CA  1 
ATOM   617  C  C   . ASP A 1 84  ? 11.864 -9.010  15.114 1.00 11.50 ? 83  ASP A C   1 
ATOM   618  O  O   . ASP A 1 84  ? 11.160 -8.610  15.994 1.00 11.25 ? 83  ASP A O   1 
ATOM   619  C  CB  . ASP A 1 84  ? 10.262 -10.688 14.232 1.00 12.10 ? 83  ASP A CB  1 
ATOM   620  C  CG  . ASP A 1 84  ? 9.332  -11.409 15.163 1.00 11.34 ? 83  ASP A CG  1 
ATOM   621  O  OD1 . ASP A 1 84  ? 9.135  -10.878 16.233 1.00 11.93 ? 83  ASP A OD1 1 
ATOM   622  O  OD2 . ASP A 1 84  ? 8.845  -12.458 14.785 1.00 9.97  ? 83  ASP A OD2 1 
ATOM   623  N  N   . LEU A 1 85  ? 12.817 -8.355  14.404 1.00 11.72 ? 84  LEU A N   1 
ATOM   624  C  CA  . LEU A 1 85  ? 13.132 -6.979  14.638 1.00 10.49 ? 84  LEU A CA  1 
ATOM   625  C  C   . LEU A 1 85  ? 12.041 -6.217  13.803 1.00 12.42 ? 84  LEU A C   1 
ATOM   626  O  O   . LEU A 1 85  ? 10.839 -6.216  14.212 1.00 12.68 ? 84  LEU A O   1 
ATOM   627  C  CB  . LEU A 1 85  ? 14.538 -6.481  14.274 1.00 8.04  ? 84  LEU A CB  1 
ATOM   628  C  CG  . LEU A 1 85  ? 15.721 -7.188  14.921 1.00 5.75  ? 84  LEU A CG  1 
ATOM   629  C  CD1 . LEU A 1 85  ? 17.024 -7.152  14.169 1.00 2.00  ? 84  LEU A CD1 1 
ATOM   630  C  CD2 . LEU A 1 85  ? 15.796 -6.542  16.352 1.00 5.55  ? 84  LEU A CD2 1 
ATOM   631  N  N   . GLY A 1 86  ? 12.441 -5.634  12.684 1.00 11.76 ? 85  GLY A N   1 
ATOM   632  C  CA  . GLY A 1 86  ? 11.348 -4.902  11.990 1.00 11.76 ? 85  GLY A CA  1 
ATOM   633  C  C   . GLY A 1 86  ? 11.096 -5.287  10.607 1.00 11.65 ? 85  GLY A C   1 
ATOM   634  O  O   . GLY A 1 86  ? 11.245 -6.373  10.101 1.00 14.23 ? 85  GLY A O   1 
ATOM   635  N  N   . ASN A 1 87  ? 10.692 -4.252  9.981  1.00 11.99 ? 86  ASN A N   1 
ATOM   636  C  CA  . ASN A 1 87  ? 10.312 -4.125  8.533  1.00 9.80  ? 86  ASN A CA  1 
ATOM   637  C  C   . ASN A 1 87  ? 11.353 -3.060  8.260  1.00 9.68  ? 86  ASN A C   1 
ATOM   638  O  O   . ASN A 1 87  ? 11.809 -2.336  9.258  1.00 10.98 ? 86  ASN A O   1 
ATOM   639  C  CB  . ASN A 1 87  ? 8.834  -3.929  8.664  1.00 9.86  ? 86  ASN A CB  1 
ATOM   640  C  CG  . ASN A 1 87  ? 8.050  -3.139  7.660  1.00 9.06  ? 86  ASN A CG  1 
ATOM   641  O  OD1 . ASN A 1 87  ? 7.624  -3.722  6.595  1.00 7.37  ? 86  ASN A OD1 1 
ATOM   642  N  ND2 . ASN A 1 87  ? 7.917  -1.854  8.116  1.00 5.78  ? 86  ASN A ND2 1 
ATOM   643  N  N   . VAL A 1 88  ? 11.781 -2.869  7.094  1.00 8.17  ? 87  VAL A N   1 
ATOM   644  C  CA  . VAL A 1 88  ? 12.773 -1.935  6.659  1.00 8.34  ? 87  VAL A CA  1 
ATOM   645  C  C   . VAL A 1 88  ? 12.471 -1.332  5.305  1.00 9.08  ? 87  VAL A C   1 
ATOM   646  O  O   . VAL A 1 88  ? 12.222 -2.179  4.412  1.00 8.63  ? 87  VAL A O   1 
ATOM   647  C  CB  . VAL A 1 88  ? 14.084 -2.776  6.653  1.00 6.57  ? 87  VAL A CB  1 
ATOM   648  C  CG1 . VAL A 1 88  ? 15.120 -2.343  5.644  1.00 7.67  ? 87  VAL A CG1 1 
ATOM   649  C  CG2 . VAL A 1 88  ? 14.630 -2.799  8.084  1.00 7.87  ? 87  VAL A CG2 1 
ATOM   650  N  N   . THR A 1 89  ? 12.548 0.024   5.220  1.00 8.16  ? 88  THR A N   1 
ATOM   651  C  CA  . THR A 1 89  ? 12.249 0.514   3.879  1.00 5.37  ? 88  THR A CA  1 
ATOM   652  C  C   . THR A 1 89  ? 13.339 0.879   2.866  1.00 4.13  ? 88  THR A C   1 
ATOM   653  O  O   . THR A 1 89  ? 14.255 1.661   2.921  1.00 3.91  ? 88  THR A O   1 
ATOM   654  C  CB  . THR A 1 89  ? 11.417 1.878   3.967  1.00 4.19  ? 88  THR A CB  1 
ATOM   655  O  OG1 . THR A 1 89  ? 10.480 1.636   5.156  1.00 5.14  ? 88  THR A OG1 1 
ATOM   656  C  CG2 . THR A 1 89  ? 10.759 2.311   2.673  1.00 2.00  ? 88  THR A CG2 1 
ATOM   657  N  N   . ALA A 1 90  ? 13.104 0.211   1.701  1.00 4.20  ? 89  ALA A N   1 
ATOM   658  C  CA  . ALA A 1 90  ? 13.857 0.403   0.511  1.00 4.73  ? 89  ALA A CA  1 
ATOM   659  C  C   . ALA A 1 90  ? 13.231 1.705   -0.097 1.00 5.36  ? 89  ALA A C   1 
ATOM   660  O  O   . ALA A 1 90  ? 11.937 1.651   -0.389 1.00 5.49  ? 89  ALA A O   1 
ATOM   661  C  CB  . ALA A 1 90  ? 13.548 -0.649  -0.529 1.00 5.58  ? 89  ALA A CB  1 
ATOM   662  N  N   . ASP A 1 91  ? 13.761 2.808   -0.380 1.00 4.40  ? 90  ASP A N   1 
ATOM   663  C  CA  . ASP A 1 91  ? 12.996 3.947   -0.996 1.00 6.37  ? 90  ASP A CA  1 
ATOM   664  C  C   . ASP A 1 91  ? 13.442 3.618   -2.468 1.00 5.99  ? 90  ASP A C   1 
ATOM   665  O  O   . ASP A 1 91  ? 13.590 2.419   -2.846 1.00 3.09  ? 90  ASP A O   1 
ATOM   666  C  CB  . ASP A 1 91  ? 13.308 5.270   -0.404 1.00 7.74  ? 90  ASP A CB  1 
ATOM   667  C  CG  . ASP A 1 91  ? 12.122 6.136   0.111  1.00 11.76 ? 90  ASP A CG  1 
ATOM   668  O  OD1 . ASP A 1 91  ? 10.956 5.578   0.296  1.00 10.35 ? 90  ASP A OD1 1 
ATOM   669  O  OD2 . ASP A 1 91  ? 12.392 7.396   0.334  1.00 9.46  ? 90  ASP A OD2 1 
ATOM   670  N  N   . LYS A 1 92  ? 13.639 4.652   -3.243 1.00 5.75  ? 91  LYS A N   1 
ATOM   671  C  CA  . LYS A 1 92  ? 14.087 4.490   -4.677 1.00 4.40  ? 91  LYS A CA  1 
ATOM   672  C  C   . LYS A 1 92  ? 15.580 4.092   -4.559 1.00 4.40  ? 91  LYS A C   1 
ATOM   673  O  O   . LYS A 1 92  ? 16.238 4.359   -3.562 1.00 2.00  ? 91  LYS A O   1 
ATOM   674  C  CB  . LYS A 1 92  ? 13.868 5.638   -5.605 1.00 3.57  ? 91  LYS A CB  1 
ATOM   675  C  CG  . LYS A 1 92  ? 12.279 5.856   -5.852 1.00 5.87  ? 91  LYS A CG  1 
ATOM   676  C  CD  . LYS A 1 92  ? 11.877 4.904   -6.967 1.00 3.31  ? 91  LYS A CD  1 
ATOM   677  C  CE  . LYS A 1 92  ? 11.401 3.544   -6.606 1.00 2.00  ? 91  LYS A CE  1 
ATOM   678  N  NZ  . LYS A 1 92  ? 9.985  4.024   -6.424 1.00 3.95  ? 91  LYS A NZ  1 
ATOM   679  N  N   . ASP A 1 93  ? 15.826 3.423   -5.682 1.00 3.98  ? 92  ASP A N   1 
ATOM   680  C  CA  . ASP A 1 93  ? 17.112 2.802   -6.030 1.00 4.63  ? 92  ASP A CA  1 
ATOM   681  C  C   . ASP A 1 93  ? 17.752 2.265   -4.734 1.00 4.01  ? 92  ASP A C   1 
ATOM   682  O  O   . ASP A 1 93  ? 18.925 2.475   -4.499 1.00 3.10  ? 92  ASP A O   1 
ATOM   683  C  CB  . ASP A 1 93  ? 18.078 3.690   -6.713 1.00 5.30  ? 92  ASP A CB  1 
ATOM   684  C  CG  . ASP A 1 93  ? 18.050 5.168   -6.343 1.00 6.50  ? 92  ASP A CG  1 
ATOM   685  O  OD1 . ASP A 1 93  ? 17.050 5.811   -6.728 1.00 4.74  ? 92  ASP A OD1 1 
ATOM   686  O  OD2 . ASP A 1 93  ? 19.045 5.625   -5.712 1.00 7.00  ? 92  ASP A OD2 1 
ATOM   687  N  N   . GLY A 1 94  ? 16.860 1.575   -4.086 1.00 3.68  ? 93  GLY A N   1 
ATOM   688  C  CA  . GLY A 1 94  ? 16.889 0.946   -2.821 1.00 4.67  ? 93  GLY A CA  1 
ATOM   689  C  C   . GLY A 1 94  ? 18.096 0.965   -1.900 1.00 2.00  ? 93  GLY A C   1 
ATOM   690  O  O   . GLY A 1 94  ? 18.808 0.064   -1.581 1.00 2.00  ? 93  GLY A O   1 
ATOM   691  N  N   . VAL A 1 95  ? 18.262 2.175   -1.412 1.00 4.14  ? 94  VAL A N   1 
ATOM   692  C  CA  . VAL A 1 95  ? 19.430 2.273   -0.439 1.00 9.50  ? 94  VAL A CA  1 
ATOM   693  C  C   . VAL A 1 95  ? 18.563 1.955   0.825  1.00 7.80  ? 94  VAL A C   1 
ATOM   694  O  O   . VAL A 1 95  ? 18.354 2.930   1.546  1.00 7.98  ? 94  VAL A O   1 
ATOM   695  C  CB  . VAL A 1 95  ? 20.252 3.584   -0.380 1.00 10.24 ? 94  VAL A CB  1 
ATOM   696  C  CG1 . VAL A 1 95  ? 21.155 3.678   0.909  1.00 11.13 ? 94  VAL A CG1 1 
ATOM   697  C  CG2 . VAL A 1 95  ? 21.089 3.931   -1.614 1.00 8.52  ? 94  VAL A CG2 1 
ATOM   698  N  N   . ALA A 1 96  ? 18.083 0.769   1.159  1.00 7.61  ? 95  ALA A N   1 
ATOM   699  C  CA  . ALA A 1 96  ? 17.276 0.714   2.435  1.00 8.32  ? 95  ALA A CA  1 
ATOM   700  C  C   . ALA A 1 96  ? 18.242 0.890   3.617  1.00 7.08  ? 95  ALA A C   1 
ATOM   701  O  O   . ALA A 1 96  ? 18.892 -0.145  4.075  1.00 6.76  ? 95  ALA A O   1 
ATOM   702  C  CB  . ALA A 1 96  ? 16.622 -0.631  2.505  1.00 9.97  ? 95  ALA A CB  1 
ATOM   703  N  N   . ASP A 1 97  ? 18.295 2.188   4.010  1.00 6.63  ? 96  ASP A N   1 
ATOM   704  C  CA  . ASP A 1 97  ? 19.206 2.601   5.123  1.00 4.70  ? 96  ASP A CA  1 
ATOM   705  C  C   . ASP A 1 97  ? 18.563 2.244   6.427  1.00 5.42  ? 96  ASP A C   1 
ATOM   706  O  O   . ASP A 1 97  ? 17.593 2.847   6.847  1.00 5.09  ? 96  ASP A O   1 
ATOM   707  C  CB  . ASP A 1 97  ? 19.593 4.066   5.260  1.00 4.29  ? 96  ASP A CB  1 
ATOM   708  C  CG  . ASP A 1 97  ? 21.083 4.227   4.898  1.00 2.83  ? 96  ASP A CG  1 
ATOM   709  O  OD1 . ASP A 1 97  ? 21.392 4.432   3.671  1.00 5.03  ? 96  ASP A OD1 1 
ATOM   710  O  OD2 . ASP A 1 97  ? 21.792 4.111   5.857  1.00 2.00  ? 96  ASP A OD2 1 
ATOM   711  N  N   . VAL A 1 98  ? 19.263 1.212   6.929  1.00 5.63  ? 97  VAL A N   1 
ATOM   712  C  CA  . VAL A 1 98  ? 18.714 0.740   8.213  1.00 6.08  ? 97  VAL A CA  1 
ATOM   713  C  C   . VAL A 1 98  ? 19.210 1.465   9.457  1.00 6.68  ? 97  VAL A C   1 
ATOM   714  O  O   . VAL A 1 98  ? 20.366 1.873   9.549  1.00 7.39  ? 97  VAL A O   1 
ATOM   715  C  CB  . VAL A 1 98  ? 19.010 -0.793  8.137  1.00 2.80  ? 97  VAL A CB  1 
ATOM   716  C  CG1 . VAL A 1 98  ? 18.648 -1.554  9.346  1.00 2.00  ? 97  VAL A CG1 1 
ATOM   717  C  CG2 . VAL A 1 98  ? 18.264 -1.280  6.910  1.00 2.00  ? 97  VAL A CG2 1 
ATOM   718  N  N   . SER A 1 99  ? 18.219 1.594   10.354 1.00 6.79  ? 98  SER A N   1 
ATOM   719  C  CA  . SER A 1 99  ? 18.543 2.192   11.650 1.00 7.22  ? 98  SER A CA  1 
ATOM   720  C  C   . SER A 1 99  ? 17.520 1.387   12.481 1.00 6.35  ? 98  SER A C   1 
ATOM   721  O  O   . SER A 1 99  ? 16.469 1.140   11.810 1.00 6.56  ? 98  SER A O   1 
ATOM   722  C  CB  . SER A 1 99  ? 18.464 3.654   11.976 1.00 9.49  ? 98  SER A CB  1 
ATOM   723  O  OG  . SER A 1 99  ? 18.849 4.074   13.360 1.00 9.69  ? 98  SER A OG  1 
ATOM   724  N  N   . ILE A 1 100 ? 17.819 1.062   13.718 1.00 6.33  ? 99  ILE A N   1 
ATOM   725  C  CA  . ILE A 1 100 ? 16.964 0.305   14.643 1.00 5.68  ? 99  ILE A CA  1 
ATOM   726  C  C   . ILE A 1 100 ? 17.633 0.385   16.053 1.00 8.12  ? 99  ILE A C   1 
ATOM   727  O  O   . ILE A 1 100 ? 18.943 0.649   15.982 1.00 7.32  ? 99  ILE A O   1 
ATOM   728  C  CB  . ILE A 1 100 ? 16.782 -1.224  14.381 1.00 3.55  ? 99  ILE A CB  1 
ATOM   729  C  CG1 . ILE A 1 100 ? 16.708 -1.656  12.879 1.00 2.05  ? 99  ILE A CG1 1 
ATOM   730  C  CG2 . ILE A 1 100 ? 15.529 -1.723  15.159 1.00 2.89  ? 99  ILE A CG2 1 
ATOM   731  C  CD1 . ILE A 1 100 ? 15.459 -2.307  12.347 1.00 2.00  ? 99  ILE A CD1 1 
ATOM   732  N  N   . GLU A 1 101 ? 16.809 0.145   17.093 1.00 3.84  ? 100 GLU A N   1 
ATOM   733  C  CA  . GLU A 1 101 ? 17.392 0.193   18.443 1.00 4.81  ? 100 GLU A CA  1 
ATOM   734  C  C   . GLU A 1 101 ? 16.653 -0.739  19.407 1.00 3.64  ? 100 GLU A C   1 
ATOM   735  O  O   . GLU A 1 101 ? 16.205 -0.361  20.483 1.00 2.00  ? 100 GLU A O   1 
ATOM   736  C  CB  . GLU A 1 101 ? 17.351 1.614   19.029 1.00 4.30  ? 100 GLU A CB  1 
ATOM   737  C  CG  . GLU A 1 101 ? 18.504 2.520   18.582 1.00 5.54  ? 100 GLU A CG  1 
ATOM   738  C  CD  . GLU A 1 101 ? 19.075 3.488   19.633 1.00 4.12  ? 100 GLU A CD  1 
ATOM   739  O  OE1 . GLU A 1 101 ? 19.304 3.094   20.833 1.00 4.53  ? 100 GLU A OE1 1 
ATOM   740  O  OE2 . GLU A 1 101 ? 19.314 4.620   19.296 1.00 2.32  ? 100 GLU A OE2 1 
ATOM   741  N  N   . ASP A 1 102 ? 16.639 -1.995  18.989 1.00 5.80  ? 101 ASP A N   1 
ATOM   742  C  CA  . ASP A 1 102 ? 15.850 -2.979  19.831 1.00 5.54  ? 101 ASP A CA  1 
ATOM   743  C  C   . ASP A 1 102 ? 16.496 -3.364  21.119 1.00 7.00  ? 101 ASP A C   1 
ATOM   744  O  O   . ASP A 1 102 ? 17.699 -3.362  21.265 1.00 6.94  ? 101 ASP A O   1 
ATOM   745  C  CB  . ASP A 1 102 ? 15.450 -4.152  18.937 1.00 2.00  ? 101 ASP A CB  1 
ATOM   746  C  CG  . ASP A 1 102 ? 14.826 -5.302  19.693 1.00 2.00  ? 101 ASP A CG  1 
ATOM   747  O  OD1 . ASP A 1 102 ? 15.486 -6.226  20.186 1.00 2.00  ? 101 ASP A OD1 1 
ATOM   748  O  OD2 . ASP A 1 102 ? 13.592 -5.369  19.833 1.00 2.00  ? 101 ASP A OD2 1 
ATOM   749  N  N   . SER A 1 103 ? 15.596 -3.677  22.103 1.00 10.35 ? 102 SER A N   1 
ATOM   750  C  CA  . SER A 1 103 ? 15.964 -4.060  23.470 1.00 9.83  ? 102 SER A CA  1 
ATOM   751  C  C   . SER A 1 103 ? 15.820 -5.530  23.848 1.00 10.46 ? 102 SER A C   1 
ATOM   752  O  O   . SER A 1 103 ? 16.156 -6.013  24.997 1.00 12.42 ? 102 SER A O   1 
ATOM   753  C  CB  . SER A 1 103 ? 15.083 -3.147  24.342 1.00 10.22 ? 102 SER A CB  1 
ATOM   754  O  OG  . SER A 1 103 ? 13.842 -2.700  23.818 1.00 8.40  ? 102 SER A OG  1 
ATOM   755  N  N   . VAL A 1 104 ? 15.320 -6.324  22.940 1.00 7.64  ? 103 VAL A N   1 
ATOM   756  C  CA  . VAL A 1 104 ? 15.110 -7.734  23.199 1.00 5.28  ? 103 VAL A CA  1 
ATOM   757  C  C   . VAL A 1 104 ? 16.276 -8.556  22.681 1.00 6.03  ? 103 VAL A C   1 
ATOM   758  O  O   . VAL A 1 104 ? 16.826 -9.357  23.488 1.00 5.80  ? 103 VAL A O   1 
ATOM   759  C  CB  . VAL A 1 104 ? 13.740 -8.131  22.590 1.00 5.38  ? 103 VAL A CB  1 
ATOM   760  C  CG1 . VAL A 1 104 ? 13.106 -9.359  23.244 1.00 4.20  ? 103 VAL A CG1 1 
ATOM   761  C  CG2 . VAL A 1 104 ? 12.757 -6.943  22.553 1.00 4.05  ? 103 VAL A CG2 1 
ATOM   762  N  N   . ILE A 1 105 ? 16.584 -8.311  21.404 1.00 4.47  ? 104 ILE A N   1 
ATOM   763  C  CA  . ILE A 1 105 ? 17.677 -9.063  20.760 1.00 4.37  ? 104 ILE A CA  1 
ATOM   764  C  C   . ILE A 1 105 ? 18.969 -8.521  21.405 1.00 7.52  ? 104 ILE A C   1 
ATOM   765  O  O   . ILE A 1 105 ? 19.120 -7.308  21.495 1.00 7.83  ? 104 ILE A O   1 
ATOM   766  C  CB  . ILE A 1 105 ? 17.541 -9.037  19.213 1.00 2.75  ? 104 ILE A CB  1 
ATOM   767  C  CG1 . ILE A 1 105 ? 18.037 -7.845  18.406 1.00 2.00  ? 104 ILE A CG1 1 
ATOM   768  C  CG2 . ILE A 1 105 ? 16.002 -9.196  18.798 1.00 4.23  ? 104 ILE A CG2 1 
ATOM   769  C  CD1 . ILE A 1 105 ? 19.538 -7.559  18.546 1.00 2.00  ? 104 ILE A CD1 1 
ATOM   770  N  N   . SER A 1 106 ? 19.869 -9.392  21.840 1.00 8.10  ? 105 SER A N   1 
ATOM   771  C  CA  . SER A 1 106 ? 21.093 -9.059  22.515 1.00 10.76 ? 105 SER A CA  1 
ATOM   772  C  C   . SER A 1 106 ? 22.343 -9.230  21.750 1.00 11.79 ? 105 SER A C   1 
ATOM   773  O  O   . SER A 1 106 ? 22.161 -9.350  20.558 1.00 11.85 ? 105 SER A O   1 
ATOM   774  C  CB  . SER A 1 106 ? 21.305 -10.120 23.649 1.00 8.26  ? 105 SER A CB  1 
ATOM   775  O  OG  . SER A 1 106 ? 20.060 -10.756 23.943 1.00 10.27 ? 105 SER A OG  1 
ATOM   776  N  N   . LEU A 1 107 ? 23.453 -9.232  22.487 1.00 12.14 ? 106 LEU A N   1 
ATOM   777  C  CA  . LEU A 1 107 ? 24.760 -9.482  21.831 1.00 11.73 ? 106 LEU A CA  1 
ATOM   778  C  C   . LEU A 1 107 ? 25.598 -10.331 22.862 1.00 11.03 ? 106 LEU A C   1 
ATOM   779  O  O   . LEU A 1 107 ? 26.866 -10.453 22.637 1.00 14.02 ? 106 LEU A O   1 
ATOM   780  C  CB  . LEU A 1 107 ? 25.510 -8.296  21.331 1.00 10.22 ? 106 LEU A CB  1 
ATOM   781  C  CG  . LEU A 1 107 ? 25.114 -7.612  20.040 1.00 8.00  ? 106 LEU A CG  1 
ATOM   782  C  CD1 . LEU A 1 107 ? 26.406 -6.879  19.574 1.00 7.95  ? 106 LEU A CD1 1 
ATOM   783  C  CD2 . LEU A 1 107 ? 24.550 -8.600  19.085 1.00 5.13  ? 106 LEU A CD2 1 
ATOM   784  N  N   . SER A 1 108 ? 25.006 -10.890 23.911 1.00 7.04  ? 107 SER A N   1 
ATOM   785  C  CA  . SER A 1 108 ? 25.903 -11.624 24.799 1.00 6.71  ? 107 SER A CA  1 
ATOM   786  C  C   . SER A 1 108 ? 25.144 -12.022 26.059 1.00 5.95  ? 107 SER A C   1 
ATOM   787  O  O   . SER A 1 108 ? 25.232 -11.207 26.997 1.00 6.81  ? 107 SER A O   1 
ATOM   788  C  CB  . SER A 1 108 ? 27.076 -10.819 25.314 1.00 6.78  ? 107 SER A CB  1 
ATOM   789  O  OG  . SER A 1 108 ? 28.111 -11.717 25.653 1.00 6.22  ? 107 SER A OG  1 
ATOM   790  N  N   . GLY A 1 109 ? 24.590 -13.159 25.822 1.00 3.18  ? 108 GLY A N   1 
ATOM   791  C  CA  . GLY A 1 109 ? 23.785 -13.959 26.692 1.00 2.00  ? 108 GLY A CA  1 
ATOM   792  C  C   . GLY A 1 109 ? 22.402 -13.965 26.172 1.00 2.00  ? 108 GLY A C   1 
ATOM   793  O  O   . GLY A 1 109 ? 22.045 -13.029 25.438 1.00 2.29  ? 108 GLY A O   1 
ATOM   794  N  N   . ASP A 1 110 ? 21.655 -14.927 26.567 1.00 2.00  ? 109 ASP A N   1 
ATOM   795  C  CA  . ASP A 1 110 ? 20.259 -15.128 26.225 1.00 3.06  ? 109 ASP A CA  1 
ATOM   796  C  C   . ASP A 1 110 ? 20.008 -15.078 24.671 1.00 3.99  ? 109 ASP A C   1 
ATOM   797  O  O   . ASP A 1 110 ? 20.390 -15.916 23.823 1.00 2.00  ? 109 ASP A O   1 
ATOM   798  C  CB  . ASP A 1 110 ? 19.220 -14.168 26.872 1.00 2.00  ? 109 ASP A CB  1 
ATOM   799  C  CG  . ASP A 1 110 ? 19.416 -13.350 28.129 1.00 3.06  ? 109 ASP A CG  1 
ATOM   800  O  OD1 . ASP A 1 110 ? 20.555 -13.112 28.617 1.00 4.89  ? 109 ASP A OD1 1 
ATOM   801  O  OD2 . ASP A 1 110 ? 18.508 -12.792 28.835 1.00 2.00  ? 109 ASP A OD2 1 
ATOM   802  N  N   . HIS A 1 111 ? 19.314 -14.012 24.432 1.00 5.52  ? 110 HIS A N   1 
ATOM   803  C  CA  . HIS A 1 111 ? 18.816 -13.592 23.071 1.00 8.53  ? 110 HIS A CA  1 
ATOM   804  C  C   . HIS A 1 111 ? 20.033 -13.290 22.291 1.00 9.29  ? 110 HIS A C   1 
ATOM   805  O  O   . HIS A 1 111 ? 20.479 -12.257 21.869 1.00 8.15  ? 110 HIS A O   1 
ATOM   806  C  CB  . HIS A 1 111 ? 17.864 -12.511 23.556 1.00 10.95 ? 110 HIS A CB  1 
ATOM   807  C  CG  . HIS A 1 111 ? 16.988 -12.742 24.799 1.00 12.33 ? 110 HIS A CG  1 
ATOM   808  N  ND1 . HIS A 1 111 ? 16.935 -11.839 25.861 1.00 9.64  ? 110 HIS A ND1 1 
ATOM   809  C  CD2 . HIS A 1 111 ? 16.138 -13.761 25.116 1.00 11.25 ? 110 HIS A CD2 1 
ATOM   810  C  CE1 . HIS A 1 111 ? 16.069 -12.366 26.705 1.00 11.20 ? 110 HIS A CE1 1 
ATOM   811  N  NE2 . HIS A 1 111 ? 15.567 -13.510 26.313 1.00 9.40  ? 110 HIS A NE2 1 
ATOM   812  N  N   . CYS A 1 112 ? 20.756 -14.430 22.128 1.00 13.61 ? 111 CYS A N   1 
ATOM   813  C  CA  . CYS A 1 112 ? 22.067 -14.604 21.467 1.00 12.52 ? 111 CYS A CA  1 
ATOM   814  C  C   . CYS A 1 112 ? 21.807 -14.791 20.057 1.00 11.21 ? 111 CYS A C   1 
ATOM   815  O  O   . CYS A 1 112 ? 21.213 -15.804 19.740 1.00 10.76 ? 111 CYS A O   1 
ATOM   816  C  CB  . CYS A 1 112 ? 22.721 -15.702 22.364 1.00 12.62 ? 111 CYS A CB  1 
ATOM   817  S  SG  . CYS A 1 112 ? 23.938 -14.757 23.398 1.00 16.04 ? 111 CYS A SG  1 
ATOM   818  N  N   . ILE A 1 113 ? 22.233 -13.776 19.361 1.00 12.62 ? 112 ILE A N   1 
ATOM   819  C  CA  . ILE A 1 113 ? 22.000 -13.795 17.872 1.00 12.12 ? 112 ILE A CA  1 
ATOM   820  C  C   . ILE A 1 113 ? 23.256 -14.044 17.072 1.00 10.52 ? 112 ILE A C   1 
ATOM   821  O  O   . ILE A 1 113 ? 23.149 -14.171 15.842 1.00 11.71 ? 112 ILE A O   1 
ATOM   822  C  CB  . ILE A 1 113 ? 21.259 -12.464 17.334 1.00 10.31 ? 112 ILE A CB  1 
ATOM   823  C  CG1 . ILE A 1 113 ? 22.097 -11.310 17.906 1.00 10.98 ? 112 ILE A CG1 1 
ATOM   824  C  CG2 . ILE A 1 113 ? 19.715 -12.223 17.596 1.00 8.54  ? 112 ILE A CG2 1 
ATOM   825  C  CD1 . ILE A 1 113 ? 21.857 -9.845  17.430 1.00 10.21 ? 112 ILE A CD1 1 
ATOM   826  N  N   . ILE A 1 114 ? 24.397 -14.091 17.695 1.00 9.98  ? 113 ILE A N   1 
ATOM   827  C  CA  . ILE A 1 114 ? 25.722 -14.337 17.052 1.00 7.75  ? 113 ILE A CA  1 
ATOM   828  C  C   . ILE A 1 114 ? 25.609 -15.822 16.578 1.00 3.03  ? 113 ILE A C   1 
ATOM   829  O  O   . ILE A 1 114 ? 25.186 -16.718 17.276 1.00 2.00  ? 113 ILE A O   1 
ATOM   830  C  CB  . ILE A 1 114 ? 26.889 -14.001 18.028 1.00 9.39  ? 113 ILE A CB  1 
ATOM   831  C  CG1 . ILE A 1 114 ? 26.590 -12.823 18.975 1.00 9.68  ? 113 ILE A CG1 1 
ATOM   832  C  CG2 . ILE A 1 114 ? 28.231 -13.806 17.197 1.00 7.80  ? 113 ILE A CG2 1 
ATOM   833  C  CD1 . ILE A 1 114 ? 25.921 -11.465 18.586 1.00 8.95  ? 113 ILE A CD1 1 
ATOM   834  N  N   . GLY A 1 115 ? 25.967 -16.044 15.371 1.00 2.00  ? 114 GLY A N   1 
ATOM   835  C  CA  . GLY A 1 115 ? 25.954 -17.231 14.623 1.00 2.00  ? 114 GLY A CA  1 
ATOM   836  C  C   . GLY A 1 115 ? 24.506 -17.623 14.247 1.00 2.00  ? 114 GLY A C   1 
ATOM   837  O  O   . GLY A 1 115 ? 24.238 -18.792 13.915 1.00 2.00  ? 114 GLY A O   1 
ATOM   838  N  N   . ARG A 1 116 ? 23.605 -16.735 14.256 1.00 3.16  ? 115 ARG A N   1 
ATOM   839  C  CA  . ARG A 1 116 ? 22.218 -16.748 13.934 1.00 5.28  ? 115 ARG A CA  1 
ATOM   840  C  C   . ARG A 1 116 ? 22.213 -16.120 12.475 1.00 7.00  ? 115 ARG A C   1 
ATOM   841  O  O   . ARG A 1 116 ? 23.278 -15.798 11.916 1.00 6.44  ? 115 ARG A O   1 
ATOM   842  C  CB  . ARG A 1 116 ? 21.233 -15.968 14.781 1.00 5.01  ? 115 ARG A CB  1 
ATOM   843  C  CG  . ARG A 1 116 ? 20.433 -16.656 15.845 1.00 7.69  ? 115 ARG A CG  1 
ATOM   844  C  CD  . ARG A 1 116 ? 21.193 -17.265 16.973 1.00 9.76  ? 115 ARG A CD  1 
ATOM   845  N  NE  . ARG A 1 116 ? 20.319 -18.177 17.639 1.00 10.78 ? 115 ARG A NE  1 
ATOM   846  C  CZ  . ARG A 1 116 ? 20.243 -18.699 18.858 1.00 11.56 ? 115 ARG A CZ  1 
ATOM   847  N  NH1 . ARG A 1 116 ? 21.043 -18.428 19.899 1.00 8.58  ? 115 ARG A NH1 1 
ATOM   848  N  NH2 . ARG A 1 116 ? 19.186 -19.557 18.940 1.00 13.03 ? 115 ARG A NH2 1 
ATOM   849  N  N   . THR A 1 117 ? 21.029 -15.954 11.880 1.00 4.51  ? 116 THR A N   1 
ATOM   850  C  CA  . THR A 1 117 ? 20.923 -15.410 10.536 1.00 3.76  ? 116 THR A CA  1 
ATOM   851  C  C   . THR A 1 117 ? 19.990 -14.253 10.572 1.00 3.86  ? 116 THR A C   1 
ATOM   852  O  O   . THR A 1 117 ? 19.124 -14.300 11.463 1.00 4.90  ? 116 THR A O   1 
ATOM   853  C  CB  . THR A 1 117 ? 20.492 -16.509 9.403  1.00 2.00  ? 116 THR A CB  1 
ATOM   854  O  OG1 . THR A 1 117 ? 21.719 -16.930 8.805  1.00 2.00  ? 116 THR A OG1 1 
ATOM   855  C  CG2 . THR A 1 117 ? 19.794 -16.204 8.108  1.00 2.00  ? 116 THR A CG2 1 
ATOM   856  N  N   . LEU A 1 118 ? 20.297 -13.356 9.633  1.00 3.32  ? 117 LEU A N   1 
ATOM   857  C  CA  . LEU A 1 118 ? 19.477 -12.149 9.490  1.00 2.00  ? 117 LEU A CA  1 
ATOM   858  C  C   . LEU A 1 118 ? 19.064 -12.285 7.938  1.00 3.68  ? 117 LEU A C   1 
ATOM   859  O  O   . LEU A 1 118 ? 19.928 -12.446 6.978  1.00 2.00  ? 117 LEU A O   1 
ATOM   860  C  CB  . LEU A 1 118 ? 20.039 -10.827 9.641  1.00 2.00  ? 117 LEU A CB  1 
ATOM   861  C  CG  . LEU A 1 118 ? 19.232 -9.576  9.953  1.00 2.00  ? 117 LEU A CG  1 
ATOM   862  C  CD1 . LEU A 1 118 ? 18.968 -9.415  11.454 1.00 2.00  ? 117 LEU A CD1 1 
ATOM   863  C  CD2 . LEU A 1 118 ? 20.012 -8.350  9.527  1.00 2.00  ? 117 LEU A CD2 1 
ATOM   864  N  N   . VAL A 1 119 ? 17.740 -12.183 7.996  1.00 5.06  ? 118 VAL A N   1 
ATOM   865  C  CA  . VAL A 1 119 ? 17.062 -12.285 6.658  1.00 9.77  ? 118 VAL A CA  1 
ATOM   866  C  C   . VAL A 1 119 ? 16.218 -10.972 6.543  1.00 9.45  ? 118 VAL A C   1 
ATOM   867  O  O   . VAL A 1 119 ? 15.589 -10.521 7.540  1.00 9.29  ? 118 VAL A O   1 
ATOM   868  C  CB  . VAL A 1 119 ? 16.344 -13.639 6.479  1.00 11.37 ? 118 VAL A CB  1 
ATOM   869  C  CG1 . VAL A 1 119 ? 15.331 -13.733 5.366  1.00 11.42 ? 118 VAL A CG1 1 
ATOM   870  C  CG2 . VAL A 1 119 ? 17.260 -14.824 6.188  1.00 10.60 ? 118 VAL A CG2 1 
ATOM   871  N  N   . VAL A 1 120 ? 16.315 -10.472 5.331  1.00 5.68  ? 119 VAL A N   1 
ATOM   872  C  CA  . VAL A 1 120 ? 15.714 -9.266  4.783  1.00 2.91  ? 119 VAL A CA  1 
ATOM   873  C  C   . VAL A 1 120 ? 14.804 -9.961  3.804  1.00 2.00  ? 119 VAL A C   1 
ATOM   874  O  O   . VAL A 1 120 ? 15.429 -10.685 2.995  1.00 2.40  ? 119 VAL A O   1 
ATOM   875  C  CB  . VAL A 1 120 ? 16.791 -8.276  4.254  1.00 2.92  ? 119 VAL A CB  1 
ATOM   876  C  CG1 . VAL A 1 120 ? 18.098 -8.823  3.801  1.00 2.00  ? 119 VAL A CG1 1 
ATOM   877  C  CG2 . VAL A 1 120 ? 16.315 -7.409  3.032  1.00 2.00  ? 119 VAL A CG2 1 
ATOM   878  N  N   . HIS A 1 121 ? 13.554 -9.754  3.895  1.00 2.00  ? 120 HIS A N   1 
ATOM   879  C  CA  . HIS A 1 121 ? 12.609 -10.495 2.979  1.00 3.05  ? 120 HIS A CA  1 
ATOM   880  C  C   . HIS A 1 121 ? 12.083 -9.724  1.799  1.00 3.22  ? 120 HIS A C   1 
ATOM   881  O  O   . HIS A 1 121 ? 12.274 -8.539  1.624  1.00 2.00  ? 120 HIS A O   1 
ATOM   882  C  CB  . HIS A 1 121 ? 11.452 -11.023 3.875  1.00 2.00  ? 120 HIS A CB  1 
ATOM   883  C  CG  . HIS A 1 121 ? 11.760 -11.960 4.986  1.00 2.00  ? 120 HIS A CG  1 
ATOM   884  N  ND1 . HIS A 1 121 ? 11.288 -13.247 4.995  1.00 2.00  ? 120 HIS A ND1 1 
ATOM   885  C  CD2 . HIS A 1 121 ? 12.473 -11.896 6.160  1.00 2.00  ? 120 HIS A CD2 1 
ATOM   886  C  CE1 . HIS A 1 121 ? 11.680 -13.853 6.005  1.00 2.00  ? 120 HIS A CE1 1 
ATOM   887  N  NE2 . HIS A 1 121 ? 12.452 -13.024 6.807  1.00 2.00  ? 120 HIS A NE2 1 
ATOM   888  N  N   . GLU A 1 122 ? 11.393 -10.469 0.962  1.00 6.13  ? 121 GLU A N   1 
ATOM   889  C  CA  . GLU A 1 122 ? 10.742 -10.007 -0.338 1.00 5.66  ? 121 GLU A CA  1 
ATOM   890  C  C   . GLU A 1 122 ? 9.375  -9.364  -0.191 1.00 4.86  ? 121 GLU A C   1 
ATOM   891  O  O   . GLU A 1 122 ? 9.295  -8.189  -0.647 1.00 2.11  ? 121 GLU A O   1 
ATOM   892  C  CB  . GLU A 1 122 ? 10.890 -11.225 -1.244 1.00 6.25  ? 121 GLU A CB  1 
ATOM   893  C  CG  . GLU A 1 122 ? 10.641 -10.790 -2.710 1.00 4.92  ? 121 GLU A CG  1 
ATOM   894  C  CD  . GLU A 1 122 ? 9.162  -11.006 -2.960 1.00 6.23  ? 121 GLU A CD  1 
ATOM   895  O  OE1 . GLU A 1 122 ? 8.744  -12.158 -2.893 1.00 6.58  ? 121 GLU A OE1 1 
ATOM   896  O  OE2 . GLU A 1 122 ? 8.616  -9.931  -3.177 1.00 7.00  ? 121 GLU A OE2 1 
ATOM   897  N  N   . LYS A 1 123 ? 8.357  -10.036 0.372  1.00 3.39  ? 122 LYS A N   1 
ATOM   898  C  CA  . LYS A 1 123 ? 7.090  -9.334  0.560  1.00 4.17  ? 122 LYS A CA  1 
ATOM   899  C  C   . LYS A 1 123 ? 7.259  -8.350  1.813  1.00 3.34  ? 122 LYS A C   1 
ATOM   900  O  O   . LYS A 1 123 ? 8.109  -8.418  2.715  1.00 4.17  ? 122 LYS A O   1 
ATOM   901  C  CB  . LYS A 1 123 ? 5.909  -10.155 0.891  1.00 3.76  ? 122 LYS A CB  1 
ATOM   902  C  CG  . LYS A 1 123 ? 4.768  -10.031 -0.233 1.00 7.75  ? 122 LYS A CG  1 
ATOM   903  C  CD  . LYS A 1 123 ? 3.437  -10.568 0.327  1.00 8.98  ? 122 LYS A CD  1 
ATOM   904  C  CE  . LYS A 1 123 ? 3.369  -11.999 0.777  1.00 9.86  ? 122 LYS A CE  1 
ATOM   905  N  NZ  . LYS A 1 123 ? 2.133  -12.451 1.437  1.00 10.82 ? 122 LYS A NZ  1 
ATOM   906  N  N   . ALA A 1 124 ? 6.466  -7.367  1.978  1.00 2.01  ? 123 ALA A N   1 
ATOM   907  C  CA  . ALA A 1 124 ? 6.226  -6.300  2.883  1.00 3.19  ? 123 ALA A CA  1 
ATOM   908  C  C   . ALA A 1 124 ? 5.707  -6.876  4.194  1.00 3.72  ? 123 ALA A C   1 
ATOM   909  O  O   . ALA A 1 124 ? 4.681  -7.559  4.098  1.00 3.09  ? 123 ALA A O   1 
ATOM   910  C  CB  . ALA A 1 124 ? 5.218  -5.491  2.096  1.00 5.76  ? 123 ALA A CB  1 
ATOM   911  N  N   . ASP A 1 125 ? 6.277  -6.652  5.343  1.00 5.51  ? 124 ASP A N   1 
ATOM   912  C  CA  . ASP A 1 125 ? 5.764  -7.334  6.621  1.00 7.09  ? 124 ASP A CA  1 
ATOM   913  C  C   . ASP A 1 125 ? 4.475  -7.008  7.237  1.00 6.98  ? 124 ASP A C   1 
ATOM   914  O  O   . ASP A 1 125 ? 4.356  -5.906  7.692  1.00 7.31  ? 124 ASP A O   1 
ATOM   915  C  CB  . ASP A 1 125 ? 6.844  -7.212  7.734  1.00 7.66  ? 124 ASP A CB  1 
ATOM   916  C  CG  . ASP A 1 125 ? 6.881  -8.229  8.846  1.00 7.33  ? 124 ASP A CG  1 
ATOM   917  O  OD1 . ASP A 1 125 ? 5.863  -8.512  9.511  1.00 4.78  ? 124 ASP A OD1 1 
ATOM   918  O  OD2 . ASP A 1 125 ? 8.074  -8.691  8.976  1.00 6.32  ? 124 ASP A OD2 1 
ATOM   919  N  N   . ASP A 1 126 ? 3.681  -8.089  7.168  1.00 7.66  ? 125 ASP A N   1 
ATOM   920  C  CA  . ASP A 1 126 ? 2.303  -7.937  7.748  1.00 9.15  ? 125 ASP A CA  1 
ATOM   921  C  C   . ASP A 1 126 ? 2.148  -7.586  9.236  1.00 6.52  ? 125 ASP A C   1 
ATOM   922  O  O   . ASP A 1 126 ? 0.966  -7.317  9.485  1.00 3.70  ? 125 ASP A O   1 
ATOM   923  C  CB  . ASP A 1 126 ? 1.395  -9.181  7.433  1.00 5.71  ? 125 ASP A CB  1 
ATOM   924  C  CG  . ASP A 1 126 ? 0.366  -8.654  6.366  1.00 5.18  ? 125 ASP A CG  1 
ATOM   925  O  OD1 . ASP A 1 126 ? 0.319  -7.439  5.911  1.00 2.00  ? 125 ASP A OD1 1 
ATOM   926  O  OD2 . ASP A 1 126 ? -0.403 -9.618  6.045  1.00 4.60  ? 125 ASP A OD2 1 
ATOM   927  N  N   . LEU A 1 127 ? 3.113  -7.565  10.052 1.00 5.85  ? 126 LEU A N   1 
ATOM   928  C  CA  . LEU A 1 127 ? 3.464  -7.327  11.405 1.00 5.91  ? 126 LEU A CA  1 
ATOM   929  C  C   . LEU A 1 127 ? 2.566  -7.916  12.511 1.00 7.27  ? 126 LEU A C   1 
ATOM   930  O  O   . LEU A 1 127 ? 2.714  -7.369  13.652 1.00 8.79  ? 126 LEU A O   1 
ATOM   931  C  CB  . LEU A 1 127 ? 3.745  -5.814  11.624 1.00 3.75  ? 126 LEU A CB  1 
ATOM   932  C  CG  . LEU A 1 127 ? 4.649  -5.016  10.728 1.00 2.00  ? 126 LEU A CG  1 
ATOM   933  C  CD1 . LEU A 1 127 ? 5.329  -3.844  11.459 1.00 2.78  ? 126 LEU A CD1 1 
ATOM   934  C  CD2 . LEU A 1 127 ? 5.817  -5.771  10.259 1.00 2.00  ? 126 LEU A CD2 1 
ATOM   935  N  N   . GLY A 1 128 ? 1.747  -8.926  12.206 1.00 8.47  ? 127 GLY A N   1 
ATOM   936  C  CA  . GLY A 1 128 ? 0.892  -9.600  13.183 1.00 7.05  ? 127 GLY A CA  1 
ATOM   937  C  C   . GLY A 1 128 ? -0.578 -9.509  13.034 1.00 7.20  ? 127 GLY A C   1 
ATOM   938  O  O   . GLY A 1 128 ? -1.459 -10.401 13.052 1.00 3.48  ? 127 GLY A O   1 
ATOM   939  N  N   . LYS A 1 129 ? -0.835 -8.235  12.881 1.00 8.26  ? 128 LYS A N   1 
ATOM   940  C  CA  . LYS A 1 129 ? -2.068 -7.520  12.679 1.00 6.04  ? 128 LYS A CA  1 
ATOM   941  C  C   . LYS A 1 129 ? -2.832 -7.992  11.471 1.00 6.37  ? 128 LYS A C   1 
ATOM   942  O  O   . LYS A 1 129 ? -3.952 -7.462  11.334 1.00 5.30  ? 128 LYS A O   1 
ATOM   943  C  CB  . LYS A 1 129 ? -1.603 -6.065  12.590 1.00 6.71  ? 128 LYS A CB  1 
ATOM   944  C  CG  . LYS A 1 129 ? -0.590 -5.521  11.597 1.00 6.83  ? 128 LYS A CG  1 
ATOM   945  C  CD  . LYS A 1 129 ? -1.246 -5.174  10.246 1.00 7.12  ? 128 LYS A CD  1 
ATOM   946  C  CE  . LYS A 1 129 ? -0.446 -4.564  9.132  1.00 6.35  ? 128 LYS A CE  1 
ATOM   947  N  NZ  . LYS A 1 129 ? 0.442  -5.594  8.499  1.00 3.71  ? 128 LYS A NZ  1 
ATOM   948  N  N   . GLY A 1 130 ? -2.303 -8.920  10.657 1.00 6.57  ? 129 GLY A N   1 
ATOM   949  C  CA  . GLY A 1 130 ? -2.827 -9.505  9.437  1.00 6.20  ? 129 GLY A CA  1 
ATOM   950  C  C   . GLY A 1 130 ? -3.842 -10.600 9.297  1.00 6.34  ? 129 GLY A C   1 
ATOM   951  O  O   . GLY A 1 130 ? -4.011 -11.140 8.171  1.00 6.75  ? 129 GLY A O   1 
ATOM   952  N  N   . GLY A 1 131 ? -4.538 -10.997 10.363 1.00 4.89  ? 130 GLY A N   1 
ATOM   953  C  CA  . GLY A 1 131 ? -5.581 -11.928 10.617 1.00 3.86  ? 130 GLY A CA  1 
ATOM   954  C  C   . GLY A 1 131 ? -5.779 -13.140 9.768  1.00 3.78  ? 130 GLY A C   1 
ATOM   955  O  O   . GLY A 1 131 ? -6.736 -13.407 9.010  1.00 2.00  ? 130 GLY A O   1 
ATOM   956  N  N   . ASN A 1 132 ? -4.741 -13.980 9.905  1.00 4.56  ? 131 ASN A N   1 
ATOM   957  C  CA  . ASN A 1 132 ? -4.434 -15.257 9.259  1.00 3.09  ? 131 ASN A CA  1 
ATOM   958  C  C   . ASN A 1 132 ? -3.262 -15.864 10.036 1.00 2.00  ? 131 ASN A C   1 
ATOM   959  O  O   . ASN A 1 132 ? -2.493 -15.234 10.774 1.00 2.00  ? 131 ASN A O   1 
ATOM   960  C  CB  . ASN A 1 132 ? -4.092 -15.148 7.747  1.00 2.00  ? 131 ASN A CB  1 
ATOM   961  C  CG  . ASN A 1 132 ? -2.758 -14.690 7.171  1.00 2.00  ? 131 ASN A CG  1 
ATOM   962  O  OD1 . ASN A 1 132 ? -1.927 -15.587 6.913  1.00 2.09  ? 131 ASN A OD1 1 
ATOM   963  N  ND2 . ASN A 1 132 ? -2.255 -13.519 6.851  1.00 2.00  ? 131 ASN A ND2 1 
ATOM   964  N  N   . GLU A 1 133 ? -3.170 -17.134 9.838  1.00 2.00  ? 132 GLU A N   1 
ATOM   965  C  CA  . GLU A 1 133 ? -2.150 -17.862 10.549 1.00 2.00  ? 132 GLU A CA  1 
ATOM   966  C  C   . GLU A 1 133 ? -0.824 -17.761 9.929  1.00 3.35  ? 132 GLU A C   1 
ATOM   967  O  O   . GLU A 1 133 ? 0.096  -18.075 10.641 1.00 7.16  ? 132 GLU A O   1 
ATOM   968  C  CB  . GLU A 1 133 ? -2.590 -19.314 10.587 1.00 2.31  ? 132 GLU A CB  1 
ATOM   969  C  CG  . GLU A 1 133 ? -2.448 -19.928 11.997 1.00 4.03  ? 132 GLU A CG  1 
ATOM   970  C  CD  . GLU A 1 133 ? -3.735 -20.389 12.621 1.00 4.48  ? 132 GLU A CD  1 
ATOM   971  O  OE1 . GLU A 1 133 ? -4.628 -20.819 11.889 1.00 2.00  ? 132 GLU A OE1 1 
ATOM   972  O  OE2 . GLU A 1 133 ? -3.749 -20.257 13.900 1.00 5.10  ? 132 GLU A OE2 1 
ATOM   973  N  N   . GLU A 1 134 ? -0.707 -17.354 8.707  1.00 5.20  ? 133 GLU A N   1 
ATOM   974  C  CA  . GLU A 1 134 ? 0.519  -17.232 7.951  1.00 5.49  ? 133 GLU A CA  1 
ATOM   975  C  C   . GLU A 1 134 ? 1.152  -15.957 8.371  1.00 4.01  ? 133 GLU A C   1 
ATOM   976  O  O   . GLU A 1 134 ? 2.295  -15.849 7.946  1.00 4.87  ? 133 GLU A O   1 
ATOM   977  C  CB  . GLU A 1 134 ? 0.291  -17.288 6.399  1.00 7.49  ? 133 GLU A CB  1 
ATOM   978  C  CG  . GLU A 1 134 ? 1.465  -18.101 5.700  1.00 7.59  ? 133 GLU A CG  1 
ATOM   979  C  CD  . GLU A 1 134 ? 1.559  -19.481 6.316  1.00 7.35  ? 133 GLU A CD  1 
ATOM   980  O  OE1 . GLU A 1 134 ? 0.637  -20.277 6.172  1.00 5.70  ? 133 GLU A OE1 1 
ATOM   981  O  OE2 . GLU A 1 134 ? 2.536  -19.832 6.976  1.00 8.87  ? 133 GLU A OE2 1 
ATOM   982  N  N   . SER A 1 135 ? 0.393  -15.156 9.118  1.00 2.00  ? 134 SER A N   1 
ATOM   983  C  CA  . SER A 1 135 ? 1.149  -13.896 9.508  1.00 2.40  ? 134 SER A CA  1 
ATOM   984  C  C   . SER A 1 135 ? 1.693  -14.458 10.860 1.00 3.19  ? 134 SER A C   1 
ATOM   985  O  O   . SER A 1 135 ? 2.938  -14.690 10.836 1.00 2.00  ? 134 SER A O   1 
ATOM   986  C  CB  . SER A 1 135 ? 0.378  -12.650 9.479  1.00 2.00  ? 134 SER A CB  1 
ATOM   987  O  OG  . SER A 1 135 ? -0.971 -12.995 8.962  1.00 4.01  ? 134 SER A OG  1 
ATOM   988  N  N   . THR A 1 136 ? 0.884  -14.685 11.909 1.00 2.00  ? 135 THR A N   1 
ATOM   989  C  CA  . THR A 1 136 ? 1.459  -15.229 13.186 1.00 2.43  ? 135 THR A CA  1 
ATOM   990  C  C   . THR A 1 136 ? 2.696  -16.136 12.974 1.00 3.37  ? 135 THR A C   1 
ATOM   991  O  O   . THR A 1 136 ? 3.523  -16.091 13.888 1.00 2.34  ? 135 THR A O   1 
ATOM   992  C  CB  . THR A 1 136 ? 0.551  -15.999 14.193 1.00 2.00  ? 135 THR A CB  1 
ATOM   993  O  OG1 . THR A 1 136 ? -0.411 -16.604 13.333 1.00 2.00  ? 135 THR A OG1 1 
ATOM   994  C  CG2 . THR A 1 136 ? 0.025  -15.059 15.306 1.00 2.85  ? 135 THR A CG2 1 
ATOM   995  N  N   . LYS A 1 137 ? 2.710  -16.861 11.807 1.00 4.76  ? 136 LYS A N   1 
ATOM   996  C  CA  . LYS A 1 137 ? 3.884  -17.708 11.530 1.00 4.96  ? 136 LYS A CA  1 
ATOM   997  C  C   . LYS A 1 137 ? 5.001  -16.669 11.183 1.00 3.62  ? 136 LYS A C   1 
ATOM   998  O  O   . LYS A 1 137 ? 5.865  -16.296 12.016 1.00 5.70  ? 136 LYS A O   1 
ATOM   999  C  CB  . LYS A 1 137 ? 3.743  -18.697 10.453 1.00 4.49  ? 136 LYS A CB  1 
ATOM   1000 C  CG  . LYS A 1 137 ? 2.504  -19.582 10.591 1.00 6.66  ? 136 LYS A CG  1 
ATOM   1001 C  CD  . LYS A 1 137 ? 2.843  -20.974 10.103 1.00 7.98  ? 136 LYS A CD  1 
ATOM   1002 C  CE  . LYS A 1 137 ? 1.697  -21.740 9.587  1.00 10.15 ? 136 LYS A CE  1 
ATOM   1003 N  NZ  . LYS A 1 137 ? 0.855  -21.196 8.509  1.00 8.27  ? 136 LYS A NZ  1 
ATOM   1004 N  N   . THR A 1 138 ? 4.996  -16.134 10.006 1.00 2.42  ? 137 THR A N   1 
ATOM   1005 C  CA  . THR A 1 138 ? 6.054  -15.150 9.644  1.00 2.91  ? 137 THR A CA  1 
ATOM   1006 C  C   . THR A 1 138 ? 5.699  -13.718 9.628  1.00 2.01  ? 137 THR A C   1 
ATOM   1007 O  O   . THR A 1 138 ? 6.444  -12.738 9.933  1.00 2.21  ? 137 THR A O   1 
ATOM   1008 C  CB  . THR A 1 138 ? 6.605  -15.679 8.240  1.00 2.00  ? 137 THR A CB  1 
ATOM   1009 O  OG1 . THR A 1 138 ? 5.541  -15.579 7.254  1.00 2.00  ? 137 THR A OG1 1 
ATOM   1010 C  CG2 . THR A 1 138 ? 7.103  -17.086 8.494  1.00 2.00  ? 137 THR A CG2 1 
ATOM   1011 N  N   . GLY A 1 139 ? 4.497  -13.390 9.261  1.00 2.61  ? 138 GLY A N   1 
ATOM   1012 C  CA  . GLY A 1 139 ? 4.301  -11.885 9.272  1.00 3.36  ? 138 GLY A CA  1 
ATOM   1013 C  C   . GLY A 1 139 ? 4.147  -11.680 7.744  1.00 2.35  ? 138 GLY A C   1 
ATOM   1014 O  O   . GLY A 1 139 ? 4.263  -10.555 7.329  1.00 2.85  ? 138 GLY A O   1 
ATOM   1015 N  N   . ASN A 1 140 ? 3.907  -12.748 7.030  1.00 2.70  ? 139 ASN A N   1 
ATOM   1016 C  CA  . ASN A 1 140 ? 3.673  -12.843 5.617  1.00 3.88  ? 139 ASN A CA  1 
ATOM   1017 C  C   . ASN A 1 140 ? 4.606  -12.413 4.529  1.00 5.69  ? 139 ASN A C   1 
ATOM   1018 O  O   . ASN A 1 140 ? 4.081  -12.547 3.362  1.00 7.29  ? 139 ASN A O   1 
ATOM   1019 C  CB  . ASN A 1 140 ? 2.425  -11.933 5.231  1.00 4.30  ? 139 ASN A CB  1 
ATOM   1020 C  CG  . ASN A 1 140 ? 1.243  -12.790 4.851  1.00 2.00  ? 139 ASN A CG  1 
ATOM   1021 O  OD1 . ASN A 1 140 ? 0.369  -13.121 5.634  1.00 2.00  ? 139 ASN A OD1 1 
ATOM   1022 N  ND2 . ASN A 1 140 ? 1.369  -13.078 3.565  1.00 2.00  ? 139 ASN A ND2 1 
ATOM   1023 N  N   . ALA A 1 141 ? 5.755  -11.992 4.892  1.00 5.81  ? 140 ALA A N   1 
ATOM   1024 C  CA  . ALA A 1 141 ? 6.826  -11.501 4.040  1.00 4.59  ? 140 ALA A CA  1 
ATOM   1025 C  C   . ALA A 1 141 ? 7.530  -12.318 2.998  1.00 7.18  ? 140 ALA A C   1 
ATOM   1026 O  O   . ALA A 1 141 ? 8.797  -12.280 2.914  1.00 7.76  ? 140 ALA A O   1 
ATOM   1027 C  CB  . ALA A 1 141 ? 7.828  -10.981 5.094  1.00 5.21  ? 140 ALA A CB  1 
ATOM   1028 N  N   . GLY A 1 142 ? 6.855  -13.075 2.140  1.00 7.93  ? 141 GLY A N   1 
ATOM   1029 C  CA  . GLY A 1 142 ? 7.267  -13.899 1.050  1.00 7.39  ? 141 GLY A CA  1 
ATOM   1030 C  C   . GLY A 1 142 ? 8.643  -14.442 0.945  1.00 7.83  ? 141 GLY A C   1 
ATOM   1031 O  O   . GLY A 1 142 ? 8.987  -15.249 1.840  1.00 9.16  ? 141 GLY A O   1 
ATOM   1032 N  N   . SER A 1 143 ? 9.531  -14.136 0.025  1.00 8.72  ? 142 SER A N   1 
ATOM   1033 C  CA  . SER A 1 143 ? 10.877 -14.761 0.029  1.00 9.28  ? 142 SER A CA  1 
ATOM   1034 C  C   . SER A 1 143 ? 11.743 -14.189 1.153  1.00 10.31 ? 142 SER A C   1 
ATOM   1035 O  O   . SER A 1 143 ? 11.412 -13.238 1.898  1.00 11.37 ? 142 SER A O   1 
ATOM   1036 C  CB  . SER A 1 143 ? 11.642 -14.583 -1.236 1.00 10.29 ? 142 SER A CB  1 
ATOM   1037 O  OG  . SER A 1 143 ? 10.974 -14.500 -2.486 1.00 13.80 ? 142 SER A OG  1 
ATOM   1038 N  N   . ARG A 1 144 ? 12.907 -14.834 1.269  1.00 9.00  ? 143 ARG A N   1 
ATOM   1039 C  CA  . ARG A 1 144 ? 14.095 -14.746 2.077  1.00 5.20  ? 143 ARG A CA  1 
ATOM   1040 C  C   . ARG A 1 144 ? 14.942 -14.180 0.888  1.00 6.74  ? 143 ARG A C   1 
ATOM   1041 O  O   . ARG A 1 144 ? 15.442 -15.069 0.109  1.00 4.60  ? 143 ARG A O   1 
ATOM   1042 C  CB  . ARG A 1 144 ? 14.592 -16.027 2.491  1.00 4.78  ? 143 ARG A CB  1 
ATOM   1043 C  CG  . ARG A 1 144 ? 15.100 -16.365 3.824  1.00 4.29  ? 143 ARG A CG  1 
ATOM   1044 C  CD  . ARG A 1 144 ? 13.958 -16.639 4.710  1.00 4.44  ? 143 ARG A CD  1 
ATOM   1045 N  NE  . ARG A 1 144 ? 13.427 -17.948 4.853  1.00 2.00  ? 143 ARG A NE  1 
ATOM   1046 C  CZ  . ARG A 1 144 ? 13.753 -18.704 5.921  1.00 3.64  ? 143 ARG A CZ  1 
ATOM   1047 N  NH1 . ARG A 1 144 ? 14.544 -18.111 6.813  1.00 2.00  ? 143 ARG A NH1 1 
ATOM   1048 N  NH2 . ARG A 1 144 ? 13.287 -20.008 6.108  1.00 3.18  ? 143 ARG A NH2 1 
ATOM   1049 N  N   . LEU A 1 145 ? 15.102 -12.849 0.670  1.00 6.90  ? 144 LEU A N   1 
ATOM   1050 C  CA  . LEU A 1 145 ? 15.925 -12.563 -0.581 1.00 8.18  ? 144 LEU A CA  1 
ATOM   1051 C  C   . LEU A 1 145 ? 17.410 -12.485 -0.283 1.00 9.38  ? 144 LEU A C   1 
ATOM   1052 O  O   . LEU A 1 145 ? 18.224 -12.786 -1.201 1.00 11.40 ? 144 LEU A O   1 
ATOM   1053 C  CB  . LEU A 1 145 ? 15.518 -11.316 -1.356 1.00 6.99  ? 144 LEU A CB  1 
ATOM   1054 C  CG  . LEU A 1 145 ? 14.254 -10.502 -1.163 1.00 5.72  ? 144 LEU A CG  1 
ATOM   1055 C  CD1 . LEU A 1 145 ? 14.472 -9.488  -0.047 1.00 2.96  ? 144 LEU A CD1 1 
ATOM   1056 C  CD2 . LEU A 1 145 ? 13.866 -9.776  -2.489 1.00 5.25  ? 144 LEU A CD2 1 
ATOM   1057 N  N   . ALA A 1 146 ? 17.780 -12.063 0.951  1.00 7.39  ? 145 ALA A N   1 
ATOM   1058 C  CA  . ALA A 1 146 ? 19.248 -12.063 1.081  1.00 4.13  ? 145 ALA A CA  1 
ATOM   1059 C  C   . ALA A 1 146 ? 19.426 -12.462 2.528  1.00 5.51  ? 145 ALA A C   1 
ATOM   1060 O  O   . ALA A 1 146 ? 18.550 -12.115 3.369  1.00 2.61  ? 145 ALA A O   1 
ATOM   1061 C  CB  . ALA A 1 146 ? 19.922 -10.816 0.797  1.00 4.19  ? 145 ALA A CB  1 
ATOM   1062 N  N   . CYS A 1 147 ? 20.613 -13.166 2.588  1.00 7.18  ? 146 CYS A N   1 
ATOM   1063 C  CA  . CYS A 1 147 ? 20.777 -13.560 4.063  1.00 7.39  ? 146 CYS A CA  1 
ATOM   1064 C  C   . CYS A 1 147 ? 22.285 -13.756 4.269  1.00 6.03  ? 146 CYS A C   1 
ATOM   1065 O  O   . CYS A 1 147 ? 22.920 -13.880 3.168  1.00 5.04  ? 146 CYS A O   1 
ATOM   1066 C  CB  . CYS A 1 147 ? 19.871 -14.730 4.430  1.00 5.62  ? 146 CYS A CB  1 
ATOM   1067 S  SG  . CYS A 1 147 ? 20.019 -16.333 3.667  1.00 6.29  ? 146 CYS A SG  1 
ATOM   1068 N  N   . GLY A 1 148 ? 22.472 -13.689 5.600  1.00 2.83  ? 147 GLY A N   1 
ATOM   1069 C  CA  . GLY A 1 148 ? 23.892 -13.877 6.053  1.00 2.55  ? 147 GLY A CA  1 
ATOM   1070 C  C   . GLY A 1 148 ? 23.939 -14.179 7.598  1.00 4.54  ? 147 GLY A C   1 
ATOM   1071 O  O   . GLY A 1 148 ? 22.982 -13.913 8.389  1.00 2.00  ? 147 GLY A O   1 
ATOM   1072 N  N   . VAL A 1 149 ? 25.118 -14.737 7.961  1.00 3.90  ? 148 VAL A N   1 
ATOM   1073 C  CA  . VAL A 1 149 ? 25.305 -15.066 9.347  1.00 3.84  ? 148 VAL A CA  1 
ATOM   1074 C  C   . VAL A 1 149 ? 25.845 -13.883 10.192 1.00 5.45  ? 148 VAL A C   1 
ATOM   1075 O  O   . VAL A 1 149 ? 26.786 -13.114 9.880  1.00 7.22  ? 148 VAL A O   1 
ATOM   1076 C  CB  . VAL A 1 149 ? 26.237 -16.313 9.503  1.00 2.00  ? 148 VAL A CB  1 
ATOM   1077 C  CG1 . VAL A 1 149 ? 26.430 -16.713 10.967 1.00 2.00  ? 148 VAL A CG1 1 
ATOM   1078 C  CG2 . VAL A 1 149 ? 25.695 -17.452 8.710  1.00 3.35  ? 148 VAL A CG2 1 
ATOM   1079 N  N   . ILE A 1 150 ? 25.215 -13.745 11.353 1.00 7.00  ? 149 ILE A N   1 
ATOM   1080 C  CA  . ILE A 1 150 ? 25.678 -12.666 12.238 1.00 9.27  ? 149 ILE A CA  1 
ATOM   1081 C  C   . ILE A 1 150 ? 26.935 -13.260 12.870 1.00 7.50  ? 149 ILE A C   1 
ATOM   1082 O  O   . ILE A 1 150 ? 27.084 -14.039 13.808 1.00 3.74  ? 149 ILE A O   1 
ATOM   1083 C  CB  . ILE A 1 150 ? 24.430 -12.190 13.110 1.00 12.15 ? 149 ILE A CB  1 
ATOM   1084 C  CG1 . ILE A 1 150 ? 23.856 -10.891 12.387 1.00 13.06 ? 149 ILE A CG1 1 
ATOM   1085 C  CG2 . ILE A 1 150 ? 24.554 -11.995 14.663 1.00 11.12 ? 149 ILE A CG2 1 
ATOM   1086 C  CD1 . ILE A 1 150 ? 22.565 -11.182 11.556 1.00 10.40 ? 149 ILE A CD1 1 
ATOM   1087 N  N   . GLY A 1 151 ? 28.022 -12.750 12.250 1.00 8.45  ? 150 GLY A N   1 
ATOM   1088 C  CA  . GLY A 1 151 ? 29.409 -13.168 12.717 1.00 8.59  ? 150 GLY A CA  1 
ATOM   1089 C  C   . GLY A 1 151 ? 29.997 -12.144 13.757 1.00 7.26  ? 150 GLY A C   1 
ATOM   1090 O  O   . GLY A 1 151 ? 29.341 -11.503 14.614 1.00 5.67  ? 150 GLY A O   1 
ATOM   1091 N  N   . ILE A 1 152 ? 31.394 -11.979 13.615 1.00 6.47  ? 151 ILE A N   1 
ATOM   1092 C  CA  . ILE A 1 152 ? 32.011 -10.989 14.583 1.00 6.96  ? 151 ILE A CA  1 
ATOM   1093 C  C   . ILE A 1 152 ? 32.986 -9.967  13.956 1.00 6.68  ? 151 ILE A C   1 
ATOM   1094 O  O   . ILE A 1 152 ? 34.128 -10.402 13.771 1.00 10.15 ? 151 ILE A O   1 
ATOM   1095 C  CB  . ILE A 1 152 ? 32.643 -11.704 15.824 1.00 3.25  ? 151 ILE A CB  1 
ATOM   1096 C  CG1 . ILE A 1 152 ? 31.516 -12.305 16.653 1.00 2.00  ? 151 ILE A CG1 1 
ATOM   1097 C  CG2 . ILE A 1 152 ? 33.527 -10.667 16.593 1.00 2.28  ? 151 ILE A CG2 1 
ATOM   1098 C  CD1 . ILE A 1 152 ? 32.015 -12.888 18.021 1.00 2.00  ? 151 ILE A CD1 1 
ATOM   1099 N  N   . ALA A 1 153 ? 32.696 -8.725  13.672 1.00 6.08  ? 152 ALA A N   1 
ATOM   1100 C  CA  . ALA A 1 153 ? 33.697 -7.813  13.094 1.00 8.76  ? 152 ALA A CA  1 
ATOM   1101 C  C   . ALA A 1 153 ? 34.580 -7.285  14.279 1.00 10.71 ? 152 ALA A C   1 
ATOM   1102 O  O   . ALA A 1 153 ? 35.075 -7.940  15.224 1.00 7.69  ? 152 ALA A O   1 
ATOM   1103 C  CB  . ALA A 1 153 ? 33.210 -6.642  12.322 1.00 8.04  ? 152 ALA A CB  1 
ATOM   1104 N  N   . GLN A 1 154 ? 34.827 -5.986  14.194 1.00 13.85 ? 153 GLN A N   1 
ATOM   1105 C  CA  . GLN A 1 154 ? 35.661 -5.182  15.155 1.00 15.46 ? 153 GLN A CA  1 
ATOM   1106 C  C   . GLN A 1 154 ? 35.020 -3.790  15.120 1.00 17.10 ? 153 GLN A C   1 
ATOM   1107 O  O   . GLN A 1 154 ? 34.656 -3.333  16.226 1.00 14.88 ? 153 GLN A O   1 
ATOM   1108 C  CB  . GLN A 1 154 ? 37.134 -5.327  14.755 1.00 14.79 ? 153 GLN A CB  1 
ATOM   1109 C  CG  . GLN A 1 154 ? 37.461 -4.771  13.353 1.00 15.32 ? 153 GLN A CG  1 
ATOM   1110 C  CD  . GLN A 1 154 ? 36.746 -5.265  12.112 1.00 15.95 ? 153 GLN A CD  1 
ATOM   1111 O  OE1 . GLN A 1 154 ? 37.320 -6.070  11.354 1.00 13.16 ? 153 GLN A OE1 1 
ATOM   1112 N  NE2 . GLN A 1 154 ? 35.469 -4.845  11.779 1.00 15.31 ? 153 GLN A NE2 1 
ATOM   1113 O  OXT . GLN A 1 154 ? 34.902 -3.254  13.947 1.00 16.96 ? 153 GLN A OXT 1 
HETATM 1114 C  C   . ACE B 1 1   ? 24.242 -27.617 24.751 1.00 3.76  ? 0   ACE B C   1 
HETATM 1115 O  O   . ACE B 1 1   ? 23.844 -26.917 24.414 1.00 2.00  ? 0   ACE B O   1 
HETATM 1116 C  CH3 . ACE B 1 1   ? 24.750 -28.282 25.261 1.00 2.00  ? 0   ACE B CH3 1 
ATOM   1117 N  N   . ALA B 1 2   ? 24.246 -29.330 24.193 1.00 5.04  ? 1   ALA B N   1 
ATOM   1118 C  CA  . ALA B 1 2   ? 23.426 -29.689 23.036 1.00 4.13  ? 1   ALA B CA  1 
ATOM   1119 C  C   . ALA B 1 2   ? 23.569 -28.663 21.892 1.00 6.15  ? 1   ALA B C   1 
ATOM   1120 O  O   . ALA B 1 2   ? 22.615 -28.296 21.122 1.00 3.52  ? 1   ALA B O   1 
ATOM   1121 C  CB  . ALA B 1 2   ? 21.942 -29.734 23.378 1.00 3.38  ? 1   ALA B CB  1 
ATOM   1122 N  N   . THR B 1 3   ? 24.844 -28.276 21.949 1.00 4.24  ? 2   THR B N   1 
ATOM   1123 C  CA  . THR B 1 3   ? 25.375 -27.254 21.013 1.00 5.34  ? 2   THR B CA  1 
ATOM   1124 C  C   . THR B 1 3   ? 25.698 -28.032 19.810 1.00 5.03  ? 2   THR B C   1 
ATOM   1125 O  O   . THR B 1 3   ? 25.954 -29.246 19.867 1.00 3.64  ? 2   THR B O   1 
ATOM   1126 C  CB  . THR B 1 3   ? 26.373 -26.453 22.002 1.00 7.71  ? 2   THR B CB  1 
ATOM   1127 O  OG1 . THR B 1 3   ? 26.781 -27.324 23.121 1.00 5.45  ? 2   THR B OG1 1 
ATOM   1128 C  CG2 . THR B 1 3   ? 25.769 -25.146 22.523 1.00 5.38  ? 2   THR B CG2 1 
ATOM   1129 N  N   . LYS B 1 4   ? 25.719 -27.434 18.644 1.00 7.41  ? 3   LYS B N   1 
ATOM   1130 C  CA  . LYS B 1 4   ? 25.909 -27.726 17.284 1.00 5.71  ? 3   LYS B CA  1 
ATOM   1131 C  C   . LYS B 1 4   ? 26.378 -26.562 16.386 1.00 6.46  ? 3   LYS B C   1 
ATOM   1132 O  O   . LYS B 1 4   ? 26.092 -25.401 16.723 1.00 2.00  ? 3   LYS B O   1 
ATOM   1133 C  CB  . LYS B 1 4   ? 24.442 -28.139 16.905 1.00 5.53  ? 3   LYS B CB  1 
ATOM   1134 C  CG  . LYS B 1 4   ? 23.993 -29.479 17.530 1.00 7.22  ? 3   LYS B CG  1 
ATOM   1135 C  CD  . LYS B 1 4   ? 22.502 -29.767 17.392 1.00 9.03  ? 3   LYS B CD  1 
ATOM   1136 C  CE  . LYS B 1 4   ? 21.972 -31.210 17.399 1.00 8.68  ? 3   LYS B CE  1 
ATOM   1137 N  NZ  . LYS B 1 4   ? 22.612 -31.917 16.246 1.00 10.30 ? 3   LYS B NZ  1 
ATOM   1138 N  N   . ALA B 1 5   ? 27.128 -26.933 15.262 1.00 7.19  ? 4   ALA B N   1 
ATOM   1139 C  CA  . ALA B 1 5   ? 27.485 -25.711 14.494 1.00 10.42 ? 4   ALA B CA  1 
ATOM   1140 C  C   . ALA B 1 5   ? 27.770 -25.915 13.024 1.00 9.48  ? 4   ALA B C   1 
ATOM   1141 O  O   . ALA B 1 5   ? 28.178 -27.176 12.847 1.00 8.65  ? 4   ALA B O   1 
ATOM   1142 C  CB  . ALA B 1 5   ? 28.778 -24.991 15.127 1.00 10.45 ? 4   ALA B CB  1 
ATOM   1143 N  N   . VAL B 1 6   ? 27.566 -24.755 12.310 1.00 5.64  ? 5   VAL B N   1 
ATOM   1144 C  CA  . VAL B 1 6   ? 27.939 -25.228 10.860 1.00 5.28  ? 5   VAL B CA  1 
ATOM   1145 C  C   . VAL B 1 6   ? 28.821 -24.108 10.197 1.00 5.22  ? 5   VAL B C   1 
ATOM   1146 O  O   . VAL B 1 6   ? 28.809 -22.927 10.765 1.00 8.20  ? 5   VAL B O   1 
ATOM   1147 C  CB  . VAL B 1 6   ? 26.942 -25.604 9.804  1.00 5.48  ? 5   VAL B CB  1 
ATOM   1148 C  CG1 . VAL B 1 6   ? 26.785 -24.662 8.514  1.00 3.91  ? 5   VAL B CG1 1 
ATOM   1149 C  CG2 . VAL B 1 6   ? 27.112 -26.946 9.028  1.00 4.37  ? 5   VAL B CG2 1 
ATOM   1150 N  N   . CYS B 1 7   ? 29.484 -24.594 9.111  1.00 4.79  ? 6   CYS B N   1 
ATOM   1151 C  CA  . CYS B 1 7   ? 30.291 -23.722 8.318  1.00 2.40  ? 6   CYS B CA  1 
ATOM   1152 C  C   . CYS B 1 7   ? 30.580 -24.197 6.850  1.00 4.15  ? 6   CYS B C   1 
ATOM   1153 O  O   . CYS B 1 7   ? 31.385 -25.091 6.377  1.00 2.00  ? 6   CYS B O   1 
ATOM   1154 C  CB  . CYS B 1 7   ? 31.704 -23.342 8.828  1.00 2.67  ? 6   CYS B CB  1 
ATOM   1155 S  SG  . CYS B 1 7   ? 32.432 -22.204 7.517  1.00 2.00  ? 6   CYS B SG  1 
ATOM   1156 N  N   . VAL B 1 8   ? 29.874 -23.432 6.050  1.00 3.67  ? 7   VAL B N   1 
ATOM   1157 C  CA  . VAL B 1 8   ? 29.814 -23.410 4.518  1.00 4.08  ? 7   VAL B CA  1 
ATOM   1158 C  C   . VAL B 1 8   ? 31.044 -22.460 4.374  1.00 7.22  ? 7   VAL B C   1 
ATOM   1159 O  O   . VAL B 1 8   ? 31.186 -21.240 4.700  1.00 6.35  ? 7   VAL B O   1 
ATOM   1160 C  CB  . VAL B 1 8   ? 28.463 -23.002 4.007  1.00 2.00  ? 7   VAL B CB  1 
ATOM   1161 C  CG1 . VAL B 1 8   ? 28.447 -21.898 3.002  1.00 2.00  ? 7   VAL B CG1 1 
ATOM   1162 C  CG2 . VAL B 1 8   ? 27.680 -24.221 3.414  1.00 2.00  ? 7   VAL B CG2 1 
ATOM   1163 N  N   . LEU B 1 9   ? 32.065 -23.087 3.873  1.00 9.25  ? 8   LEU B N   1 
ATOM   1164 C  CA  . LEU B 1 9   ? 33.328 -22.550 3.616  1.00 12.89 ? 8   LEU B CA  1 
ATOM   1165 C  C   . LEU B 1 9   ? 33.251 -22.051 2.177  1.00 13.92 ? 8   LEU B C   1 
ATOM   1166 O  O   . LEU B 1 9   ? 33.617 -22.789 1.267  1.00 16.60 ? 8   LEU B O   1 
ATOM   1167 C  CB  . LEU B 1 9   ? 34.412 -23.630 3.793  1.00 14.34 ? 8   LEU B CB  1 
ATOM   1168 C  CG  . LEU B 1 9   ? 35.888 -23.313 3.451  1.00 15.38 ? 8   LEU B CG  1 
ATOM   1169 C  CD1 . LEU B 1 9   ? 36.739 -22.905 4.619  1.00 13.41 ? 8   LEU B CD1 1 
ATOM   1170 C  CD2 . LEU B 1 9   ? 36.391 -24.616 2.826  1.00 14.71 ? 8   LEU B CD2 1 
ATOM   1171 N  N   . LYS B 1 10  ? 32.805 -20.842 1.953  1.00 14.75 ? 9   LYS B N   1 
ATOM   1172 C  CA  . LYS B 1 10  ? 32.744 -20.254 0.604  1.00 13.22 ? 9   LYS B CA  1 
ATOM   1173 C  C   . LYS B 1 10  ? 33.866 -19.186 0.500  1.00 10.89 ? 9   LYS B C   1 
ATOM   1174 O  O   . LYS B 1 10  ? 34.223 -18.321 1.281  1.00 11.40 ? 9   LYS B O   1 
ATOM   1175 C  CB  . LYS B 1 10  ? 31.486 -19.560 0.227  1.00 14.30 ? 9   LYS B CB  1 
ATOM   1176 C  CG  . LYS B 1 10  ? 30.367 -20.479 -0.116 1.00 15.25 ? 9   LYS B CG  1 
ATOM   1177 C  CD  . LYS B 1 10  ? 30.408 -21.198 -1.432 1.00 15.13 ? 9   LYS B CD  1 
ATOM   1178 C  CE  . LYS B 1 10  ? 30.082 -20.217 -2.582 1.00 14.62 ? 9   LYS B CE  1 
ATOM   1179 N  NZ  . LYS B 1 10  ? 31.370 -19.463 -2.776 1.00 15.11 ? 9   LYS B NZ  1 
ATOM   1180 N  N   . GLY B 1 11  ? 34.508 -19.262 -0.597 1.00 10.27 ? 10  GLY B N   1 
ATOM   1181 C  CA  . GLY B 1 11  ? 35.582 -18.507 -1.133 1.00 8.39  ? 10  GLY B CA  1 
ATOM   1182 C  C   . GLY B 1 11  ? 35.150 -18.202 -2.632 1.00 9.57  ? 10  GLY B C   1 
ATOM   1183 O  O   . GLY B 1 11  ? 34.107 -18.719 -3.105 1.00 4.94  ? 10  GLY B O   1 
ATOM   1184 N  N   . ASP B 1 12  ? 36.074 -17.352 -3.177 1.00 7.82  ? 11  ASP B N   1 
ATOM   1185 C  CA  . ASP B 1 12  ? 35.770 -16.971 -4.554 1.00 9.46  ? 11  ASP B CA  1 
ATOM   1186 C  C   . ASP B 1 12  ? 36.740 -17.511 -5.625 1.00 9.70  ? 11  ASP B C   1 
ATOM   1187 O  O   . ASP B 1 12  ? 36.969 -17.044 -6.798 1.00 10.10 ? 11  ASP B O   1 
ATOM   1188 C  CB  . ASP B 1 12  ? 35.466 -15.475 -4.422 1.00 8.02  ? 11  ASP B CB  1 
ATOM   1189 C  CG  . ASP B 1 12  ? 36.682 -14.651 -4.078 1.00 10.17 ? 11  ASP B CG  1 
ATOM   1190 O  OD1 . ASP B 1 12  ? 37.064 -14.717 -2.836 1.00 11.19 ? 11  ASP B OD1 1 
ATOM   1191 O  OD2 . ASP B 1 12  ? 37.173 -14.004 -5.039 1.00 6.17  ? 11  ASP B OD2 1 
ATOM   1192 N  N   . GLY B 1 13  ? 37.304 -18.635 -5.185 1.00 8.79  ? 12  GLY B N   1 
ATOM   1193 C  CA  . GLY B 1 13  ? 38.205 -19.418 -6.133 1.00 6.93  ? 12  GLY B CA  1 
ATOM   1194 C  C   . GLY B 1 13  ? 37.125 -20.630 -6.279 1.00 6.70  ? 12  GLY B C   1 
ATOM   1195 O  O   . GLY B 1 13  ? 36.004 -20.507 -5.750 1.00 4.80  ? 12  GLY B O   1 
ATOM   1196 N  N   . PRO B 1 14  ? 37.456 -21.744 -6.927 1.00 5.87  ? 13  PRO B N   1 
ATOM   1197 C  CA  . PRO B 1 14  ? 36.536 -22.914 -7.073 1.00 6.39  ? 13  PRO B CA  1 
ATOM   1198 C  C   . PRO B 1 14  ? 36.718 -23.534 -5.733 1.00 7.52  ? 13  PRO B C   1 
ATOM   1199 O  O   . PRO B 1 14  ? 37.705 -24.381 -5.868 1.00 11.77 ? 13  PRO B O   1 
ATOM   1200 C  CB  . PRO B 1 14  ? 37.111 -23.715 -8.201 1.00 6.62  ? 13  PRO B CB  1 
ATOM   1201 C  CG  . PRO B 1 14  ? 38.625 -23.375 -8.181 1.00 6.65  ? 13  PRO B CG  1 
ATOM   1202 C  CD  . PRO B 1 14  ? 38.738 -21.994 -7.588 1.00 4.87  ? 13  PRO B CD  1 
ATOM   1203 N  N   . VAL B 1 15  ? 36.082 -23.294 -4.563 1.00 4.47  ? 14  VAL B N   1 
ATOM   1204 C  CA  . VAL B 1 15  ? 36.751 -24.158 -3.509 1.00 5.11  ? 14  VAL B CA  1 
ATOM   1205 C  C   . VAL B 1 15  ? 35.949 -24.726 -2.487 1.00 3.69  ? 14  VAL B C   1 
ATOM   1206 O  O   . VAL B 1 15  ? 36.022 -25.570 -1.621 1.00 2.44  ? 14  VAL B O   1 
ATOM   1207 C  CB  . VAL B 1 15  ? 37.880 -23.142 -3.023 1.00 6.90  ? 14  VAL B CB  1 
ATOM   1208 C  CG1 . VAL B 1 15  ? 37.366 -21.688 -2.856 1.00 8.46  ? 14  VAL B CG1 1 
ATOM   1209 C  CG2 . VAL B 1 15  ? 38.535 -23.795 -1.840 1.00 5.70  ? 14  VAL B CG2 1 
ATOM   1210 N  N   . GLN B 1 16  ? 34.829 -24.613 -2.453 1.00 3.31  ? 15  GLN B N   1 
ATOM   1211 C  CA  . GLN B 1 16  ? 33.384 -24.637 -1.930 1.00 2.00  ? 15  GLN B CA  1 
ATOM   1212 C  C   . GLN B 1 16  ? 33.329 -25.857 -0.986 1.00 2.00  ? 15  GLN B C   1 
ATOM   1213 O  O   . GLN B 1 16  ? 33.481 -27.126 -1.218 1.00 2.00  ? 15  GLN B O   1 
ATOM   1214 C  CB  . GLN B 1 16  ? 32.434 -24.496 -3.085 1.00 2.78  ? 15  GLN B CB  1 
ATOM   1215 C  CG  . GLN B 1 16  ? 31.666 -23.257 -3.638 1.00 2.00  ? 15  GLN B CG  1 
ATOM   1216 C  CD  . GLN B 1 16  ? 32.411 -21.998 -3.988 1.00 3.17  ? 15  GLN B CD  1 
ATOM   1217 O  OE1 . GLN B 1 16  ? 33.076 -21.291 -3.170 1.00 2.00  ? 15  GLN B OE1 1 
ATOM   1218 N  NE2 . GLN B 1 16  ? 32.287 -21.696 -5.335 1.00 3.81  ? 15  GLN B NE2 1 
ATOM   1219 N  N   . GLY B 1 17  ? 33.186 -25.446 0.282  1.00 2.00  ? 16  GLY B N   1 
ATOM   1220 C  CA  . GLY B 1 17  ? 33.108 -26.370 1.422  1.00 7.78  ? 16  GLY B CA  1 
ATOM   1221 C  C   . GLY B 1 17  ? 31.980 -26.422 2.472  1.00 6.84  ? 16  GLY B C   1 
ATOM   1222 O  O   . GLY B 1 17  ? 31.269 -25.398 2.629  1.00 5.62  ? 16  GLY B O   1 
ATOM   1223 N  N   . ILE B 1 18  ? 31.844 -27.602 3.130  1.00 7.20  ? 17  ILE B N   1 
ATOM   1224 C  CA  . ILE B 1 18  ? 30.737 -27.728 4.252  1.00 7.83  ? 17  ILE B CA  1 
ATOM   1225 C  C   . ILE B 1 18  ? 31.499 -28.249 5.435  1.00 7.22  ? 17  ILE B C   1 
ATOM   1226 O  O   . ILE B 1 18  ? 32.336 -29.168 5.120  1.00 6.97  ? 17  ILE B O   1 
ATOM   1227 C  CB  . ILE B 1 18  ? 29.496 -28.451 3.655  1.00 7.43  ? 17  ILE B CB  1 
ATOM   1228 C  CG1 . ILE B 1 18  ? 28.342 -28.753 4.668  1.00 6.56  ? 17  ILE B CG1 1 
ATOM   1229 C  CG2 . ILE B 1 18  ? 29.910 -29.725 2.892  1.00 9.79  ? 17  ILE B CG2 1 
ATOM   1230 C  CD1 . ILE B 1 18  ? 27.167 -27.619 4.659  1.00 2.11  ? 17  ILE B CD1 1 
ATOM   1231 N  N   . ILE B 1 19  ? 31.417 -27.852 6.682  1.00 7.81  ? 18  ILE B N   1 
ATOM   1232 C  CA  . ILE B 1 19  ? 32.267 -28.361 7.803  1.00 10.16 ? 18  ILE B CA  1 
ATOM   1233 C  C   . ILE B 1 19  ? 31.694 -28.022 9.186  1.00 10.48 ? 18  ILE B C   1 
ATOM   1234 O  O   . ILE B 1 19  ? 31.412 -26.808 9.472  1.00 10.88 ? 18  ILE B O   1 
ATOM   1235 C  CB  . ILE B 1 19  ? 33.802 -27.886 7.569  1.00 10.72 ? 18  ILE B CB  1 
ATOM   1236 C  CG1 . ILE B 1 19  ? 34.727 -28.805 8.439  1.00 9.40  ? 18  ILE B CG1 1 
ATOM   1237 C  CG2 . ILE B 1 19  ? 34.432 -26.506 7.928  1.00 9.52  ? 18  ILE B CG2 1 
ATOM   1238 C  CD1 . ILE B 1 19  ? 36.053 -28.933 7.662  1.00 8.53  ? 18  ILE B CD1 1 
ATOM   1239 N  N   . ASN B 1 20  ? 31.530 -29.110 10.012 1.00 7.73  ? 19  ASN B N   1 
ATOM   1240 C  CA  . ASN B 1 20  ? 30.912 -28.904 11.295 1.00 7.56  ? 19  ASN B CA  1 
ATOM   1241 C  C   . ASN B 1 20  ? 31.500 -29.460 12.579 1.00 5.76  ? 19  ASN B C   1 
ATOM   1242 O  O   . ASN B 1 20  ? 32.243 -30.449 12.523 1.00 3.02  ? 19  ASN B O   1 
ATOM   1243 C  CB  . ASN B 1 20  ? 29.380 -29.361 11.052 1.00 7.48  ? 19  ASN B CB  1 
ATOM   1244 C  CG  . ASN B 1 20  ? 28.818 -30.197 12.234 1.00 9.28  ? 19  ASN B CG  1 
ATOM   1245 O  OD1 . ASN B 1 20  ? 28.263 -29.740 13.303 1.00 7.88  ? 19  ASN B OD1 1 
ATOM   1246 N  ND2 . ASN B 1 20  ? 29.032 -31.515 11.934 1.00 6.79  ? 19  ASN B ND2 1 
ATOM   1247 N  N   . PHE B 1 21  ? 30.930 -28.584 13.542 1.00 4.80  ? 20  PHE B N   1 
ATOM   1248 C  CA  . PHE B 1 21  ? 31.403 -28.867 14.985 1.00 4.09  ? 20  PHE B CA  1 
ATOM   1249 C  C   . PHE B 1 21  ? 30.509 -29.473 16.034 1.00 3.14  ? 20  PHE B C   1 
ATOM   1250 O  O   . PHE B 1 21  ? 29.645 -28.616 16.517 1.00 2.68  ? 20  PHE B O   1 
ATOM   1251 C  CB  . PHE B 1 21  ? 31.686 -27.461 15.459 1.00 4.92  ? 20  PHE B CB  1 
ATOM   1252 C  CG  . PHE B 1 21  ? 32.816 -26.724 14.862 1.00 8.99  ? 20  PHE B CG  1 
ATOM   1253 C  CD1 . PHE B 1 21  ? 32.628 -25.981 13.685 1.00 10.68 ? 20  PHE B CD1 1 
ATOM   1254 C  CD2 . PHE B 1 21  ? 34.112 -26.738 15.489 1.00 8.42  ? 20  PHE B CD2 1 
ATOM   1255 C  CE1 . PHE B 1 21  ? 33.709 -25.257 13.109 1.00 10.00 ? 20  PHE B CE1 1 
ATOM   1256 C  CE2 . PHE B 1 21  ? 35.152 -26.031 14.938 1.00 7.72  ? 20  PHE B CE2 1 
ATOM   1257 C  CZ  . PHE B 1 21  ? 34.943 -25.308 13.761 1.00 8.57  ? 20  PHE B CZ  1 
ATOM   1258 N  N   . GLU B 1 22  ? 30.712 -30.776 16.266 1.00 2.94  ? 21  GLU B N   1 
ATOM   1259 C  CA  . GLU B 1 22  ? 29.801 -31.426 17.339 1.00 5.13  ? 21  GLU B CA  1 
ATOM   1260 C  C   . GLU B 1 22  ? 30.532 -31.375 18.685 1.00 5.94  ? 21  GLU B C   1 
ATOM   1261 O  O   . GLU B 1 22  ? 31.769 -31.315 18.456 1.00 9.97  ? 21  GLU B O   1 
ATOM   1262 C  CB  . GLU B 1 22  ? 29.313 -32.873 17.349 1.00 3.37  ? 21  GLU B CB  1 
ATOM   1263 C  CG  . GLU B 1 22  ? 28.003 -32.936 16.472 1.00 3.48  ? 21  GLU B CG  1 
ATOM   1264 C  CD  . GLU B 1 22  ? 28.309 -33.112 14.997 1.00 3.70  ? 21  GLU B CD  1 
ATOM   1265 O  OE1 . GLU B 1 22  ? 29.438 -33.264 14.546 1.00 2.69  ? 21  GLU B OE1 1 
ATOM   1266 O  OE2 . GLU B 1 22  ? 27.318 -33.108 14.241 1.00 2.96  ? 21  GLU B OE2 1 
ATOM   1267 N  N   . GLN B 1 23  ? 30.050 -31.345 19.906 1.00 6.33  ? 22  GLN B N   1 
ATOM   1268 C  CA  . GLN B 1 23  ? 30.851 -31.246 21.161 1.00 7.12  ? 22  GLN B CA  1 
ATOM   1269 C  C   . GLN B 1 23  ? 29.879 -31.107 22.329 1.00 7.24  ? 22  GLN B C   1 
ATOM   1270 O  O   . GLN B 1 23  ? 29.090 -30.145 22.267 1.00 8.82  ? 22  GLN B O   1 
ATOM   1271 C  CB  . GLN B 1 23  ? 31.737 -30.044 21.278 1.00 8.85  ? 22  GLN B CB  1 
ATOM   1272 C  CG  . GLN B 1 23  ? 32.368 -29.779 22.648 1.00 11.25 ? 22  GLN B CG  1 
ATOM   1273 C  CD  . GLN B 1 23  ? 31.858 -28.649 23.469 1.00 11.84 ? 22  GLN B CD  1 
ATOM   1274 O  OE1 . GLN B 1 23  ? 32.261 -27.425 23.285 1.00 10.18 ? 22  GLN B OE1 1 
ATOM   1275 N  NE2 . GLN B 1 23  ? 30.974 -29.004 24.386 1.00 10.29 ? 22  GLN B NE2 1 
ATOM   1276 N  N   . LYS B 1 24  ? 29.932 -31.931 23.331 1.00 6.65  ? 23  LYS B N   1 
ATOM   1277 C  CA  . LYS B 1 24  ? 28.992 -31.833 24.439 1.00 7.50  ? 23  LYS B CA  1 
ATOM   1278 C  C   . LYS B 1 24  ? 29.528 -31.741 25.871 1.00 7.46  ? 23  LYS B C   1 
ATOM   1279 O  O   . LYS B 1 24  ? 30.639 -31.266 26.255 1.00 6.21  ? 23  LYS B O   1 
ATOM   1280 C  CB  . LYS B 1 24  ? 28.040 -33.086 24.190 1.00 5.85  ? 23  LYS B CB  1 
ATOM   1281 C  CG  . LYS B 1 24  ? 26.871 -32.604 23.273 1.00 5.36  ? 23  LYS B CG  1 
ATOM   1282 C  CD  . LYS B 1 24  ? 25.509 -33.235 23.772 1.00 5.12  ? 23  LYS B CD  1 
ATOM   1283 C  CE  . LYS B 1 24  ? 25.341 -34.661 23.526 1.00 2.00  ? 23  LYS B CE  1 
ATOM   1284 N  NZ  . LYS B 1 24  ? 26.508 -35.476 23.805 1.00 2.00  ? 23  LYS B NZ  1 
ATOM   1285 N  N   . GLU B 1 25  ? 28.637 -32.224 26.738 1.00 5.77  ? 24  GLU B N   1 
ATOM   1286 C  CA  . GLU B 1 25  ? 28.768 -32.334 28.160 1.00 5.63  ? 24  GLU B CA  1 
ATOM   1287 C  C   . GLU B 1 25  ? 29.723 -31.425 28.880 1.00 5.90  ? 24  GLU B C   1 
ATOM   1288 O  O   . GLU B 1 25  ? 30.589 -31.772 29.644 1.00 8.26  ? 24  GLU B O   1 
ATOM   1289 C  CB  . GLU B 1 25  ? 29.119 -33.824 28.528 1.00 4.55  ? 24  GLU B CB  1 
ATOM   1290 C  CG  . GLU B 1 25  ? 28.047 -34.846 28.178 1.00 5.96  ? 24  GLU B CG  1 
ATOM   1291 C  CD  . GLU B 1 25  ? 27.393 -35.053 26.805 1.00 4.89  ? 24  GLU B CD  1 
ATOM   1292 O  OE1 . GLU B 1 25  ? 26.454 -34.289 26.543 1.00 2.00  ? 24  GLU B OE1 1 
ATOM   1293 O  OE2 . GLU B 1 25  ? 27.707 -35.945 25.960 1.00 4.44  ? 24  GLU B OE2 1 
ATOM   1294 N  N   . SER B 1 26  ? 29.575 -30.140 28.687 1.00 8.46  ? 25  SER B N   1 
ATOM   1295 C  CA  . SER B 1 26  ? 30.277 -28.991 29.239 1.00 5.42  ? 25  SER B CA  1 
ATOM   1296 C  C   . SER B 1 26  ? 31.756 -28.909 28.982 1.00 5.98  ? 25  SER B C   1 
ATOM   1297 O  O   . SER B 1 26  ? 32.230 -27.763 28.901 1.00 2.00  ? 25  SER B O   1 
ATOM   1298 C  CB  . SER B 1 26  ? 29.949 -29.068 30.751 1.00 5.29  ? 25  SER B CB  1 
ATOM   1299 O  OG  . SER B 1 26  ? 29.915 -27.782 31.216 1.00 4.44  ? 25  SER B OG  1 
ATOM   1300 N  N   . ASN B 1 27  ? 32.475 -30.039 28.858 1.00 6.37  ? 26  ASN B N   1 
ATOM   1301 C  CA  . ASN B 1 27  ? 33.967 -29.788 28.565 1.00 9.08  ? 26  ASN B CA  1 
ATOM   1302 C  C   . ASN B 1 27  ? 34.382 -31.166 28.003 1.00 8.45  ? 26  ASN B C   1 
ATOM   1303 O  O   . ASN B 1 27  ? 35.274 -31.794 28.479 1.00 6.79  ? 26  ASN B O   1 
ATOM   1304 C  CB  . ASN B 1 27  ? 34.686 -29.156 29.713 1.00 9.36  ? 26  ASN B CB  1 
ATOM   1305 C  CG  . ASN B 1 27  ? 35.884 -28.217 29.582 1.00 11.64 ? 26  ASN B CG  1 
ATOM   1306 O  OD1 . ASN B 1 27  ? 35.884 -27.331 28.670 1.00 10.57 ? 26  ASN B OD1 1 
ATOM   1307 N  ND2 . ASN B 1 27  ? 36.929 -28.326 30.478 1.00 9.17  ? 26  ASN B ND2 1 
ATOM   1308 N  N   . GLY B 1 28  ? 33.602 -31.540 26.983 1.00 12.23 ? 27  GLY B N   1 
ATOM   1309 C  CA  . GLY B 1 28  ? 33.635 -32.790 26.065 1.00 9.16  ? 27  GLY B CA  1 
ATOM   1310 C  C   . GLY B 1 28  ? 34.500 -32.143 24.928 1.00 7.16  ? 27  GLY B C   1 
ATOM   1311 O  O   . GLY B 1 28  ? 34.218 -30.962 24.640 1.00 6.02  ? 27  GLY B O   1 
ATOM   1312 N  N   . PRO B 1 29  ? 35.482 -32.730 24.262 1.00 6.46  ? 28  PRO B N   1 
ATOM   1313 C  CA  . PRO B 1 29  ? 36.303 -32.046 23.214 1.00 4.75  ? 28  PRO B CA  1 
ATOM   1314 C  C   . PRO B 1 29  ? 35.537 -31.669 21.960 1.00 4.52  ? 28  PRO B C   1 
ATOM   1315 O  O   . PRO B 1 29  ? 34.328 -31.893 21.817 1.00 2.64  ? 28  PRO B O   1 
ATOM   1316 C  CB  . PRO B 1 29  ? 37.543 -32.956 23.184 1.00 3.39  ? 28  PRO B CB  1 
ATOM   1317 C  CG  . PRO B 1 29  ? 37.259 -34.251 23.790 1.00 2.00  ? 28  PRO B CG  1 
ATOM   1318 C  CD  . PRO B 1 29  ? 35.890 -34.140 24.437 1.00 2.00  ? 28  PRO B CD  1 
ATOM   1319 N  N   . VAL B 1 30  ? 36.242 -31.023 20.992 1.00 5.32  ? 29  VAL B N   1 
ATOM   1320 C  CA  . VAL B 1 30  ? 35.299 -30.679 19.869 1.00 6.56  ? 29  VAL B CA  1 
ATOM   1321 C  C   . VAL B 1 30  ? 35.656 -31.360 18.597 1.00 4.68  ? 29  VAL B C   1 
ATOM   1322 O  O   . VAL B 1 30  ? 36.840 -31.570 18.489 1.00 4.25  ? 29  VAL B O   1 
ATOM   1323 C  CB  . VAL B 1 30  ? 35.212 -29.110 19.792 1.00 6.82  ? 29  VAL B CB  1 
ATOM   1324 C  CG1 . VAL B 1 30  ? 36.553 -28.480 19.409 1.00 4.84  ? 29  VAL B CG1 1 
ATOM   1325 C  CG2 . VAL B 1 30  ? 34.082 -28.617 18.878 1.00 7.13  ? 29  VAL B CG2 1 
ATOM   1326 N  N   . LYS B 1 31  ? 34.532 -31.555 17.875 1.00 4.13  ? 30  LYS B N   1 
ATOM   1327 C  CA  . LYS B 1 31  ? 34.696 -32.232 16.595 1.00 4.73  ? 30  LYS B CA  1 
ATOM   1328 C  C   . LYS B 1 31  ? 34.398 -31.478 15.294 1.00 5.63  ? 30  LYS B C   1 
ATOM   1329 O  O   . LYS B 1 31  ? 33.554 -30.599 15.173 1.00 4.70  ? 30  LYS B O   1 
ATOM   1330 C  CB  . LYS B 1 31  ? 33.853 -33.500 16.714 1.00 2.00  ? 30  LYS B CB  1 
ATOM   1331 C  CG  . LYS B 1 31  ? 34.709 -34.566 17.354 1.00 2.00  ? 30  LYS B CG  1 
ATOM   1332 C  CD  . LYS B 1 31  ? 33.980 -36.000 17.356 1.00 3.48  ? 30  LYS B CD  1 
ATOM   1333 C  CE  . LYS B 1 31  ? 35.056 -37.105 17.260 1.00 2.00  ? 30  LYS B CE  1 
ATOM   1334 N  NZ  . LYS B 1 31  ? 36.415 -36.789 17.778 1.00 2.00  ? 30  LYS B NZ  1 
ATOM   1335 N  N   . VAL B 1 32  ? 35.207 -31.921 14.284 1.00 5.23  ? 31  VAL B N   1 
ATOM   1336 C  CA  . VAL B 1 32  ? 35.085 -31.353 12.927 1.00 4.47  ? 31  VAL B CA  1 
ATOM   1337 C  C   . VAL B 1 32  ? 35.076 -32.552 11.930 1.00 5.88  ? 31  VAL B C   1 
ATOM   1338 O  O   . VAL B 1 32  ? 35.881 -33.514 11.963 1.00 4.75  ? 31  VAL B O   1 
ATOM   1339 C  CB  . VAL B 1 32  ? 36.122 -30.368 12.431 1.00 3.04  ? 31  VAL B CB  1 
ATOM   1340 C  CG1 . VAL B 1 32  ? 36.216 -29.064 13.272 1.00 3.26  ? 31  VAL B CG1 1 
ATOM   1341 C  CG2 . VAL B 1 32  ? 37.489 -31.026 12.367 1.00 3.57  ? 31  VAL B CG2 1 
ATOM   1342 N  N   . TRP B 1 33  ? 34.085 -32.369 11.080 1.00 5.96  ? 32  TRP B N   1 
ATOM   1343 C  CA  . TRP B 1 33  ? 33.877 -33.403 10.005 1.00 5.27  ? 32  TRP B CA  1 
ATOM   1344 C  C   . TRP B 1 33  ? 33.390 -32.482 8.889  1.00 4.55  ? 32  TRP B C   1 
ATOM   1345 O  O   . TRP B 1 33  ? 32.427 -31.698 9.130  1.00 2.00  ? 32  TRP B O   1 
ATOM   1346 C  CB  . TRP B 1 33  ? 32.891 -34.526 10.246 1.00 9.96  ? 32  TRP B CB  1 
ATOM   1347 C  CG  . TRP B 1 33  ? 31.431 -34.332 10.633 1.00 12.29 ? 32  TRP B CG  1 
ATOM   1348 C  CD1 . TRP B 1 33  ? 30.892 -34.021 11.916 1.00 11.98 ? 32  TRP B CD1 1 
ATOM   1349 C  CD2 . TRP B 1 33  ? 30.306 -34.436 9.749  1.00 11.47 ? 32  TRP B CD2 1 
ATOM   1350 N  NE1 . TRP B 1 33  ? 29.542 -33.923 11.845 1.00 10.04 ? 32  TRP B NE1 1 
ATOM   1351 C  CE2 . TRP B 1 33  ? 29.130 -34.161 10.570 1.00 11.31 ? 32  TRP B CE2 1 
ATOM   1352 C  CE3 . TRP B 1 33  ? 30.201 -34.708 8.389  1.00 9.14  ? 32  TRP B CE3 1 
ATOM   1353 C  CZ2 . TRP B 1 33  ? 27.863 -34.170 10.023 1.00 9.56  ? 32  TRP B CZ2 1 
ATOM   1354 C  CZ3 . TRP B 1 33  ? 28.908 -34.692 7.858  1.00 9.47  ? 32  TRP B CZ3 1 
ATOM   1355 C  CH2 . TRP B 1 33  ? 27.791 -34.442 8.626  1.00 9.65  ? 32  TRP B CH2 1 
ATOM   1356 N  N   . GLY B 1 34  ? 34.186 -32.770 7.898  1.00 3.19  ? 33  GLY B N   1 
ATOM   1357 C  CA  . GLY B 1 34  ? 33.661 -31.790 6.701  1.00 4.07  ? 33  GLY B CA  1 
ATOM   1358 C  C   . GLY B 1 34  ? 33.893 -32.410 5.299  1.00 2.92  ? 33  GLY B C   1 
ATOM   1359 O  O   . GLY B 1 34  ? 34.163 -33.620 5.127  1.00 2.00  ? 33  GLY B O   1 
ATOM   1360 N  N   . SER B 1 35  ? 33.832 -31.623 4.253  1.00 6.47  ? 34  SER B N   1 
ATOM   1361 C  CA  . SER B 1 35  ? 34.039 -31.885 2.775  1.00 6.66  ? 34  SER B CA  1 
ATOM   1362 C  C   . SER B 1 35  ? 34.507 -30.505 2.208  1.00 6.65  ? 34  SER B C   1 
ATOM   1363 O  O   . SER B 1 35  ? 33.628 -29.612 1.835  1.00 6.92  ? 34  SER B O   1 
ATOM   1364 C  CB  . SER B 1 35  ? 32.891 -32.282 1.823  1.00 3.99  ? 34  SER B CB  1 
ATOM   1365 O  OG  . SER B 1 35  ? 33.286 -32.532 0.415  1.00 2.16  ? 34  SER B OG  1 
ATOM   1366 N  N   . ILE B 1 36  ? 35.793 -30.432 2.163  1.00 7.51  ? 35  ILE B N   1 
ATOM   1367 C  CA  . ILE B 1 36  ? 36.586 -29.211 1.664  1.00 7.55  ? 35  ILE B CA  1 
ATOM   1368 C  C   . ILE B 1 36  ? 36.599 -29.514 0.155  1.00 8.23  ? 35  ILE B C   1 
ATOM   1369 O  O   . ILE B 1 36  ? 36.412 -30.796 -0.014 1.00 7.40  ? 35  ILE B O   1 
ATOM   1370 C  CB  . ILE B 1 36  ? 37.958 -28.985 2.341  1.00 7.31  ? 35  ILE B CB  1 
ATOM   1371 C  CG1 . ILE B 1 36  ? 37.993 -29.104 3.907  1.00 4.46  ? 35  ILE B CG1 1 
ATOM   1372 C  CG2 . ILE B 1 36  ? 38.688 -27.562 2.175  1.00 8.19  ? 35  ILE B CG2 1 
ATOM   1373 C  CD1 . ILE B 1 36  ? 37.190 -28.001 4.543  1.00 2.00  ? 35  ILE B CD1 1 
ATOM   1374 N  N   . LYS B 1 37  ? 36.672 -28.490 -0.742 1.00 7.79  ? 36  LYS B N   1 
ATOM   1375 C  CA  . LYS B 1 37  ? 36.684 -28.889 -2.173 1.00 9.31  ? 36  LYS B CA  1 
ATOM   1376 C  C   . LYS B 1 37  ? 37.522 -27.954 -3.066 1.00 10.12 ? 36  LYS B C   1 
ATOM   1377 O  O   . LYS B 1 37  ? 37.661 -26.695 -2.670 1.00 9.43  ? 36  LYS B O   1 
ATOM   1378 C  CB  . LYS B 1 37  ? 35.295 -28.779 -2.753 1.00 6.61  ? 36  LYS B CB  1 
ATOM   1379 C  CG  . LYS B 1 37  ? 34.677 -29.925 -3.449 1.00 7.56  ? 36  LYS B CG  1 
ATOM   1380 C  CD  . LYS B 1 37  ? 33.127 -29.984 -3.422 1.00 5.26  ? 36  LYS B CD  1 
ATOM   1381 C  CE  . LYS B 1 37  ? 32.514 -29.780 -2.061 1.00 2.85  ? 36  LYS B CE  1 
ATOM   1382 N  NZ  . LYS B 1 37  ? 33.293 -30.570 -1.058 1.00 3.50  ? 36  LYS B NZ  1 
ATOM   1383 N  N   . GLY B 1 38  ? 37.843 -28.684 -4.121 1.00 9.57  ? 37  GLY B N   1 
ATOM   1384 C  CA  . GLY B 1 38  ? 38.658 -28.362 -5.260 1.00 7.88  ? 37  GLY B CA  1 
ATOM   1385 C  C   . GLY B 1 38  ? 40.024 -27.894 -4.702 1.00 7.93  ? 37  GLY B C   1 
ATOM   1386 O  O   . GLY B 1 38  ? 40.708 -27.214 -5.479 1.00 7.95  ? 37  GLY B O   1 
ATOM   1387 N  N   . LEU B 1 39  ? 40.437 -28.255 -3.444 1.00 7.02  ? 38  LEU B N   1 
ATOM   1388 C  CA  . LEU B 1 39  ? 41.677 -27.790 -2.847 1.00 8.04  ? 38  LEU B CA  1 
ATOM   1389 C  C   . LEU B 1 39  ? 42.955 -28.564 -3.291 1.00 6.70  ? 38  LEU B C   1 
ATOM   1390 O  O   . LEU B 1 39  ? 42.900 -29.759 -3.222 1.00 4.45  ? 38  LEU B O   1 
ATOM   1391 C  CB  . LEU B 1 39  ? 41.319 -27.730 -1.298 1.00 9.71  ? 38  LEU B CB  1 
ATOM   1392 C  CG  . LEU B 1 39  ? 41.477 -28.960 -0.389 1.00 10.11 ? 38  LEU B CG  1 
ATOM   1393 C  CD1 . LEU B 1 39  ? 41.593 -28.851 1.115  1.00 10.95 ? 38  LEU B CD1 1 
ATOM   1394 C  CD2 . LEU B 1 39  ? 40.152 -29.745 -0.436 1.00 12.12 ? 38  LEU B CD2 1 
ATOM   1395 N  N   . THR B 1 40  ? 44.071 -27.902 -3.696 1.00 5.62  ? 39  THR B N   1 
ATOM   1396 C  CA  . THR B 1 40  ? 45.379 -28.356 -4.188 1.00 4.61  ? 39  THR B CA  1 
ATOM   1397 C  C   . THR B 1 40  ? 45.886 -29.586 -3.359 1.00 3.67  ? 39  THR B C   1 
ATOM   1398 O  O   . THR B 1 40  ? 45.896 -29.358 -2.153 1.00 2.00  ? 39  THR B O   1 
ATOM   1399 C  CB  . THR B 1 40  ? 46.521 -27.228 -4.203 1.00 4.94  ? 39  THR B CB  1 
ATOM   1400 O  OG1 . THR B 1 40  ? 45.952 -25.876 -4.117 1.00 2.00  ? 39  THR B OG1 1 
ATOM   1401 C  CG2 . THR B 1 40  ? 47.514 -27.239 -5.421 1.00 2.00  ? 39  THR B CG2 1 
ATOM   1402 N  N   . GLU B 1 41  ? 46.304 -30.715 -3.894 1.00 3.74  ? 40  GLU B N   1 
ATOM   1403 C  CA  . GLU B 1 41  ? 46.724 -31.993 -3.188 1.00 4.47  ? 40  GLU B CA  1 
ATOM   1404 C  C   . GLU B 1 41  ? 47.607 -32.127 -1.937 1.00 2.73  ? 40  GLU B C   1 
ATOM   1405 O  O   . GLU B 1 41  ? 48.549 -31.518 -1.503 1.00 2.00  ? 40  GLU B O   1 
ATOM   1406 C  CB  . GLU B 1 41  ? 47.434 -33.020 -4.111 1.00 4.77  ? 40  GLU B CB  1 
ATOM   1407 C  CG  . GLU B 1 41  ? 47.824 -34.447 -3.799 1.00 7.75  ? 40  GLU B CG  1 
ATOM   1408 C  CD  . GLU B 1 41  ? 48.186 -35.428 -4.965 1.00 7.84  ? 40  GLU B CD  1 
ATOM   1409 O  OE1 . GLU B 1 41  ? 48.790 -35.264 -6.019 1.00 2.83  ? 40  GLU B OE1 1 
ATOM   1410 O  OE2 . GLU B 1 41  ? 47.767 -36.603 -4.777 1.00 7.28  ? 40  GLU B OE2 1 
ATOM   1411 N  N   . GLY B 1 42  ? 46.942 -33.192 -1.277 1.00 3.42  ? 41  GLY B N   1 
ATOM   1412 C  CA  . GLY B 1 42  ? 47.810 -33.410 0.026  1.00 5.26  ? 41  GLY B CA  1 
ATOM   1413 C  C   . GLY B 1 42  ? 47.658 -32.514 1.234  1.00 6.36  ? 41  GLY B C   1 
ATOM   1414 O  O   . GLY B 1 42  ? 46.751 -32.954 2.038  1.00 3.47  ? 41  GLY B O   1 
ATOM   1415 N  N   . LEU B 1 43  ? 48.381 -31.367 1.429  1.00 5.89  ? 42  LEU B N   1 
ATOM   1416 C  CA  . LEU B 1 43  ? 48.233 -30.554 2.614  1.00 7.71  ? 42  LEU B CA  1 
ATOM   1417 C  C   . LEU B 1 43  ? 47.969 -29.072 2.754  1.00 9.96  ? 42  LEU B C   1 
ATOM   1418 O  O   . LEU B 1 43  ? 48.644 -28.017 2.494  1.00 9.40  ? 42  LEU B O   1 
ATOM   1419 C  CB  . LEU B 1 43  ? 49.743 -30.825 3.062  1.00 9.80  ? 42  LEU B CB  1 
ATOM   1420 C  CG  . LEU B 1 43  ? 49.901 -32.134 3.840  1.00 11.00 ? 42  LEU B CG  1 
ATOM   1421 C  CD1 . LEU B 1 43  ? 51.107 -31.963 4.763  1.00 12.84 ? 42  LEU B CD1 1 
ATOM   1422 C  CD2 . LEU B 1 43  ? 48.694 -32.531 4.712  1.00 10.34 ? 42  LEU B CD2 1 
ATOM   1423 N  N   . HIS B 1 44  ? 46.730 -28.888 3.312  1.00 11.13 ? 43  HIS B N   1 
ATOM   1424 C  CA  . HIS B 1 44  ? 46.252 -27.484 3.540  1.00 10.20 ? 43  HIS B CA  1 
ATOM   1425 C  C   . HIS B 1 44  ? 46.065 -27.003 4.968  1.00 12.99 ? 43  HIS B C   1 
ATOM   1426 O  O   . HIS B 1 44  ? 45.891 -27.793 5.961  1.00 9.59  ? 43  HIS B O   1 
ATOM   1427 C  CB  . HIS B 1 44  ? 44.985 -27.506 2.672  1.00 8.03  ? 43  HIS B CB  1 
ATOM   1428 C  CG  . HIS B 1 44  ? 45.540 -27.329 1.262  1.00 7.59  ? 43  HIS B CG  1 
ATOM   1429 N  ND1 . HIS B 1 44  ? 46.380 -26.338 0.868  1.00 6.35  ? 43  HIS B ND1 1 
ATOM   1430 C  CD2 . HIS B 1 44  ? 45.286 -28.075 0.152  1.00 7.28  ? 43  HIS B CD2 1 
ATOM   1431 C  CE1 . HIS B 1 44  ? 46.620 -26.504 -0.415 1.00 7.23  ? 43  HIS B CE1 1 
ATOM   1432 N  NE2 . HIS B 1 44  ? 45.977 -27.542 -0.889 1.00 6.11  ? 43  HIS B NE2 1 
ATOM   1433 N  N   . GLY B 1 45  ? 46.105 -25.615 5.076  1.00 13.13 ? 44  GLY B N   1 
ATOM   1434 C  CA  . GLY B 1 45  ? 45.962 -24.936 6.399  1.00 10.87 ? 44  GLY B CA  1 
ATOM   1435 C  C   . GLY B 1 45  ? 44.507 -24.956 6.842  1.00 11.38 ? 44  GLY B C   1 
ATOM   1436 O  O   . GLY B 1 45  ? 43.634 -24.717 6.019  1.00 8.41  ? 44  GLY B O   1 
ATOM   1437 N  N   . PHE B 1 46  ? 44.410 -25.272 8.200  1.00 12.87 ? 45  PHE B N   1 
ATOM   1438 C  CA  . PHE B 1 46  ? 42.933 -25.312 8.663  1.00 13.18 ? 45  PHE B CA  1 
ATOM   1439 C  C   . PHE B 1 46  ? 42.883 -24.719 10.066 1.00 14.30 ? 45  PHE B C   1 
ATOM   1440 O  O   . PHE B 1 46  ? 43.159 -25.362 11.178 1.00 12.20 ? 45  PHE B O   1 
ATOM   1441 C  CB  . PHE B 1 46  ? 42.442 -26.695 8.401  1.00 13.51 ? 45  PHE B CB  1 
ATOM   1442 C  CG  . PHE B 1 46  ? 40.955 -26.959 8.404  1.00 13.25 ? 45  PHE B CG  1 
ATOM   1443 C  CD1 . PHE B 1 46  ? 40.268 -27.304 9.593  1.00 11.96 ? 45  PHE B CD1 1 
ATOM   1444 C  CD2 . PHE B 1 46  ? 40.264 -26.850 7.191  1.00 10.25 ? 45  PHE B CD2 1 
ATOM   1445 C  CE1 . PHE B 1 46  ? 38.903 -27.531 9.563  1.00 9.58  ? 45  PHE B CE1 1 
ATOM   1446 C  CE2 . PHE B 1 46  ? 38.907 -27.068 7.150  1.00 7.49  ? 45  PHE B CE2 1 
ATOM   1447 C  CZ  . PHE B 1 46  ? 38.277 -27.404 8.332  1.00 9.20  ? 45  PHE B CZ  1 
ATOM   1448 N  N   . HIS B 1 47  ? 42.527 -23.423 9.686  1.00 15.89 ? 46  HIS B N   1 
ATOM   1449 C  CA  . HIS B 1 47  ? 42.375 -22.442 10.784 1.00 15.75 ? 46  HIS B CA  1 
ATOM   1450 C  C   . HIS B 1 47  ? 40.987 -21.809 10.978 1.00 14.59 ? 46  HIS B C   1 
ATOM   1451 O  O   . HIS B 1 47  ? 40.027 -21.900 10.134 1.00 11.36 ? 46  HIS B O   1 
ATOM   1452 C  CB  . HIS B 1 47  ? 43.349 -21.273 10.490 1.00 18.87 ? 46  HIS B CB  1 
ATOM   1453 C  CG  . HIS B 1 47  ? 44.787 -21.681 10.487 1.00 18.65 ? 46  HIS B CG  1 
ATOM   1454 N  ND1 . HIS B 1 47  ? 45.761 -20.813 10.189 1.00 18.99 ? 46  HIS B ND1 1 
ATOM   1455 C  CD2 . HIS B 1 47  ? 45.431 -22.805 10.715 1.00 18.87 ? 46  HIS B CD2 1 
ATOM   1456 C  CE1 . HIS B 1 47  ? 46.949 -21.317 10.247 1.00 17.69 ? 46  HIS B CE1 1 
ATOM   1457 N  NE2 . HIS B 1 47  ? 46.790 -22.552 10.564 1.00 19.38 ? 46  HIS B NE2 1 
ATOM   1458 N  N   . VAL B 1 48  ? 40.959 -21.156 12.145 1.00 13.74 ? 47  VAL B N   1 
ATOM   1459 C  CA  . VAL B 1 48  ? 39.838 -20.408 12.661 1.00 13.62 ? 47  VAL B CA  1 
ATOM   1460 C  C   . VAL B 1 48  ? 40.297 -19.021 13.141 1.00 15.80 ? 47  VAL B C   1 
ATOM   1461 O  O   . VAL B 1 48  ? 40.790 -18.773 14.270 1.00 16.40 ? 47  VAL B O   1 
ATOM   1462 C  CB  . VAL B 1 48  ? 39.126 -21.115 13.791 1.00 13.63 ? 47  VAL B CB  1 
ATOM   1463 C  CG1 . VAL B 1 48  ? 37.962 -20.181 14.206 1.00 14.30 ? 47  VAL B CG1 1 
ATOM   1464 C  CG2 . VAL B 1 48  ? 38.634 -22.473 13.431 1.00 14.01 ? 47  VAL B CG2 1 
ATOM   1465 N  N   . HIS B 1 49  ? 40.136 -18.017 12.294 1.00 14.55 ? 48  HIS B N   1 
ATOM   1466 C  CA  . HIS B 1 49  ? 40.477 -16.639 12.548 1.00 10.73 ? 48  HIS B CA  1 
ATOM   1467 C  C   . HIS B 1 49  ? 39.239 -15.865 13.085 1.00 10.11 ? 48  HIS B C   1 
ATOM   1468 O  O   . HIS B 1 49  ? 38.105 -15.746 12.592 1.00 8.66  ? 48  HIS B O   1 
ATOM   1469 C  CB  . HIS B 1 49  ? 40.921 -15.947 11.325 1.00 9.42  ? 48  HIS B CB  1 
ATOM   1470 C  CG  . HIS B 1 49  ? 42.117 -16.575 10.678 1.00 8.26  ? 48  HIS B CG  1 
ATOM   1471 N  ND1 . HIS B 1 49  ? 43.261 -15.898 10.746 1.00 6.04  ? 48  HIS B ND1 1 
ATOM   1472 C  CD2 . HIS B 1 49  ? 42.382 -17.715 9.968  1.00 9.70  ? 48  HIS B CD2 1 
ATOM   1473 C  CE1 . HIS B 1 49  ? 44.169 -16.570 10.112 1.00 9.38  ? 48  HIS B CE1 1 
ATOM   1474 N  NE2 . HIS B 1 49  ? 43.676 -17.698 9.596  1.00 10.42 ? 48  HIS B NE2 1 
ATOM   1475 N  N   . GLU B 1 50  ? 39.672 -15.321 14.222 1.00 9.03  ? 49  GLU B N   1 
ATOM   1476 C  CA  . GLU B 1 50  ? 38.938 -14.526 15.166 1.00 7.81  ? 49  GLU B CA  1 
ATOM   1477 C  C   . GLU B 1 50  ? 37.777 -13.617 14.789 1.00 6.42  ? 49  GLU B C   1 
ATOM   1478 O  O   . GLU B 1 50  ? 36.604 -13.906 15.161 1.00 3.23  ? 49  GLU B O   1 
ATOM   1479 C  CB  . GLU B 1 50  ? 39.960 -13.617 15.963 1.00 8.56  ? 49  GLU B CB  1 
ATOM   1480 C  CG  . GLU B 1 50  ? 39.463 -12.718 17.119 1.00 5.94  ? 49  GLU B CG  1 
ATOM   1481 C  CD  . GLU B 1 50  ? 40.565 -11.841 17.718 1.00 7.53  ? 49  GLU B CD  1 
ATOM   1482 O  OE1 . GLU B 1 50  ? 41.767 -12.215 17.919 1.00 9.16  ? 49  GLU B OE1 1 
ATOM   1483 O  OE2 . GLU B 1 50  ? 40.220 -10.698 18.009 1.00 3.44  ? 49  GLU B OE2 1 
ATOM   1484 N  N   . PHE B 1 51  ? 37.960 -12.530 14.108 1.00 6.27  ? 50  PHE B N   1 
ATOM   1485 C  CA  . PHE B 1 51  ? 36.735 -11.694 13.866 1.00 5.10  ? 50  PHE B CA  1 
ATOM   1486 C  C   . PHE B 1 51  ? 36.010 -12.208 12.631 1.00 4.85  ? 50  PHE B C   1 
ATOM   1487 O  O   . PHE B 1 51  ? 36.581 -12.127 11.560 1.00 2.00  ? 50  PHE B O   1 
ATOM   1488 C  CB  . PHE B 1 51  ? 37.040 -10.180 13.753 1.00 4.41  ? 50  PHE B CB  1 
ATOM   1489 C  CG  . PHE B 1 51  ? 37.916 -9.545  14.783 1.00 4.51  ? 50  PHE B CG  1 
ATOM   1490 C  CD1 . PHE B 1 51  ? 37.357 -9.236  16.049 1.00 4.46  ? 50  PHE B CD1 1 
ATOM   1491 C  CD2 . PHE B 1 51  ? 39.267 -9.272  14.551 1.00 3.48  ? 50  PHE B CD2 1 
ATOM   1492 C  CE1 . PHE B 1 51  ? 38.130 -8.676  17.048 1.00 3.96  ? 50  PHE B CE1 1 
ATOM   1493 C  CE2 . PHE B 1 51  ? 40.057 -8.727  15.502 1.00 2.00  ? 50  PHE B CE2 1 
ATOM   1494 C  CZ  . PHE B 1 51  ? 39.473 -8.434  16.742 1.00 4.26  ? 50  PHE B CZ  1 
ATOM   1495 N  N   . GLY B 1 52  ? 34.842 -12.674 12.998 1.00 3.96  ? 51  GLY B N   1 
ATOM   1496 C  CA  . GLY B 1 52  ? 33.927 -13.201 11.986 1.00 5.29  ? 51  GLY B CA  1 
ATOM   1497 C  C   . GLY B 1 52  ? 33.200 -12.013 11.189 1.00 7.40  ? 51  GLY B C   1 
ATOM   1498 O  O   . GLY B 1 52  ? 31.952 -11.878 11.037 1.00 2.22  ? 51  GLY B O   1 
ATOM   1499 N  N   . ASP B 1 53  ? 34.130 -11.175 10.722 1.00 6.13  ? 52  ASP B N   1 
ATOM   1500 C  CA  . ASP B 1 53  ? 33.921 -9.971  9.893  1.00 5.50  ? 52  ASP B CA  1 
ATOM   1501 C  C   . ASP B 1 53  ? 34.346 -10.711 8.568  1.00 4.90  ? 52  ASP B C   1 
ATOM   1502 O  O   . ASP B 1 53  ? 35.356 -11.479 8.475  1.00 2.79  ? 52  ASP B O   1 
ATOM   1503 C  CB  . ASP B 1 53  ? 34.689 -8.773  10.167 1.00 6.12  ? 52  ASP B CB  1 
ATOM   1504 C  CG  . ASP B 1 53  ? 34.291 -7.560  9.360  1.00 7.93  ? 52  ASP B CG  1 
ATOM   1505 O  OD1 . ASP B 1 53  ? 33.080 -7.367  9.000  1.00 5.38  ? 52  ASP B OD1 1 
ATOM   1506 O  OD2 . ASP B 1 53  ? 35.268 -6.755  9.093  1.00 9.04  ? 52  ASP B OD2 1 
ATOM   1507 N  N   . ASN B 1 54  ? 33.563 -10.523 7.587  1.00 4.74  ? 53  ASN B N   1 
ATOM   1508 C  CA  . ASN B 1 54  ? 33.818 -11.209 6.292  1.00 6.28  ? 53  ASN B CA  1 
ATOM   1509 C  C   . ASN B 1 54  ? 33.315 -10.316 5.253  1.00 6.59  ? 53  ASN B C   1 
ATOM   1510 O  O   . ASN B 1 54  ? 32.797 -10.755 4.216  1.00 9.14  ? 53  ASN B O   1 
ATOM   1511 C  CB  . ASN B 1 54  ? 33.060 -12.542 6.460  1.00 5.62  ? 53  ASN B CB  1 
ATOM   1512 C  CG  . ASN B 1 54  ? 34.006 -13.722 6.463  1.00 3.59  ? 53  ASN B CG  1 
ATOM   1513 O  OD1 . ASN B 1 54  ? 33.888 -14.517 5.452  1.00 5.59  ? 53  ASN B OD1 1 
ATOM   1514 N  ND2 . ASN B 1 54  ? 34.849 -13.865 7.461  1.00 3.05  ? 53  ASN B ND2 1 
ATOM   1515 N  N   . THR B 1 55  ? 33.512 -9.084  5.675  1.00 6.40  ? 54  THR B N   1 
ATOM   1516 C  CA  . THR B 1 55  ? 32.991 -7.952  4.790  1.00 6.49  ? 54  THR B CA  1 
ATOM   1517 C  C   . THR B 1 55  ? 33.584 -7.920  3.419  1.00 7.44  ? 54  THR B C   1 
ATOM   1518 O  O   . THR B 1 55  ? 32.918 -7.746  2.405  1.00 4.51  ? 54  THR B O   1 
ATOM   1519 C  CB  . THR B 1 55  ? 33.145 -6.776  5.816  1.00 3.51  ? 54  THR B CB  1 
ATOM   1520 O  OG1 . THR B 1 55  ? 34.238 -7.337  6.510  1.00 2.00  ? 54  THR B OG1 1 
ATOM   1521 C  CG2 . THR B 1 55  ? 31.938 -6.500  6.722  1.00 3.33  ? 54  THR B CG2 1 
ATOM   1522 N  N   . ALA B 1 56  ? 34.879 -8.104  3.565  1.00 10.18 ? 55  ALA B N   1 
ATOM   1523 C  CA  . ALA B 1 56  ? 35.875 -8.208  2.497  1.00 11.51 ? 55  ALA B CA  1 
ATOM   1524 C  C   . ALA B 1 56  ? 36.137 -9.686  3.067  1.00 10.46 ? 55  ALA B C   1 
ATOM   1525 O  O   . ALA B 1 56  ? 36.820 -9.778  4.068  1.00 8.09  ? 55  ALA B O   1 
ATOM   1526 C  CB  . ALA B 1 56  ? 37.077 -7.339  2.390  1.00 12.38 ? 55  ALA B CB  1 
ATOM   1527 N  N   . GLY B 1 57  ? 35.459 -10.491 2.302  1.00 9.55  ? 56  GLY B N   1 
ATOM   1528 C  CA  . GLY B 1 57  ? 35.424 -11.950 2.468  1.00 8.53  ? 56  GLY B CA  1 
ATOM   1529 C  C   . GLY B 1 57  ? 36.336 -12.515 3.491  1.00 8.05  ? 56  GLY B C   1 
ATOM   1530 O  O   . GLY B 1 57  ? 36.092 -12.192 4.705  1.00 7.92  ? 56  GLY B O   1 
ATOM   1531 N  N   . CYS B 1 58  ? 37.330 -13.303 3.063  1.00 6.52  ? 57  CYS B N   1 
ATOM   1532 C  CA  . CYS B 1 58  ? 38.269 -13.907 4.025  1.00 5.18  ? 57  CYS B CA  1 
ATOM   1533 C  C   . CYS B 1 58  ? 39.210 -12.964 4.725  1.00 4.57  ? 57  CYS B C   1 
ATOM   1534 O  O   . CYS B 1 58  ? 39.498 -13.254 5.917  1.00 3.86  ? 57  CYS B O   1 
ATOM   1535 C  CB  . CYS B 1 58  ? 39.073 -15.032 3.313  1.00 7.15  ? 57  CYS B CB  1 
ATOM   1536 S  SG  . CYS B 1 58  ? 38.298 -16.745 2.995  1.00 5.26  ? 57  CYS B SG  1 
ATOM   1537 N  N   . THR B 1 59  ? 39.716 -11.903 4.199  1.00 5.39  ? 58  THR B N   1 
ATOM   1538 C  CA  . THR B 1 59  ? 40.673 -11.029 4.965  1.00 6.89  ? 58  THR B CA  1 
ATOM   1539 C  C   . THR B 1 59  ? 40.208 -10.187 6.146  1.00 9.32  ? 58  THR B C   1 
ATOM   1540 O  O   . THR B 1 59  ? 41.141 -9.616  6.814  1.00 7.89  ? 58  THR B O   1 
ATOM   1541 C  CB  . THR B 1 59  ? 41.485 -10.316 3.798  1.00 3.12  ? 58  THR B CB  1 
ATOM   1542 O  OG1 . THR B 1 59  ? 40.822 -9.745  2.695  1.00 2.00  ? 58  THR B OG1 1 
ATOM   1543 C  CG2 . THR B 1 59  ? 42.363 -11.562 3.308  1.00 5.32  ? 58  THR B CG2 1 
ATOM   1544 N  N   . SER B 1 60  ? 38.942 -10.078 6.500  1.00 9.61  ? 59  SER B N   1 
ATOM   1545 C  CA  . SER B 1 60  ? 38.610 -9.216  7.689  1.00 10.36 ? 59  SER B CA  1 
ATOM   1546 C  C   . SER B 1 60  ? 38.486 -10.086 8.942  1.00 11.61 ? 59  SER B C   1 
ATOM   1547 O  O   . SER B 1 60  ? 38.056 -9.666  10.065 1.00 11.29 ? 59  SER B O   1 
ATOM   1548 C  CB  . SER B 1 60  ? 37.435 -8.362  7.262  1.00 8.49  ? 59  SER B CB  1 
ATOM   1549 O  OG  . SER B 1 60  ? 36.184 -8.980  7.021  1.00 4.14  ? 59  SER B OG  1 
ATOM   1550 N  N   . ALA B 1 61  ? 38.884 -11.321 8.783  1.00 11.86 ? 60  ALA B N   1 
ATOM   1551 C  CA  . ALA B 1 61  ? 38.821 -12.315 9.910  1.00 12.66 ? 60  ALA B CA  1 
ATOM   1552 C  C   . ALA B 1 61  ? 40.003 -12.381 10.858 1.00 12.87 ? 60  ALA B C   1 
ATOM   1553 O  O   . ALA B 1 61  ? 40.055 -13.189 11.830 1.00 10.89 ? 60  ALA B O   1 
ATOM   1554 C  CB  . ALA B 1 61  ? 38.507 -13.608 9.100  1.00 10.37 ? 60  ALA B CB  1 
ATOM   1555 N  N   . GLY B 1 62  ? 41.005 -11.521 10.578 1.00 12.52 ? 61  GLY B N   1 
ATOM   1556 C  CA  . GLY B 1 62  ? 42.272 -11.285 11.212 1.00 8.98  ? 61  GLY B CA  1 
ATOM   1557 C  C   . GLY B 1 62  ? 43.141 -12.504 11.476 1.00 8.21  ? 61  GLY B C   1 
ATOM   1558 O  O   . GLY B 1 62  ? 43.297 -13.449 10.672 1.00 6.32  ? 61  GLY B O   1 
ATOM   1559 N  N   . PRO B 1 63  ? 43.744 -12.489 12.675 1.00 7.76  ? 62  PRO B N   1 
ATOM   1560 C  CA  . PRO B 1 63  ? 44.659 -13.480 13.281 1.00 6.76  ? 62  PRO B CA  1 
ATOM   1561 C  C   . PRO B 1 63  ? 43.996 -14.746 13.729 1.00 7.03  ? 62  PRO B C   1 
ATOM   1562 O  O   . PRO B 1 63  ? 42.732 -14.775 13.734 1.00 8.31  ? 62  PRO B O   1 
ATOM   1563 C  CB  . PRO B 1 63  ? 45.374 -12.682 14.359 1.00 6.96  ? 62  PRO B CB  1 
ATOM   1564 C  CG  . PRO B 1 63  ? 45.216 -11.252 13.851 1.00 6.37  ? 62  PRO B CG  1 
ATOM   1565 C  CD  . PRO B 1 63  ? 43.624 -11.413 13.708 1.00 7.83  ? 62  PRO B CD  1 
ATOM   1566 N  N   . HIS B 1 64  ? 44.779 -15.812 14.066 1.00 7.61  ? 63  HIS B N   1 
ATOM   1567 C  CA  . HIS B 1 64  ? 43.922 -16.990 14.474 1.00 8.48  ? 63  HIS B CA  1 
ATOM   1568 C  C   . HIS B 1 64  ? 43.214 -16.660 15.784 1.00 4.84  ? 63  HIS B C   1 
ATOM   1569 O  O   . HIS B 1 64  ? 43.595 -15.764 16.533 1.00 3.59  ? 63  HIS B O   1 
ATOM   1570 C  CB  . HIS B 1 64  ? 44.626 -18.394 14.662 1.00 11.16 ? 63  HIS B CB  1 
ATOM   1571 C  CG  . HIS B 1 64  ? 45.273 -18.571 13.269 1.00 13.44 ? 63  HIS B CG  1 
ATOM   1572 N  ND1 . HIS B 1 64  ? 46.580 -18.246 12.982 1.00 13.60 ? 63  HIS B ND1 1 
ATOM   1573 C  CD2 . HIS B 1 64  ? 44.645 -19.040 12.167 1.00 10.63 ? 63  HIS B CD2 1 
ATOM   1574 C  CE1 . HIS B 1 64  ? 46.707 -18.509 11.642 1.00 13.11 ? 63  HIS B CE1 1 
ATOM   1575 N  NE2 . HIS B 1 64  ? 45.613 -18.957 11.235 1.00 12.55 ? 63  HIS B NE2 1 
ATOM   1576 N  N   . PHE B 1 65  ? 42.180 -17.375 16.109 1.00 4.04  ? 64  PHE B N   1 
ATOM   1577 C  CA  . PHE B 1 65  ? 41.489 -17.112 17.386 1.00 4.19  ? 64  PHE B CA  1 
ATOM   1578 C  C   . PHE B 1 65  ? 42.647 -17.442 18.414 1.00 6.07  ? 64  PHE B C   1 
ATOM   1579 O  O   . PHE B 1 65  ? 43.319 -18.455 18.645 1.00 3.04  ? 64  PHE B O   1 
ATOM   1580 C  CB  . PHE B 1 65  ? 40.261 -17.811 17.825 1.00 5.14  ? 64  PHE B CB  1 
ATOM   1581 C  CG  . PHE B 1 65  ? 39.540 -17.247 19.011 1.00 7.93  ? 64  PHE B CG  1 
ATOM   1582 C  CD1 . PHE B 1 65  ? 39.833 -15.980 19.497 1.00 10.22 ? 64  PHE B CD1 1 
ATOM   1583 C  CD2 . PHE B 1 65  ? 38.559 -17.985 19.665 1.00 8.25  ? 64  PHE B CD2 1 
ATOM   1584 C  CE1 . PHE B 1 65  ? 39.217 -15.383 20.584 1.00 10.56 ? 64  PHE B CE1 1 
ATOM   1585 C  CE2 . PHE B 1 65  ? 37.898 -17.439 20.760 1.00 10.23 ? 64  PHE B CE2 1 
ATOM   1586 C  CZ  . PHE B 1 65  ? 38.233 -16.149 21.210 1.00 12.09 ? 64  PHE B CZ  1 
ATOM   1587 N  N   . ASN B 1 66  ? 42.814 -16.219 19.006 1.00 7.19  ? 65  ASN B N   1 
ATOM   1588 C  CA  . ASN B 1 66  ? 43.763 -16.297 19.985 1.00 8.34  ? 65  ASN B CA  1 
ATOM   1589 C  C   . ASN B 1 66  ? 43.326 -15.440 21.147 1.00 8.23  ? 65  ASN B C   1 
ATOM   1590 O  O   . ASN B 1 66  ? 43.412 -14.198 21.127 1.00 13.73 ? 65  ASN B O   1 
ATOM   1591 C  CB  . ASN B 1 66  ? 45.288 -16.000 19.627 1.00 7.76  ? 65  ASN B CB  1 
ATOM   1592 C  CG  . ASN B 1 66  ? 45.981 -15.895 21.048 1.00 10.39 ? 65  ASN B CG  1 
ATOM   1593 O  OD1 . ASN B 1 66  ? 46.176 -16.741 22.004 1.00 6.84  ? 65  ASN B OD1 1 
ATOM   1594 N  ND2 . ASN B 1 66  ? 46.387 -14.583 21.149 1.00 11.83 ? 65  ASN B ND2 1 
ATOM   1595 N  N   . PRO B 1 67  ? 42.886 -16.018 22.181 1.00 7.48  ? 66  PRO B N   1 
ATOM   1596 C  CA  . PRO B 1 67  ? 42.608 -15.099 23.250 1.00 6.77  ? 66  PRO B CA  1 
ATOM   1597 C  C   . PRO B 1 67  ? 44.043 -14.758 23.778 1.00 6.35  ? 66  PRO B C   1 
ATOM   1598 O  O   . PRO B 1 67  ? 44.592 -13.627 23.696 1.00 3.18  ? 66  PRO B O   1 
ATOM   1599 C  CB  . PRO B 1 67  ? 41.659 -15.846 24.182 1.00 9.50  ? 66  PRO B CB  1 
ATOM   1600 C  CG  . PRO B 1 67  ? 41.117 -17.021 23.320 1.00 6.95  ? 66  PRO B CG  1 
ATOM   1601 C  CD  . PRO B 1 67  ? 42.523 -17.416 22.571 1.00 7.87  ? 66  PRO B CD  1 
ATOM   1602 N  N   . LEU B 1 68  ? 44.788 -15.686 24.371 1.00 7.76  ? 67  LEU B N   1 
ATOM   1603 C  CA  . LEU B 1 68  ? 46.079 -15.824 25.085 1.00 7.07  ? 67  LEU B CA  1 
ATOM   1604 C  C   . LEU B 1 68  ? 47.344 -15.126 24.683 1.00 7.63  ? 67  LEU B C   1 
ATOM   1605 O  O   . LEU B 1 68  ? 48.027 -14.653 25.639 1.00 9.31  ? 67  LEU B O   1 
ATOM   1606 C  CB  . LEU B 1 68  ? 46.305 -17.333 25.341 1.00 6.71  ? 67  LEU B CB  1 
ATOM   1607 C  CG  . LEU B 1 68  ? 45.902 -17.699 26.787 1.00 6.53  ? 67  LEU B CG  1 
ATOM   1608 C  CD1 . LEU B 1 68  ? 44.517 -17.133 27.176 1.00 8.84  ? 67  LEU B CD1 1 
ATOM   1609 C  CD2 . LEU B 1 68  ? 45.822 -19.204 26.952 1.00 5.94  ? 67  LEU B CD2 1 
ATOM   1610 N  N   . SER B 1 69  ? 47.700 -14.962 23.492 1.00 8.32  ? 68  SER B N   1 
ATOM   1611 C  CA  . SER B 1 69  ? 48.826 -14.310 22.910 1.00 5.00  ? 68  SER B CA  1 
ATOM   1612 C  C   . SER B 1 69  ? 50.100 -15.181 22.870 1.00 5.68  ? 68  SER B C   1 
ATOM   1613 O  O   . SER B 1 69  ? 51.268 -14.789 23.051 1.00 5.55  ? 68  SER B O   1 
ATOM   1614 C  CB  . SER B 1 69  ? 49.030 -12.946 23.531 1.00 4.29  ? 68  SER B CB  1 
ATOM   1615 O  OG  . SER B 1 69  ? 47.814 -12.242 23.635 1.00 2.00  ? 68  SER B OG  1 
ATOM   1616 N  N   . ARG B 1 70  ? 49.759 -16.400 22.538 1.00 5.64  ? 69  ARG B N   1 
ATOM   1617 C  CA  . ARG B 1 70  ? 50.616 -17.521 22.284 1.00 6.38  ? 69  ARG B CA  1 
ATOM   1618 C  C   . ARG B 1 70  ? 51.326 -17.329 20.931 1.00 5.31  ? 69  ARG B C   1 
ATOM   1619 O  O   . ARG B 1 70  ? 51.060 -16.263 20.262 1.00 6.65  ? 69  ARG B O   1 
ATOM   1620 C  CB  . ARG B 1 70  ? 49.695 -18.760 22.148 1.00 3.64  ? 69  ARG B CB  1 
ATOM   1621 C  CG  . ARG B 1 70  ? 49.341 -19.008 23.566 1.00 4.86  ? 69  ARG B CG  1 
ATOM   1622 C  CD  . ARG B 1 70  ? 50.309 -19.509 24.582 1.00 2.61  ? 69  ARG B CD  1 
ATOM   1623 N  NE  . ARG B 1 70  ? 50.236 -20.954 24.788 1.00 2.00  ? 69  ARG B NE  1 
ATOM   1624 C  CZ  . ARG B 1 70  ? 51.322 -21.564 25.279 1.00 2.00  ? 69  ARG B CZ  1 
ATOM   1625 N  NH1 . ARG B 1 70  ? 52.388 -20.976 25.788 1.00 2.00  ? 69  ARG B NH1 1 
ATOM   1626 N  NH2 . ARG B 1 70  ? 51.376 -22.887 25.306 1.00 2.00  ? 69  ARG B NH2 1 
ATOM   1627 N  N   . LYS B 1 71  ? 52.163 -18.199 20.463 1.00 5.37  ? 70  LYS B N   1 
ATOM   1628 C  CA  . LYS B 1 71  ? 52.793 -17.993 19.088 1.00 7.67  ? 70  LYS B CA  1 
ATOM   1629 C  C   . LYS B 1 71  ? 52.031 -19.023 18.136 1.00 8.96  ? 70  LYS B C   1 
ATOM   1630 O  O   . LYS B 1 71  ? 50.896 -19.470 18.559 1.00 6.70  ? 70  LYS B O   1 
ATOM   1631 C  CB  . LYS B 1 71  ? 54.281 -18.095 18.976 1.00 6.36  ? 70  LYS B CB  1 
ATOM   1632 C  CG  . LYS B 1 71  ? 54.935 -16.772 19.253 1.00 7.01  ? 70  LYS B CG  1 
ATOM   1633 C  CD  . LYS B 1 71  ? 55.201 -16.504 20.686 1.00 6.66  ? 70  LYS B CD  1 
ATOM   1634 C  CE  . LYS B 1 71  ? 54.876 -15.061 21.087 1.00 5.44  ? 70  LYS B CE  1 
ATOM   1635 N  NZ  . LYS B 1 71  ? 53.460 -15.091 21.588 1.00 5.58  ? 70  LYS B NZ  1 
ATOM   1636 N  N   . HIS B 1 72  ? 52.575 -19.425 16.964 1.00 8.69  ? 71  HIS B N   1 
ATOM   1637 C  CA  . HIS B 1 72  ? 51.798 -20.353 16.140 1.00 10.51 ? 71  HIS B CA  1 
ATOM   1638 C  C   . HIS B 1 72  ? 51.814 -21.839 16.575 1.00 8.94  ? 71  HIS B C   1 
ATOM   1639 O  O   . HIS B 1 72  ? 52.727 -22.491 16.884 1.00 6.11  ? 71  HIS B O   1 
ATOM   1640 C  CB  . HIS B 1 72  ? 52.037 -20.442 14.606 1.00 12.77 ? 71  HIS B CB  1 
ATOM   1641 C  CG  . HIS B 1 72  ? 50.970 -20.912 13.624 1.00 13.86 ? 71  HIS B CG  1 
ATOM   1642 N  ND1 . HIS B 1 72  ? 49.847 -20.429 13.053 1.00 11.66 ? 71  HIS B ND1 1 
ATOM   1643 C  CD2 . HIS B 1 72  ? 51.172 -22.197 13.038 1.00 14.03 ? 71  HIS B CD2 1 
ATOM   1644 C  CE1 . HIS B 1 72  ? 49.394 -21.340 12.194 1.00 12.22 ? 71  HIS B CE1 1 
ATOM   1645 N  NE2 . HIS B 1 72  ? 50.131 -22.398 12.158 1.00 13.27 ? 71  HIS B NE2 1 
ATOM   1646 N  N   . GLY B 1 73  ? 50.512 -22.073 16.462 1.00 8.16  ? 72  GLY B N   1 
ATOM   1647 C  CA  . GLY B 1 73  ? 49.959 -23.327 16.750 1.00 9.84  ? 72  GLY B CA  1 
ATOM   1648 C  C   . GLY B 1 73  ? 50.338 -24.462 15.857 1.00 11.32 ? 72  GLY B C   1 
ATOM   1649 O  O   . GLY B 1 73  ? 50.565 -24.418 14.594 1.00 11.45 ? 72  GLY B O   1 
ATOM   1650 N  N   . GLY B 1 74  ? 50.358 -25.474 16.783 1.00 9.72  ? 73  GLY B N   1 
ATOM   1651 C  CA  . GLY B 1 74  ? 50.674 -26.739 15.984 1.00 8.75  ? 73  GLY B CA  1 
ATOM   1652 C  C   . GLY B 1 74  ? 49.246 -27.427 16.240 1.00 7.40  ? 73  GLY B C   1 
ATOM   1653 O  O   . GLY B 1 74  ? 48.492 -27.099 17.207 1.00 7.16  ? 73  GLY B O   1 
ATOM   1654 N  N   . PRO B 1 75  ? 48.876 -28.354 15.362 1.00 7.05  ? 74  PRO B N   1 
ATOM   1655 C  CA  . PRO B 1 75  ? 47.701 -29.207 15.463 1.00 5.57  ? 74  PRO B CA  1 
ATOM   1656 C  C   . PRO B 1 75  ? 47.750 -29.453 17.015 1.00 4.26  ? 74  PRO B C   1 
ATOM   1657 O  O   . PRO B 1 75  ? 46.871 -29.062 17.725 1.00 2.00  ? 74  PRO B O   1 
ATOM   1658 C  CB  . PRO B 1 75  ? 48.117 -30.454 14.733 1.00 2.00  ? 74  PRO B CB  1 
ATOM   1659 C  CG  . PRO B 1 75  ? 48.889 -29.931 13.612 1.00 2.00  ? 74  PRO B CG  1 
ATOM   1660 C  CD  . PRO B 1 75  ? 49.653 -28.766 14.168 1.00 5.34  ? 74  PRO B CD  1 
ATOM   1661 N  N   . LYS B 1 76  ? 48.829 -30.076 17.581 1.00 5.33  ? 75  LYS B N   1 
ATOM   1662 C  CA  . LYS B 1 76  ? 48.942 -30.304 19.047 1.00 8.11  ? 75  LYS B CA  1 
ATOM   1663 C  C   . LYS B 1 76  ? 50.155 -29.676 19.753 1.00 9.97  ? 75  LYS B C   1 
ATOM   1664 O  O   . LYS B 1 76  ? 50.839 -30.347 20.599 1.00 13.36 ? 75  LYS B O   1 
ATOM   1665 C  CB  . LYS B 1 76  ? 49.013 -31.795 19.415 1.00 7.13  ? 75  LYS B CB  1 
ATOM   1666 C  CG  . LYS B 1 76  ? 50.165 -32.472 18.594 1.00 7.93  ? 75  LYS B CG  1 
ATOM   1667 C  CD  . LYS B 1 76  ? 50.934 -33.362 19.636 1.00 8.61  ? 75  LYS B CD  1 
ATOM   1668 C  CE  . LYS B 1 76  ? 52.161 -34.016 18.991 1.00 7.16  ? 75  LYS B CE  1 
ATOM   1669 N  NZ  . LYS B 1 76  ? 53.043 -34.558 20.013 1.00 7.66  ? 75  LYS B NZ  1 
ATOM   1670 N  N   . ASP B 1 77  ? 50.641 -28.461 19.607 1.00 7.73  ? 76  ASP B N   1 
ATOM   1671 C  CA  . ASP B 1 77  ? 51.804 -28.063 20.368 1.00 7.17  ? 76  ASP B CA  1 
ATOM   1672 C  C   . ASP B 1 77  ? 51.250 -27.715 21.754 1.00 7.55  ? 76  ASP B C   1 
ATOM   1673 O  O   . ASP B 1 77  ? 50.023 -27.821 21.901 1.00 7.99  ? 76  ASP B O   1 
ATOM   1674 C  CB  . ASP B 1 77  ? 52.481 -26.794 19.837 1.00 5.96  ? 76  ASP B CB  1 
ATOM   1675 C  CG  . ASP B 1 77  ? 53.930 -26.613 20.435 1.00 7.24  ? 76  ASP B CG  1 
ATOM   1676 O  OD1 . ASP B 1 77  ? 54.685 -27.625 20.489 1.00 2.87  ? 76  ASP B OD1 1 
ATOM   1677 O  OD2 . ASP B 1 77  ? 54.311 -25.480 20.830 1.00 4.54  ? 76  ASP B OD2 1 
ATOM   1678 N  N   . GLU B 1 78  ? 52.159 -27.326 22.599 1.00 7.02  ? 77  GLU B N   1 
ATOM   1679 C  CA  . GLU B 1 78  ? 51.751 -26.860 23.968 1.00 7.33  ? 77  GLU B CA  1 
ATOM   1680 C  C   . GLU B 1 78  ? 51.384 -25.384 23.471 1.00 6.60  ? 77  GLU B C   1 
ATOM   1681 O  O   . GLU B 1 78  ? 50.294 -24.775 23.614 1.00 2.00  ? 77  GLU B O   1 
ATOM   1682 C  CB  . GLU B 1 78  ? 52.764 -27.010 25.060 1.00 7.26  ? 77  GLU B CB  1 
ATOM   1683 C  CG  . GLU B 1 78  ? 52.770 -26.508 26.473 1.00 6.95  ? 77  GLU B CG  1 
ATOM   1684 C  CD  . GLU B 1 78  ? 53.904 -26.657 27.477 1.00 6.67  ? 77  GLU B CD  1 
ATOM   1685 O  OE1 . GLU B 1 78  ? 53.867 -27.731 28.133 1.00 5.08  ? 77  GLU B OE1 1 
ATOM   1686 O  OE2 . GLU B 1 78  ? 54.771 -25.767 27.620 1.00 3.57  ? 77  GLU B OE2 1 
ATOM   1687 N  N   . GLU B 1 79  ? 52.342 -24.701 22.774 1.00 6.92  ? 78  GLU B N   1 
ATOM   1688 C  CA  . GLU B 1 79  ? 52.198 -23.344 22.242 1.00 6.66  ? 78  GLU B CA  1 
ATOM   1689 C  C   . GLU B 1 79  ? 51.572 -23.020 20.859 1.00 10.08 ? 78  GLU B C   1 
ATOM   1690 O  O   . GLU B 1 79  ? 52.214 -22.405 19.940 1.00 7.24  ? 78  GLU B O   1 
ATOM   1691 C  CB  . GLU B 1 79  ? 53.613 -22.795 22.219 1.00 4.30  ? 78  GLU B CB  1 
ATOM   1692 C  CG  . GLU B 1 79  ? 54.019 -22.219 23.610 1.00 2.71  ? 78  GLU B CG  1 
ATOM   1693 C  CD  . GLU B 1 79  ? 54.073 -20.736 23.718 1.00 4.44  ? 78  GLU B CD  1 
ATOM   1694 O  OE1 . GLU B 1 79  ? 53.480 -20.015 22.905 1.00 5.73  ? 78  GLU B OE1 1 
ATOM   1695 O  OE2 . GLU B 1 79  ? 54.753 -20.248 24.660 1.00 2.95  ? 78  GLU B OE2 1 
ATOM   1696 N  N   . ARG B 1 80  ? 50.260 -23.422 20.746 1.00 9.97  ? 79  ARG B N   1 
ATOM   1697 C  CA  . ARG B 1 80  ? 49.376 -23.313 19.662 1.00 10.52 ? 79  ARG B CA  1 
ATOM   1698 C  C   . ARG B 1 80  ? 48.232 -22.293 19.561 1.00 12.01 ? 79  ARG B C   1 
ATOM   1699 O  O   . ARG B 1 80  ? 47.191 -22.442 20.292 1.00 12.59 ? 79  ARG B O   1 
ATOM   1700 C  CB  . ARG B 1 80  ? 48.579 -24.654 19.576 1.00 13.18 ? 79  ARG B CB  1 
ATOM   1701 C  CG  . ARG B 1 80  ? 47.543 -25.140 20.483 1.00 13.51 ? 79  ARG B CG  1 
ATOM   1702 C  CD  . ARG B 1 80  ? 46.185 -25.013 20.713 1.00 13.54 ? 79  ARG B CD  1 
ATOM   1703 N  NE  . ARG B 1 80  ? 45.156 -25.503 19.803 1.00 14.97 ? 79  ARG B NE  1 
ATOM   1704 C  CZ  . ARG B 1 80  ? 44.860 -24.989 18.537 1.00 13.07 ? 79  ARG B CZ  1 
ATOM   1705 N  NH1 . ARG B 1 80  ? 45.524 -23.945 18.056 1.00 8.63  ? 79  ARG B NH1 1 
ATOM   1706 N  NH2 . ARG B 1 80  ? 43.893 -25.610 17.811 1.00 8.53  ? 79  ARG B NH2 1 
ATOM   1707 N  N   . HIS B 1 81  ? 48.340 -21.297 18.670 1.00 10.38 ? 80  HIS B N   1 
ATOM   1708 C  CA  . HIS B 1 81  ? 47.249 -20.230 18.479 1.00 9.32  ? 80  HIS B CA  1 
ATOM   1709 C  C   . HIS B 1 81  ? 45.912 -20.376 19.165 1.00 8.45  ? 80  HIS B C   1 
ATOM   1710 O  O   . HIS B 1 81  ? 45.725 -19.584 20.106 1.00 8.73  ? 80  HIS B O   1 
ATOM   1711 C  CB  . HIS B 1 81  ? 47.015 -20.136 16.982 1.00 5.38  ? 80  HIS B CB  1 
ATOM   1712 C  CG  . HIS B 1 81  ? 47.950 -19.151 16.446 1.00 6.32  ? 80  HIS B CG  1 
ATOM   1713 N  ND1 . HIS B 1 81  ? 49.000 -19.475 15.627 1.00 8.49  ? 80  HIS B ND1 1 
ATOM   1714 C  CD2 . HIS B 1 81  ? 48.023 -17.792 16.530 1.00 7.09  ? 80  HIS B CD2 1 
ATOM   1715 C  CE1 . HIS B 1 81  ? 49.693 -18.334 15.267 1.00 5.95  ? 80  HIS B CE1 1 
ATOM   1716 N  NE2 . HIS B 1 81  ? 49.084 -17.401 15.793 1.00 5.72  ? 80  HIS B NE2 1 
ATOM   1717 N  N   . VAL B 1 82  ? 44.999 -21.172 18.884 1.00 6.08  ? 81  VAL B N   1 
ATOM   1718 C  CA  . VAL B 1 82  ? 43.709 -21.574 19.396 1.00 9.94  ? 81  VAL B CA  1 
ATOM   1719 C  C   . VAL B 1 82  ? 42.866 -21.854 18.156 1.00 10.87 ? 81  VAL B C   1 
ATOM   1720 O  O   . VAL B 1 82  ? 42.113 -22.720 18.106 1.00 9.34  ? 81  VAL B O   1 
ATOM   1721 C  CB  . VAL B 1 82  ? 42.809 -20.747 20.400 1.00 9.71  ? 81  VAL B CB  1 
ATOM   1722 C  CG1 . VAL B 1 82  ? 41.468 -21.422 20.662 1.00 7.20  ? 81  VAL B CG1 1 
ATOM   1723 C  CG2 . VAL B 1 82  ? 43.380 -20.456 21.755 1.00 8.24  ? 81  VAL B CG2 1 
ATOM   1724 N  N   . GLY B 1 83  ? 43.219 -20.904 17.281 1.00 16.06 ? 82  GLY B N   1 
ATOM   1725 C  CA  . GLY B 1 83  ? 42.516 -20.947 15.966 1.00 16.61 ? 82  GLY B CA  1 
ATOM   1726 C  C   . GLY B 1 83  ? 43.123 -21.886 14.959 1.00 15.36 ? 82  GLY B C   1 
ATOM   1727 O  O   . GLY B 1 83  ? 42.377 -22.291 14.085 1.00 14.37 ? 82  GLY B O   1 
ATOM   1728 N  N   . ASP B 1 84  ? 44.415 -22.225 14.980 1.00 17.46 ? 83  ASP B N   1 
ATOM   1729 C  CA  . ASP B 1 84  ? 45.045 -23.158 13.993 1.00 15.52 ? 83  ASP B CA  1 
ATOM   1730 C  C   . ASP B 1 84  ? 44.741 -24.568 14.520 1.00 11.39 ? 83  ASP B C   1 
ATOM   1731 O  O   . ASP B 1 84  ? 44.987 -24.744 15.703 1.00 10.75 ? 83  ASP B O   1 
ATOM   1732 C  CB  . ASP B 1 84  ? 46.569 -23.119 13.708 1.00 15.41 ? 83  ASP B CB  1 
ATOM   1733 C  CG  . ASP B 1 84  ? 47.274 -22.412 14.865 1.00 15.89 ? 83  ASP B CG  1 
ATOM   1734 O  OD1 . ASP B 1 84  ? 46.833 -22.831 15.955 1.00 17.95 ? 83  ASP B OD1 1 
ATOM   1735 O  OD2 . ASP B 1 84  ? 48.152 -21.516 14.707 1.00 13.79 ? 83  ASP B OD2 1 
ATOM   1736 N  N   . LEU B 1 85  ? 44.270 -25.331 13.632 1.00 10.32 ? 84  LEU B N   1 
ATOM   1737 C  CA  . LEU B 1 85  ? 43.919 -26.712 13.977 1.00 9.38  ? 84  LEU B CA  1 
ATOM   1738 C  C   . LEU B 1 85  ? 44.796 -27.500 13.053 1.00 10.58 ? 84  LEU B C   1 
ATOM   1739 O  O   . LEU B 1 85  ? 44.634 -28.703 12.931 1.00 14.06 ? 84  LEU B O   1 
ATOM   1740 C  CB  . LEU B 1 85  ? 42.443 -27.040 13.871 1.00 8.14  ? 84  LEU B CB  1 
ATOM   1741 C  CG  . LEU B 1 85  ? 41.350 -25.954 14.021 1.00 7.17  ? 84  LEU B CG  1 
ATOM   1742 C  CD1 . LEU B 1 85  ? 40.011 -26.557 13.582 1.00 3.26  ? 84  LEU B CD1 1 
ATOM   1743 C  CD2 . LEU B 1 85  ? 41.463 -25.441 15.464 1.00 5.91  ? 84  LEU B CD2 1 
ATOM   1744 N  N   . GLY B 1 86  ? 45.683 -26.819 12.414 1.00 10.86 ? 85  GLY B N   1 
ATOM   1745 C  CA  . GLY B 1 86  ? 46.683 -27.538 11.529 1.00 8.43  ? 85  GLY B CA  1 
ATOM   1746 C  C   . GLY B 1 86  ? 46.683 -27.556 10.011 1.00 9.62  ? 85  GLY B C   1 
ATOM   1747 O  O   . GLY B 1 86  ? 46.909 -26.679 9.076  1.00 5.11  ? 85  GLY B O   1 
ATOM   1748 N  N   . ASN B 1 87  ? 46.372 -28.820 9.666  1.00 8.67  ? 86  ASN B N   1 
ATOM   1749 C  CA  . ASN B 1 87  ? 46.391 -29.260 8.245  1.00 10.76 ? 86  ASN B CA  1 
ATOM   1750 C  C   . ASN B 1 87  ? 45.341 -30.263 7.959  1.00 9.18  ? 86  ASN B C   1 
ATOM   1751 O  O   . ASN B 1 87  ? 44.845 -30.812 8.948  1.00 9.00  ? 86  ASN B O   1 
ATOM   1752 C  CB  . ASN B 1 87  ? 47.893 -29.677 8.097  1.00 11.40 ? 86  ASN B CB  1 
ATOM   1753 C  CG  . ASN B 1 87  ? 48.616 -29.667 6.787  1.00 14.43 ? 86  ASN B CG  1 
ATOM   1754 O  OD1 . ASN B 1 87  ? 49.173 -30.763 6.348  1.00 13.49 ? 86  ASN B OD1 1 
ATOM   1755 N  ND2 . ASN B 1 87  ? 48.726 -28.499 6.084  1.00 13.01 ? 86  ASN B ND2 1 
ATOM   1756 N  N   . VAL B 1 88  ? 45.070 -30.386 6.697  1.00 8.01  ? 87  VAL B N   1 
ATOM   1757 C  CA  . VAL B 1 88  ? 43.993 -31.288 6.182  1.00 8.25  ? 87  VAL B CA  1 
ATOM   1758 C  C   . VAL B 1 88  ? 44.518 -31.938 4.917  1.00 10.18 ? 87  VAL B C   1 
ATOM   1759 O  O   . VAL B 1 88  ? 45.400 -31.310 4.198  1.00 10.82 ? 87  VAL B O   1 
ATOM   1760 C  CB  . VAL B 1 88  ? 42.784 -30.313 6.183  1.00 7.00  ? 87  VAL B CB  1 
ATOM   1761 C  CG1 . VAL B 1 88  ? 42.083 -29.724 7.352  1.00 4.71  ? 87  VAL B CG1 1 
ATOM   1762 C  CG2 . VAL B 1 88  ? 43.331 -28.991 5.629  1.00 5.75  ? 87  VAL B CG2 1 
ATOM   1763 N  N   . THR B 1 89  ? 44.048 -33.174 4.584  1.00 8.85  ? 88  THR B N   1 
ATOM   1764 C  CA  . THR B 1 89  ? 44.570 -33.851 3.380  1.00 7.01  ? 88  THR B CA  1 
ATOM   1765 C  C   . THR B 1 89  ? 43.621 -33.917 2.212  1.00 6.42  ? 88  THR B C   1 
ATOM   1766 O  O   . THR B 1 89  ? 42.658 -34.735 2.212  1.00 7.76  ? 88  THR B O   1 
ATOM   1767 C  CB  . THR B 1 89  ? 45.149 -35.309 3.745  1.00 8.95  ? 88  THR B CB  1 
ATOM   1768 O  OG1 . THR B 1 89  ? 44.651 -35.928 5.032  1.00 8.98  ? 88  THR B OG1 1 
ATOM   1769 C  CG2 . THR B 1 89  ? 46.665 -35.458 3.874  1.00 9.43  ? 88  THR B CG2 1 
ATOM   1770 N  N   . ALA B 1 90  ? 43.905 -33.091 1.163  1.00 4.19  ? 89  ALA B N   1 
ATOM   1771 C  CA  . ALA B 1 90  ? 42.934 -33.166 0.015  1.00 3.97  ? 89  ALA B CA  1 
ATOM   1772 C  C   . ALA B 1 90  ? 43.241 -34.278 -1.007 1.00 4.32  ? 89  ALA B C   1 
ATOM   1773 O  O   . ALA B 1 90  ? 43.883 -33.987 -2.035 1.00 2.00  ? 89  ALA B O   1 
ATOM   1774 C  CB  . ALA B 1 90  ? 42.920 -31.845 -0.737 1.00 4.01  ? 89  ALA B CB  1 
ATOM   1775 N  N   . ASP B 1 91  ? 42.722 -35.476 -0.622 1.00 4.69  ? 90  ASP B N   1 
ATOM   1776 C  CA  . ASP B 1 91  ? 42.922 -36.765 -1.454 1.00 3.65  ? 90  ASP B CA  1 
ATOM   1777 C  C   . ASP B 1 91  ? 42.871 -36.361 -2.888 1.00 4.57  ? 90  ASP B C   1 
ATOM   1778 O  O   . ASP B 1 91  ? 41.816 -35.707 -3.253 1.00 6.95  ? 90  ASP B O   1 
ATOM   1779 C  CB  . ASP B 1 91  ? 41.903 -37.794 -1.063 1.00 3.40  ? 90  ASP B CB  1 
ATOM   1780 C  CG  . ASP B 1 91  ? 42.289 -39.174 -1.552 1.00 2.00  ? 90  ASP B CG  1 
ATOM   1781 O  OD1 . ASP B 1 91  ? 43.488 -39.501 -1.445 1.00 2.00  ? 90  ASP B OD1 1 
ATOM   1782 O  OD2 . ASP B 1 91  ? 41.348 -39.792 -1.995 1.00 2.00  ? 90  ASP B OD2 1 
ATOM   1783 N  N   . LYS B 1 92  ? 43.865 -36.734 -3.615 1.00 4.40  ? 91  LYS B N   1 
ATOM   1784 C  CA  . LYS B 1 92  ? 44.188 -36.457 -4.996 1.00 3.63  ? 91  LYS B CA  1 
ATOM   1785 C  C   . LYS B 1 92  ? 43.400 -35.292 -5.668 1.00 3.89  ? 91  LYS B C   1 
ATOM   1786 O  O   . LYS B 1 92  ? 44.137 -34.300 -6.041 1.00 4.60  ? 91  LYS B O   1 
ATOM   1787 C  CB  . LYS B 1 92  ? 44.027 -37.497 -6.150 1.00 4.51  ? 91  LYS B CB  1 
ATOM   1788 C  CG  . LYS B 1 92  ? 44.592 -36.909 -7.500 1.00 3.50  ? 91  LYS B CG  1 
ATOM   1789 C  CD  . LYS B 1 92  ? 46.078 -37.258 -7.776 1.00 3.65  ? 91  LYS B CD  1 
ATOM   1790 C  CE  . LYS B 1 92  ? 46.910 -36.120 -8.350 1.00 3.40  ? 91  LYS B CE  1 
ATOM   1791 N  NZ  . LYS B 1 92  ? 46.588 -34.859 -7.563 1.00 3.71  ? 91  LYS B NZ  1 
ATOM   1792 N  N   . ASP B 1 93  ? 42.144 -35.439 -5.879 1.00 4.53  ? 92  ASP B N   1 
ATOM   1793 C  CA  . ASP B 1 93  ? 41.369 -34.371 -6.576 1.00 9.06  ? 92  ASP B CA  1 
ATOM   1794 C  C   . ASP B 1 93  ? 40.788 -33.217 -5.823 1.00 10.03 ? 92  ASP B C   1 
ATOM   1795 O  O   . ASP B 1 93  ? 39.932 -32.524 -6.383 1.00 10.68 ? 92  ASP B O   1 
ATOM   1796 C  CB  . ASP B 1 93  ? 40.289 -35.097 -7.403 1.00 10.01 ? 92  ASP B CB  1 
ATOM   1797 C  CG  . ASP B 1 93  ? 41.149 -35.879 -8.452 1.00 9.79  ? 92  ASP B CG  1 
ATOM   1798 O  OD1 . ASP B 1 93  ? 41.934 -35.242 -9.164 1.00 9.53  ? 92  ASP B OD1 1 
ATOM   1799 O  OD2 . ASP B 1 93  ? 40.947 -37.098 -8.409 1.00 10.76 ? 92  ASP B OD2 1 
ATOM   1800 N  N   . GLY B 1 94  ? 41.288 -33.163 -4.637 1.00 11.40 ? 93  GLY B N   1 
ATOM   1801 C  CA  . GLY B 1 94  ? 41.137 -32.258 -3.613 1.00 10.87 ? 93  GLY B CA  1 
ATOM   1802 C  C   . GLY B 1 94  ? 39.847 -32.177 -2.893 1.00 11.87 ? 93  GLY B C   1 
ATOM   1803 O  O   . GLY B 1 94  ? 39.303 -30.972 -2.808 1.00 10.77 ? 93  GLY B O   1 
ATOM   1804 N  N   . VAL B 1 95  ? 39.502 -33.406 -2.468 1.00 10.23 ? 94  VAL B N   1 
ATOM   1805 C  CA  . VAL B 1 95  ? 38.232 -33.391 -1.706 1.00 7.07  ? 94  VAL B CA  1 
ATOM   1806 C  C   . VAL B 1 95  ? 38.876 -33.614 -0.342 1.00 6.12  ? 94  VAL B C   1 
ATOM   1807 O  O   . VAL B 1 95  ? 39.810 -34.442 -0.317 1.00 4.58  ? 94  VAL B O   1 
ATOM   1808 C  CB  . VAL B 1 95  ? 37.152 -34.405 -1.984 1.00 7.70  ? 94  VAL B CB  1 
ATOM   1809 C  CG1 . VAL B 1 95  ? 36.692 -34.462 -3.457 1.00 7.77  ? 94  VAL B CG1 1 
ATOM   1810 C  CG2 . VAL B 1 95  ? 37.467 -35.863 -1.563 1.00 7.75  ? 94  VAL B CG2 1 
ATOM   1811 N  N   . ALA B 1 96  ? 38.371 -32.893 0.635  1.00 5.66  ? 95  ALA B N   1 
ATOM   1812 C  CA  . ALA B 1 96  ? 39.047 -33.212 1.933  1.00 4.53  ? 95  ALA B CA  1 
ATOM   1813 C  C   . ALA B 1 96  ? 37.886 -33.497 2.906  1.00 5.70  ? 95  ALA B C   1 
ATOM   1814 O  O   . ALA B 1 96  ? 37.128 -32.587 3.329  1.00 2.89  ? 95  ALA B O   1 
ATOM   1815 C  CB  . ALA B 1 96  ? 39.926 -32.195 2.624  1.00 4.49  ? 95  ALA B CB  1 
ATOM   1816 N  N   . ASP B 1 97  ? 37.868 -34.817 3.159  1.00 5.21  ? 96  ASP B N   1 
ATOM   1817 C  CA  . ASP B 1 97  ? 36.896 -35.411 4.073  1.00 7.18  ? 96  ASP B CA  1 
ATOM   1818 C  C   . ASP B 1 97  ? 37.712 -35.059 5.390  1.00 8.25  ? 96  ASP B C   1 
ATOM   1819 O  O   . ASP B 1 97  ? 38.961 -35.232 5.286  1.00 7.59  ? 96  ASP B O   1 
ATOM   1820 C  CB  . ASP B 1 97  ? 36.581 -36.870 3.960  1.00 7.12  ? 96  ASP B CB  1 
ATOM   1821 C  CG  . ASP B 1 97  ? 36.719 -37.393 2.495  1.00 7.42  ? 96  ASP B CG  1 
ATOM   1822 O  OD1 . ASP B 1 97  ? 36.062 -36.757 1.663  1.00 5.33  ? 96  ASP B OD1 1 
ATOM   1823 O  OD2 . ASP B 1 97  ? 37.452 -38.402 2.299  1.00 5.27  ? 96  ASP B OD2 1 
ATOM   1824 N  N   . VAL B 1 98  ? 36.906 -34.587 6.371  1.00 4.61  ? 97  VAL B N   1 
ATOM   1825 C  CA  . VAL B 1 98  ? 37.909 -34.292 7.500  1.00 4.86  ? 97  VAL B CA  1 
ATOM   1826 C  C   . VAL B 1 98  ? 37.436 -34.696 8.843  1.00 5.67  ? 97  VAL B C   1 
ATOM   1827 O  O   . VAL B 1 98  ? 36.176 -34.980 8.924  1.00 10.00 ? 97  VAL B O   1 
ATOM   1828 C  CB  . VAL B 1 98  ? 38.174 -32.807 7.679  1.00 5.32  ? 97  VAL B CB  1 
ATOM   1829 C  CG1 . VAL B 1 98  ? 39.511 -32.660 8.432  1.00 8.50  ? 97  VAL B CG1 1 
ATOM   1830 C  CG2 . VAL B 1 98  ? 38.136 -32.030 6.424  1.00 6.40  ? 97  VAL B CG2 1 
ATOM   1831 N  N   . SER B 1 99  ? 38.247 -34.677 9.820  1.00 7.37  ? 98  SER B N   1 
ATOM   1832 C  CA  . SER B 1 99  ? 37.922 -35.008 11.209 1.00 6.15  ? 98  SER B CA  1 
ATOM   1833 C  C   . SER B 1 99  ? 38.950 -34.456 12.181 1.00 5.78  ? 98  SER B C   1 
ATOM   1834 O  O   . SER B 1 99  ? 40.139 -34.699 11.972 1.00 5.40  ? 98  SER B O   1 
ATOM   1835 C  CB  . SER B 1 99  ? 37.816 -36.519 11.421 1.00 5.19  ? 98  SER B CB  1 
ATOM   1836 O  OG  . SER B 1 99  ? 37.252 -37.017 10.177 1.00 2.97  ? 98  SER B OG  1 
ATOM   1837 N  N   . ILE B 1 100 ? 38.557 -33.757 13.177 1.00 6.41  ? 99  ILE B N   1 
ATOM   1838 C  CA  . ILE B 1 100 ? 39.439 -33.201 14.252 1.00 5.65  ? 99  ILE B CA  1 
ATOM   1839 C  C   . ILE B 1 100 ? 38.591 -33.464 15.575 1.00 7.76  ? 99  ILE B C   1 
ATOM   1840 O  O   . ILE B 1 100 ? 37.321 -33.529 15.472 1.00 5.28  ? 99  ILE B O   1 
ATOM   1841 C  CB  . ILE B 1 100 ? 39.969 -31.720 14.351 1.00 2.00  ? 99  ILE B CB  1 
ATOM   1842 C  CG1 . ILE B 1 100 ? 41.357 -31.651 13.818 1.00 2.00  ? 99  ILE B CG1 1 
ATOM   1843 C  CG2 . ILE B 1 100 ? 40.061 -31.021 15.759 1.00 2.00  ? 99  ILE B CG2 1 
ATOM   1844 C  CD1 . ILE B 1 100 ? 42.075 -30.301 13.703 1.00 2.00  ? 99  ILE B CD1 1 
ATOM   1845 N  N   . GLU B 1 101 ? 39.386 -33.591 16.627 1.00 7.27  ? 100 GLU B N   1 
ATOM   1846 C  CA  . GLU B 1 101 ? 38.952 -33.784 17.996 1.00 9.45  ? 100 GLU B CA  1 
ATOM   1847 C  C   . GLU B 1 101 ? 40.095 -32.975 18.680 1.00 12.33 ? 100 GLU B C   1 
ATOM   1848 O  O   . GLU B 1 101 ? 41.275 -33.425 18.717 1.00 15.13 ? 100 GLU B O   1 
ATOM   1849 C  CB  . GLU B 1 101 ? 39.029 -35.006 18.848 1.00 10.63 ? 100 GLU B CB  1 
ATOM   1850 C  CG  . GLU B 1 101 ? 38.442 -34.758 20.269 1.00 10.53 ? 100 GLU B CG  1 
ATOM   1851 C  CD  . GLU B 1 101 ? 37.113 -35.499 20.449 1.00 14.17 ? 100 GLU B CD  1 
ATOM   1852 O  OE1 . GLU B 1 101 ? 37.232 -36.784 20.414 1.00 12.34 ? 100 GLU B OE1 1 
ATOM   1853 O  OE2 . GLU B 1 101 ? 36.029 -34.804 20.604 1.00 11.11 ? 100 GLU B OE2 1 
ATOM   1854 N  N   . ASP B 1 102 ? 39.732 -31.820 19.190 1.00 13.75 ? 101 ASP B N   1 
ATOM   1855 C  CA  . ASP B 1 102 ? 40.895 -31.070 19.834 1.00 11.65 ? 101 ASP B CA  1 
ATOM   1856 C  C   . ASP B 1 102 ? 40.058 -30.403 20.932 1.00 13.10 ? 101 ASP B C   1 
ATOM   1857 O  O   . ASP B 1 102 ? 38.935 -30.103 20.548 1.00 10.29 ? 101 ASP B O   1 
ATOM   1858 C  CB  . ASP B 1 102 ? 41.708 -30.029 19.096 1.00 10.42 ? 101 ASP B CB  1 
ATOM   1859 C  CG  . ASP B 1 102 ? 41.910 -28.695 19.790 1.00 7.72  ? 101 ASP B CG  1 
ATOM   1860 O  OD1 . ASP B 1 102 ? 40.942 -27.990 19.761 1.00 6.71  ? 101 ASP B OD1 1 
ATOM   1861 O  OD2 . ASP B 1 102 ? 42.956 -28.272 20.394 1.00 10.05 ? 101 ASP B OD2 1 
ATOM   1862 N  N   . SER B 1 103 ? 40.823 -30.397 21.979 1.00 14.39 ? 102 SER B N   1 
ATOM   1863 C  CA  . SER B 1 103 ? 40.736 -29.929 23.305 1.00 13.25 ? 102 SER B CA  1 
ATOM   1864 C  C   . SER B 1 103 ? 40.162 -28.539 23.385 1.00 12.34 ? 102 SER B C   1 
ATOM   1865 O  O   . SER B 1 103 ? 39.077 -28.195 23.802 1.00 12.86 ? 102 SER B O   1 
ATOM   1866 C  CB  . SER B 1 103 ? 42.237 -29.849 23.822 1.00 14.48 ? 102 SER B CB  1 
ATOM   1867 O  OG  . SER B 1 103 ? 42.999 -30.989 23.323 1.00 14.10 ? 102 SER B OG  1 
ATOM   1868 N  N   . VAL B 1 104 ? 41.002 -27.663 22.889 1.00 11.40 ? 103 VAL B N   1 
ATOM   1869 C  CA  . VAL B 1 104 ? 40.938 -26.231 22.767 1.00 10.22 ? 103 VAL B CA  1 
ATOM   1870 C  C   . VAL B 1 104 ? 39.794 -25.600 22.017 1.00 10.10 ? 103 VAL B C   1 
ATOM   1871 O  O   . VAL B 1 104 ? 39.439 -24.487 22.483 1.00 12.07 ? 103 VAL B O   1 
ATOM   1872 C  CB  . VAL B 1 104 ? 42.360 -25.807 22.156 1.00 9.56  ? 103 VAL B CB  1 
ATOM   1873 C  CG1 . VAL B 1 104 ? 42.508 -24.346 21.712 1.00 8.72  ? 103 VAL B CG1 1 
ATOM   1874 C  CG2 . VAL B 1 104 ? 43.498 -26.157 23.086 1.00 8.22  ? 103 VAL B CG2 1 
ATOM   1875 N  N   . ILE B 1 105 ? 39.248 -26.192 20.967 1.00 8.83  ? 104 ILE B N   1 
ATOM   1876 C  CA  . ILE B 1 105 ? 38.155 -25.385 20.312 1.00 8.83  ? 104 ILE B CA  1 
ATOM   1877 C  C   . ILE B 1 105 ? 36.712 -25.497 20.615 1.00 9.78  ? 104 ILE B C   1 
ATOM   1878 O  O   . ILE B 1 105 ? 35.715 -25.605 19.906 1.00 8.94  ? 104 ILE B O   1 
ATOM   1879 C  CB  . ILE B 1 105 ? 38.621 -25.665 18.830 1.00 7.39  ? 104 ILE B CB  1 
ATOM   1880 C  CG1 . ILE B 1 105 ? 39.620 -24.466 18.646 1.00 5.37  ? 104 ILE B CG1 1 
ATOM   1881 C  CG2 . ILE B 1 105 ? 37.605 -25.693 17.727 1.00 7.15  ? 104 ILE B CG2 1 
ATOM   1882 C  CD1 . ILE B 1 105 ? 38.671 -23.199 18.440 1.00 5.19  ? 104 ILE B CD1 1 
ATOM   1883 N  N   . SER B 1 106 ? 36.477 -25.415 21.939 1.00 12.74 ? 105 SER B N   1 
ATOM   1884 C  CA  . SER B 1 106 ? 35.250 -25.454 22.731 1.00 8.36  ? 105 SER B CA  1 
ATOM   1885 C  C   . SER B 1 106 ? 34.310 -24.327 22.349 1.00 5.25  ? 105 SER B C   1 
ATOM   1886 O  O   . SER B 1 106 ? 34.953 -23.369 21.936 1.00 4.65  ? 105 SER B O   1 
ATOM   1887 C  CB  . SER B 1 106 ? 35.611 -25.293 24.200 1.00 7.03  ? 105 SER B CB  1 
ATOM   1888 O  OG  . SER B 1 106 ? 34.650 -26.014 24.908 1.00 6.05  ? 105 SER B OG  1 
ATOM   1889 N  N   . LEU B 1 107 ? 33.041 -24.445 22.482 1.00 4.25  ? 106 LEU B N   1 
ATOM   1890 C  CA  . LEU B 1 107 ? 32.120 -23.384 22.135 1.00 6.45  ? 106 LEU B CA  1 
ATOM   1891 C  C   . LEU B 1 107 ? 31.062 -23.011 23.184 1.00 6.07  ? 106 LEU B C   1 
ATOM   1892 O  O   . LEU B 1 107 ? 29.869 -22.923 22.721 1.00 4.45  ? 106 LEU B O   1 
ATOM   1893 C  CB  . LEU B 1 107 ? 31.446 -23.688 20.734 1.00 8.07  ? 106 LEU B CB  1 
ATOM   1894 C  CG  . LEU B 1 107 ? 30.932 -25.082 20.443 1.00 10.90 ? 106 LEU B CG  1 
ATOM   1895 C  CD1 . LEU B 1 107 ? 30.197 -25.744 21.612 1.00 11.76 ? 106 LEU B CD1 1 
ATOM   1896 C  CD2 . LEU B 1 107 ? 29.974 -24.957 19.224 1.00 11.10 ? 106 LEU B CD2 1 
ATOM   1897 N  N   . SER B 1 108 ? 31.448 -22.787 24.488 1.00 5.07  ? 107 SER B N   1 
ATOM   1898 C  CA  . SER B 1 108 ? 30.293 -22.417 25.405 1.00 2.13  ? 107 SER B CA  1 
ATOM   1899 C  C   . SER B 1 108 ? 30.909 -21.714 26.577 1.00 2.00  ? 107 SER B C   1 
ATOM   1900 O  O   . SER B 1 108 ? 31.404 -20.691 26.109 1.00 2.00  ? 107 SER B O   1 
ATOM   1901 C  CB  . SER B 1 108 ? 29.334 -23.461 25.903 1.00 4.48  ? 107 SER B CB  1 
ATOM   1902 O  OG  . SER B 1 108 ? 28.046 -23.819 25.345 1.00 2.00  ? 107 SER B OG  1 
ATOM   1903 N  N   . GLY B 1 109 ? 30.851 -22.196 27.784 1.00 2.56  ? 108 GLY B N   1 
ATOM   1904 C  CA  . GLY B 1 109 ? 31.326 -21.667 29.089 1.00 3.31  ? 108 GLY B CA  1 
ATOM   1905 C  C   . GLY B 1 109 ? 32.658 -21.010 29.162 1.00 5.89  ? 108 GLY B C   1 
ATOM   1906 O  O   . GLY B 1 109 ? 33.647 -21.604 29.635 1.00 2.88  ? 108 GLY B O   1 
ATOM   1907 N  N   . ASP B 1 110 ? 32.625 -19.720 28.677 1.00 8.18  ? 109 ASP B N   1 
ATOM   1908 C  CA  . ASP B 1 110 ? 33.731 -18.796 28.525 1.00 7.98  ? 109 ASP B CA  1 
ATOM   1909 C  C   . ASP B 1 110 ? 34.365 -19.268 27.163 1.00 9.25  ? 109 ASP B C   1 
ATOM   1910 O  O   . ASP B 1 110 ? 33.974 -20.454 26.877 1.00 10.19 ? 109 ASP B O   1 
ATOM   1911 C  CB  . ASP B 1 110 ? 34.825 -18.833 29.587 1.00 6.60  ? 109 ASP B CB  1 
ATOM   1912 C  CG  . ASP B 1 110 ? 36.082 -17.982 29.456 1.00 8.42  ? 109 ASP B CG  1 
ATOM   1913 O  OD1 . ASP B 1 110 ? 36.439 -17.620 28.233 1.00 7.87  ? 109 ASP B OD1 1 
ATOM   1914 O  OD2 . ASP B 1 110 ? 36.743 -17.655 30.477 1.00 2.92  ? 109 ASP B OD2 1 
ATOM   1915 N  N   . HIS B 1 111 ? 35.189 -18.584 26.422 1.00 10.20 ? 110 HIS B N   1 
ATOM   1916 C  CA  . HIS B 1 111 ? 35.878 -18.975 25.170 1.00 10.58 ? 110 HIS B CA  1 
ATOM   1917 C  C   . HIS B 1 111 ? 35.181 -19.477 23.908 1.00 10.57 ? 110 HIS B C   1 
ATOM   1918 O  O   . HIS B 1 111 ? 35.961 -20.090 23.037 1.00 6.38  ? 110 HIS B O   1 
ATOM   1919 C  CB  . HIS B 1 111 ? 36.870 -20.166 25.621 1.00 10.97 ? 110 HIS B CB  1 
ATOM   1920 C  CG  . HIS B 1 111 ? 38.236 -20.574 25.182 1.00 12.98 ? 110 HIS B CG  1 
ATOM   1921 N  ND1 . HIS B 1 111 ? 38.653 -21.863 24.729 1.00 13.46 ? 110 HIS B ND1 1 
ATOM   1922 C  CD2 . HIS B 1 111 ? 39.407 -19.872 25.132 1.00 11.90 ? 110 HIS B CD2 1 
ATOM   1923 C  CE1 . HIS B 1 111 ? 39.951 -21.894 24.456 1.00 11.87 ? 110 HIS B CE1 1 
ATOM   1924 N  NE2 . HIS B 1 111 ? 40.435 -20.698 24.675 1.00 10.98 ? 110 HIS B NE2 1 
ATOM   1925 N  N   . CYS B 1 112 ? 33.873 -19.319 23.673 1.00 7.82  ? 111 CYS B N   1 
ATOM   1926 C  CA  . CYS B 1 112 ? 33.108 -19.790 22.530 1.00 7.98  ? 111 CYS B CA  1 
ATOM   1927 C  C   . CYS B 1 112 ? 33.505 -19.127 21.198 1.00 7.82  ? 111 CYS B C   1 
ATOM   1928 O  O   . CYS B 1 112 ? 33.647 -17.958 21.112 1.00 6.76  ? 111 CYS B O   1 
ATOM   1929 C  CB  . CYS B 1 112 ? 31.602 -19.632 22.758 1.00 10.01 ? 111 CYS B CB  1 
ATOM   1930 S  SG  . CYS B 1 112 ? 30.701 -20.304 21.220 1.00 10.02 ? 111 CYS B SG  1 
ATOM   1931 N  N   . ILE B 1 113 ? 33.656 -19.990 20.183 1.00 8.45  ? 112 ILE B N   1 
ATOM   1932 C  CA  . ILE B 1 113 ? 34.073 -19.303 18.908 1.00 8.94  ? 112 ILE B CA  1 
ATOM   1933 C  C   . ILE B 1 113 ? 33.033 -18.975 17.853 1.00 8.71  ? 112 ILE B C   1 
ATOM   1934 O  O   . ILE B 1 113 ? 33.448 -18.527 16.746 1.00 8.43  ? 112 ILE B O   1 
ATOM   1935 C  CB  . ILE B 1 113 ? 35.352 -20.201 18.490 1.00 7.39  ? 112 ILE B CB  1 
ATOM   1936 C  CG1 . ILE B 1 113 ? 34.742 -21.524 18.041 1.00 8.92  ? 112 ILE B CG1 1 
ATOM   1937 C  CG2 . ILE B 1 113 ? 36.322 -20.102 19.680 1.00 2.00  ? 112 ILE B CG2 1 
ATOM   1938 C  CD1 . ILE B 1 113 ? 35.387 -22.145 16.724 1.00 9.57  ? 112 ILE B CD1 1 
ATOM   1939 N  N   . ILE B 1 114 ? 31.760 -19.162 18.135 1.00 7.27  ? 113 ILE B N   1 
ATOM   1940 C  CA  . ILE B 1 114 ? 30.697 -18.840 17.195 1.00 5.97  ? 113 ILE B CA  1 
ATOM   1941 C  C   . ILE B 1 114 ? 30.904 -17.315 16.961 1.00 5.04  ? 113 ILE B C   1 
ATOM   1942 O  O   . ILE B 1 114 ? 31.438 -16.451 17.715 1.00 4.34  ? 113 ILE B O   1 
ATOM   1943 C  CB  . ILE B 1 114 ? 29.335 -19.285 17.715 1.00 8.85  ? 113 ILE B CB  1 
ATOM   1944 C  CG1 . ILE B 1 114 ? 29.082 -20.803 17.600 1.00 9.46  ? 113 ILE B CG1 1 
ATOM   1945 C  CG2 . ILE B 1 114 ? 28.110 -18.514 17.025 1.00 7.59  ? 113 ILE B CG2 1 
ATOM   1946 C  CD1 . ILE B 1 114 ? 29.669 -21.770 18.644 1.00 10.53 ? 113 ILE B CD1 1 
ATOM   1947 N  N   . GLY B 1 115 ? 30.475 -16.904 15.793 1.00 3.72  ? 114 GLY B N   1 
ATOM   1948 C  CA  . GLY B 1 115 ? 30.566 -15.564 15.307 1.00 3.17  ? 114 GLY B CA  1 
ATOM   1949 C  C   . GLY B 1 115 ? 31.953 -15.274 14.739 1.00 3.81  ? 114 GLY B C   1 
ATOM   1950 O  O   . GLY B 1 115 ? 32.319 -14.109 14.532 1.00 3.29  ? 114 GLY B O   1 
ATOM   1951 N  N   . ARG B 1 116 ? 32.735 -16.269 14.452 1.00 5.52  ? 115 ARG B N   1 
ATOM   1952 C  CA  . ARG B 1 116 ? 34.079 -16.223 13.925 1.00 6.62  ? 115 ARG B CA  1 
ATOM   1953 C  C   . ARG B 1 116 ? 34.158 -17.049 12.622 1.00 5.60  ? 115 ARG B C   1 
ATOM   1954 O  O   . ARG B 1 116 ? 33.264 -17.838 12.272 1.00 2.00  ? 115 ARG B O   1 
ATOM   1955 C  CB  . ARG B 1 116 ? 35.211 -16.696 14.886 1.00 7.52  ? 115 ARG B CB  1 
ATOM   1956 C  CG  . ARG B 1 116 ? 34.896 -16.164 16.340 1.00 10.54 ? 115 ARG B CG  1 
ATOM   1957 C  CD  . ARG B 1 116 ? 35.981 -16.754 17.237 1.00 11.82 ? 115 ARG B CD  1 
ATOM   1958 N  NE  . ARG B 1 116 ? 35.655 -16.576 18.626 1.00 10.70 ? 115 ARG B NE  1 
ATOM   1959 C  CZ  . ARG B 1 116 ? 35.585 -15.406 19.259 1.00 14.14 ? 115 ARG B CZ  1 
ATOM   1960 N  NH1 . ARG B 1 116 ? 36.026 -14.275 18.620 1.00 12.53 ? 115 ARG B NH1 1 
ATOM   1961 N  NH2 . ARG B 1 116 ? 35.082 -15.447 20.531 1.00 13.10 ? 115 ARG B NH2 1 
ATOM   1962 N  N   . THR B 1 117 ? 35.340 -16.686 12.062 1.00 4.43  ? 116 THR B N   1 
ATOM   1963 C  CA  . THR B 1 117 ? 35.623 -17.295 10.816 1.00 4.59  ? 116 THR B CA  1 
ATOM   1964 C  C   . THR B 1 117 ? 36.641 -18.393 10.906 1.00 5.86  ? 116 THR B C   1 
ATOM   1965 O  O   . THR B 1 117 ? 37.495 -18.338 11.737 1.00 6.73  ? 116 THR B O   1 
ATOM   1966 C  CB  . THR B 1 117 ? 36.249 -16.250 9.835  1.00 3.39  ? 116 THR B CB  1 
ATOM   1967 O  OG1 . THR B 1 117 ? 35.464 -15.078 10.051 1.00 3.16  ? 116 THR B OG1 1 
ATOM   1968 C  CG2 . THR B 1 117 ? 36.274 -16.705 8.358  1.00 2.15  ? 116 THR B CG2 1 
ATOM   1969 N  N   . LEU B 1 118 ? 36.335 -19.278 9.965  1.00 8.43  ? 117 LEU B N   1 
ATOM   1970 C  CA  . LEU B 1 118 ? 37.189 -20.421 9.785  1.00 8.49  ? 117 LEU B CA  1 
ATOM   1971 C  C   . LEU B 1 118 ? 37.629 -20.126 8.280  1.00 10.99 ? 117 LEU B C   1 
ATOM   1972 O  O   . LEU B 1 118 ? 36.754 -19.876 7.337  1.00 10.82 ? 117 LEU B O   1 
ATOM   1973 C  CB  . LEU B 1 118 ? 36.447 -21.633 10.155 1.00 7.91  ? 117 LEU B CB  1 
ATOM   1974 C  CG  . LEU B 1 118 ? 37.225 -22.942 9.990  1.00 10.65 ? 117 LEU B CG  1 
ATOM   1975 C  CD1 . LEU B 1 118 ? 36.799 -24.137 10.918 1.00 7.65  ? 117 LEU B CD1 1 
ATOM   1976 C  CD2 . LEU B 1 118 ? 37.056 -23.275 8.478  1.00 10.85 ? 117 LEU B CD2 1 
ATOM   1977 N  N   . VAL B 1 119 ? 38.993 -20.142 8.120  1.00 8.43  ? 118 VAL B N   1 
ATOM   1978 C  CA  . VAL B 1 119 ? 39.507 -19.957 6.759  1.00 6.43  ? 118 VAL B CA  1 
ATOM   1979 C  C   . VAL B 1 119 ? 40.476 -21.217 6.613  1.00 8.08  ? 118 VAL B C   1 
ATOM   1980 O  O   . VAL B 1 119 ? 41.201 -21.560 7.667  1.00 10.15 ? 118 VAL B O   1 
ATOM   1981 C  CB  . VAL B 1 119 ? 40.190 -18.698 6.288  1.00 5.92  ? 118 VAL B CB  1 
ATOM   1982 C  CG1 . VAL B 1 119 ? 41.269 -18.127 7.193  1.00 4.72  ? 118 VAL B CG1 1 
ATOM   1983 C  CG2 . VAL B 1 119 ? 40.776 -18.883 4.870  1.00 3.34  ? 118 VAL B CG2 1 
ATOM   1984 N  N   . VAL B 1 120 ? 40.416 -21.755 5.407  1.00 6.09  ? 119 VAL B N   1 
ATOM   1985 C  CA  . VAL B 1 120 ? 41.201 -22.960 4.914  1.00 7.34  ? 119 VAL B CA  1 
ATOM   1986 C  C   . VAL B 1 120 ? 42.360 -22.398 4.133  1.00 7.99  ? 119 VAL B C   1 
ATOM   1987 O  O   . VAL B 1 120 ? 42.101 -21.771 3.025  1.00 11.12 ? 119 VAL B O   1 
ATOM   1988 C  CB  . VAL B 1 120 ? 40.217 -23.889 4.134  1.00 4.29  ? 119 VAL B CB  1 
ATOM   1989 C  CG1 . VAL B 1 120 ? 39.955 -23.677 2.627  1.00 2.13  ? 119 VAL B CG1 1 
ATOM   1990 C  CG2 . VAL B 1 120 ? 40.685 -25.273 4.215  1.00 5.68  ? 119 VAL B CG2 1 
ATOM   1991 N  N   . HIS B 1 121 ? 43.591 -22.487 4.502  1.00 7.92  ? 120 HIS B N   1 
ATOM   1992 C  CA  . HIS B 1 121 ? 44.758 -21.848 3.712  1.00 5.60  ? 120 HIS B CA  1 
ATOM   1993 C  C   . HIS B 1 121 ? 45.333 -22.494 2.500  1.00 5.16  ? 120 HIS B C   1 
ATOM   1994 O  O   . HIS B 1 121 ? 45.576 -23.712 2.310  1.00 5.56  ? 120 HIS B O   1 
ATOM   1995 C  CB  . HIS B 1 121 ? 45.980 -21.656 4.679  1.00 2.00  ? 120 HIS B CB  1 
ATOM   1996 C  CG  . HIS B 1 121 ? 45.426 -20.781 5.748  1.00 3.09  ? 120 HIS B CG  1 
ATOM   1997 N  ND1 . HIS B 1 121 ? 45.500 -19.392 5.646  1.00 2.00  ? 120 HIS B ND1 1 
ATOM   1998 C  CD2 . HIS B 1 121 ? 44.778 -21.102 6.922  1.00 4.15  ? 120 HIS B CD2 1 
ATOM   1999 C  CE1 . HIS B 1 121 ? 44.907 -18.977 6.661  1.00 5.13  ? 120 HIS B CE1 1 
ATOM   2000 N  NE2 . HIS B 1 121 ? 44.416 -19.960 7.545  1.00 5.50  ? 120 HIS B NE2 1 
ATOM   2001 N  N   . GLU B 1 122 ? 45.591 -21.614 1.614  1.00 7.52  ? 121 GLU B N   1 
ATOM   2002 C  CA  . GLU B 1 122 ? 46.176 -22.018 0.242  1.00 10.84 ? 121 GLU B CA  1 
ATOM   2003 C  C   . GLU B 1 122 ? 47.340 -23.000 0.138  1.00 10.53 ? 121 GLU B C   1 
ATOM   2004 O  O   . GLU B 1 122 ? 47.315 -23.831 -0.807 1.00 8.47  ? 121 GLU B O   1 
ATOM   2005 C  CB  . GLU B 1 122 ? 46.431 -20.651 -0.456 1.00 8.35  ? 121 GLU B CB  1 
ATOM   2006 C  CG  . GLU B 1 122 ? 47.227 -20.515 -1.672 1.00 8.24  ? 121 GLU B CG  1 
ATOM   2007 C  CD  . GLU B 1 122 ? 48.731 -20.411 -1.442 1.00 8.34  ? 121 GLU B CD  1 
ATOM   2008 O  OE1 . GLU B 1 122 ? 49.208 -19.347 -0.893 1.00 6.60  ? 121 GLU B OE1 1 
ATOM   2009 O  OE2 . GLU B 1 122 ? 49.279 -21.379 -1.855 1.00 8.96  ? 121 GLU B OE2 1 
ATOM   2010 N  N   . LYS B 1 123 ? 48.305 -22.963 1.013  1.00 9.30  ? 122 LYS B N   1 
ATOM   2011 C  CA  . LYS B 1 123 ? 49.481 -23.806 1.041  1.00 9.22  ? 122 LYS B CA  1 
ATOM   2012 C  C   . LYS B 1 123 ? 49.635 -24.733 2.235  1.00 7.75  ? 122 LYS B C   1 
ATOM   2013 O  O   . LYS B 1 123 ? 48.833 -25.012 3.135  1.00 9.58  ? 122 LYS B O   1 
ATOM   2014 C  CB  . LYS B 1 123 ? 50.558 -22.707 0.861  1.00 10.01 ? 122 LYS B CB  1 
ATOM   2015 C  CG  . LYS B 1 123 ? 52.017 -22.730 1.218  1.00 9.82  ? 122 LYS B CG  1 
ATOM   2016 C  CD  . LYS B 1 123 ? 52.806 -21.559 0.732  1.00 10.29 ? 122 LYS B CD  1 
ATOM   2017 C  CE  . LYS B 1 123 ? 53.057 -21.487 -0.752 1.00 11.80 ? 122 LYS B CE  1 
ATOM   2018 N  NZ  . LYS B 1 123 ? 51.904 -21.454 -1.696 1.00 12.32 ? 122 LYS B NZ  1 
ATOM   2019 N  N   . ALA B 1 124 ? 50.767 -25.352 2.285  1.00 8.06  ? 123 ALA B N   1 
ATOM   2020 C  CA  . ALA B 1 124 ? 51.215 -26.313 3.326  1.00 10.41 ? 123 ALA B CA  1 
ATOM   2021 C  C   . ALA B 1 124 ? 51.660 -25.614 4.609  1.00 10.13 ? 123 ALA B C   1 
ATOM   2022 O  O   . ALA B 1 124 ? 52.751 -24.947 4.798  1.00 7.96  ? 123 ALA B O   1 
ATOM   2023 C  CB  . ALA B 1 124 ? 52.245 -27.134 2.504  1.00 10.11 ? 123 ALA B CB  1 
ATOM   2024 N  N   . ASP B 1 125 ? 50.805 -25.712 5.623  1.00 12.31 ? 124 ASP B N   1 
ATOM   2025 C  CA  . ASP B 1 125 ? 50.934 -25.142 7.018  1.00 10.22 ? 124 ASP B CA  1 
ATOM   2026 C  C   . ASP B 1 125 ? 51.923 -25.990 7.854  1.00 11.15 ? 124 ASP B C   1 
ATOM   2027 O  O   . ASP B 1 125 ? 51.534 -27.154 8.156  1.00 7.52  ? 124 ASP B O   1 
ATOM   2028 C  CB  . ASP B 1 125 ? 49.615 -25.093 7.715  1.00 9.15  ? 124 ASP B CB  1 
ATOM   2029 C  CG  . ASP B 1 125 ? 49.569 -24.703 9.155  1.00 9.34  ? 124 ASP B CG  1 
ATOM   2030 O  OD1 . ASP B 1 125 ? 50.301 -25.377 9.973  1.00 6.57  ? 124 ASP B OD1 1 
ATOM   2031 O  OD2 . ASP B 1 125 ? 48.803 -23.732 9.403  1.00 8.72  ? 124 ASP B OD2 1 
ATOM   2032 N  N   . ASP B 1 126 ? 53.029 -25.294 8.118  1.00 13.40 ? 125 ASP B N   1 
ATOM   2033 C  CA  . ASP B 1 126 ? 54.199 -25.784 8.876  1.00 13.56 ? 125 ASP B CA  1 
ATOM   2034 C  C   . ASP B 1 126 ? 54.360 -25.602 10.388 1.00 11.47 ? 125 ASP B C   1 
ATOM   2035 O  O   . ASP B 1 126 ? 55.441 -25.285 10.897 1.00 9.22  ? 125 ASP B O   1 
ATOM   2036 C  CB  . ASP B 1 126 ? 55.548 -25.190 8.210  1.00 15.62 ? 125 ASP B CB  1 
ATOM   2037 C  CG  . ASP B 1 126 ? 55.620 -23.683 8.445  1.00 18.26 ? 125 ASP B CG  1 
ATOM   2038 O  OD1 . ASP B 1 126 ? 54.583 -23.199 8.949  1.00 19.31 ? 125 ASP B OD1 1 
ATOM   2039 O  OD2 . ASP B 1 126 ? 56.605 -22.958 8.178  1.00 18.19 ? 125 ASP B OD2 1 
ATOM   2040 N  N   . LEU B 1 127 ? 53.350 -25.802 11.150 1.00 10.92 ? 126 LEU B N   1 
ATOM   2041 C  CA  . LEU B 1 127 ? 53.484 -25.682 12.609 1.00 14.20 ? 126 LEU B CA  1 
ATOM   2042 C  C   . LEU B 1 127 ? 54.092 -24.469 13.314 1.00 15.91 ? 126 LEU B C   1 
ATOM   2043 O  O   . LEU B 1 127 ? 53.921 -24.373 14.593 1.00 14.01 ? 126 LEU B O   1 
ATOM   2044 C  CB  . LEU B 1 127 ? 54.276 -27.029 12.893 1.00 15.01 ? 126 LEU B CB  1 
ATOM   2045 C  CG  . LEU B 1 127 ? 53.585 -28.375 12.632 1.00 16.27 ? 126 LEU B CG  1 
ATOM   2046 C  CD1 . LEU B 1 127 ? 54.561 -29.595 12.498 1.00 14.04 ? 126 LEU B CD1 1 
ATOM   2047 C  CD2 . LEU B 1 127 ? 52.608 -28.769 13.766 1.00 14.38 ? 126 LEU B CD2 1 
ATOM   2048 N  N   . GLY B 1 128 ? 54.790 -23.456 12.707 1.00 16.09 ? 127 GLY B N   1 
ATOM   2049 C  CA  . GLY B 1 128 ? 55.321 -22.293 13.481 1.00 13.41 ? 127 GLY B CA  1 
ATOM   2050 C  C   . GLY B 1 128 ? 56.697 -22.474 14.145 1.00 12.40 ? 127 GLY B C   1 
ATOM   2051 O  O   . GLY B 1 128 ? 57.709 -21.720 14.055 1.00 9.66  ? 127 GLY B O   1 
ATOM   2052 N  N   . LYS B 1 129 ? 56.765 -23.588 14.874 1.00 11.19 ? 128 LYS B N   1 
ATOM   2053 C  CA  . LYS B 1 129 ? 58.020 -23.922 15.604 1.00 11.16 ? 128 LYS B CA  1 
ATOM   2054 C  C   . LYS B 1 129 ? 59.206 -23.868 14.628 1.00 10.64 ? 128 LYS B C   1 
ATOM   2055 O  O   . LYS B 1 129 ? 60.382 -23.853 15.098 1.00 8.32  ? 128 LYS B O   1 
ATOM   2056 C  CB  . LYS B 1 129 ? 57.854 -25.187 16.396 1.00 11.33 ? 128 LYS B CB  1 
ATOM   2057 C  CG  . LYS B 1 129 ? 56.999 -25.334 17.598 1.00 10.41 ? 128 LYS B CG  1 
ATOM   2058 C  CD  . LYS B 1 129 ? 55.506 -25.111 17.579 1.00 10.86 ? 128 LYS B CD  1 
ATOM   2059 C  CE  . LYS B 1 129 ? 55.356 -23.548 17.748 1.00 13.00 ? 128 LYS B CE  1 
ATOM   2060 N  NZ  . LYS B 1 129 ? 54.037 -23.341 18.450 1.00 14.81 ? 128 LYS B NZ  1 
ATOM   2061 N  N   . GLY B 1 130 ? 58.829 -23.815 13.332 1.00 10.18 ? 129 GLY B N   1 
ATOM   2062 C  CA  . GLY B 1 130 ? 59.934 -23.727 12.264 1.00 7.45  ? 129 GLY B CA  1 
ATOM   2063 C  C   . GLY B 1 130 ? 60.377 -22.227 12.398 1.00 4.81  ? 129 GLY B C   1 
ATOM   2064 O  O   . GLY B 1 130 ? 60.305 -21.415 11.495 1.00 2.00  ? 129 GLY B O   1 
ATOM   2065 N  N   . GLY B 1 131 ? 60.828 -21.951 13.623 1.00 4.55  ? 130 GLY B N   1 
ATOM   2066 C  CA  . GLY B 1 131 ? 61.306 -20.655 14.075 1.00 4.33  ? 130 GLY B CA  1 
ATOM   2067 C  C   . GLY B 1 131 ? 61.636 -19.645 12.986 1.00 2.75  ? 130 GLY B C   1 
ATOM   2068 O  O   . GLY B 1 131 ? 62.649 -19.853 12.339 1.00 2.00  ? 130 GLY B O   1 
ATOM   2069 N  N   . ASN B 1 132 ? 60.819 -18.654 12.863 1.00 5.06  ? 131 ASN B N   1 
ATOM   2070 C  CA  . ASN B 1 132 ? 60.767 -17.530 11.970 1.00 8.39  ? 131 ASN B CA  1 
ATOM   2071 C  C   . ASN B 1 132 ? 59.581 -16.712 12.485 1.00 10.05 ? 131 ASN B C   1 
ATOM   2072 O  O   . ASN B 1 132 ? 58.473 -17.368 12.540 1.00 9.89  ? 131 ASN B O   1 
ATOM   2073 C  CB  . ASN B 1 132 ? 60.545 -17.914 10.468 1.00 9.80  ? 131 ASN B CB  1 
ATOM   2074 C  CG  . ASN B 1 132 ? 61.606 -18.683 9.709  1.00 13.67 ? 131 ASN B CG  1 
ATOM   2075 O  OD1 . ASN B 1 132 ? 62.481 -17.958 9.053  1.00 15.05 ? 131 ASN B OD1 1 
ATOM   2076 N  ND2 . ASN B 1 132 ? 61.787 -20.027 9.595  1.00 10.23 ? 131 ASN B ND2 1 
ATOM   2077 N  N   . GLU B 1 133 ? 59.711 -15.444 12.855 1.00 9.60  ? 132 GLU B N   1 
ATOM   2078 C  CA  . GLU B 1 133 ? 58.544 -14.617 13.338 1.00 7.40  ? 132 GLU B CA  1 
ATOM   2079 C  C   . GLU B 1 133 ? 57.898 -14.358 11.981 1.00 6.50  ? 132 GLU B C   1 
ATOM   2080 O  O   . GLU B 1 133 ? 58.119 -13.344 11.286 1.00 8.33  ? 132 GLU B O   1 
ATOM   2081 C  CB  . GLU B 1 133 ? 58.741 -13.318 14.113 1.00 5.01  ? 132 GLU B CB  1 
ATOM   2082 C  CG  . GLU B 1 133 ? 58.728 -13.744 15.646 1.00 6.35  ? 132 GLU B CG  1 
ATOM   2083 C  CD  . GLU B 1 133 ? 60.059 -14.317 16.188 1.00 7.77  ? 132 GLU B CD  1 
ATOM   2084 O  OE1 . GLU B 1 133 ? 60.588 -15.415 15.845 1.00 4.59  ? 132 GLU B OE1 1 
ATOM   2085 O  OE2 . GLU B 1 133 ? 60.570 -13.478 17.087 1.00 4.60  ? 132 GLU B OE2 1 
ATOM   2086 N  N   . GLU B 1 134 ? 57.143 -15.343 11.641 1.00 4.83  ? 133 GLU B N   1 
ATOM   2087 C  CA  . GLU B 1 134 ? 56.439 -15.295 10.320 1.00 6.79  ? 133 GLU B CA  1 
ATOM   2088 C  C   . GLU B 1 134 ? 55.700 -16.590 10.332 1.00 5.62  ? 133 GLU B C   1 
ATOM   2089 O  O   . GLU B 1 134 ? 54.507 -16.518 10.463 1.00 6.14  ? 133 GLU B O   1 
ATOM   2090 C  CB  . GLU B 1 134 ? 57.431 -15.120 9.194  1.00 7.88  ? 133 GLU B CB  1 
ATOM   2091 C  CG  . GLU B 1 134 ? 56.841 -14.514 7.855  1.00 6.18  ? 133 GLU B CG  1 
ATOM   2092 C  CD  . GLU B 1 134 ? 55.492 -15.133 7.605  1.00 5.43  ? 133 GLU B CD  1 
ATOM   2093 O  OE1 . GLU B 1 134 ? 55.368 -16.254 7.104  1.00 2.79  ? 133 GLU B OE1 1 
ATOM   2094 O  OE2 . GLU B 1 134 ? 54.600 -14.408 7.969  1.00 6.43  ? 133 GLU B OE2 1 
ATOM   2095 N  N   . SER B 1 135 ? 56.447 -17.690 10.229 1.00 5.47  ? 134 SER B N   1 
ATOM   2096 C  CA  . SER B 1 135 ? 56.017 -19.091 10.240 1.00 2.74  ? 134 SER B CA  1 
ATOM   2097 C  C   . SER B 1 135 ? 55.241 -19.245 11.542 1.00 2.00  ? 134 SER B C   1 
ATOM   2098 O  O   . SER B 1 135 ? 54.388 -20.115 11.537 1.00 2.00  ? 134 SER B O   1 
ATOM   2099 C  CB  . SER B 1 135 ? 57.096 -20.107 10.117 1.00 3.02  ? 134 SER B CB  1 
ATOM   2100 O  OG  . SER B 1 135 ? 58.055 -20.030 11.141 1.00 2.00  ? 134 SER B OG  1 
ATOM   2101 N  N   . THR B 1 136 ? 55.600 -18.385 12.488 1.00 2.50  ? 135 THR B N   1 
ATOM   2102 C  CA  . THR B 1 136 ? 54.926 -18.350 13.767 1.00 5.61  ? 135 THR B CA  1 
ATOM   2103 C  C   . THR B 1 136 ? 53.691 -17.434 13.826 1.00 6.21  ? 135 THR B C   1 
ATOM   2104 O  O   . THR B 1 136 ? 52.961 -17.588 14.842 1.00 7.18  ? 135 THR B O   1 
ATOM   2105 C  CB  . THR B 1 136 ? 55.739 -17.723 14.967 1.00 5.71  ? 135 THR B CB  1 
ATOM   2106 O  OG1 . THR B 1 136 ? 56.462 -16.792 14.033 1.00 5.98  ? 135 THR B OG1 1 
ATOM   2107 C  CG2 . THR B 1 136 ? 56.313 -18.805 15.863 1.00 4.20  ? 135 THR B CG2 1 
ATOM   2108 N  N   . LYS B 1 137 ? 53.591 -16.567 12.808 1.00 6.18  ? 136 LYS B N   1 
ATOM   2109 C  CA  . LYS B 1 137 ? 52.525 -15.588 12.641 1.00 5.36  ? 136 LYS B CA  1 
ATOM   2110 C  C   . LYS B 1 137 ? 51.289 -16.421 12.343 1.00 7.44  ? 136 LYS B C   1 
ATOM   2111 O  O   . LYS B 1 137 ? 50.295 -16.704 13.093 1.00 4.92  ? 136 LYS B O   1 
ATOM   2112 C  CB  . LYS B 1 137 ? 52.756 -14.633 11.505 1.00 4.64  ? 136 LYS B CB  1 
ATOM   2113 C  CG  . LYS B 1 137 ? 52.228 -13.246 11.510 1.00 10.69 ? 136 LYS B CG  1 
ATOM   2114 C  CD  . LYS B 1 137 ? 51.043 -12.634 10.806 1.00 11.08 ? 136 LYS B CD  1 
ATOM   2115 C  CE  . LYS B 1 137 ? 51.147 -12.144 9.408  1.00 12.30 ? 136 LYS B CE  1 
ATOM   2116 N  NZ  . LYS B 1 137 ? 51.579 -13.083 8.300  1.00 14.14 ? 136 LYS B NZ  1 
ATOM   2117 N  N   . THR B 1 138 ? 51.557 -16.819 11.063 1.00 6.97  ? 137 THR B N   1 
ATOM   2118 C  CA  . THR B 1 138 ? 50.522 -17.664 10.400 1.00 6.02  ? 137 THR B CA  1 
ATOM   2119 C  C   . THR B 1 138 ? 51.013 -18.959 9.876  1.00 4.99  ? 137 THR B C   1 
ATOM   2120 O  O   . THR B 1 138 ? 50.641 -19.192 8.680  1.00 7.60  ? 137 THR B O   1 
ATOM   2121 C  CB  . THR B 1 138 ? 49.961 -16.639 9.367  1.00 4.46  ? 137 THR B CB  1 
ATOM   2122 O  OG1 . THR B 1 138 ? 51.074 -15.811 8.828  1.00 5.78  ? 137 THR B OG1 1 
ATOM   2123 C  CG2 . THR B 1 138 ? 48.943 -15.774 10.046 1.00 4.85  ? 137 THR B CG2 1 
ATOM   2124 N  N   . GLY B 1 139 ? 51.740 -19.796 10.534 1.00 3.05  ? 138 GLY B N   1 
ATOM   2125 C  CA  . GLY B 1 139 ? 52.238 -21.065 10.009 1.00 2.72  ? 138 GLY B CA  1 
ATOM   2126 C  C   . GLY B 1 139 ? 52.613 -20.989 8.492  1.00 2.89  ? 138 GLY B C   1 
ATOM   2127 O  O   . GLY B 1 139 ? 51.924 -21.813 7.839  1.00 5.48  ? 138 GLY B O   1 
ATOM   2128 N  N   . ASN B 1 140 ? 53.471 -20.274 7.906  1.00 2.00  ? 139 ASN B N   1 
ATOM   2129 C  CA  . ASN B 1 140 ? 53.854 -20.094 6.525  1.00 6.68  ? 139 ASN B CA  1 
ATOM   2130 C  C   . ASN B 1 140 ? 52.837 -20.535 5.420  1.00 9.29  ? 139 ASN B C   1 
ATOM   2131 O  O   . ASN B 1 140 ? 53.255 -20.888 4.273  1.00 10.30 ? 139 ASN B O   1 
ATOM   2132 C  CB  . ASN B 1 140 ? 55.190 -20.692 6.143  1.00 9.52  ? 139 ASN B CB  1 
ATOM   2133 C  CG  . ASN B 1 140 ? 56.361 -19.878 6.740  1.00 10.97 ? 139 ASN B CG  1 
ATOM   2134 O  OD1 . ASN B 1 140 ? 57.487 -20.427 6.706  1.00 11.17 ? 139 ASN B OD1 1 
ATOM   2135 N  ND2 . ASN B 1 140 ? 55.978 -18.691 7.229  1.00 10.75 ? 139 ASN B ND2 1 
ATOM   2136 N  N   . ALA B 1 141 ? 51.510 -20.460 5.789  1.00 8.54  ? 140 ALA B N   1 
ATOM   2137 C  CA  . ALA B 1 141 ? 50.356 -20.793 4.973  1.00 6.70  ? 140 ALA B CA  1 
ATOM   2138 C  C   . ALA B 1 141 ? 50.032 -20.051 3.665  1.00 4.73  ? 140 ALA B C   1 
ATOM   2139 O  O   . ALA B 1 141 ? 49.464 -20.792 2.780  1.00 3.35  ? 140 ALA B O   1 
ATOM   2140 C  CB  . ALA B 1 141 ? 49.102 -20.681 5.984  1.00 3.07  ? 140 ALA B CB  1 
ATOM   2141 N  N   . GLY B 1 142 ? 50.313 -18.715 3.495  1.00 2.05  ? 141 GLY B N   1 
ATOM   2142 C  CA  . GLY B 1 142 ? 49.965 -18.076 2.201  1.00 2.00  ? 141 GLY B CA  1 
ATOM   2143 C  C   . GLY B 1 142 ? 48.542 -17.671 2.119  1.00 3.49  ? 141 GLY B C   1 
ATOM   2144 O  O   . GLY B 1 142 ? 47.872 -17.516 3.210  1.00 6.34  ? 141 GLY B O   1 
ATOM   2145 N  N   . SER B 1 143 ? 47.863 -17.443 1.060  1.00 4.61  ? 142 SER B N   1 
ATOM   2146 C  CA  . SER B 1 143 ? 46.435 -17.011 1.144  1.00 5.29  ? 142 SER B CA  1 
ATOM   2147 C  C   . SER B 1 143 ? 45.426 -17.742 2.024  1.00 5.77  ? 142 SER B C   1 
ATOM   2148 O  O   . SER B 1 143 ? 45.590 -18.823 2.619  1.00 7.67  ? 142 SER B O   1 
ATOM   2149 C  CB  . SER B 1 143 ? 45.870 -17.053 -0.297 1.00 3.90  ? 142 SER B CB  1 
ATOM   2150 O  OG  . SER B 1 143 ? 46.841 -17.030 -1.312 1.00 5.09  ? 142 SER B OG  1 
ATOM   2151 N  N   . ARG B 1 144 ? 44.276 -17.160 2.111  1.00 4.96  ? 143 ARG B N   1 
ATOM   2152 C  CA  . ARG B 1 144 ? 43.088 -17.565 2.791  1.00 7.68  ? 143 ARG B CA  1 
ATOM   2153 C  C   . ARG B 1 144 ? 42.309 -17.834 1.473  1.00 10.68 ? 143 ARG B C   1 
ATOM   2154 O  O   . ARG B 1 144 ? 41.982 -16.710 0.924  1.00 12.88 ? 143 ARG B O   1 
ATOM   2155 C  CB  . ARG B 1 144 ? 42.421 -16.551 3.716  1.00 6.42  ? 143 ARG B CB  1 
ATOM   2156 C  CG  . ARG B 1 144 ? 43.193 -16.122 4.966  1.00 6.10  ? 143 ARG B CG  1 
ATOM   2157 C  CD  . ARG B 1 144 ? 42.975 -14.635 5.262  1.00 6.19  ? 143 ARG B CD  1 
ATOM   2158 N  NE  . ARG B 1 144 ? 43.952 -13.997 6.210  1.00 2.00  ? 143 ARG B NE  1 
ATOM   2159 C  CZ  . ARG B 1 144 ? 43.663 -14.074 7.501  1.00 2.00  ? 143 ARG B CZ  1 
ATOM   2160 N  NH1 . ARG B 1 144 ? 42.661 -14.700 8.158  1.00 2.00  ? 143 ARG B NH1 1 
ATOM   2161 N  NH2 . ARG B 1 144 ? 44.481 -13.425 8.267  1.00 2.00  ? 143 ARG B NH2 1 
ATOM   2162 N  N   . LEU B 1 145 ? 42.008 -18.982 0.937  1.00 11.15 ? 144 LEU B N   1 
ATOM   2163 C  CA  . LEU B 1 145 ? 41.289 -19.228 -0.322 1.00 8.62  ? 144 LEU B CA  1 
ATOM   2164 C  C   . LEU B 1 145 ? 39.783 -19.447 -0.210 1.00 8.96  ? 144 LEU B C   1 
ATOM   2165 O  O   . LEU B 1 145 ? 39.126 -19.706 -1.322 1.00 7.43  ? 144 LEU B O   1 
ATOM   2166 C  CB  . LEU B 1 145 ? 42.021 -20.408 -1.035 1.00 9.54  ? 144 LEU B CB  1 
ATOM   2167 C  CG  . LEU B 1 145 ? 42.757 -21.711 -0.778 1.00 9.53  ? 144 LEU B CG  1 
ATOM   2168 C  CD1 . LEU B 1 145 ? 42.088 -23.051 -0.393 1.00 6.35  ? 144 LEU B CD1 1 
ATOM   2169 C  CD2 . LEU B 1 145 ? 43.407 -22.215 -2.129 1.00 10.72 ? 144 LEU B CD2 1 
ATOM   2170 N  N   . ALA B 1 146 ? 39.212 -19.373 0.985  1.00 7.07  ? 145 ALA B N   1 
ATOM   2171 C  CA  . ALA B 1 146 ? 37.794 -19.548 1.293  1.00 5.39  ? 145 ALA B CA  1 
ATOM   2172 C  C   . ALA B 1 146 ? 37.492 -19.482 2.808  1.00 6.10  ? 145 ALA B C   1 
ATOM   2173 O  O   . ALA B 1 146 ? 38.232 -19.890 3.716  1.00 2.00  ? 145 ALA B O   1 
ATOM   2174 C  CB  . ALA B 1 146 ? 37.162 -20.881 0.791  1.00 4.35  ? 145 ALA B CB  1 
ATOM   2175 N  N   . CYS B 1 147 ? 36.267 -18.934 3.105  1.00 7.02  ? 146 CYS B N   1 
ATOM   2176 C  CA  . CYS B 1 147 ? 35.922 -18.862 4.582  1.00 6.43  ? 146 CYS B CA  1 
ATOM   2177 C  C   . CYS B 1 147 ? 34.469 -19.095 4.883  1.00 3.81  ? 146 CYS B C   1 
ATOM   2178 O  O   . CYS B 1 147 ? 33.551 -19.233 4.033  1.00 2.88  ? 146 CYS B O   1 
ATOM   2179 C  CB  . CYS B 1 147 ? 36.509 -17.524 5.102  1.00 7.35  ? 146 CYS B CB  1 
ATOM   2180 S  SG  . CYS B 1 147 ? 36.482 -16.156 3.756  1.00 8.53  ? 146 CYS B SG  1 
ATOM   2181 N  N   . GLY B 1 148 ? 34.186 -19.171 6.120  1.00 2.00  ? 147 GLY B N   1 
ATOM   2182 C  CA  . GLY B 1 148 ? 32.825 -19.345 6.648  1.00 2.15  ? 147 GLY B CA  1 
ATOM   2183 C  C   . GLY B 1 148 ? 32.738 -18.934 8.177  1.00 6.07  ? 147 GLY B C   1 
ATOM   2184 O  O   . GLY B 1 148 ? 33.665 -18.866 8.994  1.00 2.00  ? 147 GLY B O   1 
ATOM   2185 N  N   . VAL B 1 149 ? 31.479 -18.607 8.612  1.00 7.96  ? 148 VAL B N   1 
ATOM   2186 C  CA  . VAL B 1 149 ? 31.246 -18.260 9.976  1.00 9.13  ? 148 VAL B CA  1 
ATOM   2187 C  C   . VAL B 1 149 ? 30.577 -19.488 10.722 1.00 9.27  ? 148 VAL B C   1 
ATOM   2188 O  O   . VAL B 1 149 ? 29.628 -20.139 10.334 1.00 8.53  ? 148 VAL B O   1 
ATOM   2189 C  CB  . VAL B 1 149 ? 30.322 -17.068 10.253 1.00 10.57 ? 148 VAL B CB  1 
ATOM   2190 C  CG1 . VAL B 1 149 ? 30.683 -16.660 11.744 1.00 12.06 ? 148 VAL B CG1 1 
ATOM   2191 C  CG2 . VAL B 1 149 ? 30.259 -15.862 9.345  1.00 11.47 ? 148 VAL B CG2 1 
ATOM   2192 N  N   . ILE B 1 150 ? 31.101 -19.791 11.899 1.00 10.20 ? 149 ILE B N   1 
ATOM   2193 C  CA  . ILE B 1 150 ? 30.744 -20.791 12.874 1.00 7.53  ? 149 ILE B CA  1 
ATOM   2194 C  C   . ILE B 1 150 ? 29.453 -20.102 13.472 1.00 7.00  ? 149 ILE B C   1 
ATOM   2195 O  O   . ILE B 1 150 ? 29.528 -18.962 13.989 1.00 2.00  ? 149 ILE B O   1 
ATOM   2196 C  CB  . ILE B 1 150 ? 31.503 -21.075 14.211 1.00 9.95  ? 149 ILE B CB  1 
ATOM   2197 C  CG1 . ILE B 1 150 ? 32.962 -21.489 14.399 1.00 9.81  ? 149 ILE B CG1 1 
ATOM   2198 C  CG2 . ILE B 1 150 ? 30.693 -22.344 14.801 1.00 11.07 ? 149 ILE B CG2 1 
ATOM   2199 C  CD1 . ILE B 1 150 ? 34.101 -21.288 13.363 1.00 11.76 ? 149 ILE B CD1 1 
ATOM   2200 N  N   . GLY B 1 151 ? 28.413 -20.936 13.263 1.00 6.50  ? 150 GLY B N   1 
ATOM   2201 C  CA  . GLY B 1 151 ? 27.175 -20.204 13.939 1.00 4.90  ? 150 GLY B CA  1 
ATOM   2202 C  C   . GLY B 1 151 ? 26.497 -21.439 14.648 1.00 7.78  ? 150 GLY B C   1 
ATOM   2203 O  O   . GLY B 1 151 ? 27.108 -22.550 14.540 1.00 6.95  ? 150 GLY B O   1 
ATOM   2204 N  N   . ILE B 1 152 ? 25.317 -21.413 15.336 1.00 5.20  ? 151 ILE B N   1 
ATOM   2205 C  CA  . ILE B 1 152 ? 24.670 -22.542 15.921 1.00 5.15  ? 151 ILE B CA  1 
ATOM   2206 C  C   . ILE B 1 152 ? 23.854 -23.142 14.668 1.00 7.57  ? 151 ILE B C   1 
ATOM   2207 O  O   . ILE B 1 152 ? 23.116 -22.462 13.929 1.00 7.71  ? 151 ILE B O   1 
ATOM   2208 C  CB  . ILE B 1 152 ? 23.662 -22.505 17.104 1.00 3.98  ? 151 ILE B CB  1 
ATOM   2209 C  CG1 . ILE B 1 152 ? 22.987 -21.120 17.347 1.00 3.67  ? 151 ILE B CG1 1 
ATOM   2210 C  CG2 . ILE B 1 152 ? 24.447 -23.003 18.339 1.00 3.76  ? 151 ILE B CG2 1 
ATOM   2211 C  CD1 . ILE B 1 152 ? 23.672 -20.208 18.501 1.00 2.04  ? 151 ILE B CD1 1 
ATOM   2212 N  N   . ALA B 1 153 ? 24.087 -24.446 14.523 1.00 5.84  ? 152 ALA B N   1 
ATOM   2213 C  CA  . ALA B 1 153 ? 23.544 -25.303 13.522 1.00 6.90  ? 152 ALA B CA  1 
ATOM   2214 C  C   . ALA B 1 153 ? 22.476 -26.287 13.991 1.00 4.51  ? 152 ALA B C   1 
ATOM   2215 O  O   . ALA B 1 153 ? 22.100 -26.302 15.157 1.00 2.00  ? 152 ALA B O   1 
ATOM   2216 C  CB  . ALA B 1 153 ? 24.679 -26.260 13.034 1.00 7.85  ? 152 ALA B CB  1 
ATOM   2217 N  N   . GLN B 1 154 ? 22.056 -27.082 13.034 1.00 4.34  ? 153 GLN B N   1 
ATOM   2218 C  CA  . GLN B 1 154 ? 21.078 -28.190 13.164 1.00 5.12  ? 153 GLN B CA  1 
ATOM   2219 C  C   . GLN B 1 154 ? 21.531 -29.435 14.003 1.00 5.04  ? 153 GLN B C   1 
ATOM   2220 O  O   . GLN B 1 154 ? 20.604 -30.282 14.260 1.00 6.81  ? 153 GLN B O   1 
ATOM   2221 C  CB  . GLN B 1 154 ? 20.797 -28.642 11.748 1.00 3.98  ? 153 GLN B CB  1 
ATOM   2222 C  CG  . GLN B 1 154 ? 21.692 -29.586 10.956 1.00 2.99  ? 153 GLN B CG  1 
ATOM   2223 C  CD  . GLN B 1 154 ? 23.153 -29.468 10.803 1.00 4.75  ? 153 GLN B CD  1 
ATOM   2224 O  OE1 . GLN B 1 154 ? 23.905 -30.350 11.278 1.00 3.33  ? 153 GLN B OE1 1 
ATOM   2225 N  NE2 . GLN B 1 154 ? 23.778 -28.429 10.136 1.00 4.73  ? 153 GLN B NE2 1 
ATOM   2226 O  OXT . GLN B 1 154 ? 22.697 -29.805 14.472 1.00 2.43  ? 153 GLN B OXT 1 
HETATM 2227 CU CU  . CU  C 2 .   ? 11.699 -13.605 8.653  1.00 6.30  ? 154 CU  A CU  1 
HETATM 2228 ZN ZN  . ZN  D 3 .   ? 8.182  -13.479 13.263 1.00 7.00  ? 155 ZN  A ZN  1 
HETATM 2229 CU CU  . CU  E 2 .   ? 45.274 -19.015 9.113  1.00 13.78 ? 154 CU  B CU  1 
HETATM 2230 ZN ZN  . ZN  F 3 .   ? 47.961 -19.722 13.839 1.00 11.85 ? 155 ZN  B ZN  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   ACE 1   0   0   ACE ACE A . n 
A 1 2   ALA 2   1   1   ALA ALA A . n 
A 1 3   THR 3   2   2   THR THR A . n 
A 1 4   LYS 4   3   3   LYS LYS A . n 
A 1 5   ALA 5   4   4   ALA ALA A . n 
A 1 6   VAL 6   5   5   VAL VAL A . n 
A 1 7   CYS 7   6   6   CYS CYS A . n 
A 1 8   VAL 8   7   7   VAL VAL A . n 
A 1 9   LEU 9   8   8   LEU LEU A . n 
A 1 10  LYS 10  9   9   LYS LYS A . n 
A 1 11  GLY 11  10  10  GLY GLY A . n 
A 1 12  ASP 12  11  11  ASP ASP A . n 
A 1 13  GLY 13  12  12  GLY GLY A . n 
A 1 14  PRO 14  13  13  PRO PRO A . n 
A 1 15  VAL 15  14  14  VAL VAL A . n 
A 1 16  GLN 16  15  15  GLN GLN A . n 
A 1 17  GLY 17  16  16  GLY GLY A . n 
A 1 18  ILE 18  17  17  ILE ILE A . n 
A 1 19  ILE 19  18  18  ILE ILE A . n 
A 1 20  ASN 20  19  19  ASN ASN A . n 
A 1 21  PHE 21  20  20  PHE PHE A . n 
A 1 22  GLU 22  21  21  GLU GLU A . n 
A 1 23  GLN 23  22  22  GLN GLN A . n 
A 1 24  LYS 24  23  23  LYS LYS A . n 
A 1 25  GLU 25  24  24  GLU GLU A . n 
A 1 26  SER 26  25  25  SER SER A . n 
A 1 27  ASN 27  26  26  ASN ASN A . n 
A 1 28  GLY 28  27  27  GLY GLY A . n 
A 1 29  PRO 29  28  28  PRO PRO A . n 
A 1 30  VAL 30  29  29  VAL VAL A . n 
A 1 31  LYS 31  30  30  LYS LYS A . n 
A 1 32  VAL 32  31  31  VAL VAL A . n 
A 1 33  TRP 33  32  32  TRP TRP A . n 
A 1 34  GLY 34  33  33  GLY GLY A . n 
A 1 35  SER 35  34  34  SER SER A . n 
A 1 36  ILE 36  35  35  ILE ILE A . n 
A 1 37  LYS 37  36  36  LYS LYS A . n 
A 1 38  GLY 38  37  37  GLY GLY A . n 
A 1 39  LEU 39  38  38  LEU LEU A . n 
A 1 40  THR 40  39  39  THR THR A . n 
A 1 41  GLU 41  40  40  GLU GLU A . n 
A 1 42  GLY 42  41  41  GLY GLY A . n 
A 1 43  LEU 43  42  42  LEU LEU A . n 
A 1 44  HIS 44  43  43  HIS HIS A . n 
A 1 45  GLY 45  44  44  GLY GLY A . n 
A 1 46  PHE 46  45  45  PHE PHE A . n 
A 1 47  HIS 47  46  46  HIS HIS A . n 
A 1 48  VAL 48  47  47  VAL VAL A . n 
A 1 49  HIS 49  48  48  HIS HIS A . n 
A 1 50  GLU 50  49  49  GLU GLU A . n 
A 1 51  PHE 51  50  50  PHE PHE A . n 
A 1 52  GLY 52  51  51  GLY GLY A . n 
A 1 53  ASP 53  52  52  ASP ASP A . n 
A 1 54  ASN 54  53  53  ASN ASN A . n 
A 1 55  THR 55  54  54  THR THR A . n 
A 1 56  ALA 56  55  55  ALA ALA A . n 
A 1 57  GLY 57  56  56  GLY GLY A . n 
A 1 58  CYS 58  57  57  CYS CYS A . n 
A 1 59  THR 59  58  58  THR THR A . n 
A 1 60  SER 60  59  59  SER SER A . n 
A 1 61  ALA 61  60  60  ALA ALA A . n 
A 1 62  GLY 62  61  61  GLY GLY A . n 
A 1 63  PRO 63  62  62  PRO PRO A . n 
A 1 64  HIS 64  63  63  HIS HIS A . n 
A 1 65  PHE 65  64  64  PHE PHE A . n 
A 1 66  ASN 66  65  65  ASN ASN A . n 
A 1 67  PRO 67  66  66  PRO PRO A . n 
A 1 68  LEU 68  67  67  LEU LEU A . n 
A 1 69  SER 69  68  68  SER SER A . n 
A 1 70  ARG 70  69  69  ARG ARG A . n 
A 1 71  LYS 71  70  70  LYS LYS A . n 
A 1 72  HIS 72  71  71  HIS HIS A . n 
A 1 73  GLY 73  72  72  GLY GLY A . n 
A 1 74  GLY 74  73  73  GLY GLY A . n 
A 1 75  PRO 75  74  74  PRO PRO A . n 
A 1 76  LYS 76  75  75  LYS LYS A . n 
A 1 77  ASP 77  76  76  ASP ASP A . n 
A 1 78  GLU 78  77  77  GLU GLU A . n 
A 1 79  GLU 79  78  78  GLU GLU A . n 
A 1 80  ARG 80  79  79  ARG ARG A . n 
A 1 81  HIS 81  80  80  HIS HIS A . n 
A 1 82  VAL 82  81  81  VAL VAL A . n 
A 1 83  GLY 83  82  82  GLY GLY A . n 
A 1 84  ASP 84  83  83  ASP ASP A . n 
A 1 85  LEU 85  84  84  LEU LEU A . n 
A 1 86  GLY 86  85  85  GLY GLY A . n 
A 1 87  ASN 87  86  86  ASN ASN A . n 
A 1 88  VAL 88  87  87  VAL VAL A . n 
A 1 89  THR 89  88  88  THR THR A . n 
A 1 90  ALA 90  89  89  ALA ALA A . n 
A 1 91  ASP 91  90  90  ASP ASP A . n 
A 1 92  LYS 92  91  91  LYS LYS A . n 
A 1 93  ASP 93  92  92  ASP ASP A . n 
A 1 94  GLY 94  93  93  GLY GLY A . n 
A 1 95  VAL 95  94  94  VAL VAL A . n 
A 1 96  ALA 96  95  95  ALA ALA A . n 
A 1 97  ASP 97  96  96  ASP ASP A . n 
A 1 98  VAL 98  97  97  VAL VAL A . n 
A 1 99  SER 99  98  98  SER SER A . n 
A 1 100 ILE 100 99  99  ILE ILE A . n 
A 1 101 GLU 101 100 100 GLU GLU A . n 
A 1 102 ASP 102 101 101 ASP ASP A . n 
A 1 103 SER 103 102 102 SER SER A . n 
A 1 104 VAL 104 103 103 VAL VAL A . n 
A 1 105 ILE 105 104 104 ILE ILE A . n 
A 1 106 SER 106 105 105 SER SER A . n 
A 1 107 LEU 107 106 106 LEU LEU A . n 
A 1 108 SER 108 107 107 SER SER A . n 
A 1 109 GLY 109 108 108 GLY GLY A . n 
A 1 110 ASP 110 109 109 ASP ASP A . n 
A 1 111 HIS 111 110 110 HIS HIS A . n 
A 1 112 CYS 112 111 111 CYS CYS A . n 
A 1 113 ILE 113 112 112 ILE ILE A . n 
A 1 114 ILE 114 113 113 ILE ILE A . n 
A 1 115 GLY 115 114 114 GLY GLY A . n 
A 1 116 ARG 116 115 115 ARG ARG A . n 
A 1 117 THR 117 116 116 THR THR A . n 
A 1 118 LEU 118 117 117 LEU LEU A . n 
A 1 119 VAL 119 118 118 VAL VAL A . n 
A 1 120 VAL 120 119 119 VAL VAL A . n 
A 1 121 HIS 121 120 120 HIS HIS A . n 
A 1 122 GLU 122 121 121 GLU GLU A . n 
A 1 123 LYS 123 122 122 LYS LYS A . n 
A 1 124 ALA 124 123 123 ALA ALA A . n 
A 1 125 ASP 125 124 124 ASP ASP A . n 
A 1 126 ASP 126 125 125 ASP ASP A . n 
A 1 127 LEU 127 126 126 LEU LEU A . n 
A 1 128 GLY 128 127 127 GLY GLY A . n 
A 1 129 LYS 129 128 128 LYS LYS A . n 
A 1 130 GLY 130 129 129 GLY GLY A . n 
A 1 131 GLY 131 130 130 GLY GLY A . n 
A 1 132 ASN 132 131 131 ASN ASN A . n 
A 1 133 GLU 133 132 132 GLU GLU A . n 
A 1 134 GLU 134 133 133 GLU GLU A . n 
A 1 135 SER 135 134 134 SER SER A . n 
A 1 136 THR 136 135 135 THR THR A . n 
A 1 137 LYS 137 136 136 LYS LYS A . n 
A 1 138 THR 138 137 137 THR THR A . n 
A 1 139 GLY 139 138 138 GLY GLY A . n 
A 1 140 ASN 140 139 139 ASN ASN A . n 
A 1 141 ALA 141 140 140 ALA ALA A . n 
A 1 142 GLY 142 141 141 GLY GLY A . n 
A 1 143 SER 143 142 142 SER SER A . n 
A 1 144 ARG 144 143 143 ARG ARG A . n 
A 1 145 LEU 145 144 144 LEU LEU A . n 
A 1 146 ALA 146 145 145 ALA ALA A . n 
A 1 147 CYS 147 146 146 CYS CYS A . n 
A 1 148 GLY 148 147 147 GLY GLY A . n 
A 1 149 VAL 149 148 148 VAL VAL A . n 
A 1 150 ILE 150 149 149 ILE ILE A . n 
A 1 151 GLY 151 150 150 GLY GLY A . n 
A 1 152 ILE 152 151 151 ILE ILE A . n 
A 1 153 ALA 153 152 152 ALA ALA A . n 
A 1 154 GLN 154 153 153 GLN GLN A . n 
B 1 1   ACE 1   0   0   ACE ACE B . n 
B 1 2   ALA 2   1   1   ALA ALA B . n 
B 1 3   THR 3   2   2   THR THR B . n 
B 1 4   LYS 4   3   3   LYS LYS B . n 
B 1 5   ALA 5   4   4   ALA ALA B . n 
B 1 6   VAL 6   5   5   VAL VAL B . n 
B 1 7   CYS 7   6   6   CYS CYS B . n 
B 1 8   VAL 8   7   7   VAL VAL B . n 
B 1 9   LEU 9   8   8   LEU LEU B . n 
B 1 10  LYS 10  9   9   LYS LYS B . n 
B 1 11  GLY 11  10  10  GLY GLY B . n 
B 1 12  ASP 12  11  11  ASP ASP B . n 
B 1 13  GLY 13  12  12  GLY GLY B . n 
B 1 14  PRO 14  13  13  PRO PRO B . n 
B 1 15  VAL 15  14  14  VAL VAL B . n 
B 1 16  GLN 16  15  15  GLN GLN B . n 
B 1 17  GLY 17  16  16  GLY GLY B . n 
B 1 18  ILE 18  17  17  ILE ILE B . n 
B 1 19  ILE 19  18  18  ILE ILE B . n 
B 1 20  ASN 20  19  19  ASN ASN B . n 
B 1 21  PHE 21  20  20  PHE PHE B . n 
B 1 22  GLU 22  21  21  GLU GLU B . n 
B 1 23  GLN 23  22  22  GLN GLN B . n 
B 1 24  LYS 24  23  23  LYS LYS B . n 
B 1 25  GLU 25  24  24  GLU GLU B . n 
B 1 26  SER 26  25  25  SER SER B . n 
B 1 27  ASN 27  26  26  ASN ASN B . n 
B 1 28  GLY 28  27  27  GLY GLY B . n 
B 1 29  PRO 29  28  28  PRO PRO B . n 
B 1 30  VAL 30  29  29  VAL VAL B . n 
B 1 31  LYS 31  30  30  LYS LYS B . n 
B 1 32  VAL 32  31  31  VAL VAL B . n 
B 1 33  TRP 33  32  32  TRP TRP B . n 
B 1 34  GLY 34  33  33  GLY GLY B . n 
B 1 35  SER 35  34  34  SER SER B . n 
B 1 36  ILE 36  35  35  ILE ILE B . n 
B 1 37  LYS 37  36  36  LYS LYS B . n 
B 1 38  GLY 38  37  37  GLY GLY B . n 
B 1 39  LEU 39  38  38  LEU LEU B . n 
B 1 40  THR 40  39  39  THR THR B . n 
B 1 41  GLU 41  40  40  GLU GLU B . n 
B 1 42  GLY 42  41  41  GLY GLY B . n 
B 1 43  LEU 43  42  42  LEU LEU B . n 
B 1 44  HIS 44  43  43  HIS HIS B . n 
B 1 45  GLY 45  44  44  GLY GLY B . n 
B 1 46  PHE 46  45  45  PHE PHE B . n 
B 1 47  HIS 47  46  46  HIS HIS B . n 
B 1 48  VAL 48  47  47  VAL VAL B . n 
B 1 49  HIS 49  48  48  HIS HIS B . n 
B 1 50  GLU 50  49  49  GLU GLU B . n 
B 1 51  PHE 51  50  50  PHE PHE B . n 
B 1 52  GLY 52  51  51  GLY GLY B . n 
B 1 53  ASP 53  52  52  ASP ASP B . n 
B 1 54  ASN 54  53  53  ASN ASN B . n 
B 1 55  THR 55  54  54  THR THR B . n 
B 1 56  ALA 56  55  55  ALA ALA B . n 
B 1 57  GLY 57  56  56  GLY GLY B . n 
B 1 58  CYS 58  57  57  CYS CYS B . n 
B 1 59  THR 59  58  58  THR THR B . n 
B 1 60  SER 60  59  59  SER SER B . n 
B 1 61  ALA 61  60  60  ALA ALA B . n 
B 1 62  GLY 62  61  61  GLY GLY B . n 
B 1 63  PRO 63  62  62  PRO PRO B . n 
B 1 64  HIS 64  63  63  HIS HIS B . n 
B 1 65  PHE 65  64  64  PHE PHE B . n 
B 1 66  ASN 66  65  65  ASN ASN B . n 
B 1 67  PRO 67  66  66  PRO PRO B . n 
B 1 68  LEU 68  67  67  LEU LEU B . n 
B 1 69  SER 69  68  68  SER SER B . n 
B 1 70  ARG 70  69  69  ARG ARG B . n 
B 1 71  LYS 71  70  70  LYS LYS B . n 
B 1 72  HIS 72  71  71  HIS HIS B . n 
B 1 73  GLY 73  72  72  GLY GLY B . n 
B 1 74  GLY 74  73  73  GLY GLY B . n 
B 1 75  PRO 75  74  74  PRO PRO B . n 
B 1 76  LYS 76  75  75  LYS LYS B . n 
B 1 77  ASP 77  76  76  ASP ASP B . n 
B 1 78  GLU 78  77  77  GLU GLU B . n 
B 1 79  GLU 79  78  78  GLU GLU B . n 
B 1 80  ARG 80  79  79  ARG ARG B . n 
B 1 81  HIS 81  80  80  HIS HIS B . n 
B 1 82  VAL 82  81  81  VAL VAL B . n 
B 1 83  GLY 83  82  82  GLY GLY B . n 
B 1 84  ASP 84  83  83  ASP ASP B . n 
B 1 85  LEU 85  84  84  LEU LEU B . n 
B 1 86  GLY 86  85  85  GLY GLY B . n 
B 1 87  ASN 87  86  86  ASN ASN B . n 
B 1 88  VAL 88  87  87  VAL VAL B . n 
B 1 89  THR 89  88  88  THR THR B . n 
B 1 90  ALA 90  89  89  ALA ALA B . n 
B 1 91  ASP 91  90  90  ASP ASP B . n 
B 1 92  LYS 92  91  91  LYS LYS B . n 
B 1 93  ASP 93  92  92  ASP ASP B . n 
B 1 94  GLY 94  93  93  GLY GLY B . n 
B 1 95  VAL 95  94  94  VAL VAL B . n 
B 1 96  ALA 96  95  95  ALA ALA B . n 
B 1 97  ASP 97  96  96  ASP ASP B . n 
B 1 98  VAL 98  97  97  VAL VAL B . n 
B 1 99  SER 99  98  98  SER SER B . n 
B 1 100 ILE 100 99  99  ILE ILE B . n 
B 1 101 GLU 101 100 100 GLU GLU B . n 
B 1 102 ASP 102 101 101 ASP ASP B . n 
B 1 103 SER 103 102 102 SER SER B . n 
B 1 104 VAL 104 103 103 VAL VAL B . n 
B 1 105 ILE 105 104 104 ILE ILE B . n 
B 1 106 SER 106 105 105 SER SER B . n 
B 1 107 LEU 107 106 106 LEU LEU B . n 
B 1 108 SER 108 107 107 SER SER B . n 
B 1 109 GLY 109 108 108 GLY GLY B . n 
B 1 110 ASP 110 109 109 ASP ASP B . n 
B 1 111 HIS 111 110 110 HIS HIS B . n 
B 1 112 CYS 112 111 111 CYS CYS B . n 
B 1 113 ILE 113 112 112 ILE ILE B . n 
B 1 114 ILE 114 113 113 ILE ILE B . n 
B 1 115 GLY 115 114 114 GLY GLY B . n 
B 1 116 ARG 116 115 115 ARG ARG B . n 
B 1 117 THR 117 116 116 THR THR B . n 
B 1 118 LEU 118 117 117 LEU LEU B . n 
B 1 119 VAL 119 118 118 VAL VAL B . n 
B 1 120 VAL 120 119 119 VAL VAL B . n 
B 1 121 HIS 121 120 120 HIS HIS B . n 
B 1 122 GLU 122 121 121 GLU GLU B . n 
B 1 123 LYS 123 122 122 LYS LYS B . n 
B 1 124 ALA 124 123 123 ALA ALA B . n 
B 1 125 ASP 125 124 124 ASP ASP B . n 
B 1 126 ASP 126 125 125 ASP ASP B . n 
B 1 127 LEU 127 126 126 LEU LEU B . n 
B 1 128 GLY 128 127 127 GLY GLY B . n 
B 1 129 LYS 129 128 128 LYS LYS B . n 
B 1 130 GLY 130 129 129 GLY GLY B . n 
B 1 131 GLY 131 130 130 GLY GLY B . n 
B 1 132 ASN 132 131 131 ASN ASN B . n 
B 1 133 GLU 133 132 132 GLU GLU B . n 
B 1 134 GLU 134 133 133 GLU GLU B . n 
B 1 135 SER 135 134 134 SER SER B . n 
B 1 136 THR 136 135 135 THR THR B . n 
B 1 137 LYS 137 136 136 LYS LYS B . n 
B 1 138 THR 138 137 137 THR THR B . n 
B 1 139 GLY 139 138 138 GLY GLY B . n 
B 1 140 ASN 140 139 139 ASN ASN B . n 
B 1 141 ALA 141 140 140 ALA ALA B . n 
B 1 142 GLY 142 141 141 GLY GLY B . n 
B 1 143 SER 143 142 142 SER SER B . n 
B 1 144 ARG 144 143 143 ARG ARG B . n 
B 1 145 LEU 145 144 144 LEU LEU B . n 
B 1 146 ALA 146 145 145 ALA ALA B . n 
B 1 147 CYS 147 146 146 CYS CYS B . n 
B 1 148 GLY 148 147 147 GLY GLY B . n 
B 1 149 VAL 149 148 148 VAL VAL B . n 
B 1 150 ILE 150 149 149 ILE ILE B . n 
B 1 151 GLY 151 150 150 GLY GLY B . n 
B 1 152 ILE 152 151 151 ILE ILE B . n 
B 1 153 ALA 153 152 152 ALA ALA B . n 
B 1 154 GLN 154 153 153 GLN GLN B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 CU 1 154 154 CU CU A . 
D 3 ZN 1 155 155 ZN ZN A . 
E 2 CU 1 154 154 CU CU B . 
F 3 ZN 1 155 155 ZN ZN B . 
# 
_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 
# 
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)' 1710  ? 
1 MORE         -24   ? 
1 'SSA (A^2)'  14120 ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  NE2 ? A HIS 121 ? A HIS 120 ? 1_555 CU ? C CU . ? A CU 154 ? 1_555 ND1 ? A HIS 47 ? A HIS 46 ? 1_555 78.2  ? 
2  NE2 ? A HIS 121 ? A HIS 120 ? 1_555 CU ? C CU . ? A CU 154 ? 1_555 NE2 ? A HIS 64 ? A HIS 63 ? 1_555 167.5 ? 
3  ND1 ? A HIS 47  ? A HIS 46  ? 1_555 CU ? C CU . ? A CU 154 ? 1_555 NE2 ? A HIS 64 ? A HIS 63 ? 1_555 89.6  ? 
4  NE2 ? A HIS 121 ? A HIS 120 ? 1_555 CU ? C CU . ? A CU 154 ? 1_555 NE2 ? A HIS 49 ? A HIS 48 ? 1_555 91.8  ? 
5  ND1 ? A HIS 47  ? A HIS 46  ? 1_555 CU ? C CU . ? A CU 154 ? 1_555 NE2 ? A HIS 49 ? A HIS 48 ? 1_555 139.6 ? 
6  NE2 ? A HIS 64  ? A HIS 63  ? 1_555 CU ? C CU . ? A CU 154 ? 1_555 NE2 ? A HIS 49 ? A HIS 48 ? 1_555 95.9  ? 
7  ND1 ? A HIS 72  ? A HIS 71  ? 1_555 ZN ? D ZN . ? A ZN 155 ? 1_555 ND1 ? A HIS 64 ? A HIS 63 ? 1_555 143.8 ? 
8  ND1 ? A HIS 72  ? A HIS 71  ? 1_555 ZN ? D ZN . ? A ZN 155 ? 1_555 ND1 ? A HIS 81 ? A HIS 80 ? 1_555 113.0 ? 
9  ND1 ? A HIS 64  ? A HIS 63  ? 1_555 ZN ? D ZN . ? A ZN 155 ? 1_555 ND1 ? A HIS 81 ? A HIS 80 ? 1_555 102.3 ? 
10 ND1 ? A HIS 72  ? A HIS 71  ? 1_555 ZN ? D ZN . ? A ZN 155 ? 1_555 OD2 ? A ASP 84 ? A ASP 83 ? 1_555 75.8  ? 
11 ND1 ? A HIS 64  ? A HIS 63  ? 1_555 ZN ? D ZN . ? A ZN 155 ? 1_555 OD2 ? A ASP 84 ? A ASP 83 ? 1_555 116.3 ? 
12 ND1 ? A HIS 81  ? A HIS 80  ? 1_555 ZN ? D ZN . ? A ZN 155 ? 1_555 OD2 ? A ASP 84 ? A ASP 83 ? 1_555 62.2  ? 
13 NE2 ? B HIS 121 ? B HIS 120 ? 1_555 CU ? E CU . ? B CU 154 ? 1_555 NE2 ? B HIS 64 ? B HIS 63 ? 1_555 147.7 ? 
14 NE2 ? B HIS 121 ? B HIS 120 ? 1_555 CU ? E CU . ? B CU 154 ? 1_555 ND1 ? B HIS 47 ? B HIS 46 ? 1_555 95.4  ? 
15 NE2 ? B HIS 64  ? B HIS 63  ? 1_555 CU ? E CU . ? B CU 154 ? 1_555 ND1 ? B HIS 47 ? B HIS 46 ? 1_555 59.5  ? 
16 NE2 ? B HIS 121 ? B HIS 120 ? 1_555 CU ? E CU . ? B CU 154 ? 1_555 NE2 ? B HIS 49 ? B HIS 48 ? 1_555 98.4  ? 
17 NE2 ? B HIS 64  ? B HIS 63  ? 1_555 CU ? E CU . ? B CU 154 ? 1_555 NE2 ? B HIS 49 ? B HIS 48 ? 1_555 83.0  ? 
18 ND1 ? B HIS 47  ? B HIS 46  ? 1_555 CU ? E CU . ? B CU 154 ? 1_555 NE2 ? B HIS 49 ? B HIS 48 ? 1_555 125.0 ? 
19 ND1 ? B HIS 64  ? B HIS 63  ? 1_555 ZN ? F ZN . ? B ZN 155 ? 1_555 OD2 ? B ASP 84 ? B ASP 83 ? 1_555 146.3 ? 
20 ND1 ? B HIS 64  ? B HIS 63  ? 1_555 ZN ? F ZN . ? B ZN 155 ? 1_555 ND1 ? B HIS 81 ? B HIS 80 ? 1_555 124.7 ? 
21 OD2 ? B ASP 84  ? B ASP 83  ? 1_555 ZN ? F ZN . ? B ZN 155 ? 1_555 ND1 ? B HIS 81 ? B HIS 80 ? 1_555 71.7  ? 
22 ND1 ? B HIS 64  ? B HIS 63  ? 1_555 ZN ? F ZN . ? B ZN 155 ? 1_555 ND1 ? B HIS 72 ? B HIS 71 ? 1_555 128.8 ? 
23 OD2 ? B ASP 84  ? B ASP 83  ? 1_555 ZN ? F ZN . ? B ZN 155 ? 1_555 ND1 ? B HIS 72 ? B HIS 71 ? 1_555 77.4  ? 
24 ND1 ? B HIS 81  ? B HIS 80  ? 1_555 ZN ? F ZN . ? B ZN 155 ? 1_555 ND1 ? B HIS 72 ? B HIS 71 ? 1_555 85.2  ? 
# 
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 1994-04-30 
2 'Structure model' 1 1 2008-03-03 
3 'Structure model' 1 2 2011-07-13 
4 'Structure model' 1 3 2012-02-29 
5 'Structure model' 1 4 2017-11-29 
6 'Structure model' 1 5 2019-07-17 
7 'Structure model' 1 6 2019-08-14 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1  2 'Structure model' 'Version format compliance' 
2  3 'Structure model' 'Version format compliance' 
3  4 'Structure model' 'Database references'       
4  5 'Structure model' 'Derived calculations'      
5  5 'Structure model' Other                       
6  6 'Structure model' 'Data collection'           
7  6 'Structure model' 'Derived calculations'      
8  6 'Structure model' 'Refinement description'    
9  7 'Structure model' 'Data collection'           
10 7 'Structure model' 'Refinement description'    
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 5 'Structure model' pdbx_database_status 
2 5 'Structure model' struct_conf          
3 5 'Structure model' struct_conf_type     
4 6 'Structure model' software             
5 6 'Structure model' struct_conn          
6 7 'Structure model' software             
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 5 'Structure model' '_pdbx_database_status.process_site'  
2 6 'Structure model' '_software.classification'            
3 6 'Structure model' '_struct_conn.pdbx_leaving_atom_flag' 
4 7 'Structure model' '_software.classification'            
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
X-PLOR 'model building' . ? 1 
PROLSQ refinement       . ? 2 
X-PLOR refinement       . ? 3 
X-PLOR phasing          . ? 4 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O   B VAL 14  ? ? N   B GLN 15  ? ? 1.74 
2 1 O   A ASP 125 ? ? NZ  A LYS 128 ? ? 2.05 
3 1 ND1 A HIS 80  ? ? OD2 A ASP 83  ? ? 2.09 
4 1 ND1 B HIS 46  ? ? NE2 B HIS 63  ? ? 2.14 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1  1 CB  A THR 2   ? ? OG1 A THR 2   ? ? 1.553 1.428 0.125  0.020 N 
2  1 CD  A GLU 24  ? ? OE2 A GLU 24  ? ? 1.323 1.252 0.071  0.011 N 
3  1 CA  A GLY 27  ? ? C   A GLY 27  ? ? 1.615 1.514 0.101  0.016 N 
4  1 CA  A GLY 41  ? ? C   A GLY 41  ? ? 1.620 1.514 0.106  0.016 N 
5  1 N   A GLY 44  ? ? CA  A GLY 44  ? ? 1.549 1.456 0.093  0.015 N 
6  1 CA  A GLY 56  ? ? C   A GLY 56  ? ? 1.625 1.514 0.111  0.016 N 
7  1 N   A GLY 72  ? ? CA  A GLY 72  ? ? 1.361 1.456 -0.095 0.015 N 
8  1 CG  A HIS 80  ? ? CD2 A HIS 80  ? ? 1.441 1.354 0.087  0.009 N 
9  1 CE1 A HIS 80  ? ? NE2 A HIS 80  ? ? 1.224 1.317 -0.093 0.011 N 
10 1 CB  A SER 98  ? ? OG  A SER 98  ? ? 1.497 1.418 0.079  0.013 N 
11 1 NE2 A HIS 120 ? ? CD2 A HIS 120 ? ? 1.301 1.373 -0.072 0.011 N 
12 1 CA  B GLY 12  ? ? C   B GLY 12  ? ? 1.630 1.514 0.116  0.016 N 
13 1 C   B VAL 14  ? ? N   B GLN 15  ? ? 1.126 1.336 -0.210 0.023 Y 
14 1 N   B ILE 17  ? ? CA  B ILE 17  ? ? 1.581 1.459 0.122  0.020 N 
15 1 N   B GLY 27  ? ? CA  B GLY 27  ? ? 1.551 1.456 0.095  0.015 N 
16 1 N   B GLY 33  ? ? CA  B GLY 33  ? ? 1.634 1.456 0.178  0.015 N 
17 1 N   B GLY 41  ? ? CA  B GLY 41  ? ? 1.581 1.456 0.125  0.015 N 
18 1 CE1 B HIS 63  ? ? NE2 B HIS 63  ? ? 1.250 1.317 -0.067 0.011 N 
19 1 CG  B HIS 71  ? ? CD2 B HIS 71  ? ? 1.427 1.354 0.073  0.009 N 
20 1 CE1 B HIS 80  ? ? NE2 B HIS 80  ? ? 1.232 1.317 -0.085 0.011 N 
21 1 CD  B GLU 132 ? ? OE2 B GLU 132 ? ? 1.332 1.252 0.080  0.011 N 
22 1 N   B GLY 150 ? ? CA  B GLY 150 ? ? 1.589 1.456 0.133  0.015 N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1   1 CB  A ALA 1   ? ? CA  A ALA 1   ? ? C   A ALA 1   ? ? 100.76 110.10 -9.34  1.50 N 
2   1 CA  A ALA 1   ? ? C   A ALA 1   ? ? O   A ALA 1   ? ? 137.78 120.10 17.68  2.10 N 
3   1 CA  A ALA 1   ? ? C   A ALA 1   ? ? N   A THR 2   ? ? 99.64  117.20 -17.56 2.20 Y 
4   1 N   A THR 2   ? ? CA  A THR 2   ? ? CB  A THR 2   ? ? 94.50  110.30 -15.80 1.90 N 
5   1 OG1 A THR 2   ? ? CB  A THR 2   ? ? CG2 A THR 2   ? ? 125.00 110.00 15.00  2.30 N 
6   1 CA  A THR 2   ? ? CB  A THR 2   ? ? OG1 A THR 2   ? ? 95.90  109.00 -13.10 2.10 N 
7   1 N   A THR 2   ? ? CA  A THR 2   ? ? C   A THR 2   ? ? 128.44 111.00 17.44  2.70 N 
8   1 CD  A LYS 3   ? ? CE  A LYS 3   ? ? NZ  A LYS 3   ? ? 96.49  111.70 -15.21 2.30 N 
9   1 CA  A ALA 4   ? ? C   A ALA 4   ? ? N   A VAL 5   ? ? 103.38 117.20 -13.82 2.20 Y 
10  1 O   A ALA 4   ? ? C   A ALA 4   ? ? N   A VAL 5   ? ? 142.32 122.70 19.62  1.60 Y 
11  1 C   A ALA 4   ? ? N   A VAL 5   ? ? CA  A VAL 5   ? ? 98.17  121.70 -23.53 2.50 Y 
12  1 O   A CYS 6   ? ? C   A CYS 6   ? ? N   A VAL 7   ? ? 133.00 122.70 10.30  1.60 Y 
13  1 CA  A LEU 8   ? ? CB  A LEU 8   ? ? CG  A LEU 8   ? ? 131.98 115.30 16.68  2.30 N 
14  1 O   A LEU 8   ? ? C   A LEU 8   ? ? N   A LYS 9   ? ? 137.49 122.70 14.79  1.60 Y 
15  1 CA  A LYS 9   ? ? CB  A LYS 9   ? ? CG  A LYS 9   ? ? 127.04 113.40 13.64  2.20 N 
16  1 CA  A LYS 9   ? ? C   A LYS 9   ? ? N   A GLY 10  ? ? 128.94 116.20 12.74  2.00 Y 
17  1 N   A VAL 14  ? ? CA  A VAL 14  ? ? CB  A VAL 14  ? ? 97.91  111.50 -13.59 2.20 N 
18  1 CA  A VAL 14  ? ? CB  A VAL 14  ? ? CG1 A VAL 14  ? ? 96.58  110.90 -14.32 1.50 N 
19  1 CA  A VAL 14  ? ? CB  A VAL 14  ? ? CG2 A VAL 14  ? ? 124.59 110.90 13.69  1.50 N 
20  1 C   A VAL 14  ? ? N   A GLN 15  ? ? CA  A GLN 15  ? ? 104.28 121.70 -17.42 2.50 Y 
21  1 CA  A GLN 15  ? ? CB  A GLN 15  ? ? CG  A GLN 15  ? ? 130.61 113.40 17.21  2.20 N 
22  1 O   A ASN 19  ? ? C   A ASN 19  ? ? N   A PHE 20  ? ? 133.31 122.70 10.61  1.60 Y 
23  1 C   A ASN 19  ? ? N   A PHE 20  ? ? CA  A PHE 20  ? ? 104.93 121.70 -16.77 2.50 Y 
24  1 CA  A PHE 20  ? ? CB  A PHE 20  ? ? CG  A PHE 20  ? ? 128.85 113.90 14.95  2.40 N 
25  1 CA  A GLU 24  ? ? C   A GLU 24  ? ? O   A GLU 24  ? ? 132.96 120.10 12.86  2.10 N 
26  1 C   A ASN 26  ? ? N   A GLY 27  ? ? CA  A GLY 27  ? ? 95.68  122.30 -26.62 2.10 Y 
27  1 N   A PRO 28  ? ? CA  A PRO 28  ? ? C   A PRO 28  ? ? 136.96 112.10 24.86  2.60 N 
28  1 CA  A PRO 28  ? ? C   A PRO 28  ? ? O   A PRO 28  ? ? 136.19 120.20 15.99  2.40 N 
29  1 CA  A PRO 28  ? ? C   A PRO 28  ? ? N   A VAL 29  ? ? 101.36 117.20 -15.84 2.20 Y 
30  1 CA  A VAL 29  ? ? C   A VAL 29  ? ? N   A LYS 30  ? ? 103.84 117.20 -13.36 2.20 Y 
31  1 O   A VAL 29  ? ? C   A VAL 29  ? ? N   A LYS 30  ? ? 134.90 122.70 12.20  1.60 Y 
32  1 CA  A VAL 31  ? ? C   A VAL 31  ? ? N   A TRP 32  ? ? 103.22 117.20 -13.98 2.20 Y 
33  1 O   A TRP 32  ? ? C   A TRP 32  ? ? N   A GLY 33  ? ? 134.68 123.20 11.48  1.70 Y 
34  1 O   A SER 34  ? ? C   A SER 34  ? ? N   A ILE 35  ? ? 134.34 122.70 11.64  1.60 Y 
35  1 CA  A LEU 38  ? ? C   A LEU 38  ? ? N   A THR 39  ? ? 103.82 117.20 -13.38 2.20 Y 
36  1 C   A LEU 38  ? ? N   A THR 39  ? ? CA  A THR 39  ? ? 145.55 121.70 23.85  2.50 Y 
37  1 O   A LEU 42  ? ? C   A LEU 42  ? ? N   A HIS 43  ? ? 132.94 122.70 10.24  1.60 Y 
38  1 CA  A HIS 43  ? ? CB  A HIS 43  ? ? CG  A HIS 43  ? ? 101.64 113.60 -11.96 1.70 N 
39  1 CA  A PHE 45  ? ? C   A PHE 45  ? ? N   A HIS 46  ? ? 101.18 117.20 -16.02 2.20 Y 
40  1 CB  A HIS 48  ? ? CA  A HIS 48  ? ? C   A HIS 48  ? ? 122.47 110.40 12.07  2.00 N 
41  1 OE1 A GLU 49  ? ? CD  A GLU 49  ? ? OE2 A GLU 49  ? ? 114.67 123.30 -8.63  1.20 N 
42  1 O   A PHE 50  ? ? C   A PHE 50  ? ? N   A GLY 51  ? ? 137.06 123.20 13.86  1.70 Y 
43  1 CA  A ASP 52  ? ? CB  A ASP 52  ? ? CG  A ASP 52  ? ? 128.54 113.40 15.14  2.20 N 
44  1 CB  A ASP 52  ? ? CG  A ASP 52  ? ? OD2 A ASP 52  ? ? 127.24 118.30 8.94   0.90 N 
45  1 C   A GLY 56  ? ? N   A CYS 57  ? ? CA  A CYS 57  ? ? 143.65 121.70 21.95  2.50 Y 
46  1 N   A SER 59  ? ? CA  A SER 59  ? ? CB  A SER 59  ? ? 99.75  110.50 -10.75 1.50 N 
47  1 N   A ALA 60  ? ? CA  A ALA 60  ? ? CB  A ALA 60  ? ? 98.02  110.10 -12.08 1.40 N 
48  1 C   A GLY 61  ? ? N   A PRO 62  ? ? CA  A PRO 62  ? ? 128.90 119.30 9.60   1.50 Y 
49  1 O   A PRO 62  ? ? C   A PRO 62  ? ? N   A HIS 63  ? ? 113.09 122.70 -9.61  1.60 Y 
50  1 N   A ASN 65  ? ? CA  A ASN 65  ? ? C   A ASN 65  ? ? 128.46 111.00 17.46  2.70 N 
51  1 CA  A ASN 65  ? ? C   A ASN 65  ? ? O   A ASN 65  ? ? 106.00 120.10 -14.10 2.10 N 
52  1 CA  A ASN 65  ? ? C   A ASN 65  ? ? N   A PRO 66  ? ? 136.19 117.10 19.09  2.80 Y 
53  1 C   A ASN 65  ? ? N   A PRO 66  ? ? CA  A PRO 66  ? ? 133.57 119.30 14.27  1.50 Y 
54  1 N   A PRO 66  ? ? CA  A PRO 66  ? ? CB  A PRO 66  ? ? 94.21  103.30 -9.09  1.20 N 
55  1 CA  A PRO 66  ? ? C   A PRO 66  ? ? N   A LEU 67  ? ? 130.61 117.20 13.41  2.20 Y 
56  1 N   A LEU 67  ? ? CA  A LEU 67  ? ? CB  A LEU 67  ? ? 125.88 110.40 15.48  2.00 N 
57  1 N   A LEU 67  ? ? CA  A LEU 67  ? ? C   A LEU 67  ? ? 93.99  111.00 -17.01 2.70 N 
58  1 N   A SER 68  ? ? CA  A SER 68  ? ? CB  A SER 68  ? ? 101.47 110.50 -9.03  1.50 N 
59  1 N   A SER 68  ? ? CA  A SER 68  ? ? C   A SER 68  ? ? 132.51 111.00 21.51  2.70 N 
60  1 CA  A SER 68  ? ? C   A SER 68  ? ? O   A SER 68  ? ? 134.40 120.10 14.30  2.10 N 
61  1 CA  A SER 68  ? ? C   A SER 68  ? ? N   A ARG 69  ? ? 99.83  117.20 -17.37 2.20 Y 
62  1 NH1 A ARG 69  ? ? CZ  A ARG 69  ? ? NH2 A ARG 69  ? ? 130.69 119.40 11.29  1.10 N 
63  1 NE  A ARG 69  ? ? CZ  A ARG 69  ? ? NH1 A ARG 69  ? ? 112.61 120.30 -7.69  0.50 N 
64  1 NE  A ARG 69  ? ? CZ  A ARG 69  ? ? NH2 A ARG 69  ? ? 116.69 120.30 -3.61  0.50 N 
65  1 CB  A HIS 71  ? ? CG  A HIS 71  ? ? CD2 A HIS 71  ? ? 119.25 129.70 -10.45 1.60 N 
66  1 C   A HIS 71  ? ? N   A GLY 72  ? ? CA  A GLY 72  ? ? 135.42 122.30 13.12  2.10 Y 
67  1 N   A PRO 74  ? ? CD  A PRO 74  ? ? CG  A PRO 74  ? ? 91.65  103.20 -11.55 1.50 N 
68  1 CA  A LYS 75  ? ? CB  A LYS 75  ? ? CG  A LYS 75  ? ? 129.97 113.40 16.57  2.20 N 
69  1 N   A ASP 76  ? ? CA  A ASP 76  ? ? CB  A ASP 76  ? ? 96.10  110.60 -14.50 1.80 N 
70  1 O   A ASP 76  ? ? C   A ASP 76  ? ? N   A GLU 77  ? ? 111.92 122.70 -10.78 1.60 Y 
71  1 N   A GLU 77  ? ? CA  A GLU 77  ? ? CB  A GLU 77  ? ? 123.19 110.60 12.59  1.80 N 
72  1 OE1 A GLU 77  ? ? CD  A GLU 77  ? ? OE2 A GLU 77  ? ? 108.89 123.30 -14.41 1.20 N 
73  1 CG  A GLU 77  ? ? CD  A GLU 77  ? ? OE1 A GLU 77  ? ? 131.45 118.30 13.15  2.00 N 
74  1 N   A GLU 78  ? ? CA  A GLU 78  ? ? CB  A GLU 78  ? ? 131.57 110.60 20.97  1.80 N 
75  1 CA  A GLU 78  ? ? CB  A GLU 78  ? ? CG  A GLU 78  ? ? 129.37 113.40 15.97  2.20 N 
76  1 N   A GLU 78  ? ? CA  A GLU 78  ? ? C   A GLU 78  ? ? 89.08  111.00 -21.92 2.70 N 
77  1 CA  A HIS 80  ? ? CB  A HIS 80  ? ? CG  A HIS 80  ? ? 125.68 113.60 12.08  1.70 N 
78  1 CB  A HIS 80  ? ? CG  A HIS 80  ? ? CD2 A HIS 80  ? ? 114.09 129.70 -15.61 1.60 N 
79  1 CB  A HIS 80  ? ? CG  A HIS 80  ? ? ND1 A HIS 80  ? ? 140.85 123.20 17.65  2.50 N 
80  1 CB  A ASN 86  ? ? CA  A ASN 86  ? ? C   A ASN 86  ? ? 127.06 110.40 16.66  2.00 N 
81  1 N   A ASN 86  ? ? CA  A ASN 86  ? ? C   A ASN 86  ? ? 93.40  111.00 -17.60 2.70 N 
82  1 CA  A ALA 89  ? ? C   A ALA 89  ? ? N   A ASP 90  ? ? 130.42 117.20 13.22  2.20 Y 
83  1 N   A ASP 90  ? ? CA  A ASP 90  ? ? C   A ASP 90  ? ? 94.63  111.00 -16.37 2.70 N 
84  1 CD  A LYS 91  ? ? CE  A LYS 91  ? ? NZ  A LYS 91  ? ? 92.23  111.70 -19.47 2.30 N 
85  1 O   A LYS 91  ? ? C   A LYS 91  ? ? N   A ASP 92  ? ? 134.27 122.70 11.57  1.60 Y 
86  1 N   A VAL 94  ? ? CA  A VAL 94  ? ? C   A VAL 94  ? ? 94.47  111.00 -16.53 2.70 N 
87  1 CB  A ASP 96  ? ? CG  A ASP 96  ? ? OD2 A ASP 96  ? ? 111.95 118.30 -6.35  0.90 N 
88  1 N   A SER 98  ? ? CA  A SER 98  ? ? CB  A SER 98  ? ? 125.38 110.50 14.88  1.50 N 
89  1 O   A ILE 99  ? ? C   A ILE 99  ? ? N   A GLU 100 ? ? 132.40 122.70 9.70   1.60 Y 
90  1 O   A SER 107 ? ? C   A SER 107 ? ? N   A GLY 108 ? ? 138.35 123.20 15.15  1.70 Y 
91  1 OD1 A ASP 109 ? ? CG  A ASP 109 ? ? OD2 A ASP 109 ? ? 110.20 123.30 -13.10 1.90 N 
92  1 CB  A ASP 109 ? ? CG  A ASP 109 ? ? OD2 A ASP 109 ? ? 127.09 118.30 8.79   0.90 N 
93  1 CB  A HIS 110 ? ? CA  A HIS 110 ? ? C   A HIS 110 ? ? 122.64 110.40 12.24  2.00 N 
94  1 N   A HIS 110 ? ? CA  A HIS 110 ? ? CB  A HIS 110 ? ? 96.71  110.60 -13.89 1.80 N 
95  1 CB  A CYS 111 ? ? CA  A CYS 111 ? ? C   A CYS 111 ? ? 123.00 111.50 11.50  1.20 N 
96  1 CD  A ARG 115 ? ? NE  A ARG 115 ? ? CZ  A ARG 115 ? ? 135.56 123.60 11.96  1.40 N 
97  1 NE  A ARG 115 ? ? CZ  A ARG 115 ? ? NH1 A ARG 115 ? ? 126.80 120.30 6.50   0.50 N 
98  1 NE  A ARG 115 ? ? CZ  A ARG 115 ? ? NH2 A ARG 115 ? ? 110.29 120.30 -10.01 0.50 N 
99  1 OG1 A THR 116 ? ? CB  A THR 116 ? ? CG2 A THR 116 ? ? 95.63  110.00 -14.37 2.30 N 
100 1 CA  A THR 116 ? ? CB  A THR 116 ? ? CG2 A THR 116 ? ? 125.65 112.40 13.25  1.40 N 
101 1 O   A THR 116 ? ? C   A THR 116 ? ? N   A LEU 117 ? ? 133.62 122.70 10.92  1.60 Y 
102 1 CA  A LEU 117 ? ? C   A LEU 117 ? ? N   A VAL 118 ? ? 101.93 117.20 -15.27 2.20 Y 
103 1 O   A LEU 117 ? ? C   A LEU 117 ? ? N   A VAL 118 ? ? 134.66 122.70 11.96  1.60 Y 
104 1 OE1 A GLU 121 ? ? CD  A GLU 121 ? ? OE2 A GLU 121 ? ? 132.96 123.30 9.66   1.20 N 
105 1 O   A LYS 122 ? ? C   A LYS 122 ? ? N   A ALA 123 ? ? 111.99 122.70 -10.71 1.60 Y 
106 1 C   A LYS 122 ? ? N   A ALA 123 ? ? CA  A ALA 123 ? ? 140.17 121.70 18.47  2.50 Y 
107 1 N   A ALA 123 ? ? CA  A ALA 123 ? ? CB  A ALA 123 ? ? 100.54 110.10 -9.56  1.40 N 
108 1 CB  A ASP 124 ? ? CG  A ASP 124 ? ? OD2 A ASP 124 ? ? 109.86 118.30 -8.44  0.90 N 
109 1 O   A ASP 124 ? ? C   A ASP 124 ? ? N   A ASP 125 ? ? 134.51 122.70 11.81  1.60 Y 
110 1 CB  A ASP 125 ? ? CG  A ASP 125 ? ? OD1 A ASP 125 ? ? 125.09 118.30 6.79   0.90 N 
111 1 CB  A ASP 125 ? ? CG  A ASP 125 ? ? OD2 A ASP 125 ? ? 108.19 118.30 -10.11 0.90 N 
112 1 C   A ASP 125 ? ? N   A LEU 126 ? ? CA  A LEU 126 ? ? 143.89 121.70 22.19  2.50 Y 
113 1 N   A GLY 129 ? ? CA  A GLY 129 ? ? C   A GLY 129 ? ? 128.12 113.10 15.02  2.50 N 
114 1 C   A GLY 129 ? ? N   A GLY 130 ? ? CA  A GLY 130 ? ? 136.14 122.30 13.84  2.10 Y 
115 1 CB  A ASN 131 ? ? CG  A ASN 131 ? ? ND2 A ASN 131 ? ? 134.04 116.70 17.34  2.40 N 
116 1 O   A GLU 133 ? ? C   A GLU 133 ? ? N   A SER 134 ? ? 132.33 122.70 9.63   1.60 Y 
117 1 N   A GLY 138 ? ? CA  A GLY 138 ? ? C   A GLY 138 ? ? 97.87  113.10 -15.23 2.50 N 
118 1 N   A ALA 140 ? ? CA  A ALA 140 ? ? CB  A ALA 140 ? ? 101.05 110.10 -9.05  1.40 N 
119 1 C   A SER 142 ? ? N   A ARG 143 ? ? CA  A ARG 143 ? ? 137.60 121.70 15.90  2.50 Y 
120 1 NE  A ARG 143 ? ? CZ  A ARG 143 ? ? NH1 A ARG 143 ? ? 115.12 120.30 -5.18  0.50 N 
121 1 N   A ARG 143 ? ? CA  A ARG 143 ? ? C   A ARG 143 ? ? 92.42  111.00 -18.58 2.70 N 
122 1 O   A ALA 145 ? ? C   A ALA 145 ? ? N   A CYS 146 ? ? 135.00 122.70 12.30  1.60 Y 
123 1 C   A ALA 145 ? ? N   A CYS 146 ? ? CA  A CYS 146 ? ? 105.32 121.70 -16.38 2.50 Y 
124 1 CA  A CYS 146 ? ? CB  A CYS 146 ? ? SG  A CYS 146 ? ? 122.55 114.20 8.35   1.10 N 
125 1 O   A CYS 146 ? ? C   A CYS 146 ? ? N   A GLY 147 ? ? 142.04 123.20 18.84  1.70 Y 
126 1 CB  B THR 2   ? ? CA  B THR 2   ? ? C   B THR 2   ? ? 128.87 111.60 17.27  2.70 N 
127 1 C   B THR 2   ? ? N   B LYS 3   ? ? CA  B LYS 3   ? ? 140.28 121.70 18.58  2.50 Y 
128 1 N   B LYS 3   ? ? CA  B LYS 3   ? ? CB  B LYS 3   ? ? 99.33  110.60 -11.27 1.80 N 
129 1 O   B ALA 4   ? ? C   B ALA 4   ? ? N   B VAL 5   ? ? 140.43 122.70 17.73  1.60 Y 
130 1 C   B ALA 4   ? ? N   B VAL 5   ? ? CA  B VAL 5   ? ? 100.94 121.70 -20.76 2.50 Y 
131 1 CG1 B VAL 5   ? ? CB  B VAL 5   ? ? CG2 B VAL 5   ? ? 96.65  110.90 -14.25 1.60 N 
132 1 N   B VAL 7   ? ? CA  B VAL 7   ? ? C   B VAL 7   ? ? 94.02  111.00 -16.98 2.70 N 
133 1 N   B GLY 12  ? ? CA  B GLY 12  ? ? C   B GLY 12  ? ? 92.64  113.10 -20.46 2.50 N 
134 1 CA  B PRO 13  ? ? C   B PRO 13  ? ? O   B PRO 13  ? ? 105.62 120.20 -14.58 2.40 N 
135 1 CA  B VAL 14  ? ? C   B VAL 14  ? ? O   B VAL 14  ? ? 139.49 120.10 19.39  2.10 N 
136 1 O   B VAL 14  ? ? C   B VAL 14  ? ? N   B GLN 15  ? ? 96.21  122.70 -26.49 1.60 Y 
137 1 C   B VAL 14  ? ? N   B GLN 15  ? ? CA  B GLN 15  ? ? 160.69 121.70 38.99  2.50 Y 
138 1 CA  B GLN 15  ? ? CB  B GLN 15  ? ? CG  B GLN 15  ? ? 131.21 113.40 17.81  2.20 N 
139 1 CA  B ILE 18  ? ? CB  B ILE 18  ? ? CG2 B ILE 18  ? ? 127.43 110.90 16.53  2.00 N 
140 1 CA  B ASN 19  ? ? C   B ASN 19  ? ? N   B PHE 20  ? ? 101.07 117.20 -16.13 2.20 Y 
141 1 O   B ASN 19  ? ? C   B ASN 19  ? ? N   B PHE 20  ? ? 139.79 122.70 17.09  1.60 Y 
142 1 O   B PHE 20  ? ? C   B PHE 20  ? ? N   B GLU 21  ? ? 132.31 122.70 9.61   1.60 Y 
143 1 N   B GLU 21  ? ? CA  B GLU 21  ? ? CB  B GLU 21  ? ? 126.13 110.60 15.53  1.80 N 
144 1 N   B GLY 27  ? ? CA  B GLY 27  ? ? C   B GLY 27  ? ? 96.22  113.10 -16.88 2.50 N 
145 1 O   B VAL 29  ? ? C   B VAL 29  ? ? N   B LYS 30  ? ? 138.03 122.70 15.33  1.60 Y 
146 1 CA  B TRP 32  ? ? C   B TRP 32  ? ? N   B GLY 33  ? ? 103.16 116.20 -13.04 2.00 Y 
147 1 O   B TRP 32  ? ? C   B TRP 32  ? ? N   B GLY 33  ? ? 138.31 123.20 15.11  1.70 Y 
148 1 C   B TRP 32  ? ? N   B GLY 33  ? ? CA  B GLY 33  ? ? 103.20 122.30 -19.10 2.10 Y 
149 1 N   B SER 34  ? ? CA  B SER 34  ? ? CB  B SER 34  ? ? 122.99 110.50 12.49  1.50 N 
150 1 O   B LYS 36  ? ? C   B LYS 36  ? ? N   B GLY 37  ? ? 137.42 123.20 14.22  1.70 Y 
151 1 CB  B LEU 38  ? ? CG  B LEU 38  ? ? CD1 B LEU 38  ? ? 122.56 111.00 11.56  1.70 N 
152 1 CA  B GLU 40  ? ? CB  B GLU 40  ? ? CG  B GLU 40  ? ? 128.29 113.40 14.89  2.20 N 
153 1 OE1 B GLU 40  ? ? CD  B GLU 40  ? ? OE2 B GLU 40  ? ? 114.61 123.30 -8.69  1.20 N 
154 1 CG  B GLU 40  ? ? CD  B GLU 40  ? ? OE1 B GLU 40  ? ? 132.08 118.30 13.78  2.00 N 
155 1 N   B GLU 40  ? ? CA  B GLU 40  ? ? C   B GLU 40  ? ? 127.62 111.00 16.62  2.70 N 
156 1 CA  B GLU 40  ? ? C   B GLU 40  ? ? O   B GLU 40  ? ? 134.38 120.10 14.28  2.10 N 
157 1 CA  B GLU 40  ? ? C   B GLU 40  ? ? N   B GLY 41  ? ? 100.07 116.20 -16.13 2.00 Y 
158 1 C   B GLU 40  ? ? N   B GLY 41  ? ? CA  B GLY 41  ? ? 103.28 122.30 -19.02 2.10 Y 
159 1 N   B LEU 42  ? ? CA  B LEU 42  ? ? CB  B LEU 42  ? ? 92.16  110.40 -18.24 2.00 N 
160 1 N   B LEU 42  ? ? CA  B LEU 42  ? ? C   B LEU 42  ? ? 130.20 111.00 19.20  2.70 N 
161 1 CA  B LEU 42  ? ? C   B LEU 42  ? ? O   B LEU 42  ? ? 134.23 120.10 14.13  2.10 N 
162 1 N   B HIS 43  ? ? CA  B HIS 43  ? ? CB  B HIS 43  ? ? 99.41  110.60 -11.19 1.80 N 
163 1 CA  B HIS 43  ? ? CB  B HIS 43  ? ? CG  B HIS 43  ? ? 102.74 113.60 -10.86 1.70 N 
164 1 CA  B PHE 45  ? ? C   B PHE 45  ? ? N   B HIS 46  ? ? 96.83  117.20 -20.37 2.20 Y 
165 1 O   B PHE 45  ? ? C   B PHE 45  ? ? N   B HIS 46  ? ? 137.56 122.70 14.86  1.60 Y 
166 1 CA  B HIS 48  ? ? C   B HIS 48  ? ? N   B GLU 49  ? ? 103.83 117.20 -13.37 2.20 Y 
167 1 O   B PHE 50  ? ? C   B PHE 50  ? ? N   B GLY 51  ? ? 133.54 123.20 10.34  1.70 Y 
168 1 N   B ASP 52  ? ? CA  B ASP 52  ? ? C   B ASP 52  ? ? 92.92  111.00 -18.08 2.70 N 
169 1 N   B THR 54  ? ? CA  B THR 54  ? ? CB  B THR 54  ? ? 98.23  110.30 -12.07 1.90 N 
170 1 CA  B THR 54  ? ? CB  B THR 54  ? ? OG1 B THR 54  ? ? 95.72  109.00 -13.28 2.10 N 
171 1 N   B ALA 55  ? ? CA  B ALA 55  ? ? CB  B ALA 55  ? ? 124.12 110.10 14.02  1.40 N 
172 1 N   B ALA 55  ? ? CA  B ALA 55  ? ? C   B ALA 55  ? ? 85.26  111.00 -25.74 2.70 N 
173 1 O   B ALA 55  ? ? C   B ALA 55  ? ? N   B GLY 56  ? ? 136.91 123.20 13.71  1.70 Y 
174 1 CA  B CYS 57  ? ? CB  B CYS 57  ? ? SG  B CYS 57  ? ? 121.07 114.20 6.87   1.10 N 
175 1 CA  B THR 58  ? ? CB  B THR 58  ? ? CG2 B THR 58  ? ? 98.95  112.40 -13.45 1.40 N 
176 1 N   B ALA 60  ? ? CA  B ALA 60  ? ? CB  B ALA 60  ? ? 99.64  110.10 -10.46 1.40 N 
177 1 C   B GLY 61  ? ? N   B PRO 62  ? ? CA  B PRO 62  ? ? 129.54 119.30 10.24  1.50 Y 
178 1 N   B PRO 62  ? ? CD  B PRO 62  ? ? CG  B PRO 62  ? ? 93.10  103.20 -10.10 1.50 N 
179 1 CA  B HIS 63  ? ? CB  B HIS 63  ? ? CG  B HIS 63  ? ? 100.41 113.60 -13.19 1.70 N 
180 1 CE1 B HIS 63  ? ? NE2 B HIS 63  ? ? CD2 B HIS 63  ? ? 115.21 109.00 6.21   0.70 N 
181 1 N   B PHE 64  ? ? CA  B PHE 64  ? ? CB  B PHE 64  ? ? 124.14 110.60 13.54  1.80 N 
182 1 CA  B PHE 64  ? ? C   B PHE 64  ? ? O   B PHE 64  ? ? 133.56 120.10 13.46  2.10 N 
183 1 CA  B PHE 64  ? ? C   B PHE 64  ? ? N   B ASN 65  ? ? 100.59 117.20 -16.61 2.20 Y 
184 1 C   B PRO 66  ? ? N   B LEU 67  ? ? CA  B LEU 67  ? ? 140.18 121.70 18.48  2.50 Y 
185 1 NE  B ARG 69  ? ? CZ  B ARG 69  ? ? NH1 B ARG 69  ? ? 126.42 120.30 6.12   0.50 N 
186 1 CB  B HIS 71  ? ? CG  B HIS 71  ? ? CD2 B HIS 71  ? ? 116.31 129.70 -13.39 1.60 N 
187 1 CA  B HIS 71  ? ? C   B HIS 71  ? ? N   B GLY 72  ? ? 97.76  116.20 -18.44 2.00 Y 
188 1 O   B HIS 71  ? ? C   B HIS 71  ? ? N   B GLY 72  ? ? 133.89 123.20 10.69  1.70 Y 
189 1 CA  B GLY 72  ? ? C   B GLY 72  ? ? N   B GLY 73  ? ? 99.25  116.20 -16.95 2.00 Y 
190 1 C   B GLY 72  ? ? N   B GLY 73  ? ? CA  B GLY 73  ? ? 105.10 122.30 -17.20 2.10 Y 
191 1 N   B GLY 73  ? ? CA  B GLY 73  ? ? C   B GLY 73  ? ? 95.01  113.10 -18.09 2.50 N 
192 1 O   B LYS 75  ? ? C   B LYS 75  ? ? N   B ASP 76  ? ? 111.12 122.70 -11.58 1.60 Y 
193 1 CA  B GLU 77  ? ? CB  B GLU 77  ? ? CG  B GLU 77  ? ? 131.03 113.40 17.63  2.20 N 
194 1 N   B GLU 77  ? ? CA  B GLU 77  ? ? C   B GLU 77  ? ? 93.75  111.00 -17.25 2.70 N 
195 1 CA  B ARG 79  ? ? CB  B ARG 79  ? ? CG  B ARG 79  ? ? 127.84 113.40 14.44  2.20 N 
196 1 CB  B ARG 79  ? ? CG  B ARG 79  ? ? CD  B ARG 79  ? ? 140.29 111.60 28.69  2.60 N 
197 1 CE1 B HIS 80  ? ? NE2 B HIS 80  ? ? CD2 B HIS 80  ? ? 113.72 109.00 4.72   0.70 N 
198 1 C   B HIS 80  ? ? N   B VAL 81  ? ? CA  B VAL 81  ? ? 138.90 121.70 17.20  2.50 Y 
199 1 N   B VAL 81  ? ? CA  B VAL 81  ? ? CB  B VAL 81  ? ? 125.97 111.50 14.47  2.20 N 
200 1 CB  B ASP 83  ? ? CG  B ASP 83  ? ? OD1 B ASP 83  ? ? 110.05 118.30 -8.25  0.90 N 
201 1 CA  B GLY 85  ? ? C   B GLY 85  ? ? O   B GLY 85  ? ? 135.26 120.60 14.66  1.80 N 
202 1 CG1 B VAL 87  ? ? CB  B VAL 87  ? ? CG2 B VAL 87  ? ? 96.36  110.90 -14.54 1.60 N 
203 1 CA  B VAL 87  ? ? CB  B VAL 87  ? ? CG1 B VAL 87  ? ? 128.10 110.90 17.20  1.50 N 
204 1 CB  B ASP 90  ? ? CG  B ASP 90  ? ? OD2 B ASP 90  ? ? 112.68 118.30 -5.62  0.90 N 
205 1 CB  B LYS 91  ? ? CA  B LYS 91  ? ? C   B LYS 91  ? ? 97.30  110.40 -13.10 2.00 N 
206 1 N   B LYS 91  ? ? CA  B LYS 91  ? ? CB  B LYS 91  ? ? 123.74 110.60 13.14  1.80 N 
207 1 CB  B ASP 92  ? ? CG  B ASP 92  ? ? OD2 B ASP 92  ? ? 112.30 118.30 -6.00  0.90 N 
208 1 O   B GLY 93  ? ? C   B GLY 93  ? ? N   B VAL 94  ? ? 134.85 122.70 12.15  1.60 Y 
209 1 N   B ALA 95  ? ? CA  B ALA 95  ? ? CB  B ALA 95  ? ? 121.02 110.10 10.92  1.40 N 
210 1 O   B ASP 96  ? ? C   B ASP 96  ? ? N   B VAL 97  ? ? 133.99 122.70 11.29  1.60 Y 
211 1 C   B ASP 96  ? ? N   B VAL 97  ? ? CA  B VAL 97  ? ? 102.14 121.70 -19.56 2.50 Y 
212 1 N   B ILE 99  ? ? CA  B ILE 99  ? ? CB  B ILE 99  ? ? 126.30 110.80 15.50  2.30 N 
213 1 CB  B GLU 100 ? ? CA  B GLU 100 ? ? C   B GLU 100 ? ? 97.86  110.40 -12.54 2.00 N 
214 1 N   B GLU 100 ? ? CA  B GLU 100 ? ? CB  B GLU 100 ? ? 129.29 110.60 18.69  1.80 N 
215 1 N   B ASP 101 ? ? CA  B ASP 101 ? ? CB  B ASP 101 ? ? 122.80 110.60 12.20  1.80 N 
216 1 CB  B ASP 101 ? ? CG  B ASP 101 ? ? OD2 B ASP 101 ? ? 127.97 118.30 9.67   0.90 N 
217 1 O   B ASP 101 ? ? C   B ASP 101 ? ? N   B SER 102 ? ? 142.50 122.70 19.80  1.60 Y 
218 1 N   B ILE 104 ? ? CA  B ILE 104 ? ? CB  B ILE 104 ? ? 95.67  110.80 -15.13 2.30 N 
219 1 CA  B ILE 104 ? ? CB  B ILE 104 ? ? CG1 B ILE 104 ? ? 99.34  111.00 -11.66 1.90 N 
220 1 CA  B ILE 104 ? ? C   B ILE 104 ? ? O   B ILE 104 ? ? 132.89 120.10 12.79  2.10 N 
221 1 N   B SER 107 ? ? CA  B SER 107 ? ? CB  B SER 107 ? ? 121.04 110.50 10.54  1.50 N 
222 1 CA  B SER 107 ? ? CB  B SER 107 ? ? OG  B SER 107 ? ? 127.70 111.20 16.50  2.70 N 
223 1 CA  B SER 107 ? ? C   B SER 107 ? ? O   B SER 107 ? ? 104.96 120.10 -15.14 2.10 N 
224 1 CA  B HIS 110 ? ? CB  B HIS 110 ? ? CG  B HIS 110 ? ? 133.02 113.60 19.42  1.70 N 
225 1 NE  B ARG 115 ? ? CZ  B ARG 115 ? ? NH2 B ARG 115 ? ? 115.77 120.30 -4.53  0.50 N 
226 1 O   B ARG 115 ? ? C   B ARG 115 ? ? N   B THR 116 ? ? 132.85 122.70 10.15  1.60 Y 
227 1 O   B THR 116 ? ? C   B THR 116 ? ? N   B LEU 117 ? ? 133.60 122.70 10.90  1.60 Y 
228 1 CB  B LEU 117 ? ? CA  B LEU 117 ? ? C   B LEU 117 ? ? 121.98 110.20 11.78  1.90 N 
229 1 CA  B VAL 119 ? ? CB  B VAL 119 ? ? CG1 B VAL 119 ? ? 120.84 110.90 9.94   1.50 N 
230 1 CA  B HIS 120 ? ? CB  B HIS 120 ? ? CG  B HIS 120 ? ? 102.98 113.60 -10.62 1.70 N 
231 1 OE1 B GLU 121 ? ? CD  B GLU 121 ? ? OE2 B GLU 121 ? ? 130.61 123.30 7.31   1.20 N 
232 1 N   B LYS 122 ? ? CA  B LYS 122 ? ? CB  B LYS 122 ? ? 98.59  110.60 -12.01 1.80 N 
233 1 CA  B LYS 122 ? ? CB  B LYS 122 ? ? CG  B LYS 122 ? ? 129.55 113.40 16.15  2.20 N 
234 1 CB  B ALA 123 ? ? CA  B ALA 123 ? ? C   B ALA 123 ? ? 119.57 110.10 9.47   1.50 N 
235 1 N   B ALA 123 ? ? CA  B ALA 123 ? ? CB  B ALA 123 ? ? 99.85  110.10 -10.25 1.40 N 
236 1 O   B ASP 124 ? ? C   B ASP 124 ? ? N   B ASP 125 ? ? 133.54 122.70 10.84  1.60 Y 
237 1 CB  B ASP 125 ? ? CG  B ASP 125 ? ? OD2 B ASP 125 ? ? 125.16 118.30 6.86   0.90 N 
238 1 N   B GLU 132 ? ? CA  B GLU 132 ? ? CB  B GLU 132 ? ? 121.95 110.60 11.35  1.80 N 
239 1 OG1 B THR 135 ? ? CB  B THR 135 ? ? CG2 B THR 135 ? ? 128.77 110.00 18.77  2.30 N 
240 1 CA  B THR 135 ? ? CB  B THR 135 ? ? OG1 B THR 135 ? ? 91.22  109.00 -17.78 2.10 N 
241 1 CB  B LYS 136 ? ? CG  B LYS 136 ? ? CD  B LYS 136 ? ? 131.09 111.60 19.49  2.60 N 
242 1 CA  B LYS 136 ? ? C   B LYS 136 ? ? N   B THR 137 ? ? 100.59 117.20 -16.61 2.20 Y 
243 1 NE  B ARG 143 ? ? CZ  B ARG 143 ? ? NH1 B ARG 143 ? ? 131.45 120.30 11.15  0.50 N 
244 1 NE  B ARG 143 ? ? CZ  B ARG 143 ? ? NH2 B ARG 143 ? ? 114.16 120.30 -6.14  0.50 N 
245 1 N   B ARG 143 ? ? CA  B ARG 143 ? ? C   B ARG 143 ? ? 93.57  111.00 -17.43 2.70 N 
246 1 CA  B LEU 144 ? ? CB  B LEU 144 ? ? CG  B LEU 144 ? ? 143.01 115.30 27.71  2.30 N 
247 1 CB  B LEU 144 ? ? CG  B LEU 144 ? ? CD1 B LEU 144 ? ? 125.17 111.00 14.17  1.70 N 
248 1 CA  B VAL 148 ? ? CB  B VAL 148 ? ? CG2 B VAL 148 ? ? 122.48 110.90 11.58  1.50 N 
249 1 CB  B ILE 149 ? ? CA  B ILE 149 ? ? C   B ILE 149 ? ? 98.75  111.60 -12.85 2.00 N 
250 1 N   B ILE 149 ? ? CA  B ILE 149 ? ? CB  B ILE 149 ? ? 125.75 110.80 14.95  2.30 N 
251 1 CA  B ILE 149 ? ? CB  B ILE 149 ? ? CG1 B ILE 149 ? ? 128.16 111.00 17.16  1.90 N 
252 1 C   B ILE 149 ? ? N   B GLY 150 ? ? CA  B GLY 150 ? ? 104.47 122.30 -17.83 2.10 Y 
253 1 N   B ILE 151 ? ? CA  B ILE 151 ? ? CB  B ILE 151 ? ? 125.96 110.80 15.16  2.30 N 
# 
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   ? ? 69.04   157.68  
2  1 LYS A 3   ? ? -24.21  104.25  
3  1 CYS A 6   ? ? 176.94  136.36  
4  1 LYS A 23  ? ? -82.16  -142.23 
5  1 GLU A 24  ? ? -3.67   115.52  
6  1 SER A 25  ? ? 14.62   -81.97  
7  1 PRO A 28  ? ? -58.39  96.50   
8  1 GLU A 40  ? ? -59.77  178.19  
9  1 PHE A 45  ? ? -158.93 88.49   
10 1 ALA A 55  ? ? -155.39 80.06   
11 1 PRO A 62  ? ? -72.45  -163.47 
12 1 PHE A 64  ? ? -40.50  104.95  
13 1 PRO A 66  ? ? 6.22    -45.93  
14 1 SER A 68  ? ? -54.56  97.73   
15 1 ASP A 76  ? ? -93.06  -159.98 
16 1 LEU A 84  ? ? -83.29  -106.68 
17 1 ASP A 90  ? ? -97.07  -144.35 
18 1 ASP A 92  ? ? 35.12   48.82   
19 1 GLU A 100 ? ? -150.68 57.18   
20 1 SER A 105 ? ? -107.56 -164.30 
21 1 LEU A 106 ? ? -143.30 13.42   
22 1 SER A 107 ? ? 171.20  88.19   
23 1 ASP A 109 ? ? 51.72   -112.15 
24 1 HIS A 110 ? ? -65.70  64.87   
25 1 LEU A 126 ? ? 44.02   19.45   
26 1 LYS A 128 ? ? -56.95  -4.63   
27 1 SER A 134 ? ? -92.21  -69.94  
28 1 THR A 135 ? ? -30.34  -31.86  
29 1 LYS A 136 ? ? -72.20  -78.00  
30 1 ASN A 139 ? ? 59.21   4.38    
31 1 ALA A 140 ? ? -62.60  46.36   
32 1 ALA A 152 ? ? -81.29  -137.07 
33 1 GLN B 15  ? ? -34.04  111.34  
34 1 GLN B 22  ? ? 174.59  125.21  
35 1 LYS B 23  ? ? -126.54 -153.28 
36 1 GLU B 24  ? ? 24.01   54.47   
37 1 SER B 25  ? ? 59.92   -30.83  
38 1 ASN B 26  ? ? -161.13 54.27   
39 1 ASN B 53  ? ? -149.15 33.46   
40 1 SER B 68  ? ? 82.65   40.80   
41 1 LYS B 70  ? ? -104.78 -159.36 
42 1 HIS B 80  ? ? -8.58   -72.77  
43 1 VAL B 81  ? ? 143.96  -38.65  
44 1 ASP B 90  ? ? -36.71  127.10  
45 1 LYS B 91  ? ? 14.63   -67.88  
46 1 ILE B 104 ? ? -93.10  50.81   
47 1 SER B 107 ? ? -158.69 -116.06 
48 1 ASP B 109 ? ? 81.57   162.94  
49 1 HIS B 110 ? ? 55.73   16.79   
50 1 ASP B 125 ? ? -91.92  42.88   
51 1 LEU B 126 ? ? 51.48   -11.89  
52 1 ASN B 131 ? ? -175.66 122.69  
53 1 GLU B 133 ? ? -179.98 -69.51  
54 1 LYS B 136 ? ? -68.63  -73.05  
55 1 ASN B 139 ? ? 19.52   29.06   
56 1 SER B 142 ? ? -48.74  172.37  
57 1 ALA B 145 ? ? 176.36  146.81  
# 
loop_
_pdbx_validate_polymer_linkage.id 
_pdbx_validate_polymer_linkage.PDB_model_num 
_pdbx_validate_polymer_linkage.auth_atom_id_1 
_pdbx_validate_polymer_linkage.auth_asym_id_1 
_pdbx_validate_polymer_linkage.auth_comp_id_1 
_pdbx_validate_polymer_linkage.auth_seq_id_1 
_pdbx_validate_polymer_linkage.PDB_ins_code_1 
_pdbx_validate_polymer_linkage.label_alt_id_1 
_pdbx_validate_polymer_linkage.auth_atom_id_2 
_pdbx_validate_polymer_linkage.auth_asym_id_2 
_pdbx_validate_polymer_linkage.auth_comp_id_2 
_pdbx_validate_polymer_linkage.auth_seq_id_2 
_pdbx_validate_polymer_linkage.PDB_ins_code_2 
_pdbx_validate_polymer_linkage.label_alt_id_2 
_pdbx_validate_polymer_linkage.dist 
1 1 C A ACE 0  ? ? N A ALA 1  ? ? 1.85 
2 1 C B ACE 0  ? ? N B ALA 1  ? ? 1.80 
3 1 C B VAL 14 ? ? N B GLN 15 ? ? 1.13 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'COPPER (II) ION' CU 
3 'ZINC ION'        ZN 
# 
