3u8v.cif

data_3U8V
# 
_entry.id   3U8V 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.281 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   3U8V         
RCSB  RCSB068452   
WWPDB D_1000068452 
# 
_pdbx_database_PDB_obs_spr.id               SPRSDE 
_pdbx_database_PDB_obs_spr.date             2011-11-09 
_pdbx_database_PDB_obs_spr.pdb_id           3U8V 
_pdbx_database_PDB_obs_spr.replace_pdb_id   3DFB 
_pdbx_database_PDB_obs_spr.details          ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        3U8V 
_pdbx_database_status.recvd_initial_deposition_date   2011-10-17 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Allen, J.P.'     1 
'Francisco, W.A.' 2 
# 
_citation.id                        primary 
_citation.title                     'Three dimensional structure of the Small Metal Binding Protein, SMBP' 
_citation.journal_abbrev            'To be Published' 
_citation.journal_volume            ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.year                      ? 
_citation.journal_id_ASTM           ? 
_citation.country                   ? 
_citation.journal_id_ISSN           ? 
_citation.journal_id_CSD            0353 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_DOI      ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Allen, J.P.'     1 
primary 'Francisco, W.A.' 2 
# 
_cell.entry_id           3U8V 
_cell.length_a           35.660 
_cell.length_b           56.207 
_cell.length_c           83.923 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        90.00 
_cell.Z_PDB              8 
_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                         3U8V 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_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     nat 'Metal-binding protein smbP' 9890.737 2  ? ? ? ? 
2 non-polymer syn 'NICKEL (II) ION'            58.693   1  ? ? ? ? 
3 water       nat water                        18.015   97 ? ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;SGHTAHVDEAVKHAEEAVAHGKEGHTDQLLEHAKESLTHAKAASEAGGNTHVGHGIKHLEDAIKHGEEGHVGVATKHAQE
AIEHLRASEHKSH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SGHTAHVDEAVKHAEEAVAHGKEGHTDQLLEHAKESLTHAKAASEAGGNTHVGHGIKHLEDAIKHGEEGHVGVATKHAQE
AIEHLRASEHKSH
;
_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  SER n 
1 2  GLY n 
1 3  HIS n 
1 4  THR n 
1 5  ALA n 
1 6  HIS n 
1 7  VAL n 
1 8  ASP n 
1 9  GLU n 
1 10 ALA n 
1 11 VAL n 
1 12 LYS n 
1 13 HIS n 
1 14 ALA n 
1 15 GLU n 
1 16 GLU n 
1 17 ALA n 
1 18 VAL n 
1 19 ALA n 
1 20 HIS n 
1 21 GLY n 
1 22 LYS n 
1 23 GLU n 
1 24 GLY n 
1 25 HIS n 
1 26 THR n 
1 27 ASP n 
1 28 GLN n 
1 29 LEU n 
1 30 LEU n 
1 31 GLU n 
1 32 HIS n 
1 33 ALA n 
1 34 LYS n 
1 35 GLU n 
1 36 SER n 
1 37 LEU n 
1 38 THR n 
1 39 HIS n 
1 40 ALA n 
1 41 LYS n 
1 42 ALA n 
1 43 ALA n 
1 44 SER n 
1 45 GLU n 
1 46 ALA n 
1 47 GLY n 
1 48 GLY n 
1 49 ASN n 
1 50 THR n 
1 51 HIS n 
1 52 VAL n 
1 53 GLY n 
1 54 HIS n 
1 55 GLY n 
1 56 ILE n 
1 57 LYS n 
1 58 HIS n 
1 59 LEU n 
1 60 GLU n 
1 61 ASP n 
1 62 ALA n 
1 63 ILE n 
1 64 LYS n 
1 65 HIS n 
1 66 GLY n 
1 67 GLU n 
1 68 GLU n 
1 69 GLY n 
1 70 HIS n 
1 71 VAL n 
1 72 GLY n 
1 73 VAL n 
1 74 ALA n 
1 75 THR n 
1 76 LYS n 
1 77 HIS n 
1 78 ALA n 
1 79 GLN n 
1 80 GLU n 
1 81 ALA n 
1 82 ILE n 
1 83 GLU n 
1 84 HIS n 
1 85 LEU n 
1 86 ARG n 
1 87 ALA n 
1 88 SER n 
1 89 GLU n 
1 90 HIS n 
1 91 LYS n 
1 92 SER n 
1 93 HIS n 
# 
_entity_src_nat.entity_id                  1 
_entity_src_nat.pdbx_src_id                1 
_entity_src_nat.pdbx_alt_source_flag       sample 
_entity_src_nat.pdbx_beg_seq_num           ? 
_entity_src_nat.pdbx_end_seq_num           ? 
_entity_src_nat.common_name                ? 
_entity_src_nat.pdbx_organism_scientific   'Nitrosomonas europaea' 
_entity_src_nat.pdbx_ncbi_taxonomy_id      915 
_entity_src_nat.genus                      ? 
_entity_src_nat.species                    ? 
_entity_src_nat.strain                     ? 
_entity_src_nat.tissue                     ? 
_entity_src_nat.tissue_fraction            ? 
_entity_src_nat.pdbx_secretion             ? 
_entity_src_nat.pdbx_fragment              ? 
_entity_src_nat.pdbx_variant               ? 
_entity_src_nat.pdbx_cell_line             ? 
_entity_src_nat.pdbx_atcc                  ? 
_entity_src_nat.pdbx_cellular_location     ? 
_entity_src_nat.pdbx_organ                 ? 
_entity_src_nat.pdbx_organelle             ? 
_entity_src_nat.pdbx_cell                  ? 
_entity_src_nat.pdbx_plasmid_name          ? 
_entity_src_nat.pdbx_plasmid_details       ? 
_entity_src_nat.details                    ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    SMBP_NITEU 
_struct_ref.pdbx_db_accession          Q82S91 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SGHTAHVDEAVKHAEEAVAHGKEGHTDQLLEHAKESLTHAKAASEAGGNTHVGHGIKHLEDAIKHGEEGHVGVATKHAQE
AIEHLRASEHKSH
;
_struct_ref.pdbx_align_begin           25 
_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 3U8V A 1 ? 93 ? Q82S91 25 ? 117 ? 1 93 
2 1 3U8V B 1 ? 93 ? Q82S91 25 ? 117 ? 1 93 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE           ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE          ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE        ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'   ? 'C4 H7 N O4'     133.103 
GLN 'L-peptide linking' y GLUTAMINE         ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'   ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE           ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE         ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER             ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE        ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE           ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE            ? 'C6 H15 N2 O2 1' 147.195 
NI  non-polymer         . 'NICKEL (II) ION' ? 'Ni 2'           58.693  
SER 'L-peptide linking' y SERINE            ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE         ? 'C4 H9 N O3'     119.119 
VAL 'L-peptide linking' y VALINE            ? 'C5 H11 N O2'    117.146 
# 
_exptl.entry_id          3U8V 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.13 
_exptl_crystal.density_percent_sol   42.14 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.temp            289 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              9.0 
_exptl_crystal_grow.pdbx_details    
;The reservoir contained 20% w/v polyethylene glycol 20000, 0.1 M calcium chloride, 0.1M N-[Tris(hydroxymethyl)methyl]-3-aminopropanesulfonic acid, TAPS and 1 mM sodium azide. For crystallization, 1 UL of the protein was mixed with an equal volume of the reservoir. The total volume of the reservoir was 0.5 ml., pH 9.0, VAPOR DIFFUSION, HANGING DROP, temperature 289K
;
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           80 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               CCD 
_diffrn_detector.type                   'ADSC QUANTUM 210' 
_diffrn_detector.pdbx_collection_date   2007-10-01 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    'graphite crystal' 
_diffrn_radiation.pdbx_diffrn_protocol             MAD 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
loop_
_diffrn_radiation_wavelength.id 
_diffrn_radiation_wavelength.wavelength 
_diffrn_radiation_wavelength.wt 
1 1.0     1.0 
2 1.48525 1.0 
3 1.48634 1.0 
4 1.40127 1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'ALS BEAMLINE 5.0.3' 
_diffrn_source.pdbx_synchrotron_site       ALS 
_diffrn_source.pdbx_synchrotron_beamline   5.0.3 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        '1.0, 1.48525, 1.48634, 1.40127' 
# 
_reflns.entry_id                     3U8V 
_reflns.observed_criterion_sigma_I   1.0 
_reflns.observed_criterion_sigma_F   1.0 
_reflns.d_resolution_low             25.0 
_reflns.d_resolution_high            1.90 
_reflns.number_obs                   13646 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         98.5 
_reflns.pdbx_Rmerge_I_obs            ? 
_reflns.pdbx_Rsym_value              0.047 
_reflns.pdbx_netI_over_sigmaI        10.5 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              4.3 
_reflns.R_free_details               ? 
_reflns.limit_h_max                  ? 
_reflns.limit_h_min                  ? 
_reflns.limit_k_max                  ? 
_reflns.limit_k_min                  ? 
_reflns.limit_l_max                  ? 
_reflns.limit_l_min                  ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_chi_squared             ? 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_ordinal                 1 
_reflns.pdbx_diffrn_id               1 
# 
_reflns_shell.d_res_high             1.9 
_reflns_shell.d_res_low              2.0 
_reflns_shell.percent_possible_all   97.6 
_reflns_shell.Rmerge_I_obs           ? 
_reflns_shell.pdbx_Rsym_value        0.280 
_reflns_shell.meanI_over_sigI_obs    2.6 
_reflns_shell.pdbx_redundancy        4.4 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      ? 
_reflns_shell.number_measured_all    ? 
_reflns_shell.number_measured_obs    ? 
_reflns_shell.number_unique_obs      ? 
_reflns_shell.pdbx_chi_squared       ? 
_reflns_shell.pdbx_ordinal           1 
_reflns_shell.pdbx_diffrn_id         1 
# 
_refine.entry_id                                 3U8V 
_refine.ls_number_reflns_obs                     12927 
_refine.ls_number_reflns_all                     13646 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.0 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             46.68 
_refine.ls_d_res_high                            1.90 
_refine.ls_percent_reflns_obs                    98.19 
_refine.ls_R_factor_obs                          0.17206 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.17034 
_refine.ls_R_factor_R_free                       0.20533 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_number_reflns_R_free                  684 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.958 
_refine.correlation_coeff_Fo_to_Fc_free          0.935 
_refine.B_iso_mean                               28.085 
_refine.aniso_B[1][1]                            -1.49 
_refine.aniso_B[2][2]                            -0.38 
_refine.aniso_B[3][3]                            1.87 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][3]                            0.00 
_refine.solvent_model_details                    'BABINET MODEL WITH MASK' 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.40 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          MAD 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R_Free                  0.129 
_refine.overall_SU_ML                            0.089 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             5.741 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_refine.overall_SU_R_free                        ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_overall_ESU_R                       ? 
_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        1244 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         1 
_refine_hist.number_atoms_solvent             97 
_refine_hist.number_atoms_total               1342 
_refine_hist.d_res_high                       1.90 
_refine_hist.d_res_low                        46.68 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_restraint_function 
_refine_ls_restr.pdbx_refine_id 
r_bond_refined_d         0.019  0.020  ? 1282 ? 'X-RAY DIFFRACTION' 
r_angle_refined_deg      1.638  1.883  ? 1721 ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_1_deg   3.948  5.000  ? 162  ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_2_deg   39.114 25.077 ? 65   ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_3_deg   16.405 15.000 ? 218  ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_4_deg   9.711  15.000 ? 2    ? 'X-RAY DIFFRACTION' 
r_chiral_restr           0.110  0.200  ? 188  ? 'X-RAY DIFFRACTION' 
r_gen_planes_refined     0.007  0.020  ? 966  ? 'X-RAY DIFFRACTION' 
r_nbd_refined            0.224  0.200  ? 709  ? 'X-RAY DIFFRACTION' 
r_nbtor_refined          0.294  0.200  ? 851  ? 'X-RAY DIFFRACTION' 
r_xyhbond_nbd_refined    0.172  0.200  ? 110  ? 'X-RAY DIFFRACTION' 
r_metal_ion_refined      0.050  0.200  ? 2    ? 'X-RAY DIFFRACTION' 
r_symmetry_vdw_refined   0.198  0.200  ? 39   ? 'X-RAY DIFFRACTION' 
r_symmetry_hbond_refined 0.204  0.200  ? 8    ? 'X-RAY DIFFRACTION' 
r_mcbond_it              1.226  1.500  ? 826  ? 'X-RAY DIFFRACTION' 
r_mcangle_it             1.774  2.000  ? 1271 ? 'X-RAY DIFFRACTION' 
r_scbond_it              3.603  3.000  ? 478  ? 'X-RAY DIFFRACTION' 
r_scangle_it             5.881  4.500  ? 450  ? 'X-RAY DIFFRACTION' 
# 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.d_res_high                       1.900 
_refine_ls_shell.d_res_low                        1.949 
_refine_ls_shell.number_reflns_R_work             918 
_refine_ls_shell.R_factor_R_work                  0.193 
_refine_ls_shell.percent_reflns_obs               98.49 
_refine_ls_shell.R_factor_R_free                  0.272 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             59 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  3U8V 
_struct.title                     'Three dimensional structure of the Small Metal Binding Protein, SMBP' 
_struct.pdbx_descriptor           'Metal-binding protein smbP' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        3U8V 
_struct_keywords.pdbx_keywords   'METAL BINDING PROTEIN' 
_struct_keywords.text            'four helical bundle, metal chaperone, METAL BINDING PROTEIN' 
# 
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 3 ? 
# 
_struct_biol.id        1 
_struct_biol.details   ? 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 1 GLY A 2  ? GLU A 23 ? GLY A 2  GLU A 23 1 ? 22 
HELX_P HELX_P2 2 HIS A 25 ? SER A 44 ? HIS A 25 SER A 44 1 ? 20 
HELX_P HELX_P3 3 HIS A 51 ? GLU A 68 ? HIS A 51 GLU A 68 1 ? 18 
HELX_P HELX_P4 4 HIS A 70 ? SER A 88 ? HIS A 70 SER A 88 1 ? 19 
HELX_P HELX_P5 5 GLY B 2  ? GLU B 23 ? GLY B 2  GLU B 23 1 ? 22 
HELX_P HELX_P6 6 HIS B 25 ? SER B 44 ? HIS B 25 SER B 44 1 ? 20 
HELX_P HELX_P7 7 HIS B 51 ? GLY B 69 ? HIS B 51 GLY B 69 1 ? 19 
HELX_P HELX_P8 8 HIS B 70 ? SER B 88 ? HIS B 70 SER B 88 1 ? 19 
# 
_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 
metalc1 metalc ? ? A SER 1 N   ? ? ? 1_555 C NI . NI ? ? A SER 1 A NI 94 1_555 ? ? ? ? ? ? ? 1.884 ? 
metalc2 metalc ? ? B SER 1 N   ? ? ? 1_555 C NI . NI ? ? B SER 1 A NI 94 1_555 ? ? ? ? ? ? ? 1.922 ? 
metalc3 metalc ? ? A HIS 6 NE2 ? ? ? 1_555 C NI . NI ? ? A HIS 6 A NI 94 1_555 ? ? ? ? ? ? ? 2.082 ? 
metalc4 metalc ? ? B SER 1 O   ? ? ? 1_555 C NI . NI ? ? B SER 1 A NI 94 1_555 ? ? ? ? ? ? ? 2.089 ? 
metalc5 metalc ? ? B HIS 6 NE2 ? ? ? 1_555 C NI . NI ? ? B HIS 6 A NI 94 1_555 ? ? ? ? ? ? ? 2.099 ? 
metalc6 metalc ? ? A SER 1 O   ? ? ? 1_555 C NI . NI ? ? A SER 1 A NI 94 1_555 ? ? ? ? ? ? ? 2.162 ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
_struct_site.id                   AC1 
_struct_site.pdbx_evidence_code   Software 
_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    4 
_struct_site.details              'BINDING SITE FOR RESIDUE NI A 94' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1 AC1 4 SER A 1 ? SER A 1 . ? 1_555 ? 
2 AC1 4 HIS A 6 ? HIS A 6 . ? 1_555 ? 
3 AC1 4 SER B 1 ? SER B 1 . ? 1_555 ? 
4 AC1 4 HIS B 6 ? HIS B 6 . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          3U8V 
_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                    3U8V 
_atom_sites.fract_transf_matrix[1][1]   0.028043 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_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]   0.017792 
_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]   0.011916 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
N  
NI 
O  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . SER A 1 1  ? -12.562 -8.742  23.281 1.00 19.66 ? 1   SER A N   1 
ATOM   2    C  CA  . SER A 1 1  ? -12.864 -10.224 23.478 1.00 21.30 ? 1   SER A CA  1 
ATOM   3    C  C   . SER A 1 1  ? -11.779 -10.770 24.394 1.00 21.77 ? 1   SER A C   1 
ATOM   4    O  O   . SER A 1 1  ? -10.794 -10.109 24.633 1.00 20.18 ? 1   SER A O   1 
ATOM   5    C  CB  . SER A 1 1  ? -12.781 -10.962 22.138 1.00 20.28 ? 1   SER A CB  1 
ATOM   6    O  OG  . SER A 1 1  ? -13.569 -10.314 21.163 1.00 20.97 ? 1   SER A OG  1 
ATOM   7    N  N   . GLY A 1 2  ? -11.892 -12.024 24.824 1.00 22.61 ? 2   GLY A N   1 
ATOM   8    C  CA  . GLY A 1 2  ? -10.817 -12.576 25.608 1.00 23.08 ? 2   GLY A CA  1 
ATOM   9    C  C   . GLY A 1 2  ? -9.680  -13.048 24.761 1.00 22.51 ? 2   GLY A C   1 
ATOM   10   O  O   . GLY A 1 2  ? -9.721  -12.995 23.542 1.00 20.49 ? 2   GLY A O   1 
ATOM   11   N  N   . HIS A 1 3  ? -8.639  -13.538 25.419 1.00 24.09 ? 3   HIS A N   1 
ATOM   12   C  CA  . HIS A 1 3  ? -7.398  -13.960 24.757 1.00 22.77 ? 3   HIS A CA  1 
ATOM   13   C  C   . HIS A 1 3  ? -7.717  -15.000 23.697 1.00 21.78 ? 3   HIS A C   1 
ATOM   14   O  O   . HIS A 1 3  ? -7.263  -14.920 22.597 1.00 20.40 ? 3   HIS A O   1 
ATOM   15   C  CB  . HIS A 1 3  ? -6.451  -14.539 25.840 1.00 25.67 ? 3   HIS A CB  1 
ATOM   16   C  CG  . HIS A 1 3  ? -5.171  -15.062 25.284 1.00 26.88 ? 3   HIS A CG  1 
ATOM   17   N  ND1 . HIS A 1 3  ? -4.081  -14.250 25.035 1.00 28.97 ? 3   HIS A ND1 1 
ATOM   18   C  CD2 . HIS A 1 3  ? -4.806  -16.319 24.927 1.00 29.23 ? 3   HIS A CD2 1 
ATOM   19   C  CE1 . HIS A 1 3  ? -3.110  -14.991 24.514 1.00 31.28 ? 3   HIS A CE1 1 
ATOM   20   N  NE2 . HIS A 1 3  ? -3.514  -16.252 24.469 1.00 29.50 ? 3   HIS A NE2 1 
ATOM   21   N  N   . THR A 1 4  ? -8.578  -15.954 24.043 1.00 22.16 ? 4   THR A N   1 
ATOM   22   C  CA  . THR A 1 4  ? -8.822  -17.087 23.128 1.00 22.67 ? 4   THR A CA  1 
ATOM   23   C  C   . THR A 1 4  ? -9.413  -16.607 21.826 1.00 20.17 ? 4   THR A C   1 
ATOM   24   O  O   . THR A 1 4  ? -9.033  -17.030 20.734 1.00 19.66 ? 4   THR A O   1 
ATOM   25   C  CB  . THR A 1 4  ? -9.776  -18.069 23.777 1.00 24.10 ? 4   THR A CB  1 
ATOM   26   O  OG1 . THR A 1 4  ? -9.157  -18.572 24.954 1.00 26.95 ? 4   THR A OG1 1 
ATOM   27   C  CG2 . THR A 1 4  ? -10.095 -19.242 22.856 1.00 23.94 ? 4   THR A CG2 1 
ATOM   28   N  N   . ALA A 1 5  ? -10.402 -15.732 21.943 1.00 21.24 ? 5   ALA A N   1 
ATOM   29   C  CA  . ALA A 1 5  ? -11.103 -15.292 20.769 1.00 20.25 ? 5   ALA A CA  1 
ATOM   30   C  C   . ALA A 1 5  ? -10.178 -14.428 19.921 1.00 18.26 ? 5   ALA A C   1 
ATOM   31   O  O   . ALA A 1 5  ? -10.157 -14.500 18.688 1.00 17.79 ? 5   ALA A O   1 
ATOM   32   C  CB  . ALA A 1 5  ? -12.319 -14.496 21.251 1.00 21.65 ? 5   ALA A CB  1 
ATOM   33   N  N   . HIS A 1 6  ? -9.363  -13.593 20.555 1.00 18.08 ? 6   HIS A N   1 
ATOM   34   C  CA  . HIS A 1 6  ? -8.416  -12.792 19.770 1.00 16.52 ? 6   HIS A CA  1 
ATOM   35   C  C   . HIS A 1 6  ? -7.372  -13.616 19.062 1.00 17.33 ? 6   HIS A C   1 
ATOM   36   O  O   . HIS A 1 6  ? -7.028  -13.342 17.912 1.00 18.33 ? 6   HIS A O   1 
ATOM   37   C  CB  . HIS A 1 6  ? -7.744  -11.736 20.648 1.00 16.81 ? 6   HIS A CB  1 
ATOM   38   C  CG  . HIS A 1 6  ? -8.653  -10.599 20.997 1.00 14.62 ? 6   HIS A CG  1 
ATOM   39   N  ND1 . HIS A 1 6  ? -9.285  -9.852  20.031 1.00 16.02 ? 6   HIS A ND1 1 
ATOM   40   C  CD2 . HIS A 1 6  ? -9.028  -10.069 22.182 1.00 15.68 ? 6   HIS A CD2 1 
ATOM   41   C  CE1 . HIS A 1 6  ? -10.050 -8.934  20.604 1.00 19.80 ? 6   HIS A CE1 1 
ATOM   42   N  NE2 . HIS A 1 6  ? -9.908  -9.039  21.908 1.00 15.20 ? 6   HIS A NE2 1 
ATOM   43   N  N   . VAL A 1 7  ? -6.815  -14.596 19.756 1.00 18.12 ? 7   VAL A N   1 
ATOM   44   C  CA  . VAL A 1 7  ? -5.835  -15.445 19.104 1.00 18.47 ? 7   VAL A CA  1 
ATOM   45   C  C   . VAL A 1 7  ? -6.534  -16.142 17.949 1.00 19.37 ? 7   VAL A C   1 
ATOM   46   O  O   . VAL A 1 7  ? -5.972  -16.219 16.869 1.00 18.81 ? 7   VAL A O   1 
ATOM   47   C  CB  . VAL A 1 7  ? -5.193  -16.384 20.092 1.00 20.32 ? 7   VAL A CB  1 
ATOM   48   C  CG1 . VAL A 1 7  ? -4.329  -17.417 19.370 1.00 21.96 ? 7   VAL A CG1 1 
ATOM   49   C  CG2 . VAL A 1 7  ? -4.343  -15.542 21.035 1.00 17.45 ? 7   VAL A CG2 1 
ATOM   50   N  N   . ASP A 1 8  ? -7.766  -16.626 18.166 1.00 20.69 ? 8   ASP A N   1 
ATOM   51   C  CA  . ASP A 1 8  ? -8.487  -17.331 17.099 1.00 22.36 ? 8   ASP A CA  1 
ATOM   52   C  C   . ASP A 1 8  ? -8.713  -16.444 15.900 1.00 20.62 ? 8   ASP A C   1 
ATOM   53   O  O   . ASP A 1 8  ? -8.438  -16.856 14.762 1.00 18.78 ? 8   ASP A O   1 
ATOM   54   C  CB  . ASP A 1 8  ? -9.856  -17.808 17.606 1.00 24.69 ? 8   ASP A CB  1 
ATOM   55   C  CG  . ASP A 1 8  ? -10.617 -18.628 16.579 1.00 28.51 ? 8   ASP A CG  1 
ATOM   56   O  OD1 . ASP A 1 8  ? -11.798 -18.332 16.422 1.00 33.84 ? 8   ASP A OD1 1 
ATOM   57   O  OD2 . ASP A 1 8  ? -10.045 -19.584 16.017 1.00 34.11 ? 8   ASP A OD2 1 
ATOM   58   N  N   . GLU A 1 9  ? -9.194  -15.214 16.137 1.00 19.14 ? 9   GLU A N   1 
ATOM   59   C  CA  . GLU A 1 9  ? -9.414  -14.305 15.029 1.00 19.18 ? 9   GLU A CA  1 
ATOM   60   C  C   . GLU A 1 9  ? -8.055  -13.938 14.394 1.00 17.98 ? 9   GLU A C   1 
ATOM   61   O  O   . GLU A 1 9  ? -7.954  -13.825 13.174 1.00 17.78 ? 9   GLU A O   1 
ATOM   62   C  CB  . GLU A 1 9  ? -10.125 -13.026 15.527 1.00 19.01 ? 9   GLU A CB  1 
ATOM   63   C  CG  . GLU A 1 9  ? -11.589 -13.204 15.921 1.00 23.79 ? 9   GLU A CG  1 
ATOM   64   C  CD  . GLU A 1 9  ? -12.449 -13.792 14.800 1.00 31.04 ? 9   GLU A CD  1 
ATOM   65   O  OE1 . GLU A 1 9  ? -12.263 -13.433 13.641 1.00 28.54 ? 9   GLU A OE1 1 
ATOM   66   O  OE2 . GLU A 1 9  ? -13.292 -14.669 15.077 1.00 43.66 ? 9   GLU A OE2 1 
ATOM   67   N  N   . ALA A 1 10 ? -7.001  -13.777 15.202 1.00 16.98 ? 10  ALA A N   1 
ATOM   68   C  CA  . ALA A 1 10 ? -5.674  -13.457 14.596 1.00 15.52 ? 10  ALA A CA  1 
ATOM   69   C  C   . ALA A 1 10 ? -5.208  -14.588 13.634 1.00 16.54 ? 10  ALA A C   1 
ATOM   70   O  O   . ALA A 1 10 ? -4.755  -14.341 12.505 1.00 16.51 ? 10  ALA A O   1 
ATOM   71   C  CB  . ALA A 1 10 ? -4.620  -13.207 15.697 1.00 16.12 ? 10  ALA A CB  1 
ATOM   72   N  N   . VAL A 1 11 ? -5.380  -15.824 14.080 1.00 17.49 ? 11  VAL A N   1 
ATOM   73   C  CA  . VAL A 1 11 ? -4.996  -16.999 13.266 1.00 18.31 ? 11  VAL A CA  1 
ATOM   74   C  C   . VAL A 1 11 ? -5.842  -17.050 11.980 1.00 19.96 ? 11  VAL A C   1 
ATOM   75   O  O   . VAL A 1 11 ? -5.306  -17.170 10.866 1.00 19.57 ? 11  VAL A O   1 
ATOM   76   C  CB  . VAL A 1 11 ? -5.098  -18.292 14.087 1.00 19.53 ? 11  VAL A CB  1 
ATOM   77   C  CG1 . VAL A 1 11 ? -4.934  -19.533 13.213 1.00 20.55 ? 11  VAL A CG1 1 
ATOM   78   C  CG2 . VAL A 1 11 ? -4.056  -18.270 15.147 1.00 20.55 ? 11  VAL A CG2 1 
ATOM   79   N  N   . LYS A 1 12 ? -7.153  -16.902 12.130 1.00 20.30 ? 12  LYS A N   1 
ATOM   80   C  CA  . LYS A 1 12 ? -8.050  -16.974 11.007 1.00 21.73 ? 12  LYS A CA  1 
ATOM   81   C  C   . LYS A 1 12 ? -7.740  -15.902 9.967  1.00 18.91 ? 12  LYS A C   1 
ATOM   82   O  O   . LYS A 1 12 ? -7.781  -16.151 8.750  1.00 16.73 ? 12  LYS A O   1 
ATOM   83   C  CB  . LYS A 1 12 ? -9.514  -16.904 11.466 1.00 22.93 ? 12  LYS A CB  1 
ATOM   84   C  CG  . LYS A 1 12 ? -9.967  -18.187 12.213 1.00 28.83 ? 12  LYS A CG  1 
ATOM   85   C  CD  . LYS A 1 12 ? -11.497 -18.183 12.388 1.00 31.10 ? 12  LYS A CD  1 
ATOM   86   C  CE  . LYS A 1 12 ? -12.085 -16.785 12.682 1.00 35.76 ? 12  LYS A CE  1 
ATOM   87   N  NZ  . LYS A 1 12 ? -13.555 -16.926 13.125 1.00 39.75 ? 12  LYS A NZ  1 
ATOM   88   N  N   . HIS A 1 13 ? -7.494  -14.679 10.424 1.00 16.91 ? 13  HIS A N   1 
ATOM   89   C  CA  . HIS A 1 13 ? -7.170  -13.665 9.473  1.00 16.09 ? 13  HIS A CA  1 
ATOM   90   C  C   . HIS A 1 13 ? -5.797  -13.858 8.848  1.00 16.61 ? 13  HIS A C   1 
ATOM   91   O  O   . HIS A 1 13 ? -5.604  -13.601 7.667  1.00 17.96 ? 13  HIS A O   1 
ATOM   92   C  CB  . HIS A 1 13 ? -7.222  -12.286 10.160 1.00 14.65 ? 13  HIS A CB  1 
ATOM   93   C  CG  . HIS A 1 13 ? -8.617  -11.779 10.283 1.00 14.83 ? 13  HIS A CG  1 
ATOM   94   N  ND1 . HIS A 1 13 ? -9.355  -11.383 9.195  1.00 18.11 ? 13  HIS A ND1 1 
ATOM   95   C  CD2 . HIS A 1 13 ? -9.410  -11.592 11.372 1.00 19.62 ? 13  HIS A CD2 1 
ATOM   96   C  CE1 . HIS A 1 13 ? -10.560 -10.999 9.600  1.00 22.06 ? 13  HIS A CE1 1 
ATOM   97   N  NE2 . HIS A 1 13 ? -10.611 -11.113 10.915 1.00 21.71 ? 13  HIS A NE2 1 
ATOM   98   N  N   . ALA A 1 14 ? -4.855  -14.329 9.642  1.00 15.25 ? 14  ALA A N   1 
ATOM   99   C  CA  . ALA A 1 14 ? -3.509  -14.578 9.110  1.00 15.63 ? 14  ALA A CA  1 
ATOM   100  C  C   . ALA A 1 14 ? -3.652  -15.718 8.087  1.00 15.96 ? 14  ALA A C   1 
ATOM   101  O  O   . ALA A 1 14 ? -3.000  -15.704 7.026  1.00 16.50 ? 14  ALA A O   1 
ATOM   102  C  CB  . ALA A 1 14 ? -2.540  -14.954 10.253 1.00 13.79 ? 14  ALA A CB  1 
ATOM   103  N  N   . GLU A 1 15 ? -4.493  -16.727 8.392  1.00 15.82 ? 15  GLU A N   1 
ATOM   104  C  CA  . GLU A 1 15 ? -4.694  -17.801 7.362  1.00 18.16 ? 15  GLU A CA  1 
ATOM   105  C  C   . GLU A 1 15 ? -5.263  -17.273 6.077  1.00 18.01 ? 15  GLU A C   1 
ATOM   106  O  O   . GLU A 1 15 ? -4.914  -17.731 5.012  1.00 18.68 ? 15  GLU A O   1 
ATOM   107  C  CB  . GLU A 1 15 ? -5.564  -18.915 7.899  1.00 20.17 ? 15  GLU A CB  1 
ATOM   108  C  CG  . GLU A 1 15 ? -4.810  -19.668 9.009  1.00 22.07 ? 15  GLU A CG  1 
ATOM   109  C  CD  . GLU A 1 15 ? -5.655  -20.767 9.627  1.00 32.86 ? 15  GLU A CD  1 
ATOM   110  O  OE1 . GLU A 1 15 ? -6.895  -20.618 9.678  1.00 33.08 ? 15  GLU A OE1 1 
ATOM   111  O  OE2 . GLU A 1 15 ? -5.077  -21.767 10.073 1.00 37.21 ? 15  GLU A OE2 1 
ATOM   112  N  N   . GLU A 1 16 ? -6.217  -16.343 6.171  1.00 18.11 ? 16  GLU A N   1 
ATOM   113  C  CA  . GLU A 1 16 ? -6.784  -15.775 4.994  1.00 18.41 ? 16  GLU A CA  1 
ATOM   114  C  C   . GLU A 1 16 ? -5.738  -14.892 4.312  1.00 19.03 ? 16  GLU A C   1 
ATOM   115  O  O   . GLU A 1 16 ? -5.709  -14.861 3.093  1.00 19.27 ? 16  GLU A O   1 
ATOM   116  C  CB  . GLU A 1 16 ? -8.024  -14.910 5.320  1.00 18.45 ? 16  GLU A CB  1 
ATOM   117  C  CG  . GLU A 1 16 ? -8.975  -14.790 4.147  1.00 26.47 ? 16  GLU A CG  1 
ATOM   118  C  CD  . GLU A 1 16 ? -9.643  -16.124 3.771  1.00 34.06 ? 16  GLU A CD  1 
ATOM   119  O  OE1 . GLU A 1 16 ? -10.208 -16.231 2.669  1.00 38.42 ? 16  GLU A OE1 1 
ATOM   120  O  OE2 . GLU A 1 16 ? -9.561  -17.124 4.533  1.00 41.27 ? 16  GLU A OE2 1 
ATOM   121  N  N   . ALA A 1 17 ? -4.929  -14.124 5.080  1.00 17.17 ? 17  ALA A N   1 
ATOM   122  C  CA  . ALA A 1 17 ? -3.866  -13.360 4.437  1.00 17.09 ? 17  ALA A CA  1 
ATOM   123  C  C   . ALA A 1 17 ? -2.904  -14.296 3.636  1.00 16.48 ? 17  ALA A C   1 
ATOM   124  O  O   . ALA A 1 17 ? -2.517  -14.015 2.498  1.00 17.02 ? 17  ALA A O   1 
ATOM   125  C  CB  . ALA A 1 17 ? -3.079  -12.569 5.528  1.00 15.09 ? 17  ALA A CB  1 
ATOM   126  N  N   . VAL A 1 18 ? -2.501  -15.411 4.243  1.00 17.71 ? 18  VAL A N   1 
ATOM   127  C  CA  . VAL A 1 18 ? -1.608  -16.371 3.541  1.00 17.66 ? 18  VAL A CA  1 
ATOM   128  C  C   . VAL A 1 18 ? -2.277  -16.866 2.231  1.00 19.44 ? 18  VAL A C   1 
ATOM   129  O  O   . VAL A 1 18 ? -1.653  -16.895 1.104  1.00 21.19 ? 18  VAL A O   1 
ATOM   130  C  CB  . VAL A 1 18 ? -1.258  -17.571 4.455  1.00 16.87 ? 18  VAL A CB  1 
ATOM   131  C  CG1 . VAL A 1 18 ? -0.656  -18.756 3.583  1.00 17.38 ? 18  VAL A CG1 1 
ATOM   132  C  CG2 . VAL A 1 18 ? -0.229  -17.091 5.499  1.00 18.12 ? 18  VAL A CG2 1 
ATOM   133  N  N   . ALA A 1 19 ? -3.546  -17.257 2.339  1.00 19.80 ? 19  ALA A N   1 
ATOM   134  C  CA  . ALA A 1 19 ? -4.232  -17.779 1.188  1.00 19.92 ? 19  ALA A CA  1 
ATOM   135  C  C   . ALA A 1 19 ? -4.278  -16.723 0.036  1.00 21.66 ? 19  ALA A C   1 
ATOM   136  O  O   . ALA A 1 19 ? -4.131  -17.045 -1.159 1.00 21.75 ? 19  ALA A O   1 
ATOM   137  C  CB  . ALA A 1 19 ? -5.650  -18.258 1.584  1.00 22.12 ? 19  ALA A CB  1 
ATOM   138  N  N   . HIS A 1 20 ? -4.549  -15.469 0.405  1.00 19.25 ? 20  HIS A N   1 
ATOM   139  C  CA  . HIS A 1 20 ? -4.551  -14.361 -0.597 1.00 21.06 ? 20  HIS A CA  1 
ATOM   140  C  C   . HIS A 1 20 ? -3.165  -14.193 -1.202 1.00 18.92 ? 20  HIS A C   1 
ATOM   141  O  O   . HIS A 1 20 ? -2.990  -13.969 -2.401 1.00 22.76 ? 20  HIS A O   1 
ATOM   142  C  CB  . HIS A 1 20 ? -5.002  -13.029 0.150  1.00 18.18 ? 20  HIS A CB  1 
ATOM   143  C  CG  . HIS A 1 20 ? -6.493  -12.852 0.196  1.00 18.11 ? 20  HIS A CG  1 
ATOM   144  N  ND1 . HIS A 1 20 ? -7.264  -12.760 -0.941 1.00 20.07 ? 20  HIS A ND1 1 
ATOM   145  C  CD2 . HIS A 1 20 ? -7.346  -12.708 1.246  1.00 19.11 ? 20  HIS A CD2 1 
ATOM   146  C  CE1 . HIS A 1 20 ? -8.537  -12.578 -0.602 1.00 17.93 ? 20  HIS A CE1 1 
ATOM   147  N  NE2 . HIS A 1 20 ? -8.603  -12.518 0.722  1.00 21.00 ? 20  HIS A NE2 1 
ATOM   148  N  N   . GLY A 1 21 ? -2.161  -14.354 -0.367 1.00 21.66 ? 21  GLY A N   1 
ATOM   149  C  CA  . GLY A 1 21 ? -0.755  -14.064 -0.759 1.00 19.59 ? 21  GLY A CA  1 
ATOM   150  C  C   . GLY A 1 21 ? -0.301  -15.063 -1.753 1.00 22.09 ? 21  GLY A C   1 
ATOM   151  O  O   . GLY A 1 21 ? 0.373   -14.690 -2.713 1.00 22.92 ? 21  GLY A O   1 
ATOM   152  N  N   . LYS A 1 22 ? -0.689  -16.328 -1.544 1.00 22.15 ? 22  LYS A N   1 
ATOM   153  C  CA  . LYS A 1 22 ? -0.359  -17.378 -2.476 1.00 23.58 ? 22  LYS A CA  1 
ATOM   154  C  C   . LYS A 1 22 ? -1.027  -17.158 -3.825 1.00 24.97 ? 22  LYS A C   1 
ATOM   155  O  O   . LYS A 1 22 ? -0.549  -17.674 -4.840 1.00 26.14 ? 22  LYS A O   1 
ATOM   156  C  CB  . LYS A 1 22 ? -0.784  -18.727 -1.931 1.00 24.33 ? 22  LYS A CB  1 
ATOM   157  C  CG  . LYS A 1 22 ? -0.031  -19.122 -0.633 1.00 24.87 ? 22  LYS A CG  1 
ATOM   158  C  CD  . LYS A 1 22 ? -0.654  -20.454 -0.180 1.00 30.56 ? 22  LYS A CD  1 
ATOM   159  C  CE  . LYS A 1 22 ? 0.102   -21.210 0.927  1.00 37.21 ? 22  LYS A CE  1 
ATOM   160  N  NZ  . LYS A 1 22 ? -0.850  -22.262 1.500  1.00 37.00 ? 22  LYS A NZ  1 
ATOM   161  N  N   . GLU A 1 23 ? -2.108  -16.384 -3.850 1.00 22.82 ? 23  GLU A N   1 
ATOM   162  C  CA  . GLU A 1 23 ? -2.789  -16.034 -5.073 1.00 26.22 ? 23  GLU A CA  1 
ATOM   163  C  C   . GLU A 1 23 ? -2.282  -14.724 -5.600 1.00 26.79 ? 23  GLU A C   1 
ATOM   164  O  O   . GLU A 1 23 ? -2.745  -14.251 -6.660 1.00 28.96 ? 23  GLU A O   1 
ATOM   165  C  CB  . GLU A 1 23 ? -4.279  -15.913 -4.843 1.00 26.00 ? 23  GLU A CB  1 
ATOM   166  C  CG  . GLU A 1 23 ? -5.012  -17.232 -4.643 1.00 27.37 ? 23  GLU A CG  1 
ATOM   167  C  CD  . GLU A 1 23 ? -4.955  -18.092 -5.871 1.00 31.23 ? 23  GLU A CD  1 
ATOM   168  O  OE1 . GLU A 1 23 ? -5.747  -17.834 -6.808 1.00 31.66 ? 23  GLU A OE1 1 
ATOM   169  O  OE2 . GLU A 1 23 ? -4.155  -19.044 -5.892 1.00 32.59 ? 23  GLU A OE2 1 
ATOM   170  N  N   . GLY A 1 24 ? -1.333  -14.134 -4.899 1.00 25.13 ? 24  GLY A N   1 
ATOM   171  C  CA  . GLY A 1 24 ? -0.779  -12.815 -5.306 1.00 26.98 ? 24  GLY A CA  1 
ATOM   172  C  C   . GLY A 1 24 ? -1.744  -11.643 -5.030 1.00 26.10 ? 24  GLY A C   1 
ATOM   173  O  O   . GLY A 1 24 ? -1.612  -10.554 -5.604 1.00 27.11 ? 24  GLY A O   1 
ATOM   174  N  N   . HIS A 1 25 ? -2.718  -11.851 -4.145 1.00 25.14 ? 25  HIS A N   1 
ATOM   175  C  CA  . HIS A 1 25 ? -3.683  -10.804 -3.754 1.00 23.30 ? 25  HIS A CA  1 
ATOM   176  C  C   . HIS A 1 25 ? -3.103  -9.879  -2.705 1.00 23.07 ? 25  HIS A C   1 
ATOM   177  O  O   . HIS A 1 25 ? -3.520  -9.915  -1.531 1.00 18.33 ? 25  HIS A O   1 
ATOM   178  C  CB  . HIS A 1 25 ? -4.973  -11.456 -3.177 1.00 23.55 ? 25  HIS A CB  1 
ATOM   179  C  CG  . HIS A 1 25 ? -5.745  -12.288 -4.165 1.00 23.28 ? 25  HIS A CG  1 
ATOM   180  N  ND1 . HIS A 1 25 ? -6.703  -13.203 -3.780 1.00 22.62 ? 25  HIS A ND1 1 
ATOM   181  C  CD2 . HIS A 1 25 ? -5.693  -12.350 -5.515 1.00 27.87 ? 25  HIS A CD2 1 
ATOM   182  C  CE1 . HIS A 1 25 ? -7.224  -13.776 -4.844 1.00 22.22 ? 25  HIS A CE1 1 
ATOM   183  N  NE2 . HIS A 1 25 ? -6.649  -13.258 -5.917 1.00 25.98 ? 25  HIS A NE2 1 
ATOM   184  N  N   . THR A 1 26 ? -2.182  -9.003  -3.111 1.00 24.45 ? 26  THR A N   1 
ATOM   185  C  CA  . THR A 1 26 ? -1.438  -8.209  -2.128 1.00 23.29 ? 26  THR A CA  1 
ATOM   186  C  C   . THR A 1 26 ? -2.317  -7.369  -1.213 1.00 21.82 ? 26  THR A C   1 
ATOM   187  O  O   . THR A 1 26 ? -2.130  -7.388  -0.005 1.00 21.76 ? 26  THR A O   1 
ATOM   188  C  CB  . THR A 1 26 ? -0.355  -7.347  -2.823 1.00 24.93 ? 26  THR A CB  1 
ATOM   189  O  OG1 . THR A 1 26 ? 0.320   -8.164  -3.764 1.00 23.37 ? 26  THR A OG1 1 
ATOM   190  C  CG2 . THR A 1 26 ? 0.680   -6.883  -1.797 1.00 26.31 ? 26  THR A CG2 1 
ATOM   191  N  N   . ASP A 1 27 ? -3.286  -6.664  -1.755 1.00 24.16 ? 27  ASP A N   1 
ATOM   192  C  CA  . ASP A 1 27 ? -4.089  -5.747  -0.942 1.00 24.78 ? 27  ASP A CA  1 
ATOM   193  C  C   . ASP A 1 27 ? -4.947  -6.504  0.059  1.00 23.44 ? 27  ASP A C   1 
ATOM   194  O  O   . ASP A 1 27 ? -5.212  -6.022  1.153  1.00 22.72 ? 27  ASP A O   1 
ATOM   195  C  CB  . ASP A 1 27 ? -5.020  -4.912  -1.808 1.00 26.30 ? 27  ASP A CB  1 
ATOM   196  C  CG  . ASP A 1 27 ? -4.292  -3.853  -2.585 1.00 35.11 ? 27  ASP A CG  1 
ATOM   197  O  OD1 . ASP A 1 27 ? -3.214  -3.401  -2.167 1.00 40.26 ? 27  ASP A OD1 1 
ATOM   198  O  OD2 . ASP A 1 27 ? -4.790  -3.477  -3.631 1.00 38.99 ? 27  ASP A OD2 1 
ATOM   199  N  N   . GLN A 1 28 ? -5.466  -7.663  -0.362 1.00 22.92 ? 28  GLN A N   1 
ATOM   200  C  CA  . GLN A 1 28 ? -6.260  -8.526  0.513  1.00 20.20 ? 28  GLN A CA  1 
ATOM   201  C  C   . GLN A 1 28 ? -5.390  -9.205  1.590  1.00 19.46 ? 28  GLN A C   1 
ATOM   202  O  O   . GLN A 1 28 ? -5.793  -9.277  2.772  1.00 17.36 ? 28  GLN A O   1 
ATOM   203  C  CB  . GLN A 1 28 ? -7.070  -9.539  -0.360 1.00 22.38 ? 28  GLN A CB  1 
ATOM   204  C  CG  A GLN A 1 28 ? -8.117  -8.878  -1.336 0.50 21.50 ? 28  GLN A CG  1 
ATOM   205  C  CG  B GLN A 1 28 ? -8.493  -9.038  -0.845 0.50 25.98 ? 28  GLN A CG  1 
ATOM   206  C  CD  A GLN A 1 28 ? -7.511  -7.995  -2.439 0.50 19.52 ? 28  GLN A CD  1 
ATOM   207  C  CD  B GLN A 1 28 ? -9.178  -8.075  0.116  0.50 29.66 ? 28  GLN A CD  1 
ATOM   208  O  OE1 A GLN A 1 28 ? -6.466  -8.321  -3.058 0.50 15.80 ? 28  GLN A OE1 1 
ATOM   209  O  OE1 B GLN A 1 28 ? -9.493  -6.948  -0.266 0.50 34.81 ? 28  GLN A OE1 1 
ATOM   210  N  NE2 A GLN A 1 28 ? -8.213  -6.886  -2.737 0.50 19.48 ? 28  GLN A NE2 1 
ATOM   211  N  NE2 B GLN A 1 28 ? -9.428  -8.511  1.362  0.50 29.60 ? 28  GLN A NE2 1 
ATOM   212  N  N   . LEU A 1 29 ? -4.157  -9.615  1.242  1.00 19.40 ? 29  LEU A N   1 
ATOM   213  C  CA  . LEU A 1 29 ? -3.241  -10.081 2.267  1.00 18.02 ? 29  LEU A CA  1 
ATOM   214  C  C   . LEU A 1 29 ? -3.053  -8.946  3.278  1.00 17.26 ? 29  LEU A C   1 
ATOM   215  O  O   . LEU A 1 29 ? -3.067  -9.160  4.530  1.00 17.14 ? 29  LEU A O   1 
ATOM   216  C  CB  . LEU A 1 29 ? -1.860  -10.481 1.632  1.00 19.63 ? 29  LEU A CB  1 
ATOM   217  C  CG  . LEU A 1 29 ? -0.755  -10.795 2.660  1.00 16.94 ? 29  LEU A CG  1 
ATOM   218  C  CD1 . LEU A 1 29 ? 0.238   -11.818 2.088  1.00 17.40 ? 29  LEU A CD1 1 
ATOM   219  C  CD2 . LEU A 1 29 ? 0.022   -9.515  3.073  1.00 17.98 ? 29  LEU A CD2 1 
ATOM   220  N  N   . LEU A 1 30 ? -2.880  -7.729  2.783  1.00 18.06 ? 30  LEU A N   1 
ATOM   221  C  CA  . LEU A 1 30 ? -2.622  -6.594  3.693  1.00 17.84 ? 30  LEU A CA  1 
ATOM   222  C  C   . LEU A 1 30 ? -3.829  -6.374  4.604  1.00 17.85 ? 30  LEU A C   1 
ATOM   223  O  O   . LEU A 1 30 ? -3.681  -6.132  5.819  1.00 18.59 ? 30  LEU A O   1 
ATOM   224  C  CB  . LEU A 1 30 ? -2.319  -5.317  2.895  1.00 18.53 ? 30  LEU A CB  1 
ATOM   225  C  CG  . LEU A 1 30 ? -0.890  -5.402  2.287  1.00 21.18 ? 30  LEU A CG  1 
ATOM   226  C  CD1 . LEU A 1 30 ? -0.715  -4.257  1.330  1.00 23.57 ? 30  LEU A CD1 1 
ATOM   227  C  CD2 . LEU A 1 30 ? 0.184   -5.393  3.428  1.00 21.26 ? 30  LEU A CD2 1 
ATOM   228  N  N   . GLU A 1 31 ? -5.021  -6.422  4.009  1.00 17.13 ? 31  GLU A N   1 
ATOM   229  C  CA  . GLU A 1 31 ? -6.233  -6.168  4.774  1.00 17.31 ? 31  GLU A CA  1 
ATOM   230  C  C   . GLU A 1 31 ? -6.327  -7.155  5.926  1.00 15.61 ? 31  GLU A C   1 
ATOM   231  O  O   . GLU A 1 31 ? -6.555  -6.764  7.104  1.00 15.70 ? 31  GLU A O   1 
ATOM   232  C  CB  . GLU A 1 31 ? -7.451  -6.218  3.862  1.00 19.95 ? 31  GLU A CB  1 
ATOM   233  C  CG  . GLU A 1 31 ? -7.576  -4.857  3.218  1.00 28.67 ? 31  GLU A CG  1 
ATOM   234  C  CD  . GLU A 1 31 ? -8.976  -4.481  2.783  1.00 44.21 ? 31  GLU A CD  1 
ATOM   235  O  OE1 . GLU A 1 31 ? -9.138  -4.292  1.542  1.00 48.49 ? 31  GLU A OE1 1 
ATOM   236  O  OE2 . GLU A 1 31 ? -9.897  -4.365  3.653  1.00 45.81 ? 31  GLU A OE2 1 
ATOM   237  N  N   . HIS A 1 32 ? -6.140  -8.441  5.618  1.00 14.91 ? 32  HIS A N   1 
ATOM   238  C  CA  . HIS A 1 32 ? -6.168  -9.486  6.669  1.00 13.96 ? 32  HIS A CA  1 
ATOM   239  C  C   . HIS A 1 32 ? -5.038  -9.513  7.634  1.00 14.39 ? 32  HIS A C   1 
ATOM   240  O  O   . HIS A 1 32 ? -5.292  -9.769  8.821  1.00 14.29 ? 32  HIS A O   1 
ATOM   241  C  CB  . HIS A 1 32 ? -6.383  -10.865 6.019  1.00 14.83 ? 32  HIS A CB  1 
ATOM   242  C  CG  . HIS A 1 32 ? -7.757  -11.009 5.478  1.00 15.41 ? 32  HIS A CG  1 
ATOM   243  N  ND1 . HIS A 1 32 ? -8.824  -11.300 6.285  1.00 16.83 ? 32  HIS A ND1 1 
ATOM   244  C  CD2 . HIS A 1 32 ? -8.256  -10.850 4.220  1.00 14.94 ? 32  HIS A CD2 1 
ATOM   245  C  CE1 . HIS A 1 32 ? -9.928  -11.342 5.554  1.00 20.18 ? 32  HIS A CE1 1 
ATOM   246  N  NE2 . HIS A 1 32 ? -9.611  -11.053 4.303  1.00 19.38 ? 32  HIS A NE2 1 
ATOM   247  N  N   . ALA A 1 33 ? -3.800  -9.239  7.185  1.00 13.67 ? 33  ALA A N   1 
ATOM   248  C  CA  . ALA A 1 33 ? -2.639  -9.137  8.063  1.00 15.35 ? 33  ALA A CA  1 
ATOM   249  C  C   . ALA A 1 33 ? -2.931  -8.008  9.071  1.00 13.85 ? 33  ALA A C   1 
ATOM   250  O  O   . ALA A 1 33 ? -2.623  -8.145  10.270 1.00 14.50 ? 33  ALA A O   1 
ATOM   251  C  CB  . ALA A 1 33 ? -1.351  -8.799  7.270  1.00 14.76 ? 33  ALA A CB  1 
ATOM   252  N  N   . LYS A 1 34 ? -3.518  -6.896  8.590  1.00 15.43 ? 34  LYS A N   1 
ATOM   253  C  CA  . LYS A 1 34 ? -3.767  -5.804  9.529  1.00 14.06 ? 34  LYS A CA  1 
ATOM   254  C  C   . LYS A 1 34 ? -4.857  -6.159  10.570 1.00 15.36 ? 34  LYS A C   1 
ATOM   255  O  O   . LYS A 1 34 ? -4.715  -5.774  11.720 1.00 16.57 ? 34  LYS A O   1 
ATOM   256  C  CB  . LYS A 1 34 ? -4.134  -4.551  8.819  1.00 15.68 ? 34  LYS A CB  1 
ATOM   257  C  CG  . LYS A 1 34 ? -2.867  -3.966  8.071  1.00 13.81 ? 34  LYS A CG  1 
ATOM   258  C  CD  . LYS A 1 34 ? -3.312  -2.744  7.210  1.00 20.66 ? 34  LYS A CD  1 
ATOM   259  C  CE  . LYS A 1 34 ? -2.197  -2.311  6.320  1.00 23.92 ? 34  LYS A CE  1 
ATOM   260  N  NZ  . LYS A 1 34 ? -2.665  -1.203  5.440  1.00 27.46 ? 34  LYS A NZ  1 
ATOM   261  N  N   . GLU A 1 35 ? -5.904  -6.869  10.158 1.00 15.78 ? 35  GLU A N   1 
ATOM   262  C  CA  . GLU A 1 35 ? -6.926  -7.351  11.072 1.00 15.99 ? 35  GLU A CA  1 
ATOM   263  C  C   . GLU A 1 35 ? -6.299  -8.346  12.034 1.00 15.53 ? 35  GLU A C   1 
ATOM   264  O  O   . GLU A 1 35 ? -6.586  -8.287  13.210 1.00 16.02 ? 35  GLU A O   1 
ATOM   265  C  CB  . GLU A 1 35 ? -8.166  -7.915  10.344 1.00 16.78 ? 35  GLU A CB  1 
ATOM   266  C  CG  A GLU A 1 35 ? -8.907  -6.876  9.483  0.50 19.30 ? 35  GLU A CG  1 
ATOM   267  C  CG  B GLU A 1 35 ? -9.322  -6.966  10.672 0.50 21.62 ? 35  GLU A CG  1 
ATOM   268  C  CD  A GLU A 1 35 ? -10.127 -7.412  8.742  0.50 20.01 ? 35  GLU A CD  1 
ATOM   269  C  CD  B GLU A 1 35 ? -10.682 -7.506  10.467 0.50 23.45 ? 35  GLU A CD  1 
ATOM   270  O  OE1 A GLU A 1 35 ? -9.944  -8.072  7.675  0.50 26.43 ? 35  GLU A OE1 1 
ATOM   271  O  OE1 B GLU A 1 35 ? -10.900 -8.141  9.410  0.50 19.35 ? 35  GLU A OE1 1 
ATOM   272  O  OE2 A GLU A 1 35 ? -11.258 -7.123  9.190  0.50 24.54 ? 35  GLU A OE2 1 
ATOM   273  O  OE2 B GLU A 1 35 ? -11.541 -7.256  11.364 0.50 23.88 ? 35  GLU A OE2 1 
ATOM   274  N  N   . SER A 1 36 ? -5.501  -9.290  11.505 1.00 12.92 ? 36  SER A N   1 
ATOM   275  C  CA  . SER A 1 36 ? -4.799  -10.254 12.353 1.00 14.16 ? 36  SER A CA  1 
ATOM   276  C  C   . SER A 1 36 ? -4.002  -9.555  13.420 1.00 12.60 ? 36  SER A C   1 
ATOM   277  O  O   . SER A 1 36 ? -4.002  -9.938  14.596 1.00 14.61 ? 36  SER A O   1 
ATOM   278  C  CB  . SER A 1 36 ? -3.856  -11.100 11.491 1.00 14.94 ? 36  SER A CB  1 
ATOM   279  O  OG  . SER A 1 36 ? -3.333  -12.104 12.330 1.00 15.88 ? 36  SER A OG  1 
ATOM   280  N  N   . LEU A 1 37 ? -3.308  -8.506  13.011 1.00 13.02 ? 37  LEU A N   1 
ATOM   281  C  CA  . LEU A 1 37 ? -2.433  -7.750  13.931 1.00 13.56 ? 37  LEU A CA  1 
ATOM   282  C  C   . LEU A 1 37 ? -3.188  -7.028  15.024 1.00 14.38 ? 37  LEU A C   1 
ATOM   283  O  O   . LEU A 1 37 ? -2.792  -7.025  16.235 1.00 14.57 ? 37  LEU A O   1 
ATOM   284  C  CB  . LEU A 1 37 ? -1.587  -6.809  13.061 1.00 15.18 ? 37  LEU A CB  1 
ATOM   285  C  CG  . LEU A 1 37 ? -0.665  -5.905  13.897 1.00 16.62 ? 37  LEU A CG  1 
ATOM   286  C  CD1 . LEU A 1 37 ? 0.428   -6.789  14.658 1.00 18.35 ? 37  LEU A CD1 1 
ATOM   287  C  CD2 . LEU A 1 37 ? -0.047  -4.842  13.017 1.00 20.25 ? 37  LEU A CD2 1 
ATOM   288  N  N   . THR A 1 38 ? -4.331  -6.470  14.648 1.00 15.61 ? 38  THR A N   1 
ATOM   289  C  CA  . THR A 1 38 ? -5.171  -5.830  15.663 1.00 16.69 ? 38  THR A CA  1 
ATOM   290  C  C   . THR A 1 38 ? -5.560  -6.833  16.729 1.00 16.89 ? 38  THR A C   1 
ATOM   291  O  O   . THR A 1 38 ? -5.466  -6.552  17.960 1.00 17.99 ? 38  THR A O   1 
ATOM   292  C  CB  . THR A 1 38 ? -6.398  -5.244  15.000 1.00 16.79 ? 38  THR A CB  1 
ATOM   293  O  OG1 . THR A 1 38 ? -5.961  -4.271  14.031 1.00 16.69 ? 38  THR A OG1 1 
ATOM   294  C  CG2 . THR A 1 38 ? -7.258  -4.486  16.060 1.00 18.09 ? 38  THR A CG2 1 
ATOM   295  N  N   . HIS A 1 39 ? -5.981  -8.014  16.275 1.00 15.71 ? 39  HIS A N   1 
ATOM   296  C  CA  . HIS A 1 39 ? -6.368  -9.065  17.234 1.00 16.22 ? 39  HIS A CA  1 
ATOM   297  C  C   . HIS A 1 39 ? -5.182  -9.600  18.014 1.00 16.46 ? 39  HIS A C   1 
ATOM   298  O  O   . HIS A 1 39 ? -5.308  -9.822  19.178 1.00 18.47 ? 39  HIS A O   1 
ATOM   299  C  CB  . HIS A 1 39 ? -7.066  -10.215 16.529 1.00 16.18 ? 39  HIS A CB  1 
ATOM   300  C  CG  . HIS A 1 39 ? -8.496  -9.930  16.226 1.00 14.09 ? 39  HIS A CG  1 
ATOM   301  N  ND1 . HIS A 1 39 ? -9.467  -9.935  17.210 1.00 14.36 ? 39  HIS A ND1 1 
ATOM   302  C  CD2 . HIS A 1 39 ? -9.106  -9.563  15.078 1.00 14.27 ? 39  HIS A CD2 1 
ATOM   303  C  CE1 . HIS A 1 39 ? -10.634 -9.628  16.657 1.00 18.34 ? 39  HIS A CE1 1 
ATOM   304  N  NE2 . HIS A 1 39 ? -10.446 -9.402  15.361 1.00 13.71 ? 39  HIS A NE2 1 
ATOM   305  N  N   . ALA A 1 40 ? -4.049  -9.795  17.363 1.00 16.36 ? 40  ALA A N   1 
ATOM   306  C  CA  . ALA A 1 40 ? -2.867  -10.283 18.047 1.00 17.07 ? 40  ALA A CA  1 
ATOM   307  C  C   . ALA A 1 40 ? -2.438  -9.287  19.121 1.00 17.61 ? 40  ALA A C   1 
ATOM   308  O  O   . ALA A 1 40 ? -2.061  -9.702  20.246 1.00 17.14 ? 40  ALA A O   1 
ATOM   309  C  CB  . ALA A 1 40 ? -1.690  -10.592 17.055 1.00 16.40 ? 40  ALA A CB  1 
ATOM   310  N  N   . LYS A 1 41 ? -2.490  -7.990  18.813 1.00 17.96 ? 41  LYS A N   1 
ATOM   311  C  CA  . LYS A 1 41 ? -2.181  -6.990  19.835 1.00 18.88 ? 41  LYS A CA  1 
ATOM   312  C  C   . LYS A 1 41 ? -3.194  -7.026  20.979 1.00 19.94 ? 41  LYS A C   1 
ATOM   313  O  O   . LYS A 1 41 ? -2.829  -6.803  22.165 1.00 19.48 ? 41  LYS A O   1 
ATOM   314  C  CB  . LYS A 1 41 ? -2.131  -5.550  19.234 1.00 19.65 ? 41  LYS A CB  1 
ATOM   315  C  CG  . LYS A 1 41 ? -0.943  -5.309  18.312 1.00 19.40 ? 41  LYS A CG  1 
ATOM   316  C  CD  . LYS A 1 41 ? -1.041  -3.902  17.691 1.00 21.97 ? 41  LYS A CD  1 
ATOM   317  C  CE  A LYS A 1 41 ? 0.072   -3.688  16.663 0.50 28.59 ? 41  LYS A CE  1 
ATOM   318  C  CE  B LYS A 1 41 ? 0.138   -3.617  16.791 0.50 23.48 ? 41  LYS A CE  1 
ATOM   319  N  NZ  A LYS A 1 41 ? 1.470   -3.774  17.196 0.50 31.22 ? 41  LYS A NZ  1 
ATOM   320  N  NZ  B LYS A 1 41 ? -0.061  -2.329  16.052 0.50 15.00 ? 41  LYS A NZ  1 
ATOM   321  N  N   . ALA A 1 42 ? -4.473  -7.228  20.641 1.00 18.52 ? 42  ALA A N   1 
ATOM   322  C  CA  . ALA A 1 42 ? -5.527  -7.313  21.664 1.00 20.34 ? 42  ALA A CA  1 
ATOM   323  C  C   . ALA A 1 42 ? -5.334  -8.604  22.547 1.00 22.44 ? 42  ALA A C   1 
ATOM   324  O  O   . ALA A 1 42 ? -5.691  -8.623  23.722 1.00 22.85 ? 42  ALA A O   1 
ATOM   325  C  CB  . ALA A 1 42 ? -6.841  -7.322  20.964 1.00 18.76 ? 42  ALA A CB  1 
ATOM   326  N  N   . ALA A 1 43 ? -4.707  -9.627  21.977 1.00 23.38 ? 43  ALA A N   1 
ATOM   327  C  CA  . ALA A 1 43 ? -4.437  -10.884 22.717 1.00 26.82 ? 43  ALA A CA  1 
ATOM   328  C  C   . ALA A 1 43 ? -3.247  -10.718 23.638 1.00 30.36 ? 43  ALA A C   1 
ATOM   329  O  O   . ALA A 1 43 ? -3.166  -11.394 24.676 1.00 33.32 ? 43  ALA A O   1 
ATOM   330  C  CB  . ALA A 1 43 ? -4.154  -11.978 21.777 1.00 24.53 ? 43  ALA A CB  1 
ATOM   331  N  N   . SER A 1 44 ? -2.288  -9.867  23.252 1.00 32.44 ? 44  SER A N   1 
ATOM   332  C  CA  . SER A 1 44 ? -1.154  -9.620  24.124 1.00 36.22 ? 44  SER A CA  1 
ATOM   333  C  C   . SER A 1 44 ? -1.709  -9.253  25.491 1.00 37.92 ? 44  SER A C   1 
ATOM   334  O  O   . SER A 1 44 ? -0.965  -8.760  26.308 1.00 40.00 ? 44  SER A O   1 
ATOM   335  C  CB  . SER A 1 44 ? -0.284  -8.461  23.667 1.00 37.45 ? 44  SER A CB  1 
ATOM   336  O  OG  . SER A 1 44 ? 0.028   -8.620  22.340 1.00 39.18 ? 44  SER A OG  1 
ATOM   337  N  N   . THR A 1 50 ? 4.738   -14.978 24.862 1.00 36.19 ? 50  THR A N   1 
ATOM   338  C  CA  . THR A 1 50 ? 5.843   -14.659 23.948 1.00 36.12 ? 50  THR A CA  1 
ATOM   339  C  C   . THR A 1 50 ? 5.540   -15.100 22.528 1.00 34.04 ? 50  THR A C   1 
ATOM   340  O  O   . THR A 1 50 ? 6.015   -14.490 21.582 1.00 33.91 ? 50  THR A O   1 
ATOM   341  C  CB  . THR A 1 50 ? 7.205   -15.283 24.402 1.00 39.12 ? 50  THR A CB  1 
ATOM   342  O  OG1 . THR A 1 50 ? 7.083   -16.711 24.414 1.00 41.86 ? 50  THR A OG1 1 
ATOM   343  C  CG2 . THR A 1 50 ? 7.611   -14.798 25.791 1.00 38.54 ? 50  THR A CG2 1 
ATOM   344  N  N   . HIS A 1 51 ? 4.740   -16.155 22.379 1.00 33.83 ? 51  HIS A N   1 
ATOM   345  C  CA  . HIS A 1 51 ? 4.279   -16.652 21.082 1.00 33.06 ? 51  HIS A CA  1 
ATOM   346  C  C   . HIS A 1 51 ? 3.551   -15.504 20.385 1.00 30.71 ? 51  HIS A C   1 
ATOM   347  O  O   . HIS A 1 51 ? 3.762   -15.251 19.189 1.00 29.64 ? 51  HIS A O   1 
ATOM   348  C  CB  . HIS A 1 51 ? 3.274   -17.820 21.246 1.00 34.58 ? 51  HIS A CB  1 
ATOM   349  C  CG  . HIS A 1 51 ? 3.362   -18.499 22.582 1.00 41.75 ? 51  HIS A CG  1 
ATOM   350  N  ND1 . HIS A 1 51 ? 4.272   -19.501 22.851 1.00 50.07 ? 51  HIS A ND1 1 
ATOM   351  C  CD2 . HIS A 1 51 ? 2.697   -18.274 23.742 1.00 44.99 ? 51  HIS A CD2 1 
ATOM   352  C  CE1 . HIS A 1 51 ? 4.152   -19.881 24.116 1.00 48.58 ? 51  HIS A CE1 1 
ATOM   353  N  NE2 . HIS A 1 51 ? 3.204   -19.149 24.678 1.00 48.63 ? 51  HIS A NE2 1 
ATOM   354  N  N   . VAL A 1 52 ? 2.700   -14.811 21.141 1.00 28.80 ? 52  VAL A N   1 
ATOM   355  C  CA  . VAL A 1 52 ? 1.893   -13.748 20.562 1.00 26.69 ? 52  VAL A CA  1 
ATOM   356  C  C   . VAL A 1 52 ? 2.827   -12.651 20.085 1.00 25.71 ? 52  VAL A C   1 
ATOM   357  O  O   . VAL A 1 52 ? 2.620   -12.121 19.021 1.00 23.81 ? 52  VAL A O   1 
ATOM   358  C  CB  . VAL A 1 52 ? 0.790   -13.200 21.511 1.00 25.99 ? 52  VAL A CB  1 
ATOM   359  C  CG1 . VAL A 1 52 ? 0.046   -12.019 20.835 1.00 23.61 ? 52  VAL A CG1 1 
ATOM   360  C  CG2 . VAL A 1 52 ? -0.221  -14.318 21.786 1.00 27.00 ? 52  VAL A CG2 1 
ATOM   361  N  N   . GLY A 1 53 ? 3.856   -12.350 20.877 1.00 25.59 ? 53  GLY A N   1 
ATOM   362  C  CA  . GLY A 1 53 ? 4.799   -11.299 20.502 1.00 25.10 ? 53  GLY A CA  1 
ATOM   363  C  C   . GLY A 1 53 ? 5.556   -11.642 19.246 1.00 24.23 ? 53  GLY A C   1 
ATOM   364  O  O   . GLY A 1 53 ? 5.793   -10.780 18.446 1.00 21.49 ? 53  GLY A O   1 
ATOM   365  N  N   . HIS A 1 54 ? 5.968   -12.905 19.090 1.00 23.71 ? 54  HIS A N   1 
ATOM   366  C  CA  . HIS A 1 54 ? 6.545   -13.346 17.804 1.00 23.87 ? 54  HIS A CA  1 
ATOM   367  C  C   . HIS A 1 54 ? 5.578   -13.224 16.659 1.00 22.12 ? 54  HIS A C   1 
ATOM   368  O  O   . HIS A 1 54 ? 5.962   -12.735 15.571 1.00 22.32 ? 54  HIS A O   1 
ATOM   369  C  CB  . HIS A 1 54 ? 7.148   -14.763 17.891 1.00 24.57 ? 54  HIS A CB  1 
ATOM   370  C  CG  . HIS A 1 54 ? 8.399   -14.813 18.685 1.00 26.76 ? 54  HIS A CG  1 
ATOM   371  N  ND1 . HIS A 1 54 ? 8.547   -15.581 19.826 1.00 27.93 ? 54  HIS A ND1 1 
ATOM   372  C  CD2 . HIS A 1 54 ? 9.584   -14.198 18.488 1.00 28.91 ? 54  HIS A CD2 1 
ATOM   373  C  CE1 . HIS A 1 54 ? 9.763   -15.416 20.303 1.00 29.33 ? 54  HIS A CE1 1 
ATOM   374  N  NE2 . HIS A 1 54 ? 10.413  -14.583 19.505 1.00 33.07 ? 54  HIS A NE2 1 
ATOM   375  N  N   . GLY A 1 55 ? 4.320   -13.620 16.884 1.00 21.25 ? 55  GLY A N   1 
ATOM   376  C  CA  . GLY A 1 55 ? 3.273   -13.460 15.874 1.00 19.92 ? 55  GLY A CA  1 
ATOM   377  C  C   . GLY A 1 55 ? 3.136   -11.996 15.451 1.00 19.66 ? 55  GLY A C   1 
ATOM   378  O  O   . GLY A 1 55 ? 3.036   -11.716 14.259 1.00 18.76 ? 55  GLY A O   1 
ATOM   379  N  N   . ILE A 1 56 ? 3.067   -11.083 16.405 1.00 18.70 ? 56  ILE A N   1 
ATOM   380  C  CA  . ILE A 1 56 ? 2.965   -9.646  16.121 1.00 19.51 ? 56  ILE A CA  1 
ATOM   381  C  C   . ILE A 1 56 ? 4.120   -9.138  15.220 1.00 19.66 ? 56  ILE A C   1 
ATOM   382  O  O   . ILE A 1 56 ? 3.896   -8.403  14.261 1.00 17.76 ? 56  ILE A O   1 
ATOM   383  C  CB  . ILE A 1 56 ? 2.937   -8.846  17.440 1.00 18.73 ? 56  ILE A CB  1 
ATOM   384  C  CG1 . ILE A 1 56 ? 1.593   -9.082  18.149 1.00 16.73 ? 56  ILE A CG1 1 
ATOM   385  C  CG2 . ILE A 1 56 ? 3.228   -7.352  17.143 1.00 23.42 ? 56  ILE A CG2 1 
ATOM   386  C  CD1 . ILE A 1 56 ? 1.501   -8.442  19.601 1.00 21.67 ? 56  ILE A CD1 1 
ATOM   387  N  N   . LYS A 1 57 ? 5.344   -9.575  15.533 1.00 21.88 ? 57  LYS A N   1 
ATOM   388  C  CA  . LYS A 1 57 ? 6.563   -9.163  14.817 1.00 23.12 ? 57  LYS A CA  1 
ATOM   389  C  C   . LYS A 1 57 ? 6.446   -9.625  13.392 1.00 20.29 ? 57  LYS A C   1 
ATOM   390  O  O   . LYS A 1 57 ? 6.689   -8.849  12.445 1.00 20.57 ? 57  LYS A O   1 
ATOM   391  C  CB  . LYS A 1 57 ? 7.856   -9.709  15.474 1.00 24.70 ? 57  LYS A CB  1 
ATOM   392  C  CG  . LYS A 1 57 ? 8.390   -8.798  16.613 1.00 33.29 ? 57  LYS A CG  1 
ATOM   393  C  CD  . LYS A 1 57 ? 9.245   -9.455  17.770 1.00 34.76 ? 57  LYS A CD  1 
ATOM   394  C  CE  . LYS A 1 57 ? 9.726   -8.354  18.740 1.00 37.91 ? 57  LYS A CE  1 
ATOM   395  N  NZ  . LYS A 1 57 ? 10.681  -8.714  19.892 1.00 45.06 ? 57  LYS A NZ  1 
ATOM   396  N  N   . HIS A 1 58 ? 6.035   -10.876 13.197 1.00 17.99 ? 58  HIS A N   1 
ATOM   397  C  CA  . HIS A 1 58 ? 5.889   -11.392 11.846 1.00 17.85 ? 58  HIS A CA  1 
ATOM   398  C  C   . HIS A 1 58 ? 4.766   -10.716 11.071 1.00 17.15 ? 58  HIS A C   1 
ATOM   399  O  O   . HIS A 1 58 ? 4.896   -10.514 9.880  1.00 18.30 ? 58  HIS A O   1 
ATOM   400  C  CB  . HIS A 1 58 ? 5.641   -12.927 11.821 1.00 14.44 ? 58  HIS A CB  1 
ATOM   401  C  CG  . HIS A 1 58 ? 6.876   -13.731 12.050 1.00 17.24 ? 58  HIS A CG  1 
ATOM   402  N  ND1 . HIS A 1 58 ? 7.902   -13.825 11.118 1.00 19.97 ? 58  HIS A ND1 1 
ATOM   403  C  CD2 . HIS A 1 58 ? 7.285   -14.416 13.128 1.00 19.61 ? 58  HIS A CD2 1 
ATOM   404  C  CE1 . HIS A 1 58 ? 8.872   -14.569 11.618 1.00 24.44 ? 58  HIS A CE1 1 
ATOM   405  N  NE2 . HIS A 1 58 ? 8.529   -14.927 12.844 1.00 23.30 ? 58  HIS A NE2 1 
ATOM   406  N  N   . LEU A 1 59 ? 3.637   -10.456 11.718 1.00 16.07 ? 59  LEU A N   1 
ATOM   407  C  CA  . LEU A 1 59 ? 2.552   -9.730  11.057 1.00 17.23 ? 59  LEU A CA  1 
ATOM   408  C  C   . LEU A 1 59 ? 3.007   -8.352  10.628 1.00 16.96 ? 59  LEU A C   1 
ATOM   409  O  O   . LEU A 1 59 ? 2.651   -7.897  9.569  1.00 18.06 ? 59  LEU A O   1 
ATOM   410  C  CB  . LEU A 1 59 ? 1.346   -9.600  11.982 1.00 15.93 ? 59  LEU A CB  1 
ATOM   411  C  CG  . LEU A 1 59 ? 0.589   -10.939 12.180 1.00 15.37 ? 59  LEU A CG  1 
ATOM   412  C  CD1 . LEU A 1 59 ? -0.390  -10.777 13.359 1.00 15.86 ? 59  LEU A CD1 1 
ATOM   413  C  CD2 . LEU A 1 59 ? -0.105  -11.490 10.905 1.00 13.99 ? 59  LEU A CD2 1 
ATOM   414  N  N   . GLU A 1 60 ? 3.786   -7.698  11.448 1.00 17.97 ? 60  GLU A N   1 
ATOM   415  C  CA  . GLU A 1 60 ? 4.264   -6.334  11.124 1.00 19.84 ? 60  GLU A CA  1 
ATOM   416  C  C   . GLU A 1 60 ? 5.191   -6.440  9.905  1.00 21.12 ? 60  GLU A C   1 
ATOM   417  O  O   . GLU A 1 60 ? 5.136   -5.627  8.981  1.00 21.26 ? 60  GLU A O   1 
ATOM   418  C  CB  . GLU A 1 60 ? 5.001   -5.759  12.329 1.00 21.72 ? 60  GLU A CB  1 
ATOM   419  C  CG  . GLU A 1 60 ? 4.028   -5.303  13.470 1.00 22.53 ? 60  GLU A CG  1 
ATOM   420  C  CD  . GLU A 1 60 ? 4.719   -4.881  14.805 1.00 29.10 ? 60  GLU A CD  1 
ATOM   421  O  OE1 . GLU A 1 60 ? 4.006   -4.359  15.699 1.00 37.29 ? 60  GLU A OE1 1 
ATOM   422  O  OE2 . GLU A 1 60 ? 5.941   -5.093  14.993 1.00 35.38 ? 60  GLU A OE2 1 
ATOM   423  N  N   . ASP A 1 61 ? 6.051   -7.447  9.917  1.00 20.18 ? 61  ASP A N   1 
ATOM   424  C  CA  . ASP A 1 61 ? 6.920   -7.724  8.791  1.00 22.60 ? 61  ASP A CA  1 
ATOM   425  C  C   . ASP A 1 61 ? 6.136   -8.083  7.564  1.00 19.89 ? 61  ASP A C   1 
ATOM   426  O  O   . ASP A 1 61 ? 6.514   -7.670  6.493  1.00 22.19 ? 61  ASP A O   1 
ATOM   427  C  CB  . ASP A 1 61 ? 7.911   -8.869  9.090  1.00 22.56 ? 61  ASP A CB  1 
ATOM   428  C  CG  . ASP A 1 61 ? 9.030   -8.435  9.998  1.00 29.29 ? 61  ASP A CG  1 
ATOM   429  O  OD1 . ASP A 1 61 ? 9.174   -7.194  10.201 1.00 31.59 ? 61  ASP A OD1 1 
ATOM   430  O  OD2 . ASP A 1 61 ? 9.746   -9.322  10.536 1.00 31.54 ? 61  ASP A OD2 1 
ATOM   431  N  N   . ALA A 1 62 ? 5.073   -8.874  7.702  1.00 19.33 ? 62  ALA A N   1 
ATOM   432  C  CA  . ALA A 1 62 ? 4.239   -9.227  6.548  1.00 19.17 ? 62  ALA A CA  1 
ATOM   433  C  C   . ALA A 1 62 ? 3.646   -7.951  5.949  1.00 19.71 ? 62  ALA A C   1 
ATOM   434  O  O   . ALA A 1 62 ? 3.616   -7.766  4.747  1.00 20.13 ? 62  ALA A O   1 
ATOM   435  C  CB  . ALA A 1 62 ? 3.063   -10.211 6.954  1.00 16.58 ? 62  ALA A CB  1 
ATOM   436  N  N   . ILE A 1 63 ? 3.196   -7.056  6.789  1.00 18.77 ? 63  ILE A N   1 
ATOM   437  C  CA  . ILE A 1 63 ? 2.577   -5.815  6.261  1.00 19.37 ? 63  ILE A CA  1 
ATOM   438  C  C   . ILE A 1 63 ? 3.614   -4.980  5.556  1.00 21.21 ? 63  ILE A C   1 
ATOM   439  O  O   . ILE A 1 63 ? 3.380   -4.484  4.446  1.00 21.38 ? 63  ILE A O   1 
ATOM   440  C  CB  . ILE A 1 63 ? 1.901   -5.014  7.397  1.00 18.66 ? 63  ILE A CB  1 
ATOM   441  C  CG1 . ILE A 1 63 ? 0.681   -5.809  7.897  1.00 17.16 ? 63  ILE A CG1 1 
ATOM   442  C  CG2 . ILE A 1 63 ? 1.498   -3.634  6.912  1.00 20.24 ? 63  ILE A CG2 1 
ATOM   443  C  CD1 . ILE A 1 63 ? 0.271   -5.521  9.338  1.00 16.82 ? 63  ILE A CD1 1 
ATOM   444  N  N   . LYS A 1 64 ? 4.800   -4.860  6.160  1.00 21.60 ? 64  LYS A N   1 
ATOM   445  C  CA  . LYS A 1 64 ? 5.850   -4.044  5.521  1.00 23.97 ? 64  LYS A CA  1 
ATOM   446  C  C   . LYS A 1 64 ? 6.208   -4.593  4.123  1.00 24.76 ? 64  LYS A C   1 
ATOM   447  O  O   . LYS A 1 64 ? 6.292   -3.853  3.159  1.00 26.48 ? 64  LYS A O   1 
ATOM   448  C  CB  . LYS A 1 64 ? 7.099   -4.010  6.421  1.00 25.24 ? 64  LYS A CB  1 
ATOM   449  C  CG  . LYS A 1 64 ? 8.328   -3.341  5.751  1.00 30.76 ? 64  LYS A CG  1 
ATOM   450  C  CD  . LYS A 1 64 ? 7.982   -1.835  5.483  1.00 38.26 ? 64  LYS A CD  1 
ATOM   451  C  CE  . LYS A 1 64 ? 9.179   -0.931  4.944  1.00 42.15 ? 64  LYS A CE  1 
ATOM   452  N  NZ  . LYS A 1 64 ? 9.922   -0.223  6.076  1.00 49.63 ? 64  LYS A NZ  1 
ATOM   453  N  N   . HIS A 1 65 ? 6.435   -5.892  4.021  1.00 23.08 ? 65  HIS A N   1 
ATOM   454  C  CA  . HIS A 1 65 ? 6.783   -6.485  2.777  1.00 24.99 ? 65  HIS A CA  1 
ATOM   455  C  C   . HIS A 1 65 ? 5.680   -6.429  1.745  1.00 24.83 ? 65  HIS A C   1 
ATOM   456  O  O   . HIS A 1 65 ? 5.939   -6.199  0.557  1.00 24.25 ? 65  HIS A O   1 
ATOM   457  C  CB  . HIS A 1 65 ? 7.266   -7.912  2.978  1.00 25.80 ? 65  HIS A CB  1 
ATOM   458  C  CG  . HIS A 1 65 ? 8.642   -7.977  3.560  1.00 28.51 ? 65  HIS A CG  1 
ATOM   459  N  ND1 . HIS A 1 65 ? 9.771   -7.736  2.825  1.00 33.81 ? 65  HIS A ND1 1 
ATOM   460  C  CD2 . HIS A 1 65 ? 9.064   -8.248  4.818  1.00 29.23 ? 65  HIS A CD2 1 
ATOM   461  C  CE1 . HIS A 1 65 ? 10.841  -7.864  3.596  1.00 31.58 ? 65  HIS A CE1 1 
ATOM   462  N  NE2 . HIS A 1 65 ? 10.442  -8.177  4.813  1.00 28.02 ? 65  HIS A NE2 1 
ATOM   463  N  N   . GLY A 1 66 ? 4.454   -6.699  2.181  1.00 23.21 ? 66  GLY A N   1 
ATOM   464  C  CA  . GLY A 1 66 ? 3.304   -6.466  1.335  1.00 24.77 ? 66  GLY A CA  1 
ATOM   465  C  C   . GLY A 1 66 ? 3.209   -5.040  0.790  1.00 27.87 ? 66  GLY A C   1 
ATOM   466  O  O   . GLY A 1 66 ? 2.942   -4.812  -0.427 1.00 28.52 ? 66  GLY A O   1 
ATOM   467  N  N   . GLU A 1 67 ? 3.391   -4.071  1.679  1.00 27.17 ? 67  GLU A N   1 
ATOM   468  C  CA  . GLU A 1 67 ? 3.365   -2.701  1.235  1.00 31.45 ? 67  GLU A CA  1 
ATOM   469  C  C   . GLU A 1 67 ? 4.512   -2.428  0.236  1.00 33.42 ? 67  GLU A C   1 
ATOM   470  O  O   . GLU A 1 67 ? 4.374   -1.580  -0.632 1.00 36.04 ? 67  GLU A O   1 
ATOM   471  C  CB  . GLU A 1 67 ? 3.353   -1.767  2.447  1.00 32.09 ? 67  GLU A CB  1 
ATOM   472  C  CG  . GLU A 1 67 ? 2.162   -2.114  3.346  1.00 33.89 ? 67  GLU A CG  1 
ATOM   473  C  CD  . GLU A 1 67 ? 1.554   -0.930  4.054  1.00 44.56 ? 67  GLU A CD  1 
ATOM   474  O  OE1 . GLU A 1 67 ? 2.352   -0.079  4.566  1.00 47.57 ? 67  GLU A OE1 1 
ATOM   475  O  OE2 . GLU A 1 67 ? 0.276   -0.847  4.077  1.00 44.20 ? 67  GLU A OE2 1 
ATOM   476  N  N   . GLU A 1 68 ? 5.620   -3.170  0.361  1.00 32.98 ? 68  GLU A N   1 
ATOM   477  C  CA  . GLU A 1 68 ? 6.759   -3.215  -0.572 1.00 35.29 ? 68  GLU A CA  1 
ATOM   478  C  C   . GLU A 1 68 ? 6.641   -4.034  -1.873 1.00 34.94 ? 68  GLU A C   1 
ATOM   479  O  O   . GLU A 1 68 ? 7.552   -4.034  -2.697 1.00 37.02 ? 68  GLU A O   1 
ATOM   480  C  CB  . GLU A 1 68 ? 8.028   -3.668  0.152  1.00 34.48 ? 68  GLU A CB  1 
ATOM   481  C  CG  . GLU A 1 68 ? 8.466   -2.630  1.192  1.00 38.38 ? 68  GLU A CG  1 
ATOM   482  C  CD  . GLU A 1 68 ? 9.812   -2.916  1.862  1.00 42.11 ? 68  GLU A CD  1 
ATOM   483  O  OE1 . GLU A 1 68 ? 10.265  -2.014  2.626  1.00 50.39 ? 68  GLU A OE1 1 
ATOM   484  O  OE2 . GLU A 1 68 ? 10.433  -3.993  1.615  1.00 48.53 ? 68  GLU A OE2 1 
ATOM   485  N  N   . GLY A 1 69 ? 5.555   -4.729  -2.067 1.00 32.95 ? 69  GLY A N   1 
ATOM   486  C  CA  . GLY A 1 69 ? 5.299   -5.403  -3.335 1.00 34.37 ? 69  GLY A CA  1 
ATOM   487  C  C   . GLY A 1 69 ? 5.874   -6.809  -3.372 1.00 34.34 ? 69  GLY A C   1 
ATOM   488  O  O   . GLY A 1 69 ? 5.978   -7.415  -4.440 1.00 35.86 ? 69  GLY A O   1 
ATOM   489  N  N   . HIS A 1 70 ? 6.266   -7.324  -2.210 1.00 31.64 ? 70  HIS A N   1 
ATOM   490  C  CA  . HIS A 1 70 ? 6.854   -8.642  -2.130 1.00 29.82 ? 70  HIS A CA  1 
ATOM   491  C  C   . HIS A 1 70 ? 5.898   -9.501  -1.409 1.00 26.64 ? 70  HIS A C   1 
ATOM   492  O  O   . HIS A 1 70 ? 6.078   -9.787  -0.262 1.00 23.76 ? 70  HIS A O   1 
ATOM   493  C  CB  . HIS A 1 70 ? 8.209   -8.622  -1.449 1.00 30.40 ? 70  HIS A CB  1 
ATOM   494  C  CG  . HIS A 1 70 ? 9.219   -7.914  -2.267 1.00 31.97 ? 70  HIS A CG  1 
ATOM   495  N  ND1 . HIS A 1 70 ? 9.873   -6.787  -1.818 1.00 34.14 ? 70  HIS A ND1 1 
ATOM   496  C  CD2 . HIS A 1 70 ? 9.619   -8.109  -3.541 1.00 30.58 ? 70  HIS A CD2 1 
ATOM   497  C  CE1 . HIS A 1 70 ? 10.667  -6.335  -2.764 1.00 35.44 ? 70  HIS A CE1 1 
ATOM   498  N  NE2 . HIS A 1 70 ? 10.537  -7.119  -3.824 1.00 40.10 ? 70  HIS A NE2 1 
ATOM   499  N  N   . VAL A 1 71 ? 4.886   -9.931  -2.139 1.00 25.00 ? 71  VAL A N   1 
ATOM   500  C  CA  . VAL A 1 71 ? 3.824   -10.712 -1.564 1.00 24.55 ? 71  VAL A CA  1 
ATOM   501  C  C   . VAL A 1 71 ? 4.272   -12.131 -1.187 1.00 24.59 ? 71  VAL A C   1 
ATOM   502  O  O   . VAL A 1 71 ? 3.693   -12.713 -0.318 1.00 24.27 ? 71  VAL A O   1 
ATOM   503  C  CB  . VAL A 1 71 ? 2.609   -10.759 -2.530 1.00 25.53 ? 71  VAL A CB  1 
ATOM   504  C  CG1 . VAL A 1 71 ? 2.954   -11.556 -3.760 1.00 28.16 ? 71  VAL A CG1 1 
ATOM   505  C  CG2 . VAL A 1 71 ? 1.286   -11.238 -1.798 1.00 22.71 ? 71  VAL A CG2 1 
ATOM   506  N  N   . GLY A 1 72 ? 5.265   -12.685 -1.867 1.00 25.50 ? 72  GLY A N   1 
ATOM   507  C  CA  . GLY A 1 72 ? 5.802   -13.974 -1.454 1.00 25.75 ? 72  GLY A CA  1 
ATOM   508  C  C   . GLY A 1 72 ? 6.368   -13.806 -0.047 1.00 27.15 ? 72  GLY A C   1 
ATOM   509  O  O   . GLY A 1 72 ? 6.161   -14.705 0.868  1.00 23.64 ? 72  GLY A O   1 
ATOM   510  N  N   . VAL A 1 73 ? 7.103   -12.696 0.139  1.00 23.04 ? 73  VAL A N   1 
ATOM   511  C  CA  . VAL A 1 73 ? 7.824   -12.527 1.413  1.00 24.01 ? 73  VAL A CA  1 
ATOM   512  C  C   . VAL A 1 73 ? 6.793   -12.196 2.512  1.00 21.31 ? 73  VAL A C   1 
ATOM   513  O  O   . VAL A 1 73 ? 6.873   -12.734 3.623  1.00 20.45 ? 73  VAL A O   1 
ATOM   514  C  CB  . VAL A 1 73 ? 8.909   -11.451 1.358  1.00 25.29 ? 73  VAL A CB  1 
ATOM   515  C  CG1 . VAL A 1 73 ? 9.581   -11.337 2.760  1.00 25.63 ? 73  VAL A CG1 1 
ATOM   516  C  CG2 . VAL A 1 73 ? 9.975   -11.826 0.263  1.00 24.21 ? 73  VAL A CG2 1 
ATOM   517  N  N   . ALA A 1 74 ? 5.818   -11.367 2.171  1.00 19.51 ? 74  ALA A N   1 
ATOM   518  C  CA  . ALA A 1 74 ? 4.722   -11.091 3.111  1.00 19.01 ? 74  ALA A CA  1 
ATOM   519  C  C   . ALA A 1 74 ? 3.977   -12.381 3.484  1.00 18.50 ? 74  ALA A C   1 
ATOM   520  O  O   . ALA A 1 74 ? 3.689   -12.573 4.650  1.00 20.95 ? 74  ALA A O   1 
ATOM   521  C  CB  . ALA A 1 74 ? 3.804   -10.081 2.521  1.00 19.17 ? 74  ALA A CB  1 
ATOM   522  N  N   . THR A 1 75 ? 3.770   -13.298 2.535  1.00 19.19 ? 75  THR A N   1 
ATOM   523  C  CA  . THR A 1 75 ? 3.101   -14.600 2.773  1.00 19.61 ? 75  THR A CA  1 
ATOM   524  C  C   . THR A 1 75 ? 3.861   -15.468 3.789  1.00 19.35 ? 75  THR A C   1 
ATOM   525  O  O   . THR A 1 75 ? 3.248   -16.010 4.739  1.00 18.60 ? 75  THR A O   1 
ATOM   526  C  CB  . THR A 1 75 ? 2.887   -15.381 1.485  1.00 19.79 ? 75  THR A CB  1 
ATOM   527  O  OG1 . THR A 1 75 ? 1.988   -14.651 0.686  1.00 23.07 ? 75  THR A OG1 1 
ATOM   528  C  CG2 . THR A 1 75 ? 2.194   -16.778 1.759  1.00 22.07 ? 75  THR A CG2 1 
ATOM   529  N  N   . LYS A 1 76 ? 5.175   -15.584 3.578  1.00 20.07 ? 76  LYS A N   1 
ATOM   530  C  CA  . LYS A 1 76 ? 6.019   -16.389 4.402  1.00 20.04 ? 76  LYS A CA  1 
ATOM   531  C  C   . LYS A 1 76 ? 5.944   -15.777 5.812  1.00 19.76 ? 76  LYS A C   1 
ATOM   532  O  O   . LYS A 1 76 ? 5.855   -16.492 6.811  1.00 18.83 ? 76  LYS A O   1 
ATOM   533  C  CB  . LYS A 1 76 ? 7.484   -16.362 3.866  1.00 20.28 ? 76  LYS A CB  1 
ATOM   534  C  CG  . LYS A 1 76 ? 8.461   -16.909 4.836  1.00 23.08 ? 76  LYS A CG  1 
ATOM   535  C  CD  . LYS A 1 76 ? 8.136   -18.374 5.097  1.00 28.54 ? 76  LYS A CD  1 
ATOM   536  C  CE  . LYS A 1 76 ? 9.144   -19.012 6.030  1.00 32.31 ? 76  LYS A CE  1 
ATOM   537  N  NZ  . LYS A 1 76 ? 8.811   -20.459 6.133  1.00 34.36 ? 76  LYS A NZ  1 
ATOM   538  N  N   . HIS A 1 77 ? 5.965   -14.455 5.914  1.00 18.93 ? 77  HIS A N   1 
ATOM   539  C  CA  . HIS A 1 77 ? 5.963   -13.898 7.280  1.00 18.59 ? 77  HIS A CA  1 
ATOM   540  C  C   . HIS A 1 77 ? 4.619   -14.162 7.924  1.00 17.16 ? 77  HIS A C   1 
ATOM   541  O  O   . HIS A 1 77 ? 4.544   -14.466 9.118  1.00 18.54 ? 77  HIS A O   1 
ATOM   542  C  CB  . HIS A 1 77 ? 6.268   -12.396 7.274  1.00 17.18 ? 77  HIS A CB  1 
ATOM   543  C  CG  . HIS A 1 77 ? 7.734   -12.081 7.390  1.00 19.87 ? 77  HIS A CG  1 
ATOM   544  N  ND1 . HIS A 1 77 ? 8.465   -12.289 8.553  1.00 22.62 ? 77  HIS A ND1 1 
ATOM   545  C  CD2 . HIS A 1 77 ? 8.605   -11.551 6.496  1.00 19.88 ? 77  HIS A CD2 1 
ATOM   546  C  CE1 . HIS A 1 77 ? 9.716   -11.916 8.353  1.00 23.58 ? 77  HIS A CE1 1 
ATOM   547  N  NE2 . HIS A 1 77 ? 9.817   -11.447 7.120  1.00 21.99 ? 77  HIS A NE2 1 
ATOM   548  N  N   . ALA A 1 78 ? 3.539   -14.065 7.141  1.00 16.61 ? 78  ALA A N   1 
ATOM   549  C  CA  . ALA A 1 78 ? 2.222   -14.417 7.663  1.00 16.47 ? 78  ALA A CA  1 
ATOM   550  C  C   . ALA A 1 78 ? 2.130   -15.905 8.036  1.00 18.77 ? 78  ALA A C   1 
ATOM   551  O  O   . ALA A 1 78 ? 1.546   -16.228 9.053  1.00 18.84 ? 78  ALA A O   1 
ATOM   552  C  CB  . ALA A 1 78 ? 1.120   -14.007 6.696  1.00 15.85 ? 78  ALA A CB  1 
ATOM   553  N  N   . GLN A 1 79 ? 2.697   -16.811 7.245  1.00 19.10 ? 79  GLN A N   1 
ATOM   554  C  CA  . GLN A 1 79 ? 2.777   -18.206 7.698  1.00 21.93 ? 79  GLN A CA  1 
ATOM   555  C  C   . GLN A 1 79 ? 3.520   -18.335 9.048  1.00 22.20 ? 79  GLN A C   1 
ATOM   556  O  O   . GLN A 1 79 ? 3.093   -19.074 9.923  1.00 21.91 ? 79  GLN A O   1 
ATOM   557  C  CB  . GLN A 1 79 ? 3.494   -19.049 6.636  1.00 23.20 ? 79  GLN A CB  1 
ATOM   558  C  CG  . GLN A 1 79 ? 2.665   -19.131 5.356  1.00 27.35 ? 79  GLN A CG  1 
ATOM   559  C  CD  . GLN A 1 79 ? 3.345   -19.914 4.218  1.00 30.48 ? 79  GLN A CD  1 
ATOM   560  O  OE1 . GLN A 1 79 ? 4.551   -19.760 3.962  1.00 30.60 ? 79  GLN A OE1 1 
ATOM   561  N  NE2 . GLN A 1 79 ? 2.559   -20.757 3.536  1.00 32.64 ? 79  GLN A NE2 1 
ATOM   562  N  N   . GLU A 1 80 ? 4.657   -17.642 9.196  1.00 22.03 ? 80  GLU A N   1 
ATOM   563  C  CA  . GLU A 1 80 ? 5.426   -17.665 10.455 1.00 22.89 ? 80  GLU A CA  1 
ATOM   564  C  C   . GLU A 1 80 ? 4.577   -17.125 11.601 1.00 20.64 ? 80  GLU A C   1 
ATOM   565  O  O   . GLU A 1 80 ? 4.582   -17.714 12.697 1.00 20.57 ? 80  GLU A O   1 
ATOM   566  C  CB  . GLU A 1 80 ? 6.718   -16.868 10.324 1.00 24.72 ? 80  GLU A CB  1 
ATOM   567  C  CG  . GLU A 1 80 ? 7.685   -17.509 9.358  1.00 28.04 ? 80  GLU A CG  1 
ATOM   568  C  CD  . GLU A 1 80 ? 8.065   -18.887 9.776  1.00 34.62 ? 80  GLU A CD  1 
ATOM   569  O  OE1 . GLU A 1 80 ? 8.004   -19.802 8.944  1.00 42.16 ? 80  GLU A OE1 1 
ATOM   570  O  OE2 . GLU A 1 80 ? 8.436   -19.085 10.939 1.00 38.57 ? 80  GLU A OE2 1 
ATOM   571  N  N   . ALA A 1 81 ? 3.814   -16.049 11.360 1.00 19.62 ? 81  ALA A N   1 
ATOM   572  C  CA  . ALA A 1 81 ? 2.925   -15.521 12.389 1.00 18.26 ? 81  ALA A CA  1 
ATOM   573  C  C   . ALA A 1 81 ? 1.901   -16.586 12.834 1.00 19.17 ? 81  ALA A C   1 
ATOM   574  O  O   . ALA A 1 81 ? 1.684   -16.772 14.017 1.00 20.53 ? 81  ALA A O   1 
ATOM   575  C  CB  . ALA A 1 81 ? 2.202   -14.268 11.872 1.00 16.39 ? 81  ALA A CB  1 
ATOM   576  N  N   . ILE A 1 82 ? 1.312   -17.324 11.900 1.00 19.25 ? 82  ILE A N   1 
ATOM   577  C  CA  . ILE A 1 82 ? 0.372   -18.372 12.261 1.00 20.43 ? 82  ILE A CA  1 
ATOM   578  C  C   . ILE A 1 82 ? 1.014   -19.403 13.141 1.00 23.41 ? 82  ILE A C   1 
ATOM   579  O  O   . ILE A 1 82 ? 0.398   -19.813 14.123 1.00 24.87 ? 82  ILE A O   1 
ATOM   580  C  CB  . ILE A 1 82 ? -0.186  -19.056 11.010 1.00 20.12 ? 82  ILE A CB  1 
ATOM   581  C  CG1 . ILE A 1 82 ? -1.018  -18.037 10.246 1.00 18.66 ? 82  ILE A CG1 1 
ATOM   582  C  CG2 . ILE A 1 82 ? -1.002  -20.389 11.360 1.00 23.84 ? 82  ILE A CG2 1 
ATOM   583  C  CD1 . ILE A 1 82 ? -1.326  -18.498 8.777  1.00 21.79 ? 82  ILE A CD1 1 
ATOM   584  N  N   . GLU A 1 83 ? 2.208   -19.872 12.778 1.00 24.54 ? 83  GLU A N   1 
ATOM   585  C  CA  . GLU A 1 83 ? 2.909   -20.874 13.598 1.00 28.91 ? 83  GLU A CA  1 
ATOM   586  C  C   . GLU A 1 83 ? 3.003   -20.431 15.066 1.00 29.19 ? 83  GLU A C   1 
ATOM   587  O  O   . GLU A 1 83 ? 2.737   -21.198 16.005 1.00 29.58 ? 83  GLU A O   1 
ATOM   588  C  CB  . GLU A 1 83 ? 4.311   -21.139 13.043 1.00 30.75 ? 83  GLU A CB  1 
ATOM   589  C  CG  . GLU A 1 83 ? 4.289   -22.045 11.845 1.00 38.57 ? 83  GLU A CG  1 
ATOM   590  C  CD  . GLU A 1 83 ? 5.633   -22.121 11.119 1.00 48.73 ? 83  GLU A CD  1 
ATOM   591  O  OE1 . GLU A 1 83 ? 6.697   -22.215 11.792 1.00 54.28 ? 83  GLU A OE1 1 
ATOM   592  O  OE2 . GLU A 1 83 ? 5.614   -22.098 9.865  1.00 51.96 ? 83  GLU A OE2 1 
ATOM   593  N  N   . HIS A 1 84 ? 3.394   -19.175 15.257 1.00 27.35 ? 84  HIS A N   1 
ATOM   594  C  CA  . HIS A 1 84 ? 3.565   -18.639 16.570 1.00 27.49 ? 84  HIS A CA  1 
ATOM   595  C  C   . HIS A 1 84 ? 2.226   -18.448 17.251 1.00 28.05 ? 84  HIS A C   1 
ATOM   596  O  O   . HIS A 1 84 ? 2.061   -18.831 18.413 1.00 30.10 ? 84  HIS A O   1 
ATOM   597  C  CB  . HIS A 1 84 ? 4.307   -17.303 16.491 1.00 25.79 ? 84  HIS A CB  1 
ATOM   598  C  CG  . HIS A 1 84 ? 5.792   -17.468 16.314 1.00 25.61 ? 84  HIS A CG  1 
ATOM   599  N  ND1 . HIS A 1 84 ? 6.629   -17.872 17.333 1.00 23.50 ? 84  HIS A ND1 1 
ATOM   600  C  CD2 . HIS A 1 84 ? 6.583   -17.288 15.228 1.00 25.40 ? 84  HIS A CD2 1 
ATOM   601  C  CE1 . HIS A 1 84 ? 7.873   -17.914 16.896 1.00 27.96 ? 84  HIS A CE1 1 
ATOM   602  N  NE2 . HIS A 1 84 ? 7.879   -17.529 15.628 1.00 24.11 ? 84  HIS A NE2 1 
ATOM   603  N  N   . LEU A 1 85 ? 1.267   -17.861 16.558 1.00 25.44 ? 85  LEU A N   1 
ATOM   604  C  CA  . LEU A 1 85 ? -0.031  -17.668 17.178 1.00 26.19 ? 85  LEU A CA  1 
ATOM   605  C  C   . LEU A 1 85 ? -0.639  -19.006 17.568 1.00 28.82 ? 85  LEU A C   1 
ATOM   606  O  O   . LEU A 1 85 ? -1.306  -19.083 18.585 1.00 29.29 ? 85  LEU A O   1 
ATOM   607  C  CB  . LEU A 1 85 ? -0.997  -16.914 16.254 1.00 23.50 ? 85  LEU A CB  1 
ATOM   608  C  CG  . LEU A 1 85 ? -0.607  -15.434 16.011 1.00 23.98 ? 85  LEU A CG  1 
ATOM   609  C  CD1 . LEU A 1 85 ? -1.239  -14.886 14.721 1.00 25.09 ? 85  LEU A CD1 1 
ATOM   610  C  CD2 . LEU A 1 85 ? -0.921  -14.536 17.229 1.00 22.82 ? 85  LEU A CD2 1 
ATOM   611  N  N   . ARG A 1 86 ? -0.435  -20.037 16.754 1.00 31.46 ? 86  ARG A N   1 
ATOM   612  C  CA  . ARG A 1 86 ? -0.981  -21.361 17.066 1.00 37.18 ? 86  ARG A CA  1 
ATOM   613  C  C   . ARG A 1 86 ? -0.269  -21.968 18.249 1.00 41.83 ? 86  ARG A C   1 
ATOM   614  O  O   . ARG A 1 86 ? -0.892  -22.665 19.052 1.00 45.42 ? 86  ARG A O   1 
ATOM   615  C  CB  . ARG A 1 86 ? -0.893  -22.330 15.878 1.00 37.65 ? 86  ARG A CB  1 
ATOM   616  C  CG  . ARG A 1 86 ? -1.942  -22.062 14.847 1.00 37.84 ? 86  ARG A CG  1 
ATOM   617  C  CD  . ARG A 1 86 ? -2.029  -23.157 13.774 1.00 43.39 ? 86  ARG A CD  1 
ATOM   618  N  NE  . ARG A 1 86 ? -3.207  -22.902 12.944 1.00 48.16 ? 86  ARG A NE  1 
ATOM   619  C  CZ  . ARG A 1 86 ? -4.454  -23.222 13.315 1.00 51.62 ? 86  ARG A CZ  1 
ATOM   620  N  NH1 . ARG A 1 86 ? -5.499  -22.939 12.530 1.00 47.87 ? 86  ARG A NH1 1 
ATOM   621  N  NH2 . ARG A 1 86 ? -4.658  -23.831 14.485 1.00 53.68 ? 86  ARG A NH2 1 
ATOM   622  N  N   . ALA A 1 87 ? 1.036   -21.735 18.353 1.00 43.71 ? 87  ALA A N   1 
ATOM   623  C  CA  . ALA A 1 87 ? 1.786   -22.090 19.552 1.00 47.66 ? 87  ALA A CA  1 
ATOM   624  C  C   . ALA A 1 87 ? 1.090   -21.556 20.819 1.00 48.58 ? 87  ALA A C   1 
ATOM   625  O  O   . ALA A 1 87 ? 1.040   -22.239 21.830 1.00 51.09 ? 87  ALA A O   1 
ATOM   626  C  CB  . ALA A 1 87 ? 3.248   -21.575 19.449 1.00 47.46 ? 87  ALA A CB  1 
ATOM   627  N  N   . SER A 1 88 ? 0.510   -20.359 20.739 1.00 48.24 ? 88  SER A N   1 
ATOM   628  C  CA  . SER A 1 88 ? -0.029  -19.636 21.913 1.00 48.95 ? 88  SER A CA  1 
ATOM   629  C  C   . SER A 1 88 ? -1.491  -19.945 22.247 1.00 49.79 ? 88  SER A C   1 
ATOM   630  O  O   . SER A 1 88 ? -1.764  -20.786 23.079 1.00 52.29 ? 88  SER A O   1 
ATOM   631  C  CB  . SER A 1 88 ? 0.171   -18.125 21.737 1.00 46.84 ? 88  SER A CB  1 
ATOM   632  O  OG  . SER A 1 88 ? -0.848  -17.373 22.386 1.00 47.17 ? 88  SER A OG  1 
ATOM   633  N  N   . SER B 1 1  ? -9.147  -7.857  24.547 1.00 20.29 ? 1   SER B N   1 
ATOM   634  C  CA  . SER B 1 1  ? -9.112  -6.780  25.620 1.00 21.08 ? 1   SER B CA  1 
ATOM   635  C  C   . SER B 1 1  ? -10.534 -6.733  26.060 1.00 22.93 ? 1   SER B C   1 
ATOM   636  O  O   . SER B 1 1  ? -11.386 -7.328  25.400 1.00 21.28 ? 1   SER B O   1 
ATOM   637  C  CB  . SER B 1 1  ? -8.824  -5.424  24.994 1.00 20.06 ? 1   SER B CB  1 
ATOM   638  O  OG  . SER B 1 1  ? -7.577  -5.495  24.382 1.00 21.55 ? 1   SER B OG  1 
ATOM   639  N  N   . GLY B 1 2  ? -10.807 -6.053  27.169 1.00 23.87 ? 2   GLY B N   1 
ATOM   640  C  CA  . GLY B 1 2  ? -12.151 -6.013  27.712 1.00 25.76 ? 2   GLY B CA  1 
ATOM   641  C  C   . GLY B 1 2  ? -13.001 -5.044  26.892 1.00 24.18 ? 2   GLY B C   1 
ATOM   642  O  O   . GLY B 1 2  ? -12.510 -4.260  26.062 1.00 21.52 ? 2   GLY B O   1 
ATOM   643  N  N   . HIS B 1 3  ? -14.283 -5.009  27.222 1.00 25.44 ? 3   HIS B N   1 
ATOM   644  C  CA  . HIS B 1 3  ? -15.228 -4.215  26.469 1.00 25.71 ? 3   HIS B CA  1 
ATOM   645  C  C   . HIS B 1 3  ? -14.849 -2.736  26.383 1.00 24.90 ? 3   HIS B C   1 
ATOM   646  O  O   . HIS B 1 3  ? -14.862 -2.149  25.293 1.00 23.74 ? 3   HIS B O   1 
ATOM   647  C  CB  . HIS B 1 3  ? -16.601 -4.358  27.108 1.00 28.12 ? 3   HIS B CB  1 
ATOM   648  C  CG  . HIS B 1 3  ? -17.646 -3.515  26.460 1.00 32.21 ? 3   HIS B CG  1 
ATOM   649  N  ND1 . HIS B 1 3  ? -18.305 -3.901  25.306 1.00 34.10 ? 3   HIS B ND1 1 
ATOM   650  C  CD2 . HIS B 1 3  ? -18.188 -2.321  26.831 1.00 36.18 ? 3   HIS B CD2 1 
ATOM   651  C  CE1 . HIS B 1 3  ? -19.168 -2.949  24.968 1.00 36.74 ? 3   HIS B CE1 1 
ATOM   652  N  NE2 . HIS B 1 3  ? -19.123 -1.990  25.879 1.00 35.82 ? 3   HIS B NE2 1 
ATOM   653  N  N   . THR B 1 4  ? -14.558 -2.132  27.538 1.00 26.39 ? 4   THR B N   1 
ATOM   654  C  CA  . THR B 1 4  ? -14.228 -0.718  27.602 1.00 25.57 ? 4   THR B CA  1 
ATOM   655  C  C   . THR B 1 4  ? -12.975 -0.406  26.807 1.00 23.51 ? 4   THR B C   1 
ATOM   656  O  O   . THR B 1 4  ? -12.949 0.648   26.129 1.00 21.85 ? 4   THR B O   1 
ATOM   657  C  CB  . THR B 1 4  ? -14.089 -0.260  29.004 1.00 27.90 ? 4   THR B CB  1 
ATOM   658  O  OG1 . THR B 1 4  ? -15.344 -0.478  29.638 1.00 30.81 ? 4   THR B OG1 1 
ATOM   659  C  CG2 . THR B 1 4  ? -13.738 1.283   29.091 1.00 29.65 ? 4   THR B CG2 1 
ATOM   660  N  N   . ALA B 1 5  ? -11.951 -1.286  26.883 1.00 22.69 ? 5   ALA B N   1 
ATOM   661  C  CA  . ALA B 1 5  ? -10.673 -1.048  26.196 1.00 21.69 ? 5   ALA B CA  1 
ATOM   662  C  C   . ALA B 1 5  ? -10.968 -1.001  24.728 1.00 20.52 ? 5   ALA B C   1 
ATOM   663  O  O   . ALA B 1 5  ? -10.497 -0.138  24.014 1.00 19.46 ? 5   ALA B O   1 
ATOM   664  C  CB  . ALA B 1 5  ? -9.640  -2.208  26.454 1.00 23.89 ? 5   ALA B CB  1 
ATOM   665  N  N   . HIS B 1 6  ? -11.761 -1.947  24.246 1.00 19.52 ? 6   HIS B N   1 
ATOM   666  C  CA  . HIS B 1 6  ? -12.122 -1.916  22.789 1.00 16.79 ? 6   HIS B CA  1 
ATOM   667  C  C   . HIS B 1 6  ? -12.960 -0.727  22.356 1.00 17.30 ? 6   HIS B C   1 
ATOM   668  O  O   . HIS B 1 6  ? -12.722 -0.183  21.290 1.00 16.76 ? 6   HIS B O   1 
ATOM   669  C  CB  . HIS B 1 6  ? -12.855 -3.186  22.381 1.00 17.14 ? 6   HIS B CB  1 
ATOM   670  C  CG  . HIS B 1 6  ? -11.988 -4.398  22.372 1.00 18.33 ? 6   HIS B CG  1 
ATOM   671  N  ND1 . HIS B 1 6  ? -10.914 -4.549  21.511 1.00 17.64 ? 6   HIS B ND1 1 
ATOM   672  C  CD2 . HIS B 1 6  ? -12.094 -5.555  23.060 1.00 18.49 ? 6   HIS B CD2 1 
ATOM   673  C  CE1 . HIS B 1 6  ? -10.373 -5.741  21.710 1.00 21.38 ? 6   HIS B CE1 1 
ATOM   674  N  NE2 . HIS B 1 6  ? -11.043 -6.342  22.679 1.00 17.02 ? 6   HIS B NE2 1 
ATOM   675  N  N   . VAL B 1 7  ? -13.915 -0.289  23.181 1.00 18.75 ? 7   VAL B N   1 
ATOM   676  C  CA  . VAL B 1 7  ? -14.676 0.870   22.799 1.00 20.01 ? 7   VAL B CA  1 
ATOM   677  C  C   . VAL B 1 7  ? -13.731 2.050   22.708 1.00 21.27 ? 7   VAL B C   1 
ATOM   678  O  O   . VAL B 1 7  ? -13.863 2.867   21.812 1.00 20.64 ? 7   VAL B O   1 
ATOM   679  C  CB  . VAL B 1 7  ? -15.841 1.152   23.757 1.00 21.84 ? 7   VAL B CB  1 
ATOM   680  C  CG1 . VAL B 1 7  ? -16.499 2.484   23.440 1.00 23.80 ? 7   VAL B CG1 1 
ATOM   681  C  CG2 . VAL B 1 7  ? -16.902 -0.018  23.635 1.00 22.26 ? 7   VAL B CG2 1 
ATOM   682  N  N   . ASP B 1 8  ? -12.835 2.175   23.689 1.00 20.66 ? 8   ASP B N   1 
ATOM   683  C  CA  . ASP B 1 8  ? -11.935 3.332   23.715 1.00 21.27 ? 8   ASP B CA  1 
ATOM   684  C  C   . ASP B 1 8  ? -11.013 3.335   22.504 1.00 19.72 ? 8   ASP B C   1 
ATOM   685  O  O   . ASP B 1 8  ? -10.708 4.379   21.919 1.00 18.20 ? 8   ASP B O   1 
ATOM   686  C  CB  . ASP B 1 8  ? -11.079 3.284   24.955 1.00 21.57 ? 8   ASP B CB  1 
ATOM   687  C  CG  . ASP B 1 8  ? -11.822 3.672   26.224 1.00 28.45 ? 8   ASP B CG  1 
ATOM   688  O  OD1 . ASP B 1 8  ? -12.923 4.280   26.152 1.00 29.73 ? 8   ASP B OD1 1 
ATOM   689  O  OD2 . ASP B 1 8  ? -11.240 3.363   27.289 1.00 30.47 ? 8   ASP B OD2 1 
ATOM   690  N  N   . GLU B 1 9  ? -10.487 2.158   22.154 1.00 18.33 ? 9   GLU B N   1 
ATOM   691  C  CA  . GLU B 1 9  ? -9.683  2.043   20.929 1.00 19.42 ? 9   GLU B CA  1 
ATOM   692  C  C   . GLU B 1 9  ? -10.499 2.336   19.672 1.00 17.47 ? 9   GLU B C   1 
ATOM   693  O  O   . GLU B 1 9  ? -9.988  2.968   18.751 1.00 17.77 ? 9   GLU B O   1 
ATOM   694  C  CB  . GLU B 1 9  ? -9.066  0.627   20.788 1.00 19.86 ? 9   GLU B CB  1 
ATOM   695  C  CG  . GLU B 1 9  ? -7.890  0.421   21.733 1.00 29.42 ? 9   GLU B CG  1 
ATOM   696  C  CD  . GLU B 1 9  ? -6.624  0.945   21.061 1.00 38.95 ? 9   GLU B CD  1 
ATOM   697  O  OE1 . GLU B 1 9  ? -6.062  0.191   20.253 1.00 45.65 ? 9   GLU B OE1 1 
ATOM   698  O  OE2 . GLU B 1 9  ? -6.236  2.118   21.270 1.00 41.84 ? 9   GLU B OE2 1 
ATOM   699  N  N   . ALA B 1 10 ? -11.726 1.802   19.591 1.00 16.19 ? 10  ALA B N   1 
ATOM   700  C  CA  . ALA B 1 10 ? -12.595 2.126   18.471 1.00 14.49 ? 10  ALA B CA  1 
ATOM   701  C  C   . ALA B 1 10 ? -12.764 3.656   18.323 1.00 15.73 ? 10  ALA B C   1 
ATOM   702  O  O   . ALA B 1 10 ? -12.715 4.207   17.216 1.00 15.50 ? 10  ALA B O   1 
ATOM   703  C  CB  . ALA B 1 10 ? -13.965 1.418   18.649 1.00 15.19 ? 10  ALA B CB  1 
ATOM   704  N  N   . VAL B 1 11 ? -13.018 4.346   19.417 1.00 15.70 ? 11  VAL B N   1 
ATOM   705  C  CA  . VAL B 1 11 ? -13.227 5.783   19.343 1.00 17.45 ? 11  VAL B CA  1 
ATOM   706  C  C   . VAL B 1 11 ? -11.959 6.473   18.867 1.00 18.22 ? 11  VAL B C   1 
ATOM   707  O  O   . VAL B 1 11 ? -12.004 7.348   17.997 1.00 18.49 ? 11  VAL B O   1 
ATOM   708  C  CB  . VAL B 1 11 ? -13.645 6.331   20.760 1.00 16.96 ? 11  VAL B CB  1 
ATOM   709  C  CG1 . VAL B 1 11 ? -13.539 7.860   20.813 1.00 19.90 ? 11  VAL B CG1 1 
ATOM   710  C  CG2 . VAL B 1 11 ? -15.064 5.880   21.055 1.00 17.53 ? 11  VAL B CG2 1 
ATOM   711  N  N   . LYS B 1 12 ? -10.815 6.075   19.430 1.00 19.97 ? 12  LYS B N   1 
ATOM   712  C  CA  . LYS B 1 12 ? -9.538  6.678   19.070 1.00 22.44 ? 12  LYS B CA  1 
ATOM   713  C  C   . LYS B 1 12 ? -9.287  6.515   17.540 1.00 22.01 ? 12  LYS B C   1 
ATOM   714  O  O   . LYS B 1 12 ? -8.854  7.447   16.872 1.00 20.94 ? 12  LYS B O   1 
ATOM   715  C  CB  . LYS B 1 12 ? -8.439  5.956   19.824 1.00 23.36 ? 12  LYS B CB  1 
ATOM   716  C  CG  . LYS B 1 12 ? -7.027  6.309   19.403 1.00 29.98 ? 12  LYS B CG  1 
ATOM   717  C  CD  . LYS B 1 12 ? -5.998  5.344   20.076 1.00 32.26 ? 12  LYS B CD  1 
ATOM   718  C  CE  . LYS B 1 12 ? -5.681  4.176   19.199 1.00 34.32 ? 12  LYS B CE  1 
ATOM   719  N  NZ  . LYS B 1 12 ? -4.302  3.720   19.490 1.00 41.32 ? 12  LYS B NZ  1 
ATOM   720  N  N   . HIS B 1 13 ? -9.483  5.309   17.035 1.00 18.98 ? 13  HIS B N   1 
ATOM   721  C  CA  . HIS B 1 13 ? -9.234  5.098   15.626 1.00 19.41 ? 13  HIS B CA  1 
ATOM   722  C  C   . HIS B 1 13 ? -10.247 5.882   14.818 1.00 19.75 ? 13  HIS B C   1 
ATOM   723  O  O   . HIS B 1 13 ? -9.877  6.477   13.820 1.00 21.80 ? 13  HIS B O   1 
ATOM   724  C  CB  . HIS B 1 13 ? -9.247  3.638   15.279 1.00 19.00 ? 13  HIS B CB  1 
ATOM   725  C  CG  . HIS B 1 13 ? -8.011  2.948   15.738 1.00 21.35 ? 13  HIS B CG  1 
ATOM   726  N  ND1 . HIS B 1 13 ? -6.772  3.228   15.201 1.00 24.54 ? 13  HIS B ND1 1 
ATOM   727  C  CD2 . HIS B 1 13 ? -7.802  2.058   16.731 1.00 21.32 ? 13  HIS B CD2 1 
ATOM   728  C  CE1 . HIS B 1 13 ? -5.854  2.521   15.832 1.00 27.72 ? 13  HIS B CE1 1 
ATOM   729  N  NE2 . HIS B 1 13 ? -6.458  1.773   16.738 1.00 23.92 ? 13  HIS B NE2 1 
ATOM   730  N  N   . ALA B 1 14 ? -11.519 5.906   15.253 1.00 17.44 ? 14  ALA B N   1 
ATOM   731  C  CA  . ALA B 1 14 ? -12.549 6.596   14.486 1.00 16.77 ? 14  ALA B CA  1 
ATOM   732  C  C   . ALA B 1 14 ? -12.210 8.087   14.519 1.00 17.10 ? 14  ALA B C   1 
ATOM   733  O  O   . ALA B 1 14 ? -12.372 8.760   13.546 1.00 19.25 ? 14  ALA B O   1 
ATOM   734  C  CB  . ALA B 1 14 ? -13.924 6.339   15.051 1.00 13.89 ? 14  ALA B CB  1 
ATOM   735  N  N   . GLU B 1 15 ? -11.701 8.570   15.640 1.00 17.37 ? 15  GLU B N   1 
ATOM   736  C  CA  . GLU B 1 15 ? -11.246 9.987   15.718 1.00 19.87 ? 15  GLU B CA  1 
ATOM   737  C  C   . GLU B 1 15 ? -10.131 10.304  14.710 1.00 20.43 ? 15  GLU B C   1 
ATOM   738  O  O   . GLU B 1 15 ? -10.096 11.400  14.082 1.00 21.00 ? 15  GLU B O   1 
ATOM   739  C  CB  . GLU B 1 15 ? -10.793 10.325  17.122 1.00 18.76 ? 15  GLU B CB  1 
ATOM   740  C  CG  . GLU B 1 15 ? -11.936 10.482  18.052 1.00 22.83 ? 15  GLU B CG  1 
ATOM   741  C  CD  . GLU B 1 15 ? -11.475 10.770  19.487 1.00 32.27 ? 15  GLU B CD  1 
ATOM   742  O  OE1 . GLU B 1 15 ? -10.437 10.211  19.937 1.00 34.61 ? 15  GLU B OE1 1 
ATOM   743  O  OE2 . GLU B 1 15 ? -12.181 11.521  20.184 1.00 37.05 ? 15  GLU B OE2 1 
ATOM   744  N  N   . GLU B 1 16 ? -9.186  9.376   14.585 1.00 20.78 ? 16  GLU B N   1 
ATOM   745  C  CA  . GLU B 1 16 ? -8.117  9.548   13.600 1.00 22.15 ? 16  GLU B CA  1 
ATOM   746  C  C   . GLU B 1 16 ? -8.676  9.478   12.224 1.00 22.37 ? 16  GLU B C   1 
ATOM   747  O  O   . GLU B 1 16 ? -8.323  10.262  11.353 1.00 23.35 ? 16  GLU B O   1 
ATOM   748  C  CB  . GLU B 1 16 ? -7.034  8.499   13.762 1.00 23.96 ? 16  GLU B CB  1 
ATOM   749  C  CG  . GLU B 1 16 ? -6.223  8.732   14.969 1.00 29.65 ? 16  GLU B CG  1 
ATOM   750  C  CD  . GLU B 1 16 ? -5.419  10.012  14.885 1.00 41.50 ? 16  GLU B CD  1 
ATOM   751  O  OE1 . GLU B 1 16 ? -4.436  10.061  14.110 1.00 49.30 ? 16  GLU B OE1 1 
ATOM   752  O  OE2 . GLU B 1 16 ? -5.751  10.986  15.586 1.00 44.50 ? 16  GLU B OE2 1 
ATOM   753  N  N   . ALA B 1 17 ? -9.607  8.564   12.018 1.00 20.04 ? 17  ALA B N   1 
ATOM   754  C  CA  . ALA B 1 17 ? -10.226 8.463   10.695 1.00 19.54 ? 17  ALA B CA  1 
ATOM   755  C  C   . ALA B 1 17 ? -10.913 9.778   10.305 1.00 21.46 ? 17  ALA B C   1 
ATOM   756  O  O   . ALA B 1 17 ? -10.787 10.214  9.170  1.00 23.09 ? 17  ALA B O   1 
ATOM   757  C  CB  . ALA B 1 17 ? -11.214 7.273   10.663 1.00 19.20 ? 17  ALA B CB  1 
ATOM   758  N  N   . VAL B 1 18 ? -11.616 10.411  11.229 1.00 19.67 ? 18  VAL B N   1 
ATOM   759  C  CA  . VAL B 1 18 ? -12.313 11.658  10.952 1.00 21.81 ? 18  VAL B CA  1 
ATOM   760  C  C   . VAL B 1 18 ? -11.318 12.745  10.695 1.00 24.77 ? 18  VAL B C   1 
ATOM   761  O  O   . VAL B 1 18 ? -11.448 13.508  9.721  1.00 27.94 ? 18  VAL B O   1 
ATOM   762  C  CB  . VAL B 1 18 ? -13.256 12.068  12.138 1.00 21.51 ? 18  VAL B CB  1 
ATOM   763  C  CG1 . VAL B 1 18 ? -13.731 13.560  12.053 1.00 22.15 ? 18  VAL B CG1 1 
ATOM   764  C  CG2 . VAL B 1 18 ? -14.438 11.083  12.210 1.00 19.31 ? 18  VAL B CG2 1 
ATOM   765  N  N   . ALA B 1 19 ? -10.313 12.845  11.552 1.00 24.93 ? 19  ALA B N   1 
ATOM   766  C  CA  . ALA B 1 19 ? -9.306  13.857  11.346 1.00 27.56 ? 19  ALA B CA  1 
ATOM   767  C  C   . ALA B 1 19 ? -8.730  13.726  9.945  1.00 28.86 ? 19  ALA B C   1 
ATOM   768  O  O   . ALA B 1 19 ? -8.595  14.698  9.277  1.00 30.87 ? 19  ALA B O   1 
ATOM   769  C  CB  . ALA B 1 19 ? -8.195  13.753  12.399 1.00 28.19 ? 19  ALA B CB  1 
ATOM   770  N  N   . HIS B 1 20 ? -8.399  12.509  9.514  1.00 27.34 ? 20  HIS B N   1 
ATOM   771  C  CA  . HIS B 1 20 ? -7.844  12.281  8.182  1.00 29.92 ? 20  HIS B CA  1 
ATOM   772  C  C   . HIS B 1 20 ? -8.878  12.570  7.111  1.00 30.33 ? 20  HIS B C   1 
ATOM   773  O  O   . HIS B 1 20 ? -8.564  13.215  6.118  1.00 34.88 ? 20  HIS B O   1 
ATOM   774  C  CB  . HIS B 1 20 ? -7.340  10.817  8.047  1.00 29.86 ? 20  HIS B CB  1 
ATOM   775  C  CG  . HIS B 1 20 ? -6.003  10.592  8.674  1.00 31.84 ? 20  HIS B CG  1 
ATOM   776  N  ND1 . HIS B 1 20 ? -4.847  11.172  8.185  1.00 37.76 ? 20  HIS B ND1 1 
ATOM   777  C  CD2 . HIS B 1 20 ? -5.637  9.875   9.760  1.00 30.41 ? 20  HIS B CD2 1 
ATOM   778  C  CE1 . HIS B 1 20 ? -3.829  10.822  8.947  1.00 39.20 ? 20  HIS B CE1 1 
ATOM   779  N  NE2 . HIS B 1 20 ? -4.283  10.035  9.908  1.00 33.83 ? 20  HIS B NE2 1 
ATOM   780  N  N   . GLY B 1 21 ? -10.109 12.125  7.288  1.00 28.17 ? 21  GLY B N   1 
ATOM   781  C  CA  . GLY B 1 21 ? -11.162 12.424  6.289  1.00 31.07 ? 21  GLY B CA  1 
ATOM   782  C  C   . GLY B 1 21 ? -11.450 13.911  6.033  1.00 34.63 ? 21  GLY B C   1 
ATOM   783  O  O   . GLY B 1 21 ? -11.721 14.310  4.897  1.00 36.59 ? 21  GLY B O   1 
ATOM   784  N  N   . LYS B 1 22 ? -11.370 14.725  7.089  1.00 35.32 ? 22  LYS B N   1 
ATOM   785  C  CA  . LYS B 1 22 ? -11.564 16.186  7.023  1.00 39.15 ? 22  LYS B CA  1 
ATOM   786  C  C   . LYS B 1 22 ? -10.479 16.801  6.139  1.00 42.28 ? 22  LYS B C   1 
ATOM   787  O  O   . LYS B 1 22 ? -10.694 17.861  5.552  1.00 45.19 ? 22  LYS B O   1 
ATOM   788  C  CB  . LYS B 1 22 ? -11.617 16.847  8.425  1.00 37.38 ? 22  LYS B CB  1 
ATOM   789  C  CG  . LYS B 1 22 ? -12.789 16.316  9.309  1.00 36.92 ? 22  LYS B CG  1 
ATOM   790  C  CD  . LYS B 1 22 ? -13.309 17.172  10.515 1.00 39.32 ? 22  LYS B CD  1 
ATOM   791  C  CE  . LYS B 1 22 ? -12.327 17.424  11.712 1.00 47.71 ? 22  LYS B CE  1 
ATOM   792  N  NZ  . LYS B 1 22 ? -12.307 16.498  12.955 1.00 46.22 ? 22  LYS B NZ  1 
ATOM   793  N  N   . GLU B 1 23 ? -9.341  16.106  6.027  1.00 42.70 ? 23  GLU B N   1 
ATOM   794  C  CA  . GLU B 1 23 ? -8.195  16.574  5.229  1.00 45.86 ? 23  GLU B CA  1 
ATOM   795  C  C   . GLU B 1 23 ? -8.184  15.885  3.867  1.00 46.47 ? 23  GLU B C   1 
ATOM   796  O  O   . GLU B 1 23 ? -7.314  16.122  3.047  1.00 49.71 ? 23  GLU B O   1 
ATOM   797  C  CB  . GLU B 1 23 ? -6.866  16.309  5.950  1.00 46.66 ? 23  GLU B CB  1 
ATOM   798  C  CG  . GLU B 1 23 ? -6.667  17.014  7.270  1.00 49.56 ? 23  GLU B CG  1 
ATOM   799  C  CD  . GLU B 1 23 ? -6.389  18.493  7.102  1.00 60.79 ? 23  GLU B CD  1 
ATOM   800  O  OE1 . GLU B 1 23 ? -5.190  18.878  7.097  1.00 66.31 ? 23  GLU B OE1 1 
ATOM   801  O  OE2 . GLU B 1 23 ? -7.359  19.283  6.954  1.00 64.28 ? 23  GLU B OE2 1 
ATOM   802  N  N   . GLY B 1 24 ? -9.162  15.029  3.625  1.00 43.94 ? 24  GLY B N   1 
ATOM   803  C  CA  . GLY B 1 24 ? -9.284  14.386  2.345  1.00 44.46 ? 24  GLY B CA  1 
ATOM   804  C  C   . GLY B 1 24 ? -8.376  13.184  2.202  1.00 44.80 ? 24  GLY B C   1 
ATOM   805  O  O   . GLY B 1 24 ? -8.160  12.735  1.098  1.00 46.06 ? 24  GLY B O   1 
ATOM   806  N  N   . HIS B 1 25 ? -7.847  12.641  3.307  1.00 41.62 ? 25  HIS B N   1 
ATOM   807  C  CA  . HIS B 1 25 ? -6.960  11.478  3.204  1.00 42.21 ? 25  HIS B CA  1 
ATOM   808  C  C   . HIS B 1 25 ? -7.789  10.207  3.259  1.00 40.07 ? 25  HIS B C   1 
ATOM   809  O  O   . HIS B 1 25 ? -7.828  9.511   4.298  1.00 37.51 ? 25  HIS B O   1 
ATOM   810  C  CB  . HIS B 1 25 ? -5.898  11.425  4.322  1.00 41.13 ? 25  HIS B CB  1 
ATOM   811  C  CG  . HIS B 1 25 ? -5.099  12.680  4.465  1.00 46.37 ? 25  HIS B CG  1 
ATOM   812  N  ND1 . HIS B 1 25 ? -4.688  13.165  5.689  1.00 46.96 ? 25  HIS B ND1 1 
ATOM   813  C  CD2 . HIS B 1 25 ? -4.696  13.585  3.545  1.00 48.78 ? 25  HIS B CD2 1 
ATOM   814  C  CE1 . HIS B 1 25 ? -4.035  14.300  5.507  1.00 52.07 ? 25  HIS B CE1 1 
ATOM   815  N  NE2 . HIS B 1 25 ? -4.024  14.575  4.217  1.00 51.98 ? 25  HIS B NE2 1 
ATOM   816  N  N   . THR B 1 26 ? -8.421  9.893   2.134  1.00 40.75 ? 26  THR B N   1 
ATOM   817  C  CA  . THR B 1 26 ? -9.274  8.726   2.017  1.00 39.19 ? 26  THR B CA  1 
ATOM   818  C  C   . THR B 1 26 ? -8.602  7.421   2.537  1.00 37.95 ? 26  THR B C   1 
ATOM   819  O  O   . THR B 1 26 ? -9.217  6.685   3.346  1.00 34.39 ? 26  THR B O   1 
ATOM   820  C  CB  . THR B 1 26 ? -9.780  8.588   0.574  1.00 42.22 ? 26  THR B CB  1 
ATOM   821  O  OG1 . THR B 1 26 ? -10.389 9.834   0.171  1.00 45.43 ? 26  THR B OG1 1 
ATOM   822  C  CG2 . THR B 1 26 ? -10.802 7.490   0.470  1.00 40.77 ? 26  THR B CG2 1 
ATOM   823  N  N   . ASP B 1 27 ? -7.368  7.161   2.102  1.00 40.15 ? 27  ASP B N   1 
ATOM   824  C  CA  . ASP B 1 27 ? -6.689  5.910   2.458  1.00 41.00 ? 27  ASP B CA  1 
ATOM   825  C  C   . ASP B 1 27 ? -6.448  5.800   3.980  1.00 37.74 ? 27  ASP B C   1 
ATOM   826  O  O   . ASP B 1 27 ? -6.621  4.705   4.560  1.00 36.15 ? 27  ASP B O   1 
ATOM   827  C  CB  . ASP B 1 27 ? -5.389  5.712   1.652  1.00 44.84 ? 27  ASP B CB  1 
ATOM   828  C  CG  . ASP B 1 27 ? -5.652  5.219   0.190  1.00 52.49 ? 27  ASP B CG  1 
ATOM   829  O  OD1 . ASP B 1 27 ? -6.794  4.789   -0.139 1.00 55.39 ? 27  ASP B OD1 1 
ATOM   830  O  OD2 . ASP B 1 27 ? -4.709  5.240   -0.645 1.00 57.94 ? 27  ASP B OD2 1 
ATOM   831  N  N   . GLN B 1 28 ? -6.065  6.911   4.628  1.00 36.50 ? 28  GLN B N   1 
ATOM   832  C  CA  . GLN B 1 28 ? -5.864  6.901   6.087  1.00 34.64 ? 28  GLN B CA  1 
ATOM   833  C  C   . GLN B 1 28 ? -7.200  6.868   6.795  1.00 30.51 ? 28  GLN B C   1 
ATOM   834  O  O   . GLN B 1 28 ? -7.349  6.238   7.847  1.00 29.36 ? 28  GLN B O   1 
ATOM   835  C  CB  . GLN B 1 28 ? -5.061  8.119   6.576  1.00 36.23 ? 28  GLN B CB  1 
ATOM   836  C  CG  . GLN B 1 28 ? -3.567  8.127   6.256  1.00 45.46 ? 28  GLN B CG  1 
ATOM   837  C  CD  . GLN B 1 28 ? -2.867  6.891   6.754  1.00 52.26 ? 28  GLN B CD  1 
ATOM   838  O  OE1 . GLN B 1 28 ? -2.250  6.163   5.949  1.00 57.75 ? 28  GLN B OE1 1 
ATOM   839  N  NE2 . GLN B 1 28 ? -2.955  6.621   8.076  1.00 48.96 ? 28  GLN B NE2 1 
ATOM   840  N  N   . LEU B 1 29 ? -8.198  7.551   6.256  1.00 28.45 ? 29  LEU B N   1 
ATOM   841  C  CA  . LEU B 1 29 ? -9.510  7.374   6.818  1.00 25.96 ? 29  LEU B CA  1 
ATOM   842  C  C   . LEU B 1 29 ? -9.898  5.871   6.814  1.00 24.13 ? 29  LEU B C   1 
ATOM   843  O  O   . LEU B 1 29 ? -10.317 5.350   7.829  1.00 20.34 ? 29  LEU B O   1 
ATOM   844  C  CB  . LEU B 1 29 ? -10.560 8.268   6.163  1.00 26.93 ? 29  LEU B CB  1 
ATOM   845  C  CG  . LEU B 1 29 ? -11.986 7.841   6.553  1.00 27.47 ? 29  LEU B CG  1 
ATOM   846  C  CD1 . LEU B 1 29 ? -12.804 9.059   6.566  1.00 25.27 ? 29  LEU B CD1 1 
ATOM   847  C  CD2 . LEU B 1 29 ? -12.600 6.794   5.574  1.00 30.15 ? 29  LEU B CD2 1 
ATOM   848  N  N   . LEU B 1 30 ? -9.726  5.195   5.682  1.00 25.84 ? 30  LEU B N   1 
ATOM   849  C  CA  . LEU B 1 30 ? -10.055 3.788   5.553  1.00 25.14 ? 30  LEU B CA  1 
ATOM   850  C  C   . LEU B 1 30 ? -9.234  2.905   6.498  1.00 24.46 ? 30  LEU B C   1 
ATOM   851  O  O   . LEU B 1 30 ? -9.793  2.038   7.164  1.00 23.88 ? 30  LEU B O   1 
ATOM   852  C  CB  . LEU B 1 30 ? -9.843  3.327   4.111  1.00 29.40 ? 30  LEU B CB  1 
ATOM   853  C  CG  . LEU B 1 30 ? -10.932 3.744   3.117  1.00 30.44 ? 30  LEU B CG  1 
ATOM   854  C  CD1 . LEU B 1 30 ? -10.440 3.511   1.636  1.00 31.86 ? 30  LEU B CD1 1 
ATOM   855  C  CD2 . LEU B 1 30 ? -12.184 2.949   3.435  1.00 27.55 ? 30  LEU B CD2 1 
ATOM   856  N  N   . GLU B 1 31 ? -7.931  3.114   6.570  1.00 24.77 ? 31  GLU B N   1 
ATOM   857  C  CA  . GLU B 1 31 ? -7.093  2.291   7.482  1.00 26.76 ? 31  GLU B CA  1 
ATOM   858  C  C   . GLU B 1 31 ? -7.586  2.404   8.922  1.00 23.84 ? 31  GLU B C   1 
ATOM   859  O  O   . GLU B 1 31 ? -7.749  1.424   9.622  1.00 21.63 ? 31  GLU B O   1 
ATOM   860  C  CB  . GLU B 1 31 ? -5.651  2.760   7.405  1.00 29.66 ? 31  GLU B CB  1 
ATOM   861  C  CG  . GLU B 1 31 ? -4.658  1.668   7.807  1.00 38.70 ? 31  GLU B CG  1 
ATOM   862  C  CD  . GLU B 1 31 ? -3.335  1.790   7.105  1.00 47.81 ? 31  GLU B CD  1 
ATOM   863  O  OE1 . GLU B 1 31 ? -2.995  2.948   6.704  1.00 54.46 ? 31  GLU B OE1 1 
ATOM   864  O  OE2 . GLU B 1 31 ? -2.642  0.746   6.957  1.00 49.19 ? 31  GLU B OE2 1 
ATOM   865  N  N   . HIS B 1 32 ? -7.894  3.623   9.353  1.00 22.58 ? 32  HIS B N   1 
ATOM   866  C  CA  . HIS B 1 32 ? -8.331  3.824   10.727 1.00 23.01 ? 32  HIS B CA  1 
ATOM   867  C  C   . HIS B 1 32 ? -9.731  3.370   10.972 1.00 20.83 ? 32  HIS B C   1 
ATOM   868  O  O   . HIS B 1 32 ? -10.020 2.816   12.008 1.00 20.64 ? 32  HIS B O   1 
ATOM   869  C  CB  . HIS B 1 32 ? -8.163  5.308   11.093 1.00 24.28 ? 32  HIS B CB  1 
ATOM   870  C  CG  . HIS B 1 32 ? -6.742  5.656   11.401 1.00 26.69 ? 32  HIS B CG  1 
ATOM   871  N  ND1 . HIS B 1 32 ? -6.094  5.195   12.529 1.00 29.52 ? 32  HIS B ND1 1 
ATOM   872  C  CD2 . HIS B 1 32 ? -5.831  6.373   10.709 1.00 30.41 ? 32  HIS B CD2 1 
ATOM   873  C  CE1 . HIS B 1 32 ? -4.842  5.622   12.521 1.00 32.18 ? 32  HIS B CE1 1 
ATOM   874  N  NE2 . HIS B 1 32 ? -4.665  6.354   11.433 1.00 32.20 ? 32  HIS B NE2 1 
ATOM   875  N  N   . ALA B 1 33 ? -10.619 3.582   10.028 1.00 21.00 ? 33  ALA B N   1 
ATOM   876  C  CA  . ALA B 1 33 ? -12.005 3.114   10.225 1.00 19.73 ? 33  ALA B CA  1 
ATOM   877  C  C   . ALA B 1 33 ? -12.009 1.602   10.299 1.00 20.95 ? 33  ALA B C   1 
ATOM   878  O  O   . ALA B 1 33 ? -12.825 1.043   11.014 1.00 19.77 ? 33  ALA B O   1 
ATOM   879  C  CB  . ALA B 1 33 ? -12.909 3.570   9.087  1.00 19.90 ? 33  ALA B CB  1 
ATOM   880  N  N   . LYS B 1 34 ? -11.149 0.946   9.502  1.00 19.52 ? 34  LYS B N   1 
ATOM   881  C  CA  . LYS B 1 34 ? -11.071 -0.549  9.558  1.00 21.06 ? 34  LYS B CA  1 
ATOM   882  C  C   . LYS B 1 34 ? -10.621 -1.028  10.954 1.00 20.59 ? 34  LYS B C   1 
ATOM   883  O  O   . LYS B 1 34 ? -11.166 -1.981  11.511 1.00 20.73 ? 34  LYS B O   1 
ATOM   884  C  CB  . LYS B 1 34 ? -10.134 -1.043  8.472  1.00 21.68 ? 34  LYS B CB  1 
ATOM   885  C  CG  . LYS B 1 34 ? -10.844 -1.010  7.128  1.00 24.27 ? 34  LYS B CG  1 
ATOM   886  C  CD  . LYS B 1 34 ? -9.950  -1.248  5.906  1.00 27.90 ? 34  LYS B CD  1 
ATOM   887  C  CE  . LYS B 1 34 ? -10.743 -1.019  4.625  1.00 32.65 ? 34  LYS B CE  1 
ATOM   888  N  NZ  . LYS B 1 34 ? -9.839  -1.286  3.423  1.00 37.70 ? 34  LYS B NZ  1 
ATOM   889  N  N   . GLU B 1 35 ? -9.638  -0.333  11.516 1.00 20.15 ? 35  GLU B N   1 
ATOM   890  C  CA  . GLU B 1 35 ? -9.140  -0.658  12.867 1.00 20.25 ? 35  GLU B CA  1 
ATOM   891  C  C   . GLU B 1 35 ? -10.200 -0.390  13.892 1.00 18.82 ? 35  GLU B C   1 
ATOM   892  O  O   . GLU B 1 35 ? -10.393 -1.197  14.815 1.00 17.56 ? 35  GLU B O   1 
ATOM   893  C  CB  . GLU B 1 35 ? -7.892  0.156   13.216 1.00 20.10 ? 35  GLU B CB  1 
ATOM   894  C  CG  A GLU B 1 35 ? -6.797  0.040   12.175 0.50 22.55 ? 35  GLU B CG  1 
ATOM   895  C  CG  B GLU B 1 35 ? -6.580  -0.631  13.191 0.50 26.07 ? 35  GLU B CG  1 
ATOM   896  C  CD  A GLU B 1 35 ? -5.532  0.731   12.623 0.50 23.87 ? 35  GLU B CD  1 
ATOM   897  C  CD  B GLU B 1 35 ? -6.267  -1.219  14.536 0.50 29.91 ? 35  GLU B CD  1 
ATOM   898  O  OE1 A GLU B 1 35 ? -5.189  1.805   12.039 0.50 28.85 ? 35  GLU B OE1 1 
ATOM   899  O  OE1 B GLU B 1 35 ? -5.120  -1.673  14.801 0.50 25.56 ? 35  GLU B OE1 1 
ATOM   900  O  OE2 A GLU B 1 35 ? -4.925  0.226   13.585 0.50 15.54 ? 35  GLU B OE2 1 
ATOM   901  O  OE2 B GLU B 1 35 ? -7.203  -1.205  15.366 0.50 35.65 ? 35  GLU B OE2 1 
ATOM   902  N  N   . SER B 1 36 ? -10.864 0.770   13.760 1.00 16.58 ? 36  SER B N   1 
ATOM   903  C  CA  . SER B 1 36 ? -11.927 1.092   14.653 1.00 15.78 ? 36  SER B CA  1 
ATOM   904  C  C   . SER B 1 36 ? -12.986 -0.003  14.638 1.00 16.57 ? 36  SER B C   1 
ATOM   905  O  O   . SER B 1 36 ? -13.476 -0.389  15.668 1.00 15.99 ? 36  SER B O   1 
ATOM   906  C  CB  . SER B 1 36 ? -12.597 2.390   14.214 1.00 16.28 ? 36  SER B CB  1 
ATOM   907  O  OG  . SER B 1 36 ? -13.582 2.705   15.155 1.00 17.05 ? 36  SER B OG  1 
ATOM   908  N  N   . LEU B 1 37 ? -13.356 -0.449  13.441 1.00 15.02 ? 37  LEU B N   1 
ATOM   909  C  CA  . LEU B 1 37 ? -14.414 -1.427  13.276 1.00 17.08 ? 37  LEU B CA  1 
ATOM   910  C  C   . LEU B 1 37 ? -14.041 -2.758  13.962 1.00 17.29 ? 37  LEU B C   1 
ATOM   911  O  O   . LEU B 1 37 ? -14.904 -3.456  14.563 1.00 18.09 ? 37  LEU B O   1 
ATOM   912  C  CB  . LEU B 1 37 ? -14.617 -1.640  11.761 1.00 17.14 ? 37  LEU B CB  1 
ATOM   913  C  CG  . LEU B 1 37 ? -15.634 -2.749  11.338 1.00 20.88 ? 37  LEU B CG  1 
ATOM   914  C  CD1 . LEU B 1 37 ? -16.993 -2.443  12.000 1.00 21.44 ? 37  LEU B CD1 1 
ATOM   915  C  CD2 . LEU B 1 37 ? -15.803 -2.892  9.818  1.00 23.66 ? 37  LEU B CD2 1 
ATOM   916  N  N   . THR B 1 38 ? -12.776 -3.145  13.812 1.00 17.18 ? 38  THR B N   1 
ATOM   917  C  CA  . THR B 1 38 ? -12.280 -4.386  14.480 1.00 17.45 ? 38  THR B CA  1 
ATOM   918  C  C   . THR B 1 38 ? -12.552 -4.334  15.985 1.00 16.95 ? 38  THR B C   1 
ATOM   919  O  O   . THR B 1 38 ? -13.070 -5.301  16.579 1.00 15.18 ? 38  THR B O   1 
ATOM   920  C  CB  . THR B 1 38 ? -10.803 -4.572  14.206 1.00 18.37 ? 38  THR B CB  1 
ATOM   921  O  OG1 . THR B 1 38 ? -10.622 -4.688  12.766 1.00 18.52 ? 38  THR B OG1 1 
ATOM   922  C  CG2 . THR B 1 38 ? -10.300 -5.868  14.863 1.00 17.89 ? 38  THR B CG2 1 
ATOM   923  N  N   . HIS B 1 39 ? -12.164 -3.205  16.590 1.00 15.30 ? 39  HIS B N   1 
ATOM   924  C  CA  . HIS B 1 39 ? -12.371 -2.969  18.002 1.00 15.43 ? 39  HIS B CA  1 
ATOM   925  C  C   . HIS B 1 39 ? -13.852 -2.850  18.338 1.00 16.45 ? 39  HIS B C   1 
ATOM   926  O  O   . HIS B 1 39 ? -14.297 -3.368  19.394 1.00 16.92 ? 39  HIS B O   1 
ATOM   927  C  CB  . HIS B 1 39 ? -11.600 -1.682  18.388 1.00 13.31 ? 39  HIS B CB  1 
ATOM   928  C  CG  . HIS B 1 39 ? -10.155 -1.948  18.618 1.00 15.32 ? 39  HIS B CG  1 
ATOM   929  N  ND1 . HIS B 1 39 ? -9.721  -2.770  19.632 1.00 15.23 ? 39  HIS B ND1 1 
ATOM   930  C  CD2 . HIS B 1 39 ? -9.046  -1.599  17.922 1.00 17.60 ? 39  HIS B CD2 1 
ATOM   931  C  CE1 . HIS B 1 39 ? -8.401  -2.861  19.600 1.00 17.69 ? 39  HIS B CE1 1 
ATOM   932  N  NE2 . HIS B 1 39 ? -7.969  -2.142  18.581 1.00 17.82 ? 39  HIS B NE2 1 
ATOM   933  N  N   . ALA B 1 40 ? -14.606 -2.135  17.505 1.00 16.87 ? 40  ALA B N   1 
ATOM   934  C  CA  . ALA B 1 40 ? -16.080 -2.027  17.761 1.00 17.49 ? 40  ALA B CA  1 
ATOM   935  C  C   . ALA B 1 40 ? -16.691 -3.456  17.799 1.00 19.82 ? 40  ALA B C   1 
ATOM   936  O  O   . ALA B 1 40 ? -17.522 -3.793  18.671 1.00 19.96 ? 40  ALA B O   1 
ATOM   937  C  CB  . ALA B 1 40 ? -16.775 -1.144  16.713 1.00 17.09 ? 40  ALA B CB  1 
ATOM   938  N  N   . LYS B 1 41 ? -16.333 -4.275  16.826 1.00 17.94 ? 41  LYS B N   1 
ATOM   939  C  CA  . LYS B 1 41 ? -16.899 -5.587  16.786 1.00 21.03 ? 41  LYS B CA  1 
ATOM   940  C  C   . LYS B 1 41 ? -16.423 -6.402  17.983 1.00 21.75 ? 41  LYS B C   1 
ATOM   941  O  O   . LYS B 1 41 ? -17.150 -7.264  18.467 1.00 22.27 ? 41  LYS B O   1 
ATOM   942  C  CB  . LYS B 1 41 ? -16.520 -6.291  15.503 1.00 21.82 ? 41  LYS B CB  1 
ATOM   943  C  CG  . LYS B 1 41 ? -17.192 -5.730  14.263 1.00 24.63 ? 41  LYS B CG  1 
ATOM   944  C  CD  . LYS B 1 41 ? -16.593 -6.461  13.056 1.00 33.77 ? 41  LYS B CD  1 
ATOM   945  C  CE  . LYS B 1 41 ? -17.169 -6.021  11.743 1.00 38.50 ? 41  LYS B CE  1 
ATOM   946  N  NZ  . LYS B 1 41 ? -18.564 -6.437  11.566 1.00 47.61 ? 41  LYS B NZ  1 
ATOM   947  N  N   . ALA B 1 42 ? -15.214 -6.133  18.464 1.00 19.76 ? 42  ALA B N   1 
ATOM   948  C  CA  . ALA B 1 42 ? -14.679 -6.941  19.567 1.00 21.29 ? 42  ALA B CA  1 
ATOM   949  C  C   . ALA B 1 42 ? -15.350 -6.528  20.873 1.00 22.94 ? 42  ALA B C   1 
ATOM   950  O  O   . ALA B 1 42 ? -15.330 -7.301  21.839 1.00 25.06 ? 42  ALA B O   1 
ATOM   951  C  CB  . ALA B 1 42 ? -13.145 -6.849  19.646 1.00 18.56 ? 42  ALA B CB  1 
ATOM   952  N  N   . ALA B 1 43 ? -15.964 -5.349  20.897 1.00 23.64 ? 43  ALA B N   1 
ATOM   953  C  CA  . ALA B 1 43 ? -16.750 -4.900  22.052 1.00 28.15 ? 43  ALA B CA  1 
ATOM   954  C  C   . ALA B 1 43 ? -18.165 -5.423  22.127 1.00 33.14 ? 43  ALA B C   1 
ATOM   955  O  O   . ALA B 1 43 ? -18.791 -5.295  23.186 1.00 37.84 ? 43  ALA B O   1 
ATOM   956  C  CB  . ALA B 1 43 ? -16.807 -3.372  22.100 1.00 26.02 ? 43  ALA B CB  1 
ATOM   957  N  N   . SER B 1 44 ? -18.740 -5.902  21.033 1.00 35.41 ? 44  SER B N   1 
ATOM   958  C  CA  . SER B 1 44 ? -20.212 -6.051  21.030 1.00 40.91 ? 44  SER B CA  1 
ATOM   959  C  C   . SER B 1 44 ? -20.711 -7.177  21.911 1.00 43.54 ? 44  SER B C   1 
ATOM   960  O  O   . SER B 1 44 ? -20.475 -8.323  21.570 1.00 46.75 ? 44  SER B O   1 
ATOM   961  C  CB  . SER B 1 44 ? -20.773 -6.233  19.626 1.00 42.12 ? 44  SER B CB  1 
ATOM   962  O  OG  . SER B 1 44 ? -19.973 -5.517  18.740 1.00 42.82 ? 44  SER B OG  1 
ATOM   963  N  N   . THR B 1 50 ? -28.351 -1.188  20.762 1.00 43.65 ? 50  THR B N   1 
ATOM   964  C  CA  . THR B 1 50 ? -27.057 -0.932  21.361 1.00 38.63 ? 50  THR B CA  1 
ATOM   965  C  C   . THR B 1 50 ? -26.276 0.058   20.502 1.00 34.12 ? 50  THR B C   1 
ATOM   966  O  O   . THR B 1 50 ? -26.232 -0.012  19.249 1.00 31.37 ? 50  THR B O   1 
ATOM   967  C  CB  . THR B 1 50 ? -26.249 -2.197  21.701 1.00 40.22 ? 50  THR B CB  1 
ATOM   968  O  OG1 . THR B 1 50 ? -25.775 -2.124  23.051 1.00 46.26 ? 50  THR B OG1 1 
ATOM   969  C  CG2 . THR B 1 50 ? -25.027 -2.388  20.821 1.00 36.04 ? 50  THR B CG2 1 
ATOM   970  N  N   . HIS B 1 51 ? -25.724 1.032   21.208 1.00 30.25 ? 51  HIS B N   1 
ATOM   971  C  CA  . HIS B 1 51 ? -24.860 2.022   20.596 1.00 27.45 ? 51  HIS B CA  1 
ATOM   972  C  C   . HIS B 1 51 ? -23.651 1.420   19.933 1.00 25.71 ? 51  HIS B C   1 
ATOM   973  O  O   . HIS B 1 51 ? -23.210 1.893   18.902 1.00 23.81 ? 51  HIS B O   1 
ATOM   974  C  CB  . HIS B 1 51 ? -24.458 3.042   21.660 1.00 26.36 ? 51  HIS B CB  1 
ATOM   975  C  CG  . HIS B 1 51 ? -25.525 4.068   21.909 1.00 28.69 ? 51  HIS B CG  1 
ATOM   976  N  ND1 . HIS B 1 51 ? -25.957 4.931   20.924 1.00 29.13 ? 51  HIS B ND1 1 
ATOM   977  C  CD2 . HIS B 1 51 ? -26.236 4.379   23.020 1.00 33.56 ? 51  HIS B CD2 1 
ATOM   978  C  CE1 . HIS B 1 51 ? -26.895 5.726   21.411 1.00 34.60 ? 51  HIS B CE1 1 
ATOM   979  N  NE2 . HIS B 1 51 ? -27.087 5.408   22.679 1.00 34.48 ? 51  HIS B NE2 1 
ATOM   980  N  N   . VAL B 1 52 ? -23.094 0.355   20.499 1.00 26.54 ? 52  VAL B N   1 
ATOM   981  C  CA  . VAL B 1 52 ? -21.985 -0.308  19.778 1.00 26.03 ? 52  VAL B CA  1 
ATOM   982  C  C   . VAL B 1 52 ? -22.418 -0.800  18.385 1.00 25.95 ? 52  VAL B C   1 
ATOM   983  O  O   . VAL B 1 52 ? -21.712 -0.551  17.388 1.00 24.31 ? 52  VAL B O   1 
ATOM   984  C  CB  . VAL B 1 52 ? -21.394 -1.463  20.611 1.00 27.21 ? 52  VAL B CB  1 
ATOM   985  C  CG1 . VAL B 1 52 ? -20.302 -2.221  19.812 1.00 27.37 ? 52  VAL B CG1 1 
ATOM   986  C  CG2 . VAL B 1 52 ? -20.798 -0.855  21.908 1.00 28.84 ? 52  VAL B CG2 1 
ATOM   987  N  N   . GLY B 1 53 ? -23.576 -1.473  18.317 1.00 27.89 ? 53  GLY B N   1 
ATOM   988  C  CA  . GLY B 1 53 ? -24.141 -1.927  17.036 1.00 27.97 ? 53  GLY B CA  1 
ATOM   989  C  C   . GLY B 1 53 ? -24.287 -0.789  16.017 1.00 26.97 ? 53  GLY B C   1 
ATOM   990  O  O   . GLY B 1 53 ? -23.918 -0.893  14.850 1.00 24.93 ? 53  GLY B O   1 
ATOM   991  N  N   . HIS B 1 54 ? -24.851 0.319   16.460 1.00 26.50 ? 54  HIS B N   1 
ATOM   992  C  CA  . HIS B 1 54 ? -24.945 1.492   15.591 1.00 27.88 ? 54  HIS B CA  1 
ATOM   993  C  C   . HIS B 1 54 ? -23.588 2.045   15.108 1.00 25.45 ? 54  HIS B C   1 
ATOM   994  O  O   . HIS B 1 54 ? -23.420 2.464   13.933 1.00 24.69 ? 54  HIS B O   1 
ATOM   995  C  CB  . HIS B 1 54 ? -25.736 2.578   16.319 1.00 29.99 ? 54  HIS B CB  1 
ATOM   996  C  CG  . HIS B 1 54 ? -27.183 2.230   16.507 1.00 37.04 ? 54  HIS B CG  1 
ATOM   997  N  ND1 . HIS B 1 54 ? -27.809 2.264   17.740 1.00 44.70 ? 54  HIS B ND1 1 
ATOM   998  C  CD2 . HIS B 1 54 ? -28.123 1.818   15.625 1.00 42.66 ? 54  HIS B CD2 1 
ATOM   999  C  CE1 . HIS B 1 54 ? -29.068 1.886   17.608 1.00 44.28 ? 54  HIS B CE1 1 
ATOM   1000 N  NE2 . HIS B 1 54 ? -29.291 1.624   16.333 1.00 46.04 ? 54  HIS B NE2 1 
ATOM   1001 N  N   . GLY B 1 55 ? -22.611 2.079   16.013 1.00 23.88 ? 55  GLY B N   1 
ATOM   1002 C  CA  . GLY B 1 55 ? -21.293 2.567   15.646 1.00 21.87 ? 55  GLY B CA  1 
ATOM   1003 C  C   . GLY B 1 55 ? -20.716 1.605   14.638 1.00 22.28 ? 55  GLY B C   1 
ATOM   1004 O  O   . GLY B 1 55 ? -20.133 2.034   13.669 1.00 20.65 ? 55  GLY B O   1 
ATOM   1005 N  N   . ILE B 1 56 ? -20.897 0.291   14.861 1.00 21.43 ? 56  ILE B N   1 
ATOM   1006 C  CA  . ILE B 1 56 ? -20.411 -0.699  13.850 1.00 22.49 ? 56  ILE B CA  1 
ATOM   1007 C  C   . ILE B 1 56 ? -21.007 -0.400  12.468 1.00 24.40 ? 56  ILE B C   1 
ATOM   1008 O  O   . ILE B 1 56 ? -20.269 -0.266  11.435 1.00 25.09 ? 56  ILE B O   1 
ATOM   1009 C  CB  . ILE B 1 56 ? -20.741 -2.113  14.288 1.00 24.10 ? 56  ILE B CB  1 
ATOM   1010 C  CG1 . ILE B 1 56 ? -19.854 -2.516  15.481 1.00 21.29 ? 56  ILE B CG1 1 
ATOM   1011 C  CG2 . ILE B 1 56 ? -20.585 -3.088  13.158 1.00 25.92 ? 56  ILE B CG2 1 
ATOM   1012 C  CD1 . ILE B 1 56 ? -20.348 -3.752  16.196 1.00 28.47 ? 56  ILE B CD1 1 
ATOM   1013 N  N   . LYS B 1 57 ? -22.328 -0.262  12.447 1.00 25.30 ? 57  LYS B N   1 
ATOM   1014 C  CA  . LYS B 1 57 ? -23.064 0.001   11.208 1.00 29.32 ? 57  LYS B CA  1 
ATOM   1015 C  C   . LYS B 1 57 ? -22.537 1.286   10.541 1.00 26.23 ? 57  LYS B C   1 
ATOM   1016 O  O   . LYS B 1 57 ? -22.352 1.325   9.349  1.00 26.66 ? 57  LYS B O   1 
ATOM   1017 C  CB  . LYS B 1 57 ? -24.584 0.081   11.454 1.00 31.73 ? 57  LYS B CB  1 
ATOM   1018 C  CG  . LYS B 1 57 ? -25.351 -1.269  11.366 1.00 44.65 ? 57  LYS B CG  1 
ATOM   1019 C  CD  . LYS B 1 57 ? -25.341 -2.135  12.676 1.00 50.94 ? 57  LYS B CD  1 
ATOM   1020 C  CE  . LYS B 1 57 ? -24.379 -3.353  12.660 1.00 51.38 ? 57  LYS B CE  1 
ATOM   1021 N  NZ  . LYS B 1 57 ? -23.984 -3.632  14.094 1.00 45.38 ? 57  LYS B NZ  1 
ATOM   1022 N  N   . HIS B 1 58 ? -22.280 2.330   11.313 1.00 25.49 ? 58  HIS B N   1 
ATOM   1023 C  CA  . HIS B 1 58 ? -21.759 3.575   10.710 1.00 23.32 ? 58  HIS B CA  1 
ATOM   1024 C  C   . HIS B 1 58 ? -20.322 3.418   10.247 1.00 22.27 ? 58  HIS B C   1 
ATOM   1025 O  O   . HIS B 1 58 ? -19.967 4.025   9.283  1.00 24.52 ? 58  HIS B O   1 
ATOM   1026 C  CB  . HIS B 1 58 ? -21.820 4.743   11.661 1.00 22.80 ? 58  HIS B CB  1 
ATOM   1027 C  CG  . HIS B 1 58 ? -23.176 5.368   11.776 1.00 24.53 ? 58  HIS B CG  1 
ATOM   1028 N  ND1 . HIS B 1 58 ? -23.698 6.180   10.795 1.00 27.66 ? 58  HIS B ND1 1 
ATOM   1029 C  CD2 . HIS B 1 58 ? -24.108 5.316   12.756 1.00 27.30 ? 58  HIS B CD2 1 
ATOM   1030 C  CE1 . HIS B 1 58 ? -24.883 6.637   11.173 1.00 29.25 ? 58  HIS B CE1 1 
ATOM   1031 N  NE2 . HIS B 1 58 ? -25.160 6.115   12.355 1.00 28.42 ? 58  HIS B NE2 1 
ATOM   1032 N  N   . LEU B 1 59 ? -19.484 2.666   10.965 1.00 20.88 ? 59  LEU B N   1 
ATOM   1033 C  CA  . LEU B 1 59 ? -18.107 2.395   10.473 1.00 19.72 ? 59  LEU B CA  1 
ATOM   1034 C  C   . LEU B 1 59 ? -18.133 1.619   9.160  1.00 22.72 ? 59  LEU B C   1 
ATOM   1035 O  O   . LEU B 1 59 ? -17.415 1.942   8.210  1.00 23.12 ? 59  LEU B O   1 
ATOM   1036 C  CB  . LEU B 1 59 ? -17.306 1.637   11.522 1.00 19.11 ? 59  LEU B CB  1 
ATOM   1037 C  CG  . LEU B 1 59 ? -16.990 2.540   12.716 1.00 19.08 ? 59  LEU B CG  1 
ATOM   1038 C  CD1 . LEU B 1 59 ? -16.569 1.659   13.922 1.00 22.31 ? 59  LEU B CD1 1 
ATOM   1039 C  CD2 . LEU B 1 59 ? -15.910 3.595   12.326 1.00 15.73 ? 59  LEU B CD2 1 
ATOM   1040 N  N   . GLU B 1 60 ? -18.971 0.602   9.090  1.00 22.81 ? 60  GLU B N   1 
ATOM   1041 C  CA  . GLU B 1 60 ? -19.110 -0.144  7.843  1.00 26.15 ? 60  GLU B CA  1 
ATOM   1042 C  C   . GLU B 1 60 ? -19.525 0.776   6.714  1.00 27.83 ? 60  GLU B C   1 
ATOM   1043 O  O   . GLU B 1 60 ? -19.100 0.614   5.564  1.00 29.98 ? 60  GLU B O   1 
ATOM   1044 C  CB  . GLU B 1 60 ? -20.158 -1.249  8.015  1.00 26.97 ? 60  GLU B CB  1 
ATOM   1045 C  CG  . GLU B 1 60 ? -19.717 -2.271  9.083  1.00 29.48 ? 60  GLU B CG  1 
ATOM   1046 C  CD  . GLU B 1 60 ? -20.735 -3.392  9.322  1.00 32.81 ? 60  GLU B CD  1 
ATOM   1047 O  OE1 . GLU B 1 60 ? -20.300 -4.533  9.566  1.00 41.94 ? 60  GLU B OE1 1 
ATOM   1048 O  OE2 . GLU B 1 60 ? -21.966 -3.144  9.256  1.00 42.48 ? 60  GLU B OE2 1 
ATOM   1049 N  N   . ASP B 1 61 ? -20.398 1.733   7.015  1.00 27.69 ? 61  ASP B N   1 
ATOM   1050 C  CA  . ASP B 1 61 ? -20.800 2.720   6.017  1.00 30.13 ? 61  ASP B CA  1 
ATOM   1051 C  C   . ASP B 1 61 ? -19.686 3.694   5.638  1.00 28.48 ? 61  ASP B C   1 
ATOM   1052 O  O   . ASP B 1 61 ? -19.512 4.023   4.455  1.00 32.71 ? 61  ASP B O   1 
ATOM   1053 C  CB  . ASP B 1 61 ? -22.024 3.505   6.489  1.00 30.68 ? 61  ASP B CB  1 
ATOM   1054 C  CG  . ASP B 1 61 ? -23.327 2.742   6.303  1.00 36.35 ? 61  ASP B CG  1 
ATOM   1055 O  OD1 . ASP B 1 61 ? -23.409 1.730   5.524  1.00 43.94 ? 61  ASP B OD1 1 
ATOM   1056 O  OD2 . ASP B 1 61 ? -24.308 3.189   6.938  1.00 40.73 ? 61  ASP B OD2 1 
ATOM   1057 N  N   . ALA B 1 62 ? -18.935 4.175   6.605  1.00 27.05 ? 62  ALA B N   1 
ATOM   1058 C  CA  . ALA B 1 62 ? -17.761 5.001   6.311  1.00 26.12 ? 62  ALA B CA  1 
ATOM   1059 C  C   . ALA B 1 62 ? -16.755 4.244   5.384  1.00 27.90 ? 62  ALA B C   1 
ATOM   1060 O  O   . ALA B 1 62 ? -16.208 4.829   4.429  1.00 28.46 ? 62  ALA B O   1 
ATOM   1061 C  CB  . ALA B 1 62 ? -17.091 5.473   7.615  1.00 24.17 ? 62  ALA B CB  1 
ATOM   1062 N  N   . ILE B 1 63 ? -16.532 2.953   5.660  1.00 26.87 ? 63  ILE B N   1 
ATOM   1063 C  CA  . ILE B 1 63 ? -15.646 2.152   4.835  1.00 29.09 ? 63  ILE B CA  1 
ATOM   1064 C  C   . ILE B 1 63 ? -16.221 2.007   3.421  1.00 33.47 ? 63  ILE B C   1 
ATOM   1065 O  O   . ILE B 1 63 ? -15.525 2.284   2.449  1.00 36.10 ? 63  ILE B O   1 
ATOM   1066 C  CB  . ILE B 1 63 ? -15.321 0.787   5.488  1.00 27.49 ? 63  ILE B CB  1 
ATOM   1067 C  CG1 . ILE B 1 63 ? -14.409 1.047   6.687  1.00 26.73 ? 63  ILE B CG1 1 
ATOM   1068 C  CG2 . ILE B 1 63 ? -14.584 -0.166  4.519  1.00 29.96 ? 63  ILE B CG2 1 
ATOM   1069 C  CD1 . ILE B 1 63 ? -14.509 -0.038  7.763  1.00 23.68 ? 63  ILE B CD1 1 
ATOM   1070 N  N   . LYS B 1 64 ? -17.498 1.619   3.325  1.00 35.60 ? 64  LYS B N   1 
ATOM   1071 C  CA  . LYS B 1 64 ? -18.168 1.454   2.043  1.00 39.66 ? 64  LYS B CA  1 
ATOM   1072 C  C   . LYS B 1 64 ? -17.999 2.723   1.206  1.00 41.21 ? 64  LYS B C   1 
ATOM   1073 O  O   . LYS B 1 64 ? -17.563 2.663   0.039  1.00 43.24 ? 64  LYS B O   1 
ATOM   1074 C  CB  . LYS B 1 64 ? -19.656 1.090   2.248  1.00 40.59 ? 64  LYS B CB  1 
ATOM   1075 C  CG  . LYS B 1 64 ? -20.553 0.938   0.973  1.00 45.04 ? 64  LYS B CG  1 
ATOM   1076 C  CD  . LYS B 1 64 ? -22.025 1.303   1.403  1.00 47.14 ? 64  LYS B CD  1 
ATOM   1077 C  CE  . LYS B 1 64 ? -23.067 1.558   0.278  1.00 53.26 ? 64  LYS B CE  1 
ATOM   1078 N  NZ  . LYS B 1 64 ? -23.600 0.320   -0.468 1.00 57.08 ? 64  LYS B NZ  1 
ATOM   1079 N  N   . HIS B 1 65 ? -18.315 3.868   1.807  1.00 39.13 ? 65  HIS B N   1 
ATOM   1080 C  CA  . HIS B 1 65 ? -18.209 5.143   1.109  1.00 40.58 ? 65  HIS B CA  1 
ATOM   1081 C  C   . HIS B 1 65 ? -16.768 5.525   0.770  1.00 39.64 ? 65  HIS B C   1 
ATOM   1082 O  O   . HIS B 1 65 ? -16.480 5.899   -0.350 1.00 40.85 ? 65  HIS B O   1 
ATOM   1083 C  CB  . HIS B 1 65 ? -18.936 6.220   1.913  1.00 39.97 ? 65  HIS B CB  1 
ATOM   1084 C  CG  . HIS B 1 65 ? -20.427 6.114   1.803  1.00 43.95 ? 65  HIS B CG  1 
ATOM   1085 N  ND1 . HIS B 1 65 ? -21.112 6.545   0.688  1.00 47.64 ? 65  HIS B ND1 1 
ATOM   1086 C  CD2 . HIS B 1 65 ? -21.358 5.585   2.634  1.00 44.07 ? 65  HIS B CD2 1 
ATOM   1087 C  CE1 . HIS B 1 65 ? -22.401 6.296   0.840  1.00 51.14 ? 65  HIS B CE1 1 
ATOM   1088 N  NE2 . HIS B 1 65 ? -22.578 5.715   2.012  1.00 48.99 ? 65  HIS B NE2 1 
ATOM   1089 N  N   . GLY B 1 66 ? -15.868 5.391   1.741  1.00 36.58 ? 66  GLY B N   1 
ATOM   1090 C  CA  . GLY B 1 66 ? -14.435 5.646   1.542  1.00 37.05 ? 66  GLY B CA  1 
ATOM   1091 C  C   . GLY B 1 66 ? -13.866 4.806   0.411  1.00 39.83 ? 66  GLY B C   1 
ATOM   1092 O  O   . GLY B 1 66 ? -13.101 5.311   -0.447 1.00 42.36 ? 66  GLY B O   1 
ATOM   1093 N  N   . GLU B 1 67 ? -14.288 3.544   0.341  1.00 40.84 ? 67  GLU B N   1 
ATOM   1094 C  CA  . GLU B 1 67 ? -13.779 2.651   -0.722 1.00 45.34 ? 67  GLU B CA  1 
ATOM   1095 C  C   . GLU B 1 67 ? -14.148 3.188   -2.092 1.00 49.90 ? 67  GLU B C   1 
ATOM   1096 O  O   . GLU B 1 67 ? -13.404 3.003   -3.057 1.00 52.43 ? 67  GLU B O   1 
ATOM   1097 C  CB  . GLU B 1 67 ? -14.270 1.211   -0.569 1.00 45.72 ? 67  GLU B CB  1 
ATOM   1098 C  CG  . GLU B 1 67 ? -13.774 0.490   0.730  1.00 47.73 ? 67  GLU B CG  1 
ATOM   1099 C  CD  . GLU B 1 67 ? -12.352 -0.125  0.663  1.00 54.04 ? 67  GLU B CD  1 
ATOM   1100 O  OE1 . GLU B 1 67 ? -12.030 -1.011  1.506  1.00 52.59 ? 67  GLU B OE1 1 
ATOM   1101 O  OE2 . GLU B 1 67 ? -11.558 0.279   -0.224 1.00 58.66 ? 67  GLU B OE2 1 
ATOM   1102 N  N   . GLU B 1 68 ? -15.297 3.858   -2.169 1.00 51.19 ? 68  GLU B N   1 
ATOM   1103 C  CA  . GLU B 1 68 ? -15.798 4.399   -3.428 1.00 56.53 ? 68  GLU B CA  1 
ATOM   1104 C  C   . GLU B 1 68 ? -15.268 5.800   -3.684 1.00 56.85 ? 68  GLU B C   1 
ATOM   1105 O  O   . GLU B 1 68 ? -15.456 6.350   -4.759 1.00 59.52 ? 68  GLU B O   1 
ATOM   1106 C  CB  . GLU B 1 68 ? -17.330 4.402   -3.474 1.00 58.08 ? 68  GLU B CB  1 
ATOM   1107 C  CG  . GLU B 1 68 ? -17.952 3.040   -3.242 1.00 62.01 ? 68  GLU B CG  1 
ATOM   1108 C  CD  . GLU B 1 68 ? -19.428 3.110   -2.883 1.00 67.31 ? 68  GLU B CD  1 
ATOM   1109 O  OE1 . GLU B 1 68 ? -20.154 2.171   -3.284 1.00 71.32 ? 68  GLU B OE1 1 
ATOM   1110 O  OE2 . GLU B 1 68 ? -19.869 4.089   -2.206 1.00 65.67 ? 68  GLU B OE2 1 
ATOM   1111 N  N   . GLY B 1 69 ? -14.598 6.365   -2.688 1.00 53.54 ? 69  GLY B N   1 
ATOM   1112 C  CA  . GLY B 1 69 ? -13.962 7.668   -2.825 1.00 53.63 ? 69  GLY B CA  1 
ATOM   1113 C  C   . GLY B 1 69 ? -14.810 8.821   -2.340 1.00 52.37 ? 69  GLY B C   1 
ATOM   1114 O  O   . GLY B 1 69 ? -14.465 9.978   -2.598 1.00 53.92 ? 69  GLY B O   1 
ATOM   1115 N  N   . HIS B 1 70 ? -15.927 8.527   -1.668 1.00 49.22 ? 70  HIS B N   1 
ATOM   1116 C  CA  . HIS B 1 70 ? -16.766 9.587   -1.122 1.00 47.88 ? 70  HIS B CA  1 
ATOM   1117 C  C   . HIS B 1 70 ? -16.266 9.904   0.296  1.00 43.78 ? 70  HIS B C   1 
ATOM   1118 O  O   . HIS B 1 70 ? -16.914 9.572   1.306  1.00 40.59 ? 70  HIS B O   1 
ATOM   1119 C  CB  . HIS B 1 70 ? -18.223 9.154   -1.087 1.00 48.33 ? 70  HIS B CB  1 
ATOM   1120 C  CG  . HIS B 1 70 ? -18.703 8.493   -2.344 1.00 55.49 ? 70  HIS B CG  1 
ATOM   1121 N  ND1 . HIS B 1 70 ? -19.440 7.324   -2.336 1.00 56.87 ? 70  HIS B ND1 1 
ATOM   1122 C  CD2 . HIS B 1 70 ? -18.580 8.851   -3.646 1.00 60.22 ? 70  HIS B CD2 1 
ATOM   1123 C  CE1 . HIS B 1 70 ? -19.745 6.991   -3.578 1.00 61.82 ? 70  HIS B CE1 1 
ATOM   1124 N  NE2 . HIS B 1 70 ? -19.229 7.896   -4.392 1.00 64.18 ? 70  HIS B NE2 1 
ATOM   1125 N  N   . VAL B 1 71 ? -15.106 10.550  0.373  1.00 43.00 ? 71  VAL B N   1 
ATOM   1126 C  CA  . VAL B 1 71 ? -14.480 10.800  1.672  1.00 39.93 ? 71  VAL B CA  1 
ATOM   1127 C  C   . VAL B 1 71 ? -15.327 11.694  2.608  1.00 37.76 ? 71  VAL B C   1 
ATOM   1128 O  O   . VAL B 1 71 ? -15.305 11.521  3.827  1.00 35.10 ? 71  VAL B O   1 
ATOM   1129 C  CB  . VAL B 1 71 ? -12.989 11.243  1.491  1.00 41.44 ? 71  VAL B CB  1 
ATOM   1130 C  CG1 . VAL B 1 71 ? -12.875 12.568  0.704  1.00 43.82 ? 71  VAL B CG1 1 
ATOM   1131 C  CG2 . VAL B 1 71 ? -12.267 11.279  2.808  1.00 39.27 ? 71  VAL B CG2 1 
ATOM   1132 N  N   . GLY B 1 72 ? -16.118 12.614  2.031  1.00 40.07 ? 72  GLY B N   1 
ATOM   1133 C  CA  . GLY B 1 72 ? -16.975 13.507  2.807  1.00 38.79 ? 72  GLY B CA  1 
ATOM   1134 C  C   . GLY B 1 72 ? -18.085 12.731  3.496  1.00 37.84 ? 72  GLY B C   1 
ATOM   1135 O  O   . GLY B 1 72 ? -18.315 12.876  4.703  1.00 36.77 ? 72  GLY B O   1 
ATOM   1136 N  N   . VAL B 1 73 ? -18.779 11.874  2.751  1.00 39.60 ? 73  VAL B N   1 
ATOM   1137 C  CA  . VAL B 1 73 ? -19.821 11.058  3.385  1.00 38.57 ? 73  VAL B CA  1 
ATOM   1138 C  C   . VAL B 1 73 ? -19.206 10.045  4.363  1.00 34.17 ? 73  VAL B C   1 
ATOM   1139 O  O   . VAL B 1 73 ? -19.796 9.768   5.382  1.00 32.39 ? 73  VAL B O   1 
ATOM   1140 C  CB  . VAL B 1 73 ? -20.735 10.340  2.370  1.00 40.98 ? 73  VAL B CB  1 
ATOM   1141 C  CG1 . VAL B 1 73 ? -19.946 9.458   1.546  1.00 46.04 ? 73  VAL B CG1 1 
ATOM   1142 C  CG2 . VAL B 1 73 ? -21.779 9.481   3.089  1.00 42.41 ? 73  VAL B CG2 1 
ATOM   1143 N  N   . ALA B 1 74 ? -18.026 9.507   4.029  1.00 32.80 ? 74  ALA B N   1 
ATOM   1144 C  CA  . ALA B 1 74 ? -17.306 8.546   4.902  1.00 29.87 ? 74  ALA B CA  1 
ATOM   1145 C  C   . ALA B 1 74 ? -16.986 9.218   6.213  1.00 27.73 ? 74  ALA B C   1 
ATOM   1146 O  O   . ALA B 1 74 ? -17.200 8.645   7.301  1.00 26.16 ? 74  ALA B O   1 
ATOM   1147 C  CB  . ALA B 1 74 ? -16.020 8.094   4.227  1.00 29.46 ? 74  ALA B CB  1 
ATOM   1148 N  N   . THR B 1 75 ? -16.454 10.428  6.136  1.00 26.85 ? 75  THR B N   1 
ATOM   1149 C  CA  . THR B 1 75 ? -16.124 11.208  7.346  1.00 26.81 ? 75  THR B CA  1 
ATOM   1150 C  C   . THR B 1 75 ? -17.335 11.431  8.292  1.00 26.38 ? 75  THR B C   1 
ATOM   1151 O  O   . THR B 1 75 ? -17.212 11.282  9.530  1.00 25.34 ? 75  THR B O   1 
ATOM   1152 C  CB  . THR B 1 75 ? -15.490 12.611  6.923  1.00 28.09 ? 75  THR B CB  1 
ATOM   1153 O  OG1 . THR B 1 75 ? -14.326 12.351  6.161  1.00 31.25 ? 75  THR B OG1 1 
ATOM   1154 C  CG2 . THR B 1 75 ? -15.100 13.479  8.115  1.00 28.21 ? 75  THR B CG2 1 
ATOM   1155 N  N   . LYS B 1 76 ? -18.478 11.794  7.706  1.00 28.65 ? 76  LYS B N   1 
ATOM   1156 C  CA  . LYS B 1 76 ? -19.738 11.954  8.443  1.00 30.05 ? 76  LYS B CA  1 
ATOM   1157 C  C   . LYS B 1 76 ? -20.143 10.674  9.148  1.00 28.50 ? 76  LYS B C   1 
ATOM   1158 O  O   . LYS B 1 76 ? -20.553 10.703  10.304 1.00 27.70 ? 76  LYS B O   1 
ATOM   1159 C  CB  . LYS B 1 76 ? -20.856 12.443  7.513  1.00 32.97 ? 76  LYS B CB  1 
ATOM   1160 C  CG  . LYS B 1 76 ? -20.588 13.849  6.902  1.00 38.55 ? 76  LYS B CG  1 
ATOM   1161 C  CD  . LYS B 1 76 ? -21.459 14.079  5.629  1.00 40.93 ? 76  LYS B CD  1 
ATOM   1162 C  CE  . LYS B 1 76 ? -21.130 15.406  4.912  1.00 46.76 ? 76  LYS B CE  1 
ATOM   1163 N  NZ  . LYS B 1 76 ? -21.553 15.400  3.463  1.00 51.25 ? 76  LYS B NZ  1 
ATOM   1164 N  N   . HIS B 1 77 ? -20.011 9.533   8.470  1.00 27.32 ? 77  HIS B N   1 
ATOM   1165 C  CA  . HIS B 1 77 ? -20.350 8.260   9.092  1.00 25.57 ? 77  HIS B CA  1 
ATOM   1166 C  C   . HIS B 1 77 ? -19.402 7.968   10.207 1.00 24.76 ? 77  HIS B C   1 
ATOM   1167 O  O   . HIS B 1 77 ? -19.828 7.473   11.259 1.00 24.16 ? 77  HIS B O   1 
ATOM   1168 C  CB  . HIS B 1 77 ? -20.399 7.081   8.057  1.00 25.93 ? 77  HIS B CB  1 
ATOM   1169 C  CG  . HIS B 1 77 ? -21.702 7.035   7.317  1.00 29.70 ? 77  HIS B CG  1 
ATOM   1170 N  ND1 . HIS B 1 77 ? -22.887 6.713   7.939  1.00 31.00 ? 77  HIS B ND1 1 
ATOM   1171 C  CD2 . HIS B 1 77 ? -22.017 7.299   6.026  1.00 33.88 ? 77  HIS B CD2 1 
ATOM   1172 C  CE1 . HIS B 1 77 ? -23.877 6.760   7.059  1.00 37.48 ? 77  HIS B CE1 1 
ATOM   1173 N  NE2 . HIS B 1 77 ? -23.376 7.119   5.893  1.00 34.65 ? 77  HIS B NE2 1 
ATOM   1174 N  N   . ALA B 1 78 ? -18.124 8.280   10.007 1.00 23.86 ? 78  ALA B N   1 
ATOM   1175 C  CA  . ALA B 1 78 ? -17.122 8.044   11.078 1.00 21.59 ? 78  ALA B CA  1 
ATOM   1176 C  C   . ALA B 1 78 ? -17.464 8.915   12.304 1.00 21.51 ? 78  ALA B C   1 
ATOM   1177 O  O   . ALA B 1 78 ? -17.386 8.430   13.437 1.00 20.16 ? 78  ALA B O   1 
ATOM   1178 C  CB  . ALA B 1 78 ? -15.714 8.290   10.579 1.00 21.48 ? 78  ALA B CB  1 
ATOM   1179 N  N   . GLN B 1 79 ? -17.896 10.141  12.056 1.00 21.83 ? 79  GLN B N   1 
ATOM   1180 C  CA  . GLN B 1 79 ? -18.337 11.063  13.109 1.00 25.09 ? 79  GLN B CA  1 
ATOM   1181 C  C   . GLN B 1 79 ? -19.522 10.519  13.936 1.00 23.83 ? 79  GLN B C   1 
ATOM   1182 O  O   . GLN B 1 79 ? -19.497 10.529  15.175 1.00 23.95 ? 79  GLN B O   1 
ATOM   1183 C  CB  . GLN B 1 79 ? -18.664 12.443  12.531 1.00 25.16 ? 79  GLN B CB  1 
ATOM   1184 C  CG  . GLN B 1 79 ? -17.396 13.281  12.248 1.00 31.77 ? 79  GLN B CG  1 
ATOM   1185 C  CD  . GLN B 1 79 ? -17.644 14.615  11.500 1.00 32.35 ? 79  GLN B CD  1 
ATOM   1186 O  OE1 . GLN B 1 79 ? -18.402 14.666  10.525 1.00 38.70 ? 79  GLN B OE1 1 
ATOM   1187 N  NE2 . GLN B 1 79 ? -16.982 15.690  11.946 1.00 37.69 ? 79  GLN B NE2 1 
ATOM   1188 N  N   . GLU B 1 80 ? -20.513 9.993   13.225 1.00 23.23 ? 80  GLU B N   1 
ATOM   1189 C  CA  . GLU B 1 80 ? -21.661 9.368   13.846 1.00 24.36 ? 80  GLU B CA  1 
ATOM   1190 C  C   . GLU B 1 80 ? -21.268 8.133   14.610 1.00 21.46 ? 80  GLU B C   1 
ATOM   1191 O  O   . GLU B 1 80 ? -21.845 7.854   15.653 1.00 22.31 ? 80  GLU B O   1 
ATOM   1192 C  CB  . GLU B 1 80 ? -22.663 8.970   12.763 1.00 26.39 ? 80  GLU B CB  1 
ATOM   1193 C  CG  . GLU B 1 80 ? -23.073 10.132  11.933 1.00 34.33 ? 80  GLU B CG  1 
ATOM   1194 C  CD  . GLU B 1 80 ? -24.537 10.175  11.707 1.00 48.67 ? 80  GLU B CD  1 
ATOM   1195 O  OE1 . GLU B 1 80 ? -25.227 10.535  12.680 1.00 52.90 ? 80  GLU B OE1 1 
ATOM   1196 O  OE2 . GLU B 1 80 ? -24.996 9.872   10.575 1.00 54.36 ? 80  GLU B OE2 1 
ATOM   1197 N  N   . ALA B 1 81 ? -20.261 7.396   14.111 1.00 20.37 ? 81  ALA B N   1 
ATOM   1198 C  CA  . ALA B 1 81 ? -19.808 6.219   14.798 1.00 17.54 ? 81  ALA B CA  1 
ATOM   1199 C  C   . ALA B 1 81 ? -19.221 6.635   16.118 1.00 18.47 ? 81  ALA B C   1 
ATOM   1200 O  O   . ALA B 1 81 ? -19.469 6.005   17.139 1.00 17.70 ? 81  ALA B O   1 
ATOM   1201 C  CB  . ALA B 1 81 ? -18.767 5.491   13.963 1.00 15.40 ? 81  ALA B CB  1 
ATOM   1202 N  N   . ILE B 1 82 ? -18.432 7.734   16.135 1.00 18.26 ? 82  ILE B N   1 
ATOM   1203 C  CA  . ILE B 1 82 ? -17.857 8.158   17.408 1.00 18.86 ? 82  ILE B CA  1 
ATOM   1204 C  C   . ILE B 1 82 ? -18.925 8.512   18.408 1.00 20.73 ? 82  ILE B C   1 
ATOM   1205 O  O   . ILE B 1 82 ? -18.823 8.170   19.619 1.00 20.37 ? 82  ILE B O   1 
ATOM   1206 C  CB  . ILE B 1 82 ? -16.955 9.375   17.184 1.00 20.40 ? 82  ILE B CB  1 
ATOM   1207 C  CG1 . ILE B 1 82 ? -15.705 8.932   16.409 1.00 21.09 ? 82  ILE B CG1 1 
ATOM   1208 C  CG2 . ILE B 1 82 ? -16.580 10.090  18.541 1.00 23.02 ? 82  ILE B CG2 1 
ATOM   1209 C  CD1 . ILE B 1 82 ? -15.088 10.129  15.688 1.00 26.77 ? 82  ILE B CD1 1 
ATOM   1210 N  N   . GLU B 1 83 ? -19.941 9.243   17.954 1.00 19.61 ? 83  GLU B N   1 
ATOM   1211 C  CA  . GLU B 1 83 ? -20.967 9.650   18.900 1.00 19.95 ? 83  GLU B CA  1 
ATOM   1212 C  C   . GLU B 1 83 ? -21.650 8.389   19.481 1.00 20.82 ? 83  GLU B C   1 
ATOM   1213 O  O   . GLU B 1 83 ? -22.036 8.374   20.629 1.00 21.93 ? 83  GLU B O   1 
ATOM   1214 C  CB  . GLU B 1 83 ? -21.981 10.579  18.242 1.00 20.52 ? 83  GLU B CB  1 
ATOM   1215 C  CG  . GLU B 1 83 ? -21.324 11.961  17.912 1.00 22.30 ? 83  GLU B CG  1 
ATOM   1216 C  CD  . GLU B 1 83 ? -22.330 13.043  17.717 1.00 26.74 ? 83  GLU B CD  1 
ATOM   1217 O  OE1 . GLU B 1 83 ? -23.571 12.722  17.648 1.00 28.66 ? 83  GLU B OE1 1 
ATOM   1218 O  OE2 . GLU B 1 83 ? -21.917 14.243  17.669 1.00 28.31 ? 83  GLU B OE2 1 
ATOM   1219 N  N   . HIS B 1 84 ? -21.889 7.374   18.666 1.00 20.14 ? 84  HIS B N   1 
ATOM   1220 C  CA  . HIS B 1 84 ? -22.532 6.155   19.191 1.00 20.86 ? 84  HIS B CA  1 
ATOM   1221 C  C   . HIS B 1 84 ? -21.599 5.456   20.136 1.00 20.28 ? 84  HIS B C   1 
ATOM   1222 O  O   . HIS B 1 84 ? -22.035 5.017   21.224 1.00 22.02 ? 84  HIS B O   1 
ATOM   1223 C  CB  . HIS B 1 84 ? -22.944 5.182   18.066 1.00 20.17 ? 84  HIS B CB  1 
ATOM   1224 C  CG  . HIS B 1 84 ? -24.265 5.541   17.431 1.00 20.98 ? 84  HIS B CG  1 
ATOM   1225 N  ND1 . HIS B 1 84 ? -25.481 5.398   18.078 1.00 25.91 ? 84  HIS B ND1 1 
ATOM   1226 C  CD2 . HIS B 1 84 ? -24.552 6.074   16.217 1.00 24.09 ? 84  HIS B CD2 1 
ATOM   1227 C  CE1 . HIS B 1 84 ? -26.458 5.822   17.297 1.00 24.83 ? 84  HIS B CE1 1 
ATOM   1228 N  NE2 . HIS B 1 84 ? -25.925 6.229   16.155 1.00 24.96 ? 84  HIS B NE2 1 
ATOM   1229 N  N   . LEU B 1 85 ? -20.340 5.310   19.725 1.00 18.70 ? 85  LEU B N   1 
ATOM   1230 C  CA  . LEU B 1 85 ? -19.377 4.609   20.602 1.00 21.90 ? 85  LEU B CA  1 
ATOM   1231 C  C   . LEU B 1 85 ? -19.242 5.320   21.929 1.00 23.38 ? 85  LEU B C   1 
ATOM   1232 O  O   . LEU B 1 85 ? -19.216 4.684   22.974 1.00 25.69 ? 85  LEU B O   1 
ATOM   1233 C  CB  . LEU B 1 85 ? -18.039 4.437   19.939 1.00 18.83 ? 85  LEU B CB  1 
ATOM   1234 C  CG  . LEU B 1 85 ? -18.081 3.544   18.698 1.00 20.65 ? 85  LEU B CG  1 
ATOM   1235 C  CD1 . LEU B 1 85 ? -16.811 3.796   17.971 1.00 22.55 ? 85  LEU B CD1 1 
ATOM   1236 C  CD2 . LEU B 1 85 ? -18.226 2.104   19.152 1.00 20.06 ? 85  LEU B CD2 1 
ATOM   1237 N  N   . ARG B 1 86 ? -19.200 6.646   21.898 1.00 24.38 ? 86  ARG B N   1 
ATOM   1238 C  CA  . ARG B 1 86 ? -19.131 7.402   23.153 1.00 26.32 ? 86  ARG B CA  1 
ATOM   1239 C  C   . ARG B 1 86 ? -20.418 7.297   23.963 1.00 28.65 ? 86  ARG B C   1 
ATOM   1240 O  O   . ARG B 1 86 ? -20.356 7.295   25.194 1.00 31.67 ? 86  ARG B O   1 
ATOM   1241 C  CB  . ARG B 1 86 ? -18.775 8.867   22.899 1.00 26.73 ? 86  ARG B CB  1 
ATOM   1242 C  CG  . ARG B 1 86 ? -17.372 9.103   22.366 1.00 28.07 ? 86  ARG B CG  1 
ATOM   1243 C  CD  . ARG B 1 86 ? -17.036 10.584  22.492 1.00 35.98 ? 86  ARG B CD  1 
ATOM   1244 N  NE  . ARG B 1 86 ? -15.693 10.908  21.991 1.00 43.65 ? 86  ARG B NE  1 
ATOM   1245 C  CZ  . ARG B 1 86 ? -14.570 10.729  22.700 1.00 48.24 ? 86  ARG B CZ  1 
ATOM   1246 N  NH1 . ARG B 1 86 ? -13.384 11.049  22.195 1.00 47.52 ? 86  ARG B NH1 1 
ATOM   1247 N  NH2 . ARG B 1 86 ? -14.630 10.223  23.933 1.00 50.22 ? 86  ARG B NH2 1 
ATOM   1248 N  N   . ALA B 1 87 ? -21.576 7.222   23.299 1.00 28.14 ? 87  ALA B N   1 
ATOM   1249 C  CA  . ALA B 1 87 ? -22.868 6.983   23.976 1.00 29.70 ? 87  ALA B CA  1 
ATOM   1250 C  C   . ALA B 1 87 ? -22.929 5.595   24.592 1.00 30.15 ? 87  ALA B C   1 
ATOM   1251 O  O   . ALA B 1 87 ? -23.743 5.344   25.464 1.00 30.81 ? 87  ALA B O   1 
ATOM   1252 C  CB  . ALA B 1 87 ? -24.018 7.153   23.035 1.00 29.22 ? 87  ALA B CB  1 
ATOM   1253 N  N   . SER B 1 88 ? -22.117 4.663   24.128 1.00 30.31 ? 88  SER B N   1 
ATOM   1254 C  CA  . SER B 1 88 ? -22.200 3.343   24.786 1.00 32.80 ? 88  SER B CA  1 
ATOM   1255 C  C   . SER B 1 88 ? -21.654 3.490   26.240 1.00 35.02 ? 88  SER B C   1 
ATOM   1256 O  O   . SER B 1 88 ? -22.074 2.731   27.124 1.00 39.77 ? 88  SER B O   1 
ATOM   1257 C  CB  . SER B 1 88 ? -21.501 2.264   23.970 1.00 31.55 ? 88  SER B CB  1 
ATOM   1258 O  OG  . SER B 1 88 ? -20.126 2.402   24.095 1.00 31.35 ? 88  SER B OG  1 
HETATM 1259 NI NI  . NI  C 2 .  ? -10.784 -8.208  23.604 1.00 18.89 ? 94  NI  A NI  1 
HETATM 1260 O  O   . HOH D 3 .  ? -3.860  -8.190  26.954 1.00 46.27 ? 95  HOH A O   1 
HETATM 1261 O  O   . HOH D 3 .  ? -7.988  -4.000  12.222 1.00 21.30 ? 96  HOH A O   1 
HETATM 1262 O  O   . HOH D 3 .  ? 6.462   -20.598 7.569  1.00 41.99 ? 97  HOH A O   1 
HETATM 1263 O  O   . HOH D 3 .  ? -5.271  -4.038  19.035 1.00 23.01 ? 98  HOH A O   1 
HETATM 1264 O  O   . HOH D 3 .  ? 4.430   -3.136  9.523  1.00 26.91 ? 99  HOH A O   1 
HETATM 1265 O  O   . HOH D 3 .  ? -14.903 -9.649  17.121 1.00 29.44 ? 100 HOH A O   1 
HETATM 1266 O  O   . HOH D 3 .  ? -3.229  -21.254 2.244  1.00 30.62 ? 101 HOH A O   1 
HETATM 1267 O  O   . HOH D 3 .  ? -7.846  -4.505  7.532  1.00 19.75 ? 102 HOH A O   1 
HETATM 1268 O  O   . HOH D 3 .  ? -7.543  -19.327 20.408 1.00 23.56 ? 103 HOH A O   1 
HETATM 1269 O  O   . HOH D 3 .  ? -4.650  -19.769 -8.400 1.00 31.60 ? 104 HOH A O   1 
HETATM 1270 O  O   . HOH D 3 .  ? -3.393  -3.394  12.210 1.00 23.31 ? 105 HOH A O   1 
HETATM 1271 O  O   . HOH D 3 .  ? -10.559 -10.895 1.816  1.00 27.70 ? 106 HOH A O   1 
HETATM 1272 O  O   . HOH D 3 .  ? -4.415  -19.679 -1.823 1.00 27.46 ? 107 HOH A O   1 
HETATM 1273 O  O   . HOH D 3 .  ? -8.770  -13.089 28.525 1.00 36.65 ? 108 HOH A O   1 
HETATM 1274 O  O   . HOH D 3 .  ? 2.597   -7.110  -4.890 1.00 35.91 ? 109 HOH A O   1 
HETATM 1275 O  O   . HOH D 3 .  ? -3.977  -20.188 4.701  1.00 24.98 ? 110 HOH A O   1 
HETATM 1276 O  O   . HOH D 3 .  ? -6.650  -12.937 -8.866 1.00 31.42 ? 111 HOH A O   1 
HETATM 1277 O  O   . HOH D 3 .  ? 10.391  -6.409  0.780  1.00 36.64 ? 112 HOH A O   1 
HETATM 1278 O  O   . HOH D 3 .  ? 9.705   -16.800 13.984 1.00 33.21 ? 113 HOH A O   1 
HETATM 1279 O  O   . HOH D 3 .  ? 8.588   -21.990 10.271 1.00 35.87 ? 114 HOH A O   1 
HETATM 1280 O  O   . HOH D 3 .  ? -6.858  -2.358  5.986  1.00 42.48 ? 115 HOH A O   1 
HETATM 1281 O  O   . HOH D 3 .  ? -10.229 -16.166 26.419 1.00 39.75 ? 116 HOH A O   1 
HETATM 1282 O  O   . HOH D 3 .  ? -12.152 -20.379 14.302 1.00 47.62 ? 117 HOH A O   1 
HETATM 1283 O  O   . HOH D 3 .  ? -7.561  -3.203  9.710  1.00 28.45 ? 118 HOH A O   1 
HETATM 1284 O  O   . HOH D 3 .  ? -4.630  -21.538 -0.252 1.00 28.78 ? 119 HOH A O   1 
HETATM 1285 O  O   . HOH D 3 .  ? -13.230 -10.845 18.667 1.00 33.97 ? 120 HOH A O   1 
HETATM 1286 O  O   . HOH D 3 .  ? -9.459  -17.873 7.663  1.00 33.39 ? 121 HOH A O   1 
HETATM 1287 O  O   . HOH D 3 .  ? 9.968   -11.417 12.122 1.00 39.52 ? 122 HOH A O   1 
HETATM 1288 O  O   . HOH D 3 .  ? -3.288  -6.391  -4.877 1.00 39.41 ? 123 HOH A O   1 
HETATM 1289 O  O   . HOH D 3 .  ? -6.162  -20.001 23.397 1.00 44.20 ? 124 HOH A O   1 
HETATM 1290 O  O   . HOH D 3 .  ? 0.961   -4.910  21.486 1.00 45.91 ? 125 HOH A O   1 
HETATM 1291 O  O   . HOH D 3 .  ? 8.620   -6.659  13.047 1.00 42.26 ? 126 HOH A O   1 
HETATM 1292 O  O   . HOH D 3 .  ? -4.285  -15.496 -8.561 1.00 37.32 ? 127 HOH A O   1 
HETATM 1293 O  O   . HOH D 3 .  ? 2.812   -15.643 -2.998 1.00 40.34 ? 128 HOH A O   1 
HETATM 1294 O  O   . HOH D 3 .  ? -12.050 -14.582 9.774  1.00 54.62 ? 129 HOH A O   1 
HETATM 1295 O  O   . HOH D 3 .  ? -12.247 -8.936  13.414 1.00 38.06 ? 130 HOH A O   1 
HETATM 1296 O  O   . HOH D 3 .  ? 5.766   -17.465 0.241  1.00 35.70 ? 131 HOH A O   1 
HETATM 1297 O  O   . HOH D 3 .  ? -2.640  -18.347 -8.488 1.00 42.55 ? 132 HOH A O   1 
HETATM 1298 O  O   . HOH D 3 .  ? -4.084  -21.447 -9.977 1.00 57.13 ? 133 HOH A O   1 
HETATM 1299 O  O   . HOH D 3 .  ? 1.802   -21.427 8.943  1.00 35.06 ? 134 HOH A O   1 
HETATM 1300 O  O   . HOH D 3 .  ? 5.871   -19.273 1.924  1.00 39.66 ? 135 HOH A O   1 
HETATM 1301 O  O   . HOH D 3 .  ? -4.507  -2.405  3.984  1.00 36.70 ? 136 HOH A O   1 
HETATM 1302 O  O   . HOH D 3 .  ? -5.013  -3.215  1.574  1.00 38.18 ? 137 HOH A O   1 
HETATM 1303 O  O   . HOH D 3 .  ? -7.507  -2.600  0.651  1.00 43.90 ? 138 HOH A O   1 
HETATM 1304 O  O   . HOH D 3 .  ? -13.717 -5.881  10.803 1.00 40.94 ? 139 HOH A O   1 
HETATM 1305 O  O   . HOH D 3 .  ? -13.295 -8.835  8.656  1.00 39.38 ? 140 HOH A O   1 
HETATM 1306 O  O   . HOH D 3 .  ? -12.958 -11.098 12.486 1.00 39.45 ? 141 HOH A O   1 
HETATM 1307 O  O   . HOH D 3 .  ? -14.315 -13.504 17.909 1.00 34.00 ? 142 HOH A O   1 
HETATM 1308 O  O   . HOH D 3 .  ? -1.708  -1.964  11.144 1.00 45.09 ? 143 HOH A O   1 
HETATM 1309 O  O   . HOH D 3 .  ? -10.391 -4.869  7.369  1.00 50.54 ? 144 HOH A O   1 
HETATM 1310 O  O   . HOH D 3 .  ? -1.653  -20.451 -7.353 1.00 52.13 ? 145 HOH A O   1 
HETATM 1311 O  O   . HOH D 3 .  ? -6.593  -20.741 -7.756 1.00 44.92 ? 146 HOH A O   1 
HETATM 1312 O  O   . HOH D 3 .  ? -3.159  -20.562 -4.057 1.00 30.65 ? 147 HOH A O   1 
HETATM 1313 O  O   . HOH D 3 .  ? -5.747  -22.223 6.009  1.00 44.44 ? 148 HOH A O   1 
HETATM 1314 O  O   . HOH D 3 .  ? 6.386   -8.217  19.424 1.00 33.38 ? 149 HOH A O   1 
HETATM 1315 O  O   . HOH E 3 .  ? -4.580  -3.731  21.570 1.00 41.68 ? 94  HOH B O   1 
HETATM 1316 O  O   . HOH E 3 .  ? -26.804 6.751   14.044 1.00 21.01 ? 95  HOH B O   1 
HETATM 1317 O  O   . HOH E 3 .  ? -4.902  -5.767  26.033 1.00 45.70 ? 96  HOH B O   1 
HETATM 1318 O  O   . HOH E 3 .  ? -6.322  -0.799  8.988  1.00 24.51 ? 97  HOH B O   1 
HETATM 1319 O  O   . HOH E 3 .  ? -8.805  -9.559  27.490 1.00 26.77 ? 98  HOH B O   1 
HETATM 1320 O  O   . HOH E 3 .  ? -13.277 -7.802  15.742 1.00 21.05 ? 99  HOH B O   1 
HETATM 1321 O  O   . HOH E 3 .  ? -12.268 -3.880  9.963  1.00 21.10 ? 100 HOH B O   1 
HETATM 1322 O  O   . HOH E 3 .  ? -22.041 10.735  22.100 1.00 21.72 ? 101 HOH B O   1 
HETATM 1323 O  O   . HOH E 3 .  ? -4.612  8.755   2.556  1.00 42.49 ? 102 HOH B O   1 
HETATM 1324 O  O   . HOH E 3 .  ? -11.206 13.569  15.054 1.00 26.20 ? 103 HOH B O   1 
HETATM 1325 O  O   . HOH E 3 .  ? -11.531 -3.058  29.490 1.00 29.52 ? 104 HOH B O   1 
HETATM 1326 O  O   . HOH E 3 .  ? -28.411 7.391   24.267 1.00 33.48 ? 105 HOH B O   1 
HETATM 1327 O  O   . HOH E 3 .  ? -7.436  0.327   3.955  1.00 34.35 ? 106 HOH B O   1 
HETATM 1328 O  O   . HOH E 3 .  ? -14.636 -3.518  30.336 1.00 33.05 ? 107 HOH B O   1 
HETATM 1329 O  O   . HOH E 3 .  ? -18.326 12.562  -0.314 1.00 38.64 ? 108 HOH B O   1 
HETATM 1330 O  O   . HOH E 3 .  ? -10.036 9.162   22.422 1.00 32.43 ? 109 HOH B O   1 
HETATM 1331 O  O   . HOH E 3 .  ? -18.261 12.889  16.119 1.00 29.75 ? 110 HOH B O   1 
HETATM 1332 O  O   . HOH E 3 .  ? -25.743 1.068   24.123 1.00 34.16 ? 111 HOH B O   1 
HETATM 1333 O  O   . HOH E 3 .  ? -5.436  -1.472  17.671 1.00 31.11 ? 112 HOH B O   1 
HETATM 1334 O  O   . HOH E 3 .  ? -8.764  -4.893  28.767 1.00 32.69 ? 113 HOH B O   1 
HETATM 1335 O  O   . HOH E 3 .  ? -6.868  -3.588  22.756 1.00 32.20 ? 114 HOH B O   1 
HETATM 1336 O  O   . HOH E 3 .  ? -17.317 1.909   27.623 1.00 40.14 ? 115 HOH B O   1 
HETATM 1337 O  O   . HOH E 3 .  ? -7.887  10.002  19.936 1.00 36.05 ? 116 HOH B O   1 
HETATM 1338 O  O   . HOH E 3 .  ? -19.345 12.569  20.911 1.00 41.46 ? 117 HOH B O   1 
HETATM 1339 O  O   . HOH E 3 .  ? -10.734 6.667   23.362 1.00 27.39 ? 118 HOH B O   1 
HETATM 1340 O  O   . HOH E 3 .  ? -17.870 -1.613  4.776  1.00 35.83 ? 119 HOH B O   1 
HETATM 1341 O  O   . HOH E 3 .  ? -5.965  8.874   0.022  1.00 52.31 ? 120 HOH B O   1 
HETATM 1342 O  O   . HOH E 3 .  ? -2.678  -2.630  14.564 1.00 41.28 ? 121 HOH B O   1 
HETATM 1343 O  O   . HOH E 3 .  ? -12.282 -9.750  27.828 1.00 38.34 ? 122 HOH B O   1 
HETATM 1344 O  O   . HOH E 3 .  ? -17.545 4.799   26.252 1.00 45.22 ? 123 HOH B O   1 
HETATM 1345 O  O   . HOH E 3 .  ? -20.620 1.120   28.525 1.00 51.22 ? 124 HOH B O   1 
HETATM 1346 O  O   . HOH E 3 .  ? -2.808  0.719   14.906 1.00 41.44 ? 125 HOH B O   1 
HETATM 1347 O  O   . HOH E 3 .  ? -21.345 10.523  -1.761 1.00 51.20 ? 126 HOH B O   1 
HETATM 1348 O  O   . HOH E 3 .  ? -18.103 -9.598  16.625 1.00 51.07 ? 127 HOH B O   1 
HETATM 1349 O  O   . HOH E 3 .  ? -25.828 3.430   9.543  1.00 48.98 ? 128 HOH B O   1 
HETATM 1350 O  O   . HOH E 3 .  ? -14.125 -9.055  26.289 1.00 34.11 ? 129 HOH B O   1 
HETATM 1351 O  O   . HOH E 3 .  ? -15.365 -7.112  24.671 1.00 35.58 ? 130 HOH B O   1 
HETATM 1352 O  O   . HOH E 3 .  ? -24.489 8.991   15.630 1.00 33.02 ? 131 HOH B O   1 
HETATM 1353 O  O   . HOH E 3 .  ? -6.139  2.414   3.265  1.00 39.01 ? 132 HOH B O   1 
HETATM 1354 O  O   . HOH E 3 .  ? -0.447  2.613   6.733  1.00 46.60 ? 133 HOH B O   1 
HETATM 1355 O  O   . HOH E 3 .  ? -6.359  -1.038  24.595 1.00 44.32 ? 134 HOH B O   1 
HETATM 1356 O  O   . HOH E 3 .  ? -8.122  1.256   25.054 1.00 35.78 ? 135 HOH B O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . SER A 1  ? 0.2595 0.2550 0.2323 -0.0077 0.0782  -0.0098 1  SER A N   
2    C CA  . SER A 1  ? 0.2779 0.2775 0.2539 -0.0201 0.0884  0.0039  1  SER A CA  
3    C C   . SER A 1  ? 0.2983 0.2823 0.2465 -0.0216 0.0862  0.0172  1  SER A C   
4    O O   . SER A 1  ? 0.2858 0.2619 0.2190 -0.0155 0.0750  0.0140  1  SER A O   
5    C CB  . SER A 1  ? 0.2592 0.2526 0.2587 -0.0263 0.0836  0.0073  1  SER A CB  
6    O OG  . SER A 1  ? 0.2544 0.2651 0.2772 -0.0213 0.0809  -0.0048 1  SER A OG  
7    N N   . GLY A 2  ? 0.3128 0.2915 0.2546 -0.0300 0.0964  0.0329  2  GLY A N   
8    C CA  . GLY A 2  ? 0.3326 0.2971 0.2472 -0.0269 0.0928  0.0483  2  GLY A CA  
9    C C   . GLY A 2  ? 0.3297 0.2749 0.2505 -0.0243 0.0799  0.0545  2  GLY A C   
10   O O   . GLY A 2  ? 0.2974 0.2388 0.2425 -0.0264 0.0746  0.0472  2  GLY A O   
11   N N   . HIS A 3  ? 0.3602 0.2969 0.2581 -0.0178 0.0749  0.0684  3  HIS A N   
12   C CA  . HIS A 3  ? 0.3464 0.2705 0.2482 -0.0116 0.0620  0.0742  3  HIS A CA  
13   C C   . HIS A 3  ? 0.3332 0.2372 0.2571 -0.0177 0.0677  0.0788  3  HIS A C   
14   O O   . HIS A 3  ? 0.3105 0.2118 0.2526 -0.0168 0.0589  0.0715  3  HIS A O   
15   C CB  . HIS A 3  ? 0.3937 0.3166 0.2651 -0.0011 0.0589  0.0920  3  HIS A CB  
16   C CG  . HIS A 3  ? 0.4104 0.3256 0.2854 0.0087  0.0466  0.0990  3  HIS A CG  
17   N ND1 . HIS A 3  ? 0.4296 0.3637 0.3077 0.0138  0.0298  0.0880  3  HIS A ND1 
18   C CD2 . HIS A 3  ? 0.4475 0.3387 0.3246 0.0146  0.0496  0.1149  3  HIS A CD2 
19   C CE1 . HIS A 3  ? 0.4590 0.3868 0.3427 0.0231  0.0228  0.0967  3  HIS A CE1 
20   N NE2 . HIS A 3  ? 0.4464 0.3465 0.3282 0.0257  0.0343  0.1131  3  HIS A NE2 
21   N N   . THR A 4  ? 0.3429 0.2341 0.2650 -0.0262 0.0843  0.0894  4  THR A N   
22   C CA  . THR A 4  ? 0.3512 0.2183 0.2920 -0.0342 0.0911  0.0925  4  THR A CA  
23   C C   . THR A 4  ? 0.3042 0.1853 0.2768 -0.0420 0.0872  0.0721  4  THR A C   
24   O O   . THR A 4  ? 0.2958 0.1667 0.2843 -0.0421 0.0816  0.0670  4  THR A O   
25   C CB  . THR A 4  ? 0.3766 0.2281 0.3111 -0.0469 0.1121  0.1053  4  THR A CB  
26   O OG1 . THR A 4  ? 0.4289 0.2653 0.3297 -0.0368 0.1155  0.1283  4  THR A OG1 
27   C CG2 . THR A 4  ? 0.3774 0.2005 0.3319 -0.0591 0.1208  0.1050  4  THR A CG2 
28   N N   . ALA A 5  ? 0.3065 0.2134 0.2873 -0.0469 0.0907  0.0601  5  ALA A N   
29   C CA  . ALA A 5  ? 0.2785 0.2031 0.2878 -0.0519 0.0876  0.0428  5  ALA A CA  
30   C C   . ALA A 5  ? 0.2509 0.1788 0.2639 -0.0407 0.0699  0.0352  5  ALA A C   
31   O O   . ALA A 5  ? 0.2378 0.1687 0.2694 -0.0420 0.0641  0.0270  5  ALA A O   
32   C CB  . ALA A 5  ? 0.2848 0.2384 0.2992 -0.0545 0.0953  0.0336  5  ALA A CB  
33   N N   . HIS A 6  ? 0.2546 0.1833 0.2491 -0.0309 0.0615  0.0374  6  HIS A N   
34   C CA  . HIS A 6  ? 0.2331 0.1634 0.2312 -0.0240 0.0468  0.0313  6  HIS A CA  
35   C C   . HIS A 6  ? 0.2462 0.1642 0.2482 -0.0219 0.0405  0.0370  6  HIS A C   
36   O O   . HIS A 6  ? 0.2528 0.1752 0.2684 -0.0208 0.0330  0.0303  6  HIS A O   
37   C CB  . HIS A 6  ? 0.2419 0.1762 0.2206 -0.0179 0.0400  0.0295  6  HIS A CB  
38   C CG  . HIS A 6  ? 0.2110 0.1556 0.1890 -0.0167 0.0437  0.0182  6  HIS A CG  
39   N ND1 . HIS A 6  ? 0.2211 0.1712 0.2163 -0.0146 0.0420  0.0085  6  HIS A ND1 
40   C CD2 . HIS A 6  ? 0.2278 0.1788 0.1890 -0.0147 0.0490  0.0148  6  HIS A CD2 
41   C CE1 . HIS A 6  ? 0.2681 0.2253 0.2588 -0.0101 0.0466  -0.0002 6  HIS A CE1 
42   N NE2 . HIS A 6  ? 0.2164 0.1744 0.1869 -0.0109 0.0513  0.0020  6  HIS A NE2 
43   N N   . VAL A 7  ? 0.2655 0.1690 0.2539 -0.0190 0.0436  0.0501  7  VAL A N   
44   C CA  . VAL A 7  ? 0.2727 0.1639 0.2653 -0.0134 0.0387  0.0550  7  VAL A CA  
45   C C   . VAL A 7  ? 0.2793 0.1631 0.2935 -0.0216 0.0444  0.0470  7  VAL A C   
46   O O   . VAL A 7  ? 0.2674 0.1539 0.2933 -0.0187 0.0375  0.0404  7  VAL A O   
47   C CB  . VAL A 7  ? 0.3082 0.1830 0.2807 -0.0049 0.0416  0.0724  7  VAL A CB  
48   C CG1 . VAL A 7  ? 0.3325 0.1906 0.3113 0.0036  0.0390  0.0768  7  VAL A CG1 
49   C CG2 . VAL A 7  ? 0.2720 0.1657 0.2254 0.0035  0.0316  0.0753  7  VAL A CG2 
50   N N   . ASP A 8  ? 0.2957 0.1747 0.3156 -0.0332 0.0574  0.0459  8  ASP A N   
51   C CA  . ASP A 8  ? 0.3104 0.1869 0.3524 -0.0441 0.0629  0.0348  8  ASP A CA  
52   C C   . ASP A 8  ? 0.2734 0.1773 0.3326 -0.0437 0.0533  0.0192  8  ASP A C   
53   O O   . ASP A 8  ? 0.2461 0.1503 0.3174 -0.0441 0.0492  0.0106  8  ASP A O   
54   C CB  . ASP A 8  ? 0.3379 0.2146 0.3858 -0.0600 0.0788  0.0340  8  ASP A CB  
55   C CG  . ASP A 8  ? 0.3784 0.2548 0.4500 -0.0752 0.0852  0.0199  8  ASP A CG  
56   O OD1 . ASP A 8  ? 0.4315 0.3351 0.5191 -0.0866 0.0903  0.0090  8  ASP A OD1 
57   O OD2 . ASP A 8  ? 0.4573 0.3077 0.5311 -0.0754 0.0858  0.0190  8  ASP A OD2 
58   N N   . GLU A 9  ? 0.2477 0.1734 0.3061 -0.0411 0.0498  0.0157  9  GLU A N   
59   C CA  . GLU A 9  ? 0.2366 0.1848 0.3075 -0.0375 0.0411  0.0048  9  GLU A CA  
60   C C   . GLU A 9  ? 0.2248 0.1684 0.2899 -0.0287 0.0296  0.0072  9  GLU A C   
61   O O   . GLU A 9  ? 0.2150 0.1702 0.2904 -0.0275 0.0240  0.0001  9  GLU A O   
62   C CB  . GLU A 9  ? 0.2299 0.1946 0.2978 -0.0327 0.0408  0.0024  9  GLU A CB  
63   C CG  . GLU A 9  ? 0.2807 0.2635 0.3598 -0.0400 0.0518  -0.0033 9  GLU A CG  
64   C CD  . GLU A 9  ? 0.3572 0.3617 0.4606 -0.0483 0.0532  -0.0152 9  GLU A CD  
65   O OE1 . GLU A 9  ? 0.3190 0.3355 0.4299 -0.0425 0.0435  -0.0212 9  GLU A OE1 
66   O OE2 . GLU A 9  ? 0.5113 0.5218 0.6257 -0.0624 0.0647  -0.0190 9  GLU A OE2 
67   N N   . ALA A 10 ? 0.2215 0.1533 0.2705 -0.0232 0.0262  0.0166  10 ALA A N   
68   C CA  . ALA A 10 ? 0.2028 0.1371 0.2497 -0.0170 0.0162  0.0177  10 ALA A CA  
69   C C   . ALA A 10 ? 0.2138 0.1441 0.2706 -0.0159 0.0162  0.0148  10 ALA A C   
70   O O   . ALA A 10 ? 0.2068 0.1495 0.2709 -0.0140 0.0106  0.0092  10 ALA A O   
71   C CB  . ALA A 10 ? 0.2175 0.1475 0.2475 -0.0122 0.0121  0.0262  10 ALA A CB  
72   N N   . VAL A 11 ? 0.2325 0.1436 0.2883 -0.0173 0.0240  0.0185  11 VAL A N   
73   C CA  . VAL A 11 ? 0.2441 0.1435 0.3082 -0.0156 0.0260  0.0137  11 VAL A CA  
74   C C   . VAL A 11 ? 0.2543 0.1686 0.3356 -0.0240 0.0267  -0.0025 11 VAL A C   
75   O O   . VAL A 11 ? 0.2437 0.1684 0.3315 -0.0203 0.0219  -0.0109 11 VAL A O   
76   C CB  . VAL A 11 ? 0.2728 0.1394 0.3298 -0.0157 0.0365  0.0225  11 VAL A CB  
77   C CG1 . VAL A 11 ? 0.2891 0.1360 0.3557 -0.0156 0.0412  0.0138  11 VAL A CG1 
78   C CG2 . VAL A 11 ? 0.2941 0.1537 0.3329 -0.0025 0.0327  0.0385  11 VAL A CG2 
79   N N   . LYS A 12 ? 0.2537 0.1757 0.3420 -0.0346 0.0323  -0.0077 12 LYS A N   
80   C CA  . LYS A 12 ? 0.2589 0.2026 0.3640 -0.0424 0.0321  -0.0239 12 LYS A CA  
81   C C   . LYS A 12 ? 0.2135 0.1852 0.3196 -0.0344 0.0210  -0.0274 12 LYS A C   
82   O O   . LYS A 12 ? 0.1775 0.1660 0.2921 -0.0350 0.0176  -0.0395 12 LYS A O   
83   C CB  . LYS A 12 ? 0.2670 0.2229 0.3813 -0.0541 0.0397  -0.0283 12 LYS A CB  
84   C CG  . LYS A 12 ? 0.3504 0.2785 0.4665 -0.0676 0.0541  -0.0270 12 LYS A CG  
85   C CD  . LYS A 12 ? 0.3661 0.3176 0.4978 -0.0831 0.0625  -0.0362 12 LYS A CD  
86   C CE  . LYS A 12 ? 0.4142 0.3989 0.5457 -0.0748 0.0572  -0.0340 12 LYS A CE  
87   N NZ  . LYS A 12 ? 0.4515 0.4604 0.5985 -0.0891 0.0683  -0.0413 12 LYS A NZ  
88   N N   . HIS A 13 ? 0.1899 0.1665 0.2861 -0.0275 0.0161  -0.0175 13 HIS A N   
89   C CA  . HIS A 13 ? 0.1738 0.1693 0.2684 -0.0208 0.0078  -0.0176 13 HIS A CA  
90   C C   . HIS A 13 ? 0.1822 0.1762 0.2725 -0.0162 0.0034  -0.0158 13 HIS A C   
91   O O   . HIS A 13 ? 0.1924 0.2052 0.2847 -0.0136 -0.0008 -0.0201 13 HIS A O   
92   C CB  . HIS A 13 ? 0.1598 0.1527 0.2440 -0.0160 0.0055  -0.0083 13 HIS A CB  
93   C CG  . HIS A 13 ? 0.1555 0.1623 0.2458 -0.0151 0.0078  -0.0122 13 HIS A CG  
94   N ND1 . HIS A 13 ? 0.1858 0.2184 0.2840 -0.0105 0.0039  -0.0179 13 HIS A ND1 
95   C CD2 . HIS A 13 ? 0.2175 0.2208 0.3071 -0.0165 0.0136  -0.0115 13 HIS A CD2 
96   C CE1 . HIS A 13 ? 0.2291 0.2752 0.3338 -0.0081 0.0067  -0.0210 13 HIS A CE1 
97   N NE2 . HIS A 13 ? 0.2323 0.2606 0.3322 -0.0123 0.0134  -0.0177 13 HIS A NE2 
98   N N   . ALA A 14 ? 0.1732 0.1490 0.2573 -0.0141 0.0047  -0.0091 14 ALA A N   
99   C CA  . ALA A 14 ? 0.1769 0.1573 0.2597 -0.0081 0.0011  -0.0084 14 ALA A CA  
100  C C   . ALA A 14 ? 0.1768 0.1602 0.2694 -0.0081 0.0039  -0.0218 14 ALA A C   
101  O O   . ALA A 14 ? 0.1771 0.1783 0.2717 -0.0041 0.0009  -0.0273 14 ALA A O   
102  C CB  . ALA A 14 ? 0.1612 0.1265 0.2364 -0.0029 0.0012  0.0011  14 ALA A CB  
103  N N   . GLU A 15 ? 0.1789 0.1449 0.2772 -0.0140 0.0108  -0.0284 15 GLU A N   
104  C CA  . GLU A 15 ? 0.2049 0.1718 0.3131 -0.0167 0.0140  -0.0459 15 GLU A CA  
105  C C   . GLU A 15 ? 0.1895 0.1913 0.3035 -0.0197 0.0090  -0.0579 15 GLU A C   
106  O O   . GLU A 15 ? 0.1927 0.2074 0.3096 -0.0174 0.0079  -0.0708 15 GLU A O   
107  C CB  . GLU A 15 ? 0.2375 0.1773 0.3517 -0.0270 0.0239  -0.0519 15 GLU A CB  
108  C CG  . GLU A 15 ? 0.2774 0.1789 0.3821 -0.0197 0.0295  -0.0383 15 GLU A CG  
109  C CD  . GLU A 15 ? 0.4248 0.2918 0.5321 -0.0313 0.0421  -0.0400 15 GLU A CD  
110  O OE1 . GLU A 15 ? 0.4212 0.2986 0.5370 -0.0470 0.0463  -0.0466 15 GLU A OE1 
111  O OE2 . GLU A 15 ? 0.4943 0.3242 0.5952 -0.0244 0.0486  -0.0339 15 GLU A OE2 
112  N N   . GLU A 16 ? 0.1849 0.2037 0.2996 -0.0234 0.0064  -0.0545 16 GLU A N   
113  C CA  . GLU A 16 ? 0.1758 0.2302 0.2934 -0.0224 0.0006  -0.0626 16 GLU A CA  
114  C C   . GLU A 16 ? 0.1830 0.2509 0.2892 -0.0127 -0.0052 -0.0529 16 GLU A C   
115  O O   . GLU A 16 ? 0.1774 0.2721 0.2827 -0.0100 -0.0086 -0.0610 16 GLU A O   
116  C CB  . GLU A 16 ? 0.1701 0.2400 0.2907 -0.0238 -0.0010 -0.0589 16 GLU A CB  
117  C CG  . GLU A 16 ? 0.2555 0.3664 0.3838 -0.0237 -0.0060 -0.0723 16 GLU A CG  
118  C CD  . GLU A 16 ? 0.3434 0.4630 0.4876 -0.0375 -0.0018 -0.0960 16 GLU A CD  
119  O OE1 . GLU A 16 ? 0.3839 0.5416 0.5342 -0.0385 -0.0069 -0.1117 16 GLU A OE1 
120  O OE2 . GLU A 16 ? 0.4437 0.5309 0.5934 -0.0478 0.0071  -0.0998 16 GLU A OE2 
121  N N   . ALA A 17 ? 0.1677 0.2201 0.2647 -0.0090 -0.0059 -0.0362 17 ALA A N   
122  C CA  . ALA A 17 ? 0.1655 0.2303 0.2536 -0.0041 -0.0091 -0.0278 17 ALA A CA  
123  C C   . ALA A 17 ? 0.1532 0.2287 0.2443 -0.0010 -0.0078 -0.0380 17 ALA A C   
124  O O   . ALA A 17 ? 0.1530 0.2538 0.2398 0.0019  -0.0094 -0.0399 17 ALA A O   
125  C CB  . ALA A 17 ? 0.1486 0.1949 0.2296 -0.0047 -0.0092 -0.0128 17 ALA A CB  
126  N N   . VAL A 18 ? 0.1735 0.2290 0.2704 0.0001  -0.0041 -0.0437 18 VAL A N   
127  C CA  . VAL A 18 ? 0.1695 0.2317 0.2700 0.0066  -0.0019 -0.0552 18 VAL A CA  
128  C C   . VAL A 18 ? 0.1839 0.2672 0.2877 0.0044  -0.0017 -0.0748 18 VAL A C   
129  O O   . VAL A 18 ? 0.1979 0.3085 0.2987 0.0095  -0.0023 -0.0825 18 VAL A O   
130  C CB  . VAL A 18 ? 0.1689 0.1982 0.2737 0.0111  0.0029  -0.0573 18 VAL A CB  
131  C CG1 . VAL A 18 ? 0.1732 0.2042 0.2831 0.0195  0.0068  -0.0751 18 VAL A CG1 
132  C CG2 . VAL A 18 ? 0.1882 0.2120 0.2881 0.0171  0.0007  -0.0398 18 VAL A CG2 
133  N N   . ALA A 19 ? 0.1885 0.2652 0.2986 -0.0039 -0.0007 -0.0848 19 ALA A N   
134  C CA  . ALA A 19 ? 0.1806 0.2811 0.2952 -0.0080 -0.0014 -0.1067 19 ALA A CA  
135  C C   . ALA A 19 ? 0.1913 0.3357 0.2961 -0.0034 -0.0082 -0.1028 19 ALA A C   
136  O O   . ALA A 19 ? 0.1838 0.3570 0.2857 -0.0008 -0.0093 -0.1181 19 ALA A O   
137  C CB  . ALA A 19 ? 0.2074 0.2999 0.3332 -0.0209 0.0008  -0.1178 19 ALA A CB  
138  N N   . HIS A 20 ? 0.1619 0.3096 0.2598 -0.0017 -0.0119 -0.0825 20 HIS A N   
139  C CA  . HIS A 20 ? 0.1783 0.3590 0.2630 0.0046  -0.0169 -0.0724 20 HIS A CA  
140  C C   . HIS A 20 ? 0.1510 0.3415 0.2262 0.0093  -0.0145 -0.0665 20 HIS A C   
141  O O   . HIS A 20 ? 0.1920 0.4156 0.2572 0.0136  -0.0158 -0.0688 20 HIS A O   
142  C CB  . HIS A 20 ? 0.1483 0.3156 0.2268 0.0065  -0.0191 -0.0498 20 HIS A CB  
143  C CG  . HIS A 20 ? 0.1410 0.3217 0.2255 0.0070  -0.0229 -0.0547 20 HIS A CG  
144  N ND1 . HIS A 20 ? 0.1530 0.3746 0.2350 0.0121  -0.0286 -0.0631 20 HIS A ND1 
145  C CD2 . HIS A 20 ? 0.1563 0.3207 0.2492 0.0040  -0.0219 -0.0524 20 HIS A CD2 
146  C CE1 . HIS A 20 ? 0.1192 0.3517 0.2103 0.0126  -0.0316 -0.0663 20 HIS A CE1 
147  N NE2 . HIS A 20 ? 0.1675 0.3649 0.2654 0.0076  -0.0268 -0.0596 20 HIS A NE2 
148  N N   . GLY A 21 ? 0.1925 0.3591 0.2714 0.0088  -0.0107 -0.0597 21 GLY A N   
149  C CA  . GLY A 21 ? 0.1637 0.3437 0.2370 0.0120  -0.0077 -0.0522 21 GLY A CA  
150  C C   . GLY A 21 ? 0.1868 0.3900 0.2623 0.0172  -0.0051 -0.0722 21 GLY A C   
151  O O   . GLY A 21 ? 0.1901 0.4241 0.2567 0.0200  -0.0031 -0.0696 21 GLY A O   
152  N N   . LYS A 22 ? 0.1895 0.3764 0.2757 0.0178  -0.0037 -0.0926 22 LYS A N   
153  C CA  . LYS A 22 ? 0.2014 0.4045 0.2899 0.0231  -0.0004 -0.1166 22 LYS A CA  
154  C C   . LYS A 22 ? 0.2088 0.4523 0.2875 0.0219  -0.0037 -0.1282 22 LYS A C   
155  O O   . LYS A 22 ? 0.2160 0.4864 0.2908 0.0272  -0.0011 -0.1454 22 LYS A O   
156  C CB  . LYS A 22 ? 0.2186 0.3864 0.3192 0.0217  0.0030  -0.1357 22 LYS A CB  
157  C CG  . LYS A 22 ? 0.2363 0.3652 0.3433 0.0274  0.0065  -0.1239 22 LYS A CG  
158  C CD  . LYS A 22 ? 0.3191 0.4072 0.4348 0.0246  0.0117  -0.1409 22 LYS A CD  
159  C CE  . LYS A 22 ? 0.4160 0.4625 0.5353 0.0351  0.0166  -0.1327 22 LYS A CE  
160  N NZ  . LYS A 22 ? 0.4271 0.4269 0.5518 0.0263  0.0229  -0.1427 22 LYS A NZ  
161  N N   . GLU A 23 ? 0.1804 0.4321 0.2544 0.0170  -0.0096 -0.1191 23 GLU A N   
162  C CA  . GLU A 23 ? 0.2128 0.5080 0.2754 0.0187  -0.0146 -0.1258 23 GLU A CA  
163  C C   . GLU A 23 ? 0.2192 0.5359 0.2629 0.0242  -0.0151 -0.0994 23 GLU A C   
164  O O   . GLU A 23 ? 0.2390 0.5938 0.2675 0.0289  -0.0192 -0.0979 23 GLU A O   
165  C CB  . GLU A 23 ? 0.2072 0.5051 0.2758 0.0134  -0.0211 -0.1300 23 GLU A CB  
166  C CG  . GLU A 23 ? 0.2222 0.5092 0.3084 0.0036  -0.0198 -0.1604 23 GLU A CG  
167  C CD  . GLU A 23 ? 0.2612 0.5807 0.3448 0.0035  -0.0198 -0.1911 23 GLU A CD  
168  O OE1 . GLU A 23 ? 0.2532 0.6196 0.3302 0.0040  -0.0271 -0.2009 23 GLU A OE1 
169  O OE2 . GLU A 23 ? 0.2834 0.5833 0.3714 0.0043  -0.0128 -0.2068 23 GLU A OE2 
170  N N   . GLY A 24 ? 0.2058 0.5000 0.2492 0.0232  -0.0107 -0.0786 24 GLY A N   
171  C CA  . GLY A 24 ? 0.2310 0.5373 0.2569 0.0242  -0.0085 -0.0515 24 GLY A CA  
172  C C   . GLY A 24 ? 0.2272 0.5207 0.2437 0.0251  -0.0133 -0.0303 24 GLY A C   
173  O O   . GLY A 24 ? 0.2431 0.5459 0.2408 0.0279  -0.0119 -0.0084 24 GLY A O   
174  N N   . HIS A 25 ? 0.2186 0.4891 0.2475 0.0236  -0.0179 -0.0357 25 HIS A N   
175  C CA  . HIS A 25 ? 0.2016 0.4591 0.2246 0.0272  -0.0221 -0.0184 25 HIS A CA  
176  C C   . HIS A 25 ? 0.2125 0.4301 0.2341 0.0224  -0.0179 0.0028  25 HIS A C   
177  O O   . HIS A 25 ? 0.1584 0.3471 0.1910 0.0192  -0.0187 0.0017  25 HIS A O   
178  C CB  . HIS A 25 ? 0.2001 0.4548 0.2397 0.0261  -0.0273 -0.0355 25 HIS A CB  
179  C CG  . HIS A 25 ? 0.1816 0.4781 0.2247 0.0279  -0.0324 -0.0594 25 HIS A CG  
180  N ND1 . HIS A 25 ? 0.1661 0.4650 0.2282 0.0210  -0.0346 -0.0820 25 HIS A ND1 
181  C CD2 . HIS A 25 ? 0.2298 0.5695 0.2596 0.0340  -0.0353 -0.0659 25 HIS A CD2 
182  C CE1 . HIS A 25 ? 0.1468 0.4886 0.2087 0.0216  -0.0393 -0.1034 25 HIS A CE1 
183  N NE2 . HIS A 25 ? 0.1922 0.5613 0.2335 0.0309  -0.0406 -0.0940 25 HIS A NE2 
184  N N   . THR A 26 ? 0.2352 0.4517 0.2422 0.0205  -0.0127 0.0217  26 THR A N   
185  C CA  . THR A 26 ? 0.2322 0.4131 0.2398 0.0114  -0.0078 0.0368  26 THR A CA  
186  C C   . THR A 26 ? 0.2254 0.3719 0.2316 0.0138  -0.0102 0.0470  26 THR A C   
187  O O   . THR A 26 ? 0.2304 0.3498 0.2466 0.0070  -0.0095 0.0445  26 THR A O   
188  C CB  . THR A 26 ? 0.2557 0.4432 0.2482 0.0053  0.0001  0.0552  26 THR A CB  
189  O OG1 . THR A 26 ? 0.2227 0.4495 0.2159 0.0060  0.0025  0.0437  26 THR A OG1 
190  C CG2 . THR A 26 ? 0.2794 0.4406 0.2795 -0.0092 0.0053  0.0616  26 THR A CG2 
191  N N   . ASP A 27 ? 0.2582 0.4081 0.2516 0.0254  -0.0131 0.0575  27 ASP A N   
192  C CA  . ASP A 27 ? 0.2779 0.3948 0.2687 0.0310  -0.0142 0.0678  27 ASP A CA  
193  C C   . ASP A 27 ? 0.2556 0.3694 0.2657 0.0314  -0.0185 0.0499  27 ASP A C   
194  O O   . ASP A 27 ? 0.2557 0.3387 0.2690 0.0301  -0.0172 0.0527  27 ASP A O   
195  C CB  . ASP A 27 ? 0.2999 0.4264 0.2731 0.0489  -0.0172 0.0830  27 ASP A CB  
196  C CG  . ASP A 27 ? 0.4236 0.5377 0.3727 0.0489  -0.0103 0.1081  27 ASP A CG  
197  O OD1 . ASP A 27 ? 0.4989 0.5848 0.4459 0.0332  -0.0021 0.1159  27 ASP A OD1 
198  O OD2 . ASP A 27 ? 0.4718 0.6065 0.4033 0.0639  -0.0126 0.1205  27 ASP A OD2 
199  N N   . GLN A 28 ? 0.2341 0.3807 0.2560 0.0328  -0.0229 0.0309  28 GLN A N   
200  C CA  . GLN A 28 ? 0.1938 0.3388 0.2348 0.0295  -0.0247 0.0135  28 GLN A CA  
201  C C   . GLN A 28 ? 0.1898 0.3090 0.2407 0.0170  -0.0203 0.0073  28 GLN A C   
202  O O   . GLN A 28 ? 0.1678 0.2655 0.2262 0.0139  -0.0189 0.0053  28 GLN A O   
203  C CB  . GLN A 28 ? 0.2042 0.3915 0.2545 0.0317  -0.0297 -0.0064 28 GLN A CB  
204  C CG  A GLN A 28 ? 0.1844 0.4068 0.2258 0.0472  -0.0366 -0.0012 28 GLN A CG  
205  C CG  B GLN A 28 ? 0.2400 0.4575 0.2897 0.0453  -0.0365 -0.0058 28 GLN A CG  
206  C CD  A GLN A 28 ? 0.1644 0.3959 0.1813 0.0568  -0.0367 0.0185  28 GLN A CD  
207  C CD  B GLN A 28 ? 0.2946 0.4878 0.3445 0.0531  -0.0357 0.0066  28 GLN A CD  
208  O OE1 A GLN A 28 ? 0.1175 0.3558 0.1271 0.0505  -0.0334 0.0178  28 GLN A OE1 
209  O OE1 B GLN A 28 ? 0.3650 0.5575 0.4001 0.0688  -0.0378 0.0241  28 GLN A OE1 
210  N NE2 A GLN A 28 ? 0.1677 0.4018 0.1708 0.0737  -0.0400 0.0367  28 GLN A NE2 
211  N NE2 B GLN A 28 ? 0.2959 0.4681 0.3607 0.0438  -0.0318 -0.0019 28 GLN A NE2 
212  N N   . LEU A 29 ? 0.1883 0.3111 0.2377 0.0116  -0.0177 0.0061  29 LEU A N   
213  C CA  . LEU A 29 ? 0.1755 0.2771 0.2320 0.0039  -0.0145 0.0040  29 LEU A CA  
214  C C   . LEU A 29 ? 0.1778 0.2503 0.2278 0.0005  -0.0131 0.0182  29 LEU A C   
215  O O   . LEU A 29 ? 0.1813 0.2335 0.2366 -0.0031 -0.0125 0.0158  29 LEU A O   
216  C CB  . LEU A 29 ? 0.1908 0.3082 0.2467 0.0015  -0.0120 0.0023  29 LEU A CB  
217  C CG  . LEU A 29 ? 0.1595 0.2622 0.2221 -0.0034 -0.0099 0.0028  29 LEU A CG  
218  C CD1 . LEU A 29 ? 0.1560 0.2797 0.2254 -0.0003 -0.0080 -0.0079 29 LEU A CD1 
219  C CD2 . LEU A 29 ? 0.1785 0.2711 0.2335 -0.0111 -0.0082 0.0184  29 LEU A CD2 
220  N N   . LEU A 30 ? 0.1939 0.2619 0.2306 0.0015  -0.0119 0.0328  30 LEU A N   
221  C CA  . LEU A 30 ? 0.2041 0.2399 0.2337 -0.0038 -0.0094 0.0436  30 LEU A CA  
222  C C   . LEU A 30 ? 0.2095 0.2275 0.2413 0.0025  -0.0109 0.0407  30 LEU A C   
223  O O   . LEU A 30 ? 0.2261 0.2216 0.2587 -0.0028 -0.0095 0.0391  30 LEU A O   
224  C CB  . LEU A 30 ? 0.2213 0.2484 0.2345 -0.0041 -0.0056 0.0610  30 LEU A CB  
225  C CG  . LEU A 30 ? 0.2496 0.2933 0.2619 -0.0156 -0.0014 0.0644  30 LEU A CG  
226  C CD1 . LEU A 30 ? 0.2883 0.3250 0.2822 -0.0164 0.0042  0.0836  30 LEU A CD1 
227  C CD2 . LEU A 30 ? 0.2514 0.2838 0.2725 -0.0302 0.0001  0.0596  30 LEU A CD2 
228  N N   . GLU A 31 ? 0.1950 0.2283 0.2275 0.0143  -0.0136 0.0392  31 GLU A N   
229  C CA  . GLU A 31 ? 0.1989 0.2234 0.2353 0.0218  -0.0142 0.0360  31 GLU A CA  
230  C C   . GLU A 31 ? 0.1744 0.1953 0.2235 0.0138  -0.0129 0.0234  31 GLU A C   
231  O O   . GLU A 31 ? 0.1831 0.1827 0.2309 0.0127  -0.0104 0.0233  31 GLU A O   
232  C CB  . GLU A 31 ? 0.2215 0.2760 0.2604 0.0357  -0.0185 0.0341  31 GLU A CB  
233  C CG  . GLU A 31 ? 0.3417 0.3846 0.3628 0.0488  -0.0185 0.0522  31 GLU A CG  
234  C CD  . GLU A 31 ? 0.5312 0.5960 0.5528 0.0690  -0.0229 0.0537  31 GLU A CD  
235  O OE1 . GLU A 31 ? 0.5803 0.6701 0.5923 0.0800  -0.0269 0.0617  31 GLU A OE1 
236  O OE2 . GLU A 31 ? 0.5493 0.6109 0.5804 0.0751  -0.0225 0.0472  31 GLU A OE2 
237  N N   . HIS A 32 ? 0.1560 0.1951 0.2155 0.0087  -0.0136 0.0129  32 HIS A N   
238  C CA  . HIS A 32 ? 0.1437 0.1742 0.2126 0.0016  -0.0108 0.0041  32 HIS A CA  
239  C C   . HIS A 32 ? 0.1576 0.1676 0.2216 -0.0045 -0.0093 0.0084  32 HIS A C   
240  O O   . HIS A 32 ? 0.1608 0.1571 0.2252 -0.0068 -0.0067 0.0071  32 HIS A O   
241  C CB  . HIS A 32 ? 0.1444 0.1939 0.2252 -0.0015 -0.0106 -0.0092 32 HIS A CB  
242  C CG  . HIS A 32 ? 0.1405 0.2145 0.2304 0.0012  -0.0120 -0.0182 32 HIS A CG  
243  N ND1 . HIS A 32 ? 0.1554 0.2293 0.2550 -0.0022 -0.0085 -0.0241 32 HIS A ND1 
244  C CD2 . HIS A 32 ? 0.1239 0.2293 0.2145 0.0072  -0.0168 -0.0225 32 HIS A CD2 
245  C CE1 . HIS A 32 ? 0.1836 0.2902 0.2928 0.0007  -0.0112 -0.0332 32 HIS A CE1 
246  N NE2 . HIS A 32 ? 0.1690 0.2953 0.2719 0.0075  -0.0172 -0.0322 32 HIS A NE2 
247  N N   . ALA A 33 ? 0.1494 0.1614 0.2086 -0.0071 -0.0106 0.0135  33 ALA A N   
248  C CA  . ALA A 33 ? 0.1752 0.1767 0.2311 -0.0129 -0.0106 0.0167  33 ALA A CA  
249  C C   . ALA A 33 ? 0.1664 0.1466 0.2133 -0.0153 -0.0098 0.0208  33 ALA A C   
250  O O   . ALA A 33 ? 0.1784 0.1496 0.2228 -0.0185 -0.0098 0.0192  33 ALA A O   
251  C CB  . ALA A 33 ? 0.1639 0.1787 0.2182 -0.0170 -0.0112 0.0210  33 ALA A CB  
252  N N   . LYS A 34 ? 0.1914 0.1632 0.2317 -0.0121 -0.0089 0.0259  34 LYS A N   
253  C CA  . LYS A 34 ? 0.1855 0.1323 0.2167 -0.0133 -0.0070 0.0273  34 LYS A CA  
254  C C   . LYS A 34 ? 0.2024 0.1455 0.2359 -0.0080 -0.0053 0.0207  34 LYS A C   
255  O O   . LYS A 34 ? 0.2247 0.1533 0.2515 -0.0115 -0.0040 0.0177  34 LYS A O   
256  C CB  . LYS A 34 ? 0.2140 0.1458 0.2360 -0.0082 -0.0052 0.0355  34 LYS A CB  
257  C CG  . LYS A 34 ? 0.1933 0.1220 0.2095 -0.0188 -0.0038 0.0438  34 LYS A CG  
258  C CD  . LYS A 34 ? 0.2909 0.1997 0.2943 -0.0117 -0.0004 0.0567  34 LYS A CD  
259  C CE  . LYS A 34 ? 0.3339 0.2437 0.3313 -0.0230 0.0031  0.0670  34 LYS A CE  
260  N NZ  . LYS A 34 ? 0.3914 0.2790 0.3730 -0.0140 0.0074  0.0833  34 LYS A NZ  
261  N N   . GLU A 35 ? 0.1991 0.1586 0.2420 -0.0013 -0.0048 0.0173  35 GLU A N   
262  C CA  . GLU A 35 ? 0.1993 0.1612 0.2470 0.0008  -0.0013 0.0112  35 GLU A CA  
263  C C   . GLU A 35 ? 0.1948 0.1532 0.2419 -0.0070 0.0002  0.0096  35 GLU A C   
264  O O   . GLU A 35 ? 0.2057 0.1560 0.2470 -0.0079 0.0036  0.0082  35 GLU A O   
265  C CB  . GLU A 35 ? 0.1968 0.1830 0.2579 0.0062  -0.0007 0.0060  35 GLU A CB  
266  C CG  A GLU A 35 ? 0.2264 0.2208 0.2862 0.0192  -0.0032 0.0093  35 GLU A CG  
267  C CG  B GLU A 35 ? 0.2581 0.2451 0.3184 0.0171  0.0015  0.0051  35 GLU A CG  
268  C CD  A GLU A 35 ? 0.2188 0.2482 0.2934 0.0249  -0.0045 0.0021  35 GLU A CD  
269  C CD  B GLU A 35 ? 0.2660 0.2829 0.3420 0.0209  0.0034  -0.0028 35 GLU A CD  
270  O OE1 A GLU A 35 ? 0.2916 0.3410 0.3717 0.0223  -0.0082 -0.0008 35 GLU A OE1 
271  O OE1 B GLU A 35 ? 0.2026 0.2438 0.2888 0.0198  -0.0001 -0.0066 35 GLU A OE1 
272  O OE2 A GLU A 35 ? 0.2702 0.3110 0.3512 0.0324  -0.0020 -0.0020 35 GLU A OE2 
273  O OE2 B GLU A 35 ? 0.2698 0.2895 0.3482 0.0246  0.0086  -0.0068 35 GLU A OE2 
274  N N   . SER A 36 ? 0.1577 0.1233 0.2099 -0.0103 -0.0019 0.0102  36 SER A N   
275  C CA  . SER A 36 ? 0.1760 0.1363 0.2258 -0.0133 -0.0010 0.0115  36 SER A CA  
276  C C   . SER A 36 ? 0.1631 0.1151 0.2004 -0.0154 -0.0032 0.0144  36 SER A C   
277  O O   . SER A 36 ? 0.1929 0.1397 0.2225 -0.0154 -0.0013 0.0159  36 SER A O   
278  C CB  . SER A 36 ? 0.1809 0.1497 0.2371 -0.0127 -0.0036 0.0112  36 SER A CB  
279  O OG  . SER A 36 ? 0.1961 0.1574 0.2497 -0.0112 -0.0022 0.0139  36 SER A OG  
280  N N   . LEU A 37 ? 0.1698 0.1213 0.2037 -0.0185 -0.0068 0.0151  37 LEU A N   
281  C CA  . LEU A 37 ? 0.1816 0.1284 0.2053 -0.0244 -0.0095 0.0141  37 LEU A CA  
282  C C   . LEU A 37 ? 0.2003 0.1329 0.2132 -0.0241 -0.0065 0.0097  37 LEU A C   
283  O O   . LEU A 37 ? 0.2057 0.1394 0.2084 -0.0266 -0.0077 0.0068  37 LEU A O   
284  C CB  . LEU A 37 ? 0.2014 0.1491 0.2262 -0.0314 -0.0116 0.0153  37 LEU A CB  
285  C CG  . LEU A 37 ? 0.2236 0.1676 0.2404 -0.0424 -0.0139 0.0108  37 LEU A CG  
286  C CD1 . LEU A 37 ? 0.2368 0.2052 0.2552 -0.0431 -0.0195 0.0095  37 LEU A CD1 
287  C CD2 . LEU A 37 ? 0.2714 0.2091 0.2889 -0.0528 -0.0126 0.0127  37 LEU A CD2 
288  N N   . THR A 38 ? 0.2184 0.1419 0.2329 -0.0188 -0.0025 0.0084  38 THR A N   
289  C CA  . THR A 38 ? 0.2387 0.1511 0.2442 -0.0155 0.0019  0.0025  38 THR A CA  
290  C C   . THR A 38 ? 0.2391 0.1609 0.2415 -0.0145 0.0053  0.0023  38 THR A C   
291  O O   . THR A 38 ? 0.2585 0.1776 0.2474 -0.0159 0.0066  -0.0022 38 THR A O   
292  C CB  . THR A 38 ? 0.2397 0.1477 0.2505 -0.0056 0.0055  0.0020  38 THR A CB  
293  O OG1 . THR A 38 ? 0.2436 0.1379 0.2526 -0.0056 0.0032  0.0059  38 THR A OG1 
294  C CG2 . THR A 38 ? 0.2626 0.1602 0.2646 0.0005  0.0110  -0.0061 38 THR A CG2 
295  N N   . HIS A 39 ? 0.2172 0.1494 0.2305 -0.0131 0.0075  0.0068  39 HIS A N   
296  C CA  . HIS A 39 ? 0.2237 0.1594 0.2331 -0.0137 0.0132  0.0098  39 HIS A CA  
297  C C   . HIS A 39 ? 0.2308 0.1664 0.2282 -0.0150 0.0091  0.0154  39 HIS A C   
298  O O   . HIS A 39 ? 0.2606 0.1965 0.2445 -0.0143 0.0125  0.0177  39 HIS A O   
299  C CB  . HIS A 39 ? 0.2162 0.1579 0.2407 -0.0149 0.0178  0.0118  39 HIS A CB  
300  C CG  . HIS A 39 ? 0.1826 0.1348 0.2181 -0.0134 0.0234  0.0056  39 HIS A CG  
301  N ND1 . HIS A 39 ? 0.1853 0.1427 0.2177 -0.0139 0.0323  0.0036  39 HIS A ND1 
302  C CD2 . HIS A 39 ? 0.1764 0.1403 0.2256 -0.0098 0.0212  0.0010  39 HIS A CD2 
303  C CE1 . HIS A 39 ? 0.2253 0.1995 0.2722 -0.0108 0.0353  -0.0032 39 HIS A CE1 
304  N NE2 . HIS A 39 ? 0.1619 0.1405 0.2186 -0.0075 0.0279  -0.0045 39 HIS A NE2 
305  N N   . ALA A 40 ? 0.2266 0.1661 0.2287 -0.0154 0.0021  0.0179  40 ALA A N   
306  C CA  . ALA A 40 ? 0.2363 0.1830 0.2292 -0.0135 -0.0033 0.0230  40 ALA A CA  
307  C C   . ALA A 40 ? 0.2466 0.1986 0.2240 -0.0169 -0.0071 0.0169  40 ALA A C   
308  O O   . ALA A 40 ? 0.2428 0.2031 0.2054 -0.0133 -0.0087 0.0209  40 ALA A O   
309  C CB  . ALA A 40 ? 0.2206 0.1778 0.2247 -0.0124 -0.0099 0.0245  40 ALA A CB  
310  N N   . LYS A 41 ? 0.2524 0.1988 0.2312 -0.0233 -0.0084 0.0073  41 LYS A N   
311  C CA  . LYS A 41 ? 0.2687 0.2158 0.2327 -0.0287 -0.0108 -0.0029 41 LYS A CA  
312  C C   . LYS A 41 ? 0.2882 0.2318 0.2377 -0.0240 -0.0039 -0.0053 41 LYS A C   
313  O O   . LYS A 41 ? 0.2849 0.2383 0.2169 -0.0252 -0.0063 -0.0108 41 LYS A O   
314  C CB  . LYS A 41 ? 0.2828 0.2137 0.2502 -0.0369 -0.0107 -0.0128 41 LYS A CB  
315  C CG  . LYS A 41 ? 0.2736 0.2117 0.2517 -0.0458 -0.0163 -0.0115 41 LYS A CG  
316  C CD  . LYS A 41 ? 0.3143 0.2275 0.2929 -0.0543 -0.0132 -0.0175 41 LYS A CD  
317  C CE  A LYS A 41 ? 0.3918 0.3133 0.3812 -0.0651 -0.0160 -0.0138 41 LYS A CE  
318  C CE  B LYS A 41 ? 0.3274 0.2491 0.3156 -0.0663 -0.0163 -0.0152 41 LYS A CE  
319  N NZ  A LYS A 41 ? 0.4152 0.3648 0.4061 -0.0770 -0.0229 -0.0201 41 LYS A NZ  
320  N NZ  B LYS A 41 ? 0.2310 0.1212 0.2177 -0.0735 -0.0107 -0.0160 41 LYS A NZ  
321  N N   . ALA A 42 ? 0.2709 0.2053 0.2273 -0.0192 0.0047  -0.0029 42 ALA A N   
322  C CA  . ALA A 42 ? 0.2972 0.2333 0.2424 -0.0153 0.0135  -0.0049 42 ALA A CA  
323  C C   . ALA A 42 ? 0.3243 0.2710 0.2575 -0.0130 0.0159  0.0078  42 ALA A C   
324  O O   . ALA A 42 ? 0.3333 0.2866 0.2482 -0.0113 0.0210  0.0072  42 ALA A O   
325  C CB  . ALA A 42 ? 0.2734 0.2057 0.2338 -0.0116 0.0215  -0.0053 42 ALA A CB  
326  N N   . ALA A 43 ? 0.3336 0.2803 0.2747 -0.0117 0.0124  0.0194  43 ALA A N   
327  C CA  . ALA A 43 ? 0.3805 0.3294 0.3090 -0.0066 0.0150  0.0346  43 ALA A CA  
328  C C   . ALA A 43 ? 0.4263 0.3917 0.3356 -0.0025 0.0051  0.0356  43 ALA A C   
329  O O   . ALA A 43 ? 0.4686 0.4396 0.3576 0.0039  0.0075  0.0471  43 ALA A O   
330  C CB  . ALA A 43 ? 0.3498 0.2894 0.2930 -0.0042 0.0149  0.0443  43 ALA A CB  
331  N N   . SER A 44 ? 0.4471 0.4230 0.3627 -0.0067 -0.0058 0.0245  44 SER A N   
332  C CA  . SER A 44 ? 0.4918 0.4921 0.3921 -0.0052 -0.0164 0.0213  44 SER A CA  
333  C C   . SER A 44 ? 0.5195 0.5265 0.3947 -0.0047 -0.0122 0.0164  44 SER A C   
334  O O   . SER A 44 ? 0.5433 0.5731 0.4036 -0.0061 -0.0207 0.0074  44 SER A O   
335  C CB  . SER A 44 ? 0.5007 0.5112 0.4110 -0.0163 -0.0256 0.0046  44 SER A CB  
336  O OG  . SER A 44 ? 0.5173 0.5213 0.4500 -0.0183 -0.0267 0.0077  44 SER A OG  
337  N N   . THR A 50 ? 0.4621 0.5647 0.3482 0.0907  -0.0597 0.0975  50 THR A N   
338  C CA  . THR A 50 ? 0.4415 0.5765 0.3545 0.0891  -0.0695 0.0850  50 THR A CA  
339  C C   . THR A 50 ? 0.4179 0.5209 0.3545 0.0866  -0.0607 0.0842  50 THR A C   
340  O O   . THR A 50 ? 0.4029 0.5233 0.3624 0.0750  -0.0639 0.0698  50 THR A O   
341  C CB  . THR A 50 ? 0.4652 0.6462 0.3752 0.1147  -0.0830 0.0940  50 THR A CB  
342  O OG1 . THR A 50 ? 0.5140 0.6624 0.4141 0.1416  -0.0765 0.1181  50 THR A OG1 
343  C CG2 . THR A 50 ? 0.4511 0.6756 0.3375 0.1172  -0.0944 0.0921  50 THR A CG2 
344  N N   . HIS A 51 ? 0.4326 0.4897 0.3630 0.0960  -0.0488 0.0990  51 HIS A N   
345  C CA  . HIS A 51 ? 0.4272 0.4517 0.3773 0.0924  -0.0395 0.0960  51 HIS A CA  
346  C C   . HIS A 51 ? 0.3941 0.4151 0.3576 0.0663  -0.0363 0.0784  51 HIS A C   
347  O O   . HIS A 51 ? 0.3721 0.3976 0.3564 0.0595  -0.0365 0.0680  51 HIS A O   
348  C CB  . HIS A 51 ? 0.4679 0.4398 0.4063 0.0988  -0.0251 0.1116  51 HIS A CB  
349  C CG  . HIS A 51 ? 0.5707 0.5359 0.4798 0.1165  -0.0243 0.1332  51 HIS A CG  
350  N ND1 . HIS A 51 ? 0.6784 0.6447 0.5792 0.1450  -0.0283 0.1497  51 HIS A ND1 
351  C CD2 . HIS A 51 ? 0.6213 0.5825 0.5057 0.1116  -0.0201 0.1418  51 HIS A CD2 
352  C CE1 . HIS A 51 ? 0.6714 0.6325 0.5418 0.1572  -0.0268 0.1698  51 HIS A CE1 
353  N NE2 . HIS A 51 ? 0.6763 0.6355 0.5359 0.1361  -0.0216 0.1648  51 HIS A NE2 
354  N N   . VAL A 52 ? 0.3770 0.3905 0.3267 0.0538  -0.0329 0.0759  52 VAL A N   
355  C CA  . VAL A 52 ? 0.3497 0.3549 0.3094 0.0336  -0.0289 0.0614  52 VAL A CA  
356  C C   . VAL A 52 ? 0.3229 0.3587 0.2952 0.0235  -0.0385 0.0473  52 VAL A C   
357  O O   . VAL A 52 ? 0.2958 0.3253 0.2835 0.0129  -0.0360 0.0391  52 VAL A O   
358  C CB  . VAL A 52 ? 0.3507 0.3436 0.2934 0.0250  -0.0225 0.0600  52 VAL A CB  
359  C CG1 . VAL A 52 ? 0.3191 0.3045 0.2736 0.0085  -0.0194 0.0448  52 VAL A CG1 
360  C CG2 . VAL A 52 ? 0.3764 0.3384 0.3110 0.0303  -0.0098 0.0741  52 VAL A CG2 
361  N N   . GLY A 53 ? 0.3122 0.3827 0.2773 0.0265  -0.0489 0.0450  53 GLY A N   
362  C CA  . GLY A 53 ? 0.2912 0.3933 0.2693 0.0126  -0.0568 0.0302  53 GLY A CA  
363  C C   . GLY A 53 ? 0.2682 0.3836 0.2690 0.0154  -0.0578 0.0300  53 GLY A C   
364  O O   . GLY A 53 ? 0.2269 0.3485 0.2411 -0.0006 -0.0572 0.0200  53 GLY A O   
365  N N   . HIS A 54 ? 0.2593 0.3786 0.2629 0.0369  -0.0585 0.0413  54 HIS A N   
366  C CA  . HIS A 54 ? 0.2513 0.3798 0.2760 0.0419  -0.0571 0.0397  54 HIS A CA  
367  C C   . HIS A 54 ? 0.2377 0.3324 0.2702 0.0316  -0.0472 0.0364  54 HIS A C   
368  O O   . HIS A 54 ? 0.2305 0.3391 0.2784 0.0221  -0.0464 0.0289  54 HIS A O   
369  C CB  . HIS A 54 ? 0.2583 0.3923 0.2832 0.0704  -0.0589 0.0512  54 HIS A CB  
370  C CG  . HIS A 54 ? 0.2696 0.4538 0.2934 0.0834  -0.0711 0.0527  54 HIS A CG  
371  N ND1 . HIS A 54 ? 0.2904 0.4761 0.2949 0.1057  -0.0756 0.0671  54 HIS A ND1 
372  C CD2 . HIS A 54 ? 0.2728 0.5126 0.3129 0.0773  -0.0798 0.0418  54 HIS A CD2 
373  C CE1 . HIS A 54 ? 0.2872 0.5309 0.2962 0.1147  -0.0883 0.0642  54 HIS A CE1 
374  N NE2 . HIS A 54 ? 0.3151 0.5940 0.3476 0.0963  -0.0909 0.0476  54 HIS A NE2 
375  N N   . GLY A 55 ? 0.2435 0.2985 0.2655 0.0324  -0.0395 0.0418  55 GLY A N   
376  C CA  . GLY A 55 ? 0.2328 0.2619 0.2621 0.0226  -0.0313 0.0374  55 GLY A CA  
377  C C   . GLY A 55 ? 0.2261 0.2617 0.2591 0.0039  -0.0321 0.0284  55 GLY A C   
378  O O   . GLY A 55 ? 0.2111 0.2468 0.2548 -0.0017 -0.0294 0.0244  55 GLY A O   
379  N N   . ILE A 56 ? 0.2169 0.2546 0.2390 -0.0049 -0.0348 0.0253  56 ILE A N   
380  C CA  . ILE A 56 ? 0.2276 0.2629 0.2508 -0.0223 -0.0344 0.0168  56 ILE A CA  
381  C C   . ILE A 56 ? 0.2163 0.2773 0.2533 -0.0314 -0.0373 0.0126  56 ILE A C   
382  O O   . ILE A 56 ? 0.1939 0.2451 0.2358 -0.0414 -0.0329 0.0111  56 ILE A O   
383  C CB  . ILE A 56 ? 0.2225 0.2584 0.2308 -0.0294 -0.0375 0.0108  56 ILE A CB  
384  C CG1 . ILE A 56 ? 0.2105 0.2199 0.2053 -0.0237 -0.0313 0.0140  56 ILE A CG1 
385  C CG2 . ILE A 56 ? 0.2820 0.3154 0.2926 -0.0487 -0.0373 0.0002  56 ILE A CG2 
386  C CD1 . ILE A 56 ? 0.2783 0.2908 0.2544 -0.0276 -0.0336 0.0071  56 ILE A CD1 
387  N N   . LYS A 57 ? 0.2306 0.3273 0.2735 -0.0266 -0.0441 0.0120  57 LYS A N   
388  C CA  . LYS A 57 ? 0.2295 0.3612 0.2878 -0.0362 -0.0463 0.0071  57 LYS A CA  
389  C C   . LYS A 57 ? 0.1912 0.3196 0.2603 -0.0312 -0.0403 0.0107  57 LYS A C   
390  O O   . LYS A 57 ? 0.1908 0.3241 0.2665 -0.0453 -0.0360 0.0089  57 LYS A O   
391  C CB  . LYS A 57 ? 0.2313 0.4109 0.2962 -0.0271 -0.0555 0.0053  57 LYS A CB  
392  C CG  . LYS A 57 ? 0.3346 0.5365 0.3936 -0.0420 -0.0628 -0.0046 57 LYS A CG  
393  C CD  . LYS A 57 ? 0.3400 0.5852 0.3955 -0.0266 -0.0745 -0.0045 57 LYS A CD  
394  C CE  . LYS A 57 ? 0.3730 0.6435 0.4238 -0.0474 -0.0814 -0.0196 57 LYS A CE  
395  N NZ  . LYS A 57 ? 0.4460 0.7724 0.4935 -0.0367 -0.0952 -0.0234 57 LYS A NZ  
396  N N   . HIS A 58 ? 0.1657 0.2832 0.2348 -0.0120 -0.0388 0.0158  58 HIS A N   
397  C CA  . HIS A 58 ? 0.1613 0.2773 0.2395 -0.0068 -0.0334 0.0156  58 HIS A CA  
398  C C   . HIS A 58 ? 0.1631 0.2517 0.2366 -0.0171 -0.0273 0.0159  58 HIS A C   
399  O O   . HIS A 58 ? 0.1727 0.2707 0.2519 -0.0208 -0.0237 0.0150  58 HIS A O   
400  C CB  . HIS A 58 ? 0.1219 0.2258 0.2008 0.0147  -0.0319 0.0181  58 HIS A CB  
401  C CG  . HIS A 58 ? 0.1445 0.2793 0.2312 0.0314  -0.0365 0.0186  58 HIS A CG  
402  N ND1 . HIS A 58 ? 0.1618 0.3334 0.2636 0.0345  -0.0363 0.0132  58 HIS A ND1 
403  C CD2 . HIS A 58 ? 0.1751 0.3140 0.2561 0.0475  -0.0416 0.0246  58 HIS A CD2 
404  C CE1 . HIS A 58 ? 0.2078 0.4055 0.3151 0.0535  -0.0414 0.0146  58 HIS A CE1 
405  N NE2 . HIS A 58 ? 0.2046 0.3823 0.2984 0.0623  -0.0453 0.0226  58 HIS A NE2 
406  N N   . LEU A 59 ? 0.1632 0.2214 0.2259 -0.0189 -0.0260 0.0176  59 LEU A N   
407  C CA  . LEU A 59 ? 0.1864 0.2232 0.2451 -0.0255 -0.0214 0.0181  59 LEU A CA  
408  C C   . LEU A 59 ? 0.1824 0.2226 0.2395 -0.0405 -0.0202 0.0188  59 LEU A C   
409  O O   . LEU A 59 ? 0.1980 0.2336 0.2545 -0.0430 -0.0164 0.0219  59 LEU A O   
410  C CB  . LEU A 59 ? 0.1821 0.1921 0.2310 -0.0242 -0.0200 0.0186  59 LEU A CB  
411  C CG  . LEU A 59 ? 0.1780 0.1777 0.2282 -0.0131 -0.0174 0.0192  59 LEU A CG  
412  C CD1 . LEU A 59 ? 0.1940 0.1746 0.2339 -0.0137 -0.0150 0.0204  59 LEU A CD1 
413  C CD2 . LEU A 59 ? 0.1581 0.1570 0.2166 -0.0100 -0.0138 0.0159  59 LEU A CD2 
414  N N   . GLU A 60 ? 0.1932 0.2411 0.2486 -0.0509 -0.0231 0.0160  60 GLU A N   
415  C CA  . GLU A 60 ? 0.2184 0.2633 0.2722 -0.0695 -0.0201 0.0157  60 GLU A CA  
416  C C   . GLU A 60 ? 0.2213 0.2952 0.2859 -0.0740 -0.0172 0.0186  60 GLU A C   
417  O O   . GLU A 60 ? 0.2273 0.2919 0.2885 -0.0835 -0.0109 0.0244  60 GLU A O   
418  C CB  . GLU A 60 ? 0.2399 0.2934 0.2920 -0.0820 -0.0244 0.0076  60 GLU A CB  
419  C CG  . GLU A 60 ? 0.2656 0.2872 0.3031 -0.0808 -0.0249 0.0034  60 GLU A CG  
420  C CD  . GLU A 60 ? 0.3458 0.3811 0.3789 -0.0913 -0.0307 -0.0080 60 GLU A CD  
421  O OE1 . GLU A 60 ? 0.4620 0.4729 0.4819 -0.0922 -0.0300 -0.0139 60 GLU A OE1 
422  O OE2 . GLU A 60 ? 0.4089 0.4836 0.4517 -0.0975 -0.0361 -0.0125 60 GLU A OE2 
423  N N   . ASP A 61 ? 0.1938 0.3031 0.2700 -0.0655 -0.0209 0.0155  61 ASP A N   
424  C CA  . ASP A 61 ? 0.2094 0.3524 0.2969 -0.0661 -0.0176 0.0162  61 ASP A CA  
425  C C   . ASP A 61 ? 0.1801 0.3119 0.2636 -0.0568 -0.0127 0.0205  61 ASP A C   
426  O O   . ASP A 61 ? 0.2041 0.3505 0.2886 -0.0641 -0.0069 0.0243  61 ASP A O   
427  C CB  . ASP A 61 ? 0.1911 0.3738 0.2921 -0.0521 -0.0229 0.0109  61 ASP A CB  
428  C CG  . ASP A 61 ? 0.2630 0.4780 0.3719 -0.0631 -0.0282 0.0056  61 ASP A CG  
429  O OD1 . ASP A 61 ? 0.2954 0.5035 0.4013 -0.0865 -0.0259 0.0040  61 ASP A OD1 
430  O OD2 . ASP A 61 ? 0.2780 0.5246 0.3956 -0.0479 -0.0347 0.0023  61 ASP A OD2 
431  N N   . ALA A 62 ? 0.1818 0.2918 0.2608 -0.0420 -0.0145 0.0195  62 ALA A N   
432  C CA  . ALA A 62 ? 0.1828 0.2870 0.2587 -0.0343 -0.0111 0.0202  62 ALA A CA  
433  C C   . ALA A 62 ? 0.1993 0.2861 0.2637 -0.0442 -0.0071 0.0289  62 ALA A C   
434  O O   . ALA A 62 ? 0.2020 0.3002 0.2627 -0.0440 -0.0031 0.0330  62 ALA A O   
435  C CB  . ALA A 62 ? 0.1578 0.2398 0.2324 -0.0214 -0.0131 0.0158  62 ALA A CB  
436  N N   . ILE A 63 ? 0.1992 0.2580 0.2560 -0.0512 -0.0076 0.0321  63 ILE A N   
437  C CA  . ILE A 63 ? 0.2191 0.2537 0.2632 -0.0567 -0.0031 0.0418  63 ILE A CA  
438  C C   . ILE A 63 ? 0.2394 0.2848 0.2817 -0.0721 0.0032  0.0492  63 ILE A C   
439  O O   . ILE A 63 ? 0.2456 0.2886 0.2783 -0.0716 0.0084  0.0599  63 ILE A O   
440  C CB  . ILE A 63 ? 0.2245 0.2234 0.2608 -0.0595 -0.0039 0.0411  63 ILE A CB  
441  C CG1 . ILE A 63 ? 0.2077 0.1990 0.2451 -0.0444 -0.0076 0.0358  63 ILE A CG1 
442  C CG2 . ILE A 63 ? 0.2592 0.2281 0.2818 -0.0644 0.0019  0.0518  63 ILE A CG2 
443  C CD1 . ILE A 63 ? 0.2120 0.1819 0.2453 -0.0456 -0.0091 0.0306  63 ILE A CD1 
444  N N   . LYS A 64 ? 0.2356 0.2979 0.2871 -0.0860 0.0030  0.0440  64 LYS A N   
445  C CA  . LYS A 64 ? 0.2607 0.3370 0.3131 -0.1056 0.0109  0.0502  64 LYS A CA  
446  C C   . LYS A 64 ? 0.2586 0.3692 0.3131 -0.0996 0.0154  0.0550  64 LYS A C   
447  O O   . LYS A 64 ? 0.2850 0.3918 0.3291 -0.1078 0.0239  0.0675  64 LYS A O   
448  C CB  . LYS A 64 ? 0.2630 0.3659 0.3299 -0.1212 0.0085  0.0398  64 LYS A CB  
449  C CG  . LYS A 64 ? 0.3216 0.4518 0.3955 -0.1446 0.0176  0.0434  64 LYS A CG  
450  C CD  . LYS A 64 ? 0.4384 0.5201 0.4954 -0.1636 0.0278  0.0553  64 LYS A CD  
451  C CE  . LYS A 64 ? 0.4806 0.5784 0.5426 -0.1950 0.0404  0.0603  64 LYS A CE  
452  N NZ  . LYS A 64 ? 0.5726 0.6687 0.6444 -0.2218 0.0398  0.0465  64 LYS A NZ  
453  N N   . HIS A 65 ? 0.2226 0.3653 0.2888 -0.0847 0.0105  0.0452  65 HIS A N   
454  C CA  . HIS A 65 ? 0.2348 0.4116 0.3031 -0.0777 0.0146  0.0454  65 HIS A CA  
455  C C   . HIS A 65 ? 0.2428 0.4056 0.2950 -0.0670 0.0164  0.0526  65 HIS A C   
456  O O   . HIS A 65 ? 0.2314 0.4144 0.2757 -0.0690 0.0233  0.0601  65 HIS A O   
457  C CB  . HIS A 65 ? 0.2294 0.4374 0.3135 -0.0620 0.0095  0.0311  65 HIS A CB  
458  C CG  . HIS A 65 ? 0.2464 0.4894 0.3473 -0.0700 0.0089  0.0255  65 HIS A CG  
459  N ND1 . HIS A 65 ? 0.2963 0.5827 0.4058 -0.0804 0.0164  0.0262  65 HIS A ND1 
460  C CD2 . HIS A 65 ? 0.2509 0.4978 0.3618 -0.0685 0.0016  0.0189  65 HIS A CD2 
461  C CE1 . HIS A 65 ? 0.2514 0.5702 0.3784 -0.0853 0.0132  0.0189  65 HIS A CE1 
462  N NE2 . HIS A 65 ? 0.2139 0.5096 0.3410 -0.0772 0.0034  0.0147  65 HIS A NE2 
463  N N   . GLY A 66 ? 0.2333 0.3679 0.2809 -0.0550 0.0101  0.0498  66 GLY A N   
464  C CA  . GLY A 66 ? 0.2615 0.3850 0.2945 -0.0453 0.0101  0.0567  66 GLY A CA  
465  C C   . GLY A 66 ? 0.3135 0.4171 0.3283 -0.0540 0.0171  0.0764  66 GLY A C   
466  O O   . GLY A 66 ? 0.3223 0.4384 0.3230 -0.0482 0.0207  0.0866  66 GLY A O   
467  N N   . GLU A 67 ? 0.3163 0.3869 0.3292 -0.0668 0.0193  0.0820  67 GLU A N   
468  C CA  . GLU A 67 ? 0.3860 0.4278 0.3811 -0.0761 0.0279  0.1010  67 GLU A CA  
469  C C   . GLU A 67 ? 0.4028 0.4724 0.3947 -0.0907 0.0383  0.1108  67 GLU A C   
470  O O   . GLU A 67 ? 0.4473 0.5027 0.4196 -0.0927 0.0466  0.1303  67 GLU A O   
471  C CB  . GLU A 67 ? 0.4090 0.4069 0.4035 -0.0884 0.0289  0.1004  67 GLU A CB  
472  C CG  . GLU A 67 ? 0.4377 0.4156 0.4344 -0.0719 0.0199  0.0908  67 GLU A CG  
473  C CD  . GLU A 67 ? 0.5940 0.5200 0.5792 -0.0736 0.0226  0.0959  67 GLU A CD  
474  O OE1 . GLU A 67 ? 0.6398 0.5439 0.6238 -0.0945 0.0287  0.0959  67 GLU A OE1 
475  O OE2 . GLU A 67 ? 0.5974 0.5065 0.5755 -0.0541 0.0190  0.0982  67 GLU A OE2 
476  N N   . GLU A 68 ? 0.3773 0.4882 0.3878 -0.0990 0.0384  0.0981  68 GLU A N   
477  C CA  . GLU A 68 ? 0.3915 0.5447 0.4047 -0.1104 0.0480  0.1023  68 GLU A CA  
478  C C   . GLU A 68 ? 0.3755 0.5692 0.3827 -0.0943 0.0489  0.1015  68 GLU A C   
479  O O   . GLU A 68 ? 0.3892 0.6206 0.3966 -0.1029 0.0584  0.1052  68 GLU A O   
480  C CB  . GLU A 68 ? 0.3612 0.5492 0.3996 -0.1234 0.0473  0.0870  68 GLU A CB  
481  C CG  . GLU A 68 ? 0.4189 0.5782 0.4614 -0.1475 0.0498  0.0881  68 GLU A CG  
482  C CD  . GLU A 68 ? 0.4431 0.6461 0.5108 -0.1630 0.0489  0.0735  68 GLU A CD  
483  O OE1 . GLU A 68 ? 0.5522 0.7385 0.6239 -0.1870 0.0517  0.0719  68 GLU A OE1 
484  O OE2 . GLU A 68 ? 0.5017 0.7567 0.5853 -0.1513 0.0458  0.0629  68 GLU A OE2 
485  N N   . GLY A 69 ? 0.3531 0.5434 0.3556 -0.0727 0.0400  0.0947  69 GLY A N   
486  C CA  . GLY A 69 ? 0.3620 0.5882 0.3555 -0.0582 0.0404  0.0919  69 GLY A CA  
487  C C   . GLY A 69 ? 0.3417 0.6085 0.3547 -0.0499 0.0371  0.0683  69 GLY A C   
488  O O   . GLY A 69 ? 0.3503 0.6540 0.3582 -0.0408 0.0395  0.0617  69 GLY A O   
489  N N   . HIS A 70 ? 0.3029 0.5628 0.3366 -0.0514 0.0319  0.0556  70 HIS A N   
490  C CA  . HIS A 70 ? 0.2634 0.5545 0.3153 -0.0405 0.0292  0.0351  70 HIS A CA  
491  C C   . HIS A 70 ? 0.2303 0.4944 0.2877 -0.0270 0.0194  0.0227  70 HIS A C   
492  O O   . HIS A 70 ? 0.1949 0.4434 0.2644 -0.0269 0.0148  0.0180  70 HIS A O   
493  C CB  . HIS A 70 ? 0.2571 0.5701 0.3278 -0.0507 0.0320  0.0321  70 HIS A CB  
494  C CG  . HIS A 70 ? 0.2659 0.6144 0.3344 -0.0663 0.0439  0.0419  70 HIS A CG  
495  N ND1 . HIS A 70 ? 0.2945 0.6373 0.3654 -0.0904 0.0498  0.0540  70 HIS A ND1 
496  C CD2 . HIS A 70 ? 0.2371 0.6258 0.2991 -0.0634 0.0525  0.0417  70 HIS A CD2 
497  C CE1 . HIS A 70 ? 0.3004 0.6783 0.3679 -0.1031 0.0625  0.0623  70 HIS A CE1 
498  N NE2 . HIS A 70 ? 0.3515 0.7595 0.4127 -0.0861 0.0644  0.0558  70 HIS A NE2 
499  N N   . VAL A 71 ? 0.2130 0.4761 0.2608 -0.0161 0.0167  0.0169  71 VAL A N   
500  C CA  . VAL A 71 ? 0.2139 0.4521 0.2667 -0.0066 0.0090  0.0050  71 VAL A CA  
501  C C   . VAL A 71 ? 0.2071 0.4508 0.2764 0.0034  0.0077  -0.0146 71 VAL A C   
502  O O   . VAL A 71 ? 0.2101 0.4261 0.2859 0.0073  0.0033  -0.0207 71 VAL A O   
503  C CB  . VAL A 71 ? 0.2289 0.4726 0.2685 0.0003  0.0063  0.0021  71 VAL A CB  
504  C CG1 . VAL A 71 ? 0.2498 0.5331 0.2870 0.0077  0.0093  -0.0129 71 VAL A CG1 
505  C CG2 . VAL A 71 ? 0.2008 0.4160 0.2462 0.0047  -0.0009 -0.0067 71 VAL A CG2 
506  N N   . GLY A 72 ? 0.2053 0.4837 0.2799 0.0088  0.0126  -0.0239 72 GLY A N   
507  C CA  . GLY A 72 ? 0.2030 0.4824 0.2928 0.0218  0.0121  -0.0407 72 GLY A CA  
508  C C   . GLY A 72 ? 0.2228 0.4858 0.3231 0.0195  0.0089  -0.0320 72 GLY A C   
509  O O   . GLY A 72 ? 0.1848 0.4212 0.2922 0.0294  0.0052  -0.0383 72 GLY A O   
510  N N   . VAL A 73 ? 0.1654 0.4444 0.2656 0.0059  0.0108  -0.0179 73 VAL A N   
511  C CA  . VAL A 73 ? 0.1750 0.4510 0.2861 0.0029  0.0071  -0.0131 73 VAL A CA  
512  C C   . VAL A 73 ? 0.1586 0.3882 0.2628 -0.0018 0.0011  -0.0063 73 VAL A C   
513  O O   . VAL A 73 ? 0.1508 0.3657 0.2607 0.0054  -0.0037 -0.0081 73 VAL A O   
514  C CB  . VAL A 73 ? 0.1792 0.4871 0.2947 -0.0143 0.0114  -0.0037 73 VAL A CB  
515  C CG1 . VAL A 73 ? 0.1792 0.4884 0.3063 -0.0173 0.0053  -0.0025 73 VAL A CG1 
516  C CG2 . VAL A 73 ? 0.1448 0.5066 0.2686 -0.0094 0.0191  -0.0111 73 VAL A CG2 
517  N N   . ALA A 74 ? 0.1471 0.3562 0.2380 -0.0110 0.0019  0.0016  74 ALA A N   
518  C CA  . ALA A 74 ? 0.1562 0.3251 0.2410 -0.0131 -0.0027 0.0059  74 ALA A CA  
519  C C   . ALA A 74 ? 0.1547 0.3048 0.2436 0.0002  -0.0054 -0.0050 74 ALA A C   
520  O O   . ALA A 74 ? 0.1931 0.3198 0.2830 0.0013  -0.0085 -0.0032 74 ALA A O   
521  C CB  . ALA A 74 ? 0.1673 0.3226 0.2384 -0.0200 -0.0011 0.0152  74 ALA A CB  
522  N N   . THR A 75 ? 0.1590 0.3200 0.2500 0.0092  -0.0033 -0.0171 75 THR A N   
523  C CA  . THR A 75 ? 0.1699 0.3096 0.2656 0.0188  -0.0036 -0.0297 75 THR A CA  
524  C C   . THR A 75 ? 0.1678 0.2964 0.2712 0.0293  -0.0041 -0.0306 75 THR A C   
525  O O   . THR A 75 ? 0.1694 0.2655 0.2720 0.0316  -0.0048 -0.0293 75 THR A O   
526  C CB  . THR A 75 ? 0.1665 0.3225 0.2629 0.0248  -0.0006 -0.0463 75 THR A CB  
527  O OG1 . THR A 75 ? 0.2080 0.3734 0.2951 0.0176  -0.0017 -0.0443 75 THR A OG1 
528  C CG2 . THR A 75 ? 0.2032 0.3301 0.3054 0.0312  0.0010  -0.0619 75 THR A CG2 
529  N N   . LYS A 76 ? 0.1647 0.3230 0.2750 0.0364  -0.0033 -0.0316 76 LYS A N   
530  C CA  . LYS A 76 ? 0.1623 0.3192 0.2799 0.0511  -0.0047 -0.0317 76 LYS A CA  
531  C C   . LYS A 76 ? 0.1653 0.3069 0.2786 0.0446  -0.0100 -0.0179 76 LYS A C   
532  O O   . LYS A 76 ? 0.1620 0.2800 0.2736 0.0549  -0.0117 -0.0145 76 LYS A O   
533  C CB  . LYS A 76 ? 0.1458 0.3511 0.2738 0.0587  -0.0034 -0.0350 76 LYS A CB  
534  C CG  . LYS A 76 ? 0.1755 0.3899 0.3117 0.0747  -0.0071 -0.0319 76 LYS A CG  
535  C CD  . LYS A 76 ? 0.2572 0.4348 0.3924 0.0962  -0.0050 -0.0383 76 LYS A CD  
536  C CE  . LYS A 76 ? 0.3001 0.4866 0.4411 0.1187  -0.0089 -0.0327 76 LYS A CE  
537  N NZ  . LYS A 76 ? 0.3419 0.4840 0.4796 0.1403  -0.0043 -0.0380 76 LYS A NZ  
538  N N   . HIS A 77 ? 0.1524 0.3050 0.2620 0.0277  -0.0118 -0.0100 77 HIS A N   
539  C CA  . HIS A 77 ? 0.1536 0.2941 0.2586 0.0218  -0.0168 -0.0009 77 HIS A CA  
540  C C   . HIS A 77 ? 0.1527 0.2510 0.2483 0.0214  -0.0164 0.0014  77 HIS A C   
541  O O   . HIS A 77 ? 0.1770 0.2595 0.2678 0.0262  -0.0189 0.0066  77 HIS A O   
542  C CB  . HIS A 77 ? 0.1316 0.2866 0.2344 0.0020  -0.0175 0.0046  77 HIS A CB  
543  C CG  . HIS A 77 ? 0.1479 0.3457 0.2614 -0.0014 -0.0193 0.0039  77 HIS A CG  
544  N ND1 . HIS A 77 ? 0.1763 0.3890 0.2941 0.0043  -0.0259 0.0044  77 HIS A ND1 
545  C CD2 . HIS A 77 ? 0.1332 0.3675 0.2547 -0.0108 -0.0152 0.0026  77 HIS A CD2 
546  C CE1 . HIS A 77 ? 0.1686 0.4283 0.2992 -0.0017 -0.0265 0.0015  77 HIS A CE1 
547  N NE2 . HIS A 77 ? 0.1434 0.4155 0.2768 -0.0124 -0.0192 0.0006  77 HIS A NE2 
548  N N   . ALA A 78 ? 0.1514 0.2359 0.2439 0.0159  -0.0129 -0.0024 78 ALA A N   
549  C CA  . ALA A 78 ? 0.1622 0.2138 0.2497 0.0147  -0.0113 -0.0025 78 ALA A CA  
550  C C   . ALA A 78 ? 0.1974 0.2282 0.2874 0.0269  -0.0083 -0.0065 78 ALA A C   
551  O O   . ALA A 78 ? 0.2088 0.2139 0.2932 0.0269  -0.0069 -0.0010 78 ALA A O   
552  C CB  . ALA A 78 ? 0.1551 0.2060 0.2413 0.0076  -0.0094 -0.0071 78 ALA A CB  
553  N N   . GLN A 79 ? 0.1966 0.2354 0.2935 0.0374  -0.0059 -0.0157 79 GLN A N   
554  C CA  . GLN A 79 ? 0.2414 0.2528 0.3390 0.0512  -0.0020 -0.0178 79 GLN A CA  
555  C C   . GLN A 79 ? 0.2484 0.2549 0.3404 0.0621  -0.0056 -0.0035 79 GLN A C   
556  O O   . GLN A 79 ? 0.2582 0.2311 0.3430 0.0675  -0.0022 0.0034  79 GLN A O   
557  C CB  . GLN A 79 ? 0.2507 0.2745 0.3565 0.0641  0.0009  -0.0313 79 GLN A CB  
558  C CG  . GLN A 79 ? 0.3009 0.3286 0.4095 0.0544  0.0044  -0.0477 79 GLN A CG  
559  C CD  . GLN A 79 ? 0.3332 0.3767 0.4481 0.0666  0.0080  -0.0648 79 GLN A CD  
560  O OE1 . GLN A 79 ? 0.3229 0.3978 0.4419 0.0775  0.0065  -0.0637 79 GLN A OE1 
561  N NE2 . GLN A 79 ? 0.3663 0.3912 0.4829 0.0637  0.0132  -0.0829 79 GLN A NE2 
562  N N   . GLU A 80 ? 0.2330 0.2762 0.3279 0.0651  -0.0119 0.0008  80 GLU A N   
563  C CA  . GLU A 80 ? 0.2431 0.2938 0.3329 0.0755  -0.0176 0.0125  80 GLU A CA  
564  C C   . GLU A 80 ? 0.2261 0.2555 0.3026 0.0643  -0.0187 0.0219  80 GLU A C   
565  O O   . GLU A 80 ? 0.2345 0.2464 0.3005 0.0752  -0.0191 0.0323  80 GLU A O   
566  C CB  . GLU A 80 ? 0.2461 0.3485 0.3448 0.0746  -0.0243 0.0115  80 GLU A CB  
567  C CG  . GLU A 80 ? 0.2744 0.4043 0.3865 0.0898  -0.0225 0.0028  80 GLU A CG  
568  C CD  . GLU A 80 ? 0.3638 0.4766 0.4750 0.1178  -0.0215 0.0056  80 GLU A CD  
569  O OE1 . GLU A 80 ? 0.4628 0.5607 0.5786 0.1294  -0.0150 -0.0040 80 GLU A OE1 
570  O OE2 . GLU A 80 ? 0.4162 0.5289 0.5205 0.1297  -0.0269 0.0172  80 GLU A OE2 
571  N N   . ALA A 81 ? 0.2136 0.2430 0.2888 0.0448  -0.0183 0.0190  81 ALA A N   
572  C CA  . ALA A 81 ? 0.2068 0.2170 0.2700 0.0354  -0.0180 0.0253  81 ALA A CA  
573  C C   . ALA A 81 ? 0.2333 0.2050 0.2900 0.0395  -0.0104 0.0291  81 ALA A C   
574  O O   . ALA A 81 ? 0.2594 0.2171 0.3036 0.0425  -0.0096 0.0390  81 ALA A O   
575  C CB  . ALA A 81 ? 0.1819 0.1948 0.2459 0.0180  -0.0175 0.0206  81 ALA A CB  
576  N N   . ILE A 82 ? 0.2370 0.1929 0.3016 0.0388  -0.0041 0.0209  82 ILE A N   
577  C CA  . ILE A 82 ? 0.2656 0.1841 0.3265 0.0385  0.0050  0.0227  82 ILE A CA  
578  C C   . ILE A 82 ? 0.3135 0.2112 0.3648 0.0558  0.0069  0.0350  82 ILE A C   
579  O O   . ILE A 82 ? 0.3450 0.2156 0.3842 0.0545  0.0129  0.0459  82 ILE A O   
580  C CB  . ILE A 82 ? 0.2608 0.1699 0.3337 0.0340  0.0108  0.0074  82 ILE A CB  
581  C CG1 . ILE A 82 ? 0.2330 0.1635 0.3123 0.0188  0.0087  -0.0017 82 ILE A CG1 
582  C CG2 . ILE A 82 ? 0.3235 0.1879 0.3945 0.0320  0.0225  0.0074  82 ILE A CG2 
583  C CD1 . ILE A 82 ? 0.2661 0.2048 0.3569 0.0157  0.0108  -0.0196 82 ILE A CD1 
584  N N   . GLU A 83 ? 0.3222 0.2322 0.3779 0.0735  0.0030  0.0342  83 GLU A N   
585  C CA  . GLU A 83 ? 0.3871 0.2787 0.4327 0.0961  0.0040  0.0480  83 GLU A CA  
586  C C   . GLU A 83 ? 0.3944 0.2921 0.4223 0.0986  -0.0007 0.0652  83 GLU A C   
587  O O   . GLU A 83 ? 0.4156 0.2811 0.4272 0.1076  0.0050  0.0808  83 GLU A O   
588  C CB  . GLU A 83 ? 0.3975 0.3182 0.4527 0.1170  -0.0022 0.0438  83 GLU A CB  
589  C CG  . GLU A 83 ? 0.4988 0.4014 0.5653 0.1229  0.0050  0.0289  83 GLU A CG  
590  C CD  . GLU A 83 ? 0.6102 0.5522 0.6891 0.1415  -0.0003 0.0209  83 GLU A CD  
591  O OE1 . GLU A 83 ? 0.6736 0.6385 0.7503 0.1624  -0.0071 0.0316  83 GLU A OE1 
592  O OE2 . GLU A 83 ? 0.6428 0.5977 0.7338 0.1357  0.0023  0.0032  83 GLU A OE2 
593  N N   . HIS A 84 ? 0.3569 0.2957 0.3865 0.0898  -0.0104 0.0621  84 HIS A N   
594  C CA  . HIS A 84 ? 0.3595 0.3119 0.3730 0.0908  -0.0162 0.0732  84 HIS A CA  
595  C C   . HIS A 84 ? 0.3801 0.3047 0.3809 0.0758  -0.0082 0.0778  84 HIS A C   
596  O O   . HIS A 84 ? 0.4172 0.3282 0.3984 0.0830  -0.0058 0.0926  84 HIS A O   
597  C CB  . HIS A 84 ? 0.3195 0.3201 0.3403 0.0810  -0.0272 0.0641  84 HIS A CB  
598  C CG  . HIS A 84 ? 0.3008 0.3414 0.3308 0.0974  -0.0362 0.0632  84 HIS A CG  
599  N ND1 . HIS A 84 ? 0.2712 0.3313 0.2906 0.1175  -0.0437 0.0745  84 HIS A ND1 
600  C CD2 . HIS A 84 ? 0.2819 0.3520 0.3313 0.0976  -0.0387 0.0523  84 HIS A CD2 
601  C CE1 . HIS A 84 ? 0.3084 0.4113 0.3428 0.1295  -0.0510 0.0694  84 HIS A CE1 
602  N NE2 . HIS A 84 ? 0.2510 0.3611 0.3040 0.1162  -0.0475 0.0556  84 HIS A NE2 
603  N N   . LEU A 85 ? 0.3454 0.2649 0.3562 0.0566  -0.0038 0.0660  85 LEU A N   
604  C CA  . LEU A 85 ? 0.3643 0.2643 0.3663 0.0434  0.0043  0.0686  85 LEU A CA  
605  C C   . LEU A 85 ? 0.4139 0.2734 0.4077 0.0476  0.0167  0.0798  85 LEU A C   
606  O O   . LEU A 85 ? 0.4294 0.2758 0.4077 0.0435  0.0233  0.0901  85 LEU A O   
607  C CB  . LEU A 85 ? 0.3241 0.2284 0.3405 0.0258  0.0068  0.0540  85 LEU A CB  
608  C CG  . LEU A 85 ? 0.3189 0.2532 0.3389 0.0190  -0.0024 0.0459  85 LEU A CG  
609  C CD1 . LEU A 85 ? 0.3264 0.2656 0.3615 0.0089  -0.0012 0.0339  85 LEU A CD1 
610  C CD2 . LEU A 85 ? 0.3076 0.2470 0.3123 0.0139  -0.0037 0.0486  85 LEU A CD2 
611  N N   . ARG A 86 ? 0.4513 0.2894 0.4548 0.0544  0.0212  0.0768  86 ARG A N   
612  C CA  . ARG A 86 ? 0.5421 0.3327 0.5379 0.0565  0.0350  0.0868  86 ARG A CA  
613  C C   . ARG A 86 ? 0.6134 0.3901 0.5859 0.0775  0.0348  0.1100  86 ARG A C   
614  O O   . ARG A 86 ? 0.6761 0.4174 0.6324 0.0758  0.0469  0.1255  86 ARG A O   
615  C CB  . ARG A 86 ? 0.5508 0.3178 0.5620 0.0591  0.0403  0.0746  86 ARG A CB  
616  C CG  . ARG A 86 ? 0.5451 0.3174 0.5752 0.0365  0.0445  0.0539  86 ARG A CG  
617  C CD  . ARG A 86 ? 0.6204 0.3652 0.6631 0.0359  0.0519  0.0392  86 ARG A CD  
618  N NE  . ARG A 86 ? 0.6718 0.4273 0.7308 0.0122  0.0557  0.0196  86 ARG A NE  
619  C CZ  . ARG A 86 ? 0.7213 0.4581 0.7820 -0.0076 0.0674  0.0189  86 ARG A CZ  
620  N NH1 . ARG A 86 ? 0.6612 0.4185 0.7391 -0.0275 0.0688  -0.0004 86 ARG A NH1 
621  N NH2 . ARG A 86 ? 0.7645 0.4656 0.8094 -0.0073 0.0780  0.0383  86 ARG A NH2 
622  N N   . ALA A 87 ? 0.6279 0.4345 0.5983 0.0976  0.0217  0.1133  87 ALA A N   
623  C CA  . ALA A 87 ? 0.6851 0.4938 0.6321 0.1202  0.0175  0.1352  87 ALA A CA  
624  C C   . ALA A 87 ? 0.7026 0.5157 0.6277 0.1098  0.0201  0.1466  87 ALA A C   
625  O O   . ALA A 87 ? 0.7500 0.5405 0.6505 0.1219  0.0261  0.1688  87 ALA A O   
626  C CB  . ALA A 87 ? 0.6631 0.5238 0.6165 0.1380  0.0001  0.1312  87 ALA A CB  
627  N N   . SER A 88 ? 0.6868 0.5264 0.6197 0.0884  0.0170  0.1317  88 SER A N   
628  C CA  . SER A 88 ? 0.6976 0.5512 0.6110 0.0799  0.0176  0.1371  88 SER A CA  
629  C C   . SER A 88 ? 0.7207 0.5429 0.6282 0.0628  0.0350  0.1416  88 SER A C   
630  O O   . SER A 88 ? 0.7685 0.5634 0.6548 0.0687  0.0456  0.1619  88 SER A O   
631  C CB  . SER A 88 ? 0.6532 0.5498 0.5766 0.0679  0.0058  0.1179  88 SER A CB  
632  O OG  . SER A 88 ? 0.6596 0.5588 0.5739 0.0525  0.0114  0.1139  88 SER A OG  
633  N N   . SER B 1  ? 0.3672 0.1889 0.2149 0.0670  0.0119  0.0200  1  SER B N   
634  C CA  . SER B 1  ? 0.3847 0.2149 0.2015 0.0621  0.0069  0.0217  1  SER B CA  
635  C C   . SER B 1  ? 0.4186 0.2261 0.2267 0.0523  0.0284  0.0233  1  SER B C   
636  O O   . SER B 1  ? 0.3922 0.1880 0.2284 0.0458  0.0411  0.0213  1  SER B O   
637  C CB  . SER B 1  ? 0.3563 0.2175 0.1885 0.0520  -0.0040 0.0056  1  SER B CB  
638  O OG  . SER B 1  ? 0.3591 0.2473 0.2125 0.0596  -0.0188 0.0058  1  SER B OG  
639  N N   . GLY B 2  ? 0.4453 0.2462 0.2156 0.0519  0.0323  0.0266  2  GLY B N   
640  C CA  . GLY B 2  ? 0.4782 0.2607 0.2400 0.0462  0.0584  0.0317  2  GLY B CA  
641  C C   . GLY B 2  ? 0.4418 0.2410 0.2359 0.0330  0.0636  0.0138  2  GLY B C   
642  O O   . GLY B 2  ? 0.3953 0.2160 0.2064 0.0287  0.0469  -0.0015 2  GLY B O   
643  N N   . HIS B 3  ? 0.4583 0.2488 0.2596 0.0281  0.0883  0.0182  3  HIS B N   
644  C CA  . HIS B 3  ? 0.4442 0.2509 0.2818 0.0180  0.0940  0.0042  3  HIS B CA  
645  C C   . HIS B 3  ? 0.4353 0.2545 0.2562 0.0185  0.0803  -0.0126 3  HIS B C   
646  O O   . HIS B 3  ? 0.4048 0.2411 0.2562 0.0121  0.0690  -0.0256 3  HIS B O   
647  C CB  . HIS B 3  ? 0.4738 0.2733 0.3213 0.0159  0.1254  0.0153  3  HIS B CB  
648  C CG  . HIS B 3  ? 0.5056 0.3249 0.3933 0.0087  0.1317  0.0030  3  HIS B CG  
649  N ND1 . HIS B 3  ? 0.5048 0.3384 0.4525 -0.0027 0.1267  -0.0026 3  HIS B ND1 
650  C CD2 . HIS B 3  ? 0.5578 0.3830 0.4336 0.0135  0.1418  -0.0048 3  HIS B CD2 
651  C CE1 . HIS B 3  ? 0.5236 0.3756 0.4969 -0.0044 0.1315  -0.0118 3  HIS B CE1 
652  N NE2 . HIS B 3  ? 0.5275 0.3739 0.4595 0.0059  0.1425  -0.0129 3  HIS B NE2 
653  N N   . THR B 4  ? 0.4758 0.2820 0.2451 0.0265  0.0812  -0.0121 4  THR B N   
654  C CA  . THR B 4  ? 0.4708 0.2795 0.2212 0.0259  0.0673  -0.0291 4  THR B CA  
655  C C   . THR B 4  ? 0.4337 0.2597 0.1998 0.0200  0.0377  -0.0369 4  THR B C   
656  O O   . THR B 4  ? 0.4036 0.2390 0.1876 0.0131  0.0289  -0.0494 4  THR B O   
657  C CB  . THR B 4  ? 0.5297 0.3150 0.2155 0.0367  0.0698  -0.0298 4  THR B CB  
658  O OG1 . THR B 4  ? 0.5737 0.3470 0.2497 0.0438  0.1044  -0.0206 4  THR B OG1 
659  C CG2 . THR B 4  ? 0.5606 0.3399 0.2259 0.0347  0.0518  -0.0513 4  THR B CG2 
660  N N   . ALA B 5  ? 0.4231 0.2539 0.1852 0.0239  0.0242  -0.0273 5  ALA B N   
661  C CA  . ALA B 5  ? 0.3961 0.2497 0.1785 0.0204  -0.0006 -0.0312 5  ALA B CA  
662  C C   . ALA B 5  ? 0.3600 0.2309 0.1889 0.0138  0.0034  -0.0361 5  ALA B C   
663  O O   . ALA B 5  ? 0.3351 0.2222 0.1821 0.0074  -0.0075 -0.0431 5  ALA B O   
664  C CB  . ALA B 5  ? 0.4235 0.2823 0.2020 0.0304  -0.0115 -0.0174 5  ALA B CB  
665  N N   . HIS B 6  ? 0.3428 0.2083 0.1906 0.0153  0.0184  -0.0319 6  HIS B N   
666  C CA  . HIS B 6  ? 0.2914 0.1703 0.1763 0.0109  0.0186  -0.0393 6  HIS B CA  
667  C C   . HIS B 6  ? 0.2928 0.1758 0.1887 0.0041  0.0219  -0.0492 6  HIS B C   
668  O O   . HIS B 6  ? 0.2756 0.1726 0.1884 0.0018  0.0142  -0.0544 6  HIS B O   
669  C CB  . HIS B 6  ? 0.2932 0.1610 0.1969 0.0122  0.0287  -0.0361 6  HIS B CB  
670  C CG  . HIS B 6  ? 0.3116 0.1730 0.2117 0.0214  0.0240  -0.0282 6  HIS B CG  
671  N ND1 . HIS B 6  ? 0.2950 0.1720 0.2033 0.0287  0.0125  -0.0310 6  HIS B ND1 
672  C CD2 . HIS B 6  ? 0.3238 0.1631 0.2155 0.0263  0.0318  -0.0163 6  HIS B CD2 
673  C CE1 . HIS B 6  ? 0.3476 0.2124 0.2521 0.0396  0.0122  -0.0228 6  HIS B CE1 
674  N NE2 . HIS B 6  ? 0.3045 0.1447 0.1973 0.0378  0.0224  -0.0132 6  HIS B NE2 
675  N N   . VAL B 7  ? 0.3192 0.1896 0.2035 0.0034  0.0349  -0.0501 7  VAL B N   
676  C CA  . VAL B 7  ? 0.3304 0.2036 0.2262 0.0004  0.0378  -0.0590 7  VAL B CA  
677  C C   . VAL B 7  ? 0.3501 0.2251 0.2330 -0.0026 0.0221  -0.0648 7  VAL B C   
678  O O   . VAL B 7  ? 0.3340 0.2159 0.2345 -0.0057 0.0174  -0.0692 7  VAL B O   
679  C CB  . VAL B 7  ? 0.3610 0.2216 0.2474 0.0042  0.0582  -0.0586 7  VAL B CB  
680  C CG1 . VAL B 7  ? 0.3825 0.2437 0.2783 0.0051  0.0598  -0.0682 7  VAL B CG1 
681  C CG2 . VAL B 7  ? 0.3541 0.2189 0.2727 0.0027  0.0748  -0.0499 7  VAL B CG2 
682  N N   . ASP B 8  ? 0.3555 0.2219 0.2075 -0.0021 0.0130  -0.0641 8  ASP B N   
683  C CA  . ASP B 8  ? 0.3654 0.2316 0.2110 -0.0088 -0.0049 -0.0704 8  ASP B CA  
684  C C   . ASP B 8  ? 0.3262 0.2181 0.2049 -0.0145 -0.0157 -0.0650 8  ASP B C   
685  O O   . ASP B 8  ? 0.3011 0.1965 0.1939 -0.0220 -0.0226 -0.0670 8  ASP B O   
686  C CB  . ASP B 8  ? 0.3847 0.2404 0.1944 -0.0075 -0.0186 -0.0711 8  ASP B CB  
687  C CG  . ASP B 8  ? 0.4979 0.3223 0.2606 -0.0002 -0.0094 -0.0790 8  ASP B CG  
688  O OD1 . ASP B 8  ? 0.5182 0.3301 0.2814 0.0028  0.0072  -0.0855 8  ASP B OD1 
689  O OD2 . ASP B 8  ? 0.5402 0.3537 0.2637 0.0049  -0.0197 -0.0780 8  ASP B OD2 
690  N N   . GLU B 9  ? 0.2995 0.2076 0.1891 -0.0093 -0.0157 -0.0566 9  GLU B N   
691  C CA  . GLU B 9  ? 0.2955 0.2289 0.2135 -0.0095 -0.0197 -0.0508 9  GLU B CA  
692  C C   . GLU B 9  ? 0.2653 0.2003 0.1981 -0.0088 -0.0111 -0.0535 9  GLU B C   
693  O O   . GLU B 9  ? 0.2597 0.2085 0.2070 -0.0113 -0.0133 -0.0493 9  GLU B O   
694  C CB  . GLU B 9  ? 0.2956 0.2406 0.2185 0.0010  -0.0188 -0.0433 9  GLU B CB  
695  C CG  . GLU B 9  ? 0.4153 0.3700 0.3324 0.0025  -0.0328 -0.0368 9  GLU B CG  
696  C CD  . GLU B 9  ? 0.5145 0.5022 0.4632 -0.0015 -0.0421 -0.0303 9  GLU B CD  
697  O OE1 . GLU B 9  ? 0.5864 0.5941 0.5539 0.0091  -0.0360 -0.0232 9  GLU B OE1 
698  O OE2 . GLU B 9  ? 0.5468 0.5392 0.5039 -0.0150 -0.0533 -0.0320 9  GLU B OE2 
699  N N   . ALA B 10 ? 0.2535 0.1766 0.1850 -0.0047 -0.0017 -0.0583 10 ALA B N   
700  C CA  . ALA B 10 ? 0.2269 0.1519 0.1718 -0.0032 0.0011  -0.0621 10 ALA B CA  
701  C C   . ALA B 10 ? 0.2437 0.1643 0.1896 -0.0083 -0.0012 -0.0630 10 ALA B C   
702  O O   . ALA B 10 ? 0.2358 0.1634 0.1895 -0.0069 -0.0034 -0.0597 10 ALA B O   
703  C CB  . ALA B 10 ? 0.2362 0.1517 0.1891 -0.0012 0.0087  -0.0672 10 ALA B CB  
704  N N   . VAL B 11 ? 0.2528 0.1572 0.1865 -0.0121 0.0000  -0.0673 11 VAL B N   
705  C CA  . VAL B 11 ? 0.2794 0.1709 0.2126 -0.0156 -0.0024 -0.0699 11 VAL B CA  
706  C C   . VAL B 11 ? 0.2843 0.1832 0.2247 -0.0244 -0.0125 -0.0625 11 VAL B C   
707  O O   . VAL B 11 ? 0.2849 0.1821 0.2356 -0.0260 -0.0129 -0.0571 11 VAL B O   
708  C CB  . VAL B 11 ? 0.2896 0.1556 0.1992 -0.0153 0.0010  -0.0793 11 VAL B CB  
709  C CG1 . VAL B 11 ? 0.3358 0.1798 0.2405 -0.0198 -0.0054 -0.0842 11 VAL B CG1 
710  C CG2 . VAL B 11 ? 0.2966 0.1598 0.2096 -0.0059 0.0172  -0.0824 11 VAL B CG2 
711  N N   . LYS B 12 ? 0.3037 0.2126 0.2423 -0.0299 -0.0204 -0.0596 12 LYS B N   
712  C CA  . LYS B 12 ? 0.3241 0.2473 0.2814 -0.0406 -0.0297 -0.0503 12 LYS B CA  
713  C C   . LYS B 12 ? 0.3047 0.2506 0.2810 -0.0355 -0.0208 -0.0371 12 LYS B C   
714  O O   . LYS B 12 ? 0.2851 0.2339 0.2766 -0.0426 -0.0203 -0.0268 12 LYS B O   
715  C CB  . LYS B 12 ? 0.3294 0.2694 0.2886 -0.0429 -0.0401 -0.0480 12 LYS B CB  
716  C CG  . LYS B 12 ? 0.3926 0.3609 0.3855 -0.0532 -0.0485 -0.0352 12 LYS B CG  
717  C CD  . LYS B 12 ? 0.4110 0.4037 0.4111 -0.0499 -0.0592 -0.0315 12 LYS B CD  
718  C CE  . LYS B 12 ? 0.4238 0.4438 0.4365 -0.0346 -0.0455 -0.0213 12 LYS B CE  
719  N NZ  . LYS B 12 ? 0.4914 0.5463 0.5324 -0.0340 -0.0559 -0.0109 12 LYS B NZ  
720  N N   . HIS B 13 ? 0.2632 0.2222 0.2356 -0.0229 -0.0138 -0.0369 13 HIS B N   
721  C CA  . HIS B 13 ? 0.2610 0.2370 0.2392 -0.0142 -0.0057 -0.0273 13 HIS B CA  
722  C C   . HIS B 13 ? 0.2729 0.2338 0.2436 -0.0110 -0.0031 -0.0276 13 HIS B C   
723  O O   . HIS B 13 ? 0.2956 0.2635 0.2693 -0.0093 0.0020  -0.0147 13 HIS B O   
724  C CB  . HIS B 13 ? 0.2556 0.2405 0.2259 0.0000  -0.0016 -0.0313 13 HIS B CB  
725  C CG  . HIS B 13 ? 0.2747 0.2799 0.2566 0.0016  -0.0025 -0.0252 13 HIS B CG  
726  N ND1 . HIS B 13 ? 0.2985 0.3322 0.3016 0.0017  0.0023  -0.0104 13 HIS B ND1 
727  C CD2 . HIS B 13 ? 0.2761 0.2791 0.2547 0.0037  -0.0075 -0.0292 13 HIS B CD2 
728  C CE1 . HIS B 13 ? 0.3284 0.3799 0.3448 0.0046  -0.0017 -0.0070 13 HIS B CE1 
729  N NE2 . HIS B 13 ? 0.2932 0.3243 0.2913 0.0070  -0.0084 -0.0183 13 HIS B NE2 
730  N N   . ALA B 14 ? 0.2526 0.1946 0.2154 -0.0089 -0.0055 -0.0397 14 ALA B N   
731  C CA  . ALA B 14 ? 0.2485 0.1800 0.2088 -0.0029 -0.0057 -0.0396 14 ALA B CA  
732  C C   . ALA B 14 ? 0.2555 0.1731 0.2209 -0.0115 -0.0062 -0.0303 14 ALA B C   
733  O O   . ALA B 14 ? 0.2847 0.1988 0.2481 -0.0067 -0.0046 -0.0198 14 ALA B O   
734  C CB  . ALA B 14 ? 0.2149 0.1356 0.1774 0.0009  -0.0067 -0.0525 14 ALA B CB  
735  N N   . GLU B 15 ? 0.2613 0.1679 0.2307 -0.0241 -0.0099 -0.0341 15 GLU B N   
736  C CA  . GLU B 15 ? 0.2967 0.1842 0.2742 -0.0360 -0.0134 -0.0269 15 GLU B CA  
737  C C   . GLU B 15 ? 0.2921 0.1978 0.2862 -0.0420 -0.0089 -0.0053 15 GLU B C   
738  O O   . GLU B 15 ? 0.3023 0.1932 0.3026 -0.0457 -0.0061 0.0085  15 GLU B O   
739  C CB  . GLU B 15 ? 0.2890 0.1599 0.2640 -0.0488 -0.0231 -0.0385 15 GLU B CB  
740  C CG  . GLU B 15 ? 0.3563 0.2003 0.3107 -0.0412 -0.0223 -0.0561 15 GLU B CG  
741  C CD  . GLU B 15 ? 0.4885 0.3113 0.4263 -0.0503 -0.0331 -0.0701 15 GLU B CD  
742  O OE1 . GLU B 15 ? 0.5115 0.3516 0.4521 -0.0589 -0.0426 -0.0687 15 GLU B OE1 
743  O OE2 . GLU B 15 ? 0.5669 0.3551 0.4857 -0.0461 -0.0327 -0.0833 15 GLU B OE2 
744  N N   . GLU B 16 ? 0.2831 0.2203 0.2861 -0.0421 -0.0060 0.0001  16 GLU B N   
745  C CA  . GLU B 16 ? 0.2861 0.2480 0.3076 -0.0443 0.0042  0.0229  16 GLU B CA  
746  C C   . GLU B 16 ? 0.2956 0.2582 0.2962 -0.0266 0.0158  0.0327  16 GLU B C   
747  O O   . GLU B 16 ? 0.3065 0.2690 0.3117 -0.0275 0.0256  0.0538  16 GLU B O   
748  C CB  . GLU B 16 ? 0.2919 0.2899 0.3288 -0.0430 0.0067  0.0259  16 GLU B CB  
749  C CG  . GLU B 16 ? 0.3541 0.3568 0.4159 -0.0614 -0.0080 0.0219  16 GLU B CG  
750  C CD  . GLU B 16 ? 0.4924 0.4948 0.5897 -0.0828 -0.0108 0.0379  16 GLU B CD  
751  O OE1 . GLU B 16 ? 0.5696 0.6049 0.6986 -0.0854 0.0020  0.0608  16 GLU B OE1 
752  O OE2 . GLU B 16 ? 0.5425 0.5104 0.6378 -0.0971 -0.0246 0.0283  16 GLU B OE2 
753  N N   . ALA B 17 ? 0.2748 0.2355 0.2511 -0.0105 0.0133  0.0178  17 ALA B N   
754  C CA  . ALA B 17 ? 0.2777 0.2366 0.2281 0.0080  0.0179  0.0234  17 ALA B CA  
755  C C   . ALA B 17 ? 0.3118 0.2458 0.2578 0.0078  0.0157  0.0331  17 ALA B C   
756  O O   . ALA B 17 ? 0.3378 0.2715 0.2682 0.0176  0.0237  0.0518  17 ALA B O   
757  C CB  . ALA B 17 ? 0.2798 0.2375 0.2122 0.0214  0.0091  0.0020  17 ALA B CB  
758  N N   . VAL B 18 ? 0.2933 0.2044 0.2496 -0.0004 0.0066  0.0220  18 VAL B N   
759  C CA  . VAL B 18 ? 0.3304 0.2136 0.2845 0.0021  0.0041  0.0300  18 VAL B CA  
760  C C   . VAL B 18 ? 0.3667 0.2400 0.3343 -0.0113 0.0123  0.0534  18 VAL B C   
761  O O   . VAL B 18 ? 0.4145 0.2752 0.3720 -0.0037 0.0179  0.0742  18 VAL B O   
762  C CB  . VAL B 18 ? 0.3319 0.1912 0.2941 -0.0011 -0.0043 0.0104  18 VAL B CB  
763  C CG1 . VAL B 18 ? 0.3514 0.1743 0.3161 0.0001  -0.0056 0.0191  18 VAL B CG1 
764  C CG2 . VAL B 18 ? 0.3017 0.1732 0.2587 0.0128  -0.0097 -0.0071 18 VAL B CG2 
765  N N   . ALA B 19 ? 0.3589 0.2371 0.3513 -0.0318 0.0118  0.0522  19 ALA B N   
766  C CA  . ALA B 19 ? 0.3862 0.2577 0.4034 -0.0494 0.0179  0.0752  19 ALA B CA  
767  C C   . ALA B 19 ? 0.3968 0.2918 0.4081 -0.0396 0.0369  0.1042  19 ALA B C   
768  O O   . ALA B 19 ? 0.4269 0.3050 0.4411 -0.0419 0.0457  0.1285  19 ALA B O   
769  C CB  . ALA B 19 ? 0.3788 0.2635 0.4288 -0.0728 0.0105  0.0689  19 ALA B CB  
770  N N   . HIS B 20 ? 0.3697 0.3003 0.3689 -0.0265 0.0445  0.1018  20 HIS B N   
771  C CA  . HIS B 20 ? 0.4001 0.3527 0.3838 -0.0117 0.0655  0.1270  20 HIS B CA  
772  C C   . HIS B 20 ? 0.4279 0.3586 0.3659 0.0111  0.0657  0.1335  20 HIS B C   
773  O O   . HIS B 20 ? 0.4911 0.4176 0.4167 0.0175  0.0820  0.1632  20 HIS B O   
774  C CB  . HIS B 20 ? 0.3901 0.3793 0.3652 0.0014  0.0718  0.1167  20 HIS B CB  
775  C CG  . HIS B 20 ? 0.3886 0.4103 0.4108 -0.0154 0.0781  0.1237  20 HIS B CG  
776  N ND1 . HIS B 20 ? 0.4446 0.4894 0.5007 -0.0250 0.0986  0.1557  20 HIS B ND1 
777  C CD2 . HIS B 20 ? 0.3580 0.3950 0.4026 -0.0243 0.0658  0.1050  20 HIS B CD2 
778  C CE1 . HIS B 20 ? 0.4365 0.5132 0.5398 -0.0397 0.0961  0.1548  20 HIS B CE1 
779  N NE2 . HIS B 20 ? 0.3738 0.4446 0.4669 -0.0383 0.0752  0.1240  20 HIS B NE2 
780  N N   . GLY B 21 ? 0.4126 0.3303 0.3273 0.0237  0.0476  0.1084  21 GLY B N   
781  C CA  . GLY B 21 ? 0.4686 0.3680 0.3441 0.0462  0.0412  0.1134  21 GLY B CA  
782  C C   . GLY B 21 ? 0.5236 0.3900 0.4022 0.0435  0.0428  0.1363  21 GLY B C   
783  O O   . GLY B 21 ? 0.5632 0.4196 0.4074 0.0622  0.0472  0.1572  21 GLY B O   
784  N N   . LYS B 22 ? 0.5270 0.3725 0.4425 0.0219  0.0384  0.1322  22 LYS B N   
785  C CA  . LYS B 22 ? 0.5858 0.3913 0.5103 0.0164  0.0393  0.1517  22 LYS B CA  
786  C C   . LYS B 22 ? 0.6242 0.4307 0.5516 0.0101  0.0619  0.1918  22 LYS B C   
787  O O   . LYS B 22 ? 0.6746 0.4489 0.5934 0.0148  0.0669  0.2176  22 LYS B O   
788  C CB  . LYS B 22 ? 0.5611 0.3391 0.5202 -0.0054 0.0287  0.1335  22 LYS B CB  
789  C CG  . LYS B 22 ? 0.5575 0.3335 0.5118 0.0042  0.0122  0.0979  22 LYS B CG  
790  C CD  . LYS B 22 ? 0.5960 0.3322 0.5659 -0.0040 0.0029  0.0795  22 LYS B CD  
791  C CE  . LYS B 22 ? 0.6982 0.4231 0.6916 -0.0322 -0.0001 0.0681  22 LYS B CE  
792  N NZ  . LYS B 22 ? 0.6731 0.4155 0.6674 -0.0384 -0.0076 0.0377  22 LYS B NZ  
793  N N   . GLU B 23 ? 0.6123 0.4569 0.5532 0.0016  0.0772  0.1989  23 GLU B N   
794  C CA  . GLU B 23 ? 0.6444 0.5007 0.5976 -0.0053 0.1047  0.2395  23 GLU B CA  
795  C C   . GLU B 23 ? 0.6627 0.5408 0.5619 0.0258  0.1221  0.2552  23 GLU B C   
796  O O   . GLU B 23 ? 0.6996 0.5917 0.5974 0.0280  0.1504  0.2907  23 GLU B O   
797  C CB  . GLU B 23 ? 0.6243 0.5141 0.6344 -0.0328 0.1126  0.2407  23 GLU B CB  
798  C CG  . GLU B 23 ? 0.6519 0.5193 0.7120 -0.0650 0.0937  0.2259  23 GLU B CG  
799  C CD  . GLU B 23 ? 0.7978 0.6263 0.8856 -0.0845 0.0997  0.2554  23 GLU B CD  
800  O OE1 . GLU B 23 ? 0.8444 0.6907 0.9844 -0.1096 0.1130  0.2802  23 GLU B OE1 
801  O OE2 . GLU B 23 ? 0.8667 0.6468 0.9288 -0.0748 0.0915  0.2556  23 GLU B OE2 
802  N N   . GLY B 24 ? 0.6451 0.5252 0.4992 0.0504  0.1051  0.2286  24 GLY B N   
803  C CA  . GLY B 24 ? 0.6684 0.5600 0.4607 0.0822  0.1146  0.2370  24 GLY B CA  
804  C C   . GLY B 24 ? 0.6604 0.5923 0.4495 0.0880  0.1306  0.2297  24 GLY B C   
805  O O   . GLY B 24 ? 0.6904 0.6316 0.4281 0.1141  0.1466  0.2417  24 GLY B O   
806  N N   . HIS B 25 ? 0.5961 0.5500 0.4352 0.0669  0.1262  0.2097  25 HIS B N   
807  C CA  . HIS B 25 ? 0.5906 0.5825 0.4306 0.0751  0.1414  0.2035  25 HIS B CA  
808  C C   . HIS B 25 ? 0.5769 0.5664 0.3794 0.0936  0.1195  0.1646  25 HIS B C   
809  O O   . HIS B 25 ? 0.5315 0.5297 0.3638 0.0813  0.1049  0.1380  25 HIS B O   
810  C CB  . HIS B 25 ? 0.5435 0.5633 0.4558 0.0462  0.1456  0.2032  25 HIS B CB  
811  C CG  . HIS B 25 ? 0.5922 0.6129 0.5566 0.0201  0.1601  0.2371  25 HIS B CG  
812  N ND1 . HIS B 25 ? 0.5786 0.5998 0.6060 -0.0132 0.1457  0.2305  25 HIS B ND1 
813  C CD2 . HIS B 25 ? 0.6254 0.6413 0.5867 0.0216  0.1857  0.2777  25 HIS B CD2 
814  C CE1 . HIS B 25 ? 0.6315 0.6485 0.6983 -0.0334 0.1600  0.2640  25 HIS B CE1 
815  N NE2 . HIS B 25 ? 0.6435 0.6579 0.6737 -0.0134 0.1865  0.2952  25 HIS B NE2 
816  N N   . THR B 26 ? 0.6120 0.5881 0.3482 0.1231  0.1165  0.1622  26 THR B N   
817  C CA  . THR B 26 ? 0.6069 0.5759 0.3062 0.1403  0.0926  0.1258  26 THR B CA  
818  C C   . THR B 26 ? 0.5782 0.5698 0.2940 0.1401  0.0974  0.1047  26 THR B C   
819  O O   . THR B 26 ? 0.5294 0.5157 0.2616 0.1319  0.0744  0.0741  26 THR B O   
820  C CB  . THR B 26 ? 0.6772 0.6300 0.2968 0.1742  0.0899  0.1292  26 THR B CB  
821  O OG1 . THR B 26 ? 0.7290 0.6602 0.3370 0.1750  0.0844  0.1519  26 THR B OG1 
822  C CG2 . THR B 26 ? 0.6734 0.6140 0.2616 0.1875  0.0572  0.0892  26 THR B CG2 
823  N N   . ASP B 27 ? 0.5980 0.6145 0.3129 0.1496  0.1285  0.1235  27 ASP B N   
824  C CA  . ASP B 27 ? 0.5983 0.6351 0.3246 0.1561  0.1349  0.1061  27 ASP B CA  
825  C C   . ASP B 27 ? 0.5292 0.5793 0.3254 0.1261  0.1229  0.0955  27 ASP B C   
826  O O   . ASP B 27 ? 0.5085 0.5568 0.3081 0.1282  0.1093  0.0687  27 ASP B O   
827  C CB  . ASP B 27 ? 0.6408 0.7065 0.3564 0.1763  0.1747  0.1314  27 ASP B CB  
828  C CG  . ASP B 27 ? 0.7744 0.8216 0.3985 0.2170  0.1839  0.1276  27 ASP B CG  
829  O OD1 . ASP B 27 ? 0.8394 0.8530 0.4121 0.2287  0.1535  0.0989  27 ASP B OD1 
830  O OD2 . ASP B 27 ? 0.8441 0.9109 0.4465 0.2386  0.2216  0.1529  27 ASP B OD2 
831  N N   . GLN B 28 ? 0.4933 0.5522 0.3411 0.0991  0.1263  0.1160  28 GLN B N   
832  C CA  . GLN B 28 ? 0.4484 0.5150 0.3526 0.0720  0.1114  0.1047  28 GLN B CA  
833  C C   . GLN B 28 ? 0.4097 0.4449 0.3046 0.0639  0.0820  0.0776  28 GLN B C   
834  O O   . GLN B 28 ? 0.3887 0.4240 0.3028 0.0545  0.0680  0.0574  28 GLN B O   
835  C CB  . GLN B 28 ? 0.4454 0.5255 0.4056 0.0446  0.1193  0.1309  28 GLN B CB  
836  C CG  . GLN B 28 ? 0.5347 0.6586 0.5339 0.0441  0.1476  0.1593  28 GLN B CG  
837  C CD  . GLN B 28 ? 0.6043 0.7589 0.6225 0.0525  0.1483  0.1460  28 GLN B CD  
838  O OE1 . GLN B 28 ? 0.6713 0.8493 0.6735 0.0781  0.1723  0.1541  28 GLN B OE1 
839  N NE2 . GLN B 28 ? 0.5536 0.7057 0.6011 0.0346  0.1230  0.1257  28 GLN B NE2 
840  N N   . LEU B 29 ? 0.4014 0.4109 0.2687 0.0685  0.0734  0.0788  29 LEU B N   
841  C CA  . LEU B 29 ? 0.3791 0.3659 0.2412 0.0655  0.0484  0.0533  29 LEU B CA  
842  C C   . LEU B 29 ? 0.3622 0.3499 0.2045 0.0788  0.0382  0.0264  29 LEU B C   
843  O O   . LEU B 29 ? 0.3086 0.2925 0.1718 0.0681  0.0259  0.0080  29 LEU B O   
844  C CB  . LEU B 29 ? 0.4072 0.3704 0.2457 0.0728  0.0388  0.0590  29 LEU B CB  
845  C CG  . LEU B 29 ? 0.4197 0.3684 0.2556 0.0751  0.0137  0.0319  29 LEU B CG  
846  C CD1 . LEU B 29 ? 0.3962 0.3257 0.2384 0.0724  0.0057  0.0403  29 LEU B CD1 
847  C CD2 . LEU B 29 ? 0.4683 0.4152 0.2622 0.0977  0.0011  0.0154  29 LEU B CD2 
848  N N   . LEU B 30 ? 0.3976 0.3868 0.1975 0.1027  0.0445  0.0251  30 LEU B N   
849  C CA  . LEU B 30 ? 0.3984 0.3804 0.1763 0.1161  0.0336  -0.0013 30 LEU B CA  
850  C C   . LEU B 30 ? 0.3746 0.3710 0.1836 0.1090  0.0407  -0.0076 30 LEU B C   
851  O O   . LEU B 30 ? 0.3683 0.3531 0.1861 0.1042  0.0259  -0.0289 30 LEU B O   
852  C CB  . LEU B 30 ? 0.4741 0.4507 0.1922 0.1461  0.0411  -0.0013 30 LEU B CB  
853  C CG  . LEU B 30 ? 0.5094 0.4649 0.1823 0.1595  0.0226  -0.0055 30 LEU B CG  
854  C CD1 . LEU B 30 ? 0.5529 0.5031 0.1546 0.1927  0.0367  0.0015  30 LEU B CD1 
855  C CD2 . LEU B 30 ? 0.4772 0.4150 0.1545 0.1553  -0.0104 -0.0380 30 LEU B CD2 
856  N N   . GLU B 31 ? 0.3633 0.3856 0.1924 0.1084  0.0627  0.0126  31 GLU B N   
857  C CA  . GLU B 31 ? 0.3720 0.4114 0.2333 0.1041  0.0668  0.0088  31 GLU B CA  
858  C C   . GLU B 31 ? 0.3263 0.3580 0.2214 0.0798  0.0490  -0.0010 31 GLU B C   
859  O O   . GLU B 31 ? 0.2993 0.3234 0.1991 0.0799  0.0404  -0.0163 31 GLU B O   
860  C CB  . GLU B 31 ? 0.3859 0.4623 0.2786 0.1030  0.0906  0.0360  31 GLU B CB  
861  C CG  . GLU B 31 ? 0.4864 0.5849 0.3990 0.1137  0.0989  0.0336  31 GLU B CG  
862  C CD  . GLU B 31 ? 0.5837 0.7209 0.5119 0.1282  0.1289  0.0589  31 GLU B CD  
863  O OE1 . GLU B 31 ? 0.6571 0.8103 0.6018 0.1177  0.1424  0.0840  31 GLU B OE1 
864  O OE2 . GLU B 31 ? 0.5969 0.7480 0.5239 0.1504  0.1408  0.0552  31 GLU B OE2 
865  N N   . HIS B 32 ? 0.3054 0.3337 0.2188 0.0608  0.0440  0.0079  32 HIS B N   
866  C CA  . HIS B 32 ? 0.3062 0.3247 0.2435 0.0410  0.0300  -0.0015 32 HIS B CA  
867  C C   . HIS B 32 ? 0.2916 0.2854 0.2144 0.0421  0.0158  -0.0219 32 HIS B C   
868  O O   . HIS B 32 ? 0.2879 0.2750 0.2212 0.0349  0.0092  -0.0326 32 HIS B O   
869  C CB  . HIS B 32 ? 0.3153 0.3327 0.2745 0.0222  0.0296  0.0126  32 HIS B CB  
870  C CG  . HIS B 32 ? 0.3253 0.3700 0.3189 0.0115  0.0375  0.0301  32 HIS B CG  
871  N ND1 . HIS B 32 ? 0.3489 0.4064 0.3663 0.0027  0.0294  0.0253  32 HIS B ND1 
872  C CD2 . HIS B 32 ? 0.3596 0.4243 0.3715 0.0087  0.0524  0.0543  32 HIS B CD2 
873  C CE1 . HIS B 32 ? 0.3605 0.4478 0.4145 -0.0061 0.0356  0.0439  32 HIS B CE1 
874  N NE2 . HIS B 32 ? 0.3586 0.4514 0.4133 -0.0040 0.0514  0.0625  32 HIS B NE2 
875  N N   . ALA B 33 ? 0.3053 0.2869 0.2056 0.0515  0.0108  -0.0259 33 ALA B N   
876  C CA  . ALA B 33 ? 0.2956 0.2601 0.1938 0.0513  -0.0046 -0.0448 33 ALA B CA  
877  C C   . ALA B 33 ? 0.3148 0.2742 0.2070 0.0583  -0.0082 -0.0602 33 ALA B C   
878  O O   . ALA B 33 ? 0.2984 0.2476 0.2054 0.0507  -0.0163 -0.0721 33 ALA B O   
879  C CB  . ALA B 33 ? 0.3078 0.2638 0.1846 0.0623  -0.0142 -0.0462 33 ALA B CB  
880  N N   . LYS B 34 ? 0.3025 0.2668 0.1725 0.0744  -0.0005 -0.0591 34 LYS B N   
881  C CA  . LYS B 34 ? 0.3285 0.2807 0.1909 0.0835  -0.0039 -0.0749 34 LYS B CA  
882  C C   . LYS B 34 ? 0.3120 0.2678 0.2027 0.0720  0.0002  -0.0719 34 LYS B C   
883  O O   . LYS B 34 ? 0.3173 0.2555 0.2147 0.0686  -0.0068 -0.0835 34 LYS B O   
884  C CB  . LYS B 34 ? 0.3458 0.3018 0.1761 0.1071  0.0074  -0.0734 34 LYS B CB  
885  C CG  . LYS B 34 ? 0.3981 0.3380 0.1861 0.1225  -0.0031 -0.0844 34 LYS B CG  
886  C CD  . LYS B 34 ? 0.4582 0.4007 0.2011 0.1505  0.0125  -0.0806 34 LYS B CD  
887  C CE  . LYS B 34 ? 0.5413 0.4656 0.2336 0.1657  -0.0017 -0.0902 34 LYS B CE  
888  N NZ  . LYS B 34 ? 0.6239 0.5477 0.2607 0.1977  0.0179  -0.0862 34 LYS B NZ  
889  N N   . GLU B 35 ? 0.2933 0.2709 0.2012 0.0654  0.0100  -0.0551 35 GLU B N   
890  C CA  . GLU B 35 ? 0.2860 0.2682 0.2151 0.0560  0.0100  -0.0511 35 GLU B CA  
891  C C   . GLU B 35 ? 0.2704 0.2367 0.2079 0.0401  0.0021  -0.0571 35 GLU B C   
892  O O   . GLU B 35 ? 0.2571 0.2119 0.1983 0.0375  0.0004  -0.0607 35 GLU B O   
893  C CB  . GLU B 35 ? 0.2678 0.2786 0.2174 0.0500  0.0163  -0.0333 35 GLU B CB  
894  C CG  A GLU B 35 ? 0.2909 0.3257 0.2401 0.0661  0.0304  -0.0222 35 GLU B CG  
895  C CG  B GLU B 35 ? 0.3325 0.3653 0.2928 0.0636  0.0242  -0.0252 35 GLU B CG  
896  C CD  A GLU B 35 ? 0.2845 0.3535 0.2691 0.0571  0.0352  -0.0030 35 GLU B CD  
897  C CD  B GLU B 35 ? 0.3773 0.4088 0.3503 0.0588  0.0158  -0.0251 35 GLU B CD  
898  O OE1 A GLU B 35 ? 0.3388 0.4231 0.3343 0.0507  0.0433  0.0116  35 GLU B OE1 
899  O OE1 B GLU B 35 ? 0.3085 0.3631 0.2994 0.0676  0.0181  -0.0155 35 GLU B OE1 
900  O OE2 A GLU B 35 ? 0.1693 0.2486 0.1726 0.0552  0.0290  -0.0015 35 GLU B OE2 
901  O OE2 B GLU B 35 ? 0.4605 0.4685 0.4256 0.0474  0.0073  -0.0333 35 GLU B OE2 
902  N N   . SER B 36 ? 0.2417 0.2068 0.1816 0.0313  -0.0004 -0.0559 36 SER B N   
903  C CA  . SER B 36 ? 0.2333 0.1851 0.1811 0.0204  -0.0039 -0.0615 36 SER B CA  
904  C C   . SER B 36 ? 0.2472 0.1845 0.1981 0.0226  -0.0077 -0.0734 36 SER B C   
905  O O   . SER B 36 ? 0.2400 0.1683 0.1995 0.0159  -0.0048 -0.0745 36 SER B O   
906  C CB  . SER B 36 ? 0.2396 0.1898 0.1893 0.0168  -0.0061 -0.0598 36 SER B CB  
907  O OG  . SER B 36 ? 0.2498 0.1891 0.2090 0.0094  -0.0061 -0.0650 36 SER B OG  
908  N N   . LEU B 37 ? 0.2313 0.1651 0.1743 0.0317  -0.0145 -0.0817 37 LEU B N   
909  C CA  . LEU B 37 ? 0.2591 0.1782 0.2116 0.0308  -0.0233 -0.0949 37 LEU B CA  
910  C C   . LEU B 37 ? 0.2657 0.1705 0.2207 0.0307  -0.0191 -0.0963 37 LEU B C   
911  O O   . LEU B 37 ? 0.2736 0.1652 0.2485 0.0219  -0.0198 -0.0997 37 LEU B O   
912  C CB  . LEU B 37 ? 0.2678 0.1827 0.2006 0.0434  -0.0361 -0.1058 37 LEU B CB  
913  C CG  . LEU B 37 ? 0.3184 0.2147 0.2604 0.0422  -0.0529 -0.1241 37 LEU B CG  
914  C CD1 . LEU B 37 ? 0.3095 0.2120 0.2930 0.0264  -0.0572 -0.1241 37 LEU B CD1 
915  C CD2 . LEU B 37 ? 0.3665 0.2549 0.2777 0.0571  -0.0705 -0.1382 37 LEU B CD2 
916  N N   . THR B 38 ? 0.2689 0.1767 0.2072 0.0419  -0.0139 -0.0917 38 THR B N   
917  C CA  . THR B 38 ? 0.2772 0.1698 0.2160 0.0458  -0.0099 -0.0903 38 THR B CA  
918  C C   . THR B 38 ? 0.2675 0.1573 0.2193 0.0333  -0.0035 -0.0799 38 THR B C   
919  O O   . THR B 38 ? 0.2493 0.1181 0.2095 0.0293  -0.0014 -0.0797 38 THR B O   
920  C CB  . THR B 38 ? 0.2889 0.1945 0.2147 0.0616  -0.0037 -0.0833 38 THR B CB  
921  O OG1 . THR B 38 ? 0.2978 0.2024 0.2035 0.0771  -0.0055 -0.0930 38 THR B OG1 
922  C CG2 . THR B 38 ? 0.2886 0.1765 0.2149 0.0696  -0.0010 -0.0807 38 THR B CG2 
923  N N   . HIS B 39 ? 0.2411 0.1490 0.1913 0.0278  0.0000  -0.0707 39 HIS B N   
924  C CA  . HIS B 39 ? 0.2443 0.1479 0.1942 0.0193  0.0056  -0.0628 39 HIS B CA  
925  C C   . HIS B 39 ? 0.2558 0.1494 0.2198 0.0096  0.0107  -0.0664 39 HIS B C   
926  O O   . HIS B 39 ? 0.2658 0.1464 0.2305 0.0058  0.0201  -0.0597 39 HIS B O   
927  C CB  . HIS B 39 ? 0.2139 0.1350 0.1567 0.0158  0.0034  -0.0571 39 HIS B CB  
928  C CG  . HIS B 39 ? 0.2362 0.1707 0.1752 0.0225  -0.0006 -0.0488 39 HIS B CG  
929  N ND1 . HIS B 39 ? 0.2408 0.1671 0.1708 0.0271  -0.0012 -0.0417 39 HIS B ND1 
930  C CD2 . HIS B 39 ? 0.2545 0.2126 0.2015 0.0274  -0.0033 -0.0441 39 HIS B CD2 
931  C CE1 . HIS B 39 ? 0.2634 0.2100 0.1987 0.0345  -0.0073 -0.0344 39 HIS B CE1 
932  N NE2 . HIS B 39 ? 0.2533 0.2215 0.2024 0.0338  -0.0073 -0.0354 39 HIS B NE2 
933  N N   . ALA B 40 ? 0.2543 0.1561 0.2304 0.0069  0.0060  -0.0741 40 ALA B N   
934  C CA  . ALA B 40 ? 0.2546 0.1544 0.2556 -0.0009 0.0106  -0.0767 40 ALA B CA  
935  C C   . ALA B 40 ? 0.2823 0.1671 0.3037 -0.0052 0.0113  -0.0782 40 ALA B C   
936  O O   . ALA B 40 ? 0.2792 0.1590 0.3202 -0.0128 0.0241  -0.0711 40 ALA B O   
937  C CB  . ALA B 40 ? 0.2411 0.1535 0.2549 0.0000  0.0008  -0.0844 40 ALA B CB  
938  N N   . LYS B 41 ? 0.2627 0.1383 0.2805 -0.0002 -0.0012 -0.0873 41 LYS B N   
939  C CA  . LYS B 41 ? 0.3020 0.1565 0.3404 -0.0058 -0.0040 -0.0910 41 LYS B CA  
940  C C   . LYS B 41 ? 0.3199 0.1564 0.3502 -0.0060 0.0109  -0.0762 41 LYS B C   
941  O O   . LYS B 41 ? 0.3240 0.1436 0.3787 -0.0155 0.0177  -0.0706 41 LYS B O   
942  C CB  . LYS B 41 ? 0.3210 0.1614 0.3468 0.0032  -0.0217 -0.1072 41 LYS B CB  
943  C CG  . LYS B 41 ? 0.3511 0.2028 0.3818 0.0041  -0.0402 -0.1224 41 LYS B CG  
944  C CD  . LYS B 41 ? 0.4836 0.3156 0.4841 0.0186  -0.0553 -0.1391 41 LYS B CD  
945  C CE  . LYS B 41 ? 0.5445 0.3820 0.5361 0.0237  -0.0768 -0.1551 41 LYS B CE  
946  N NZ  . LYS B 41 ? 0.6479 0.4803 0.6807 0.0085  -0.0960 -0.1667 41 LYS B NZ  
947  N N   . ALA B 42 ? 0.3039 0.1444 0.3025 0.0043  0.0152  -0.0681 42 ALA B N   
948  C CA  . ALA B 42 ? 0.3337 0.1563 0.3188 0.0080  0.0254  -0.0529 42 ALA B CA  
949  C C   . ALA B 42 ? 0.3543 0.1781 0.3391 0.0003  0.0424  -0.0390 42 ALA B C   
950  O O   . ALA B 42 ? 0.3906 0.1947 0.3669 0.0012  0.0542  -0.0237 42 ALA B O   
951  C CB  . ALA B 42 ? 0.3059 0.1367 0.2627 0.0228  0.0204  -0.0485 42 ALA B CB  
952  N N   . ALA B 43 ? 0.3546 0.1979 0.3457 -0.0049 0.0455  -0.0433 43 ALA B N   
953  C CA  . ALA B 43 ? 0.4121 0.2558 0.4019 -0.0089 0.0651  -0.0327 43 ALA B CA  
954  C C   . ALA B 43 ? 0.4611 0.3033 0.4948 -0.0199 0.0789  -0.0277 43 ALA B C   
955  O O   . ALA B 43 ? 0.5216 0.3624 0.5540 -0.0208 0.1019  -0.0143 43 ALA B O   
956  C CB  . ALA B 43 ? 0.3830 0.2444 0.3611 -0.0070 0.0639  -0.0400 43 ALA B CB  
957  N N   . SER B 44 ? 0.4757 0.3206 0.5493 -0.0280 0.0656  -0.0387 44 SER B N   
958  C CA  . SER B 44 ? 0.5231 0.3789 0.6523 -0.0409 0.0750  -0.0356 44 SER B CA  
959  C C   . SER B 44 ? 0.5555 0.3926 0.7061 -0.0500 0.0962  -0.0160 44 SER B C   
960  O O   . SER B 44 ? 0.6015 0.4138 0.7611 -0.0552 0.0867  -0.0165 44 SER B O   
961  C CB  . SER B 44 ? 0.5224 0.3869 0.6908 -0.0483 0.0493  -0.0542 44 SER B CB  
962  O OG  . SER B 44 ? 0.5404 0.4113 0.6752 -0.0372 0.0302  -0.0688 44 SER B OG  
963  N N   . THR B 50 ? 0.3680 0.4466 0.8437 -0.0373 0.1308  -0.0251 50 THR B N   
964  C CA  . THR B 50 ? 0.3487 0.3875 0.7315 -0.0278 0.1392  -0.0272 50 THR B CA  
965  C C   . THR B 50 ? 0.3112 0.3390 0.6462 -0.0169 0.1102  -0.0449 50 THR B C   
966  O O   . THR B 50 ? 0.2695 0.3038 0.6188 -0.0211 0.0758  -0.0570 50 THR B O   
967  C CB  . THR B 50 ? 0.3891 0.3968 0.7421 -0.0405 0.1403  -0.0212 50 THR B CB  
968  O OG1 . THR B 50 ? 0.4910 0.4773 0.7893 -0.0310 0.1733  -0.0078 50 THR B OG1 
969  C CG2 . THR B 50 ? 0.3611 0.3438 0.6646 -0.0414 0.1062  -0.0375 50 THR B CG2 
970  N N   . HIS B 51 ? 0.2870 0.2972 0.5652 -0.0019 0.1256  -0.0455 51 HIS B N   
971  C CA  . HIS B 51 ? 0.2728 0.2671 0.5031 0.0067  0.1040  -0.0581 51 HIS B CA  
972  C C   . HIS B 51 ? 0.2691 0.2448 0.4629 -0.0019 0.0795  -0.0646 51 HIS B C   
973  O O   . HIS B 51 ? 0.2497 0.2244 0.4307 0.0007  0.0554  -0.0731 51 HIS B O   
974  C CB  . HIS B 51 ? 0.2841 0.2563 0.4611 0.0210  0.1251  -0.0583 51 HIS B CB  
975  C CG  . HIS B 51 ? 0.2995 0.2864 0.5043 0.0371  0.1421  -0.0578 51 HIS B CG  
976  N ND1 . HIS B 51 ? 0.2915 0.2919 0.5233 0.0448  0.1231  -0.0638 51 HIS B ND1 
977  C CD2 . HIS B 51 ? 0.3596 0.3485 0.5669 0.0503  0.1775  -0.0512 51 HIS B CD2 
978  C CE1 . HIS B 51 ? 0.3495 0.3606 0.6046 0.0620  0.1449  -0.0614 51 HIS B CE1 
979  N NE2 . HIS B 51 ? 0.3547 0.3598 0.5955 0.0661  0.1795  -0.0544 51 HIS B NE2 
980  N N   . VAL B 52 ? 0.2907 0.2511 0.4666 -0.0100 0.0871  -0.0587 52 VAL B N   
981  C CA  . VAL B 52 ? 0.2985 0.2440 0.4467 -0.0152 0.0644  -0.0650 52 VAL B CA  
982  C C   . VAL B 52 ? 0.2814 0.2389 0.4657 -0.0209 0.0376  -0.0749 52 VAL B C   
983  O O   . VAL B 52 ? 0.2709 0.2238 0.4289 -0.0163 0.0163  -0.0841 52 VAL B O   
984  C CB  . VAL B 52 ? 0.3268 0.2525 0.4547 -0.0205 0.0763  -0.0556 52 VAL B CB  
985  C CG1 . VAL B 52 ? 0.3409 0.2527 0.4465 -0.0222 0.0544  -0.0625 52 VAL B CG1 
986  C CG2 . VAL B 52 ? 0.3693 0.2803 0.4462 -0.0117 0.0954  -0.0488 52 VAL B CG2 
987  N N   . GLY B 53 ? 0.2810 0.2540 0.5248 -0.0306 0.0384  -0.0727 53 GLY B N   
988  C CA  . GLY B 53 ? 0.2659 0.2499 0.5470 -0.0367 0.0077  -0.0850 53 GLY B CA  
989  C C   . GLY B 53 ? 0.2508 0.2494 0.5245 -0.0245 -0.0134 -0.0939 53 GLY B C   
990  O O   . GLY B 53 ? 0.2341 0.2263 0.4868 -0.0209 -0.0408 -0.1058 53 GLY B O   
991  N N   . HIS B 54 ? 0.2346 0.2501 0.5223 -0.0156 0.0009  -0.0871 54 HIS B N   
992  C CA  . HIS B 54 ? 0.2528 0.2767 0.5298 -0.0018 -0.0163 -0.0916 54 HIS B CA  
993  C C   . HIS B 54 ? 0.2532 0.2528 0.4609 0.0060  -0.0235 -0.0944 54 HIS B C   
994  O O   . HIS B 54 ? 0.2494 0.2491 0.4395 0.0140  -0.0464 -0.0992 54 HIS B O   
995  C CB  . HIS B 54 ? 0.2659 0.3056 0.5680 0.0089  0.0050  -0.0833 54 HIS B CB  
996  C CG  . HIS B 54 ? 0.3164 0.3917 0.6992 0.0047  0.0098  -0.0785 54 HIS B CG  
997  N ND1 . HIS B 54 ? 0.3995 0.4866 0.8123 0.0058  0.0460  -0.0668 54 HIS B ND1 
998  C CD2 . HIS B 54 ? 0.3580 0.4619 0.8009 -0.0006 -0.0171 -0.0832 54 HIS B CD2 
999  C CE1 . HIS B 54 ? 0.3537 0.4793 0.8493 0.0003  0.0443  -0.0620 54 HIS B CE1 
1000 N NE2 . HIS B 54 ? 0.3647 0.5018 0.8829 -0.0047 0.0035  -0.0727 54 HIS B NE2 
1001 N N   . GLY B 55 ? 0.2527 0.2328 0.4217 0.0043  -0.0040 -0.0896 55 GLY B N   
1002 C CA  . GLY B 55 ? 0.2507 0.2136 0.3667 0.0087  -0.0091 -0.0897 55 GLY B CA  
1003 C C   . GLY B 55 ? 0.2624 0.2208 0.3632 0.0071  -0.0274 -0.0965 55 GLY B C   
1004 O O   . GLY B 55 ? 0.2521 0.2076 0.3249 0.0148  -0.0395 -0.0975 55 GLY B O   
1005 N N   . ILE B 56 ? 0.2472 0.2020 0.3650 -0.0016 -0.0279 -0.1005 56 ILE B N   
1006 C CA  . ILE B 56 ? 0.2701 0.2138 0.3705 -0.0004 -0.0467 -0.1110 56 ILE B CA  
1007 C C   . ILE B 56 ? 0.2906 0.2428 0.3936 0.0072  -0.0735 -0.1209 56 ILE B C   
1008 O O   . ILE B 56 ? 0.3165 0.2606 0.3764 0.0188  -0.0849 -0.1251 56 ILE B O   
1009 C CB  . ILE B 56 ? 0.2855 0.2186 0.4116 -0.0118 -0.0454 -0.1144 56 ILE B CB  
1010 C CG1 . ILE B 56 ? 0.2615 0.1804 0.3670 -0.0141 -0.0224 -0.1033 56 ILE B CG1 
1011 C CG2 . ILE B 56 ? 0.3176 0.2352 0.4321 -0.0096 -0.0694 -0.1304 56 ILE B CG2 
1012 C CD1 . ILE B 56 ? 0.3464 0.2533 0.4820 -0.0260 -0.0139 -0.0994 56 ILE B CD1 
1013 N N   . LYS B 57 ? 0.2795 0.2499 0.4320 0.0027  -0.0827 -0.1229 57 LYS B N   
1014 C CA  . LYS B 57 ? 0.3239 0.3055 0.4848 0.0103  -0.1133 -0.1323 57 LYS B CA  
1015 C C   . LYS B 57 ? 0.2996 0.2804 0.4165 0.0273  -0.1149 -0.1249 57 LYS B C   
1016 O O   . LYS B 57 ? 0.3184 0.2934 0.4012 0.0388  -0.1361 -0.1312 57 LYS B O   
1017 C CB  . LYS B 57 ? 0.3204 0.3305 0.5546 0.0031  -0.1210 -0.1318 57 LYS B CB  
1018 C CG  . LYS B 57 ? 0.4664 0.4790 0.7511 -0.0139 -0.1385 -0.1434 57 LYS B CG  
1019 C CD  . LYS B 57 ? 0.5380 0.5441 0.8536 -0.0312 -0.1089 -0.1344 57 LYS B CD  
1020 C CE  . LYS B 57 ? 0.5682 0.5374 0.8464 -0.0369 -0.1091 -0.1421 57 LYS B CE  
1021 N NZ  . LYS B 57 ? 0.4946 0.4554 0.7743 -0.0439 -0.0717 -0.1249 57 LYS B NZ  
1022 N N   . HIS B 58 ? 0.2906 0.2733 0.4048 0.0294  -0.0921 -0.1112 58 HIS B N   
1023 C CA  . HIS B 58 ? 0.2773 0.2543 0.3545 0.0429  -0.0924 -0.1015 58 HIS B CA  
1024 C C   . HIS B 58 ? 0.2875 0.2480 0.3105 0.0463  -0.0868 -0.0987 58 HIS B C   
1025 O O   . HIS B 58 ? 0.3284 0.2847 0.3185 0.0583  -0.0939 -0.0926 58 HIS B O   
1026 C CB  . HIS B 58 ? 0.2676 0.2434 0.3554 0.0433  -0.0714 -0.0901 58 HIS B CB  
1027 C CG  . HIS B 58 ? 0.2685 0.2617 0.4020 0.0499  -0.0759 -0.0886 58 HIS B CG  
1028 N ND1 . HIS B 58 ? 0.3065 0.3051 0.4393 0.0649  -0.0947 -0.0843 58 HIS B ND1 
1029 C CD2 . HIS B 58 ? 0.2823 0.2905 0.4643 0.0461  -0.0623 -0.0887 58 HIS B CD2 
1030 C CE1 . HIS B 58 ? 0.3036 0.3212 0.4866 0.0707  -0.0940 -0.0824 58 HIS B CE1 
1031 N NE2 . HIS B 58 ? 0.2799 0.3052 0.4949 0.0594  -0.0727 -0.0852 58 HIS B NE2 
1032 N N   . LEU B 59 ? 0.2750 0.2279 0.2904 0.0374  -0.0720 -0.1000 59 LEU B N   
1033 C CA  . LEU B 59 ? 0.2777 0.2215 0.2500 0.0428  -0.0664 -0.0969 59 LEU B CA  
1034 C C   . LEU B 59 ? 0.3269 0.2649 0.2715 0.0547  -0.0855 -0.1087 59 LEU B C   
1035 O O   . LEU B 59 ? 0.3469 0.2813 0.2502 0.0683  -0.0849 -0.1030 59 LEU B O   
1036 C CB  . LEU B 59 ? 0.2706 0.2097 0.2457 0.0334  -0.0506 -0.0964 59 LEU B CB  
1037 C CG  . LEU B 59 ? 0.2669 0.2070 0.2510 0.0251  -0.0339 -0.0854 59 LEU B CG  
1038 C CD1 . LEU B 59 ? 0.3074 0.2427 0.2974 0.0166  -0.0227 -0.0861 59 LEU B CD1 
1039 C CD2 . LEU B 59 ? 0.2321 0.1726 0.1929 0.0286  -0.0280 -0.0725 59 LEU B CD2 
1040 N N   . GLU B 60 ? 0.3219 0.2568 0.2879 0.0501  -0.1022 -0.1251 60 GLU B N   
1041 C CA  . GLU B 60 ? 0.3782 0.3011 0.3143 0.0617  -0.1263 -0.1417 60 GLU B CA  
1042 C C   . GLU B 60 ? 0.4063 0.3345 0.3167 0.0771  -0.1436 -0.1385 60 GLU B C   
1043 O O   . GLU B 60 ? 0.4554 0.3716 0.3121 0.0947  -0.1536 -0.1438 60 GLU B O   
1044 C CB  . GLU B 60 ? 0.3765 0.2950 0.3534 0.0492  -0.1467 -0.1602 60 GLU B CB  
1045 C CG  . GLU B 60 ? 0.4058 0.3125 0.4020 0.0359  -0.1287 -0.1607 60 GLU B CG  
1046 C CD  . GLU B 60 ? 0.4345 0.3336 0.4784 0.0201  -0.1454 -0.1749 60 GLU B CD  
1047 O OE1 . GLU B 60 ? 0.5599 0.4348 0.5989 0.0160  -0.1421 -0.1822 60 GLU B OE1 
1048 O OE2 . GLU B 60 ? 0.5354 0.4527 0.6259 0.0116  -0.1619 -0.1776 60 GLU B OE2 
1049 N N   . ASP B 61 ? 0.3873 0.3318 0.3329 0.0735  -0.1470 -0.1293 61 ASP B N   
1050 C CA  . ASP B 61 ? 0.4247 0.3730 0.3472 0.0901  -0.1628 -0.1217 61 ASP B CA  
1051 C C   . ASP B 61 ? 0.4222 0.3627 0.2971 0.1017  -0.1415 -0.1005 61 ASP B C   
1052 O O   . ASP B 61 ? 0.4949 0.4279 0.3200 0.1206  -0.1515 -0.0955 61 ASP B O   
1053 C CB  . ASP B 61 ? 0.4065 0.3745 0.3846 0.0860  -0.1702 -0.1160 61 ASP B CB  
1054 C CG  . ASP B 61 ? 0.4579 0.4406 0.4827 0.0804  -0.2016 -0.1340 61 ASP B CG  
1055 O OD1 . ASP B 61 ? 0.5641 0.5366 0.5689 0.0822  -0.2276 -0.1535 61 ASP B OD1 
1056 O OD2 . ASP B 61 ? 0.4858 0.4908 0.5710 0.0747  -0.2009 -0.1290 61 ASP B OD2 
1057 N N   . ALA B 62 ? 0.3991 0.3406 0.2881 0.0906  -0.1132 -0.0869 62 ALA B N   
1058 C CA  . ALA B 62 ? 0.4006 0.3363 0.2555 0.0964  -0.0922 -0.0660 62 ALA B CA  
1059 C C   . ALA B 62 ? 0.4424 0.3721 0.2457 0.1097  -0.0872 -0.0680 62 ALA B C   
1060 O O   . ALA B 62 ? 0.4649 0.3906 0.2258 0.1251  -0.0800 -0.0519 62 ALA B O   
1061 C CB  . ALA B 62 ? 0.3657 0.3031 0.2496 0.0790  -0.0681 -0.0561 62 ALA B CB  
1062 N N   . ILE B 63 ? 0.4292 0.3564 0.2352 0.1060  -0.0887 -0.0862 63 ILE B N   
1063 C CA  . ILE B 63 ? 0.4762 0.3950 0.2341 0.1221  -0.0832 -0.0916 63 ILE B CA  
1064 C C   . ILE B 63 ? 0.5533 0.4592 0.2592 0.1442  -0.1073 -0.1022 63 ILE B C   
1065 O O   . ILE B 63 ? 0.6063 0.5075 0.2576 0.1646  -0.0962 -0.0909 63 ILE B O   
1066 C CB  . ILE B 63 ? 0.4530 0.3656 0.2261 0.1150  -0.0807 -0.1092 63 ILE B CB  
1067 C CG1 . ILE B 63 ? 0.4278 0.3540 0.2339 0.1002  -0.0550 -0.0934 63 ILE B CG1 
1068 C CG2 . ILE B 63 ? 0.5071 0.4049 0.2264 0.1372  -0.0786 -0.1206 63 ILE B CG2 
1069 C CD1 . ILE B 63 ? 0.3804 0.3011 0.2183 0.0870  -0.0557 -0.1062 63 ILE B CD1 
1070 N N   . LYS B 64 ? 0.5755 0.4772 0.2998 0.1404  -0.1402 -0.1223 64 LYS B N   
1071 C CA  . LYS B 64 ? 0.6468 0.5360 0.3242 0.1601  -0.1722 -0.1363 64 LYS B CA  
1072 C C   . LYS B 64 ? 0.6798 0.5712 0.3147 0.1786  -0.1662 -0.1109 64 LYS B C   
1073 O O   . LYS B 64 ? 0.7348 0.6119 0.2963 0.2039  -0.1673 -0.1095 64 LYS B O   
1074 C CB  . LYS B 64 ? 0.6403 0.5348 0.3671 0.1475  -0.2100 -0.1566 64 LYS B CB  
1075 C CG  . LYS B 64 ? 0.7128 0.5976 0.4011 0.1655  -0.2549 -0.1743 64 LYS B CG  
1076 C CD  . LYS B 64 ? 0.7060 0.6153 0.4697 0.1507  -0.2830 -0.1767 64 LYS B CD  
1077 C CE  . LYS B 64 ? 0.7895 0.7014 0.5328 0.1677  -0.3311 -0.1863 64 LYS B CE  
1078 N NZ  . LYS B 64 ? 0.8503 0.7439 0.5745 0.1695  -0.3770 -0.2233 64 LYS B NZ  
1079 N N   . HIS B 65 ? 0.6348 0.5402 0.3117 0.1677  -0.1576 -0.0898 65 HIS B N   
1080 C CA  . HIS B 65 ? 0.6649 0.5679 0.3090 0.1832  -0.1513 -0.0622 65 HIS B CA  
1081 C C   . HIS B 65 ? 0.6680 0.5668 0.2712 0.1913  -0.1135 -0.0373 65 HIS B C   
1082 O O   . HIS B 65 ? 0.7075 0.5963 0.2482 0.2146  -0.1102 -0.0225 65 HIS B O   
1083 C CB  . HIS B 65 ? 0.6341 0.5473 0.3372 0.1699  -0.1518 -0.0487 65 HIS B CB  
1084 C CG  . HIS B 65 ? 0.6712 0.5934 0.4051 0.1721  -0.1900 -0.0647 65 HIS B CG  
1085 N ND1 . HIS B 65 ? 0.7315 0.6496 0.4292 0.1949  -0.2189 -0.0608 65 HIS B ND1 
1086 C CD2 . HIS B 65 ? 0.6456 0.5834 0.4454 0.1553  -0.2045 -0.0834 65 HIS B CD2 
1087 C CE1 . HIS B 65 ? 0.7543 0.6886 0.5003 0.1911  -0.2525 -0.0776 65 HIS B CE1 
1088 N NE2 . HIS B 65 ? 0.7011 0.6485 0.5120 0.1666  -0.2423 -0.0906 65 HIS B NE2 
1089 N N   . GLY B 66 ? 0.6139 0.5223 0.2538 0.1728  -0.0853 -0.0319 66 GLY B N   
1090 C CA  . GLY B 66 ? 0.6251 0.5383 0.2443 0.1768  -0.0489 -0.0085 66 GLY B CA  
1091 C C   . GLY B 66 ? 0.6859 0.5914 0.2359 0.2037  -0.0437 -0.0154 66 GLY B C   
1092 O O   . GLY B 66 ? 0.7333 0.6384 0.2379 0.2215  -0.0199 0.0099  66 GLY B O   
1093 N N   . GLU B 67 ? 0.7061 0.6019 0.2438 0.2086  -0.0656 -0.0492 67 GLU B N   
1094 C CA  . GLU B 67 ? 0.7925 0.6731 0.2573 0.2374  -0.0626 -0.0621 67 GLU B CA  
1095 C C   . GLU B 67 ? 0.8808 0.7461 0.2689 0.2659  -0.0742 -0.0535 67 GLU B C   
1096 O O   . GLU B 67 ? 0.9393 0.7959 0.2570 0.2941  -0.0546 -0.0463 67 GLU B O   
1097 C CB  . GLU B 67 ? 0.8029 0.6663 0.2678 0.2365  -0.0894 -0.1028 67 GLU B CB  
1098 C CG  . GLU B 67 ? 0.8037 0.6773 0.3325 0.2137  -0.0749 -0.1098 67 GLU B CG  
1099 C CD  . GLU B 67 ? 0.8889 0.7663 0.3980 0.2281  -0.0404 -0.1043 67 GLU B CD  
1100 O OE1 . GLU B 67 ? 0.8586 0.7357 0.4038 0.2174  -0.0365 -0.1165 67 GLU B OE1 
1101 O OE2 . GLU B 67 ? 0.9624 0.8446 0.4220 0.2515  -0.0157 -0.0854 67 GLU B OE2 
1102 N N   . GLU B 68 ? 0.8939 0.7567 0.2944 0.2613  -0.1048 -0.0528 68 GLU B N   
1103 C CA  . GLU B 68 ? 0.9907 0.8381 0.3189 0.2893  -0.1233 -0.0443 68 GLU B CA  
1104 C C   . GLU B 68 ? 0.9961 0.8492 0.3149 0.2941  -0.0920 0.0022  68 GLU B C   
1105 O O   . GLU B 68 ? 1.0571 0.8961 0.3082 0.3203  -0.0976 0.0188  68 GLU B O   
1106 C CB  . GLU B 68 ? 1.0048 0.8489 0.3532 0.2854  -0.1759 -0.0657 68 GLU B CB  
1107 C CG  . GLU B 68 ? 1.0509 0.8878 0.4175 0.2766  -0.2101 -0.1103 68 GLU B CG  
1108 C CD  . GLU B 68 ? 1.0942 0.9422 0.5211 0.2611  -0.2549 -0.1262 68 GLU B CD  
1109 O OE1 . GLU B 68 ? 1.1525 0.9888 0.5686 0.2639  -0.2964 -0.1606 68 GLU B OE1 
1110 O OE2 . GLU B 68 ? 1.0465 0.9145 0.5342 0.2466  -0.2490 -0.1051 68 GLU B OE2 
1111 N N   . GLY B 69 ? 0.9259 0.7968 0.3116 0.2685  -0.0605 0.0235  69 GLY B N   
1112 C CA  . GLY B 69 ? 0.9252 0.7989 0.3136 0.2673  -0.0282 0.0681  69 GLY B CA  
1113 C C   . GLY B 69 ? 0.8954 0.7649 0.3295 0.2529  -0.0436 0.0820  69 GLY B C   
1114 O O   . GLY B 69 ? 0.9190 0.7813 0.3485 0.2545  -0.0230 0.1193  69 GLY B O   
1115 N N   . HIS B 70 ? 0.8395 0.7122 0.3185 0.2404  -0.0779 0.0539  70 HIS B N   
1116 C CA  . HIS B 70 ? 0.8073 0.6774 0.3346 0.2296  -0.0903 0.0647  70 HIS B CA  
1117 C C   . HIS B 70 ? 0.7274 0.6068 0.3293 0.1974  -0.0676 0.0675  70 HIS B C   
1118 O O   . HIS B 70 ? 0.6659 0.5543 0.3221 0.1803  -0.0815 0.0447  70 HIS B O   
1119 C CB  . HIS B 70 ? 0.8055 0.6800 0.3509 0.2335  -0.1355 0.0357  70 HIS B CB  
1120 C CG  . HIS B 70 ? 0.9222 0.7888 0.3972 0.2614  -0.1669 0.0204  70 HIS B CG  
1121 N ND1 . HIS B 70 ? 0.9347 0.8075 0.4186 0.2595  -0.2019 -0.0183 70 HIS B ND1 
1122 C CD2 . HIS B 70 ? 1.0155 0.8652 0.4072 0.2922  -0.1709 0.0382  70 HIS B CD2 
1123 C CE1 . HIS B 70 ? 1.0272 0.8861 0.4358 0.2874  -0.2297 -0.0272 70 HIS B CE1 
1124 N NE2 . HIS B 70 ? 1.0822 0.9272 0.4292 0.3094  -0.2108 0.0068  70 HIS B NE2 
1125 N N   . VAL B 71 ? 0.7173 0.5949 0.3216 0.1892  -0.0328 0.0963  71 VAL B N   
1126 C CA  . VAL B 71 ? 0.6546 0.5399 0.3228 0.1591  -0.0145 0.0972  71 VAL B CA  
1127 C C   . VAL B 71 ? 0.6144 0.4877 0.3326 0.1449  -0.0268 0.0947  71 VAL B C   
1128 O O   . VAL B 71 ? 0.5628 0.4421 0.3287 0.1237  -0.0255 0.0787  71 VAL B O   
1129 C CB  . VAL B 71 ? 0.6723 0.5628 0.3394 0.1519  0.0230  0.1286  71 VAL B CB  
1130 C CG1 . VAL B 71 ? 0.7170 0.5866 0.3615 0.1607  0.0361  0.1685  71 VAL B CG1 
1131 C CG2 . VAL B 71 ? 0.6200 0.5221 0.3501 0.1213  0.0350  0.1240  71 VAL B CG2 
1132 N N   . GLY B 72 ? 0.6549 0.5098 0.3577 0.1602  -0.0392 0.1098  72 GLY B N   
1133 C CA  . GLY B 72 ? 0.6289 0.4698 0.3750 0.1535  -0.0494 0.1082  72 GLY B CA  
1134 C C   . GLY B 72 ? 0.5998 0.4581 0.3797 0.1513  -0.0729 0.0742  72 GLY B C   
1135 O O   . GLY B 72 ? 0.5707 0.4290 0.3975 0.1349  -0.0690 0.0616  72 GLY B O   
1136 N N   . VAL B 73 ? 0.6254 0.4979 0.3815 0.1677  -0.0974 0.0587  73 VAL B N   
1137 C CA  . VAL B 73 ? 0.5918 0.4842 0.3896 0.1623  -0.1189 0.0283  73 VAL B CA  
1138 C C   . VAL B 73 ? 0.5240 0.4283 0.3459 0.1399  -0.1046 0.0090  73 VAL B C   
1139 O O   . VAL B 73 ? 0.4825 0.3966 0.3516 0.1275  -0.1067 -0.0068 73 VAL B O   
1140 C CB  . VAL B 73 ? 0.6263 0.5304 0.4003 0.1816  -0.1544 0.0137  73 VAL B CB  
1141 C CG1 . VAL B 73 ? 0.7105 0.6119 0.4271 0.1886  -0.1529 0.0083  73 VAL B CG1 
1142 C CG2 . VAL B 73 ? 0.6175 0.5450 0.4489 0.1707  -0.1743 -0.0151 73 VAL B CG2 
1143 N N   . ALA B 74 ? 0.5180 0.4219 0.3063 0.1376  -0.0886 0.0128  74 ALA B N   
1144 C CA  . ALA B 74 ? 0.4711 0.3852 0.2786 0.1196  -0.0749 -0.0021 74 ALA B CA  
1145 C C   . ALA B 74 ? 0.4313 0.3415 0.2807 0.0993  -0.0578 0.0031  74 ALA B C   
1146 O O   . ALA B 74 ? 0.3981 0.3154 0.2804 0.0855  -0.0570 -0.0138 74 ALA B O   
1147 C CB  . ALA B 74 ? 0.4794 0.3947 0.2453 0.1255  -0.0574 0.0071  74 ALA B CB  
1148 N N   . THR B 75 ? 0.4263 0.3218 0.2722 0.0973  -0.0442 0.0266  75 THR B N   
1149 C CA  . THR B 75 ? 0.4182 0.3020 0.2984 0.0782  -0.0318 0.0296  75 THR B CA  
1150 C C   . THR B 75 ? 0.4033 0.2823 0.3168 0.0769  -0.0416 0.0132  75 THR B C   
1151 O O   . THR B 75 ? 0.3827 0.2606 0.3195 0.0623  -0.0345 0.0009  75 THR B O   
1152 C CB  . THR B 75 ? 0.4448 0.3056 0.3169 0.0769  -0.0193 0.0594  75 THR B CB  
1153 O OG1 . THR B 75 ? 0.4890 0.3605 0.3378 0.0772  -0.0043 0.0768  75 THR B OG1 
1154 C CG2 . THR B 75 ? 0.4423 0.2834 0.3463 0.0564  -0.0111 0.0598  75 THR B CG2 
1155 N N   . LYS B 76 ? 0.4323 0.3098 0.3466 0.0942  -0.0569 0.0144  76 LYS B N   
1156 C CA  . LYS B 76 ? 0.4365 0.3175 0.3879 0.0979  -0.0646 0.0010  76 LYS B CA  
1157 C C   . LYS B 76 ? 0.4008 0.3056 0.3766 0.0889  -0.0670 -0.0214 76 LYS B C   
1158 O O   . LYS B 76 ? 0.3809 0.2858 0.3857 0.0819  -0.0578 -0.0312 76 LYS B O   
1159 C CB  . LYS B 76 ? 0.4723 0.3558 0.4244 0.1206  -0.0845 0.0082  76 LYS B CB  
1160 C CG  . LYS B 76 ? 0.5608 0.4136 0.4904 0.1318  -0.0805 0.0345  76 LYS B CG  
1161 C CD  . LYS B 76 ? 0.5950 0.4531 0.5070 0.1583  -0.1046 0.0453  76 LYS B CD  
1162 C CE  . LYS B 76 ? 0.6901 0.5140 0.5725 0.1712  -0.0992 0.0766  76 LYS B CE  
1163 N NZ  . LYS B 76 ? 0.7593 0.5873 0.6005 0.1970  -0.1213 0.0909  76 LYS B NZ  
1164 N N   . HIS B 77 ? 0.3855 0.3065 0.3461 0.0900  -0.0779 -0.0293 77 HIS B N   
1165 C CA  . HIS B 77 ? 0.3497 0.2877 0.3344 0.0799  -0.0802 -0.0486 77 HIS B CA  
1166 C C   . HIS B 77 ? 0.3413 0.2731 0.3264 0.0634  -0.0595 -0.0508 77 HIS B C   
1167 O O   . HIS B 77 ? 0.3226 0.2603 0.3352 0.0547  -0.0528 -0.0610 77 HIS B O   
1168 C CB  . HIS B 77 ? 0.3575 0.3056 0.3220 0.0856  -0.0997 -0.0593 77 HIS B CB  
1169 C CG  . HIS B 77 ? 0.3953 0.3564 0.3768 0.0979  -0.1280 -0.0658 77 HIS B CG  
1170 N ND1 . HIS B 77 ? 0.3862 0.3666 0.4249 0.0923  -0.1359 -0.0763 77 HIS B ND1 
1171 C CD2 . HIS B 77 ? 0.4588 0.4186 0.4100 0.1162  -0.1511 -0.0619 77 HIS B CD2 
1172 C CE1 . HIS B 77 ? 0.4598 0.4539 0.5104 0.1050  -0.1656 -0.0797 77 HIS B CE1 
1173 N NE2 . HIS B 77 ? 0.4477 0.4275 0.4413 0.1204  -0.1771 -0.0719 77 HIS B NE2 
1174 N N   . ALA B 78 ? 0.3426 0.2643 0.2995 0.0595  -0.0490 -0.0395 78 ALA B N   
1175 C CA  . ALA B 78 ? 0.3141 0.2326 0.2734 0.0439  -0.0337 -0.0410 78 ALA B CA  
1176 C C   . ALA B 78 ? 0.3119 0.2157 0.2896 0.0372  -0.0256 -0.0431 78 ALA B C   
1177 O O   . ALA B 78 ? 0.2921 0.1960 0.2779 0.0284  -0.0183 -0.0525 78 ALA B O   
1178 C CB  . ALA B 78 ? 0.3206 0.2377 0.2577 0.0409  -0.0251 -0.0264 78 ALA B CB  
1179 N N   . GLN B 79 ? 0.3205 0.2087 0.3002 0.0443  -0.0269 -0.0349 79 GLN B N   
1180 C CA  . GLN B 79 ? 0.3647 0.2322 0.3565 0.0433  -0.0196 -0.0392 79 GLN B CA  
1181 C C   . GLN B 79 ? 0.3364 0.2160 0.3530 0.0482  -0.0158 -0.0534 79 GLN B C   
1182 O O   . GLN B 79 ? 0.3413 0.2108 0.3579 0.0428  -0.0039 -0.0620 79 GLN B O   
1183 C CB  . GLN B 79 ? 0.3737 0.2186 0.3637 0.0540  -0.0227 -0.0267 79 GLN B CB  
1184 C CG  . GLN B 79 ? 0.4708 0.2929 0.4434 0.0431  -0.0189 -0.0110 79 GLN B CG  
1185 C CD  . GLN B 79 ? 0.4887 0.2835 0.4570 0.0538  -0.0212 0.0070  79 GLN B CD  
1186 O OE1 . GLN B 79 ? 0.5675 0.3706 0.5325 0.0717  -0.0296 0.0155  79 GLN B OE1 
1187 N NE2 . GLN B 79 ? 0.5684 0.3278 0.5360 0.0425  -0.0160 0.0134  79 GLN B NE2 
1188 N N   . GLU B 80 ? 0.3143 0.2170 0.3515 0.0580  -0.0262 -0.0548 80 GLU B N   
1189 C CA  . GLU B 80 ? 0.3101 0.2325 0.3830 0.0606  -0.0222 -0.0644 80 GLU B CA  
1190 C C   . GLU B 80 ? 0.2709 0.2013 0.3431 0.0468  -0.0136 -0.0719 80 GLU B C   
1191 O O   . GLU B 80 ? 0.2741 0.2087 0.3649 0.0455  0.0012  -0.0765 80 GLU B O   
1192 C CB  . GLU B 80 ? 0.3183 0.2666 0.4179 0.0703  -0.0423 -0.0644 80 GLU B CB  
1193 C CG  . GLU B 80 ? 0.4220 0.3630 0.5194 0.0872  -0.0535 -0.0542 80 GLU B CG  
1194 C CD  . GLU B 80 ? 0.5787 0.5462 0.7243 0.1008  -0.0649 -0.0558 80 GLU B CD  
1195 O OE1 . GLU B 80 ? 0.6203 0.5916 0.7979 0.1054  -0.0478 -0.0581 80 GLU B OE1 
1196 O OE2 . GLU B 80 ? 0.6431 0.6281 0.7943 0.1084  -0.0909 -0.0549 80 GLU B OE2 
1197 N N   . ALA B 81 ? 0.2648 0.1958 0.3135 0.0388  -0.0203 -0.0713 81 ALA B N   
1198 C CA  . ALA B 81 ? 0.2287 0.1632 0.2746 0.0280  -0.0132 -0.0766 81 ALA B CA  
1199 C C   . ALA B 81 ? 0.2518 0.1691 0.2811 0.0223  0.0027  -0.0765 81 ALA B C   
1200 O O   . ALA B 81 ? 0.2402 0.1580 0.2744 0.0187  0.0146  -0.0799 81 ALA B O   
1201 C CB  . ALA B 81 ? 0.2090 0.1452 0.2311 0.0253  -0.0223 -0.0756 81 ALA B CB  
1202 N N   . ILE B 82 ? 0.2625 0.1614 0.2700 0.0214  0.0021  -0.0723 82 ILE B N   
1203 C CA  . ILE B 82 ? 0.2832 0.1619 0.2713 0.0155  0.0111  -0.0761 82 ILE B CA  
1204 C C   . ILE B 82 ? 0.3080 0.1773 0.3024 0.0238  0.0251  -0.0829 82 ILE B C   
1205 O O   . ILE B 82 ? 0.3120 0.1723 0.2895 0.0220  0.0364  -0.0880 82 ILE B O   
1206 C CB  . ILE B 82 ? 0.3147 0.1727 0.2875 0.0108  0.0049  -0.0712 82 ILE B CB  
1207 C CG1 . ILE B 82 ? 0.3205 0.1925 0.2882 0.0022  -0.0025 -0.0618 82 ILE B CG1 
1208 C CG2 . ILE B 82 ? 0.3650 0.1934 0.3164 0.0060  0.0087  -0.0802 82 ILE B CG2 
1209 C CD1 . ILE B 82 ? 0.3974 0.2565 0.3635 -0.0012 -0.0069 -0.0501 82 ILE B CD1 
1210 N N   . GLU B 83 ? 0.2864 0.1569 0.3020 0.0357  0.0258  -0.0820 83 GLU B N   
1211 C CA  . GLU B 83 ? 0.2900 0.1536 0.3143 0.0476  0.0433  -0.0877 83 GLU B CA  
1212 C C   . GLU B 83 ? 0.2855 0.1740 0.3314 0.0461  0.0573  -0.0874 83 GLU B C   
1213 O O   . GLU B 83 ? 0.3053 0.1858 0.3422 0.0519  0.0778  -0.0904 83 GLU B O   
1214 C CB  . GLU B 83 ? 0.2872 0.1534 0.3391 0.0636  0.0411  -0.0848 83 GLU B CB  
1215 C CG  . GLU B 83 ? 0.3302 0.1600 0.3570 0.0656  0.0322  -0.0832 83 GLU B CG  
1216 C CD  . GLU B 83 ? 0.3840 0.2030 0.4291 0.0860  0.0357  -0.0819 83 GLU B CD  
1217 O OE1 . GLU B 83 ? 0.3850 0.2341 0.4699 0.0995  0.0423  -0.0807 83 GLU B OE1 
1218 O OE2 . GLU B 83 ? 0.4237 0.2035 0.4485 0.0891  0.0320  -0.0814 83 GLU B OE2 
1219 N N   . HIS B 84 ? 0.2581 0.1741 0.3329 0.0398  0.0471  -0.0834 84 HIS B N   
1220 C CA  . HIS B 84 ? 0.2516 0.1873 0.3535 0.0350  0.0597  -0.0812 84 HIS B CA  
1221 C C   . HIS B 84 ? 0.2623 0.1818 0.3266 0.0265  0.0686  -0.0806 84 HIS B C   
1222 O O   . HIS B 84 ? 0.2848 0.2032 0.3485 0.0283  0.0908  -0.0773 84 HIS B O   
1223 C CB  . HIS B 84 ? 0.2215 0.1832 0.3616 0.0280  0.0414  -0.0802 84 HIS B CB  
1224 C CG  . HIS B 84 ? 0.2055 0.1933 0.3984 0.0368  0.0347  -0.0794 84 HIS B CG  
1225 N ND1 . HIS B 84 ? 0.2439 0.2542 0.4865 0.0408  0.0534  -0.0753 84 HIS B ND1 
1226 C CD2 . HIS B 84 ? 0.2379 0.2349 0.4424 0.0442  0.0112  -0.0803 84 HIS B CD2 
1227 C CE1 . HIS B 84 ? 0.2062 0.2418 0.4953 0.0496  0.0396  -0.0747 84 HIS B CE1 
1228 N NE2 . HIS B 84 ? 0.2195 0.2457 0.4830 0.0523  0.0122  -0.0780 84 HIS B NE2 
1229 N N   . LEU B 85 ? 0.2554 0.1649 0.2901 0.0188  0.0526  -0.0816 85 LEU B N   
1230 C CA  . LEU B 85 ? 0.3112 0.2082 0.3126 0.0124  0.0570  -0.0800 85 LEU B CA  
1231 C C   . LEU B 85 ? 0.3500 0.2236 0.3148 0.0183  0.0705  -0.0835 85 LEU B C   
1232 O O   . LEU B 85 ? 0.3884 0.2547 0.3330 0.0194  0.0842  -0.0801 85 LEU B O   
1233 C CB  . LEU B 85 ? 0.2788 0.1745 0.2621 0.0057  0.0387  -0.0795 85 LEU B CB  
1234 C CG  . LEU B 85 ? 0.2886 0.2014 0.2947 0.0034  0.0268  -0.0784 85 LEU B CG  
1235 C CD1 . LEU B 85 ? 0.3191 0.2317 0.3061 0.0018  0.0139  -0.0766 85 LEU B CD1 
1236 C CD2 . LEU B 85 ? 0.2779 0.1921 0.2920 -0.0007 0.0333  -0.0758 85 LEU B CD2 
1237 N N   . ARG B 86 ? 0.3722 0.2295 0.3245 0.0236  0.0666  -0.0902 86 ARG B N   
1238 C CA  . ARG B 86 ? 0.4206 0.2479 0.3316 0.0314  0.0772  -0.0983 86 ARG B CA  
1239 C C   . ARG B 86 ? 0.4470 0.2767 0.3651 0.0459  0.1062  -0.0972 86 ARG B C   
1240 O O   . ARG B 86 ? 0.5064 0.3152 0.3817 0.0535  0.1210  -0.1005 86 ARG B O   
1241 C CB  . ARG B 86 ? 0.4387 0.2406 0.3363 0.0330  0.0648  -0.1072 86 ARG B CB  
1242 C CG  . ARG B 86 ? 0.4602 0.2574 0.3488 0.0177  0.0405  -0.1061 86 ARG B CG  
1243 C CD  . ARG B 86 ? 0.5781 0.3397 0.4492 0.0173  0.0310  -0.1153 86 ARG B CD  
1244 N NE  . ARG B 86 ? 0.6755 0.4351 0.5480 0.0001  0.0096  -0.1113 86 ARG B NE  
1245 C CZ  . ARG B 86 ? 0.7432 0.4963 0.5934 -0.0113 -0.0040 -0.1155 86 ARG B CZ  
1246 N NH1 . ARG B 86 ? 0.7274 0.4860 0.5920 -0.0277 -0.0220 -0.1093 86 ARG B NH1 
1247 N NH2 . ARG B 86 ? 0.7835 0.5265 0.5981 -0.0053 0.0005  -0.1242 86 ARG B NH2 
1248 N N   . ALA B 87 ? 0.4139 0.2702 0.3851 0.0510  0.1146  -0.0919 87 ALA B N   
1249 C CA  . ALA B 87 ? 0.4206 0.2913 0.4166 0.0636  0.1456  -0.0862 87 ALA B CA  
1250 C C   . ALA B 87 ? 0.4214 0.3040 0.4202 0.0560  0.1610  -0.0743 87 ALA B C   
1251 O O   . ALA B 87 ? 0.4262 0.3140 0.4303 0.0657  0.1921  -0.0666 87 ALA B O   
1252 C CB  . ALA B 87 ? 0.3809 0.2845 0.4446 0.0683  0.1449  -0.0819 87 ALA B CB  
1253 N N   . SER B 88 ? 0.4224 0.3089 0.4202 0.0402  0.1423  -0.0706 88 SER B N   
1254 C CA  . SER B 88 ? 0.4523 0.3429 0.4513 0.0344  0.1585  -0.0573 88 SER B CA  
1255 C C   . SER B 88 ? 0.5147 0.3740 0.4421 0.0446  0.1743  -0.0568 88 SER B C   
1256 O O   . SER B 88 ? 0.5778 0.4359 0.4976 0.0483  0.2008  -0.0429 88 SER B O   
1257 C CB  . SER B 88 ? 0.4293 0.3267 0.4429 0.0187  0.1359  -0.0543 88 SER B CB  
1258 O OG  . SER B 88 ? 0.4500 0.3276 0.4136 0.0170  0.1180  -0.0596 88 SER B OG  
# 
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  SER 1  1  1  SER SER A . n 
A 1 2  GLY 2  2  2  GLY GLY A . n 
A 1 3  HIS 3  3  3  HIS HIS A . n 
A 1 4  THR 4  4  4  THR THR A . n 
A 1 5  ALA 5  5  5  ALA ALA A . n 
A 1 6  HIS 6  6  6  HIS HIS A . n 
A 1 7  VAL 7  7  7  VAL VAL A . n 
A 1 8  ASP 8  8  8  ASP ASP A . n 
A 1 9  GLU 9  9  9  GLU GLU A . n 
A 1 10 ALA 10 10 10 ALA ALA A . n 
A 1 11 VAL 11 11 11 VAL VAL A . n 
A 1 12 LYS 12 12 12 LYS LYS A . n 
A 1 13 HIS 13 13 13 HIS HIS A . n 
A 1 14 ALA 14 14 14 ALA ALA A . n 
A 1 15 GLU 15 15 15 GLU GLU A . n 
A 1 16 GLU 16 16 16 GLU GLU A . n 
A 1 17 ALA 17 17 17 ALA ALA A . n 
A 1 18 VAL 18 18 18 VAL VAL A . n 
A 1 19 ALA 19 19 19 ALA ALA A . n 
A 1 20 HIS 20 20 20 HIS HIS A . n 
A 1 21 GLY 21 21 21 GLY GLY A . n 
A 1 22 LYS 22 22 22 LYS LYS A . n 
A 1 23 GLU 23 23 23 GLU GLU A . n 
A 1 24 GLY 24 24 24 GLY GLY A . n 
A 1 25 HIS 25 25 25 HIS HIS A . n 
A 1 26 THR 26 26 26 THR THR A . n 
A 1 27 ASP 27 27 27 ASP ASP A . n 
A 1 28 GLN 28 28 28 GLN GLN A . n 
A 1 29 LEU 29 29 29 LEU LEU A . n 
A 1 30 LEU 30 30 30 LEU LEU A . n 
A 1 31 GLU 31 31 31 GLU GLU A . n 
A 1 32 HIS 32 32 32 HIS HIS A . n 
A 1 33 ALA 33 33 33 ALA ALA A . n 
A 1 34 LYS 34 34 34 LYS LYS A . n 
A 1 35 GLU 35 35 35 GLU GLU A . n 
A 1 36 SER 36 36 36 SER SER A . n 
A 1 37 LEU 37 37 37 LEU LEU A . n 
A 1 38 THR 38 38 38 THR THR A . n 
A 1 39 HIS 39 39 39 HIS HIS A . n 
A 1 40 ALA 40 40 40 ALA ALA A . n 
A 1 41 LYS 41 41 41 LYS LYS A . n 
A 1 42 ALA 42 42 42 ALA ALA A . n 
A 1 43 ALA 43 43 43 ALA ALA A . n 
A 1 44 SER 44 44 44 SER SER A . n 
A 1 45 GLU 45 45 ?  ?   ?   A . n 
A 1 46 ALA 46 46 ?  ?   ?   A . n 
A 1 47 GLY 47 47 ?  ?   ?   A . n 
A 1 48 GLY 48 48 ?  ?   ?   A . n 
A 1 49 ASN 49 49 ?  ?   ?   A . n 
A 1 50 THR 50 50 50 THR THR A . n 
A 1 51 HIS 51 51 51 HIS HIS A . n 
A 1 52 VAL 52 52 52 VAL VAL A . n 
A 1 53 GLY 53 53 53 GLY GLY A . n 
A 1 54 HIS 54 54 54 HIS HIS A . n 
A 1 55 GLY 55 55 55 GLY GLY A . n 
A 1 56 ILE 56 56 56 ILE ILE A . n 
A 1 57 LYS 57 57 57 LYS LYS A . n 
A 1 58 HIS 58 58 58 HIS HIS A . n 
A 1 59 LEU 59 59 59 LEU LEU A . n 
A 1 60 GLU 60 60 60 GLU GLU A . n 
A 1 61 ASP 61 61 61 ASP ASP A . n 
A 1 62 ALA 62 62 62 ALA ALA A . n 
A 1 63 ILE 63 63 63 ILE ILE A . n 
A 1 64 LYS 64 64 64 LYS LYS A . n 
A 1 65 HIS 65 65 65 HIS HIS A . n 
A 1 66 GLY 66 66 66 GLY GLY A . n 
A 1 67 GLU 67 67 67 GLU GLU A . n 
A 1 68 GLU 68 68 68 GLU GLU A . n 
A 1 69 GLY 69 69 69 GLY GLY A . n 
A 1 70 HIS 70 70 70 HIS HIS A . n 
A 1 71 VAL 71 71 71 VAL VAL A . n 
A 1 72 GLY 72 72 72 GLY GLY A . n 
A 1 73 VAL 73 73 73 VAL VAL A . n 
A 1 74 ALA 74 74 74 ALA ALA A . n 
A 1 75 THR 75 75 75 THR THR A . n 
A 1 76 LYS 76 76 76 LYS LYS A . n 
A 1 77 HIS 77 77 77 HIS HIS A . n 
A 1 78 ALA 78 78 78 ALA ALA A . n 
A 1 79 GLN 79 79 79 GLN GLN A . n 
A 1 80 GLU 80 80 80 GLU GLU A . n 
A 1 81 ALA 81 81 81 ALA ALA A . n 
A 1 82 ILE 82 82 82 ILE ILE A . n 
A 1 83 GLU 83 83 83 GLU GLU A . n 
A 1 84 HIS 84 84 84 HIS HIS A . n 
A 1 85 LEU 85 85 85 LEU LEU A . n 
A 1 86 ARG 86 86 86 ARG ARG A . n 
A 1 87 ALA 87 87 87 ALA ALA A . n 
A 1 88 SER 88 88 88 SER SER A . n 
A 1 89 GLU 89 89 ?  ?   ?   A . n 
A 1 90 HIS 90 90 ?  ?   ?   A . n 
A 1 91 LYS 91 91 ?  ?   ?   A . n 
A 1 92 SER 92 92 ?  ?   ?   A . n 
A 1 93 HIS 93 93 ?  ?   ?   A . n 
B 1 1  SER 1  1  1  SER SER B . n 
B 1 2  GLY 2  2  2  GLY GLY B . n 
B 1 3  HIS 3  3  3  HIS HIS B . n 
B 1 4  THR 4  4  4  THR THR B . n 
B 1 5  ALA 5  5  5  ALA ALA B . n 
B 1 6  HIS 6  6  6  HIS HIS B . n 
B 1 7  VAL 7  7  7  VAL VAL B . n 
B 1 8  ASP 8  8  8  ASP ASP B . n 
B 1 9  GLU 9  9  9  GLU GLU B . n 
B 1 10 ALA 10 10 10 ALA ALA B . n 
B 1 11 VAL 11 11 11 VAL VAL B . n 
B 1 12 LYS 12 12 12 LYS LYS B . n 
B 1 13 HIS 13 13 13 HIS HIS B . n 
B 1 14 ALA 14 14 14 ALA ALA B . n 
B 1 15 GLU 15 15 15 GLU GLU B . n 
B 1 16 GLU 16 16 16 GLU GLU B . n 
B 1 17 ALA 17 17 17 ALA ALA B . n 
B 1 18 VAL 18 18 18 VAL VAL B . n 
B 1 19 ALA 19 19 19 ALA ALA B . n 
B 1 20 HIS 20 20 20 HIS HIS B . n 
B 1 21 GLY 21 21 21 GLY GLY B . n 
B 1 22 LYS 22 22 22 LYS LYS B . n 
B 1 23 GLU 23 23 23 GLU GLU B . n 
B 1 24 GLY 24 24 24 GLY GLY B . n 
B 1 25 HIS 25 25 25 HIS HIS B . n 
B 1 26 THR 26 26 26 THR THR B . n 
B 1 27 ASP 27 27 27 ASP ASP B . n 
B 1 28 GLN 28 28 28 GLN GLN B . n 
B 1 29 LEU 29 29 29 LEU LEU B . n 
B 1 30 LEU 30 30 30 LEU LEU B . n 
B 1 31 GLU 31 31 31 GLU GLU B . n 
B 1 32 HIS 32 32 32 HIS HIS B . n 
B 1 33 ALA 33 33 33 ALA ALA B . n 
B 1 34 LYS 34 34 34 LYS LYS B . n 
B 1 35 GLU 35 35 35 GLU GLU B . n 
B 1 36 SER 36 36 36 SER SER B . n 
B 1 37 LEU 37 37 37 LEU LEU B . n 
B 1 38 THR 38 38 38 THR THR B . n 
B 1 39 HIS 39 39 39 HIS HIS B . n 
B 1 40 ALA 40 40 40 ALA ALA B . n 
B 1 41 LYS 41 41 41 LYS LYS B . n 
B 1 42 ALA 42 42 42 ALA ALA B . n 
B 1 43 ALA 43 43 43 ALA ALA B . n 
B 1 44 SER 44 44 44 SER SER B . n 
B 1 45 GLU 45 45 ?  ?   ?   B . n 
B 1 46 ALA 46 46 ?  ?   ?   B . n 
B 1 47 GLY 47 47 ?  ?   ?   B . n 
B 1 48 GLY 48 48 ?  ?   ?   B . n 
B 1 49 ASN 49 49 ?  ?   ?   B . n 
B 1 50 THR 50 50 50 THR THR B . n 
B 1 51 HIS 51 51 51 HIS HIS B . n 
B 1 52 VAL 52 52 52 VAL VAL B . n 
B 1 53 GLY 53 53 53 GLY GLY B . n 
B 1 54 HIS 54 54 54 HIS HIS B . n 
B 1 55 GLY 55 55 55 GLY GLY B . n 
B 1 56 ILE 56 56 56 ILE ILE B . n 
B 1 57 LYS 57 57 57 LYS LYS B . n 
B 1 58 HIS 58 58 58 HIS HIS B . n 
B 1 59 LEU 59 59 59 LEU LEU B . n 
B 1 60 GLU 60 60 60 GLU GLU B . n 
B 1 61 ASP 61 61 61 ASP ASP B . n 
B 1 62 ALA 62 62 62 ALA ALA B . n 
B 1 63 ILE 63 63 63 ILE ILE B . n 
B 1 64 LYS 64 64 64 LYS LYS B . n 
B 1 65 HIS 65 65 65 HIS HIS B . n 
B 1 66 GLY 66 66 66 GLY GLY B . n 
B 1 67 GLU 67 67 67 GLU GLU B . n 
B 1 68 GLU 68 68 68 GLU GLU B . n 
B 1 69 GLY 69 69 69 GLY GLY B . n 
B 1 70 HIS 70 70 70 HIS HIS B . n 
B 1 71 VAL 71 71 71 VAL VAL B . n 
B 1 72 GLY 72 72 72 GLY GLY B . n 
B 1 73 VAL 73 73 73 VAL VAL B . n 
B 1 74 ALA 74 74 74 ALA ALA B . n 
B 1 75 THR 75 75 75 THR THR B . n 
B 1 76 LYS 76 76 76 LYS LYS B . n 
B 1 77 HIS 77 77 77 HIS HIS B . n 
B 1 78 ALA 78 78 78 ALA ALA B . n 
B 1 79 GLN 79 79 79 GLN GLN B . n 
B 1 80 GLU 80 80 80 GLU GLU B . n 
B 1 81 ALA 81 81 81 ALA ALA B . n 
B 1 82 ILE 82 82 82 ILE ILE B . n 
B 1 83 GLU 83 83 83 GLU GLU B . n 
B 1 84 HIS 84 84 84 HIS HIS B . n 
B 1 85 LEU 85 85 85 LEU LEU B . n 
B 1 86 ARG 86 86 86 ARG ARG B . n 
B 1 87 ALA 87 87 87 ALA ALA B . n 
B 1 88 SER 88 88 88 SER SER B . n 
B 1 89 GLU 89 89 ?  ?   ?   B . n 
B 1 90 HIS 90 90 ?  ?   ?   B . n 
B 1 91 LYS 91 91 ?  ?   ?   B . n 
B 1 92 SER 92 92 ?  ?   ?   B . n 
B 1 93 HIS 93 93 ?  ?   ?   B . n 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly   ?    monomeric 1 
2 author_defined_assembly   ?    monomeric 1 
3 software_defined_assembly PISA dimeric   2 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D     
2 1 B,E       
3 1 A,B,C,D,E 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
3 'ABSA (A^2)' 810  ? 
3 MORE         -14  ? 
3 'SSA (A^2)'  7980 ? 
# 
_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  N   ? A SER 1 ? A SER 1 ? 1_555 NI ? C NI . ? A NI 94 ? 1_555 N   ? B SER 1 ? B SER 1 ? 1_555 160.0 ? 
2  N   ? A SER 1 ? A SER 1 ? 1_555 NI ? C NI . ? A NI 94 ? 1_555 NE2 ? A HIS 6 ? A HIS 6 ? 1_555 98.3  ? 
3  N   ? B SER 1 ? B SER 1 ? 1_555 NI ? C NI . ? A NI 94 ? 1_555 NE2 ? A HIS 6 ? A HIS 6 ? 1_555 96.6  ? 
4  N   ? A SER 1 ? A SER 1 ? 1_555 NI ? C NI . ? A NI 94 ? 1_555 O   ? B SER 1 ? B SER 1 ? 1_555 89.7  ? 
5  N   ? B SER 1 ? B SER 1 ? 1_555 NI ? C NI . ? A NI 94 ? 1_555 O   ? B SER 1 ? B SER 1 ? 1_555 75.3  ? 
6  NE2 ? A HIS 6 ? A HIS 6 ? 1_555 NI ? C NI . ? A NI 94 ? 1_555 O   ? B SER 1 ? B SER 1 ? 1_555 171.9 ? 
7  N   ? A SER 1 ? A SER 1 ? 1_555 NI ? C NI . ? A NI 94 ? 1_555 NE2 ? B HIS 6 ? B HIS 6 ? 1_555 93.4  ? 
8  N   ? B SER 1 ? B SER 1 ? 1_555 NI ? C NI . ? A NI 94 ? 1_555 NE2 ? B HIS 6 ? B HIS 6 ? 1_555 99.2  ? 
9  NE2 ? A HIS 6 ? A HIS 6 ? 1_555 NI ? C NI . ? A NI 94 ? 1_555 NE2 ? B HIS 6 ? B HIS 6 ? 1_555 92.7  ? 
10 O   ? B SER 1 ? B SER 1 ? 1_555 NI ? C NI . ? A NI 94 ? 1_555 NE2 ? B HIS 6 ? B HIS 6 ? 1_555 88.2  ? 
11 N   ? A SER 1 ? A SER 1 ? 1_555 NI ? C NI . ? A NI 94 ? 1_555 O   ? A SER 1 ? A SER 1 ? 1_555 80.1  ? 
12 N   ? B SER 1 ? B SER 1 ? 1_555 NI ? C NI . ? A NI 94 ? 1_555 O   ? A SER 1 ? A SER 1 ? 1_555 86.0  ? 
13 NE2 ? A HIS 6 ? A HIS 6 ? 1_555 NI ? C NI . ? A NI 94 ? 1_555 O   ? A SER 1 ? A SER 1 ? 1_555 92.2  ? 
14 O   ? B SER 1 ? B SER 1 ? 1_555 NI ? C NI . ? A NI 94 ? 1_555 O   ? A SER 1 ? A SER 1 ? 1_555 87.7  ? 
15 NE2 ? B HIS 6 ? B HIS 6 ? 1_555 NI ? C NI . ? A NI 94 ? 1_555 O   ? A SER 1 ? A SER 1 ? 1_555 172.4 ? 
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2011-11-09 
# 
_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_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][3] 
'X-RAY DIFFRACTION' 1 ? refined -0.7389  -12.2269 10.0138 -0.1355 -0.1369 -0.0701 -0.0067 -0.0108 0.0112  3.8573 1.6708 4.5633 
-0.4139 -0.8883 0.7213  -0.0289 0.1417 -0.1890 0.1380  -0.0323 -0.0098 0.0778  0.2741 0.0612 
'X-RAY DIFFRACTION' 2 ? refined -15.1109 4.5214   12.5569 -0.0423 -0.1029 -0.0880 0.0251  -0.0201 -0.0613 4.1253 5.8558 3.9078 
-1.7613 0.2611  -0.9773 0.1876  0.4000 0.1089  -0.3167 -0.2748 0.2815  -0.0929 0.0759 0.0872 
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
'X-RAY DIFFRACTION' 1 1 A 1 ? ? A 88 ? ? ? ? 
'X-RAY DIFFRACTION' 2 2 B 1 ? ? B 88 ? ? ? ? 
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
ADSC   'data collection' Quantum  ? 1 
SOLVE  phasing           .        ? 2 
REFMAC refinement        5.2.0005 ? 3 
MOSFLM 'data reduction'  .        ? 4 
SCALA  'data scaling'    .        ? 5 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    HIS 
_pdbx_validate_torsion.auth_asym_id    A 
_pdbx_validate_torsion.auth_seq_id     70 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             -112.21 
_pdbx_validate_torsion.psi             78.83 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLU 45 ? A GLU 45 
2  1 Y 1 A ALA 46 ? A ALA 46 
3  1 Y 1 A GLY 47 ? A GLY 47 
4  1 Y 1 A GLY 48 ? A GLY 48 
5  1 Y 1 A ASN 49 ? A ASN 49 
6  1 Y 1 A GLU 89 ? A GLU 89 
7  1 Y 1 A HIS 90 ? A HIS 90 
8  1 Y 1 A LYS 91 ? A LYS 91 
9  1 Y 1 A SER 92 ? A SER 92 
10 1 Y 1 A HIS 93 ? A HIS 93 
11 1 Y 1 B GLU 45 ? B GLU 45 
12 1 Y 1 B ALA 46 ? B ALA 46 
13 1 Y 1 B GLY 47 ? B GLY 47 
14 1 Y 1 B GLY 48 ? B GLY 48 
15 1 Y 1 B ASN 49 ? B ASN 49 
16 1 Y 1 B GLU 89 ? B GLU 89 
17 1 Y 1 B HIS 90 ? B HIS 90 
18 1 Y 1 B LYS 91 ? B LYS 91 
19 1 Y 1 B SER 92 ? B SER 92 
20 1 Y 1 B HIS 93 ? B HIS 93 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'NICKEL (II) ION' NI  
3 water             HOH 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 NI  1  94  1  NI  NI  A . 
D 3 HOH 1  95  95 HOH HOH A . 
D 3 HOH 2  96  2  HOH HOH A . 
D 3 HOH 3  97  97 HOH HOH A . 
D 3 HOH 4  98  3  HOH HOH A . 
D 3 HOH 5  99  7  HOH HOH A . 
D 3 HOH 6  100 9  HOH HOH A . 
D 3 HOH 7  101 10 HOH HOH A . 
D 3 HOH 8  102 11 HOH HOH A . 
D 3 HOH 9  103 12 HOH HOH A . 
D 3 HOH 10 104 14 HOH HOH A . 
D 3 HOH 11 105 15 HOH HOH A . 
D 3 HOH 12 106 16 HOH HOH A . 
D 3 HOH 13 107 18 HOH HOH A . 
D 3 HOH 14 108 20 HOH HOH A . 
D 3 HOH 15 109 21 HOH HOH A . 
D 3 HOH 16 110 22 HOH HOH A . 
D 3 HOH 17 111 26 HOH HOH A . 
D 3 HOH 18 112 29 HOH HOH A . 
D 3 HOH 19 113 32 HOH HOH A . 
D 3 HOH 20 114 34 HOH HOH A . 
D 3 HOH 21 115 36 HOH HOH A . 
D 3 HOH 22 116 37 HOH HOH A . 
D 3 HOH 23 117 38 HOH HOH A . 
D 3 HOH 24 118 39 HOH HOH A . 
D 3 HOH 25 119 41 HOH HOH A . 
D 3 HOH 26 120 45 HOH HOH A . 
D 3 HOH 27 121 46 HOH HOH A . 
D 3 HOH 28 122 47 HOH HOH A . 
D 3 HOH 29 123 48 HOH HOH A . 
D 3 HOH 30 124 49 HOH HOH A . 
D 3 HOH 31 125 52 HOH HOH A . 
D 3 HOH 32 126 58 HOH HOH A . 
D 3 HOH 33 127 59 HOH HOH A . 
D 3 HOH 34 128 60 HOH HOH A . 
D 3 HOH 35 129 61 HOH HOH A . 
D 3 HOH 36 130 67 HOH HOH A . 
D 3 HOH 37 131 71 HOH HOH A . 
D 3 HOH 38 132 72 HOH HOH A . 
D 3 HOH 39 133 73 HOH HOH A . 
D 3 HOH 40 134 74 HOH HOH A . 
D 3 HOH 41 135 75 HOH HOH A . 
D 3 HOH 42 136 76 HOH HOH A . 
D 3 HOH 43 137 77 HOH HOH A . 
D 3 HOH 44 138 79 HOH HOH A . 
D 3 HOH 45 139 80 HOH HOH A . 
D 3 HOH 46 140 81 HOH HOH A . 
D 3 HOH 47 141 82 HOH HOH A . 
D 3 HOH 48 142 83 HOH HOH A . 
D 3 HOH 49 143 85 HOH HOH A . 
D 3 HOH 50 144 86 HOH HOH A . 
D 3 HOH 51 145 87 HOH HOH A . 
D 3 HOH 52 146 88 HOH HOH A . 
D 3 HOH 53 147 89 HOH HOH A . 
D 3 HOH 54 148 90 HOH HOH A . 
D 3 HOH 55 149 91 HOH HOH A . 
E 3 HOH 1  94  94 HOH HOH B . 
E 3 HOH 2  95  1  HOH HOH B . 
E 3 HOH 3  96  96 HOH HOH B . 
E 3 HOH 4  97  4  HOH HOH B . 
E 3 HOH 5  98  5  HOH HOH B . 
E 3 HOH 6  99  6  HOH HOH B . 
E 3 HOH 7  100 8  HOH HOH B . 
E 3 HOH 8  101 13 HOH HOH B . 
E 3 HOH 9  102 17 HOH HOH B . 
E 3 HOH 10 103 19 HOH HOH B . 
E 3 HOH 11 104 23 HOH HOH B . 
E 3 HOH 12 105 24 HOH HOH B . 
E 3 HOH 13 106 25 HOH HOH B . 
E 3 HOH 14 107 27 HOH HOH B . 
E 3 HOH 15 108 28 HOH HOH B . 
E 3 HOH 16 109 30 HOH HOH B . 
E 3 HOH 17 110 31 HOH HOH B . 
E 3 HOH 18 111 33 HOH HOH B . 
E 3 HOH 19 112 35 HOH HOH B . 
E 3 HOH 20 113 40 HOH HOH B . 
E 3 HOH 21 114 42 HOH HOH B . 
E 3 HOH 22 115 43 HOH HOH B . 
E 3 HOH 23 116 44 HOH HOH B . 
E 3 HOH 24 117 50 HOH HOH B . 
E 3 HOH 25 118 51 HOH HOH B . 
E 3 HOH 26 119 53 HOH HOH B . 
E 3 HOH 27 120 54 HOH HOH B . 
E 3 HOH 28 121 55 HOH HOH B . 
E 3 HOH 29 122 56 HOH HOH B . 
E 3 HOH 30 123 57 HOH HOH B . 
E 3 HOH 31 124 62 HOH HOH B . 
E 3 HOH 32 125 63 HOH HOH B . 
E 3 HOH 33 126 64 HOH HOH B . 
E 3 HOH 34 127 65 HOH HOH B . 
E 3 HOH 35 128 66 HOH HOH B . 
E 3 HOH 36 129 68 HOH HOH B . 
E 3 HOH 37 130 69 HOH HOH B . 
E 3 HOH 38 131 70 HOH HOH B . 
E 3 HOH 39 132 78 HOH HOH B . 
E 3 HOH 40 133 84 HOH HOH B . 
E 3 HOH 41 134 92 HOH HOH B . 
E 3 HOH 42 135 93 HOH HOH B . 
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