data_1LED # _entry.id 1LED # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.287 _audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic # loop_ _database_2.database_id _database_2.database_code PDB 1LED WWPDB D_1000174682 # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 1LED _pdbx_database_status.recvd_initial_deposition_date 1992-12-17 _pdbx_database_status.deposit_site ? _pdbx_database_status.process_site BNL _pdbx_database_status.status_code_sf REL _pdbx_database_status.status_code_mr ? _pdbx_database_status.SG_entry ? _pdbx_database_status.pdb_format_compatible Y _pdbx_database_status.status_code_cs ? _pdbx_database_status.methods_development_category ? # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Delbaere, L.' 1 'Vandonselaar, M.' 2 'Quail, J.' 3 # loop_ _citation.id _citation.title _citation.journal_abbrev _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 _citation.book_publisher _citation.pdbx_database_id_PubMed _citation.pdbx_database_id_DOI primary ;Structures of the lectin IV of Griffonia simplicifolia and its complex with the Lewis b human blood group determinant at 2.0 A resolution. ; J.Mol.Biol. 230 950 965 1993 JMOBAK UK 0022-2836 0070 ? 8478943 10.1006/jmbi.1993.1212 1 'Molecular Recognition of a Human Blood Group Determinant by a Plant Lectin' Can.J.Chem. 68 1116 ? 1990 CJCHAG CA 0008-4042 0015 ? ? ? 2 'Structures of Griffonia Simplicifolia Lectin Iv and its Complex with a Synthetic Lewis B Blood Group Determinant' Trans.Am.Crystallogr.Assoc. 25 65 ? 1991 TACAAH US 0065-8006 0285 ? ? ? # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Delbaere, L.T.' 1 primary 'Vandonselaar, M.' 2 primary 'Prasad, L.' 3 primary 'Quail, J.W.' 4 primary 'Wilson, K.S.' 5 primary 'Dauter, Z.' 6 1 'Delbaere, L.T.J.' 7 1 'Vandonselaar, M.' 8 1 'Prasad, L.' 9 1 'Quail, J.W.' 10 1 'Pearlstone, J.R.' 11 1 'Carpenter, M.R.' 12 1 'Smillie, L.B.' 13 1 'Nikrad, P.V.' 14 1 'Spohr, U.' 15 1 'Lemieux, R.U.' 16 2 'Delbaere, L.T.J.' 17 2 'Vandonselaar, M.' 18 2 'Prasad, L.' 19 2 'Quail, J.W.' 20 2 'Nikrad, P.V.' 21 2 'Pearlstone, J.R.' 22 2 'Carpenter, M.R.' 23 2 'Smillie, L.B.' 24 2 'Spohr, U.' 25 2 'Lemieux, R.U.' 26 # _cell.entry_id 1LED _cell.length_a 78.900 _cell.length_b 78.900 _cell.length_c 89.100 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 90.00 _cell.Z_PDB 8 _cell.pdbx_unique_axis ? # _symmetry.entry_id 1LED _symmetry.space_group_name_H-M 'P 42 21 2' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 94 # loop_ _entity.id _entity.type _entity.src_method _entity.pdbx_description _entity.formula_weight _entity.pdbx_number_of_molecules _entity.pdbx_ec _entity.pdbx_mutation _entity.pdbx_fragment _entity.details 1 polymer man 'WEST-CENTRAL AFRICAN LEGUME LECTIN IV' 26816.678 1 ? ? ? ? 2 non-polymer man ALPHA-L-FUCOSE 164.156 3 ? ? ? ? 3 non-polymer man BETA-D-GALACTOSE 180.156 1 ? ? ? ? 4 non-polymer man BETA-METHYL-N-ACETYL-D-GLUCOSAMINE 235.234 1 ? ? ? ? 5 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 2 ? ? ? ? 6 non-polymer syn 'MANGANESE (II) ION' 54.938 1 ? ? ? ? 7 non-polymer syn 'CALCIUM ION' 40.078 1 ? ? ? ? 8 non-polymer syn 'SULFATE ION' 96.063 1 ? ? ? ? 9 water nat water 18.015 144 ? ? ? ? # _entity_poly.entity_id 1 _entity_poly.type 'polypeptide(L)' _entity_poly.nstd_linkage no _entity_poly.nstd_monomer yes _entity_poly.pdbx_seq_one_letter_code ;(PCA)NTVNFTYPDFWSYSLKNGTEITFLGDATRIPGALQLTKTDANGNPVRSSAGQASYSEPVFLWDSTGKAASFYTSF TFLLKNYGAPTADGLAFFLAPVDSSVKDYGGFLGLFRHETAADPSKNQVVAVEFDTWINKDWNDPPYPHIGIDVNSIVSV ATTRWENDDAYGSSIATAHITYDARSKILTVLLSYEHGRDYILSHVVDLAKVLPQKVRIGFSAGVGYDEVTYILSWHFFS TLDGTNK ; _entity_poly.pdbx_seq_one_letter_code_can ;ENTVNFTYPDFWSYSLKNGTEITFLGDATRIPGALQLTKTDANGNPVRSSAGQASYSEPVFLWDSTGKAASFYTSFTFLL KNYGAPTADGLAFFLAPVDSSVKDYGGFLGLFRHETAADPSKNQVVAVEFDTWINKDWNDPPYPHIGIDVNSIVSVATTR WENDDAYGSSIATAHITYDARSKILTVLLSYEHGRDYILSHVVDLAKVLPQKVRIGFSAGVGYDEVTYILSWHFFSTLDG TNK ; _entity_poly.pdbx_strand_id A _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 PCA n 1 2 ASN n 1 3 THR n 1 4 VAL n 1 5 ASN n 1 6 PHE n 1 7 THR n 1 8 TYR n 1 9 PRO n 1 10 ASP n 1 11 PHE n 1 12 TRP n 1 13 SER n 1 14 TYR n 1 15 SER n 1 16 LEU n 1 17 LYS n 1 18 ASN n 1 19 GLY n 1 20 THR n 1 21 GLU n 1 22 ILE n 1 23 THR n 1 24 PHE n 1 25 LEU n 1 26 GLY n 1 27 ASP n 1 28 ALA n 1 29 THR n 1 30 ARG n 1 31 ILE n 1 32 PRO n 1 33 GLY n 1 34 ALA n 1 35 LEU n 1 36 GLN n 1 37 LEU n 1 38 THR n 1 39 LYS n 1 40 THR n 1 41 ASP n 1 42 ALA n 1 43 ASN n 1 44 GLY n 1 45 ASN n 1 46 PRO n 1 47 VAL n 1 48 ARG n 1 49 SER n 1 50 SER n 1 51 ALA n 1 52 GLY n 1 53 GLN n 1 54 ALA n 1 55 SER n 1 56 TYR n 1 57 SER n 1 58 GLU n 1 59 PRO n 1 60 VAL n 1 61 PHE n 1 62 LEU n 1 63 TRP n 1 64 ASP n 1 65 SER n 1 66 THR n 1 67 GLY n 1 68 LYS n 1 69 ALA n 1 70 ALA n 1 71 SER n 1 72 PHE n 1 73 TYR n 1 74 THR n 1 75 SER n 1 76 PHE n 1 77 THR n 1 78 PHE n 1 79 LEU n 1 80 LEU n 1 81 LYS n 1 82 ASN n 1 83 TYR n 1 84 GLY n 1 85 ALA n 1 86 PRO n 1 87 THR n 1 88 ALA n 1 89 ASP n 1 90 GLY n 1 91 LEU n 1 92 ALA n 1 93 PHE n 1 94 PHE n 1 95 LEU n 1 96 ALA n 1 97 PRO n 1 98 VAL n 1 99 ASP n 1 100 SER n 1 101 SER n 1 102 VAL n 1 103 LYS n 1 104 ASP n 1 105 TYR n 1 106 GLY n 1 107 GLY n 1 108 PHE n 1 109 LEU n 1 110 GLY n 1 111 LEU n 1 112 PHE n 1 113 ARG n 1 114 HIS n 1 115 GLU n 1 116 THR n 1 117 ALA n 1 118 ALA n 1 119 ASP n 1 120 PRO n 1 121 SER n 1 122 LYS n 1 123 ASN n 1 124 GLN n 1 125 VAL n 1 126 VAL n 1 127 ALA n 1 128 VAL n 1 129 GLU n 1 130 PHE n 1 131 ASP n 1 132 THR n 1 133 TRP n 1 134 ILE n 1 135 ASN n 1 136 LYS n 1 137 ASP n 1 138 TRP n 1 139 ASN n 1 140 ASP n 1 141 PRO n 1 142 PRO n 1 143 TYR n 1 144 PRO n 1 145 HIS n 1 146 ILE n 1 147 GLY n 1 148 ILE n 1 149 ASP n 1 150 VAL n 1 151 ASN n 1 152 SER n 1 153 ILE n 1 154 VAL n 1 155 SER n 1 156 VAL n 1 157 ALA n 1 158 THR n 1 159 THR n 1 160 ARG n 1 161 TRP n 1 162 GLU n 1 163 ASN n 1 164 ASP n 1 165 ASP n 1 166 ALA n 1 167 TYR n 1 168 GLY n 1 169 SER n 1 170 SER n 1 171 ILE n 1 172 ALA n 1 173 THR n 1 174 ALA n 1 175 HIS n 1 176 ILE n 1 177 THR n 1 178 TYR n 1 179 ASP n 1 180 ALA n 1 181 ARG n 1 182 SER n 1 183 LYS n 1 184 ILE n 1 185 LEU n 1 186 THR n 1 187 VAL n 1 188 LEU n 1 189 LEU n 1 190 SER n 1 191 TYR n 1 192 GLU n 1 193 HIS n 1 194 GLY n 1 195 ARG n 1 196 ASP n 1 197 TYR n 1 198 ILE n 1 199 LEU n 1 200 SER n 1 201 HIS n 1 202 VAL n 1 203 VAL n 1 204 ASP n 1 205 LEU n 1 206 ALA n 1 207 LYS n 1 208 VAL n 1 209 LEU n 1 210 PRO n 1 211 GLN n 1 212 LYS n 1 213 VAL n 1 214 ARG n 1 215 ILE n 1 216 GLY n 1 217 PHE n 1 218 SER n 1 219 ALA n 1 220 GLY n 1 221 VAL n 1 222 GLY n 1 223 TYR n 1 224 ASP n 1 225 GLU n 1 226 VAL n 1 227 THR n 1 228 TYR n 1 229 ILE n 1 230 LEU n 1 231 SER n 1 232 TRP n 1 233 HIS n 1 234 PHE n 1 235 PHE n 1 236 SER n 1 237 THR n 1 238 LEU n 1 239 ASP n 1 240 GLY n 1 241 THR n 1 242 ASN n 1 243 LYS n # _entity_src_gen.entity_id 1 _entity_src_gen.pdbx_src_id 1 _entity_src_gen.pdbx_alt_source_flag sample _entity_src_gen.pdbx_seq_type ? _entity_src_gen.pdbx_beg_seq_num ? _entity_src_gen.pdbx_end_seq_num ? _entity_src_gen.gene_src_common_name ? _entity_src_gen.gene_src_genus ? _entity_src_gen.pdbx_gene_src_gene ? _entity_src_gen.gene_src_species ? _entity_src_gen.gene_src_strain ? _entity_src_gen.gene_src_tissue ? _entity_src_gen.gene_src_tissue_fraction ? _entity_src_gen.gene_src_details ? _entity_src_gen.pdbx_gene_src_fragment ? _entity_src_gen.pdbx_gene_src_scientific_name 'Griffonia simplicifolia' _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 3850 _entity_src_gen.pdbx_gene_src_variant ? _entity_src_gen.pdbx_gene_src_cell_line ? _entity_src_gen.pdbx_gene_src_atcc ? _entity_src_gen.pdbx_gene_src_organ ? _entity_src_gen.pdbx_gene_src_organelle ? _entity_src_gen.pdbx_gene_src_cell ? _entity_src_gen.pdbx_gene_src_cellular_location ? _entity_src_gen.host_org_common_name ? _entity_src_gen.pdbx_host_org_scientific_name ? _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id ? _entity_src_gen.host_org_genus ? _entity_src_gen.pdbx_host_org_gene ? _entity_src_gen.pdbx_host_org_organ ? _entity_src_gen.host_org_species ? _entity_src_gen.pdbx_host_org_tissue ? _entity_src_gen.pdbx_host_org_tissue_fraction ? _entity_src_gen.pdbx_host_org_strain ? _entity_src_gen.pdbx_host_org_variant ? _entity_src_gen.pdbx_host_org_cell_line ? _entity_src_gen.pdbx_host_org_atcc ? _entity_src_gen.pdbx_host_org_culture_collection ? _entity_src_gen.pdbx_host_org_cell ? _entity_src_gen.pdbx_host_org_organelle ? _entity_src_gen.pdbx_host_org_cellular_location ? _entity_src_gen.pdbx_host_org_vector_type ? _entity_src_gen.pdbx_host_org_vector ? _entity_src_gen.host_org_details ? _entity_src_gen.expression_system_id ? _entity_src_gen.plasmid_name ? _entity_src_gen.plasmid_details ? _entity_src_gen.pdbx_description ? # _struct_ref.id 1 _struct_ref.db_name UNP _struct_ref.db_code LEC4_GRISI _struct_ref.entity_id 1 _struct_ref.pdbx_db_accession P24146 _struct_ref.pdbx_align_begin 1 _struct_ref.pdbx_seq_one_letter_code ;QNTVNFTYPDFWSYSLKNGTEITFLGDATRIPGALQLTKTDANGNPVRSSAGQASYSEPVFLWDSTGKAASFYTSFTFLL KNYGAPTADGLAFFLAPVDSSVKDYGGFLGLFRHETAADPSKNQVVAVEFDTWINKDWNDPPYPHIGIDVNSIVSVATTR WENDDAYGSSIATAHITYDARSKILTVLLSYEHGRDYILSHVVDLAKVLPQKVRIGFSAGVGYDEVTYILSWHFFSTLDG TNK ; _struct_ref.pdbx_db_isoform ? # _struct_ref_seq.align_id 1 _struct_ref_seq.ref_id 1 _struct_ref_seq.pdbx_PDB_id_code 1LED _struct_ref_seq.pdbx_strand_id A _struct_ref_seq.seq_align_beg 2 _struct_ref_seq.pdbx_seq_align_beg_ins_code ? _struct_ref_seq.seq_align_end 243 _struct_ref_seq.pdbx_seq_align_end_ins_code ? _struct_ref_seq.pdbx_db_accession P24146 _struct_ref_seq.db_align_beg 2 _struct_ref_seq.pdbx_db_align_beg_ins_code ? _struct_ref_seq.db_align_end 243 _struct_ref_seq.pdbx_db_align_end_ins_code ? _struct_ref_seq.pdbx_auth_seq_align_beg 2 _struct_ref_seq.pdbx_auth_seq_align_end 243 # 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 CA non-polymer . 'CALCIUM ION' ? 'Ca 2' 40.078 FUC saccharide . ALPHA-L-FUCOSE ? 'C6 H12 O5' 164.156 GAL D-saccharide . BETA-D-GALACTOSE ? 'C6 H12 O6' 180.156 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 MAG D-saccharide . BETA-METHYL-N-ACETYL-D-GLUCOSAMINE ? 'C9 H17 N O6' 235.234 MN non-polymer . 'MANGANESE (II) ION' ? 'Mn 2' 54.938 NAG D-saccharide . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6' 221.208 PCA 'L-peptide linking' n 'PYROGLUTAMIC ACID' ? 'C5 H7 N O3' 129.114 PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.189 PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.130 SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093 SO4 non-polymer . 'SULFATE ION' ? 'O4 S -2' 96.063 THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3' 119.119 TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2' 204.225 TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3' 181.189 VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2' 117.146 # _exptl.entry_id 1LED _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number ? # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 2.58 _exptl_crystal.density_percent_sol 52.41 _exptl_crystal.description ? # _diffrn.id 1 _diffrn.ambient_temp ? _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l ? _diffrn_radiation.monochromator ? _diffrn_radiation.pdbx_diffrn_protocol ? _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength . _diffrn_radiation_wavelength.wt 1.0 # _refine.entry_id 1LED _refine.ls_number_reflns_obs 19212 _refine.ls_number_reflns_all ? _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F ? _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low ? _refine.ls_d_res_high 2.0 _refine.ls_percent_reflns_obs ? _refine.ls_R_factor_obs 0.181 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work ? _refine.ls_R_factor_R_free ? _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free ? _refine.ls_number_reflns_R_free ? _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.B_iso_mean ? _refine.aniso_B[1][1] ? _refine.aniso_B[2][2] ? _refine.aniso_B[3][3] ? _refine.aniso_B[1][2] ? _refine.aniso_B[1][3] ? _refine.aniso_B[2][3] ? _refine.solvent_model_details ? _refine.solvent_model_param_ksol ? _refine.solvent_model_param_bsol ? _refine.pdbx_ls_cross_valid_method ? _refine.details ;RESIDUES 1 AND 241 - 243 HAVE VERY HIGH TEMPERATURE FACTORS AND ARE NOT WELL DETERMINED. ; _refine.pdbx_starting_model ? _refine.pdbx_method_to_determine_struct ? _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_stereochemistry_target_values ? _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details ? _refine.pdbx_overall_ESU_R ? _refine.pdbx_overall_ESU_R_Free ? _refine.overall_SU_ML ? _refine.overall_SU_B ? _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.correlation_coeff_Fo_to_Fc ? _refine.correlation_coeff_Fo_to_Fc_free ? _refine.pdbx_solvent_vdw_probe_radii ? _refine.pdbx_solvent_ion_probe_radii ? _refine.pdbx_solvent_shrinkage_radii ? _refine.pdbx_overall_phase_error ? _refine.overall_SU_R_Cruickshank_DPI ? _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 1904 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 92 _refine_hist.number_atoms_solvent 144 _refine_hist.number_atoms_total 2140 _refine_hist.d_res_high 2.0 _refine_hist.d_res_low . # loop_ _refine_ls_restr.type _refine_ls_restr.dev_ideal _refine_ls_restr.dev_ideal_target _refine_ls_restr.weight _refine_ls_restr.number _refine_ls_restr.pdbx_refine_id _refine_ls_restr.pdbx_restraint_function p_bond_d 0.016 ? ? ? 'X-RAY DIFFRACTION' ? p_angle_d 3.02 ? ? ? 'X-RAY DIFFRACTION' ? p_angle_deg ? ? ? ? 'X-RAY DIFFRACTION' ? p_planar_d ? ? ? ? 'X-RAY DIFFRACTION' ? p_hb_or_metal_coord ? ? ? ? 'X-RAY DIFFRACTION' ? p_mcbond_it ? ? ? ? 'X-RAY DIFFRACTION' ? p_mcangle_it ? ? ? ? 'X-RAY DIFFRACTION' ? p_scbond_it ? ? ? ? 'X-RAY DIFFRACTION' ? p_scangle_it ? ? ? ? 'X-RAY DIFFRACTION' ? p_plane_restr ? ? ? ? 'X-RAY DIFFRACTION' ? p_chiral_restr ? ? ? ? 'X-RAY DIFFRACTION' ? p_singtor_nbd ? ? ? ? 'X-RAY DIFFRACTION' ? p_multtor_nbd ? ? ? ? 'X-RAY DIFFRACTION' ? p_xhyhbond_nbd ? ? ? ? 'X-RAY DIFFRACTION' ? p_xyhbond_nbd ? ? ? ? 'X-RAY DIFFRACTION' ? p_planar_tor ? ? ? ? 'X-RAY DIFFRACTION' ? p_staggered_tor ? ? ? ? 'X-RAY DIFFRACTION' ? p_orthonormal_tor ? ? ? ? 'X-RAY DIFFRACTION' ? p_transverse_tor ? ? ? ? 'X-RAY DIFFRACTION' ? p_special_tor ? ? ? ? 'X-RAY DIFFRACTION' ? # _struct.entry_id 1LED _struct.title ;STRUCTURES OF THE LECTIN IV OF GRIFFONIA SIMPLICIFOLIA AND ITS COMPLEX WITH THE LEWIS B HUMAN BLOOD GROUP DETERMINANT AT 2.0 ANGSTROMS RESOLUTION ; _struct.pdbx_descriptor 'LECTIN (FOURTH ISOLATED FROM (GRIFFONIA SIMPLICIFOLIA)) COMPLEX WITH LEWIS B HUMAN BLOOD GROUP DETERMINANT (GS4LEB)' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 1LED _struct_keywords.pdbx_keywords LECTIN _struct_keywords.text LECTIN # 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 2 ? C N N 3 ? D N N 2 ? E N N 4 ? F N N 5 ? G N N 5 ? H N N 2 ? I N N 6 ? J N N 7 ? K N N 8 ? L N N 9 ? # _struct_biol.id 1 # 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 H1 GLU A 162 ? TYR A 167 ? GLU A 162 TYR A 167 1 ? 6 HELX_P HELX_P2 H2 LEU A 205 ? LEU A 209 ? LEU A 205 LEU A 209 1 ? 5 # _struct_conf_type.id HELX_P _struct_conf_type.criteria ? _struct_conf_type.reference ? # loop_ _struct_conn.id _struct_conn.conn_type_id _struct_conn.pdbx_leaving_atom_flag _struct_conn.pdbx_PDB_id _struct_conn.ptnr1_label_asym_id _struct_conn.ptnr1_label_comp_id _struct_conn.ptnr1_label_seq_id _struct_conn.ptnr1_label_atom_id _struct_conn.pdbx_ptnr1_label_alt_id _struct_conn.pdbx_ptnr1_PDB_ins_code _struct_conn.pdbx_ptnr1_standard_comp_id _struct_conn.ptnr1_symmetry _struct_conn.ptnr2_label_asym_id _struct_conn.ptnr2_label_comp_id _struct_conn.ptnr2_label_seq_id _struct_conn.ptnr2_label_atom_id _struct_conn.pdbx_ptnr2_label_alt_id _struct_conn.pdbx_ptnr2_PDB_ins_code _struct_conn.ptnr1_auth_asym_id _struct_conn.ptnr1_auth_comp_id _struct_conn.ptnr1_auth_seq_id _struct_conn.ptnr2_auth_asym_id _struct_conn.ptnr2_auth_comp_id _struct_conn.ptnr2_auth_seq_id _struct_conn.ptnr2_symmetry _struct_conn.pdbx_ptnr3_label_atom_id _struct_conn.pdbx_ptnr3_label_seq_id _struct_conn.pdbx_ptnr3_label_comp_id _struct_conn.pdbx_ptnr3_label_asym_id _struct_conn.pdbx_ptnr3_label_alt_id _struct_conn.pdbx_ptnr3_PDB_ins_code _struct_conn.details _struct_conn.pdbx_dist_value _struct_conn.pdbx_value_order covale1 covale ? ? A ASN 18 ND2 ? ? ? 1_555 G NAG . C1 ? ? A ASN 18 A NAG 257 1_555 ? ? ? ? ? ? ? 1.443 ? covale2 covale ? ? B FUC . C1 ? ? ? 1_555 C GAL . O2 ? ? A FUC 252 A GAL 253 1_555 ? ? ? ? ? ? ? 1.411 ? covale3 covale ? ? C GAL . C1 ? ? ? 1_555 E MAG . O3 ? ? A GAL 253 A MAG 255 1_555 ? ? ? ? ? ? ? 1.428 ? covale4 covale ? ? E MAG . O4 ? ? ? 1_555 D FUC . C1 ? ? A MAG 255 A FUC 254 1_555 ? ? ? ? ? ? ? 1.458 ? covale5 covale ? ? F NAG . C1 ? ? ? 1_555 G NAG . O4 ? ? A NAG 256 A NAG 257 1_555 ? ? ? ? ? ? ? 1.419 ? covale6 covale ? ? G NAG . O3 ? ? ? 1_555 H FUC . C1 ? ? A NAG 257 A FUC 262 1_555 ? ? ? ? ? ? ? 1.427 ? covale7 covale ? ? A PCA 1 C ? ? ? 1_555 A ASN 2 N ? ? A PCA 1 A ASN 2 1_555 ? ? ? ? ? ? ? 1.352 ? metalc1 metalc ? ? I MN . MN ? ? ? 1_555 A HIS 145 NE2 ? ? A MN 250 A HIS 145 1_555 ? ? ? ? ? ? ? 2.218 ? metalc2 metalc ? ? I MN . MN ? ? ? 1_555 A ASP 131 OD2 ? ? A MN 250 A ASP 131 1_555 ? ? ? ? ? ? ? 2.053 ? metalc3 metalc ? ? I MN . MN ? ? ? 1_555 A ASP 140 OD1 ? ? A MN 250 A ASP 140 1_555 ? ? ? ? ? ? ? 2.376 ? metalc4 metalc ? ? I MN . MN ? ? ? 1_555 L HOH . O ? ? A MN 250 A HOH 305 1_555 ? ? ? ? ? ? ? 2.057 ? metalc5 metalc ? ? I MN . MN ? ? ? 1_555 L HOH . O ? ? A MN 250 A HOH 332 1_555 ? ? ? ? ? ? ? 2.183 ? metalc6 metalc ? ? I MN . MN ? ? ? 1_555 A GLU 129 OE2 ? ? A MN 250 A GLU 129 1_555 ? ? ? ? ? ? ? 2.243 ? metalc7 metalc ? ? J CA . CA ? ? ? 1_555 L HOH . O ? ? A CA 251 A HOH 329 1_555 ? ? ? ? ? ? ? 2.210 ? metalc8 metalc ? ? J CA . CA ? ? ? 1_555 A ASP 131 OD2 ? ? A CA 251 A ASP 131 1_555 ? ? ? ? ? ? ? 2.658 ? metalc9 metalc ? ? J CA . CA ? ? ? 1_555 A TRP 133 O ? ? A CA 251 A TRP 133 1_555 ? ? ? ? ? ? ? 2.304 ? metalc10 metalc ? ? J CA . CA ? ? ? 1_555 A ASN 135 OD1 ? ? A CA 251 A ASN 135 1_555 ? ? ? ? ? ? ? 2.467 ? metalc11 metalc ? ? J CA . CA ? ? ? 1_555 A ASP 140 OD2 ? ? A CA 251 A ASP 140 1_555 ? ? ? ? ? ? ? 2.287 ? metalc12 metalc ? ? J CA . CA ? ? ? 1_555 A ASP 131 OD1 ? ? A CA 251 A ASP 131 1_555 ? ? ? ? ? ? ? 2.395 ? metalc13 metalc ? ? J CA . CA ? ? ? 1_555 L HOH . O ? ? A CA 251 A HOH 333 1_555 ? ? ? ? ? ? ? 2.551 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference covale ? ? metalc ? ? # loop_ _struct_mon_prot_cis.pdbx_id _struct_mon_prot_cis.label_comp_id _struct_mon_prot_cis.label_seq_id _struct_mon_prot_cis.label_asym_id _struct_mon_prot_cis.label_alt_id _struct_mon_prot_cis.pdbx_PDB_ins_code _struct_mon_prot_cis.auth_comp_id _struct_mon_prot_cis.auth_seq_id _struct_mon_prot_cis.auth_asym_id _struct_mon_prot_cis.pdbx_label_comp_id_2 _struct_mon_prot_cis.pdbx_label_seq_id_2 _struct_mon_prot_cis.pdbx_label_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_ins_code_2 _struct_mon_prot_cis.pdbx_auth_comp_id_2 _struct_mon_prot_cis.pdbx_auth_seq_id_2 _struct_mon_prot_cis.pdbx_auth_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_model_num _struct_mon_prot_cis.pdbx_omega_angle 1 ALA 85 A . ? ALA 85 A PRO 86 A ? PRO 86 A 1 -6.36 2 ALA 88 A . ? ALA 88 A ASP 89 A ? ASP 89 A 1 1.48 3 VAL 221 A . ? VAL 221 A GLY 222 A ? GLY 222 A 1 1.00 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details B1 ? 6 ? B2 ? 7 ? B3 ? 4 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense B1 1 2 ? anti-parallel B1 2 3 ? anti-parallel B1 3 4 ? anti-parallel B1 4 5 ? anti-parallel B1 5 6 ? anti-parallel B2 1 2 ? anti-parallel B2 2 3 ? anti-parallel B2 3 4 ? anti-parallel B2 4 5 ? anti-parallel B2 5 6 ? anti-parallel B2 6 7 ? anti-parallel B3 1 2 ? anti-parallel B3 2 3 ? anti-parallel B3 3 4 ? anti-parallel # loop_ _struct_sheet_range.sheet_id _struct_sheet_range.id _struct_sheet_range.beg_label_comp_id _struct_sheet_range.beg_label_asym_id _struct_sheet_range.beg_label_seq_id _struct_sheet_range.pdbx_beg_PDB_ins_code _struct_sheet_range.end_label_comp_id _struct_sheet_range.end_label_asym_id _struct_sheet_range.end_label_seq_id _struct_sheet_range.pdbx_end_PDB_ins_code _struct_sheet_range.beg_auth_comp_id _struct_sheet_range.beg_auth_asym_id _struct_sheet_range.beg_auth_seq_id _struct_sheet_range.end_auth_comp_id _struct_sheet_range.end_auth_asym_id _struct_sheet_range.end_auth_seq_id B1 1 VAL A 4 ? TYR A 8 ? VAL A 4 TYR A 8 B1 2 TRP A 232 ? THR A 237 ? TRP A 232 THR A 237 B1 3 SER A 71 ? PHE A 78 ? SER A 71 PHE A 78 B1 4 ALA A 172 ? ASP A 179 ? ALA A 172 ASP A 179 B1 5 LYS A 183 ? TYR A 191 ? LYS A 183 TYR A 191 B1 6 ARG A 195 ? VAL A 203 ? ARG A 195 VAL A 203 B2 1 THR A 23 ? LEU A 25 ? THR A 23 LEU A 25 B2 2 SER A 50 ? TYR A 56 ? SER A 50 TYR A 56 B2 3 ARG A 214 ? VAL A 221 ? ARG A 214 VAL A 221 B2 4 GLY A 90 ? ALA A 96 ? GLY A 90 ALA A 96 B2 5 VAL A 125 ? ASP A 131 ? VAL A 125 ASP A 131 B2 6 HIS A 145 ? ASN A 151 ? HIS A 145 ASN A 151 B2 7 ALA A 157 ? THR A 159 ? ALA A 157 THR A 159 B3 1 THR A 29 ? ILE A 31 ? THR A 29 ILE A 31 B3 2 ALA A 34 ? LEU A 37 ? ALA A 34 LEU A 37 B3 3 ASP A 224 ? ILE A 229 ? ASP A 224 ILE A 229 B3 4 LEU A 79 ? TYR A 83 ? LEU A 79 TYR A 83 # loop_ _pdbx_struct_sheet_hbond.sheet_id _pdbx_struct_sheet_hbond.range_id_1 _pdbx_struct_sheet_hbond.range_id_2 _pdbx_struct_sheet_hbond.range_1_label_atom_id _pdbx_struct_sheet_hbond.range_1_label_comp_id _pdbx_struct_sheet_hbond.range_1_label_asym_id _pdbx_struct_sheet_hbond.range_1_label_seq_id _pdbx_struct_sheet_hbond.range_1_PDB_ins_code _pdbx_struct_sheet_hbond.range_1_auth_atom_id _pdbx_struct_sheet_hbond.range_1_auth_comp_id _pdbx_struct_sheet_hbond.range_1_auth_asym_id _pdbx_struct_sheet_hbond.range_1_auth_seq_id _pdbx_struct_sheet_hbond.range_2_label_atom_id _pdbx_struct_sheet_hbond.range_2_label_comp_id _pdbx_struct_sheet_hbond.range_2_label_asym_id _pdbx_struct_sheet_hbond.range_2_label_seq_id _pdbx_struct_sheet_hbond.range_2_PDB_ins_code _pdbx_struct_sheet_hbond.range_2_auth_atom_id _pdbx_struct_sheet_hbond.range_2_auth_comp_id _pdbx_struct_sheet_hbond.range_2_auth_asym_id _pdbx_struct_sheet_hbond.range_2_auth_seq_id B1 1 2 O TYR A 8 ? O TYR A 8 N TRP A 232 ? N TRP A 232 B1 2 3 O THR A 237 ? O THR A 237 N SER A 71 ? N SER A 71 B1 3 4 O PHE A 78 ? O PHE A 78 N ALA A 172 ? N ALA A 172 B1 4 5 O ASP A 179 ? O ASP A 179 N ILE A 184 ? N ILE A 184 B1 5 6 N TYR A 191 ? N TYR A 191 O ARG A 195 ? O ARG A 195 B2 1 2 O LEU A 25 ? O LEU A 25 N GLN A 53 ? N GLN A 53 B2 2 3 N TYR A 56 ? N TYR A 56 O ILE A 215 ? O ILE A 215 B2 3 4 N ARG A 214 ? N ARG A 214 O GLY A 90 ? O GLY A 90 B2 4 5 O LEU A 95 ? O LEU A 95 N VAL A 126 ? N VAL A 126 B2 5 6 O ASP A 131 ? O ASP A 131 N HIS A 145 ? N HIS A 145 B2 6 7 O ILE A 148 ? O ILE A 148 N ALA A 157 ? N ALA A 157 B3 1 2 O ILE A 31 ? O ILE A 31 N ALA A 34 ? N ALA A 34 B3 2 3 N LEU A 37 ? N LEU A 37 O THR A 227 ? O THR A 227 B3 3 4 O TYR A 228 ? O TYR A 228 N LEU A 79 ? N LEU A 79 # loop_ _struct_site.id _struct_site.pdbx_evidence_code _struct_site.pdbx_auth_asym_id _struct_site.pdbx_auth_comp_id _struct_site.pdbx_auth_seq_id _struct_site.pdbx_auth_ins_code _struct_site.pdbx_num_residues _struct_site.details CHO Unknown ? ? ? ? 12 ? MN Unknown ? ? ? ? 6 ? CA Unknown ? ? ? ? 6 ? AC1 Software ? ? ? ? 10 'BINDING SITE FOR RESIDUE FUC A 252' AC2 Software ? ? ? ? 10 'BINDING SITE FOR RESIDUE GAL A 253' AC3 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE MAG A 255' AC4 Software ? ? ? ? 9 'BINDING SITE FOR RESIDUE FUC A 254' AC5 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE NAG A 256' AC6 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE NAG A 257' AC7 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE FUC A 262' AC8 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE MN A 250' AC9 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE CA A 251' BC1 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE SO4 A 500' # 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 CHO 12 ARG A 48 ? ARG A 48 . ? 1_555 ? 2 CHO 12 SER A 49 ? SER A 49 . ? 1_555 ? 3 CHO 12 ASP A 89 ? ASP A 89 . ? 1_555 ? 4 CHO 12 TYR A 105 ? TYR A 105 . ? 1_555 ? 5 CHO 12 GLY A 107 ? GLY A 107 . ? 1_555 ? 6 CHO 12 PHE A 108 ? PHE A 108 . ? 1_555 ? 7 CHO 12 HIS A 114 ? HIS A 114 . ? 1_555 ? 8 CHO 12 TRP A 133 ? TRP A 133 . ? 1_555 ? 9 CHO 12 ASN A 135 ? ASN A 135 . ? 1_555 ? 10 CHO 12 TRP A 138 ? TRP A 138 . ? 1_555 ? 11 CHO 12 GLY A 222 ? GLY A 222 . ? 1_555 ? 12 CHO 12 TYR A 223 ? TYR A 223 . ? 1_555 ? 13 MN 6 GLU A 129 ? GLU A 129 . ? 1_555 ? 14 MN 6 ASP A 131 ? ASP A 131 . ? 1_555 ? 15 MN 6 ASP A 140 ? ASP A 140 . ? 1_555 ? 16 MN 6 HIS A 145 ? HIS A 145 . ? 1_555 ? 17 MN 6 HOH L . ? HOH A 305 . ? 1_555 ? 18 MN 6 HOH L . ? HOH A 332 . ? 1_555 ? 19 CA 6 ASP A 131 ? ASP A 131 . ? 1_555 ? 20 CA 6 TRP A 133 ? TRP A 133 . ? 1_555 ? 21 CA 6 ASN A 135 ? ASN A 135 . ? 1_555 ? 22 CA 6 ASP A 140 ? ASP A 140 . ? 1_555 ? 23 CA 6 HOH L . ? HOH A 329 . ? 1_555 ? 24 CA 6 HOH L . ? HOH A 333 . ? 1_555 ? 25 AC1 10 PHE A 108 ? PHE A 108 . ? 1_555 ? 26 AC1 10 HIS A 114 ? HIS A 114 . ? 1_555 ? 27 AC1 10 ASN A 135 ? ASN A 135 . ? 1_555 ? 28 AC1 10 ASP A 137 ? ASP A 137 . ? 1_555 ? 29 AC1 10 TRP A 138 ? TRP A 138 . ? 1_555 ? 30 AC1 10 GAL C . ? GAL A 253 . ? 1_555 ? 31 AC1 10 MAG E . ? MAG A 255 . ? 1_555 ? 32 AC1 10 HOH L . ? HOH A 382 . ? 1_555 ? 33 AC1 10 HOH L . ? HOH A 450 . ? 1_555 ? 34 AC1 10 HOH L . ? HOH A 454 . ? 1_555 ? 35 AC2 10 ASP A 89 ? ASP A 89 . ? 1_555 ? 36 AC2 10 GLY A 107 ? GLY A 107 . ? 1_555 ? 37 AC2 10 TRP A 133 ? TRP A 133 . ? 1_555 ? 38 AC2 10 ASN A 135 ? ASN A 135 . ? 1_555 ? 39 AC2 10 GLY A 222 ? GLY A 222 . ? 1_555 ? 40 AC2 10 TYR A 223 ? TYR A 223 . ? 1_555 ? 41 AC2 10 FUC B . ? FUC A 252 . ? 1_555 ? 42 AC2 10 FUC D . ? FUC A 254 . ? 1_555 ? 43 AC2 10 MAG E . ? MAG A 255 . ? 1_555 ? 44 AC2 10 HOH L . ? HOH A 382 . ? 1_555 ? 45 AC3 6 FUC B . ? FUC A 252 . ? 1_555 ? 46 AC3 6 GAL C . ? GAL A 253 . ? 1_555 ? 47 AC3 6 FUC D . ? FUC A 254 . ? 1_555 ? 48 AC3 6 HOH L . ? HOH A 453 . ? 1_555 ? 49 AC3 6 HOH L . ? HOH A 455 . ? 1_555 ? 50 AC3 6 HOH L . ? HOH A 458 . ? 1_555 ? 51 AC4 9 ARG A 48 ? ARG A 48 . ? 1_555 ? 52 AC4 9 SER A 49 ? SER A 49 . ? 1_555 ? 53 AC4 9 TYR A 105 ? TYR A 105 . ? 1_555 ? 54 AC4 9 VAL A 221 ? VAL A 221 . ? 1_555 ? 55 AC4 9 GLY A 222 ? GLY A 222 . ? 1_555 ? 56 AC4 9 GAL C . ? GAL A 253 . ? 1_555 ? 57 AC4 9 MAG E . ? MAG A 255 . ? 1_555 ? 58 AC4 9 HOH L . ? HOH A 456 . ? 1_555 ? 59 AC4 9 HOH L . ? HOH A 457 . ? 1_555 ? 60 AC5 4 LEU A 25 ? LEU A 25 . ? 1_555 ? 61 AC5 4 SER A 101 ? SER A 101 . ? 1_555 ? 62 AC5 4 NAG G . ? NAG A 257 . ? 1_555 ? 63 AC5 4 FUC H . ? FUC A 262 . ? 1_555 ? 64 AC6 6 ASN A 18 ? ASN A 18 . ? 1_555 ? 65 AC6 6 PHE A 24 ? PHE A 24 . ? 1_555 ? 66 AC6 6 LEU A 25 ? LEU A 25 . ? 1_555 ? 67 AC6 6 NAG F . ? NAG A 256 . ? 1_555 ? 68 AC6 6 FUC H . ? FUC A 262 . ? 1_555 ? 69 AC6 6 HOH L . ? HOH A 425 . ? 1_555 ? 70 AC7 5 PHE A 24 ? PHE A 24 . ? 1_555 ? 71 AC7 5 LEU A 25 ? LEU A 25 . ? 1_555 ? 72 AC7 5 GLY A 26 ? GLY A 26 . ? 1_555 ? 73 AC7 5 NAG F . ? NAG A 256 . ? 1_555 ? 74 AC7 5 NAG G . ? NAG A 257 . ? 1_555 ? 75 AC8 6 GLU A 129 ? GLU A 129 . ? 1_555 ? 76 AC8 6 ASP A 131 ? ASP A 131 . ? 1_555 ? 77 AC8 6 ASP A 140 ? ASP A 140 . ? 1_555 ? 78 AC8 6 HIS A 145 ? HIS A 145 . ? 1_555 ? 79 AC8 6 HOH L . ? HOH A 305 . ? 1_555 ? 80 AC8 6 HOH L . ? HOH A 332 . ? 1_555 ? 81 AC9 6 ASP A 131 ? ASP A 131 . ? 1_555 ? 82 AC9 6 TRP A 133 ? TRP A 133 . ? 1_555 ? 83 AC9 6 ASN A 135 ? ASN A 135 . ? 1_555 ? 84 AC9 6 ASP A 140 ? ASP A 140 . ? 1_555 ? 85 AC9 6 HOH L . ? HOH A 329 . ? 1_555 ? 86 AC9 6 HOH L . ? HOH A 333 . ? 1_555 ? 87 BC1 5 TYR A 8 ? TYR A 8 . ? 1_555 ? 88 BC1 5 SER A 13 ? SER A 13 . ? 1_555 ? 89 BC1 5 LEU A 16 ? LEU A 16 . ? 1_555 ? 90 BC1 5 GLU A 21 ? GLU A 21 . ? 1_555 ? 91 BC1 5 ARG A 30 ? ARG A 30 . ? 1_555 ? # _database_PDB_matrix.entry_id 1LED _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 1LED _atom_sites.fract_transf_matrix[1][1] 0.012674 _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] 0.012674 _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] 0.011223 _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_sites_footnote.id _atom_sites_footnote.text 1 'RESIDUE PRO 86 IS A CIS PROLINE.' 2 'PEPTIDE BONDS ALA 88 - ASP 89 AND VAL 221 - GLY 222 ARE CIS PEPTIDE BONDS AND ARE INVOLVED IN CARBOHYDRATE BINDING SITE.' 3 'WATERS 403 AND 404 OCCUPY SPECIAL POSITIONS AND ARE SHARED BY TWO SYMMETRY RELATED MOLECULES.' # loop_ _atom_type.symbol C CA MN N O S # loop_ _atom_site.group_PDB _atom_site.id _atom_site.type_symbol _atom_site.label_atom_id _atom_site.label_alt_id _atom_site.label_comp_id _atom_site.label_asym_id _atom_site.label_entity_id _atom_site.label_seq_id _atom_site.pdbx_PDB_ins_code _atom_site.Cartn_x _atom_site.Cartn_y _atom_site.Cartn_z _atom_site.occupancy _atom_site.B_iso_or_equiv _atom_site.pdbx_formal_charge _atom_site.auth_seq_id _atom_site.auth_comp_id _atom_site.auth_asym_id _atom_site.auth_atom_id _atom_site.pdbx_PDB_model_num HETATM 1 N N . PCA A 1 1 ? 8.275 43.710 8.383 1.00 79.07 ? 1 PCA A N 1 HETATM 2 C CA . PCA A 1 1 ? 8.404 42.670 7.347 1.00 75.35 ? 1 PCA A CA 1 HETATM 3 C CB . PCA A 1 1 ? 9.637 43.068 6.569 1.00 79.17 ? 1 PCA A CB 1 HETATM 4 C CG . PCA A 1 1 ? 10.406 43.764 7.680 1.00 81.69 ? 1 PCA A CG 1 HETATM 5 C CD . PCA A 1 1 ? 9.410 44.408 8.649 1.00 83.13 ? 1 PCA A CD 1 HETATM 6 O OE . PCA A 1 1 ? 9.778 45.328 9.394 1.00 84.35 ? 1 PCA A OE 1 HETATM 7 C C . PCA A 1 1 ? 8.466 41.191 7.787 1.00 71.67 ? 1 PCA A C 1 HETATM 8 O O . PCA A 1 1 ? 8.719 40.893 8.960 1.00 72.39 ? 1 PCA A O 1 ATOM 9 N N . ASN A 1 2 ? 8.208 40.213 6.890 1.00 65.75 ? 2 ASN A N 1 ATOM 10 C CA . ASN A 1 2 ? 8.271 38.783 7.254 1.00 57.64 ? 2 ASN A CA 1 ATOM 11 C C . ASN A 1 2 ? 9.578 38.043 6.988 1.00 51.09 ? 2 ASN A C 1 ATOM 12 O O . ASN A 1 2 ? 9.780 36.896 7.361 1.00 50.51 ? 2 ASN A O 1 ATOM 13 C CB . ASN A 1 2 ? 7.181 38.005 6.547 1.00 59.37 ? 2 ASN A CB 1 ATOM 14 C CG . ASN A 1 2 ? 5.880 37.962 7.330 1.00 60.07 ? 2 ASN A CG 1 ATOM 15 O OD1 . ASN A 1 2 ? 4.840 37.632 6.791 1.00 61.39 ? 2 ASN A OD1 1 ATOM 16 N ND2 . ASN A 1 2 ? 5.763 38.272 8.605 1.00 61.52 ? 2 ASN A ND2 1 ATOM 17 N N . THR A 1 3 ? 10.501 38.695 6.316 1.00 44.01 ? 3 THR A N 1 ATOM 18 C CA . THR A 1 3 ? 11.776 38.074 5.999 1.00 38.17 ? 3 THR A CA 1 ATOM 19 C C . THR A 1 3 ? 12.952 38.775 6.679 1.00 36.64 ? 3 THR A C 1 ATOM 20 O O . THR A 1 3 ? 12.851 39.922 7.109 1.00 37.02 ? 3 THR A O 1 ATOM 21 C CB . THR A 1 3 ? 11.952 38.051 4.445 1.00 36.25 ? 3 THR A CB 1 ATOM 22 O OG1 . THR A 1 3 ? 11.862 39.377 3.948 1.00 37.04 ? 3 THR A OG1 1 ATOM 23 C CG2 . THR A 1 3 ? 10.863 37.239 3.768 1.00 34.16 ? 3 THR A CG2 1 ATOM 24 N N . VAL A 1 4 ? 14.080 38.124 6.902 1.00 34.53 ? 4 VAL A N 1 ATOM 25 C CA . VAL A 1 4 ? 15.246 38.734 7.541 1.00 33.77 ? 4 VAL A CA 1 ATOM 26 C C . VAL A 1 4 ? 16.476 38.792 6.608 1.00 34.42 ? 4 VAL A C 1 ATOM 27 O O . VAL A 1 4 ? 16.745 37.886 5.802 1.00 32.55 ? 4 VAL A O 1 ATOM 28 C CB . VAL A 1 4 ? 15.643 37.932 8.830 1.00 32.36 ? 4 VAL A CB 1 ATOM 29 C CG1 . VAL A 1 4 ? 16.799 38.615 9.539 1.00 34.40 ? 4 VAL A CG1 1 ATOM 30 C CG2 . VAL A 1 4 ? 14.501 37.871 9.813 1.00 31.59 ? 4 VAL A CG2 1 ATOM 31 N N . ASN A 1 5 ? 17.221 39.888 6.662 1.00 33.51 ? 5 ASN A N 1 ATOM 32 C CA . ASN A 1 5 ? 18.444 39.967 5.888 1.00 34.70 ? 5 ASN A CA 1 ATOM 33 C C . ASN A 1 5 ? 19.532 40.739 6.644 1.00 32.69 ? 5 ASN A C 1 ATOM 34 O O . ASN A 1 5 ? 19.440 41.961 6.760 1.00 35.56 ? 5 ASN A O 1 ATOM 35 C CB . ASN A 1 5 ? 18.261 40.654 4.515 1.00 39.14 ? 5 ASN A CB 1 ATOM 36 C CG . ASN A 1 5 ? 19.516 40.597 3.608 1.00 45.98 ? 5 ASN A CG 1 ATOM 37 O OD1 . ASN A 1 5 ? 20.544 39.942 3.852 1.00 45.83 ? 5 ASN A OD1 1 ATOM 38 N ND2 . ASN A 1 5 ? 19.549 41.243 2.450 1.00 50.96 ? 5 ASN A ND2 1 ATOM 39 N N . PHE A 1 6 ? 20.550 40.085 7.220 1.00 26.81 ? 6 PHE A N 1 ATOM 40 C CA . PHE A 1 6 ? 21.625 40.813 7.889 1.00 21.16 ? 6 PHE A CA 1 ATOM 41 C C . PHE A 1 6 ? 22.978 40.208 7.557 1.00 20.91 ? 6 PHE A C 1 ATOM 42 O O . PHE A 1 6 ? 23.166 39.031 7.193 1.00 20.92 ? 6 PHE A O 1 ATOM 43 C CB . PHE A 1 6 ? 21.491 40.851 9.453 1.00 20.45 ? 6 PHE A CB 1 ATOM 44 C CG . PHE A 1 6 ? 21.567 39.530 10.199 1.00 20.40 ? 6 PHE A CG 1 ATOM 45 C CD1 . PHE A 1 6 ? 22.788 38.977 10.522 1.00 19.51 ? 6 PHE A CD1 1 ATOM 46 C CD2 . PHE A 1 6 ? 20.395 38.893 10.584 1.00 22.51 ? 6 PHE A CD2 1 ATOM 47 C CE1 . PHE A 1 6 ? 22.822 37.798 11.232 1.00 18.47 ? 6 PHE A CE1 1 ATOM 48 C CE2 . PHE A 1 6 ? 20.430 37.712 11.297 1.00 19.57 ? 6 PHE A CE2 1 ATOM 49 C CZ . PHE A 1 6 ? 21.652 37.171 11.619 1.00 20.88 ? 6 PHE A CZ 1 ATOM 50 N N . THR A 1 7 ? 23.937 41.103 7.648 1.00 18.21 ? 7 THR A N 1 ATOM 51 C CA . THR A 1 7 ? 25.314 40.743 7.420 1.00 18.73 ? 7 THR A CA 1 ATOM 52 C C . THR A 1 7 ? 26.270 41.424 8.377 1.00 18.61 ? 7 THR A C 1 ATOM 53 O O . THR A 1 7 ? 26.321 42.642 8.460 1.00 20.76 ? 7 THR A O 1 ATOM 54 C CB . THR A 1 7 ? 25.842 41.108 5.993 1.00 17.93 ? 7 THR A CB 1 ATOM 55 O OG1 . THR A 1 7 ? 25.035 40.440 5.052 1.00 21.28 ? 7 THR A OG1 1 ATOM 56 C CG2 . THR A 1 7 ? 27.230 40.621 5.702 1.00 17.14 ? 7 THR A CG2 1 ATOM 57 N N . TYR A 1 8 ? 27.049 40.616 9.077 1.00 18.61 ? 8 TYR A N 1 ATOM 58 C CA . TYR A 1 8 ? 28.093 41.085 9.963 1.00 18.73 ? 8 TYR A CA 1 ATOM 59 C C . TYR A 1 8 ? 29.388 40.522 9.369 1.00 18.40 ? 8 TYR A C 1 ATOM 60 O O . TYR A 1 8 ? 29.648 39.317 9.450 1.00 17.82 ? 8 TYR A O 1 ATOM 61 C CB . TYR A 1 8 ? 27.966 40.567 11.388 1.00 19.42 ? 8 TYR A CB 1 ATOM 62 C CG . TYR A 1 8 ? 26.712 41.078 12.062 1.00 22.09 ? 8 TYR A CG 1 ATOM 63 C CD1 . TYR A 1 8 ? 26.642 42.375 12.517 1.00 22.67 ? 8 TYR A CD1 1 ATOM 64 C CD2 . TYR A 1 8 ? 25.642 40.222 12.214 1.00 23.90 ? 8 TYR A CD2 1 ATOM 65 C CE1 . TYR A 1 8 ? 25.481 42.811 13.129 1.00 27.02 ? 8 TYR A CE1 1 ATOM 66 C CE2 . TYR A 1 8 ? 24.488 40.638 12.822 1.00 26.99 ? 8 TYR A CE2 1 ATOM 67 C CZ . TYR A 1 8 ? 24.417 41.936 13.276 1.00 30.38 ? 8 TYR A CZ 1 ATOM 68 O OH . TYR A 1 8 ? 23.252 42.340 13.900 1.00 33.60 ? 8 TYR A OH 1 ATOM 69 N N . PRO A 1 9 ? 30.208 41.335 8.671 1.00 18.64 ? 9 PRO A N 1 ATOM 70 C CA . PRO A 1 9 ? 31.432 40.889 7.986 1.00 20.16 ? 9 PRO A CA 1 ATOM 71 C C . PRO A 1 9 ? 32.541 40.454 8.936 1.00 18.24 ? 9 PRO A C 1 ATOM 72 O O . PRO A 1 9 ? 33.439 39.667 8.676 1.00 20.15 ? 9 PRO A O 1 ATOM 73 C CB . PRO A 1 9 ? 31.815 42.076 7.112 1.00 18.52 ? 9 PRO A CB 1 ATOM 74 C CG . PRO A 1 9 ? 30.549 42.876 7.026 1.00 20.76 ? 9 PRO A CG 1 ATOM 75 C CD . PRO A 1 9 ? 29.966 42.754 8.405 1.00 17.25 ? 9 PRO A CD 1 ATOM 76 N N . ASP A 1 10 ? 32.463 41.018 10.118 1.00 20.61 ? 10 ASP A N 1 ATOM 77 C CA . ASP A 1 10 ? 33.378 40.750 11.215 1.00 22.05 ? 10 ASP A CA 1 ATOM 78 C C . ASP A 1 10 ? 32.673 41.260 12.473 1.00 23.81 ? 10 ASP A C 1 ATOM 79 O O . ASP A 1 10 ? 31.603 41.881 12.351 1.00 22.27 ? 10 ASP A O 1 ATOM 80 C CB . ASP A 1 10 ? 34.702 41.523 11.006 1.00 26.25 ? 10 ASP A CB 1 ATOM 81 C CG . ASP A 1 10 ? 34.604 43.070 10.859 1.00 30.36 ? 10 ASP A CG 1 ATOM 82 O OD1 . ASP A 1 10 ? 34.078 43.767 11.745 1.00 26.18 ? 10 ASP A OD1 1 ATOM 83 O OD2 . ASP A 1 10 ? 35.075 43.576 9.834 1.00 35.25 ? 10 ASP A OD2 1 ATOM 84 N N . PHE A 1 11 ? 33.200 41.068 13.682 1.00 23.01 ? 11 PHE A N 1 ATOM 85 C CA . PHE A 1 11 ? 32.574 41.649 14.875 1.00 23.89 ? 11 PHE A CA 1 ATOM 86 C C . PHE A 1 11 ? 33.543 42.622 15.619 1.00 25.61 ? 11 PHE A C 1 ATOM 87 O O . PHE A 1 11 ? 33.671 42.693 16.850 1.00 25.55 ? 11 PHE A O 1 ATOM 88 C CB . PHE A 1 11 ? 32.110 40.545 15.810 1.00 19.50 ? 11 PHE A CB 1 ATOM 89 C CG . PHE A 1 11 ? 30.938 39.754 15.265 1.00 17.58 ? 11 PHE A CG 1 ATOM 90 C CD1 . PHE A 1 11 ? 29.690 40.346 15.211 1.00 17.52 ? 11 PHE A CD1 1 ATOM 91 C CD2 . PHE A 1 11 ? 31.124 38.447 14.848 1.00 17.47 ? 11 PHE A CD2 1 ATOM 92 C CE1 . PHE A 1 11 ? 28.629 39.606 14.735 1.00 17.43 ? 11 PHE A CE1 1 ATOM 93 C CE2 . PHE A 1 11 ? 30.062 37.722 14.376 1.00 10.20 ? 11 PHE A CE2 1 ATOM 94 C CZ . PHE A 1 11 ? 28.820 38.306 14.324 1.00 15.05 ? 11 PHE A CZ 1 ATOM 95 N N . TRP A 1 12 ? 34.336 43.411 14.865 1.00 26.75 ? 12 TRP A N 1 ATOM 96 C CA . TRP A 1 12 ? 35.246 44.383 15.496 1.00 31.80 ? 12 TRP A CA 1 ATOM 97 C C . TRP A 1 12 ? 34.502 45.544 16.155 1.00 34.79 ? 12 TRP A C 1 ATOM 98 O O . TRP A 1 12 ? 35.042 46.273 16.967 1.00 37.65 ? 12 TRP A O 1 ATOM 99 C CB . TRP A 1 12 ? 36.287 44.878 14.471 1.00 27.82 ? 12 TRP A CB 1 ATOM 100 C CG . TRP A 1 12 ? 37.366 43.803 14.344 1.00 25.57 ? 12 TRP A CG 1 ATOM 101 C CD1 . TRP A 1 12 ? 37.440 43.071 13.194 1.00 26.07 ? 12 TRP A CD1 1 ATOM 102 C CD2 . TRP A 1 12 ? 38.239 43.324 15.327 1.00 26.11 ? 12 TRP A CD2 1 ATOM 103 N NE1 . TRP A 1 12 ? 38.312 42.121 13.440 1.00 23.08 ? 12 TRP A NE1 1 ATOM 104 C CE2 . TRP A 1 12 ? 38.808 42.229 14.685 1.00 24.32 ? 12 TRP A CE2 1 ATOM 105 C CE3 . TRP A 1 12 ? 38.628 43.615 16.626 1.00 23.45 ? 12 TRP A CE3 1 ATOM 106 C CZ2 . TRP A 1 12 ? 39.739 41.407 15.311 1.00 26.03 ? 12 TRP A CZ2 1 ATOM 107 C CZ3 . TRP A 1 12 ? 39.552 42.801 17.245 1.00 21.54 ? 12 TRP A CZ3 1 ATOM 108 C CH2 . TRP A 1 12 ? 40.102 41.711 16.603 1.00 22.00 ? 12 TRP A CH2 1 ATOM 109 N N . SER A 1 13 ? 33.169 45.597 15.947 1.00 40.87 ? 13 SER A N 1 ATOM 110 C CA . SER A 1 13 ? 32.276 46.586 16.569 1.00 41.07 ? 13 SER A CA 1 ATOM 111 C C . SER A 1 13 ? 31.573 45.952 17.782 1.00 40.90 ? 13 SER A C 1 ATOM 112 O O . SER A 1 13 ? 30.380 45.740 17.964 1.00 42.06 ? 13 SER A O 1 ATOM 113 C CB . SER A 1 13 ? 31.198 47.082 15.611 1.00 41.92 ? 13 SER A CB 1 ATOM 114 O OG . SER A 1 13 ? 30.455 48.100 16.284 1.00 44.82 ? 13 SER A OG 1 ATOM 115 N N . TYR A 1 14 ? 32.440 45.655 18.724 1.00 43.95 ? 14 TYR A N 1 ATOM 116 C CA . TYR A 1 14 ? 32.059 45.017 19.959 1.00 44.67 ? 14 TYR A CA 1 ATOM 117 C C . TYR A 1 14 ? 31.327 45.844 21.013 1.00 46.12 ? 14 TYR A C 1 ATOM 118 O O . TYR A 1 14 ? 31.009 45.366 22.107 1.00 45.19 ? 14 TYR A O 1 ATOM 119 C CB . TYR A 1 14 ? 33.323 44.446 20.612 1.00 44.08 ? 14 TYR A CB 1 ATOM 120 C CG . TYR A 1 14 ? 34.299 45.513 21.159 1.00 41.84 ? 14 TYR A CG 1 ATOM 121 C CD1 . TYR A 1 14 ? 34.186 45.940 22.479 1.00 40.94 ? 14 TYR A CD1 1 ATOM 122 C CD2 . TYR A 1 14 ? 35.364 45.947 20.387 1.00 38.46 ? 14 TYR A CD2 1 ATOM 123 C CE1 . TYR A 1 14 ? 35.119 46.783 23.021 1.00 39.59 ? 14 TYR A CE1 1 ATOM 124 C CE2 . TYR A 1 14 ? 36.309 46.793 20.929 1.00 38.48 ? 14 TYR A CE2 1 ATOM 125 C CZ . TYR A 1 14 ? 36.192 47.195 22.251 1.00 39.21 ? 14 TYR A CZ 1 ATOM 126 O OH . TYR A 1 14 ? 37.176 47.984 22.847 1.00 36.48 ? 14 TYR A OH 1 ATOM 127 N N . SER A 1 15 ? 31.088 47.105 20.733 1.00 47.16 ? 15 SER A N 1 ATOM 128 C CA . SER A 1 15 ? 30.446 47.875 21.757 1.00 47.92 ? 15 SER A CA 1 ATOM 129 C C . SER A 1 15 ? 28.920 47.834 21.818 1.00 46.94 ? 15 SER A C 1 ATOM 130 O O . SER A 1 15 ? 28.370 48.503 22.696 1.00 48.16 ? 15 SER A O 1 ATOM 131 C CB . SER A 1 15 ? 30.972 49.309 21.620 1.00 50.47 ? 15 SER A CB 1 ATOM 132 O OG . SER A 1 15 ? 31.215 49.956 22.874 1.00 51.92 ? 15 SER A OG 1 ATOM 133 N N . LEU A 1 16 ? 28.163 47.152 20.931 1.00 43.97 ? 16 LEU A N 1 ATOM 134 C CA . LEU A 1 16 ? 26.712 47.112 21.071 1.00 40.79 ? 16 LEU A CA 1 ATOM 135 C C . LEU A 1 16 ? 26.166 46.458 22.342 1.00 38.85 ? 16 LEU A C 1 ATOM 136 O O . LEU A 1 16 ? 26.678 45.419 22.798 1.00 39.49 ? 16 LEU A O 1 ATOM 137 C CB . LEU A 1 16 ? 26.051 46.413 19.930 1.00 39.06 ? 16 LEU A CB 1 ATOM 138 C CG . LEU A 1 16 ? 25.300 47.401 19.061 1.00 42.46 ? 16 LEU A CG 1 ATOM 139 C CD1 . LEU A 1 16 ? 26.213 47.769 17.913 1.00 42.90 ? 16 LEU A CD1 1 ATOM 140 C CD2 . LEU A 1 16 ? 24.024 46.807 18.517 1.00 43.60 ? 16 LEU A CD2 1 ATOM 141 N N . LYS A 1 17 ? 25.129 47.058 22.904 1.00 36.65 ? 17 LYS A N 1 ATOM 142 C CA . LYS A 1 17 ? 24.517 46.490 24.108 1.00 36.21 ? 17 LYS A CA 1 ATOM 143 C C . LYS A 1 17 ? 23.834 45.099 23.968 1.00 33.04 ? 17 LYS A C 1 ATOM 144 O O . LYS A 1 17 ? 23.198 44.758 22.960 1.00 31.20 ? 17 LYS A O 1 ATOM 145 C CB . LYS A 1 17 ? 23.482 47.509 24.663 1.00 38.71 ? 17 LYS A CB 1 ATOM 146 C CG . LYS A 1 17 ? 24.139 48.731 25.348 1.00 43.22 ? 17 LYS A CG 1 ATOM 147 C CD . LYS A 1 17 ? 23.140 49.550 26.167 1.00 44.21 ? 17 LYS A CD 1 ATOM 148 C CE . LYS A 1 17 ? 23.518 49.668 27.650 1.00 44.85 ? 17 LYS A CE 1 ATOM 149 N NZ . LYS A 1 17 ? 22.330 49.742 28.503 1.00 46.05 ? 17 LYS A NZ 1 ATOM 150 N N . ASN A 1 18 ? 24.048 44.228 24.943 1.00 30.61 ? 18 ASN A N 1 ATOM 151 C CA . ASN A 1 18 ? 23.440 42.902 24.955 1.00 31.78 ? 18 ASN A CA 1 ATOM 152 C C . ASN A 1 18 ? 21.913 42.995 24.722 1.00 33.36 ? 18 ASN A C 1 ATOM 153 O O . ASN A 1 18 ? 21.210 43.888 25.222 1.00 35.51 ? 18 ASN A O 1 ATOM 154 C CB . ASN A 1 18 ? 23.730 42.240 26.299 1.00 27.83 ? 18 ASN A CB 1 ATOM 155 C CG . ASN A 1 18 ? 23.024 40.916 26.472 1.00 30.38 ? 18 ASN A CG 1 ATOM 156 O OD1 . ASN A 1 18 ? 22.956 40.158 25.495 1.00 31.52 ? 18 ASN A OD1 1 ATOM 157 N ND2 . ASN A 1 18 ? 22.456 40.621 27.639 1.00 30.09 ? 18 ASN A ND2 1 ATOM 158 N N . GLY A 1 19 ? 21.434 42.143 23.819 1.00 31.93 ? 19 GLY A N 1 ATOM 159 C CA . GLY A 1 19 ? 20.017 42.105 23.507 1.00 29.06 ? 19 GLY A CA 1 ATOM 160 C C . GLY A 1 19 ? 19.565 43.091 22.465 1.00 27.50 ? 19 GLY A C 1 ATOM 161 O O . GLY A 1 19 ? 18.397 43.119 22.126 1.00 24.37 ? 19 GLY A O 1 ATOM 162 N N . THR A 1 20 ? 20.378 43.994 21.952 1.00 31.16 ? 20 THR A N 1 ATOM 163 C CA . THR A 1 20 ? 19.824 44.869 20.925 1.00 36.02 ? 20 THR A CA 1 ATOM 164 C C . THR A 1 20 ? 19.959 44.179 19.556 1.00 38.09 ? 20 THR A C 1 ATOM 165 O O . THR A 1 20 ? 18.959 44.087 18.817 1.00 42.66 ? 20 THR A O 1 ATOM 166 C CB . THR A 1 20 ? 20.549 46.232 20.971 1.00 37.79 ? 20 THR A CB 1 ATOM 167 O OG1 . THR A 1 20 ? 21.946 46.050 20.719 1.00 39.38 ? 20 THR A OG1 1 ATOM 168 C CG2 . THR A 1 20 ? 20.326 46.868 22.344 1.00 36.94 ? 20 THR A CG2 1 ATOM 169 N N . GLU A 1 21 ? 21.136 43.674 19.144 1.00 33.95 ? 21 GLU A N 1 ATOM 170 C CA . GLU A 1 21 ? 21.220 42.976 17.841 1.00 33.35 ? 21 GLU A CA 1 ATOM 171 C C . GLU A 1 21 ? 21.373 41.469 18.021 1.00 29.43 ? 21 GLU A C 1 ATOM 172 O O . GLU A 1 21 ? 20.744 40.646 17.359 1.00 27.32 ? 21 GLU A O 1 ATOM 173 C CB . GLU A 1 21 ? 22.386 43.453 17.039 1.00 33.58 ? 21 GLU A CB 1 ATOM 174 C CG . GLU A 1 21 ? 21.937 44.652 16.278 1.00 39.40 ? 21 GLU A CG 1 ATOM 175 C CD . GLU A 1 21 ? 22.963 45.206 15.318 1.00 45.25 ? 21 GLU A CD 1 ATOM 176 O OE1 . GLU A 1 21 ? 24.174 45.017 15.486 1.00 47.27 ? 21 GLU A OE1 1 ATOM 177 O OE2 . GLU A 1 21 ? 22.519 45.830 14.361 1.00 52.12 ? 21 GLU A OE2 1 ATOM 178 N N . ILE A 1 22 ? 22.277 41.162 18.946 1.00 25.05 ? 22 ILE A N 1 ATOM 179 C CA . ILE A 1 22 ? 22.611 39.822 19.370 1.00 23.42 ? 22 ILE A CA 1 ATOM 180 C C . ILE A 1 22 ? 22.440 39.736 20.904 1.00 23.97 ? 22 ILE A C 1 ATOM 181 O O . ILE A 1 22 ? 22.810 40.606 21.712 1.00 23.69 ? 22 ILE A O 1 ATOM 182 C CB . ILE A 1 22 ? 24.084 39.497 18.935 1.00 22.70 ? 22 ILE A CB 1 ATOM 183 C CG1 . ILE A 1 22 ? 24.193 39.598 17.416 1.00 23.32 ? 22 ILE A CG1 1 ATOM 184 C CG2 . ILE A 1 22 ? 24.486 38.094 19.449 1.00 22.35 ? 22 ILE A CG2 1 ATOM 185 C CD1 . ILE A 1 22 ? 25.498 39.123 16.789 1.00 27.26 ? 22 ILE A CD1 1 ATOM 186 N N . THR A 1 23 ? 21.868 38.632 21.334 1.00 23.61 ? 23 THR A N 1 ATOM 187 C CA . THR A 1 23 ? 21.635 38.360 22.737 1.00 22.45 ? 23 THR A CA 1 ATOM 188 C C . THR A 1 23 ? 22.584 37.303 23.191 1.00 22.16 ? 23 THR A C 1 ATOM 189 O O . THR A 1 23 ? 22.677 36.257 22.570 1.00 22.64 ? 23 THR A O 1 ATOM 190 C CB . THR A 1 23 ? 20.240 37.812 23.017 1.00 24.37 ? 23 THR A CB 1 ATOM 191 O OG1 . THR A 1 23 ? 19.352 38.831 22.569 1.00 25.57 ? 23 THR A OG1 1 ATOM 192 C CG2 . THR A 1 23 ? 19.991 37.449 24.489 1.00 22.16 ? 23 THR A CG2 1 ATOM 193 N N . PHE A 1 24 ? 23.272 37.524 24.292 1.00 22.14 ? 24 PHE A N 1 ATOM 194 C CA . PHE A 1 24 ? 24.197 36.538 24.805 1.00 22.32 ? 24 PHE A CA 1 ATOM 195 C C . PHE A 1 24 ? 23.592 35.875 26.034 1.00 24.42 ? 24 PHE A C 1 ATOM 196 O O . PHE A 1 24 ? 23.095 36.585 26.900 1.00 24.56 ? 24 PHE A O 1 ATOM 197 C CB . PHE A 1 24 ? 25.535 37.204 25.177 1.00 23.31 ? 24 PHE A CB 1 ATOM 198 C CG . PHE A 1 24 ? 26.205 37.868 23.979 1.00 22.99 ? 24 PHE A CG 1 ATOM 199 C CD1 . PHE A 1 24 ? 25.840 39.155 23.630 1.00 25.47 ? 24 PHE A CD1 1 ATOM 200 C CD2 . PHE A 1 24 ? 27.148 37.181 23.252 1.00 24.26 ? 24 PHE A CD2 1 ATOM 201 C CE1 . PHE A 1 24 ? 26.412 39.774 22.551 1.00 25.44 ? 24 PHE A CE1 1 ATOM 202 C CE2 . PHE A 1 24 ? 27.728 37.799 22.168 1.00 24.61 ? 24 PHE A CE2 1 ATOM 203 C CZ . PHE A 1 24 ? 27.358 39.086 21.826 1.00 26.74 ? 24 PHE A CZ 1 ATOM 204 N N . LEU A 1 25 ? 23.574 34.547 26.111 1.00 23.61 ? 25 LEU A N 1 ATOM 205 C CA . LEU A 1 25 ? 23.048 33.773 27.213 1.00 21.00 ? 25 LEU A CA 1 ATOM 206 C C . LEU A 1 25 ? 24.099 32.858 27.842 1.00 22.85 ? 25 LEU A C 1 ATOM 207 O O . LEU A 1 25 ? 25.005 32.317 27.174 1.00 23.98 ? 25 LEU A O 1 ATOM 208 C CB . LEU A 1 25 ? 21.883 32.910 26.727 1.00 19.16 ? 25 LEU A CB 1 ATOM 209 C CG . LEU A 1 25 ? 20.692 33.563 26.048 1.00 20.50 ? 25 LEU A CG 1 ATOM 210 C CD1 . LEU A 1 25 ? 19.677 32.461 25.714 1.00 17.55 ? 25 LEU A CD1 1 ATOM 211 C CD2 . LEU A 1 25 ? 20.065 34.618 26.959 1.00 19.39 ? 25 LEU A CD2 1 ATOM 212 N N . GLY A 1 26 ? 23.984 32.562 29.129 1.00 22.18 ? 26 GLY A N 1 ATOM 213 C CA . GLY A 1 26 ? 24.937 31.693 29.797 1.00 21.67 ? 26 GLY A CA 1 ATOM 214 C C . GLY A 1 26 ? 26.339 32.281 29.844 1.00 23.44 ? 26 GLY A C 1 ATOM 215 O O . GLY A 1 26 ? 26.525 33.444 30.203 1.00 25.22 ? 26 GLY A O 1 ATOM 216 N N . ASP A 1 27 ? 27.338 31.500 29.434 1.00 24.25 ? 27 ASP A N 1 ATOM 217 C CA . ASP A 1 27 ? 28.727 31.953 29.405 1.00 24.57 ? 27 ASP A CA 1 ATOM 218 C C . ASP A 1 27 ? 29.219 32.597 28.104 1.00 25.28 ? 27 ASP A C 1 ATOM 219 O O . ASP A 1 27 ? 30.410 32.858 27.937 1.00 26.37 ? 27 ASP A O 1 ATOM 220 C CB . ASP A 1 27 ? 29.606 30.771 29.725 1.00 25.21 ? 27 ASP A CB 1 ATOM 221 C CG . ASP A 1 27 ? 29.462 30.318 31.167 1.00 28.00 ? 27 ASP A CG 1 ATOM 222 O OD1 . ASP A 1 27 ? 29.164 31.155 32.021 1.00 29.82 ? 27 ASP A OD1 1 ATOM 223 O OD2 . ASP A 1 27 ? 29.657 29.131 31.424 1.00 30.77 ? 27 ASP A OD2 1 ATOM 224 N N . ALA A 1 28 ? 28.321 32.813 27.136 1.00 25.07 ? 28 ALA A N 1 ATOM 225 C CA . ALA A 1 28 ? 28.691 33.416 25.876 1.00 24.75 ? 28 ALA A CA 1 ATOM 226 C C . ALA A 1 28 ? 28.866 34.890 26.116 1.00 26.64 ? 28 ALA A C 1 ATOM 227 O O . ALA A 1 28 ? 28.060 35.557 26.778 1.00 27.96 ? 28 ALA A O 1 ATOM 228 C CB . ALA A 1 28 ? 27.625 33.304 24.829 1.00 20.00 ? 28 ALA A CB 1 ATOM 229 N N . THR A 1 29 ? 29.923 35.393 25.521 1.00 26.14 ? 29 THR A N 1 ATOM 230 C CA . THR A 1 29 ? 30.227 36.797 25.654 1.00 25.55 ? 29 THR A CA 1 ATOM 231 C C . THR A 1 29 ? 30.700 37.484 24.394 1.00 24.56 ? 29 THR A C 1 ATOM 232 O O . THR A 1 29 ? 31.228 36.856 23.470 1.00 25.36 ? 29 THR A O 1 ATOM 233 C CB . THR A 1 29 ? 31.275 36.918 26.765 1.00 26.66 ? 29 THR A CB 1 ATOM 234 O OG1 . THR A 1 29 ? 31.478 38.294 26.853 1.00 34.22 ? 29 THR A OG1 1 ATOM 235 C CG2 . THR A 1 29 ? 32.609 36.206 26.541 1.00 26.68 ? 29 THR A CG2 1 ATOM 236 N N . ARG A 1 30 ? 30.507 38.792 24.310 1.00 26.33 ? 30 ARG A N 1 ATOM 237 C CA . ARG A 1 30 ? 30.992 39.544 23.152 1.00 27.81 ? 30 ARG A CA 1 ATOM 238 C C . ARG A 1 30 ? 32.444 39.969 23.431 1.00 27.96 ? 30 ARG A C 1 ATOM 239 O O . ARG A 1 30 ? 32.800 40.398 24.526 1.00 31.06 ? 30 ARG A O 1 ATOM 240 C CB . ARG A 1 30 ? 30.113 40.783 22.922 1.00 28.73 ? 30 ARG A CB 1 ATOM 241 C CG . ARG A 1 30 ? 30.426 41.551 21.667 1.00 30.37 ? 30 ARG A CG 1 ATOM 242 C CD . ARG A 1 30 ? 29.464 42.721 21.407 1.00 38.51 ? 30 ARG A CD 1 ATOM 243 N NE . ARG A 1 30 ? 28.140 42.513 20.774 1.00 42.23 ? 30 ARG A NE 1 ATOM 244 C CZ . ARG A 1 30 ? 27.897 42.555 19.438 1.00 39.44 ? 30 ARG A CZ 1 ATOM 245 N NH1 . ARG A 1 30 ? 28.871 42.765 18.551 1.00 40.77 ? 30 ARG A NH1 1 ATOM 246 N NH2 . ARG A 1 30 ? 26.632 42.544 18.986 1.00 36.98 ? 30 ARG A NH2 1 ATOM 247 N N . ILE A 1 31 ? 33.392 39.717 22.568 1.00 26.08 ? 31 ILE A N 1 ATOM 248 C CA . ILE A 1 31 ? 34.763 40.161 22.789 1.00 22.73 ? 31 ILE A CA 1 ATOM 249 C C . ILE A 1 31 ? 35.154 41.000 21.552 1.00 24.06 ? 31 ILE A C 1 ATOM 250 O O . ILE A 1 31 ? 34.410 40.936 20.547 1.00 22.04 ? 31 ILE A O 1 ATOM 251 C CB . ILE A 1 31 ? 35.761 38.970 22.967 1.00 22.31 ? 31 ILE A CB 1 ATOM 252 C CG1 . ILE A 1 31 ? 35.868 38.021 21.751 1.00 21.89 ? 31 ILE A CG1 1 ATOM 253 C CG2 . ILE A 1 31 ? 35.304 38.249 24.230 1.00 25.41 ? 31 ILE A CG2 1 ATOM 254 C CD1 . ILE A 1 31 ? 36.993 36.968 21.886 1.00 20.13 ? 31 ILE A CD1 1 ATOM 255 N N . PRO A 1 32 ? 36.230 41.837 21.501 1.00 23.95 ? 32 PRO A N 1 ATOM 256 C CA . PRO A 1 32 ? 36.629 42.531 20.279 1.00 22.37 ? 32 PRO A CA 1 ATOM 257 C C . PRO A 1 32 ? 36.823 41.559 19.105 1.00 20.05 ? 32 PRO A C 1 ATOM 258 O O . PRO A 1 32 ? 37.614 40.617 19.204 1.00 19.96 ? 32 PRO A O 1 ATOM 259 C CB . PRO A 1 32 ? 37.914 43.278 20.682 1.00 22.85 ? 32 PRO A CB 1 ATOM 260 C CG . PRO A 1 32 ? 37.845 43.387 22.174 1.00 22.28 ? 32 PRO A CG 1 ATOM 261 C CD . PRO A 1 32 ? 37.243 42.052 22.548 1.00 21.33 ? 32 PRO A CD 1 ATOM 262 N N . GLY A 1 33 ? 36.005 41.672 18.071 1.00 19.38 ? 33 GLY A N 1 ATOM 263 C CA . GLY A 1 33 ? 36.161 40.806 16.907 1.00 19.97 ? 33 GLY A CA 1 ATOM 264 C C . GLY A 1 33 ? 35.432 39.474 16.879 1.00 21.36 ? 33 GLY A C 1 ATOM 265 O O . GLY A 1 33 ? 35.403 38.804 15.839 1.00 21.23 ? 33 GLY A O 1 ATOM 266 N N . ALA A 1 34 ? 34.778 39.091 17.965 1.00 18.57 ? 34 ALA A N 1 ATOM 267 C CA . ALA A 1 34 ? 34.101 37.805 18.012 1.00 19.35 ? 34 ALA A CA 1 ATOM 268 C C . ALA A 1 34 ? 32.990 37.611 19.040 1.00 18.15 ? 34 ALA A C 1 ATOM 269 O O . ALA A 1 34 ? 32.837 38.350 20.016 1.00 18.26 ? 34 ALA A O 1 ATOM 270 C CB . ALA A 1 34 ? 35.133 36.645 18.268 1.00 14.29 ? 34 ALA A CB 1 ATOM 271 N N . LEU A 1 35 ? 32.137 36.638 18.740 1.00 18.96 ? 35 LEU A N 1 ATOM 272 C CA . LEU A 1 35 ? 31.108 36.237 19.674 1.00 17.81 ? 35 LEU A CA 1 ATOM 273 C C . LEU A 1 35 ? 31.824 35.031 20.307 1.00 19.58 ? 35 LEU A C 1 ATOM 274 O O . LEU A 1 35 ? 32.250 34.108 19.591 1.00 20.43 ? 35 LEU A O 1 ATOM 275 C CB . LEU A 1 35 ? 29.842 35.778 18.981 1.00 15.42 ? 35 LEU A CB 1 ATOM 276 C CG . LEU A 1 35 ? 29.226 36.698 17.929 1.00 17.25 ? 35 LEU A CG 1 ATOM 277 C CD1 . LEU A 1 35 ? 27.867 36.106 17.496 1.00 18.62 ? 35 LEU A CD1 1 ATOM 278 C CD2 . LEU A 1 35 ? 29.028 38.108 18.469 1.00 17.24 ? 35 LEU A CD2 1 ATOM 279 N N . GLN A 1 36 ? 32.154 35.026 21.616 1.00 19.58 ? 36 GLN A N 1 ATOM 280 C CA . GLN A 1 36 ? 32.830 33.902 22.273 1.00 19.81 ? 36 GLN A CA 1 ATOM 281 C C . GLN A 1 36 ? 31.750 33.005 22.907 1.00 21.30 ? 36 GLN A C 1 ATOM 282 O O . GLN A 1 36 ? 30.965 33.494 23.733 1.00 22.96 ? 36 GLN A O 1 ATOM 283 C CB . GLN A 1 36 ? 33.764 34.458 23.321 1.00 19.68 ? 36 GLN A CB 1 ATOM 284 C CG . GLN A 1 36 ? 34.534 33.322 23.963 1.00 18.11 ? 36 GLN A CG 1 ATOM 285 C CD . GLN A 1 36 ? 35.551 33.839 24.961 1.00 22.05 ? 36 GLN A CD 1 ATOM 286 O OE1 . GLN A 1 36 ? 36.226 34.845 24.759 1.00 22.16 ? 36 GLN A OE1 1 ATOM 287 N NE2 . GLN A 1 36 ? 35.709 33.207 26.093 1.00 20.94 ? 36 GLN A NE2 1 ATOM 288 N N . LEU A 1 37 ? 31.678 31.703 22.631 1.00 19.68 ? 37 LEU A N 1 ATOM 289 C CA . LEU A 1 37 ? 30.548 30.947 23.190 1.00 22.24 ? 37 LEU A CA 1 ATOM 290 C C . LEU A 1 37 ? 30.550 30.326 24.597 1.00 21.28 ? 37 LEU A C 1 ATOM 291 O O . LEU A 1 37 ? 29.512 30.175 25.237 1.00 22.87 ? 37 LEU A O 1 ATOM 292 C CB . LEU A 1 37 ? 30.191 29.912 22.106 1.00 20.53 ? 37 LEU A CB 1 ATOM 293 C CG . LEU A 1 37 ? 29.859 30.458 20.689 1.00 19.88 ? 37 LEU A CG 1 ATOM 294 C CD1 . LEU A 1 37 ? 29.504 29.290 19.789 1.00 19.37 ? 37 LEU A CD1 1 ATOM 295 C CD2 . LEU A 1 37 ? 28.730 31.450 20.735 1.00 18.61 ? 37 LEU A CD2 1 ATOM 296 N N . THR A 1 38 ? 31.722 29.963 25.087 1.00 23.65 ? 38 THR A N 1 ATOM 297 C CA . THR A 1 38 ? 31.911 29.403 26.407 1.00 24.14 ? 38 THR A CA 1 ATOM 298 C C . THR A 1 38 ? 33.010 30.169 27.126 1.00 27.98 ? 38 THR A C 1 ATOM 299 O O . THR A 1 38 ? 33.737 30.991 26.546 1.00 27.40 ? 38 THR A O 1 ATOM 300 C CB . THR A 1 38 ? 32.304 27.938 26.403 1.00 21.61 ? 38 THR A CB 1 ATOM 301 O OG1 . THR A 1 38 ? 33.451 27.761 25.619 1.00 21.28 ? 38 THR A OG1 1 ATOM 302 C CG2 . THR A 1 38 ? 31.110 27.100 25.941 1.00 25.63 ? 38 THR A CG2 1 ATOM 303 N N . LYS A 1 39 ? 33.163 29.897 28.418 1.00 29.14 ? 39 LYS A N 1 ATOM 304 C CA . LYS A 1 39 ? 34.111 30.623 29.233 1.00 30.15 ? 39 LYS A CA 1 ATOM 305 C C . LYS A 1 39 ? 35.594 30.366 29.163 1.00 29.26 ? 39 LYS A C 1 ATOM 306 O O . LYS A 1 39 ? 36.058 29.251 28.981 1.00 26.60 ? 39 LYS A O 1 ATOM 307 C CB . LYS A 1 39 ? 33.651 30.470 30.687 1.00 34.51 ? 39 LYS A CB 1 ATOM 308 C CG . LYS A 1 39 ? 34.203 31.509 31.645 1.00 39.76 ? 39 LYS A CG 1 ATOM 309 C CD . LYS A 1 39 ? 33.616 31.206 33.004 1.00 46.93 ? 39 LYS A CD 1 ATOM 310 C CE . LYS A 1 39 ? 34.136 32.217 34.020 1.00 51.51 ? 39 LYS A CE 1 ATOM 311 N NZ . LYS A 1 39 ? 33.385 32.143 35.266 1.00 55.72 ? 39 LYS A NZ 1 ATOM 312 N N . THR A 1 40 ? 36.366 31.423 29.243 1.00 30.36 ? 40 THR A N 1 ATOM 313 C CA . THR A 1 40 ? 37.818 31.298 29.279 1.00 33.95 ? 40 THR A CA 1 ATOM 314 C C . THR A 1 40 ? 38.355 32.046 30.497 1.00 37.65 ? 40 THR A C 1 ATOM 315 O O . THR A 1 40 ? 37.686 32.889 31.110 1.00 36.12 ? 40 THR A O 1 ATOM 316 C CB . THR A 1 40 ? 38.554 31.889 28.037 1.00 33.21 ? 40 THR A CB 1 ATOM 317 O OG1 . THR A 1 40 ? 38.187 33.268 27.897 1.00 33.00 ? 40 THR A OG1 1 ATOM 318 C CG2 . THR A 1 40 ? 38.278 31.029 26.795 1.00 31.53 ? 40 THR A CG2 1 ATOM 319 N N . ASP A 1 41 ? 39.528 31.648 30.987 1.00 43.88 ? 41 ASP A N 1 ATOM 320 C CA . ASP A 1 41 ? 40.154 32.349 32.108 1.00 49.41 ? 41 ASP A CA 1 ATOM 321 C C . ASP A 1 41 ? 40.871 33.576 31.519 1.00 53.49 ? 41 ASP A C 1 ATOM 322 O O . ASP A 1 41 ? 40.961 33.705 30.291 1.00 55.79 ? 41 ASP A O 1 ATOM 323 C CB . ASP A 1 41 ? 41.190 31.446 32.825 1.00 46.71 ? 41 ASP A CB 1 ATOM 324 C CG . ASP A 1 41 ? 42.397 30.945 32.031 1.00 48.31 ? 41 ASP A CG 1 ATOM 325 O OD1 . ASP A 1 41 ? 42.870 31.596 31.097 1.00 48.16 ? 41 ASP A OD1 1 ATOM 326 O OD2 . ASP A 1 41 ? 42.890 29.866 32.363 1.00 49.14 ? 41 ASP A OD2 1 ATOM 327 N N . ALA A 1 42 ? 41.562 34.368 32.347 1.00 58.34 ? 42 ALA A N 1 ATOM 328 C CA . ALA A 1 42 ? 42.312 35.562 31.913 1.00 60.35 ? 42 ALA A CA 1 ATOM 329 C C . ALA A 1 42 ? 43.169 35.447 30.644 1.00 61.96 ? 42 ALA A C 1 ATOM 330 O O . ALA A 1 42 ? 43.156 36.293 29.756 1.00 61.41 ? 42 ALA A O 1 ATOM 331 C CB . ALA A 1 42 ? 43.237 36.001 33.025 1.00 61.79 ? 42 ALA A CB 1 ATOM 332 N N . ASN A 1 43 ? 43.888 34.329 30.543 1.00 63.19 ? 43 ASN A N 1 ATOM 333 C CA . ASN A 1 43 ? 44.754 34.034 29.401 1.00 64.80 ? 43 ASN A CA 1 ATOM 334 C C . ASN A 1 43 ? 44.026 33.460 28.168 1.00 64.34 ? 43 ASN A C 1 ATOM 335 O O . ASN A 1 43 ? 44.656 32.919 27.235 1.00 66.06 ? 43 ASN A O 1 ATOM 336 C CB . ASN A 1 43 ? 45.826 33.035 29.830 1.00 67.92 ? 43 ASN A CB 1 ATOM 337 C CG . ASN A 1 43 ? 46.450 33.432 31.149 1.00 72.64 ? 43 ASN A CG 1 ATOM 338 O OD1 . ASN A 1 43 ? 45.811 33.332 32.193 1.00 76.16 ? 43 ASN A OD1 1 ATOM 339 N ND2 . ASN A 1 43 ? 47.659 33.956 31.215 1.00 74.84 ? 43 ASN A ND2 1 ATOM 340 N N . GLY A 1 44 ? 42.683 33.524 28.117 1.00 60.65 ? 44 GLY A N 1 ATOM 341 C CA . GLY A 1 44 ? 41.943 32.966 26.986 1.00 54.58 ? 44 GLY A CA 1 ATOM 342 C C . GLY A 1 44 ? 41.991 31.434 26.992 1.00 50.03 ? 44 GLY A C 1 ATOM 343 O O . GLY A 1 44 ? 41.755 30.729 25.985 1.00 50.90 ? 44 GLY A O 1 ATOM 344 N N . ASN A 1 45 ? 42.339 30.898 28.166 1.00 44.75 ? 45 ASN A N 1 ATOM 345 C CA . ASN A 1 45 ? 42.389 29.456 28.255 1.00 43.34 ? 45 ASN A CA 1 ATOM 346 C C . ASN A 1 45 ? 41.025 28.936 28.637 1.00 39.25 ? 45 ASN A C 1 ATOM 347 O O . ASN A 1 45 ? 40.399 29.489 29.538 1.00 36.02 ? 45 ASN A O 1 ATOM 348 C CB . ASN A 1 45 ? 43.369 28.942 29.286 1.00 47.02 ? 45 ASN A CB 1 ATOM 349 C CG . ASN A 1 45 ? 44.794 29.327 28.947 1.00 50.41 ? 45 ASN A CG 1 ATOM 350 O OD1 . ASN A 1 45 ? 45.511 29.786 29.827 1.00 54.21 ? 45 ASN A OD1 1 ATOM 351 N ND2 . ASN A 1 45 ? 45.291 29.245 27.723 1.00 48.47 ? 45 ASN A ND2 1 ATOM 352 N N . PRO A 1 46 ? 40.520 27.932 27.929 1.00 37.07 ? 46 PRO A N 1 ATOM 353 C CA . PRO A 1 46 ? 39.203 27.346 28.127 1.00 36.05 ? 46 PRO A CA 1 ATOM 354 C C . PRO A 1 46 ? 38.913 26.720 29.482 1.00 36.37 ? 46 PRO A C 1 ATOM 355 O O . PRO A 1 46 ? 39.709 25.979 30.062 1.00 36.74 ? 46 PRO A O 1 ATOM 356 C CB . PRO A 1 46 ? 39.076 26.315 27.053 1.00 36.20 ? 46 PRO A CB 1 ATOM 357 C CG . PRO A 1 46 ? 40.123 26.686 26.039 1.00 36.62 ? 46 PRO A CG 1 ATOM 358 C CD . PRO A 1 46 ? 41.244 27.197 26.907 1.00 35.37 ? 46 PRO A CD 1 ATOM 359 N N . VAL A 1 47 ? 37.758 27.033 30.023 1.00 36.93 ? 47 VAL A N 1 ATOM 360 C CA . VAL A 1 47 ? 37.290 26.475 31.291 1.00 36.02 ? 47 VAL A CA 1 ATOM 361 C C . VAL A 1 47 ? 36.542 25.134 31.056 1.00 36.62 ? 47 VAL A C 1 ATOM 362 O O . VAL A 1 47 ? 36.019 24.909 29.952 1.00 34.48 ? 47 VAL A O 1 ATOM 363 C CB . VAL A 1 47 ? 36.438 27.632 31.880 1.00 35.73 ? 47 VAL A CB 1 ATOM 364 C CG1 . VAL A 1 47 ? 35.218 27.229 32.671 1.00 36.66 ? 47 VAL A CG1 1 ATOM 365 C CG2 . VAL A 1 47 ? 37.419 28.398 32.749 1.00 36.88 ? 47 VAL A CG2 1 ATOM 366 N N . ARG A 1 48 ? 36.552 24.140 31.962 1.00 34.48 ? 48 ARG A N 1 ATOM 367 C CA . ARG A 1 48 ? 35.756 22.921 31.713 1.00 33.72 ? 48 ARG A CA 1 ATOM 368 C C . ARG A 1 48 ? 34.259 23.146 32.038 1.00 30.39 ? 48 ARG A C 1 ATOM 369 O O . ARG A 1 48 ? 33.911 24.140 32.676 1.00 28.89 ? 48 ARG A O 1 ATOM 370 C CB . ARG A 1 48 ? 36.198 21.732 32.564 1.00 33.63 ? 48 ARG A CB 1 ATOM 371 C CG . ARG A 1 48 ? 37.575 21.239 32.235 1.00 38.82 ? 48 ARG A CG 1 ATOM 372 C CD . ARG A 1 48 ? 37.738 19.856 32.861 1.00 44.48 ? 48 ARG A CD 1 ATOM 373 N NE . ARG A 1 48 ? 39.062 19.306 32.569 1.00 51.69 ? 48 ARG A NE 1 ATOM 374 C CZ . ARG A 1 48 ? 39.279 18.144 31.917 1.00 55.23 ? 48 ARG A CZ 1 ATOM 375 N NH1 . ARG A 1 48 ? 38.285 17.356 31.453 1.00 55.35 ? 48 ARG A NH1 1 ATOM 376 N NH2 . ARG A 1 48 ? 40.547 17.764 31.714 1.00 56.70 ? 48 ARG A NH2 1 ATOM 377 N N . SER A 1 49 ? 33.310 22.302 31.649 1.00 29.07 ? 49 SER A N 1 ATOM 378 C CA . SER A 1 49 ? 31.880 22.479 31.981 1.00 27.69 ? 49 SER A CA 1 ATOM 379 C C . SER A 1 49 ? 31.182 23.838 31.897 1.00 27.26 ? 49 SER A C 1 ATOM 380 O O . SER A 1 49 ? 30.582 24.412 32.809 1.00 27.61 ? 49 SER A O 1 ATOM 381 C CB . SER A 1 49 ? 31.631 21.931 33.385 1.00 27.96 ? 49 SER A CB 1 ATOM 382 O OG . SER A 1 49 ? 32.237 20.645 33.514 1.00 28.62 ? 49 SER A OG 1 ATOM 383 N N . SER A 1 50 ? 31.112 24.293 30.658 1.00 26.54 ? 50 SER A N 1 ATOM 384 C CA . SER A 1 50 ? 30.509 25.576 30.366 1.00 22.83 ? 50 SER A CA 1 ATOM 385 C C . SER A 1 50 ? 29.577 25.553 29.150 1.00 21.20 ? 50 SER A C 1 ATOM 386 O O . SER A 1 50 ? 29.788 24.784 28.225 1.00 21.99 ? 50 SER A O 1 ATOM 387 C CB . SER A 1 50 ? 31.662 26.576 30.170 1.00 21.82 ? 50 SER A CB 1 ATOM 388 O OG . SER A 1 50 ? 31.228 27.820 29.624 1.00 22.36 ? 50 SER A OG 1 ATOM 389 N N . ALA A 1 51 ? 28.548 26.370 29.115 1.00 19.38 ? 51 ALA A N 1 ATOM 390 C CA . ALA A 1 51 ? 27.633 26.449 28.006 1.00 19.97 ? 51 ALA A CA 1 ATOM 391 C C . ALA A 1 51 ? 27.216 27.896 27.771 1.00 20.26 ? 51 ALA A C 1 ATOM 392 O O . ALA A 1 51 ? 27.089 28.724 28.675 1.00 21.63 ? 51 ALA A O 1 ATOM 393 C CB . ALA A 1 51 ? 26.353 25.647 28.237 1.00 19.02 ? 51 ALA A CB 1 ATOM 394 N N . GLY A 1 52 ? 27.052 28.255 26.514 1.00 18.60 ? 52 GLY A N 1 ATOM 395 C CA . GLY A 1 52 ? 26.653 29.599 26.169 1.00 16.15 ? 52 GLY A CA 1 ATOM 396 C C . GLY A 1 52 ? 26.005 29.663 24.802 1.00 19.27 ? 52 GLY A C 1 ATOM 397 O O . GLY A 1 52 ? 26.126 28.761 23.956 1.00 20.18 ? 52 GLY A O 1 ATOM 398 N N . GLN A 1 53 ? 25.246 30.740 24.610 1.00 20.09 ? 53 GLN A N 1 ATOM 399 C CA . GLN A 1 53 ? 24.574 30.954 23.348 1.00 20.18 ? 53 GLN A CA 1 ATOM 400 C C . GLN A 1 53 ? 24.572 32.398 22.874 1.00 21.85 ? 53 GLN A C 1 ATOM 401 O O . GLN A 1 53 ? 24.494 33.317 23.689 1.00 22.45 ? 53 GLN A O 1 ATOM 402 C CB . GLN A 1 53 ? 23.112 30.493 23.408 1.00 20.55 ? 53 GLN A CB 1 ATOM 403 C CG . GLN A 1 53 ? 22.926 28.991 23.571 1.00 17.25 ? 53 GLN A CG 1 ATOM 404 C CD . GLN A 1 53 ? 21.474 28.562 23.597 1.00 17.99 ? 53 GLN A CD 1 ATOM 405 O OE1 . GLN A 1 53 ? 20.554 29.371 23.630 1.00 19.99 ? 53 GLN A OE1 1 ATOM 406 N NE2 . GLN A 1 53 ? 21.134 27.309 23.620 1.00 16.05 ? 53 GLN A NE2 1 ATOM 407 N N . ALA A 1 54 ? 24.761 32.634 21.576 1.00 20.27 ? 54 ALA A N 1 ATOM 408 C CA . ALA A 1 54 ? 24.704 33.968 21.034 1.00 19.77 ? 54 ALA A CA 1 ATOM 409 C C . ALA A 1 54 ? 23.636 33.853 19.948 1.00 21.56 ? 54 ALA A C 1 ATOM 410 O O . ALA A 1 54 ? 23.726 33.109 18.959 1.00 21.35 ? 54 ALA A O 1 ATOM 411 C CB . ALA A 1 54 ? 26.043 34.373 20.435 1.00 20.56 ? 54 ALA A CB 1 ATOM 412 N N . SER A 1 55 ? 22.526 34.542 20.121 1.00 21.77 ? 55 SER A N 1 ATOM 413 C CA . SER A 1 55 ? 21.453 34.449 19.142 1.00 22.38 ? 55 SER A CA 1 ATOM 414 C C . SER A 1 55 ? 20.981 35.767 18.568 1.00 22.05 ? 55 SER A C 1 ATOM 415 O O . SER A 1 55 ? 21.189 36.818 19.169 1.00 23.23 ? 55 SER A O 1 ATOM 416 C CB . SER A 1 55 ? 20.281 33.696 19.799 1.00 24.88 ? 55 SER A CB 1 ATOM 417 O OG . SER A 1 55 ? 19.961 34.237 21.077 1.00 31.74 ? 55 SER A OG 1 ATOM 418 N N . TYR A 1 56 ? 20.417 35.807 17.372 1.00 20.29 ? 56 TYR A N 1 ATOM 419 C CA . TYR A 1 56 ? 19.943 37.056 16.838 1.00 20.53 ? 56 TYR A CA 1 ATOM 420 C C . TYR A 1 56 ? 18.823 37.556 17.747 1.00 22.33 ? 56 TYR A C 1 ATOM 421 O O . TYR A 1 56 ? 17.985 36.784 18.203 1.00 21.96 ? 56 TYR A O 1 ATOM 422 C CB . TYR A 1 56 ? 19.417 36.841 15.449 1.00 19.43 ? 56 TYR A CB 1 ATOM 423 C CG . TYR A 1 56 ? 18.984 38.117 14.740 1.00 23.13 ? 56 TYR A CG 1 ATOM 424 C CD1 . TYR A 1 56 ? 19.867 39.176 14.553 1.00 26.72 ? 56 TYR A CD1 1 ATOM 425 C CD2 . TYR A 1 56 ? 17.712 38.161 14.212 1.00 25.39 ? 56 TYR A CD2 1 ATOM 426 C CE1 . TYR A 1 56 ? 19.472 40.285 13.837 1.00 27.18 ? 56 TYR A CE1 1 ATOM 427 C CE2 . TYR A 1 56 ? 17.311 39.258 13.495 1.00 28.42 ? 56 TYR A CE2 1 ATOM 428 C CZ . TYR A 1 56 ? 18.193 40.295 13.309 1.00 30.30 ? 56 TYR A CZ 1 ATOM 429 O OH . TYR A 1 56 ? 17.771 41.358 12.528 1.00 36.49 ? 56 TYR A OH 1 ATOM 430 N N . SER A 1 57 ? 18.748 38.827 18.108 1.00 25.78 ? 57 SER A N 1 ATOM 431 C CA . SER A 1 57 ? 17.673 39.309 18.997 1.00 27.97 ? 57 SER A CA 1 ATOM 432 C C . SER A 1 57 ? 16.274 39.280 18.406 1.00 30.23 ? 57 SER A C 1 ATOM 433 O O . SER A 1 57 ? 15.339 38.895 19.095 1.00 33.82 ? 57 SER A O 1 ATOM 434 C CB . SER A 1 57 ? 17.929 40.752 19.471 1.00 26.56 ? 57 SER A CB 1 ATOM 435 O OG . SER A 1 57 ? 19.138 40.752 20.225 1.00 28.72 ? 57 SER A OG 1 ATOM 436 N N . GLU A 1 58 ? 16.037 39.635 17.158 1.00 30.76 ? 58 GLU A N 1 ATOM 437 C CA . GLU A 1 58 ? 14.691 39.587 16.646 1.00 32.14 ? 58 GLU A CA 1 ATOM 438 C C . GLU A 1 58 ? 14.166 38.171 16.401 1.00 32.54 ? 58 GLU A C 1 ATOM 439 O O . GLU A 1 58 ? 14.921 37.279 16.018 1.00 29.46 ? 58 GLU A O 1 ATOM 440 C CB . GLU A 1 58 ? 14.630 40.338 15.360 1.00 38.89 ? 58 GLU A CB 1 ATOM 441 C CG . GLU A 1 58 ? 14.723 41.853 15.354 1.00 52.81 ? 58 GLU A CG 1 ATOM 442 C CD . GLU A 1 58 ? 13.821 42.486 14.266 1.00 63.86 ? 58 GLU A CD 1 ATOM 443 O OE1 . GLU A 1 58 ? 13.970 42.174 13.058 1.00 67.39 ? 58 GLU A OE1 1 ATOM 444 O OE2 . GLU A 1 58 ? 12.946 43.289 14.648 1.00 68.36 ? 58 GLU A OE2 1 ATOM 445 N N . PRO A 1 59 ? 12.878 37.884 16.574 1.00 33.38 ? 59 PRO A N 1 ATOM 446 C CA . PRO A 1 59 ? 12.257 36.639 16.121 1.00 32.48 ? 59 PRO A CA 1 ATOM 447 C C . PRO A 1 59 ? 12.304 36.484 14.599 1.00 29.76 ? 59 PRO A C 1 ATOM 448 O O . PRO A 1 59 ? 12.162 37.452 13.841 1.00 28.13 ? 59 PRO A O 1 ATOM 449 C CB . PRO A 1 59 ? 10.826 36.709 16.661 1.00 35.26 ? 59 PRO A CB 1 ATOM 450 C CG . PRO A 1 59 ? 10.868 37.815 17.711 1.00 36.13 ? 59 PRO A CG 1 ATOM 451 C CD . PRO A 1 59 ? 11.881 38.792 17.146 1.00 33.79 ? 59 PRO A CD 1 ATOM 452 N N . VAL A 1 60 ? 12.515 35.268 14.124 1.00 27.52 ? 60 VAL A N 1 ATOM 453 C CA . VAL A 1 60 ? 12.566 35.007 12.705 1.00 23.95 ? 60 VAL A CA 1 ATOM 454 C C . VAL A 1 60 ? 11.317 34.245 12.261 1.00 23.55 ? 60 VAL A C 1 ATOM 455 O O . VAL A 1 60 ? 10.963 33.206 12.821 1.00 23.90 ? 60 VAL A O 1 ATOM 456 C CB . VAL A 1 60 ? 13.869 34.210 12.407 1.00 24.57 ? 60 VAL A CB 1 ATOM 457 C CG1 . VAL A 1 60 ? 13.966 33.809 10.939 1.00 22.86 ? 60 VAL A CG1 1 ATOM 458 C CG2 . VAL A 1 60 ? 15.066 35.098 12.748 1.00 22.57 ? 60 VAL A CG2 1 ATOM 459 N N . PHE A 1 61 ? 10.592 34.763 11.271 1.00 23.43 ? 61 PHE A N 1 ATOM 460 C CA . PHE A 1 61 ? 9.429 34.084 10.761 1.00 24.19 ? 61 PHE A CA 1 ATOM 461 C C . PHE A 1 61 ? 9.833 32.866 9.960 1.00 25.09 ? 61 PHE A C 1 ATOM 462 O O . PHE A 1 61 ? 10.662 32.912 9.054 1.00 25.45 ? 61 PHE A O 1 ATOM 463 C CB . PHE A 1 61 ? 8.614 34.983 9.842 1.00 24.67 ? 61 PHE A CB 1 ATOM 464 C CG . PHE A 1 61 ? 7.543 34.263 8.994 1.00 28.58 ? 61 PHE A CG 1 ATOM 465 C CD1 . PHE A 1 61 ? 6.320 33.914 9.545 1.00 30.47 ? 61 PHE A CD1 1 ATOM 466 C CD2 . PHE A 1 61 ? 7.791 33.952 7.664 1.00 26.97 ? 61 PHE A CD2 1 ATOM 467 C CE1 . PHE A 1 61 ? 5.374 33.264 8.759 1.00 30.34 ? 61 PHE A CE1 1 ATOM 468 C CE2 . PHE A 1 61 ? 6.848 33.306 6.893 1.00 27.18 ? 61 PHE A CE2 1 ATOM 469 C CZ . PHE A 1 61 ? 5.635 32.960 7.437 1.00 30.30 ? 61 PHE A CZ 1 ATOM 470 N N . LEU A 1 62 ? 9.219 31.756 10.278 1.00 25.99 ? 62 LEU A N 1 ATOM 471 C CA . LEU A 1 62 ? 9.464 30.545 9.533 1.00 26.57 ? 62 LEU A CA 1 ATOM 472 C C . LEU A 1 62 ? 8.282 30.075 8.661 1.00 28.83 ? 62 LEU A C 1 ATOM 473 O O . LEU A 1 62 ? 8.424 29.728 7.482 1.00 27.11 ? 62 LEU A O 1 ATOM 474 C CB . LEU A 1 62 ? 9.828 29.412 10.459 1.00 27.13 ? 62 LEU A CB 1 ATOM 475 C CG . LEU A 1 62 ? 11.306 29.160 10.705 1.00 30.52 ? 62 LEU A CG 1 ATOM 476 C CD1 . LEU A 1 62 ? 11.314 27.816 11.422 1.00 31.66 ? 62 LEU A CD1 1 ATOM 477 C CD2 . LEU A 1 62 ? 12.185 29.130 9.447 1.00 26.22 ? 62 LEU A CD2 1 ATOM 478 N N . TRP A 1 63 ? 7.073 30.068 9.209 1.00 29.51 ? 63 TRP A N 1 ATOM 479 C CA . TRP A 1 63 ? 5.905 29.603 8.481 1.00 29.68 ? 63 TRP A CA 1 ATOM 480 C C . TRP A 1 63 ? 4.624 30.098 9.111 1.00 32.05 ? 63 TRP A C 1 ATOM 481 O O . TRP A 1 63 ? 4.628 30.629 10.224 1.00 31.90 ? 63 TRP A O 1 ATOM 482 C CB . TRP A 1 63 ? 5.855 28.075 8.492 1.00 27.40 ? 63 TRP A CB 1 ATOM 483 C CG . TRP A 1 63 ? 5.838 27.447 9.901 1.00 31.09 ? 63 TRP A CG 1 ATOM 484 C CD1 . TRP A 1 63 ? 6.983 27.214 10.614 1.00 32.00 ? 63 TRP A CD1 1 ATOM 485 C CD2 . TRP A 1 63 ? 4.722 27.013 10.589 1.00 35.73 ? 63 TRP A CD2 1 ATOM 486 N NE1 . TRP A 1 63 ? 6.603 26.642 11.727 1.00 33.42 ? 63 TRP A NE1 1 ATOM 487 C CE2 . TRP A 1 63 ? 5.277 26.512 11.760 1.00 35.54 ? 63 TRP A CE2 1 ATOM 488 C CE3 . TRP A 1 63 ? 3.341 26.979 10.396 1.00 39.20 ? 63 TRP A CE3 1 ATOM 489 C CZ2 . TRP A 1 63 ? 4.478 25.964 12.745 1.00 38.47 ? 63 TRP A CZ2 1 ATOM 490 C CZ3 . TRP A 1 63 ? 2.542 26.428 11.388 1.00 38.34 ? 63 TRP A CZ3 1 ATOM 491 C CH2 . TRP A 1 63 ? 3.107 25.927 12.547 1.00 36.68 ? 63 TRP A CH2 1 ATOM 492 N N . ASP A 1 64 ? 3.519 29.994 8.404 1.00 33.70 ? 64 ASP A N 1 ATOM 493 C CA . ASP A 1 64 ? 2.250 30.343 9.018 1.00 34.88 ? 64 ASP A CA 1 ATOM 494 C C . ASP A 1 64 ? 1.190 29.407 8.468 1.00 38.49 ? 64 ASP A C 1 ATOM 495 O O . ASP A 1 64 ? 1.389 28.671 7.501 1.00 36.59 ? 64 ASP A O 1 ATOM 496 C CB . ASP A 1 64 ? 1.828 31.784 8.762 1.00 31.36 ? 64 ASP A CB 1 ATOM 497 C CG . ASP A 1 64 ? 1.535 32.216 7.351 1.00 32.78 ? 64 ASP A CG 1 ATOM 498 O OD1 . ASP A 1 64 ? 1.467 31.405 6.426 1.00 33.05 ? 64 ASP A OD1 1 ATOM 499 O OD2 . ASP A 1 64 ? 1.375 33.420 7.184 1.00 39.37 ? 64 ASP A OD2 1 ATOM 500 N N . SER A 1 65 ? 0.008 29.461 9.048 1.00 43.02 ? 65 SER A N 1 ATOM 501 C CA . SER A 1 65 ? -1.107 28.615 8.621 1.00 46.41 ? 65 SER A CA 1 ATOM 502 C C . SER A 1 65 ? -1.444 28.688 7.134 1.00 48.21 ? 65 SER A C 1 ATOM 503 O O . SER A 1 65 ? -1.739 27.674 6.494 1.00 50.80 ? 65 SER A O 1 ATOM 504 C CB . SER A 1 65 ? -2.374 28.986 9.365 1.00 48.78 ? 65 SER A CB 1 ATOM 505 O OG . SER A 1 65 ? -2.656 30.399 9.268 1.00 52.47 ? 65 SER A OG 1 ATOM 506 N N . THR A 1 66 ? -1.300 29.892 6.552 1.00 47.35 ? 66 THR A N 1 ATOM 507 C CA . THR A 1 66 ? -1.609 30.138 5.139 1.00 46.10 ? 66 THR A CA 1 ATOM 508 C C . THR A 1 66 ? -0.685 29.549 4.079 1.00 45.54 ? 66 THR A C 1 ATOM 509 O O . THR A 1 66 ? -0.764 29.937 2.912 1.00 46.50 ? 66 THR A O 1 ATOM 510 C CB . THR A 1 66 ? -1.718 31.660 4.838 1.00 45.99 ? 66 THR A CB 1 ATOM 511 O OG1 . THR A 1 66 ? -0.439 32.263 4.868 1.00 45.71 ? 66 THR A OG1 1 ATOM 512 C CG2 . THR A 1 66 ? -2.582 32.344 5.883 1.00 47.53 ? 66 THR A CG2 1 ATOM 513 N N . GLY A 1 67 ? 0.190 28.600 4.437 1.00 43.63 ? 67 GLY A N 1 ATOM 514 C CA . GLY A 1 67 ? 1.116 27.981 3.500 1.00 40.51 ? 67 GLY A CA 1 ATOM 515 C C . GLY A 1 67 ? 2.461 28.695 3.329 1.00 40.02 ? 67 GLY A C 1 ATOM 516 O O . GLY A 1 67 ? 3.427 28.047 2.905 1.00 40.55 ? 67 GLY A O 1 ATOM 517 N N . LYS A 1 68 ? 2.536 30.016 3.596 1.00 38.63 ? 68 LYS A N 1 ATOM 518 C CA . LYS A 1 68 ? 3.781 30.791 3.496 1.00 37.09 ? 68 LYS A CA 1 ATOM 519 C C . LYS A 1 68 ? 4.849 30.238 4.419 1.00 34.52 ? 68 LYS A C 1 ATOM 520 O O . LYS A 1 68 ? 4.679 30.067 5.621 1.00 34.52 ? 68 LYS A O 1 ATOM 521 C CB . LYS A 1 68 ? 3.641 32.248 3.897 1.00 38.90 ? 68 LYS A CB 1 ATOM 522 C CG . LYS A 1 68 ? 2.774 32.973 2.892 1.00 49.34 ? 68 LYS A CG 1 ATOM 523 C CD . LYS A 1 68 ? 1.969 34.133 3.501 1.00 57.07 ? 68 LYS A CD 1 ATOM 524 C CE . LYS A 1 68 ? 2.691 35.479 3.569 1.00 59.12 ? 68 LYS A CE 1 ATOM 525 N NZ . LYS A 1 68 ? 2.780 35.976 4.933 1.00 61.98 ? 68 LYS A NZ 1 ATOM 526 N N . ALA A 1 69 ? 5.977 29.933 3.819 1.00 33.17 ? 69 ALA A N 1 ATOM 527 C CA . ALA A 1 69 ? 7.122 29.394 4.528 1.00 31.77 ? 69 ALA A CA 1 ATOM 528 C C . ALA A 1 69 ? 8.433 29.979 4.000 1.00 31.12 ? 69 ALA A C 1 ATOM 529 O O . ALA A 1 69 ? 8.634 30.265 2.803 1.00 32.01 ? 69 ALA A O 1 ATOM 530 C CB . ALA A 1 69 ? 7.181 27.886 4.374 1.00 28.96 ? 69 ALA A CB 1 ATOM 531 N N . ALA A 1 70 ? 9.304 30.261 4.959 1.00 28.23 ? 70 ALA A N 1 ATOM 532 C CA . ALA A 1 70 ? 10.613 30.813 4.671 1.00 25.26 ? 70 ALA A CA 1 ATOM 533 C C . ALA A 1 70 ? 11.748 29.843 4.360 1.00 23.07 ? 70 ALA A C 1 ATOM 534 O O . ALA A 1 70 ? 11.986 28.826 5.034 1.00 22.70 ? 70 ALA A O 1 ATOM 535 C CB . ALA A 1 70 ? 11.114 31.660 5.828 1.00 24.37 ? 70 ALA A CB 1 ATOM 536 N N . SER A 1 71 ? 12.341 30.133 3.214 1.00 18.62 ? 71 SER A N 1 ATOM 537 C CA . SER A 1 71 ? 13.528 29.410 2.806 1.00 16.98 ? 71 SER A CA 1 ATOM 538 C C . SER A 1 71 ? 14.633 30.306 3.354 1.00 17.23 ? 71 SER A C 1 ATOM 539 O O . SER A 1 71 ? 14.460 31.524 3.533 1.00 18.05 ? 71 SER A O 1 ATOM 540 C CB . SER A 1 71 ? 13.767 29.329 1.313 1.00 16.06 ? 71 SER A CB 1 ATOM 541 O OG . SER A 1 71 ? 12.871 28.419 0.692 1.00 18.18 ? 71 SER A OG 1 ATOM 542 N N . PHE A 1 72 ? 15.809 29.787 3.643 1.00 16.62 ? 72 PHE A N 1 ATOM 543 C CA . PHE A 1 72 ? 16.859 30.631 4.172 1.00 15.92 ? 72 PHE A CA 1 ATOM 544 C C . PHE A 1 72 ? 18.266 30.140 3.877 1.00 14.60 ? 72 PHE A C 1 ATOM 545 O O . PHE A 1 72 ? 18.543 29.000 3.540 1.00 13.75 ? 72 PHE A O 1 ATOM 546 C CB . PHE A 1 72 ? 16.698 30.788 5.740 1.00 16.43 ? 72 PHE A CB 1 ATOM 547 C CG . PHE A 1 72 ? 16.963 29.562 6.650 1.00 20.25 ? 72 PHE A CG 1 ATOM 548 C CD1 . PHE A 1 72 ? 18.258 29.095 6.904 1.00 20.21 ? 72 PHE A CD1 1 ATOM 549 C CD2 . PHE A 1 72 ? 15.903 28.888 7.230 1.00 21.02 ? 72 PHE A CD2 1 ATOM 550 C CE1 . PHE A 1 72 ? 18.472 27.990 7.713 1.00 21.13 ? 72 PHE A CE1 1 ATOM 551 C CE2 . PHE A 1 72 ? 16.135 27.785 8.040 1.00 20.60 ? 72 PHE A CE2 1 ATOM 552 C CZ . PHE A 1 72 ? 17.409 27.326 8.283 1.00 20.40 ? 72 PHE A CZ 1 ATOM 553 N N . TYR A 1 73 ? 19.159 31.070 4.027 1.00 13.46 ? 73 TYR A N 1 ATOM 554 C CA . TYR A 1 73 ? 20.565 30.795 3.922 1.00 14.02 ? 73 TYR A CA 1 ATOM 555 C C . TYR A 1 73 ? 21.348 31.611 4.990 1.00 13.41 ? 73 TYR A C 1 ATOM 556 O O . TYR A 1 73 ? 21.200 32.832 5.171 1.00 15.46 ? 73 TYR A O 1 ATOM 557 C CB . TYR A 1 73 ? 20.991 31.146 2.534 1.00 13.73 ? 73 TYR A CB 1 ATOM 558 C CG . TYR A 1 73 ? 22.489 31.255 2.459 1.00 17.49 ? 73 TYR A CG 1 ATOM 559 C CD1 . TYR A 1 73 ? 23.344 30.240 2.768 1.00 18.68 ? 73 TYR A CD1 1 ATOM 560 C CD2 . TYR A 1 73 ? 22.962 32.448 2.110 1.00 19.49 ? 73 TYR A CD2 1 ATOM 561 C CE1 . TYR A 1 73 ? 24.663 30.480 2.712 1.00 15.11 ? 73 TYR A CE1 1 ATOM 562 C CE2 . TYR A 1 73 ? 24.263 32.688 2.043 1.00 17.82 ? 73 TYR A CE2 1 ATOM 563 C CZ . TYR A 1 73 ? 25.063 31.689 2.347 1.00 15.01 ? 73 TYR A CZ 1 ATOM 564 O OH . TYR A 1 73 ? 26.380 31.912 2.210 1.00 32.09 ? 73 TYR A OH 1 ATOM 565 N N . THR A 1 74 ? 22.230 30.938 5.707 1.00 12.33 ? 74 THR A N 1 ATOM 566 C CA . THR A 1 74 ? 23.070 31.571 6.702 1.00 13.34 ? 74 THR A CA 1 ATOM 567 C C . THR A 1 74 ? 24.515 31.159 6.462 1.00 14.21 ? 74 THR A C 1 ATOM 568 O O . THR A 1 74 ? 24.830 30.018 6.123 1.00 13.60 ? 74 THR A O 1 ATOM 569 C CB . THR A 1 74 ? 22.701 31.181 8.207 1.00 15.89 ? 74 THR A CB 1 ATOM 570 O OG1 . THR A 1 74 ? 23.389 32.159 8.985 1.00 16.22 ? 74 THR A OG1 1 ATOM 571 C CG2 . THR A 1 74 ? 23.085 29.758 8.708 1.00 14.44 ? 74 THR A CG2 1 ATOM 572 N N . SER A 1 75 ? 25.462 32.051 6.615 1.00 13.09 ? 75 SER A N 1 ATOM 573 C CA . SER A 1 75 ? 26.870 31.689 6.459 1.00 13.49 ? 75 SER A CA 1 ATOM 574 C C . SER A 1 75 ? 27.621 32.308 7.619 1.00 13.82 ? 75 SER A C 1 ATOM 575 O O . SER A 1 75 ? 27.204 33.346 8.159 1.00 15.99 ? 75 SER A O 1 ATOM 576 C CB . SER A 1 75 ? 27.568 32.234 5.248 1.00 12.55 ? 75 SER A CB 1 ATOM 577 O OG . SER A 1 75 ? 27.546 33.658 5.281 1.00 18.79 ? 75 SER A OG 1 ATOM 578 N N . PHE A 1 76 ? 28.700 31.690 8.051 1.00 13.33 ? 76 PHE A N 1 ATOM 579 C CA . PHE A 1 76 ? 29.433 32.242 9.147 1.00 12.14 ? 76 PHE A CA 1 ATOM 580 C C . PHE A 1 76 ? 30.802 31.653 9.174 1.00 13.60 ? 76 PHE A C 1 ATOM 581 O O . PHE A 1 76 ? 31.029 30.552 8.687 1.00 15.55 ? 76 PHE A O 1 ATOM 582 C CB . PHE A 1 76 ? 28.742 31.936 10.506 1.00 13.90 ? 76 PHE A CB 1 ATOM 583 C CG . PHE A 1 76 ? 28.384 30.470 10.821 1.00 13.87 ? 76 PHE A CG 1 ATOM 584 C CD1 . PHE A 1 76 ? 27.184 29.936 10.359 1.00 13.04 ? 76 PHE A CD1 1 ATOM 585 C CD2 . PHE A 1 76 ? 29.245 29.683 11.571 1.00 12.68 ? 76 PHE A CD2 1 ATOM 586 C CE1 . PHE A 1 76 ? 26.860 28.625 10.650 1.00 13.70 ? 76 PHE A CE1 1 ATOM 587 C CE2 . PHE A 1 76 ? 28.909 28.374 11.860 1.00 12.88 ? 76 PHE A CE2 1 ATOM 588 C CZ . PHE A 1 76 ? 27.721 27.850 11.396 1.00 12.77 ? 76 PHE A CZ 1 ATOM 589 N N . THR A 1 77 ? 31.745 32.386 9.706 1.00 12.55 ? 77 THR A N 1 ATOM 590 C CA . THR A 1 77 ? 33.072 31.823 9.817 1.00 15.49 ? 77 THR A CA 1 ATOM 591 C C . THR A 1 77 ? 33.308 31.706 11.306 1.00 15.70 ? 77 THR A C 1 ATOM 592 O O . THR A 1 77 ? 32.755 32.423 12.151 1.00 17.43 ? 77 THR A O 1 ATOM 593 C CB . THR A 1 77 ? 34.178 32.690 9.231 1.00 17.01 ? 77 THR A CB 1 ATOM 594 O OG1 . THR A 1 77 ? 34.051 33.952 9.851 1.00 23.75 ? 77 THR A OG1 1 ATOM 595 C CG2 . THR A 1 77 ? 34.081 32.857 7.733 1.00 15.25 ? 77 THR A CG2 1 ATOM 596 N N . PHE A 1 78 ? 33.998 30.636 11.651 1.00 17.85 ? 78 PHE A N 1 ATOM 597 C CA . PHE A 1 78 ? 34.299 30.412 13.043 1.00 17.96 ? 78 PHE A CA 1 ATOM 598 C C . PHE A 1 78 ? 35.668 29.799 13.253 1.00 18.80 ? 78 PHE A C 1 ATOM 599 O O . PHE A 1 78 ? 36.250 29.174 12.360 1.00 17.29 ? 78 PHE A O 1 ATOM 600 C CB . PHE A 1 78 ? 33.260 29.483 13.725 1.00 14.29 ? 78 PHE A CB 1 ATOM 601 C CG . PHE A 1 78 ? 33.196 28.073 13.184 1.00 16.42 ? 78 PHE A CG 1 ATOM 602 C CD1 . PHE A 1 78 ? 32.439 27.803 12.088 1.00 19.32 ? 78 PHE A CD1 1 ATOM 603 C CD2 . PHE A 1 78 ? 33.883 27.052 13.799 1.00 17.86 ? 78 PHE A CD2 1 ATOM 604 C CE1 . PHE A 1 78 ? 32.369 26.510 11.615 1.00 22.59 ? 78 PHE A CE1 1 ATOM 605 C CE2 . PHE A 1 78 ? 33.811 25.767 13.322 1.00 18.77 ? 78 PHE A CE2 1 ATOM 606 C CZ . PHE A 1 78 ? 33.045 25.487 12.221 1.00 20.04 ? 78 PHE A CZ 1 ATOM 607 N N . LEU A 1 79 ? 36.166 30.034 14.463 1.00 18.21 ? 79 LEU A N 1 ATOM 608 C CA . LEU A 1 79 ? 37.432 29.480 14.893 1.00 19.20 ? 79 LEU A CA 1 ATOM 609 C C . LEU A 1 79 ? 37.139 28.646 16.138 1.00 18.84 ? 79 LEU A C 1 ATOM 610 O O . LEU A 1 79 ? 36.815 29.181 17.217 1.00 19.88 ? 79 LEU A O 1 ATOM 611 C CB . LEU A 1 79 ? 38.461 30.547 15.286 1.00 20.59 ? 79 LEU A CB 1 ATOM 612 C CG . LEU A 1 79 ? 39.764 30.083 15.979 1.00 22.43 ? 79 LEU A CG 1 ATOM 613 C CD1 . LEU A 1 79 ? 40.523 29.212 15.012 1.00 21.13 ? 79 LEU A CD1 1 ATOM 614 C CD2 . LEU A 1 79 ? 40.617 31.288 16.432 1.00 21.30 ? 79 LEU A CD2 1 ATOM 615 N N . LEU A 1 80 ? 37.204 27.326 15.957 1.00 17.16 ? 80 LEU A N 1 ATOM 616 C CA . LEU A 1 80 ? 37.019 26.404 17.055 1.00 18.48 ? 80 LEU A CA 1 ATOM 617 C C . LEU A 1 80 ? 38.469 26.190 17.562 1.00 21.38 ? 80 LEU A C 1 ATOM 618 O O . LEU A 1 80 ? 39.259 25.458 16.986 1.00 20.51 ? 80 LEU A O 1 ATOM 619 C CB . LEU A 1 80 ? 36.400 25.146 16.514 1.00 18.59 ? 80 LEU A CB 1 ATOM 620 C CG . LEU A 1 80 ? 36.414 23.910 17.383 1.00 23.08 ? 80 LEU A CG 1 ATOM 621 C CD1 . LEU A 1 80 ? 35.820 24.189 18.711 1.00 23.82 ? 80 LEU A CD1 1 ATOM 622 C CD2 . LEU A 1 80 ? 35.542 22.876 16.763 1.00 26.36 ? 80 LEU A CD2 1 ATOM 623 N N . LYS A 1 81 ? 38.889 26.898 18.596 1.00 22.01 ? 81 LYS A N 1 ATOM 624 C CA . LYS A 1 81 ? 40.223 26.795 19.147 1.00 25.00 ? 81 LYS A CA 1 ATOM 625 C C . LYS A 1 81 ? 40.418 25.602 20.096 1.00 25.41 ? 81 LYS A C 1 ATOM 626 O O . LYS A 1 81 ? 39.752 25.441 21.111 1.00 26.58 ? 81 LYS A O 1 ATOM 627 C CB . LYS A 1 81 ? 40.495 28.111 19.831 1.00 25.78 ? 81 LYS A CB 1 ATOM 628 C CG . LYS A 1 81 ? 41.837 28.209 20.554 1.00 32.04 ? 81 LYS A CG 1 ATOM 629 C CD . LYS A 1 81 ? 43.045 28.256 19.633 1.00 32.83 ? 81 LYS A CD 1 ATOM 630 C CE . LYS A 1 81 ? 44.374 28.441 20.377 1.00 29.74 ? 81 LYS A CE 1 ATOM 631 N NZ . LYS A 1 81 ? 45.428 28.512 19.380 1.00 32.04 ? 81 LYS A NZ 1 ATOM 632 N N . ASN A 1 82 ? 41.358 24.739 19.750 1.00 27.24 ? 82 ASN A N 1 ATOM 633 C CA . ASN A 1 82 ? 41.724 23.509 20.467 1.00 29.12 ? 82 ASN A CA 1 ATOM 634 C C . ASN A 1 82 ? 43.095 23.556 21.146 1.00 30.48 ? 82 ASN A C 1 ATOM 635 O O . ASN A 1 82 ? 44.108 23.909 20.538 1.00 30.25 ? 82 ASN A O 1 ATOM 636 C CB . ASN A 1 82 ? 41.780 22.296 19.540 1.00 28.83 ? 82 ASN A CB 1 ATOM 637 C CG . ASN A 1 82 ? 40.575 22.193 18.625 1.00 32.32 ? 82 ASN A CG 1 ATOM 638 O OD1 . ASN A 1 82 ? 40.598 22.774 17.543 1.00 36.57 ? 82 ASN A OD1 1 ATOM 639 N ND2 . ASN A 1 82 ? 39.487 21.508 18.915 1.00 27.82 ? 82 ASN A ND2 1 ATOM 640 N N . TYR A 1 83 ? 43.150 23.127 22.403 1.00 30.96 ? 83 TYR A N 1 ATOM 641 C CA . TYR A 1 83 ? 44.371 23.107 23.185 1.00 30.80 ? 83 TYR A CA 1 ATOM 642 C C . TYR A 1 83 ? 44.891 21.707 23.400 1.00 34.06 ? 83 TYR A C 1 ATOM 643 O O . TYR A 1 83 ? 45.412 21.332 24.436 1.00 41.89 ? 83 TYR A O 1 ATOM 644 C CB . TYR A 1 83 ? 44.111 23.764 24.511 1.00 28.24 ? 83 TYR A CB 1 ATOM 645 C CG . TYR A 1 83 ? 44.038 25.258 24.390 1.00 28.82 ? 83 TYR A CG 1 ATOM 646 C CD1 . TYR A 1 83 ? 42.864 25.838 23.980 1.00 31.08 ? 83 TYR A CD1 1 ATOM 647 C CD2 . TYR A 1 83 ? 45.158 26.016 24.672 1.00 30.38 ? 83 TYR A CD2 1 ATOM 648 C CE1 . TYR A 1 83 ? 42.810 27.202 23.849 1.00 33.22 ? 83 TYR A CE1 1 ATOM 649 C CE2 . TYR A 1 83 ? 45.112 27.388 24.546 1.00 30.41 ? 83 TYR A CE2 1 ATOM 650 C CZ . TYR A 1 83 ? 43.931 27.956 24.137 1.00 34.32 ? 83 TYR A CZ 1 ATOM 651 O OH . TYR A 1 83 ? 43.848 29.322 24.026 1.00 39.56 ? 83 TYR A OH 1 ATOM 652 N N . GLY A 1 84 ? 44.837 20.908 22.377 1.00 35.55 ? 84 GLY A N 1 ATOM 653 C CA . GLY A 1 84 ? 45.287 19.528 22.413 1.00 35.70 ? 84 GLY A CA 1 ATOM 654 C C . GLY A 1 84 ? 44.344 18.727 21.546 1.00 35.51 ? 84 GLY A C 1 ATOM 655 O O . GLY A 1 84 ? 43.481 19.293 20.859 1.00 36.06 ? 84 GLY A O 1 ATOM 656 N N . ALA A 1 85 ? 44.503 17.422 21.460 1.00 36.33 ? 85 ALA A N 1 ATOM 657 C CA . ALA A 1 85 ? 43.567 16.628 20.675 1.00 37.77 ? 85 ALA A CA 1 ATOM 658 C C . ALA A 1 85 ? 43.297 15.347 21.443 1.00 39.58 ? 85 ALA A C 1 ATOM 659 O O . ALA A 1 85 ? 44.250 14.787 21.983 1.00 45.44 ? 85 ALA A O 1 ATOM 660 C CB . ALA A 1 85 ? 44.121 16.234 19.337 1.00 36.97 ? 85 ALA A CB 1 ATOM 661 N N . PRO A 1 86 ? 42.083 14.828 21.610 1.00 38.14 ? 86 PRO A N 1 ATOM 662 C CA . PRO A 1 86 ? 40.836 15.446 21.214 1.00 35.24 ? 86 PRO A CA 1 ATOM 663 C C . PRO A 1 86 ? 40.414 16.522 22.185 1.00 31.40 ? 86 PRO A C 1 ATOM 664 O O . PRO A 1 86 ? 41.109 16.774 23.170 1.00 31.10 ? 86 PRO A O 1 ATOM 665 C CB . PRO A 1 86 ? 39.892 14.272 21.160 1.00 38.94 ? 86 PRO A CB 1 ATOM 666 C CG . PRO A 1 86 ? 40.334 13.476 22.366 1.00 38.79 ? 86 PRO A CG 1 ATOM 667 C CD . PRO A 1 86 ? 41.840 13.502 22.175 1.00 38.24 ? 86 PRO A CD 1 ATOM 668 N N . THR A 1 87 ? 39.306 17.174 21.900 1.00 27.24 ? 87 THR A N 1 ATOM 669 C CA . THR A 1 87 ? 38.771 18.204 22.771 1.00 24.73 ? 87 THR A CA 1 ATOM 670 C C . THR A 1 87 ? 37.274 17.945 22.892 1.00 23.12 ? 87 THR A C 1 ATOM 671 O O . THR A 1 87 ? 36.773 16.966 22.326 1.00 22.77 ? 87 THR A O 1 ATOM 672 C CB . THR A 1 87 ? 39.012 19.663 22.224 1.00 25.24 ? 87 THR A CB 1 ATOM 673 O OG1 . THR A 1 87 ? 38.311 19.887 21.008 1.00 24.67 ? 87 THR A OG1 1 ATOM 674 C CG2 . THR A 1 87 ? 40.508 19.879 21.943 1.00 25.18 ? 87 THR A CG2 1 ATOM 675 N N . ALA A 1 88 ? 36.548 18.717 23.698 1.00 21.93 ? 88 ALA A N 1 ATOM 676 C CA . ALA A 1 88 ? 35.105 18.519 23.807 1.00 21.96 ? 88 ALA A CA 1 ATOM 677 C C . ALA A 1 88 ? 34.409 19.841 24.108 1.00 21.04 ? 88 ALA A C 1 ATOM 678 O O . ALA A 1 88 ? 34.967 20.706 24.799 1.00 20.71 ? 88 ALA A O 1 ATOM 679 C CB . ALA A 1 88 ? 34.764 17.519 24.924 1.00 19.65 ? 88 ALA A CB 1 ATOM 680 N N . ASP A 1 89 ? 33.168 20.145 23.725 1.00 21.94 ? 89 ASP A N 1 ATOM 681 C CA . ASP A 1 89 ? 32.249 19.269 22.984 1.00 21.99 ? 89 ASP A CA 1 ATOM 682 C C . ASP A 1 89 ? 31.766 19.615 21.594 1.00 22.55 ? 89 ASP A C 1 ATOM 683 O O . ASP A 1 89 ? 31.142 18.826 20.899 1.00 21.21 ? 89 ASP A O 1 ATOM 684 C CB . ASP A 1 89 ? 31.022 19.075 23.793 1.00 21.08 ? 89 ASP A CB 1 ATOM 685 C CG . ASP A 1 89 ? 31.285 18.037 24.861 1.00 23.12 ? 89 ASP A CG 1 ATOM 686 O OD1 . ASP A 1 89 ? 31.147 16.851 24.560 1.00 22.27 ? 89 ASP A OD1 1 ATOM 687 O OD2 . ASP A 1 89 ? 31.635 18.436 25.970 1.00 25.67 ? 89 ASP A OD2 1 ATOM 688 N N . GLY A 1 90 ? 32.010 20.859 21.212 1.00 20.79 ? 90 GLY A N 1 ATOM 689 C CA . GLY A 1 90 ? 31.610 21.336 19.905 1.00 19.92 ? 90 GLY A CA 1 ATOM 690 C C . GLY A 1 90 ? 30.713 22.572 19.968 1.00 20.06 ? 90 GLY A C 1 ATOM 691 O O . GLY A 1 90 ? 30.590 23.235 21.006 1.00 18.52 ? 90 GLY A O 1 ATOM 692 N N . LEU A 1 91 ? 30.105 22.844 18.811 1.00 16.49 ? 91 LEU A N 1 ATOM 693 C CA . LEU A 1 91 ? 29.249 23.995 18.669 1.00 17.70 ? 91 LEU A CA 1 ATOM 694 C C . LEU A 1 91 ? 28.068 23.640 17.773 1.00 17.15 ? 91 LEU A C 1 ATOM 695 O O . LEU A 1 91 ? 28.033 22.572 17.155 1.00 15.81 ? 91 LEU A O 1 ATOM 696 C CB . LEU A 1 91 ? 30.018 25.202 18.033 1.00 14.22 ? 91 LEU A CB 1 ATOM 697 C CG . LEU A 1 91 ? 30.394 25.086 16.561 1.00 18.66 ? 91 LEU A CG 1 ATOM 698 C CD1 . LEU A 1 91 ? 30.037 26.360 15.867 1.00 19.79 ? 91 LEU A CD1 1 ATOM 699 C CD2 . LEU A 1 91 ? 31.834 24.643 16.438 1.00 17.00 ? 91 LEU A CD2 1 ATOM 700 N N . ALA A 1 92 ? 27.078 24.514 17.700 1.00 17.98 ? 92 ALA A N 1 ATOM 701 C CA . ALA A 1 92 ? 25.941 24.283 16.839 1.00 18.73 ? 92 ALA A CA 1 ATOM 702 C C . ALA A 1 92 ? 25.250 25.560 16.467 1.00 16.05 ? 92 ALA A C 1 ATOM 703 O O . ALA A 1 92 ? 25.282 26.570 17.160 1.00 16.82 ? 92 ALA A O 1 ATOM 704 C CB . ALA A 1 92 ? 24.836 23.404 17.480 1.00 17.26 ? 92 ALA A CB 1 ATOM 705 N N . PHE A 1 93 ? 24.751 25.499 15.255 1.00 15.22 ? 93 PHE A N 1 ATOM 706 C CA . PHE A 1 93 ? 23.943 26.596 14.746 1.00 16.43 ? 93 PHE A CA 1 ATOM 707 C C . PHE A 1 93 ? 22.513 26.096 15.043 1.00 15.70 ? 93 PHE A C 1 ATOM 708 O O . PHE A 1 93 ? 22.199 24.936 14.729 1.00 16.23 ? 93 PHE A O 1 ATOM 709 C CB . PHE A 1 93 ? 24.112 26.794 13.227 1.00 14.94 ? 93 PHE A CB 1 ATOM 710 C CG . PHE A 1 93 ? 23.083 27.790 12.688 1.00 13.91 ? 93 PHE A CG 1 ATOM 711 C CD1 . PHE A 1 93 ? 23.280 29.135 12.876 1.00 15.00 ? 93 PHE A CD1 1 ATOM 712 C CD2 . PHE A 1 93 ? 21.935 27.339 12.090 1.00 13.80 ? 93 PHE A CD2 1 ATOM 713 C CE1 . PHE A 1 93 ? 22.330 30.041 12.483 1.00 16.26 ? 93 PHE A CE1 1 ATOM 714 C CE2 . PHE A 1 93 ? 20.983 28.257 11.696 1.00 18.04 ? 93 PHE A CE2 1 ATOM 715 C CZ . PHE A 1 93 ? 21.173 29.603 11.894 1.00 16.78 ? 93 PHE A CZ 1 ATOM 716 N N . PHE A 1 94 ? 21.583 26.875 15.570 1.00 13.92 ? 94 PHE A N 1 ATOM 717 C CA . PHE A 1 94 ? 20.259 26.319 15.852 1.00 13.48 ? 94 PHE A CA 1 ATOM 718 C C . PHE A 1 94 ? 19.100 27.249 15.584 1.00 13.90 ? 94 PHE A C 1 ATOM 719 O O . PHE A 1 94 ? 19.236 28.463 15.393 1.00 15.60 ? 94 PHE A O 1 ATOM 720 C CB . PHE A 1 94 ? 20.192 25.873 17.345 1.00 14.23 ? 94 PHE A CB 1 ATOM 721 C CG . PHE A 1 94 ? 20.177 27.053 18.333 1.00 17.40 ? 94 PHE A CG 1 ATOM 722 C CD1 . PHE A 1 94 ? 21.358 27.611 18.781 1.00 16.70 ? 94 PHE A CD1 1 ATOM 723 C CD2 . PHE A 1 94 ? 18.973 27.643 18.710 1.00 20.21 ? 94 PHE A CD2 1 ATOM 724 C CE1 . PHE A 1 94 ? 21.318 28.745 19.572 1.00 16.66 ? 94 PHE A CE1 1 ATOM 725 C CE2 . PHE A 1 94 ? 18.948 28.778 19.500 1.00 21.65 ? 94 PHE A CE2 1 ATOM 726 C CZ . PHE A 1 94 ? 20.130 29.340 19.934 1.00 18.99 ? 94 PHE A CZ 1 ATOM 727 N N . LEU A 1 95 ? 17.936 26.633 15.634 1.00 15.42 ? 95 LEU A N 1 ATOM 728 C CA . LEU A 1 95 ? 16.659 27.306 15.494 1.00 16.36 ? 95 LEU A CA 1 ATOM 729 C C . LEU A 1 95 ? 15.818 26.673 16.596 1.00 15.51 ? 95 LEU A C 1 ATOM 730 O O . LEU A 1 95 ? 15.631 25.466 16.722 1.00 17.84 ? 95 LEU A O 1 ATOM 731 C CB . LEU A 1 95 ? 15.980 27.065 14.140 1.00 16.70 ? 95 LEU A CB 1 ATOM 732 C CG . LEU A 1 95 ? 16.682 27.560 12.886 1.00 19.24 ? 95 LEU A CG 1 ATOM 733 C CD1 . LEU A 1 95 ? 17.330 26.347 12.272 1.00 20.11 ? 95 LEU A CD1 1 ATOM 734 C CD2 . LEU A 1 95 ? 15.736 28.187 11.890 1.00 18.20 ? 95 LEU A CD2 1 ATOM 735 N N . ALA A 1 96 ? 15.355 27.527 17.470 1.00 18.60 ? 96 ALA A N 1 ATOM 736 C CA . ALA A 1 96 ? 14.558 27.105 18.607 1.00 19.56 ? 96 ALA A CA 1 ATOM 737 C C . ALA A 1 96 ? 13.407 28.072 18.935 1.00 22.52 ? 96 ALA A C 1 ATOM 738 O O . ALA A 1 96 ? 13.364 29.154 18.324 1.00 20.33 ? 96 ALA A O 1 ATOM 739 C CB . ALA A 1 96 ? 15.509 26.982 19.784 1.00 16.87 ? 96 ALA A CB 1 ATOM 740 N N . PRO A 1 97 ? 12.442 27.821 19.864 1.00 24.47 ? 97 PRO A N 1 ATOM 741 C CA . PRO A 1 97 ? 11.409 28.796 20.235 1.00 23.63 ? 97 PRO A CA 1 ATOM 742 C C . PRO A 1 97 ? 11.993 30.116 20.755 1.00 24.09 ? 97 PRO A C 1 ATOM 743 O O . PRO A 1 97 ? 13.031 30.115 21.434 1.00 22.69 ? 97 PRO A O 1 ATOM 744 C CB . PRO A 1 97 ? 10.596 28.048 21.245 1.00 24.95 ? 97 PRO A CB 1 ATOM 745 C CG . PRO A 1 97 ? 10.793 26.580 20.880 1.00 24.11 ? 97 PRO A CG 1 ATOM 746 C CD . PRO A 1 97 ? 12.268 26.567 20.613 1.00 24.02 ? 97 PRO A CD 1 ATOM 747 N N . VAL A 1 98 ? 11.342 31.245 20.489 1.00 24.86 ? 98 VAL A N 1 ATOM 748 C CA . VAL A 1 98 ? 11.806 32.584 20.908 1.00 30.02 ? 98 VAL A CA 1 ATOM 749 C C . VAL A 1 98 ? 12.150 32.807 22.406 1.00 32.60 ? 98 VAL A C 1 ATOM 750 O O . VAL A 1 98 ? 13.024 33.564 22.833 1.00 34.54 ? 98 VAL A O 1 ATOM 751 C CB . VAL A 1 98 ? 10.716 33.577 20.437 1.00 32.81 ? 98 VAL A CB 1 ATOM 752 C CG1 . VAL A 1 98 ? 11.150 35.000 20.771 1.00 36.31 ? 98 VAL A CG1 1 ATOM 753 C CG2 . VAL A 1 98 ? 10.513 33.491 18.931 1.00 30.08 ? 98 VAL A CG2 1 ATOM 754 N N . ASP A 1 99 ? 11.367 32.092 23.194 1.00 34.42 ? 99 ASP A N 1 ATOM 755 C CA . ASP A 1 99 ? 11.406 32.016 24.655 1.00 36.05 ? 99 ASP A CA 1 ATOM 756 C C . ASP A 1 99 ? 12.406 30.985 25.242 1.00 33.75 ? 99 ASP A C 1 ATOM 757 O O . ASP A 1 99 ? 12.596 30.885 26.456 1.00 35.11 ? 99 ASP A O 1 ATOM 758 C CB . ASP A 1 99 ? 9.959 31.698 25.143 1.00 40.28 ? 99 ASP A CB 1 ATOM 759 C CG . ASP A 1 99 ? 9.388 30.392 24.549 1.00 47.75 ? 99 ASP A CG 1 ATOM 760 O OD1 . ASP A 1 99 ? 9.642 29.300 25.077 1.00 52.12 ? 99 ASP A OD1 1 ATOM 761 O OD2 . ASP A 1 99 ? 8.700 30.458 23.521 1.00 52.61 ? 99 ASP A OD2 1 ATOM 762 N N . SER A 1 100 ? 13.070 30.146 24.450 1.00 30.30 ? 100 SER A N 1 ATOM 763 C CA . SER A 1 100 ? 13.991 29.162 25.022 1.00 27.87 ? 100 SER A CA 1 ATOM 764 C C . SER A 1 100 ? 15.285 29.793 25.509 1.00 27.35 ? 100 SER A C 1 ATOM 765 O O . SER A 1 100 ? 15.623 30.947 25.215 1.00 25.58 ? 100 SER A O 1 ATOM 766 C CB . SER A 1 100 ? 14.341 28.067 24.004 1.00 25.37 ? 100 SER A CB 1 ATOM 767 O OG . SER A 1 100 ? 14.963 28.610 22.854 1.00 26.92 ? 100 SER A OG 1 ATOM 768 N N . SER A 1 101 ? 16.005 29.058 26.332 1.00 25.15 ? 101 SER A N 1 ATOM 769 C CA . SER A 1 101 ? 17.253 29.539 26.869 1.00 25.84 ? 101 SER A CA 1 ATOM 770 C C . SER A 1 101 ? 18.331 28.478 26.816 1.00 25.59 ? 101 SER A C 1 ATOM 771 O O . SER A 1 101 ? 18.062 27.326 26.440 1.00 24.13 ? 101 SER A O 1 ATOM 772 C CB . SER A 1 101 ? 17.085 29.971 28.329 1.00 29.91 ? 101 SER A CB 1 ATOM 773 O OG . SER A 1 101 ? 18.303 30.474 28.901 1.00 34.71 ? 101 SER A OG 1 ATOM 774 N N . VAL A 1 102 ? 19.557 28.832 27.228 1.00 25.80 ? 102 VAL A N 1 ATOM 775 C CA . VAL A 1 102 ? 20.659 27.865 27.214 1.00 24.86 ? 102 VAL A CA 1 ATOM 776 C C . VAL A 1 102 ? 20.418 26.732 28.202 1.00 24.57 ? 102 VAL A C 1 ATOM 777 O O . VAL A 1 102 ? 19.886 26.891 29.300 1.00 29.15 ? 102 VAL A O 1 ATOM 778 C CB . VAL A 1 102 ? 22.003 28.622 27.484 1.00 24.21 ? 102 VAL A CB 1 ATOM 779 C CG1 . VAL A 1 102 ? 21.985 29.333 28.820 1.00 24.58 ? 102 VAL A CG1 1 ATOM 780 C CG2 . VAL A 1 102 ? 23.133 27.629 27.420 1.00 19.16 ? 102 VAL A CG2 1 ATOM 781 N N . LYS A 1 103 ? 20.712 25.537 27.766 1.00 23.46 ? 103 LYS A N 1 ATOM 782 C CA . LYS A 1 103 ? 20.505 24.384 28.593 1.00 20.42 ? 103 LYS A CA 1 ATOM 783 C C . LYS A 1 103 ? 21.757 23.692 29.052 1.00 21.40 ? 103 LYS A C 1 ATOM 784 O O . LYS A 1 103 ? 22.715 24.395 29.370 1.00 24.18 ? 103 LYS A O 1 ATOM 785 C CB . LYS A 1 103 ? 19.603 23.417 27.858 1.00 20.64 ? 103 LYS A CB 1 ATOM 786 C CG . LYS A 1 103 ? 18.335 24.137 27.499 1.00 21.03 ? 103 LYS A CG 1 ATOM 787 C CD . LYS A 1 103 ? 17.403 23.140 26.926 1.00 26.14 ? 103 LYS A CD 1 ATOM 788 C CE . LYS A 1 103 ? 16.125 23.917 26.747 1.00 29.95 ? 103 LYS A CE 1 ATOM 789 N NZ . LYS A 1 103 ? 15.101 23.020 26.268 1.00 38.37 ? 103 LYS A NZ 1 ATOM 790 N N . ASP A 1 104 ? 21.904 22.372 29.063 1.00 22.82 ? 104 ASP A N 1 ATOM 791 C CA . ASP A 1 104 ? 23.122 21.799 29.599 1.00 24.45 ? 104 ASP A CA 1 ATOM 792 C C . ASP A 1 104 ? 24.407 21.857 28.835 1.00 26.34 ? 104 ASP A C 1 ATOM 793 O O . ASP A 1 104 ? 24.446 21.891 27.602 1.00 27.06 ? 104 ASP A O 1 ATOM 794 C CB . ASP A 1 104 ? 22.871 20.332 29.963 1.00 27.63 ? 104 ASP A CB 1 ATOM 795 C CG . ASP A 1 104 ? 21.920 20.127 31.157 1.00 30.63 ? 104 ASP A CG 1 ATOM 796 O OD1 . ASP A 1 104 ? 21.651 21.091 31.893 1.00 30.72 ? 104 ASP A OD1 1 ATOM 797 O OD2 . ASP A 1 104 ? 21.445 19.001 31.340 1.00 29.49 ? 104 ASP A OD2 1 ATOM 798 N N . TYR A 1 105 ? 25.493 21.863 29.585 1.00 25.37 ? 105 TYR A N 1 ATOM 799 C CA . TYR A 1 105 ? 26.775 21.893 28.916 1.00 25.01 ? 105 TYR A CA 1 ATOM 800 C C . TYR A 1 105 ? 27.262 20.513 28.504 1.00 23.14 ? 105 TYR A C 1 ATOM 801 O O . TYR A 1 105 ? 26.505 19.533 28.516 1.00 21.26 ? 105 TYR A O 1 ATOM 802 C CB . TYR A 1 105 ? 27.774 22.583 29.807 1.00 28.01 ? 105 TYR A CB 1 ATOM 803 C CG . TYR A 1 105 ? 27.850 22.104 31.238 1.00 32.41 ? 105 TYR A CG 1 ATOM 804 C CD1 . TYR A 1 105 ? 28.233 20.809 31.499 1.00 34.39 ? 105 TYR A CD1 1 ATOM 805 C CD2 . TYR A 1 105 ? 27.591 22.997 32.253 1.00 35.38 ? 105 TYR A CD2 1 ATOM 806 C CE1 . TYR A 1 105 ? 28.372 20.388 32.789 1.00 40.37 ? 105 TYR A CE1 1 ATOM 807 C CE2 . TYR A 1 105 ? 27.735 22.584 33.561 1.00 40.39 ? 105 TYR A CE2 1 ATOM 808 C CZ . TYR A 1 105 ? 28.130 21.281 33.811 1.00 42.44 ? 105 TYR A CZ 1 ATOM 809 O OH . TYR A 1 105 ? 28.326 20.840 35.107 1.00 47.20 ? 105 TYR A OH 1 ATOM 810 N N . GLY A 1 106 ? 28.549 20.370 28.196 1.00 22.19 ? 106 GLY A N 1 ATOM 811 C CA . GLY A 1 106 ? 29.043 19.087 27.739 1.00 21.16 ? 106 GLY A CA 1 ATOM 812 C C . GLY A 1 106 ? 28.458 18.731 26.369 1.00 20.87 ? 106 GLY A C 1 ATOM 813 O O . GLY A 1 106 ? 28.112 19.617 25.583 1.00 20.69 ? 106 GLY A O 1 ATOM 814 N N . GLY A 1 107 ? 28.301 17.449 26.069 1.00 19.59 ? 107 GLY A N 1 ATOM 815 C CA . GLY A 1 107 ? 27.765 16.956 24.796 1.00 19.15 ? 107 GLY A CA 1 ATOM 816 C C . GLY A 1 107 ? 26.357 17.431 24.394 1.00 19.24 ? 107 GLY A C 1 ATOM 817 O O . GLY A 1 107 ? 25.910 17.207 23.276 1.00 21.55 ? 107 GLY A O 1 ATOM 818 N N . PHE A 1 108 ? 25.609 18.077 25.277 1.00 19.34 ? 108 PHE A N 1 ATOM 819 C CA . PHE A 1 108 ? 24.292 18.597 24.942 1.00 22.16 ? 108 PHE A CA 1 ATOM 820 C C . PHE A 1 108 ? 24.357 19.934 24.192 1.00 22.15 ? 108 PHE A C 1 ATOM 821 O O . PHE A 1 108 ? 23.348 20.528 23.762 1.00 20.81 ? 108 PHE A O 1 ATOM 822 C CB . PHE A 1 108 ? 23.468 18.779 26.204 1.00 25.41 ? 108 PHE A CB 1 ATOM 823 C CG . PHE A 1 108 ? 23.306 17.427 26.827 1.00 27.00 ? 108 PHE A CG 1 ATOM 824 C CD1 . PHE A 1 108 ? 22.658 16.440 26.128 1.00 29.63 ? 108 PHE A CD1 1 ATOM 825 C CD2 . PHE A 1 108 ? 23.915 17.191 28.036 1.00 31.75 ? 108 PHE A CD2 1 ATOM 826 C CE1 . PHE A 1 108 ? 22.643 15.180 26.649 1.00 31.78 ? 108 PHE A CE1 1 ATOM 827 C CE2 . PHE A 1 108 ? 23.894 15.921 28.556 1.00 31.99 ? 108 PHE A CE2 1 ATOM 828 C CZ . PHE A 1 108 ? 23.258 14.923 27.855 1.00 35.29 ? 108 PHE A CZ 1 ATOM 829 N N . LEU A 1 109 ? 25.594 20.458 24.117 1.00 19.92 ? 109 LEU A N 1 ATOM 830 C CA . LEU A 1 109 ? 25.873 21.694 23.391 1.00 19.20 ? 109 LEU A CA 1 ATOM 831 C C . LEU A 1 109 ? 25.049 22.948 23.718 1.00 19.47 ? 109 LEU A C 1 ATOM 832 O O . LEU A 1 109 ? 24.820 23.838 22.897 1.00 19.10 ? 109 LEU A O 1 ATOM 833 C CB . LEU A 1 109 ? 25.735 21.311 21.945 1.00 16.18 ? 109 LEU A CB 1 ATOM 834 C CG . LEU A 1 109 ? 26.569 20.200 21.454 1.00 16.20 ? 109 LEU A CG 1 ATOM 835 C CD1 . LEU A 1 109 ? 26.174 19.976 20.011 1.00 16.81 ? 109 LEU A CD1 1 ATOM 836 C CD2 . LEU A 1 109 ? 28.033 20.546 21.604 1.00 14.80 ? 109 LEU A CD2 1 ATOM 837 N N . GLY A 1 110 ? 24.580 23.023 24.968 1.00 18.79 ? 110 GLY A N 1 ATOM 838 C CA . GLY A 1 110 ? 23.758 24.115 25.479 1.00 17.66 ? 110 GLY A CA 1 ATOM 839 C C . GLY A 1 110 ? 22.332 24.048 24.930 1.00 17.79 ? 110 GLY A C 1 ATOM 840 O O . GLY A 1 110 ? 21.467 24.904 25.153 1.00 17.20 ? 110 GLY A O 1 ATOM 841 N N . LEU A 1 111 ? 22.034 22.957 24.237 1.00 18.15 ? 111 LEU A N 1 ATOM 842 C CA . LEU A 1 111 ? 20.728 22.857 23.612 1.00 20.00 ? 111 LEU A CA 1 ATOM 843 C C . LEU A 1 111 ? 19.674 21.966 24.210 1.00 20.31 ? 111 LEU A C 1 ATOM 844 O O . LEU A 1 111 ? 18.475 22.117 23.981 1.00 21.19 ? 111 LEU A O 1 ATOM 845 C CB . LEU A 1 111 ? 20.950 22.454 22.154 1.00 19.18 ? 111 LEU A CB 1 ATOM 846 C CG . LEU A 1 111 ? 21.656 23.408 21.191 1.00 19.25 ? 111 LEU A CG 1 ATOM 847 C CD1 . LEU A 1 111 ? 21.784 22.728 19.856 1.00 19.56 ? 111 LEU A CD1 1 ATOM 848 C CD2 . LEU A 1 111 ? 20.867 24.685 21.035 1.00 18.33 ? 111 LEU A CD2 1 ATOM 849 N N . PHE A 1 112 ? 20.154 21.016 24.986 1.00 21.91 ? 112 PHE A N 1 ATOM 850 C CA . PHE A 1 112 ? 19.296 20.038 25.631 1.00 25.23 ? 112 PHE A CA 1 ATOM 851 C C . PHE A 1 112 ? 19.612 19.873 27.111 1.00 27.40 ? 112 PHE A C 1 ATOM 852 O O . PHE A 1 112 ? 20.684 20.206 27.604 1.00 24.41 ? 112 PHE A O 1 ATOM 853 C CB . PHE A 1 112 ? 19.455 18.642 24.966 1.00 22.73 ? 112 PHE A CB 1 ATOM 854 C CG . PHE A 1 112 ? 19.317 18.603 23.442 1.00 23.38 ? 112 PHE A CG 1 ATOM 855 C CD1 . PHE A 1 112 ? 18.065 18.432 22.866 1.00 24.00 ? 112 PHE A CD1 1 ATOM 856 C CD2 . PHE A 1 112 ? 20.429 18.802 22.644 1.00 20.34 ? 112 PHE A CD2 1 ATOM 857 C CE1 . PHE A 1 112 ? 17.941 18.476 21.495 1.00 25.10 ? 112 PHE A CE1 1 ATOM 858 C CE2 . PHE A 1 112 ? 20.293 18.846 21.275 1.00 21.12 ? 112 PHE A CE2 1 ATOM 859 C CZ . PHE A 1 112 ? 19.057 18.686 20.696 1.00 24.28 ? 112 PHE A CZ 1 ATOM 860 N N . ARG A 1 113 ? 18.606 19.389 27.811 1.00 30.71 ? 113 ARG A N 1 ATOM 861 C CA . ARG A 1 113 ? 18.686 19.073 29.227 1.00 33.16 ? 113 ARG A CA 1 ATOM 862 C C . ARG A 1 113 ? 18.962 17.543 29.287 1.00 33.78 ? 113 ARG A C 1 ATOM 863 O O . ARG A 1 113 ? 18.320 16.702 28.650 1.00 31.18 ? 113 ARG A O 1 ATOM 864 C CB . ARG A 1 113 ? 17.362 19.378 29.930 1.00 35.87 ? 113 ARG A CB 1 ATOM 865 C CG . ARG A 1 113 ? 16.664 20.721 29.636 1.00 41.01 ? 113 ARG A CG 1 ATOM 866 C CD . ARG A 1 113 ? 16.666 21.776 30.724 1.00 41.09 ? 113 ARG A CD 1 ATOM 867 N NE . ARG A 1 113 ? 18.024 22.121 31.109 1.00 43.92 ? 113 ARG A NE 1 ATOM 868 C CZ . ARG A 1 113 ? 18.371 23.363 31.473 1.00 42.74 ? 113 ARG A CZ 1 ATOM 869 N NH1 . ARG A 1 113 ? 17.506 24.380 31.500 1.00 42.74 ? 113 ARG A NH1 1 ATOM 870 N NH2 . ARG A 1 113 ? 19.627 23.583 31.841 1.00 42.78 ? 113 ARG A NH2 1 ATOM 871 N N . HIS A 1 114 ? 20.010 17.089 29.947 1.00 35.32 ? 114 HIS A N 1 ATOM 872 C CA . HIS A 1 114 ? 20.347 15.679 30.086 1.00 38.88 ? 114 HIS A CA 1 ATOM 873 C C . HIS A 1 114 ? 19.217 14.628 30.154 1.00 37.94 ? 114 HIS A C 1 ATOM 874 O O . HIS A 1 114 ? 19.229 13.598 29.482 1.00 33.83 ? 114 HIS A O 1 ATOM 875 C CB . HIS A 1 114 ? 21.237 15.629 31.316 1.00 48.02 ? 114 HIS A CB 1 ATOM 876 C CG . HIS A 1 114 ? 21.751 14.237 31.639 1.00 59.31 ? 114 HIS A CG 1 ATOM 877 N ND1 . HIS A 1 114 ? 22.690 13.492 31.027 1.00 64.06 ? 114 HIS A ND1 1 ATOM 878 C CD2 . HIS A 1 114 ? 21.227 13.479 32.670 1.00 63.51 ? 114 HIS A CD2 1 ATOM 879 C CE1 . HIS A 1 114 ? 22.744 12.325 31.629 1.00 65.51 ? 114 HIS A CE1 1 ATOM 880 N NE2 . HIS A 1 114 ? 21.864 12.332 32.610 1.00 67.40 ? 114 HIS A NE2 1 ATOM 881 N N . GLU A 1 115 ? 18.191 14.958 30.940 1.00 38.56 ? 115 GLU A N 1 ATOM 882 C CA . GLU A 1 115 ? 17.023 14.090 31.170 1.00 40.79 ? 115 GLU A CA 1 ATOM 883 C C . GLU A 1 115 ? 16.113 13.825 29.992 1.00 38.11 ? 115 GLU A C 1 ATOM 884 O O . GLU A 1 115 ? 15.474 12.786 29.889 1.00 39.66 ? 115 GLU A O 1 ATOM 885 C CB . GLU A 1 115 ? 16.031 14.609 32.212 1.00 44.02 ? 115 GLU A CB 1 ATOM 886 C CG . GLU A 1 115 ? 16.551 15.039 33.572 1.00 56.51 ? 115 GLU A CG 1 ATOM 887 C CD . GLU A 1 115 ? 17.392 16.317 33.526 1.00 61.85 ? 115 GLU A CD 1 ATOM 888 O OE1 . GLU A 1 115 ? 16.907 17.326 33.002 1.00 63.97 ? 115 GLU A OE1 1 ATOM 889 O OE2 . GLU A 1 115 ? 18.539 16.284 33.995 1.00 68.27 ? 115 GLU A OE2 1 ATOM 890 N N . THR A 1 116 ? 16.004 14.812 29.113 1.00 35.79 ? 116 THR A N 1 ATOM 891 C CA . THR A 1 116 ? 15.115 14.675 27.957 1.00 33.01 ? 116 THR A CA 1 ATOM 892 C C . THR A 1 116 ? 15.745 14.751 26.576 1.00 31.71 ? 116 THR A C 1 ATOM 893 O O . THR A 1 116 ? 15.054 14.757 25.556 1.00 31.52 ? 116 THR A O 1 ATOM 894 C CB . THR A 1 116 ? 14.013 15.729 28.007 1.00 30.92 ? 116 THR A CB 1 ATOM 895 O OG1 . THR A 1 116 ? 14.613 16.985 28.262 1.00 32.35 ? 116 THR A OG1 1 ATOM 896 C CG2 . THR A 1 116 ? 12.990 15.392 29.069 1.00 32.44 ? 116 THR A CG2 1 ATOM 897 N N . ALA A 1 117 ? 17.078 14.678 26.539 1.00 31.45 ? 117 ALA A N 1 ATOM 898 C CA . ALA A 1 117 ? 17.862 14.764 25.315 1.00 29.51 ? 117 ALA A CA 1 ATOM 899 C C . ALA A 1 117 ? 17.615 13.753 24.181 1.00 28.19 ? 117 ALA A C 1 ATOM 900 O O . ALA A 1 117 ? 17.778 14.091 23.007 1.00 27.70 ? 117 ALA A O 1 ATOM 901 C CB . ALA A 1 117 ? 19.340 14.733 25.727 1.00 28.32 ? 117 ALA A CB 1 ATOM 902 N N . ALA A 1 118 ? 17.212 12.525 24.492 1.00 24.29 ? 118 ALA A N 1 ATOM 903 C CA . ALA A 1 118 ? 16.945 11.491 23.507 1.00 21.89 ? 118 ALA A CA 1 ATOM 904 C C . ALA A 1 118 ? 15.449 11.276 23.293 1.00 21.61 ? 118 ALA A C 1 ATOM 905 O O . ALA A 1 118 ? 14.969 10.262 22.778 1.00 23.28 ? 118 ALA A O 1 ATOM 906 C CB . ALA A 1 118 ? 17.530 10.191 23.970 1.00 22.24 ? 118 ALA A CB 1 ATOM 907 N N . ASP A 1 119 ? 14.676 12.234 23.784 1.00 21.63 ? 119 ASP A N 1 ATOM 908 C CA . ASP A 1 119 ? 13.234 12.204 23.648 1.00 23.60 ? 119 ASP A CA 1 ATOM 909 C C . ASP A 1 119 ? 12.720 13.320 22.732 1.00 23.11 ? 119 ASP A C 1 ATOM 910 O O . ASP A 1 119 ? 12.490 14.465 23.154 1.00 23.58 ? 119 ASP A O 1 ATOM 911 C CB . ASP A 1 119 ? 12.562 12.317 25.051 1.00 23.25 ? 119 ASP A CB 1 ATOM 912 C CG . ASP A 1 119 ? 11.041 12.003 25.075 1.00 28.74 ? 119 ASP A CG 1 ATOM 913 O OD1 . ASP A 1 119 ? 10.344 12.101 24.067 1.00 26.77 ? 119 ASP A OD1 1 ATOM 914 O OD2 . ASP A 1 119 ? 10.528 11.690 26.144 1.00 35.30 ? 119 ASP A OD2 1 ATOM 915 N N . PRO A 1 120 ? 12.419 13.028 21.469 1.00 23.83 ? 120 PRO A N 1 ATOM 916 C CA . PRO A 1 120 ? 11.895 14.022 20.539 1.00 26.14 ? 120 PRO A CA 1 ATOM 917 C C . PRO A 1 120 ? 10.619 14.766 20.986 1.00 26.00 ? 120 PRO A C 1 ATOM 918 O O . PRO A 1 120 ? 10.420 15.964 20.749 1.00 26.94 ? 120 PRO A O 1 ATOM 919 C CB . PRO A 1 120 ? 11.699 13.230 19.250 1.00 25.97 ? 120 PRO A CB 1 ATOM 920 C CG . PRO A 1 120 ? 12.688 12.112 19.330 1.00 26.57 ? 120 PRO A CG 1 ATOM 921 C CD . PRO A 1 120 ? 12.623 11.744 20.818 1.00 25.23 ? 120 PRO A CD 1 ATOM 922 N N . SER A 1 121 ? 9.745 14.095 21.757 1.00 26.75 ? 121 SER A N 1 ATOM 923 C CA . SER A 1 121 ? 8.490 14.751 22.182 1.00 25.31 ? 121 SER A CA 1 ATOM 924 C C . SER A 1 121 ? 8.635 15.865 23.171 1.00 24.07 ? 121 SER A C 1 ATOM 925 O O . SER A 1 121 ? 7.754 16.712 23.265 1.00 25.31 ? 121 SER A O 1 ATOM 926 C CB . SER A 1 121 ? 7.484 13.767 22.805 1.00 23.96 ? 121 SER A CB 1 ATOM 927 O OG . SER A 1 121 ? 8.037 13.191 23.962 1.00 24.83 ? 121 SER A OG 1 ATOM 928 N N . LYS A 1 122 ? 9.784 15.872 23.840 1.00 23.27 ? 122 LYS A N 1 ATOM 929 C CA . LYS A 1 122 ? 10.076 16.883 24.854 1.00 26.16 ? 122 LYS A CA 1 ATOM 930 C C . LYS A 1 122 ? 10.975 18.023 24.380 1.00 27.09 ? 122 LYS A C 1 ATOM 931 O O . LYS A 1 122 ? 11.395 18.856 25.179 1.00 26.62 ? 122 LYS A O 1 ATOM 932 C CB . LYS A 1 122 ? 10.770 16.272 26.080 1.00 30.95 ? 122 LYS A CB 1 ATOM 933 C CG . LYS A 1 122 ? 10.093 15.094 26.778 1.00 38.67 ? 122 LYS A CG 1 ATOM 934 C CD . LYS A 1 122 ? 8.906 15.586 27.553 1.00 48.43 ? 122 LYS A CD 1 ATOM 935 C CE . LYS A 1 122 ? 8.516 14.578 28.636 1.00 55.56 ? 122 LYS A CE 1 ATOM 936 N NZ . LYS A 1 122 ? 7.829 15.288 29.714 1.00 60.15 ? 122 LYS A NZ 1 ATOM 937 N N . ASN A 1 123 ? 11.374 18.053 23.105 1.00 25.37 ? 123 ASN A N 1 ATOM 938 C CA . ASN A 1 123 ? 12.205 19.132 22.593 1.00 24.42 ? 123 ASN A CA 1 ATOM 939 C C . ASN A 1 123 ? 11.669 19.722 21.304 1.00 25.09 ? 123 ASN A C 1 ATOM 940 O O . ASN A 1 123 ? 10.900 19.090 20.589 1.00 24.33 ? 123 ASN A O 1 ATOM 941 C CB . ASN A 1 123 ? 13.604 18.691 22.268 1.00 20.67 ? 123 ASN A CB 1 ATOM 942 C CG . ASN A 1 123 ? 14.250 18.101 23.462 1.00 18.94 ? 123 ASN A CG 1 ATOM 943 O OD1 . ASN A 1 123 ? 14.624 18.834 24.351 1.00 21.06 ? 123 ASN A OD1 1 ATOM 944 N ND2 . ASN A 1 123 ? 14.383 16.805 23.611 1.00 19.02 ? 123 ASN A ND2 1 ATOM 945 N N . GLN A 1 124 ? 11.914 21.014 21.135 1.00 26.31 ? 124 GLN A N 1 ATOM 946 C CA . GLN A 1 124 ? 11.562 21.745 19.909 1.00 28.08 ? 124 GLN A CA 1 ATOM 947 C C . GLN A 1 124 ? 12.800 22.509 19.463 1.00 25.82 ? 124 GLN A C 1 ATOM 948 O O . GLN A 1 124 ? 13.020 23.663 19.830 1.00 27.55 ? 124 GLN A O 1 ATOM 949 C CB . GLN A 1 124 ? 10.470 22.764 20.115 1.00 31.81 ? 124 GLN A CB 1 ATOM 950 C CG . GLN A 1 124 ? 9.168 22.093 20.441 1.00 41.38 ? 124 GLN A CG 1 ATOM 951 C CD . GLN A 1 124 ? 8.094 23.141 20.392 1.00 46.38 ? 124 GLN A CD 1 ATOM 952 O OE1 . GLN A 1 124 ? 8.077 24.140 21.122 1.00 48.82 ? 124 GLN A OE1 1 ATOM 953 N NE2 . GLN A 1 124 ? 7.187 22.894 19.464 1.00 49.20 ? 124 GLN A NE2 1 ATOM 954 N N . VAL A 1 125 ? 13.656 21.833 18.718 1.00 21.91 ? 125 VAL A N 1 ATOM 955 C CA . VAL A 1 125 ? 14.895 22.425 18.234 1.00 22.19 ? 125 VAL A CA 1 ATOM 956 C C . VAL A 1 125 ? 15.477 21.641 17.069 1.00 20.54 ? 125 VAL A C 1 ATOM 957 O O . VAL A 1 125 ? 15.350 20.418 16.979 1.00 19.90 ? 125 VAL A O 1 ATOM 958 C CB . VAL A 1 125 ? 15.956 22.514 19.411 1.00 21.86 ? 125 VAL A CB 1 ATOM 959 C CG1 . VAL A 1 125 ? 16.171 21.127 19.980 1.00 24.01 ? 125 VAL A CG1 1 ATOM 960 C CG2 . VAL A 1 125 ? 17.317 23.030 18.944 1.00 21.37 ? 125 VAL A CG2 1 ATOM 961 N N . VAL A 1 126 ? 15.983 22.423 16.105 1.00 20.27 ? 126 VAL A N 1 ATOM 962 C CA . VAL A 1 126 ? 16.666 21.908 14.926 1.00 17.60 ? 126 VAL A CA 1 ATOM 963 C C . VAL A 1 126 ? 18.006 22.632 14.975 1.00 16.34 ? 126 VAL A C 1 ATOM 964 O O . VAL A 1 126 ? 18.148 23.841 15.183 1.00 14.97 ? 126 VAL A O 1 ATOM 965 C CB . VAL A 1 126 ? 15.969 22.222 13.583 1.00 16.66 ? 126 VAL A CB 1 ATOM 966 C CG1 . VAL A 1 126 ? 16.775 21.749 12.393 1.00 17.44 ? 126 VAL A CG1 1 ATOM 967 C CG2 . VAL A 1 126 ? 14.706 21.377 13.497 1.00 20.84 ? 126 VAL A CG2 1 ATOM 968 N N . ALA A 1 127 ? 19.018 21.791 14.910 1.00 17.18 ? 127 ALA A N 1 ATOM 969 C CA . ALA A 1 127 ? 20.388 22.257 14.946 1.00 16.80 ? 127 ALA A CA 1 ATOM 970 C C . ALA A 1 127 ? 21.359 21.521 14.052 1.00 16.21 ? 127 ALA A C 1 ATOM 971 O O . ALA A 1 127 ? 21.186 20.335 13.735 1.00 16.89 ? 127 ALA A O 1 ATOM 972 C CB . ALA A 1 127 ? 20.980 22.153 16.353 1.00 13.66 ? 127 ALA A CB 1 ATOM 973 N N . VAL A 1 128 ? 22.357 22.275 13.594 1.00 14.38 ? 128 VAL A N 1 ATOM 974 C CA . VAL A 1 128 ? 23.408 21.681 12.815 1.00 14.19 ? 128 VAL A CA 1 ATOM 975 C C . VAL A 1 128 ? 24.582 21.690 13.794 1.00 14.06 ? 128 VAL A C 1 ATOM 976 O O . VAL A 1 128 ? 25.029 22.739 14.265 1.00 15.06 ? 128 VAL A O 1 ATOM 977 C CB . VAL A 1 128 ? 23.719 22.501 11.556 1.00 16.32 ? 128 VAL A CB 1 ATOM 978 C CG1 . VAL A 1 128 ? 25.000 21.960 10.900 1.00 14.61 ? 128 VAL A CG1 1 ATOM 979 C CG2 . VAL A 1 128 ? 22.526 22.408 10.600 1.00 12.39 ? 128 VAL A CG2 1 ATOM 980 N N . GLU A 1 129 ? 25.030 20.510 14.200 1.00 13.88 ? 129 GLU A N 1 ATOM 981 C CA . GLU A 1 129 ? 26.106 20.417 15.147 1.00 13.84 ? 129 GLU A CA 1 ATOM 982 C C . GLU A 1 129 ? 27.448 20.041 14.548 1.00 14.44 ? 129 GLU A C 1 ATOM 983 O O . GLU A 1 129 ? 27.562 19.329 13.570 1.00 14.53 ? 129 GLU A O 1 ATOM 984 C CB . GLU A 1 129 ? 25.752 19.407 16.232 1.00 14.23 ? 129 GLU A CB 1 ATOM 985 C CG . GLU A 1 129 ? 25.606 18.012 15.638 1.00 16.88 ? 129 GLU A CG 1 ATOM 986 C CD . GLU A 1 129 ? 25.589 16.872 16.645 1.00 20.56 ? 129 GLU A CD 1 ATOM 987 O OE1 . GLU A 1 129 ? 24.813 16.951 17.592 1.00 18.33 ? 129 GLU A OE1 1 ATOM 988 O OE2 . GLU A 1 129 ? 26.341 15.913 16.469 1.00 19.89 ? 129 GLU A OE2 1 ATOM 989 N N . PHE A 1 130 ? 28.490 20.605 15.105 1.00 15.49 ? 130 PHE A N 1 ATOM 990 C CA . PHE A 1 130 ? 29.865 20.375 14.716 1.00 14.36 ? 130 PHE A CA 1 ATOM 991 C C . PHE A 1 130 ? 30.415 19.776 16.016 1.00 15.18 ? 130 PHE A C 1 ATOM 992 O O . PHE A 1 130 ? 30.831 20.425 16.970 1.00 15.57 ? 130 PHE A O 1 ATOM 993 C CB . PHE A 1 130 ? 30.497 21.714 14.378 1.00 16.41 ? 130 PHE A CB 1 ATOM 994 C CG . PHE A 1 130 ? 29.842 22.420 13.200 1.00 16.90 ? 130 PHE A CG 1 ATOM 995 C CD1 . PHE A 1 130 ? 30.249 22.112 11.924 1.00 17.53 ? 130 PHE A CD1 1 ATOM 996 C CD2 . PHE A 1 130 ? 28.848 23.350 13.416 1.00 15.83 ? 130 PHE A CD2 1 ATOM 997 C CE1 . PHE A 1 130 ? 29.648 22.748 10.867 1.00 19.10 ? 130 PHE A CE1 1 ATOM 998 C CE2 . PHE A 1 130 ? 28.255 23.979 12.352 1.00 17.46 ? 130 PHE A CE2 1 ATOM 999 C CZ . PHE A 1 130 ? 28.654 23.679 11.079 1.00 15.72 ? 130 PHE A CZ 1 ATOM 1000 N N . ASP A 1 131 ? 30.300 18.465 16.057 1.00 16.29 ? 131 ASP A N 1 ATOM 1001 C CA . ASP A 1 131 ? 30.662 17.664 17.205 1.00 17.32 ? 131 ASP A CA 1 ATOM 1002 C C . ASP A 1 131 ? 32.092 17.172 17.333 1.00 17.40 ? 131 ASP A C 1 ATOM 1003 O O . ASP A 1 131 ? 32.549 16.347 16.553 1.00 16.59 ? 131 ASP A O 1 ATOM 1004 C CB . ASP A 1 131 ? 29.685 16.504 17.199 1.00 17.51 ? 131 ASP A CB 1 ATOM 1005 C CG . ASP A 1 131 ? 29.473 15.777 18.520 1.00 19.48 ? 131 ASP A CG 1 ATOM 1006 O OD1 . ASP A 1 131 ? 30.306 15.850 19.414 1.00 19.78 ? 131 ASP A OD1 1 ATOM 1007 O OD2 . ASP A 1 131 ? 28.447 15.116 18.659 1.00 18.64 ? 131 ASP A OD2 1 ATOM 1008 N N . THR A 1 132 ? 32.812 17.622 18.348 1.00 18.26 ? 132 THR A N 1 ATOM 1009 C CA . THR A 1 132 ? 34.212 17.214 18.565 1.00 19.54 ? 132 THR A CA 1 ATOM 1010 C C . THR A 1 132 ? 34.451 16.029 19.515 1.00 22.70 ? 132 THR A C 1 ATOM 1011 O O . THR A 1 132 ? 35.531 15.433 19.588 1.00 25.40 ? 132 THR A O 1 ATOM 1012 C CB . THR A 1 132 ? 35.034 18.404 19.111 1.00 20.62 ? 132 THR A CB 1 ATOM 1013 O OG1 . THR A 1 132 ? 34.396 18.962 20.288 1.00 19.17 ? 132 THR A OG1 1 ATOM 1014 C CG2 . THR A 1 132 ? 35.161 19.454 18.021 1.00 21.48 ? 132 THR A CG2 1 ATOM 1015 N N . TRP A 1 133 ? 33.409 15.599 20.224 1.00 23.31 ? 133 TRP A N 1 ATOM 1016 C CA . TRP A 1 133 ? 33.483 14.526 21.191 1.00 24.89 ? 133 TRP A CA 1 ATOM 1017 C C . TRP A 1 133 ? 32.553 13.355 20.998 1.00 24.71 ? 133 TRP A C 1 ATOM 1018 O O . TRP A 1 133 ? 31.321 13.450 20.937 1.00 24.55 ? 133 TRP A O 1 ATOM 1019 C CB . TRP A 1 133 ? 33.227 15.103 22.565 1.00 29.47 ? 133 TRP A CB 1 ATOM 1020 C CG . TRP A 1 133 ? 33.356 14.072 23.670 1.00 32.34 ? 133 TRP A CG 1 ATOM 1021 C CD1 . TRP A 1 133 ? 32.294 13.389 24.209 1.00 31.93 ? 133 TRP A CD1 1 ATOM 1022 C CD2 . TRP A 1 133 ? 34.553 13.733 24.206 1.00 35.74 ? 133 TRP A CD2 1 ATOM 1023 N NE1 . TRP A 1 133 ? 32.839 12.600 25.086 1.00 32.92 ? 133 TRP A NE1 1 ATOM 1024 C CE2 . TRP A 1 133 ? 34.175 12.769 25.126 1.00 37.91 ? 133 TRP A CE2 1 ATOM 1025 C CE3 . TRP A 1 133 ? 35.870 14.117 24.007 1.00 38.11 ? 133 TRP A CE3 1 ATOM 1026 C CZ2 . TRP A 1 133 ? 35.160 12.169 25.899 1.00 39.33 ? 133 TRP A CZ2 1 ATOM 1027 C CZ3 . TRP A 1 133 ? 36.848 13.517 24.770 1.00 38.02 ? 133 TRP A CZ3 1 ATOM 1028 C CH2 . TRP A 1 133 ? 36.486 12.555 25.698 1.00 39.91 ? 133 TRP A CH2 1 ATOM 1029 N N . ILE A 1 134 ? 33.162 12.188 21.030 1.00 25.86 ? 134 ILE A N 1 ATOM 1030 C CA . ILE A 1 134 ? 32.329 11.022 20.866 1.00 26.03 ? 134 ILE A CA 1 ATOM 1031 C C . ILE A 1 134 ? 31.664 10.612 22.177 1.00 27.09 ? 134 ILE A C 1 ATOM 1032 O O . ILE A 1 134 ? 32.297 10.194 23.148 1.00 29.17 ? 134 ILE A O 1 ATOM 1033 C CB . ILE A 1 134 ? 33.158 9.847 20.290 1.00 24.79 ? 134 ILE A CB 1 ATOM 1034 C CG1 . ILE A 1 134 ? 33.857 10.262 18.994 1.00 24.17 ? 134 ILE A CG1 1 ATOM 1035 C CG2 . ILE A 1 134 ? 32.221 8.671 19.975 1.00 22.76 ? 134 ILE A CG2 1 ATOM 1036 C CD1 . ILE A 1 134 ? 35.047 9.367 18.630 1.00 24.49 ? 134 ILE A CD1 1 ATOM 1037 N N . ASN A 1 135 ? 30.392 10.974 22.298 1.00 27.76 ? 135 ASN A N 1 ATOM 1038 C CA . ASN A 1 135 ? 29.577 10.566 23.426 1.00 29.05 ? 135 ASN A CA 1 ATOM 1039 C C . ASN A 1 135 ? 28.924 9.232 23.029 1.00 33.82 ? 135 ASN A C 1 ATOM 1040 O O . ASN A 1 135 ? 27.870 9.115 22.382 1.00 31.76 ? 135 ASN A O 1 ATOM 1041 C CB . ASN A 1 135 ? 28.434 11.486 23.745 1.00 26.92 ? 135 ASN A CB 1 ATOM 1042 C CG . ASN A 1 135 ? 28.930 12.829 24.216 1.00 28.12 ? 135 ASN A CG 1 ATOM 1043 O OD1 . ASN A 1 135 ? 29.393 13.609 23.404 1.00 31.15 ? 135 ASN A OD1 1 ATOM 1044 N ND2 . ASN A 1 135 ? 28.938 13.230 25.469 1.00 23.38 ? 135 ASN A ND2 1 ATOM 1045 N N . LYS A 1 136 ? 29.635 8.189 23.433 1.00 37.99 ? 136 LYS A N 1 ATOM 1046 C CA . LYS A 1 136 ? 29.253 6.806 23.216 1.00 41.70 ? 136 LYS A CA 1 ATOM 1047 C C . LYS A 1 136 ? 27.851 6.523 23.731 1.00 40.37 ? 136 LYS A C 1 ATOM 1048 O O . LYS A 1 136 ? 26.965 5.991 23.068 1.00 40.67 ? 136 LYS A O 1 ATOM 1049 C CB . LYS A 1 136 ? 30.285 5.950 23.923 1.00 48.42 ? 136 LYS A CB 1 ATOM 1050 C CG . LYS A 1 136 ? 31.322 5.325 22.987 1.00 56.23 ? 136 LYS A CG 1 ATOM 1051 C CD . LYS A 1 136 ? 32.504 4.765 23.789 1.00 62.09 ? 136 LYS A CD 1 ATOM 1052 C CE . LYS A 1 136 ? 33.519 5.871 24.080 1.00 67.14 ? 136 LYS A CE 1 ATOM 1053 N NZ . LYS A 1 136 ? 34.090 6.367 22.830 1.00 68.95 ? 136 LYS A NZ 1 ATOM 1054 N N . ASP A 1 137 ? 27.622 7.091 24.907 1.00 40.56 ? 137 ASP A N 1 ATOM 1055 C CA . ASP A 1 137 ? 26.338 6.962 25.571 1.00 43.22 ? 137 ASP A CA 1 ATOM 1056 C C . ASP A 1 137 ? 25.128 7.683 24.939 1.00 41.85 ? 137 ASP A C 1 ATOM 1057 O O . ASP A 1 137 ? 23.979 7.479 25.342 1.00 45.13 ? 137 ASP A O 1 ATOM 1058 C CB . ASP A 1 137 ? 26.554 7.389 27.055 1.00 47.36 ? 137 ASP A CB 1 ATOM 1059 C CG . ASP A 1 137 ? 26.893 8.842 27.374 1.00 48.81 ? 137 ASP A CG 1 ATOM 1060 O OD1 . ASP A 1 137 ? 27.717 9.476 26.697 1.00 45.92 ? 137 ASP A OD1 1 ATOM 1061 O OD2 . ASP A 1 137 ? 26.295 9.323 28.340 1.00 52.20 ? 137 ASP A OD2 1 ATOM 1062 N N . TRP A 1 138 ? 25.302 8.555 23.945 1.00 39.58 ? 138 TRP A N 1 ATOM 1063 C CA . TRP A 1 138 ? 24.169 9.231 23.308 1.00 37.58 ? 138 TRP A CA 1 ATOM 1064 C C . TRP A 1 138 ? 24.133 8.977 21.806 1.00 36.59 ? 138 TRP A C 1 ATOM 1065 O O . TRP A 1 138 ? 23.598 9.736 20.994 1.00 36.37 ? 138 TRP A O 1 ATOM 1066 C CB . TRP A 1 138 ? 24.206 10.747 23.542 1.00 38.28 ? 138 TRP A CB 1 ATOM 1067 C CG . TRP A 1 138 ? 24.023 11.105 25.004 1.00 38.28 ? 138 TRP A CG 1 ATOM 1068 C CD1 . TRP A 1 138 ? 25.105 11.379 25.790 1.00 39.41 ? 138 TRP A CD1 1 ATOM 1069 C CD2 . TRP A 1 138 ? 22.845 11.191 25.690 1.00 38.19 ? 138 TRP A CD2 1 ATOM 1070 N NE1 . TRP A 1 138 ? 24.628 11.640 26.983 1.00 40.19 ? 138 TRP A NE1 1 ATOM 1071 C CE2 . TRP A 1 138 ? 23.295 11.540 26.966 1.00 38.55 ? 138 TRP A CE2 1 ATOM 1072 C CE3 . TRP A 1 138 ? 21.502 11.033 25.427 1.00 37.19 ? 138 TRP A CE3 1 ATOM 1073 C CZ2 . TRP A 1 138 ? 22.425 11.748 28.013 1.00 36.88 ? 138 TRP A CZ2 1 ATOM 1074 C CZ3 . TRP A 1 138 ? 20.622 11.242 26.476 1.00 37.37 ? 138 TRP A CZ3 1 ATOM 1075 C CH2 . TRP A 1 138 ? 21.075 11.594 27.747 1.00 38.94 ? 138 TRP A CH2 1 ATOM 1076 N N . ASN A 1 139 ? 24.742 7.853 21.439 1.00 35.02 ? 139 ASN A N 1 ATOM 1077 C CA . ASN A 1 139 ? 24.820 7.392 20.054 1.00 36.55 ? 139 ASN A CA 1 ATOM 1078 C C . ASN A 1 139 ? 25.660 8.166 19.041 1.00 33.28 ? 139 ASN A C 1 ATOM 1079 O O . ASN A 1 139 ? 25.348 8.215 17.845 1.00 30.55 ? 139 ASN A O 1 ATOM 1080 C CB . ASN A 1 139 ? 23.401 7.251 19.443 1.00 43.41 ? 139 ASN A CB 1 ATOM 1081 C CG . ASN A 1 139 ? 22.779 5.882 19.590 1.00 45.48 ? 139 ASN A CG 1 ATOM 1082 O OD1 . ASN A 1 139 ? 23.349 4.868 19.206 1.00 50.36 ? 139 ASN A OD1 1 ATOM 1083 N ND2 . ASN A 1 139 ? 21.595 5.754 20.145 1.00 47.86 ? 139 ASN A ND2 1 ATOM 1084 N N . ASP A 1 140 ? 26.702 8.868 19.487 1.00 31.44 ? 140 ASP A N 1 ATOM 1085 C CA . ASP A 1 140 ? 27.560 9.555 18.539 1.00 28.47 ? 140 ASP A CA 1 ATOM 1086 C C . ASP A 1 140 ? 28.259 8.558 17.660 1.00 30.58 ? 140 ASP A C 1 ATOM 1087 O O . ASP A 1 140 ? 28.624 7.480 18.136 1.00 31.54 ? 140 ASP A O 1 ATOM 1088 C CB . ASP A 1 140 ? 28.640 10.355 19.193 1.00 23.53 ? 140 ASP A CB 1 ATOM 1089 C CG . ASP A 1 140 ? 28.146 11.737 19.541 1.00 19.84 ? 140 ASP A CG 1 ATOM 1090 O OD1 . ASP A 1 140 ? 27.114 12.171 19.032 1.00 20.19 ? 140 ASP A OD1 1 ATOM 1091 O OD2 . ASP A 1 140 ? 28.828 12.413 20.300 1.00 21.85 ? 140 ASP A OD2 1 ATOM 1092 N N . PRO A 1 141 ? 28.409 8.797 16.357 1.00 30.90 ? 141 PRO A N 1 ATOM 1093 C CA . PRO A 1 141 ? 29.327 8.006 15.553 1.00 30.51 ? 141 PRO A CA 1 ATOM 1094 C C . PRO A 1 141 ? 30.772 8.024 16.111 1.00 30.47 ? 141 PRO A C 1 ATOM 1095 O O . PRO A 1 141 ? 31.177 8.929 16.859 1.00 28.79 ? 141 PRO A O 1 ATOM 1096 C CB . PRO A 1 141 ? 29.137 8.610 14.153 1.00 30.06 ? 141 PRO A CB 1 ATOM 1097 C CG . PRO A 1 141 ? 28.683 10.023 14.414 1.00 29.31 ? 141 PRO A CG 1 ATOM 1098 C CD . PRO A 1 141 ? 27.746 9.863 15.606 1.00 28.49 ? 141 PRO A CD 1 ATOM 1099 N N . PRO A 1 142 ? 31.596 7.021 15.802 1.00 30.41 ? 142 PRO A N 1 ATOM 1100 C CA . PRO A 1 142 ? 32.926 6.860 16.381 1.00 30.56 ? 142 PRO A CA 1 ATOM 1101 C C . PRO A 1 142 ? 34.031 7.774 15.811 1.00 29.65 ? 142 PRO A C 1 ATOM 1102 O O . PRO A 1 142 ? 35.186 7.397 15.566 1.00 29.73 ? 142 PRO A O 1 ATOM 1103 C CB . PRO A 1 142 ? 33.124 5.337 16.196 1.00 30.75 ? 142 PRO A CB 1 ATOM 1104 C CG . PRO A 1 142 ? 32.565 5.082 14.809 1.00 27.13 ? 142 PRO A CG 1 ATOM 1105 C CD . PRO A 1 142 ? 31.271 5.894 14.915 1.00 30.49 ? 142 PRO A CD 1 ATOM 1106 N N . TYR A 1 143 ? 33.686 9.038 15.567 1.00 28.05 ? 143 TYR A N 1 ATOM 1107 C CA . TYR A 1 143 ? 34.629 10.025 15.048 1.00 25.52 ? 143 TYR A CA 1 ATOM 1108 C C . TYR A 1 143 ? 34.064 11.410 15.254 1.00 23.88 ? 143 TYR A C 1 ATOM 1109 O O . TYR A 1 143 ? 32.836 11.488 15.395 1.00 22.73 ? 143 TYR A O 1 ATOM 1110 C CB . TYR A 1 143 ? 34.916 9.879 13.554 1.00 25.90 ? 143 TYR A CB 1 ATOM 1111 C CG . TYR A 1 143 ? 33.753 9.414 12.736 1.00 24.16 ? 143 TYR A CG 1 ATOM 1112 C CD1 . TYR A 1 143 ? 32.761 10.270 12.362 1.00 22.80 ? 143 TYR A CD1 1 ATOM 1113 C CD2 . TYR A 1 143 ? 33.736 8.089 12.406 1.00 27.11 ? 143 TYR A CD2 1 ATOM 1114 C CE1 . TYR A 1 143 ? 31.695 9.790 11.656 1.00 25.02 ? 143 TYR A CE1 1 ATOM 1115 C CE2 . TYR A 1 143 ? 32.683 7.594 11.705 1.00 28.42 ? 143 TYR A CE2 1 ATOM 1116 C CZ . TYR A 1 143 ? 31.674 8.450 11.330 1.00 29.35 ? 143 TYR A CZ 1 ATOM 1117 O OH . TYR A 1 143 ? 30.581 7.905 10.691 1.00 31.57 ? 143 TYR A OH 1 ATOM 1118 N N . PRO A 1 144 ? 34.840 12.511 15.275 1.00 23.29 ? 144 PRO A N 1 ATOM 1119 C CA . PRO A 1 144 ? 34.275 13.843 15.149 1.00 21.37 ? 144 PRO A CA 1 ATOM 1120 C C . PRO A 1 144 ? 33.358 13.893 13.912 1.00 18.56 ? 144 PRO A C 1 ATOM 1121 O O . PRO A 1 144 ? 33.581 13.275 12.876 1.00 20.03 ? 144 PRO A O 1 ATOM 1122 C CB . PRO A 1 144 ? 35.531 14.717 15.147 1.00 22.18 ? 144 PRO A CB 1 ATOM 1123 C CG . PRO A 1 144 ? 36.698 13.849 14.798 1.00 21.97 ? 144 PRO A CG 1 ATOM 1124 C CD . PRO A 1 144 ? 36.297 12.562 15.447 1.00 22.75 ? 144 PRO A CD 1 ATOM 1125 N N . HIS A 1 145 ? 32.225 14.539 14.043 1.00 16.66 ? 145 HIS A N 1 ATOM 1126 C CA . HIS A 1 145 ? 31.256 14.588 12.980 1.00 16.30 ? 145 HIS A CA 1 ATOM 1127 C C . HIS A 1 145 ? 30.452 15.879 12.913 1.00 17.51 ? 145 HIS A C 1 ATOM 1128 O O . HIS A 1 145 ? 30.417 16.709 13.822 1.00 19.43 ? 145 HIS A O 1 ATOM 1129 C CB . HIS A 1 145 ? 30.276 13.379 13.152 1.00 15.53 ? 145 HIS A CB 1 ATOM 1130 C CG . HIS A 1 145 ? 29.761 13.271 14.601 1.00 17.61 ? 145 HIS A CG 1 ATOM 1131 N ND1 . HIS A 1 145 ? 30.450 12.852 15.676 1.00 17.66 ? 145 HIS A ND1 1 ATOM 1132 C CD2 . HIS A 1 145 ? 28.516 13.657 15.059 1.00 17.61 ? 145 HIS A CD2 1 ATOM 1133 C CE1 . HIS A 1 145 ? 29.706 12.966 16.739 1.00 13.56 ? 145 HIS A CE1 1 ATOM 1134 N NE2 . HIS A 1 145 ? 28.548 13.449 16.369 1.00 16.35 ? 145 HIS A NE2 1 ATOM 1135 N N . ILE A 1 146 ? 29.818 16.068 11.769 1.00 17.03 ? 146 ILE A N 1 ATOM 1136 C CA . ILE A 1 146 ? 28.920 17.187 11.579 1.00 19.06 ? 146 ILE A CA 1 ATOM 1137 C C . ILE A 1 146 ? 27.570 16.485 11.623 1.00 17.49 ? 146 ILE A C 1 ATOM 1138 O O . ILE A 1 146 ? 27.415 15.414 11.054 1.00 16.49 ? 146 ILE A O 1 ATOM 1139 C CB . ILE A 1 146 ? 29.117 17.875 10.194 1.00 22.10 ? 146 ILE A CB 1 ATOM 1140 C CG1 . ILE A 1 146 ? 30.492 18.566 10.168 1.00 22.66 ? 146 ILE A CG1 1 ATOM 1141 C CG2 . ILE A 1 146 ? 28.021 18.910 9.947 1.00 19.53 ? 146 ILE A CG2 1 ATOM 1142 C CD1 . ILE A 1 146 ? 31.102 18.639 8.751 1.00 23.47 ? 146 ILE A CD1 1 ATOM 1143 N N . GLY A 1 147 ? 26.545 16.990 12.269 1.00 17.79 ? 147 GLY A N 1 ATOM 1144 C CA . GLY A 1 147 ? 25.261 16.305 12.280 1.00 16.90 ? 147 GLY A CA 1 ATOM 1145 C C . GLY A 1 147 ? 24.061 17.224 12.250 1.00 16.24 ? 147 GLY A C 1 ATOM 1146 O O . GLY A 1 147 ? 24.178 18.409 12.538 1.00 15.28 ? 147 GLY A O 1 ATOM 1147 N N . ILE A 1 148 ? 22.902 16.672 11.870 1.00 17.48 ? 148 ILE A N 1 ATOM 1148 C CA . ILE A 1 148 ? 21.663 17.428 11.847 1.00 15.53 ? 148 ILE A CA 1 ATOM 1149 C C . ILE A 1 148 ? 20.828 16.801 12.950 1.00 17.06 ? 148 ILE A C 1 ATOM 1150 O O . ILE A 1 148 ? 20.589 15.590 12.988 1.00 17.35 ? 148 ILE A O 1 ATOM 1151 C CB . ILE A 1 148 ? 20.973 17.310 10.458 1.00 17.76 ? 148 ILE A CB 1 ATOM 1152 C CG1 . ILE A 1 148 ? 21.745 18.161 9.470 1.00 18.80 ? 148 ILE A CG1 1 ATOM 1153 C CG2 . ILE A 1 148 ? 19.521 17.804 10.496 1.00 18.10 ? 148 ILE A CG2 1 ATOM 1154 C CD1 . ILE A 1 148 ? 21.584 17.717 7.997 1.00 20.70 ? 148 ILE A CD1 1 ATOM 1155 N N . ASP A 1 149 ? 20.417 17.657 13.865 1.00 16.32 ? 149 ASP A N 1 ATOM 1156 C CA . ASP A 1 149 ? 19.636 17.301 15.034 1.00 17.10 ? 149 ASP A CA 1 ATOM 1157 C C . ASP A 1 149 ? 18.236 17.820 14.979 1.00 17.05 ? 149 ASP A C 1 ATOM 1158 O O . ASP A 1 149 ? 18.006 19.024 14.818 1.00 20.90 ? 149 ASP A O 1 ATOM 1159 C CB . ASP A 1 149 ? 20.233 17.867 16.317 1.00 17.83 ? 149 ASP A CB 1 ATOM 1160 C CG . ASP A 1 149 ? 21.646 17.415 16.569 1.00 19.93 ? 149 ASP A CG 1 ATOM 1161 O OD1 . ASP A 1 149 ? 22.120 16.501 15.893 1.00 17.90 ? 149 ASP A OD1 1 ATOM 1162 O OD2 . ASP A 1 149 ? 22.269 18.018 17.435 1.00 21.25 ? 149 ASP A OD2 1 ATOM 1163 N N . VAL A 1 150 ? 17.297 16.927 15.112 1.00 16.23 ? 150 VAL A N 1 ATOM 1164 C CA . VAL A 1 150 ? 15.911 17.328 15.062 1.00 17.03 ? 150 VAL A CA 1 ATOM 1165 C C . VAL A 1 150 ? 15.265 16.821 16.360 1.00 18.27 ? 150 VAL A C 1 ATOM 1166 O O . VAL A 1 150 ? 15.105 15.618 16.567 1.00 20.92 ? 150 VAL A O 1 ATOM 1167 C CB . VAL A 1 150 ? 15.260 16.714 13.742 1.00 19.30 ? 150 VAL A CB 1 ATOM 1168 C CG1 . VAL A 1 150 ? 13.789 17.186 13.625 1.00 18.41 ? 150 VAL A CG1 1 ATOM 1169 C CG2 . VAL A 1 150 ? 15.961 17.198 12.464 1.00 16.12 ? 150 VAL A CG2 1 ATOM 1170 N N . ASN A 1 151 ? 14.996 17.738 17.281 1.00 19.39 ? 151 ASN A N 1 ATOM 1171 C CA . ASN A 1 151 ? 14.372 17.496 18.583 1.00 20.75 ? 151 ASN A CA 1 ATOM 1172 C C . ASN A 1 151 ? 15.053 16.508 19.531 1.00 20.65 ? 151 ASN A C 1 ATOM 1173 O O . ASN A 1 151 ? 14.505 15.973 20.492 1.00 22.29 ? 151 ASN A O 1 ATOM 1174 C CB . ASN A 1 151 ? 12.941 17.049 18.333 1.00 20.38 ? 151 ASN A CB 1 ATOM 1175 C CG . ASN A 1 151 ? 12.099 18.154 17.744 1.00 22.29 ? 151 ASN A CG 1 ATOM 1176 O OD1 . ASN A 1 151 ? 12.443 19.335 17.821 1.00 24.08 ? 151 ASN A OD1 1 ATOM 1177 N ND2 . ASN A 1 151 ? 10.957 17.885 17.147 1.00 23.54 ? 151 ASN A ND2 1 ATOM 1178 N N . SER A 1 152 ? 16.314 16.255 19.272 1.00 20.56 ? 152 SER A N 1 ATOM 1179 C CA . SER A 1 152 ? 17.069 15.322 20.073 1.00 20.18 ? 152 SER A CA 1 ATOM 1180 C C . SER A 1 152 ? 18.571 15.442 19.803 1.00 21.14 ? 152 SER A C 1 ATOM 1181 O O . SER A 1 152 ? 18.977 15.868 18.717 1.00 20.19 ? 152 SER A O 1 ATOM 1182 C CB . SER A 1 152 ? 16.581 13.914 19.754 1.00 18.28 ? 152 SER A CB 1 ATOM 1183 O OG . SER A 1 152 ? 17.470 12.894 20.190 1.00 20.71 ? 152 SER A OG 1 ATOM 1184 N N . ILE A 1 153 ? 19.443 15.161 20.782 1.00 20.08 ? 153 ILE A N 1 ATOM 1185 C CA . ILE A 1 153 ? 20.876 15.222 20.576 1.00 18.87 ? 153 ILE A CA 1 ATOM 1186 C C . ILE A 1 153 ? 21.350 14.062 19.694 1.00 18.67 ? 153 ILE A C 1 ATOM 1187 O O . ILE A 1 153 ? 22.478 14.089 19.217 1.00 18.97 ? 153 ILE A O 1 ATOM 1188 C CB . ILE A 1 153 ? 21.546 15.220 21.975 1.00 18.05 ? 153 ILE A CB 1 ATOM 1189 C CG1 . ILE A 1 153 ? 22.992 15.705 21.892 1.00 16.65 ? 153 ILE A CG1 1 ATOM 1190 C CG2 . ILE A 1 153 ? 21.601 13.785 22.522 1.00 21.70 ? 153 ILE A CG2 1 ATOM 1191 C CD1 . ILE A 1 153 ? 23.264 17.089 21.270 1.00 16.00 ? 153 ILE A CD1 1 ATOM 1192 N N . VAL A 1 154 ? 20.554 13.008 19.474 1.00 18.00 ? 154 VAL A N 1 ATOM 1193 C CA . VAL A 1 154 ? 20.924 11.870 18.625 1.00 19.24 ? 154 VAL A CA 1 ATOM 1194 C C . VAL A 1 154 ? 20.556 12.296 17.198 1.00 19.99 ? 154 VAL A C 1 ATOM 1195 O O . VAL A 1 154 ? 19.386 12.279 16.802 1.00 20.17 ? 154 VAL A O 1 ATOM 1196 C CB . VAL A 1 154 ? 20.122 10.593 19.020 1.00 19.53 ? 154 VAL A CB 1 ATOM 1197 C CG1 . VAL A 1 154 ? 20.612 9.435 18.169 1.00 17.41 ? 154 VAL A CG1 1 ATOM 1198 C CG2 . VAL A 1 154 ? 20.275 10.288 20.513 1.00 19.35 ? 154 VAL A CG2 1 ATOM 1199 N N . SER A 1 155 ? 21.551 12.736 16.434 1.00 20.56 ? 155 SER A N 1 ATOM 1200 C CA . SER A 1 155 ? 21.393 13.259 15.068 1.00 20.94 ? 155 SER A CA 1 ATOM 1201 C C . SER A 1 155 ? 20.641 12.428 14.064 1.00 21.93 ? 155 SER A C 1 ATOM 1202 O O . SER A 1 155 ? 20.913 11.226 13.983 1.00 22.29 ? 155 SER A O 1 ATOM 1203 C CB . SER A 1 155 ? 22.721 13.520 14.396 1.00 17.41 ? 155 SER A CB 1 ATOM 1204 O OG . SER A 1 155 ? 23.621 14.181 15.276 1.00 19.09 ? 155 SER A OG 1 ATOM 1205 N N . VAL A 1 156 ? 19.738 12.995 13.261 1.00 20.74 ? 156 VAL A N 1 ATOM 1206 C CA . VAL A 1 156 ? 19.044 12.155 12.278 1.00 21.34 ? 156 VAL A CA 1 ATOM 1207 C C . VAL A 1 156 ? 19.982 11.774 11.115 1.00 22.70 ? 156 VAL A C 1 ATOM 1208 O O . VAL A 1 156 ? 19.733 10.895 10.286 1.00 24.46 ? 156 VAL A O 1 ATOM 1209 C CB . VAL A 1 156 ? 17.791 12.904 11.759 1.00 21.15 ? 156 VAL A CB 1 ATOM 1210 C CG1 . VAL A 1 156 ? 16.898 13.187 12.961 1.00 22.80 ? 156 VAL A CG1 1 ATOM 1211 C CG2 . VAL A 1 156 ? 18.152 14.194 11.021 1.00 22.47 ? 156 VAL A CG2 1 ATOM 1212 N N . ALA A 1 157 ? 21.132 12.441 10.996 1.00 22.13 ? 157 ALA A N 1 ATOM 1213 C CA . ALA A 1 157 ? 22.119 12.200 9.949 1.00 19.38 ? 157 ALA A CA 1 ATOM 1214 C C . ALA A 1 157 ? 23.445 12.867 10.332 1.00 19.45 ? 157 ALA A C 1 ATOM 1215 O O . ALA A 1 157 ? 23.485 13.909 11.004 1.00 17.49 ? 157 ALA A O 1 ATOM 1216 C CB . ALA A 1 157 ? 21.675 12.799 8.611 1.00 19.49 ? 157 ALA A CB 1 ATOM 1217 N N . THR A 1 158 ? 24.548 12.270 9.941 1.00 16.98 ? 158 THR A N 1 ATOM 1218 C CA . THR A 1 158 ? 25.874 12.800 10.252 1.00 17.61 ? 158 THR A CA 1 ATOM 1219 C C . THR A 1 158 ? 26.866 12.579 9.125 1.00 17.60 ? 158 THR A C 1 ATOM 1220 O O . THR A 1 158 ? 26.554 11.881 8.166 1.00 21.45 ? 158 THR A O 1 ATOM 1221 C CB . THR A 1 158 ? 26.536 12.146 11.524 1.00 17.97 ? 158 THR A CB 1 ATOM 1222 O OG1 . THR A 1 158 ? 26.587 10.715 11.315 1.00 21.35 ? 158 THR A OG1 1 ATOM 1223 C CG2 . THR A 1 158 ? 25.775 12.440 12.782 1.00 16.72 ? 158 THR A CG2 1 ATOM 1224 N N . THR A 1 159 ? 28.030 13.206 9.087 1.00 16.60 ? 159 THR A N 1 ATOM 1225 C CA . THR A 1 159 ? 29.005 12.921 8.056 1.00 15.19 ? 159 THR A CA 1 ATOM 1226 C C . THR A 1 159 ? 30.307 13.078 8.808 1.00 18.30 ? 159 THR A C 1 ATOM 1227 O O . THR A 1 159 ? 30.421 13.822 9.796 1.00 17.49 ? 159 THR A O 1 ATOM 1228 C CB . THR A 1 159 ? 28.965 13.883 6.862 1.00 15.90 ? 159 THR A CB 1 ATOM 1229 O OG1 . THR A 1 159 ? 29.768 13.228 5.873 1.00 16.59 ? 159 THR A OG1 1 ATOM 1230 C CG2 . THR A 1 159 ? 29.433 15.300 7.139 1.00 17.09 ? 159 THR A CG2 1 ATOM 1231 N N . ARG A 1 160 ? 31.316 12.318 8.453 1.00 20.59 ? 160 ARG A N 1 ATOM 1232 C CA . ARG A 1 160 ? 32.612 12.396 9.108 1.00 22.97 ? 160 ARG A CA 1 ATOM 1233 C C . ARG A 1 160 ? 33.291 13.780 9.031 1.00 23.50 ? 160 ARG A C 1 ATOM 1234 O O . ARG A 1 160 ? 33.270 14.470 7.994 1.00 21.64 ? 160 ARG A O 1 ATOM 1235 C CB . ARG A 1 160 ? 33.482 11.302 8.458 1.00 24.96 ? 160 ARG A CB 1 ATOM 1236 C CG . ARG A 1 160 ? 34.843 11.109 9.080 1.00 35.35 ? 160 ARG A CG 1 ATOM 1237 C CD . ARG A 1 160 ? 35.494 9.747 8.728 1.00 44.45 ? 160 ARG A CD 1 ATOM 1238 N NE . ARG A 1 160 ? 35.784 8.902 9.914 1.00 52.12 ? 160 ARG A NE 1 ATOM 1239 C CZ . ARG A 1 160 ? 36.898 9.012 10.680 1.00 56.14 ? 160 ARG A CZ 1 ATOM 1240 N NH1 . ARG A 1 160 ? 37.848 9.919 10.414 1.00 60.25 ? 160 ARG A NH1 1 ATOM 1241 N NH2 . ARG A 1 160 ? 37.091 8.206 11.734 1.00 58.12 ? 160 ARG A NH2 1 ATOM 1242 N N . TRP A 1 161 ? 33.840 14.244 10.154 1.00 21.17 ? 161 TRP A N 1 ATOM 1243 C CA . TRP A 1 161 ? 34.596 15.517 10.207 1.00 22.67 ? 161 TRP A CA 1 ATOM 1244 C C . TRP A 1 161 ? 36.030 15.032 10.499 1.00 21.99 ? 161 TRP A C 1 ATOM 1245 O O . TRP A 1 161 ? 36.305 14.445 11.553 1.00 22.95 ? 161 TRP A O 1 ATOM 1246 C CB . TRP A 1 161 ? 34.077 16.441 11.348 1.00 19.27 ? 161 TRP A CB 1 ATOM 1247 C CG . TRP A 1 161 ? 34.581 17.894 11.511 1.00 23.33 ? 161 TRP A CG 1 ATOM 1248 C CD1 . TRP A 1 161 ? 35.345 18.603 10.590 1.00 21.97 ? 161 TRP A CD1 1 ATOM 1249 C CD2 . TRP A 1 161 ? 34.295 18.661 12.627 1.00 21.57 ? 161 TRP A CD2 1 ATOM 1250 N NE1 . TRP A 1 161 ? 35.547 19.791 11.127 1.00 22.32 ? 161 TRP A NE1 1 ATOM 1251 C CE2 . TRP A 1 161 ? 34.934 19.871 12.333 1.00 21.41 ? 161 TRP A CE2 1 ATOM 1252 C CE3 . TRP A 1 161 ? 33.615 18.495 13.811 1.00 17.68 ? 161 TRP A CE3 1 ATOM 1253 C CZ2 . TRP A 1 161 ? 34.891 20.947 13.209 1.00 18.08 ? 161 TRP A CZ2 1 ATOM 1254 C CZ3 . TRP A 1 161 ? 33.588 19.572 14.674 1.00 19.92 ? 161 TRP A CZ3 1 ATOM 1255 C CH2 . TRP A 1 161 ? 34.206 20.772 14.388 1.00 18.82 ? 161 TRP A CH2 1 ATOM 1256 N N . GLU A 1 162 ? 36.996 15.148 9.610 1.00 22.64 ? 162 GLU A N 1 ATOM 1257 C CA . GLU A 1 162 ? 38.343 14.655 9.937 1.00 24.35 ? 162 GLU A CA 1 ATOM 1258 C C . GLU A 1 162 ? 39.056 15.286 11.132 1.00 24.34 ? 162 GLU A C 1 ATOM 1259 O O . GLU A 1 162 ? 39.025 16.492 11.382 1.00 21.34 ? 162 GLU A O 1 ATOM 1260 C CB . GLU A 1 162 ? 39.231 14.815 8.753 1.00 23.46 ? 162 GLU A CB 1 ATOM 1261 C CG . GLU A 1 162 ? 38.661 14.000 7.610 1.00 32.00 ? 162 GLU A CG 1 ATOM 1262 C CD . GLU A 1 162 ? 39.473 14.060 6.324 1.00 37.88 ? 162 GLU A CD 1 ATOM 1263 O OE1 . GLU A 1 162 ? 40.378 14.900 6.177 1.00 45.79 ? 162 GLU A OE1 1 ATOM 1264 O OE2 . GLU A 1 162 ? 39.189 13.243 5.448 1.00 43.73 ? 162 GLU A OE2 1 ATOM 1265 N N . ASN A 1 163 ? 39.726 14.435 11.892 1.00 24.30 ? 163 ASN A N 1 ATOM 1266 C CA . ASN A 1 163 ? 40.480 14.830 13.071 1.00 26.03 ? 163 ASN A CA 1 ATOM 1267 C C . ASN A 1 163 ? 41.297 16.063 12.903 1.00 24.99 ? 163 ASN A C 1 ATOM 1268 O O . ASN A 1 163 ? 41.261 16.964 13.724 1.00 27.59 ? 163 ASN A O 1 ATOM 1269 C CB . ASN A 1 163 ? 41.401 13.724 13.497 1.00 30.67 ? 163 ASN A CB 1 ATOM 1270 C CG . ASN A 1 163 ? 40.528 12.666 14.134 1.00 36.17 ? 163 ASN A CG 1 ATOM 1271 O OD1 . ASN A 1 163 ? 40.462 12.510 15.339 1.00 44.19 ? 163 ASN A OD1 1 ATOM 1272 N ND2 . ASN A 1 163 ? 39.702 11.896 13.474 1.00 41.92 ? 163 ASN A ND2 1 ATOM 1273 N N . ASP A 1 164 ? 41.951 16.128 11.765 1.00 26.07 ? 164 ASP A N 1 ATOM 1274 C CA . ASP A 1 164 ? 42.759 17.283 11.439 1.00 28.40 ? 164 ASP A CA 1 ATOM 1275 C C . ASP A 1 164 ? 42.020 18.590 11.278 1.00 28.11 ? 164 ASP A C 1 ATOM 1276 O O . ASP A 1 164 ? 42.569 19.680 11.445 1.00 27.88 ? 164 ASP A O 1 ATOM 1277 C CB . ASP A 1 164 ? 43.503 17.054 10.164 1.00 37.17 ? 164 ASP A CB 1 ATOM 1278 C CG . ASP A 1 164 ? 44.764 16.211 10.308 1.00 44.48 ? 164 ASP A CG 1 ATOM 1279 O OD1 . ASP A 1 164 ? 45.320 16.080 11.419 1.00 47.32 ? 164 ASP A OD1 1 ATOM 1280 O OD2 . ASP A 1 164 ? 45.180 15.691 9.266 1.00 49.74 ? 164 ASP A OD2 1 ATOM 1281 N N . ASP A 1 165 ? 40.758 18.490 10.873 1.00 27.58 ? 165 ASP A N 1 ATOM 1282 C CA . ASP A 1 165 ? 39.980 19.695 10.724 1.00 25.38 ? 165 ASP A CA 1 ATOM 1283 C C . ASP A 1 165 ? 39.304 19.967 12.028 1.00 23.53 ? 165 ASP A C 1 ATOM 1284 O O . ASP A 1 165 ? 39.449 21.082 12.499 1.00 20.04 ? 165 ASP A O 1 ATOM 1285 C CB . ASP A 1 165 ? 38.977 19.535 9.597 1.00 25.30 ? 165 ASP A CB 1 ATOM 1286 C CG . ASP A 1 165 ? 39.701 19.564 8.243 1.00 28.06 ? 165 ASP A CG 1 ATOM 1287 O OD1 . ASP A 1 165 ? 40.597 20.403 8.058 1.00 28.63 ? 165 ASP A OD1 1 ATOM 1288 O OD2 . ASP A 1 165 ? 39.397 18.744 7.371 1.00 26.57 ? 165 ASP A OD2 1 ATOM 1289 N N . ALA A 1 166 ? 38.688 18.961 12.649 1.00 22.96 ? 166 ALA A N 1 ATOM 1290 C CA . ALA A 1 166 ? 38.011 19.131 13.939 1.00 24.25 ? 166 ALA A CA 1 ATOM 1291 C C . ALA A 1 166 ? 38.894 19.683 15.062 1.00 25.21 ? 166 ALA A C 1 ATOM 1292 O O . ALA A 1 166 ? 38.497 20.549 15.859 1.00 23.98 ? 166 ALA A O 1 ATOM 1293 C CB . ALA A 1 166 ? 37.455 17.797 14.420 1.00 21.50 ? 166 ALA A CB 1 ATOM 1294 N N . TYR A 1 167 ? 40.138 19.179 15.121 1.00 24.54 ? 167 TYR A N 1 ATOM 1295 C CA . TYR A 1 167 ? 41.074 19.645 16.145 1.00 25.04 ? 167 TYR A CA 1 ATOM 1296 C C . TYR A 1 167 ? 42.206 20.492 15.579 1.00 25.60 ? 167 TYR A C 1 ATOM 1297 O O . TYR A 1 167 ? 43.183 20.773 16.255 1.00 27.90 ? 167 TYR A O 1 ATOM 1298 C CB . TYR A 1 167 ? 41.686 18.464 16.891 1.00 23.56 ? 167 TYR A CB 1 ATOM 1299 C CG . TYR A 1 167 ? 40.652 17.456 17.339 1.00 23.40 ? 167 TYR A CG 1 ATOM 1300 C CD1 . TYR A 1 167 ? 39.637 17.838 18.197 1.00 22.79 ? 167 TYR A CD1 1 ATOM 1301 C CD2 . TYR A 1 167 ? 40.711 16.176 16.820 1.00 24.33 ? 167 TYR A CD2 1 ATOM 1302 C CE1 . TYR A 1 167 ? 38.663 16.931 18.545 1.00 19.31 ? 167 TYR A CE1 1 ATOM 1303 C CE2 . TYR A 1 167 ? 39.744 15.263 17.178 1.00 22.78 ? 167 TYR A CE2 1 ATOM 1304 C CZ . TYR A 1 167 ? 38.732 15.658 18.027 1.00 22.87 ? 167 TYR A CZ 1 ATOM 1305 O OH . TYR A 1 167 ? 37.786 14.737 18.386 1.00 23.62 ? 167 TYR A OH 1 ATOM 1306 N N . GLY A 1 168 ? 42.126 21.004 14.361 1.00 23.83 ? 168 GLY A N 1 ATOM 1307 C CA . GLY A 1 168 ? 43.216 21.786 13.810 1.00 22.15 ? 168 GLY A CA 1 ATOM 1308 C C . GLY A 1 168 ? 43.197 23.264 14.113 1.00 22.37 ? 168 GLY A C 1 ATOM 1309 O O . GLY A 1 168 ? 44.154 23.951 13.773 1.00 24.08 ? 168 GLY A O 1 ATOM 1310 N N . SER A 1 169 ? 42.153 23.834 14.715 1.00 22.60 ? 169 SER A N 1 ATOM 1311 C CA . SER A 1 169 ? 42.092 25.266 14.998 1.00 22.50 ? 169 SER A CA 1 ATOM 1312 C C . SER A 1 169 ? 42.278 26.259 13.838 1.00 23.15 ? 169 SER A C 1 ATOM 1313 O O . SER A 1 169 ? 42.899 27.317 13.958 1.00 23.78 ? 169 SER A O 1 ATOM 1314 C CB . SER A 1 169 ? 43.093 25.673 16.095 1.00 22.66 ? 169 SER A CB 1 ATOM 1315 O OG . SER A 1 169 ? 42.778 25.011 17.307 1.00 22.21 ? 169 SER A OG 1 ATOM 1316 N N . SER A 1 170 ? 41.777 25.945 12.639 1.00 23.11 ? 170 SER A N 1 ATOM 1317 C CA . SER A 1 170 ? 41.839 26.868 11.504 1.00 21.29 ? 170 SER A CA 1 ATOM 1318 C C . SER A 1 170 ? 40.482 27.517 11.349 1.00 21.67 ? 170 SER A C 1 ATOM 1319 O O . SER A 1 170 ? 39.469 26.928 11.730 1.00 20.59 ? 170 SER A O 1 ATOM 1320 C CB . SER A 1 170 ? 41.979 26.283 10.159 1.00 21.34 ? 170 SER A CB 1 ATOM 1321 O OG . SER A 1 170 ? 43.226 25.685 10.077 1.00 33.01 ? 170 SER A OG 1 ATOM 1322 N N . ILE A 1 171 ? 40.407 28.703 10.751 1.00 19.27 ? 171 ILE A N 1 ATOM 1323 C CA . ILE A 1 171 ? 39.121 29.336 10.531 1.00 18.27 ? 171 ILE A CA 1 ATOM 1324 C C . ILE A 1 171 ? 38.395 28.520 9.469 1.00 17.66 ? 171 ILE A C 1 ATOM 1325 O O . ILE A 1 171 ? 38.963 28.071 8.480 1.00 17.76 ? 171 ILE A O 1 ATOM 1326 C CB . ILE A 1 171 ? 39.322 30.794 10.058 1.00 18.89 ? 171 ILE A CB 1 ATOM 1327 C CG1 . ILE A 1 171 ? 40.078 31.598 11.158 1.00 20.60 ? 171 ILE A CG1 1 ATOM 1328 C CG2 . ILE A 1 171 ? 37.967 31.409 9.724 1.00 18.26 ? 171 ILE A CG2 1 ATOM 1329 C CD1 . ILE A 1 171 ? 40.528 33.043 10.807 1.00 22.20 ? 171 ILE A CD1 1 ATOM 1330 N N . ALA A 1 172 ? 37.137 28.227 9.711 1.00 15.79 ? 172 ALA A N 1 ATOM 1331 C CA . ALA A 1 172 ? 36.329 27.491 8.772 1.00 16.34 ? 172 ALA A CA 1 ATOM 1332 C C . ALA A 1 172 ? 35.094 28.321 8.412 1.00 14.55 ? 172 ALA A C 1 ATOM 1333 O O . ALA A 1 172 ? 34.651 29.175 9.177 1.00 14.48 ? 172 ALA A O 1 ATOM 1334 C CB . ALA A 1 172 ? 35.873 26.191 9.374 1.00 15.77 ? 172 ALA A CB 1 ATOM 1335 N N . THR A 1 173 ? 34.602 28.116 7.206 1.00 14.40 ? 173 THR A N 1 ATOM 1336 C CA . THR A 1 173 ? 33.430 28.788 6.714 1.00 15.70 ? 173 THR A CA 1 ATOM 1337 C C . THR A 1 173 ? 32.269 27.839 6.506 1.00 15.03 ? 173 THR A C 1 ATOM 1338 O O . THR A 1 173 ? 32.395 26.806 5.865 1.00 17.07 ? 173 THR A O 1 ATOM 1339 C CB . THR A 1 173 ? 33.663 29.453 5.395 1.00 17.15 ? 173 THR A CB 1 ATOM 1340 O OG1 . THR A 1 173 ? 34.775 30.320 5.611 1.00 20.76 ? 173 THR A OG1 1 ATOM 1341 C CG2 . THR A 1 173 ? 32.442 30.259 4.919 1.00 15.20 ? 173 THR A CG2 1 ATOM 1342 N N . ALA A 1 174 ? 31.118 28.126 7.087 1.00 14.88 ? 174 ALA A N 1 ATOM 1343 C CA . ALA A 1 174 ? 29.947 27.292 6.935 1.00 14.20 ? 174 ALA A CA 1 ATOM 1344 C C . ALA A 1 174 ? 28.813 27.970 6.202 1.00 15.12 ? 174 ALA A C 1 ATOM 1345 O O . ALA A 1 174 ? 28.541 29.167 6.360 1.00 17.42 ? 174 ALA A O 1 ATOM 1346 C CB . ALA A 1 174 ? 29.360 26.877 8.270 1.00 13.41 ? 174 ALA A CB 1 ATOM 1347 N N . HIS A 1 175 ? 28.104 27.189 5.389 1.00 14.54 ? 175 HIS A N 1 ATOM 1348 C CA . HIS A 1 175 ? 26.951 27.659 4.652 1.00 13.12 ? 175 HIS A CA 1 ATOM 1349 C C . HIS A 1 175 ? 25.848 26.679 4.994 1.00 12.79 ? 175 HIS A C 1 ATOM 1350 O O . HIS A 1 175 ? 26.014 25.468 4.930 1.00 14.21 ? 175 HIS A O 1 ATOM 1351 C CB . HIS A 1 175 ? 27.115 27.612 3.150 1.00 10.09 ? 175 HIS A CB 1 ATOM 1352 C CG . HIS A 1 175 ? 28.055 28.660 2.643 1.00 13.55 ? 175 HIS A CG 1 ATOM 1353 N ND1 . HIS A 1 175 ? 27.778 29.898 2.317 1.00 13.97 ? 175 HIS A ND1 1 ATOM 1354 C CD2 . HIS A 1 175 ? 29.399 28.509 2.437 1.00 16.99 ? 175 HIS A CD2 1 ATOM 1355 C CE1 . HIS A 1 175 ? 28.851 30.542 1.923 1.00 16.01 ? 175 HIS A CE1 1 ATOM 1356 N NE2 . HIS A 1 175 ? 29.817 29.686 1.999 1.00 16.80 ? 175 HIS A NE2 1 ATOM 1357 N N . ILE A 1 176 ? 24.741 27.171 5.515 1.00 12.64 ? 176 ILE A N 1 ATOM 1358 C CA . ILE A 1 176 ? 23.613 26.298 5.815 1.00 12.62 ? 176 ILE A CA 1 ATOM 1359 C C . ILE A 1 176 ? 22.406 26.832 5.031 1.00 14.18 ? 176 ILE A C 1 ATOM 1360 O O . ILE A 1 176 ? 22.083 28.035 5.058 1.00 12.74 ? 176 ILE A O 1 ATOM 1361 C CB . ILE A 1 176 ? 23.363 26.296 7.334 1.00 14.08 ? 176 ILE A CB 1 ATOM 1362 C CG1 . ILE A 1 176 ? 24.622 25.677 8.010 1.00 11.58 ? 176 ILE A CG1 1 ATOM 1363 C CG2 . ILE A 1 176 ? 22.011 25.560 7.656 1.00 13.47 ? 176 ILE A CG2 1 ATOM 1364 C CD1 . ILE A 1 176 ? 24.642 25.892 9.513 1.00 14.69 ? 176 ILE A CD1 1 ATOM 1365 N N . THR A 1 177 ? 21.696 25.981 4.292 1.00 13.21 ? 177 THR A N 1 ATOM 1366 C CA . THR A 1 177 ? 20.552 26.465 3.534 1.00 12.42 ? 177 THR A CA 1 ATOM 1367 C C . THR A 1 177 ? 19.340 25.618 3.813 1.00 14.68 ? 177 THR A C 1 ATOM 1368 O O . THR A 1 177 ? 19.414 24.445 4.175 1.00 13.88 ? 177 THR A O 1 ATOM 1369 C CB . THR A 1 177 ? 20.755 26.429 1.985 1.00 11.28 ? 177 THR A CB 1 ATOM 1370 O OG1 . THR A 1 177 ? 21.120 25.109 1.596 1.00 11.34 ? 177 THR A OG1 1 ATOM 1371 C CG2 . THR A 1 177 ? 21.854 27.365 1.539 1.00 10.47 ? 177 THR A CG2 1 ATOM 1372 N N . TYR A 1 178 ? 18.182 26.214 3.716 1.00 14.40 ? 178 TYR A N 1 ATOM 1373 C CA . TYR A 1 178 ? 16.966 25.456 3.891 1.00 15.29 ? 178 TYR A CA 1 ATOM 1374 C C . TYR A 1 178 ? 16.039 25.875 2.756 1.00 16.64 ? 178 TYR A C 1 ATOM 1375 O O . TYR A 1 178 ? 15.826 27.067 2.518 1.00 16.75 ? 178 TYR A O 1 ATOM 1376 C CB . TYR A 1 178 ? 16.275 25.766 5.220 1.00 13.54 ? 178 TYR A CB 1 ATOM 1377 C CG . TYR A 1 178 ? 14.942 25.052 5.394 1.00 14.69 ? 178 TYR A CG 1 ATOM 1378 C CD1 . TYR A 1 178 ? 14.923 23.677 5.484 1.00 16.58 ? 178 TYR A CD1 1 ATOM 1379 C CD2 . TYR A 1 178 ? 13.757 25.782 5.425 1.00 15.85 ? 178 TYR A CD2 1 ATOM 1380 C CE1 . TYR A 1 178 ? 13.706 23.052 5.593 1.00 14.04 ? 178 TYR A CE1 1 ATOM 1381 C CE2 . TYR A 1 178 ? 12.531 25.155 5.531 1.00 15.99 ? 178 TYR A CE2 1 ATOM 1382 C CZ . TYR A 1 178 ? 12.526 23.780 5.612 1.00 18.55 ? 178 TYR A CZ 1 ATOM 1383 O OH . TYR A 1 178 ? 11.325 23.098 5.695 1.00 20.33 ? 178 TYR A OH 1 ATOM 1384 N N . ASP A 1 179 ? 15.531 24.889 2.013 1.00 16.17 ? 179 ASP A N 1 ATOM 1385 C CA . ASP A 1 179 ? 14.596 25.110 0.940 1.00 14.74 ? 179 ASP A CA 1 ATOM 1386 C C . ASP A 1 179 ? 13.230 24.758 1.542 1.00 16.46 ? 179 ASP A C 1 ATOM 1387 O O . ASP A 1 179 ? 12.960 23.574 1.765 1.00 16.50 ? 179 ASP A O 1 ATOM 1388 C CB . ASP A 1 179 ? 14.896 24.194 -0.218 1.00 14.49 ? 179 ASP A CB 1 ATOM 1389 C CG . ASP A 1 179 ? 13.985 24.423 -1.424 1.00 17.60 ? 179 ASP A CG 1 ATOM 1390 O OD1 . ASP A 1 179 ? 12.791 24.668 -1.271 1.00 18.89 ? 179 ASP A OD1 1 ATOM 1391 O OD2 . ASP A 1 179 ? 14.456 24.343 -2.553 1.00 17.73 ? 179 ASP A OD2 1 ATOM 1392 N N . ALA A 1 180 ? 12.345 25.732 1.767 1.00 16.22 ? 180 ALA A N 1 ATOM 1393 C CA . ALA A 1 180 ? 11.024 25.501 2.347 1.00 18.01 ? 180 ALA A CA 1 ATOM 1394 C C . ALA A 1 180 ? 10.041 24.781 1.451 1.00 20.67 ? 180 ALA A C 1 ATOM 1395 O O . ALA A 1 180 ? 9.077 24.239 1.955 1.00 23.25 ? 180 ALA A O 1 ATOM 1396 C CB . ALA A 1 180 ? 10.404 26.816 2.753 1.00 15.40 ? 180 ALA A CB 1 ATOM 1397 N N . ARG A 1 181 ? 10.264 24.752 0.126 1.00 21.61 ? 181 ARG A N 1 ATOM 1398 C CA . ARG A 1 181 ? 9.393 24.039 -0.802 1.00 19.13 ? 181 ARG A CA 1 ATOM 1399 C C . ARG A 1 181 ? 9.778 22.566 -0.762 1.00 21.18 ? 181 ARG A C 1 ATOM 1400 O O . ARG A 1 181 ? 8.945 21.706 -0.489 1.00 23.03 ? 181 ARG A O 1 ATOM 1401 C CB . ARG A 1 181 ? 9.529 24.491 -2.263 1.00 16.90 ? 181 ARG A CB 1 ATOM 1402 C CG . ARG A 1 181 ? 9.031 25.891 -2.610 1.00 20.02 ? 181 ARG A CG 1 ATOM 1403 C CD . ARG A 1 181 ? 9.883 27.018 -2.014 1.00 23.84 ? 181 ARG A CD 1 ATOM 1404 N NE . ARG A 1 181 ? 11.267 26.755 -2.422 1.00 28.47 ? 181 ARG A NE 1 ATOM 1405 C CZ . ARG A 1 181 ? 12.042 27.528 -3.176 1.00 25.80 ? 181 ARG A CZ 1 ATOM 1406 N NH1 . ARG A 1 181 ? 11.623 28.693 -3.651 1.00 26.63 ? 181 ARG A NH1 1 ATOM 1407 N NH2 . ARG A 1 181 ? 13.227 27.055 -3.565 1.00 22.47 ? 181 ARG A NH2 1 ATOM 1408 N N . SER A 1 182 ? 11.029 22.162 -0.946 1.00 18.97 ? 182 SER A N 1 ATOM 1409 C CA . SER A 1 182 ? 11.320 20.746 -0.878 1.00 17.84 ? 182 SER A CA 1 ATOM 1410 C C . SER A 1 182 ? 11.674 20.194 0.493 1.00 19.68 ? 182 SER A C 1 ATOM 1411 O O . SER A 1 182 ? 11.944 18.994 0.618 1.00 22.86 ? 182 SER A O 1 ATOM 1412 C CB . SER A 1 182 ? 12.447 20.410 -1.826 1.00 17.39 ? 182 SER A CB 1 ATOM 1413 O OG . SER A 1 182 ? 13.538 21.275 -1.567 1.00 20.10 ? 182 SER A OG 1 ATOM 1414 N N . LYS A 1 183 ? 11.642 21.004 1.564 1.00 20.13 ? 183 LYS A N 1 ATOM 1415 C CA . LYS A 1 183 ? 11.968 20.654 2.971 1.00 19.53 ? 183 LYS A CA 1 ATOM 1416 C C . LYS A 1 183 ? 13.356 20.052 3.135 1.00 19.35 ? 183 LYS A C 1 ATOM 1417 O O . LYS A 1 183 ? 13.599 19.020 3.758 1.00 20.15 ? 183 LYS A O 1 ATOM 1418 C CB . LYS A 1 183 ? 11.011 19.622 3.628 1.00 21.26 ? 183 LYS A CB 1 ATOM 1419 C CG . LYS A 1 183 ? 9.546 19.672 3.310 1.00 25.71 ? 183 LYS A CG 1 ATOM 1420 C CD . LYS A 1 183 ? 9.037 21.068 3.405 1.00 24.03 ? 183 LYS A CD 1 ATOM 1421 C CE . LYS A 1 183 ? 7.626 20.862 2.977 1.00 30.69 ? 183 LYS A CE 1 ATOM 1422 N NZ . LYS A 1 183 ? 6.971 22.132 3.142 1.00 34.17 ? 183 LYS A NZ 1 ATOM 1423 N N . ILE A 1 184 ? 14.323 20.687 2.501 1.00 17.91 ? 184 ILE A N 1 ATOM 1424 C CA . ILE A 1 184 ? 15.679 20.208 2.567 1.00 17.01 ? 184 ILE A CA 1 ATOM 1425 C C . ILE A 1 184 ? 16.651 21.181 3.255 1.00 17.78 ? 184 ILE A C 1 ATOM 1426 O O . ILE A 1 184 ? 16.704 22.379 2.941 1.00 17.03 ? 184 ILE A O 1 ATOM 1427 C CB . ILE A 1 184 ? 16.121 19.892 1.122 1.00 18.55 ? 184 ILE A CB 1 ATOM 1428 C CG1 . ILE A 1 184 ? 15.376 18.686 0.557 1.00 16.26 ? 184 ILE A CG1 1 ATOM 1429 C CG2 . ILE A 1 184 ? 17.595 19.571 1.119 1.00 17.56 ? 184 ILE A CG2 1 ATOM 1430 C CD1 . ILE A 1 184 ? 15.670 18.396 -0.952 1.00 12.28 ? 184 ILE A CD1 1 ATOM 1431 N N . LEU A 1 185 ? 17.392 20.641 4.227 1.00 17.05 ? 185 LEU A N 1 ATOM 1432 C CA . LEU A 1 185 ? 18.395 21.351 4.987 1.00 17.30 ? 185 LEU A CA 1 ATOM 1433 C C . LEU A 1 185 ? 19.747 20.821 4.501 1.00 17.22 ? 185 LEU A C 1 ATOM 1434 O O . LEU A 1 185 ? 19.975 19.602 4.460 1.00 16.96 ? 185 LEU A O 1 ATOM 1435 C CB . LEU A 1 185 ? 18.254 21.075 6.478 1.00 20.19 ? 185 LEU A CB 1 ATOM 1436 C CG . LEU A 1 185 ? 19.115 21.909 7.429 1.00 23.94 ? 185 LEU A CG 1 ATOM 1437 C CD1 . LEU A 1 185 ? 18.492 23.294 7.612 1.00 25.88 ? 185 LEU A CD1 1 ATOM 1438 C CD2 . LEU A 1 185 ? 19.139 21.260 8.791 1.00 25.21 ? 185 LEU A CD2 1 ATOM 1439 N N . THR A 1 186 ? 20.636 21.733 4.111 1.00 15.68 ? 186 THR A N 1 ATOM 1440 C CA . THR A 1 186 ? 21.983 21.404 3.603 1.00 14.54 ? 186 THR A CA 1 ATOM 1441 C C . THR A 1 186 ? 23.019 22.189 4.382 1.00 15.99 ? 186 THR A C 1 ATOM 1442 O O . THR A 1 186 ? 22.849 23.377 4.647 1.00 15.33 ? 186 THR A O 1 ATOM 1443 C CB . THR A 1 186 ? 22.238 21.781 2.086 1.00 15.27 ? 186 THR A CB 1 ATOM 1444 O OG1 . THR A 1 186 ? 21.321 20.986 1.335 1.00 14.23 ? 186 THR A OG1 1 ATOM 1445 C CG2 . THR A 1 186 ? 23.694 21.554 1.570 1.00 12.02 ? 186 THR A CG2 1 ATOM 1446 N N . VAL A 1 187 ? 24.103 21.503 4.715 1.00 15.47 ? 187 VAL A N 1 ATOM 1447 C CA . VAL A 1 187 ? 25.224 22.083 5.413 1.00 16.65 ? 187 VAL A CA 1 ATOM 1448 C C . VAL A 1 187 ? 26.476 21.902 4.532 1.00 15.30 ? 187 VAL A C 1 ATOM 1449 O O . VAL A 1 187 ? 26.794 20.827 4.006 1.00 14.70 ? 187 VAL A O 1 ATOM 1450 C CB . VAL A 1 187 ? 25.552 21.399 6.779 1.00 18.40 ? 187 VAL A CB 1 ATOM 1451 C CG1 . VAL A 1 187 ? 26.647 22.254 7.437 1.00 15.45 ? 187 VAL A CG1 1 ATOM 1452 C CG2 . VAL A 1 187 ? 24.302 21.202 7.623 1.00 18.69 ? 187 VAL A CG2 1 ATOM 1453 N N . LEU A 1 188 ? 27.191 22.990 4.354 1.00 15.36 ? 188 LEU A N 1 ATOM 1454 C CA . LEU A 1 188 ? 28.459 22.985 3.619 1.00 16.10 ? 188 LEU A CA 1 ATOM 1455 C C . LEU A 1 188 ? 29.496 23.604 4.548 1.00 16.17 ? 188 LEU A C 1 ATOM 1456 O O . LEU A 1 188 ? 29.323 24.704 5.073 1.00 16.43 ? 188 LEU A O 1 ATOM 1457 C CB . LEU A 1 188 ? 28.439 23.836 2.321 1.00 16.68 ? 188 LEU A CB 1 ATOM 1458 C CG . LEU A 1 188 ? 29.764 24.172 1.561 1.00 17.26 ? 188 LEU A CG 1 ATOM 1459 C CD1 . LEU A 1 188 ? 30.439 22.911 1.036 1.00 13.24 ? 188 LEU A CD1 1 ATOM 1460 C CD2 . LEU A 1 188 ? 29.424 25.158 0.446 1.00 13.24 ? 188 LEU A CD2 1 ATOM 1461 N N . LEU A 1 189 ? 30.566 22.877 4.801 1.00 14.45 ? 189 LEU A N 1 ATOM 1462 C CA . LEU A 1 189 ? 31.659 23.371 5.618 1.00 16.25 ? 189 LEU A CA 1 ATOM 1463 C C . LEU A 1 189 ? 32.937 23.338 4.753 1.00 18.85 ? 189 LEU A C 1 ATOM 1464 O O . LEU A 1 189 ? 33.320 22.328 4.164 1.00 19.09 ? 189 LEU A O 1 ATOM 1465 C CB . LEU A 1 189 ? 31.860 22.493 6.842 1.00 15.93 ? 189 LEU A CB 1 ATOM 1466 C CG . LEU A 1 189 ? 32.950 22.974 7.804 1.00 15.76 ? 189 LEU A CG 1 ATOM 1467 C CD1 . LEU A 1 189 ? 32.538 24.308 8.396 1.00 13.83 ? 189 LEU A CD1 1 ATOM 1468 C CD2 . LEU A 1 189 ? 33.149 21.956 8.890 1.00 13.08 ? 189 LEU A CD2 1 ATOM 1469 N N . SER A 1 190 ? 33.605 24.468 4.665 1.00 19.35 ? 190 SER A N 1 ATOM 1470 C CA . SER A 1 190 ? 34.824 24.629 3.882 1.00 21.24 ? 190 SER A CA 1 ATOM 1471 C C . SER A 1 190 ? 36.047 25.164 4.612 1.00 19.44 ? 190 SER A C 1 ATOM 1472 O O . SER A 1 190 ? 35.944 25.994 5.508 1.00 18.24 ? 190 SER A O 1 ATOM 1473 C CB . SER A 1 190 ? 34.653 25.590 2.709 1.00 19.74 ? 190 SER A CB 1 ATOM 1474 O OG . SER A 1 190 ? 33.549 25.193 1.915 1.00 27.50 ? 190 SER A OG 1 ATOM 1475 N N . TYR A 1 191 ? 37.226 24.644 4.318 1.00 20.34 ? 191 TYR A N 1 ATOM 1476 C CA . TYR A 1 191 ? 38.479 25.117 4.903 1.00 22.32 ? 191 TYR A CA 1 ATOM 1477 C C . TYR A 1 191 ? 39.230 25.622 3.696 1.00 24.21 ? 191 TYR A C 1 ATOM 1478 O O . TYR A 1 191 ? 39.342 24.960 2.669 1.00 20.96 ? 191 TYR A O 1 ATOM 1479 C CB . TYR A 1 191 ? 39.287 24.010 5.566 1.00 20.18 ? 191 TYR A CB 1 ATOM 1480 C CG . TYR A 1 191 ? 38.596 23.590 6.858 1.00 19.40 ? 191 TYR A CG 1 ATOM 1481 C CD1 . TYR A 1 191 ? 37.573 22.659 6.816 1.00 18.95 ? 191 TYR A CD1 1 ATOM 1482 C CD2 . TYR A 1 191 ? 38.980 24.174 8.040 1.00 17.16 ? 191 TYR A CD2 1 ATOM 1483 C CE1 . TYR A 1 191 ? 36.924 22.290 7.968 1.00 18.86 ? 191 TYR A CE1 1 ATOM 1484 C CE2 . TYR A 1 191 ? 38.347 23.813 9.202 1.00 19.69 ? 191 TYR A CE2 1 ATOM 1485 C CZ . TYR A 1 191 ? 37.325 22.876 9.147 1.00 21.59 ? 191 TYR A CZ 1 ATOM 1486 O OH . TYR A 1 191 ? 36.685 22.497 10.309 1.00 19.73 ? 191 TYR A OH 1 ATOM 1487 N N . GLU A 1 192 ? 39.757 26.808 3.850 1.00 29.71 ? 192 GLU A N 1 ATOM 1488 C CA . GLU A 1 192 ? 40.477 27.478 2.804 1.00 36.97 ? 192 GLU A CA 1 ATOM 1489 C C . GLU A 1 192 ? 41.491 26.673 2.044 1.00 38.05 ? 192 GLU A C 1 ATOM 1490 O O . GLU A 1 192 ? 41.490 26.699 0.807 1.00 41.81 ? 192 GLU A O 1 ATOM 1491 C CB . GLU A 1 192 ? 41.152 28.660 3.369 1.00 42.69 ? 192 GLU A CB 1 ATOM 1492 C CG . GLU A 1 192 ? 41.032 29.758 2.345 1.00 52.91 ? 192 GLU A CG 1 ATOM 1493 C CD . GLU A 1 192 ? 41.300 31.105 2.976 1.00 60.35 ? 192 GLU A CD 1 ATOM 1494 O OE1 . GLU A 1 192 ? 42.477 31.403 3.220 1.00 64.94 ? 192 GLU A OE1 1 ATOM 1495 O OE2 . GLU A 1 192 ? 40.324 31.827 3.236 1.00 65.06 ? 192 GLU A OE2 1 ATOM 1496 N N . HIS A 1 193 ? 42.421 25.981 2.646 1.00 38.27 ? 193 HIS A N 1 ATOM 1497 C CA . HIS A 1 193 ? 43.264 25.227 1.698 1.00 41.70 ? 193 HIS A CA 1 ATOM 1498 C C . HIS A 1 193 ? 43.088 23.746 1.946 1.00 41.12 ? 193 HIS A C 1 ATOM 1499 O O . HIS A 1 193 ? 43.982 22.905 1.801 1.00 42.60 ? 193 HIS A O 1 ATOM 1500 C CB . HIS A 1 193 ? 44.745 25.624 1.849 1.00 48.42 ? 193 HIS A CB 1 ATOM 1501 C CG . HIS A 1 193 ? 44.922 27.067 1.411 1.00 51.82 ? 193 HIS A CG 1 ATOM 1502 N ND1 . HIS A 1 193 ? 44.798 27.557 0.172 1.00 52.55 ? 193 HIS A ND1 1 ATOM 1503 C CD2 . HIS A 1 193 ? 45.133 28.111 2.285 1.00 53.24 ? 193 HIS A CD2 1 ATOM 1504 C CE1 . HIS A 1 193 ? 44.907 28.856 0.248 1.00 52.96 ? 193 HIS A CE1 1 ATOM 1505 N NE2 . HIS A 1 193 ? 45.106 29.169 1.514 1.00 55.91 ? 193 HIS A NE2 1 ATOM 1506 N N . GLY A 1 194 ? 41.849 23.449 2.308 1.00 38.18 ? 194 GLY A N 1 ATOM 1507 C CA . GLY A 1 194 ? 41.543 22.083 2.635 1.00 32.30 ? 194 GLY A CA 1 ATOM 1508 C C . GLY A 1 194 ? 40.380 21.517 1.883 1.00 28.75 ? 194 GLY A C 1 ATOM 1509 O O . GLY A 1 194 ? 40.066 21.886 0.758 1.00 32.25 ? 194 GLY A O 1 ATOM 1510 N N . ARG A 1 195 ? 39.661 20.677 2.595 1.00 25.80 ? 195 ARG A N 1 ATOM 1511 C CA . ARG A 1 195 ? 38.523 20.009 2.009 1.00 20.00 ? 195 ARG A CA 1 ATOM 1512 C C . ARG A 1 195 ? 37.212 20.650 2.411 1.00 18.17 ? 195 ARG A C 1 ATOM 1513 O O . ARG A 1 195 ? 37.127 21.599 3.200 1.00 17.47 ? 195 ARG A O 1 ATOM 1514 C CB . ARG A 1 195 ? 38.601 18.554 2.434 1.00 17.24 ? 195 ARG A CB 1 ATOM 1515 C CG . ARG A 1 195 ? 38.479 18.294 3.925 1.00 16.22 ? 195 ARG A CG 1 ATOM 1516 C CD . ARG A 1 195 ? 38.120 16.838 4.093 1.00 18.15 ? 195 ARG A CD 1 ATOM 1517 N NE . ARG A 1 195 ? 36.772 16.654 3.582 1.00 20.78 ? 195 ARG A NE 1 ATOM 1518 C CZ . ARG A 1 195 ? 36.072 15.510 3.633 1.00 21.42 ? 195 ARG A CZ 1 ATOM 1519 N NH1 . ARG A 1 195 ? 36.527 14.372 4.161 1.00 21.04 ? 195 ARG A NH1 1 ATOM 1520 N NH2 . ARG A 1 195 ? 34.826 15.523 3.187 1.00 18.91 ? 195 ARG A NH2 1 ATOM 1521 N N . ASP A 1 196 ? 36.209 20.119 1.761 1.00 15.78 ? 196 ASP A N 1 ATOM 1522 C CA . ASP A 1 196 ? 34.846 20.549 1.998 1.00 15.88 ? 196 ASP A CA 1 ATOM 1523 C C . ASP A 1 196 ? 34.071 19.384 2.602 1.00 14.94 ? 196 ASP A C 1 ATOM 1524 O O . ASP A 1 196 ? 34.417 18.218 2.446 1.00 15.37 ? 196 ASP A O 1 ATOM 1525 C CB . ASP A 1 196 ? 34.146 20.961 0.701 1.00 13.63 ? 196 ASP A CB 1 ATOM 1526 C CG . ASP A 1 196 ? 34.818 22.081 -0.056 1.00 16.21 ? 196 ASP A CG 1 ATOM 1527 O OD1 . ASP A 1 196 ? 35.251 23.052 0.529 1.00 16.53 ? 196 ASP A OD1 1 ATOM 1528 O OD2 . ASP A 1 196 ? 34.904 21.996 -1.267 1.00 18.42 ? 196 ASP A OD2 1 ATOM 1529 N N . TYR A 1 197 ? 33.000 19.705 3.285 1.00 14.15 ? 197 TYR A N 1 ATOM 1530 C CA . TYR A 1 197 ? 32.137 18.726 3.924 1.00 13.76 ? 197 TYR A CA 1 ATOM 1531 C C . TYR A 1 197 ? 30.719 19.066 3.521 1.00 14.53 ? 197 TYR A C 1 ATOM 1532 O O . TYR A 1 197 ? 30.281 20.216 3.585 1.00 15.32 ? 197 TYR A O 1 ATOM 1533 C CB . TYR A 1 197 ? 32.277 18.817 5.434 1.00 16.79 ? 197 TYR A CB 1 ATOM 1534 C CG . TYR A 1 197 ? 33.669 18.449 5.939 1.00 19.32 ? 197 TYR A CG 1 ATOM 1535 C CD1 . TYR A 1 197 ? 33.906 17.110 6.184 1.00 15.45 ? 197 TYR A CD1 1 ATOM 1536 C CD2 . TYR A 1 197 ? 34.645 19.430 6.168 1.00 17.17 ? 197 TYR A CD2 1 ATOM 1537 C CE1 . TYR A 1 197 ? 35.115 16.741 6.686 1.00 17.59 ? 197 TYR A CE1 1 ATOM 1538 C CE2 . TYR A 1 197 ? 35.869 19.053 6.670 1.00 15.29 ? 197 TYR A CE2 1 ATOM 1539 C CZ . TYR A 1 197 ? 36.072 17.705 6.917 1.00 16.10 ? 197 TYR A CZ 1 ATOM 1540 O OH . TYR A 1 197 ? 37.251 17.264 7.467 1.00 17.70 ? 197 TYR A OH 1 ATOM 1541 N N . ILE A 1 198 ? 29.975 18.051 3.117 1.00 14.63 ? 198 ILE A N 1 ATOM 1542 C CA . ILE A 1 198 ? 28.618 18.204 2.616 1.00 13.89 ? 198 ILE A CA 1 ATOM 1543 C C . ILE A 1 198 ? 27.663 17.313 3.378 1.00 14.34 ? 198 ILE A C 1 ATOM 1544 O O . ILE A 1 198 ? 27.956 16.136 3.558 1.00 14.90 ? 198 ILE A O 1 ATOM 1545 C CB . ILE A 1 198 ? 28.534 17.831 1.051 1.00 14.73 ? 198 ILE A CB 1 ATOM 1546 C CG1 . ILE A 1 198 ? 29.539 18.641 0.223 1.00 13.55 ? 198 ILE A CG1 1 ATOM 1547 C CG2 . ILE A 1 198 ? 27.130 18.099 0.501 1.00 14.20 ? 198 ILE A CG2 1 ATOM 1548 C CD1 . ILE A 1 198 ? 30.858 17.897 -0.054 1.00 12.94 ? 198 ILE A CD1 1 ATOM 1549 N N . LEU A 1 199 ? 26.551 17.836 3.890 1.00 13.77 ? 199 LEU A N 1 ATOM 1550 C CA . LEU A 1 199 ? 25.591 16.992 4.564 1.00 14.77 ? 199 LEU A CA 1 ATOM 1551 C C . LEU A 1 199 ? 24.231 17.592 4.321 1.00 15.49 ? 199 LEU A C 1 ATOM 1552 O O . LEU A 1 199 ? 24.007 18.749 4.652 1.00 16.37 ? 199 LEU A O 1 ATOM 1553 C CB . LEU A 1 199 ? 25.814 16.907 6.073 1.00 13.82 ? 199 LEU A CB 1 ATOM 1554 C CG . LEU A 1 199 ? 24.773 16.027 6.823 1.00 13.34 ? 199 LEU A CG 1 ATOM 1555 C CD1 . LEU A 1 199 ? 24.955 14.557 6.512 1.00 12.53 ? 199 LEU A CD1 1 ATOM 1556 C CD2 . LEU A 1 199 ? 24.949 16.228 8.288 1.00 11.33 ? 199 LEU A CD2 1 ATOM 1557 N N . SER A 1 200 ? 23.291 16.849 3.741 1.00 16.10 ? 200 SER A N 1 ATOM 1558 C CA . SER A 1 200 ? 21.955 17.359 3.462 1.00 16.46 ? 200 SER A CA 1 ATOM 1559 C C . SER A 1 200 ? 20.940 16.348 3.939 1.00 17.25 ? 200 SER A C 1 ATOM 1560 O O . SER A 1 200 ? 21.169 15.133 3.924 1.00 17.25 ? 200 SER A O 1 ATOM 1561 C CB . SER A 1 200 ? 21.627 17.554 2.001 1.00 14.54 ? 200 SER A CB 1 ATOM 1562 O OG . SER A 1 200 ? 22.529 18.416 1.344 1.00 15.40 ? 200 SER A OG 1 ATOM 1563 N N . HIS A 1 201 ? 19.788 16.817 4.356 1.00 16.78 ? 201 HIS A N 1 ATOM 1564 C CA . HIS A 1 201 ? 18.760 15.919 4.835 1.00 16.57 ? 201 HIS A CA 1 ATOM 1565 C C . HIS A 1 201 ? 17.374 16.523 4.709 1.00 17.98 ? 201 HIS A C 1 ATOM 1566 O O . HIS A 1 201 ? 17.180 17.740 4.844 1.00 16.85 ? 201 HIS A O 1 ATOM 1567 C CB . HIS A 1 201 ? 19.057 15.571 6.315 1.00 20.45 ? 201 HIS A CB 1 ATOM 1568 C CG . HIS A 1 201 ? 18.326 14.333 6.803 1.00 22.26 ? 201 HIS A CG 1 ATOM 1569 N ND1 . HIS A 1 201 ? 18.629 13.073 6.515 1.00 25.84 ? 201 HIS A ND1 1 ATOM 1570 C CD2 . HIS A 1 201 ? 17.192 14.341 7.581 1.00 25.52 ? 201 HIS A CD2 1 ATOM 1571 C CE1 . HIS A 1 201 ? 17.722 12.316 7.081 1.00 25.29 ? 201 HIS A CE1 1 ATOM 1572 N NE2 . HIS A 1 201 ? 16.877 13.089 7.708 1.00 26.85 ? 201 HIS A NE2 1 ATOM 1573 N N . VAL A 1 202 ? 16.386 15.686 4.421 1.00 17.10 ? 202 VAL A N 1 ATOM 1574 C CA . VAL A 1 202 ? 15.036 16.199 4.342 1.00 19.92 ? 202 VAL A CA 1 ATOM 1575 C C . VAL A 1 202 ? 14.511 16.435 5.768 1.00 22.27 ? 202 VAL A C 1 ATOM 1576 O O . VAL A 1 202 ? 14.666 15.568 6.635 1.00 23.07 ? 202 VAL A O 1 ATOM 1577 C CB . VAL A 1 202 ? 14.103 15.190 3.590 1.00 18.58 ? 202 VAL A CB 1 ATOM 1578 C CG1 . VAL A 1 202 ? 12.646 15.639 3.575 1.00 20.10 ? 202 VAL A CG1 1 ATOM 1579 C CG2 . VAL A 1 202 ? 14.542 15.115 2.150 1.00 18.50 ? 202 VAL A CG2 1 ATOM 1580 N N . VAL A 1 203 ? 14.011 17.623 6.099 1.00 23.00 ? 203 VAL A N 1 ATOM 1581 C CA . VAL A 1 203 ? 13.412 17.947 7.395 1.00 26.99 ? 203 VAL A CA 1 ATOM 1582 C C . VAL A 1 203 ? 12.442 19.113 7.185 1.00 27.29 ? 203 VAL A C 1 ATOM 1583 O O . VAL A 1 203 ? 12.779 20.169 6.649 1.00 25.92 ? 203 VAL A O 1 ATOM 1584 C CB . VAL A 1 203 ? 14.464 18.339 8.555 1.00 30.39 ? 203 VAL A CB 1 ATOM 1585 C CG1 . VAL A 1 203 ? 15.345 19.524 8.242 1.00 31.30 ? 203 VAL A CG1 1 ATOM 1586 C CG2 . VAL A 1 203 ? 13.644 18.687 9.817 1.00 30.20 ? 203 VAL A CG2 1 ATOM 1587 N N . ASP A 1 204 ? 11.172 18.895 7.537 1.00 26.79 ? 204 ASP A N 1 ATOM 1588 C CA . ASP A 1 204 ? 10.142 19.908 7.398 1.00 25.66 ? 204 ASP A CA 1 ATOM 1589 C C . ASP A 1 204 ? 10.068 20.707 8.675 1.00 25.86 ? 204 ASP A C 1 ATOM 1590 O O . ASP A 1 204 ? 9.464 20.284 9.662 1.00 25.78 ? 204 ASP A O 1 ATOM 1591 C CB . ASP A 1 204 ? 8.779 19.269 7.138 1.00 28.98 ? 204 ASP A CB 1 ATOM 1592 C CG . ASP A 1 204 ? 7.653 20.217 6.741 1.00 29.08 ? 204 ASP A CG 1 ATOM 1593 O OD1 . ASP A 1 204 ? 7.745 21.429 6.907 1.00 31.22 ? 204 ASP A OD1 1 ATOM 1594 O OD2 . ASP A 1 204 ? 6.660 19.722 6.221 1.00 34.51 ? 204 ASP A OD2 1 ATOM 1595 N N . LEU A 1 205 ? 10.650 21.895 8.612 1.00 25.09 ? 205 LEU A N 1 ATOM 1596 C CA . LEU A 1 205 ? 10.698 22.800 9.740 1.00 24.91 ? 205 LEU A CA 1 ATOM 1597 C C . LEU A 1 205 ? 9.338 23.174 10.319 1.00 25.72 ? 205 LEU A C 1 ATOM 1598 O O . LEU A 1 205 ? 9.166 23.280 11.526 1.00 23.89 ? 205 LEU A O 1 ATOM 1599 C CB . LEU A 1 205 ? 11.486 24.022 9.268 1.00 24.44 ? 205 LEU A CB 1 ATOM 1600 C CG . LEU A 1 205 ? 12.932 24.111 9.725 1.00 27.52 ? 205 LEU A CG 1 ATOM 1601 C CD1 . LEU A 1 205 ? 13.653 22.767 9.632 1.00 28.70 ? 205 LEU A CD1 1 ATOM 1602 C CD2 . LEU A 1 205 ? 13.569 25.225 8.929 1.00 26.22 ? 205 LEU A CD2 1 ATOM 1603 N N . ALA A 1 206 ? 8.375 23.362 9.418 1.00 28.53 ? 206 ALA A N 1 ATOM 1604 C CA . ALA A 1 206 ? 6.975 23.667 9.734 1.00 29.43 ? 206 ALA A CA 1 ATOM 1605 C C . ALA A 1 206 ? 6.371 22.604 10.654 1.00 29.25 ? 206 ALA A C 1 ATOM 1606 O O . ALA A 1 206 ? 5.628 22.859 11.587 1.00 32.08 ? 206 ALA A O 1 ATOM 1607 C CB . ALA A 1 206 ? 6.136 23.696 8.459 1.00 28.48 ? 206 ALA A CB 1 ATOM 1608 N N . LYS A 1 207 ? 6.767 21.363 10.456 1.00 29.98 ? 207 LYS A N 1 ATOM 1609 C CA . LYS A 1 207 ? 6.293 20.284 11.288 1.00 32.29 ? 207 LYS A CA 1 ATOM 1610 C C . LYS A 1 207 ? 7.019 20.184 12.609 1.00 31.90 ? 207 LYS A C 1 ATOM 1611 O O . LYS A 1 207 ? 6.478 19.544 13.494 1.00 32.18 ? 207 LYS A O 1 ATOM 1612 C CB . LYS A 1 207 ? 6.462 18.926 10.659 1.00 38.10 ? 207 LYS A CB 1 ATOM 1613 C CG . LYS A 1 207 ? 5.468 18.664 9.546 1.00 48.81 ? 207 LYS A CG 1 ATOM 1614 C CD . LYS A 1 207 ? 5.732 17.215 9.163 1.00 56.22 ? 207 LYS A CD 1 ATOM 1615 C CE . LYS A 1 207 ? 4.906 16.824 7.954 1.00 61.21 ? 207 LYS A CE 1 ATOM 1616 N NZ . LYS A 1 207 ? 4.997 15.385 7.759 1.00 67.34 ? 207 LYS A NZ 1 ATOM 1617 N N . VAL A 1 208 ? 8.228 20.715 12.817 1.00 29.57 ? 208 VAL A N 1 ATOM 1618 C CA . VAL A 1 208 ? 8.889 20.580 14.110 1.00 28.35 ? 208 VAL A CA 1 ATOM 1619 C C . VAL A 1 208 ? 9.122 21.841 14.932 1.00 27.70 ? 208 VAL A C 1 ATOM 1620 O O . VAL A 1 208 ? 9.383 21.769 16.137 1.00 29.87 ? 208 VAL A O 1 ATOM 1621 C CB . VAL A 1 208 ? 10.255 19.856 13.943 1.00 29.25 ? 208 VAL A CB 1 ATOM 1622 C CG1 . VAL A 1 208 ? 9.944 18.400 13.664 1.00 27.73 ? 208 VAL A CG1 1 ATOM 1623 C CG2 . VAL A 1 208 ? 11.101 20.446 12.822 1.00 27.29 ? 208 VAL A CG2 1 ATOM 1624 N N . LEU A 1 209 ? 8.995 23.024 14.342 1.00 23.51 ? 209 LEU A N 1 ATOM 1625 C CA . LEU A 1 209 ? 9.240 24.250 15.054 1.00 23.34 ? 209 LEU A CA 1 ATOM 1626 C C . LEU A 1 209 ? 8.041 25.159 15.005 1.00 23.44 ? 209 LEU A C 1 ATOM 1627 O O . LEU A 1 209 ? 7.249 25.033 14.072 1.00 25.16 ? 209 LEU A O 1 ATOM 1628 C CB . LEU A 1 209 ? 10.422 24.943 14.428 1.00 21.38 ? 209 LEU A CB 1 ATOM 1629 C CG . LEU A 1 209 ? 11.761 24.280 14.655 1.00 20.25 ? 209 LEU A CG 1 ATOM 1630 C CD1 . LEU A 1 209 ? 12.754 24.820 13.647 1.00 17.06 ? 209 LEU A CD1 1 ATOM 1631 C CD2 . LEU A 1 209 ? 12.200 24.519 16.081 1.00 20.92 ? 209 LEU A CD2 1 ATOM 1632 N N . PRO A 1 210 ? 7.826 26.066 15.952 1.00 23.38 ? 210 PRO A N 1 ATOM 1633 C CA . PRO A 1 210 ? 6.770 27.064 15.840 1.00 24.63 ? 210 PRO A CA 1 ATOM 1634 C C . PRO A 1 210 ? 6.960 28.036 14.684 1.00 26.04 ? 210 PRO A C 1 ATOM 1635 O O . PRO A 1 210 ? 8.019 28.139 14.056 1.00 24.99 ? 210 PRO A O 1 ATOM 1636 C CB . PRO A 1 210 ? 6.748 27.763 17.174 1.00 24.18 ? 210 PRO A CB 1 ATOM 1637 C CG . PRO A 1 210 ? 8.166 27.563 17.680 1.00 25.72 ? 210 PRO A CG 1 ATOM 1638 C CD . PRO A 1 210 ? 8.534 26.144 17.222 1.00 22.83 ? 210 PRO A CD 1 ATOM 1639 N N . GLN A 1 211 ? 5.915 28.786 14.413 1.00 26.06 ? 211 GLN A N 1 ATOM 1640 C CA . GLN A 1 211 ? 5.910 29.759 13.346 1.00 29.04 ? 211 GLN A CA 1 ATOM 1641 C C . GLN A 1 211 ? 6.978 30.834 13.409 1.00 28.12 ? 211 GLN A C 1 ATOM 1642 O O . GLN A 1 211 ? 7.355 31.409 12.392 1.00 28.55 ? 211 GLN A O 1 ATOM 1643 C CB . GLN A 1 211 ? 4.586 30.432 13.313 1.00 33.71 ? 211 GLN A CB 1 ATOM 1644 C CG . GLN A 1 211 ? 3.516 29.409 13.071 1.00 41.02 ? 211 GLN A CG 1 ATOM 1645 C CD . GLN A 1 211 ? 2.140 30.016 13.182 1.00 46.23 ? 211 GLN A CD 1 ATOM 1646 O OE1 . GLN A 1 211 ? 1.417 29.751 14.137 1.00 51.82 ? 211 GLN A OE1 1 ATOM 1647 N NE2 . GLN A 1 211 ? 1.732 30.896 12.290 1.00 46.78 ? 211 GLN A NE2 1 ATOM 1648 N N . LYS A 1 212 ? 7.417 31.203 14.599 1.00 26.72 ? 212 LYS A N 1 ATOM 1649 C CA . LYS A 1 212 ? 8.469 32.199 14.720 1.00 26.76 ? 212 LYS A CA 1 ATOM 1650 C C . LYS A 1 212 ? 9.557 31.604 15.598 1.00 26.39 ? 212 LYS A C 1 ATOM 1651 O O . LYS A 1 212 ? 9.262 31.019 16.649 1.00 26.23 ? 212 LYS A O 1 ATOM 1652 C CB . LYS A 1 212 ? 7.965 33.442 15.360 1.00 30.05 ? 212 LYS A CB 1 ATOM 1653 C CG . LYS A 1 212 ? 7.332 34.441 14.417 1.00 35.31 ? 212 LYS A CG 1 ATOM 1654 C CD . LYS A 1 212 ? 7.215 35.616 15.371 1.00 47.71 ? 212 LYS A CD 1 ATOM 1655 C CE . LYS A 1 212 ? 6.991 36.990 14.717 1.00 56.33 ? 212 LYS A CE 1 ATOM 1656 N NZ . LYS A 1 212 ? 7.049 38.056 15.730 1.00 60.92 ? 212 LYS A NZ 1 ATOM 1657 N N . VAL A 1 213 ? 10.834 31.718 15.237 1.00 24.85 ? 213 VAL A N 1 ATOM 1658 C CA . VAL A 1 213 ? 11.905 31.117 16.053 1.00 20.75 ? 213 VAL A CA 1 ATOM 1659 C C . VAL A 1 213 ? 13.051 32.060 16.399 1.00 20.60 ? 213 VAL A C 1 ATOM 1660 O O . VAL A 1 213 ? 13.039 33.230 16.017 1.00 21.88 ? 213 VAL A O 1 ATOM 1661 C CB . VAL A 1 213 ? 12.513 29.856 15.321 1.00 17.85 ? 213 VAL A CB 1 ATOM 1662 C CG1 . VAL A 1 213 ? 11.486 28.692 15.206 1.00 16.04 ? 213 VAL A CG1 1 ATOM 1663 C CG2 . VAL A 1 213 ? 13.037 30.311 13.957 1.00 15.72 ? 213 VAL A CG2 1 ATOM 1664 N N . ARG A 1 214 ? 13.967 31.655 17.255 1.00 19.87 ? 214 ARG A N 1 ATOM 1665 C CA . ARG A 1 214 ? 15.146 32.479 17.492 1.00 21.90 ? 214 ARG A CA 1 ATOM 1666 C C . ARG A 1 214 ? 16.262 31.640 16.827 1.00 19.16 ? 214 ARG A C 1 ATOM 1667 O O . ARG A 1 214 ? 16.227 30.393 16.767 1.00 17.88 ? 214 ARG A O 1 ATOM 1668 C CB . ARG A 1 214 ? 15.485 32.704 18.999 1.00 22.38 ? 214 ARG A CB 1 ATOM 1669 C CG . ARG A 1 214 ? 15.685 31.495 19.914 1.00 25.46 ? 214 ARG A CG 1 ATOM 1670 C CD . ARG A 1 214 ? 15.802 31.862 21.428 1.00 23.30 ? 214 ARG A CD 1 ATOM 1671 N NE . ARG A 1 214 ? 17.177 32.105 21.799 1.00 25.37 ? 214 ARG A NE 1 ATOM 1672 C CZ . ARG A 1 214 ? 17.990 31.193 22.340 1.00 18.77 ? 214 ARG A CZ 1 ATOM 1673 N NH1 . ARG A 1 214 ? 17.638 29.944 22.668 1.00 19.08 ? 214 ARG A NH1 1 ATOM 1674 N NH2 . ARG A 1 214 ? 19.216 31.610 22.566 1.00 19.44 ? 214 ARG A NH2 1 ATOM 1675 N N . ILE A 1 215 ? 17.221 32.335 16.238 1.00 18.63 ? 215 ILE A N 1 ATOM 1676 C CA . ILE A 1 215 ? 18.343 31.678 15.570 1.00 17.73 ? 215 ILE A CA 1 ATOM 1677 C C . ILE A 1 215 ? 19.672 32.019 16.197 1.00 17.96 ? 215 ILE A C 1 ATOM 1678 O O . ILE A 1 215 ? 19.871 33.114 16.719 1.00 20.85 ? 215 ILE A O 1 ATOM 1679 C CB . ILE A 1 215 ? 18.428 32.038 14.037 1.00 16.76 ? 215 ILE A CB 1 ATOM 1680 C CG1 . ILE A 1 215 ? 18.548 33.532 13.823 1.00 19.09 ? 215 ILE A CG1 1 ATOM 1681 C CG2 . ILE A 1 215 ? 17.168 31.505 13.321 1.00 18.34 ? 215 ILE A CG2 1 ATOM 1682 C CD1 . ILE A 1 215 ? 18.728 33.951 12.335 1.00 20.29 ? 215 ILE A CD1 1 ATOM 1683 N N . GLY A 1 216 ? 20.633 31.135 16.209 1.00 15.53 ? 216 GLY A N 1 ATOM 1684 C CA . GLY A 1 216 ? 21.893 31.529 16.809 1.00 14.30 ? 216 GLY A CA 1 ATOM 1685 C C . GLY A 1 216 ? 22.870 30.408 16.915 1.00 14.90 ? 216 GLY A C 1 ATOM 1686 O O . GLY A 1 216 ? 22.705 29.352 16.296 1.00 16.21 ? 216 GLY A O 1 ATOM 1687 N N . PHE A 1 217 ? 23.873 30.631 17.738 1.00 13.24 ? 217 PHE A N 1 ATOM 1688 C CA . PHE A 1 217 ? 24.937 29.675 17.947 1.00 14.13 ? 217 PHE A CA 1 ATOM 1689 C C . PHE A 1 217 ? 24.925 29.178 19.369 1.00 18.46 ? 217 PHE A C 1 ATOM 1690 O O . PHE A 1 217 ? 24.701 29.959 20.288 1.00 20.50 ? 217 PHE A O 1 ATOM 1691 C CB . PHE A 1 217 ? 26.289 30.305 17.702 1.00 13.56 ? 217 PHE A CB 1 ATOM 1692 C CG . PHE A 1 217 ? 26.366 30.858 16.289 1.00 15.59 ? 217 PHE A CG 1 ATOM 1693 C CD1 . PHE A 1 217 ? 26.635 30.007 15.234 1.00 15.33 ? 217 PHE A CD1 1 ATOM 1694 C CD2 . PHE A 1 217 ? 26.092 32.202 16.076 1.00 15.67 ? 217 PHE A CD2 1 ATOM 1695 C CE1 . PHE A 1 217 ? 26.613 30.516 13.963 1.00 15.86 ? 217 PHE A CE1 1 ATOM 1696 C CE2 . PHE A 1 217 ? 26.073 32.696 14.796 1.00 13.09 ? 217 PHE A CE2 1 ATOM 1697 C CZ . PHE A 1 217 ? 26.331 31.855 13.746 1.00 14.11 ? 217 PHE A CZ 1 ATOM 1698 N N . SER A 1 218 ? 25.158 27.905 19.617 1.00 20.68 ? 218 SER A N 1 ATOM 1699 C CA . SER A 1 218 ? 25.171 27.372 20.963 1.00 18.94 ? 218 SER A CA 1 ATOM 1700 C C . SER A 1 218 ? 26.366 26.474 21.133 1.00 20.89 ? 218 SER A C 1 ATOM 1701 O O . SER A 1 218 ? 26.763 25.779 20.195 1.00 22.85 ? 218 SER A O 1 ATOM 1702 C CB . SER A 1 218 ? 23.967 26.513 21.259 1.00 18.90 ? 218 SER A CB 1 ATOM 1703 O OG . SER A 1 218 ? 23.796 26.307 22.657 1.00 18.03 ? 218 SER A OG 1 ATOM 1704 N N . ALA A 1 219 ? 27.046 26.527 22.258 1.00 20.77 ? 219 ALA A N 1 ATOM 1705 C CA . ALA A 1 219 ? 28.178 25.632 22.465 1.00 20.43 ? 219 ALA A CA 1 ATOM 1706 C C . ALA A 1 219 ? 28.108 25.085 23.893 1.00 21.43 ? 219 ALA A C 1 ATOM 1707 O O . ALA A 1 219 ? 27.471 25.632 24.811 1.00 21.95 ? 219 ALA A O 1 ATOM 1708 C CB . ALA A 1 219 ? 29.564 26.319 22.315 1.00 17.92 ? 219 ALA A CB 1 ATOM 1709 N N . GLY A 1 220 ? 28.762 23.942 24.010 1.00 19.71 ? 220 GLY A N 1 ATOM 1710 C CA . GLY A 1 220 ? 28.859 23.251 25.249 1.00 20.67 ? 220 GLY A CA 1 ATOM 1711 C C . GLY A 1 220 ? 30.236 22.630 25.363 1.00 22.19 ? 220 GLY A C 1 ATOM 1712 O O . GLY A 1 220 ? 30.808 22.153 24.389 1.00 22.65 ? 220 GLY A O 1 ATOM 1713 N N . VAL A 1 221 ? 30.872 22.767 26.524 1.00 22.68 ? 221 VAL A N 1 ATOM 1714 C CA . VAL A 1 221 ? 32.173 22.149 26.796 1.00 21.54 ? 221 VAL A CA 1 ATOM 1715 C C . VAL A 1 221 ? 32.019 21.443 28.149 1.00 22.97 ? 221 VAL A C 1 ATOM 1716 O O . VAL A 1 221 ? 31.145 21.785 28.959 1.00 23.42 ? 221 VAL A O 1 ATOM 1717 C CB . VAL A 1 221 ? 33.393 23.151 26.896 1.00 20.48 ? 221 VAL A CB 1 ATOM 1718 C CG1 . VAL A 1 221 ? 33.582 23.721 25.490 1.00 21.70 ? 221 VAL A CG1 1 ATOM 1719 C CG2 . VAL A 1 221 ? 33.233 24.218 27.970 1.00 16.92 ? 221 VAL A CG2 1 ATOM 1720 N N . GLY A 1 222 ? 32.774 20.450 28.543 1.00 20.65 ? 222 GLY A N 1 ATOM 1721 C CA . GLY A 1 222 ? 33.870 19.895 27.767 1.00 22.43 ? 222 GLY A CA 1 ATOM 1722 C C . GLY A 1 222 ? 35.210 20.385 28.301 1.00 24.94 ? 222 GLY A C 1 ATOM 1723 O O . GLY A 1 222 ? 35.300 20.859 29.440 1.00 27.32 ? 222 GLY A O 1 ATOM 1724 N N . TYR A 1 223 ? 36.240 20.346 27.485 1.00 23.97 ? 223 TYR A N 1 ATOM 1725 C CA . TYR A 1 223 ? 37.544 20.762 27.936 1.00 26.52 ? 223 TYR A CA 1 ATOM 1726 C C . TYR A 1 223 ? 38.462 21.089 26.770 1.00 27.11 ? 223 TYR A C 1 ATOM 1727 O O . TYR A 1 223 ? 38.251 20.591 25.647 1.00 27.12 ? 223 TYR A O 1 ATOM 1728 C CB . TYR A 1 223 ? 38.196 19.634 28.797 1.00 25.07 ? 223 TYR A CB 1 ATOM 1729 C CG . TYR A 1 223 ? 38.584 18.361 28.056 1.00 25.58 ? 223 TYR A CG 1 ATOM 1730 C CD1 . TYR A 1 223 ? 37.620 17.433 27.754 1.00 27.91 ? 223 TYR A CD1 1 ATOM 1731 C CD2 . TYR A 1 223 ? 39.885 18.174 27.619 1.00 28.32 ? 223 TYR A CD2 1 ATOM 1732 C CE1 . TYR A 1 223 ? 37.956 16.333 27.003 1.00 29.80 ? 223 TYR A CE1 1 ATOM 1733 C CE2 . TYR A 1 223 ? 40.234 17.073 26.867 1.00 27.11 ? 223 TYR A CE2 1 ATOM 1734 C CZ . TYR A 1 223 ? 39.246 16.172 26.569 1.00 29.94 ? 223 TYR A CZ 1 ATOM 1735 O OH . TYR A 1 223 ? 39.520 15.087 25.779 1.00 35.60 ? 223 TYR A OH 1 ATOM 1736 N N . ASP A 1 224 ? 39.497 21.888 27.051 1.00 26.58 ? 224 ASP A N 1 ATOM 1737 C CA . ASP A 1 224 ? 40.510 22.284 26.067 1.00 25.79 ? 224 ASP A CA 1 ATOM 1738 C C . ASP A 1 224 ? 40.011 22.844 24.732 1.00 25.51 ? 224 ASP A C 1 ATOM 1739 O O . ASP A 1 224 ? 40.613 22.729 23.660 1.00 24.44 ? 224 ASP A O 1 ATOM 1740 C CB . ASP A 1 224 ? 41.411 21.071 25.808 1.00 25.12 ? 224 ASP A CB 1 ATOM 1741 C CG . ASP A 1 224 ? 42.461 20.792 26.875 1.00 26.28 ? 224 ASP A CG 1 ATOM 1742 O OD1 . ASP A 1 224 ? 42.616 21.607 27.775 1.00 28.78 ? 224 ASP A OD1 1 ATOM 1743 O OD2 . ASP A 1 224 ? 43.146 19.773 26.771 1.00 28.55 ? 224 ASP A OD2 1 ATOM 1744 N N . GLU A 1 225 ? 38.905 23.540 24.824 1.00 24.59 ? 225 GLU A N 1 ATOM 1745 C CA . GLU A 1 225 ? 38.289 24.065 23.633 1.00 24.16 ? 225 GLU A CA 1 ATOM 1746 C C . GLU A 1 225 ? 37.433 25.285 23.868 1.00 22.57 ? 225 GLU A C 1 ATOM 1747 O O . GLU A 1 225 ? 36.861 25.439 24.944 1.00 22.50 ? 225 GLU A O 1 ATOM 1748 C CB . GLU A 1 225 ? 37.463 22.891 23.058 1.00 25.99 ? 225 GLU A CB 1 ATOM 1749 C CG . GLU A 1 225 ? 36.496 23.198 21.954 1.00 25.85 ? 225 GLU A CG 1 ATOM 1750 C CD . GLU A 1 225 ? 35.406 22.180 21.708 1.00 23.73 ? 225 GLU A CD 1 ATOM 1751 O OE1 . GLU A 1 225 ? 35.752 21.039 21.456 1.00 21.66 ? 225 GLU A OE1 1 ATOM 1752 O OE2 . GLU A 1 225 ? 34.231 22.552 21.734 1.00 22.18 ? 225 GLU A OE2 1 ATOM 1753 N N . VAL A 1 226 ? 37.398 26.168 22.883 1.00 20.75 ? 226 VAL A N 1 ATOM 1754 C CA . VAL A 1 226 ? 36.541 27.334 22.935 1.00 22.21 ? 226 VAL A CA 1 ATOM 1755 C C . VAL A 1 226 ? 36.223 27.770 21.487 1.00 22.59 ? 226 VAL A C 1 ATOM 1756 O O . VAL A 1 226 ? 37.057 27.701 20.576 1.00 22.69 ? 226 VAL A O 1 ATOM 1757 C CB . VAL A 1 226 ? 37.235 28.464 23.778 1.00 23.06 ? 226 VAL A CB 1 ATOM 1758 C CG1 . VAL A 1 226 ? 38.654 28.729 23.258 1.00 23.09 ? 226 VAL A CG1 1 ATOM 1759 C CG2 . VAL A 1 226 ? 36.319 29.702 23.793 1.00 17.44 ? 226 VAL A CG2 1 ATOM 1760 N N . THR A 1 227 ? 34.983 28.146 21.205 1.00 21.19 ? 227 THR A N 1 ATOM 1761 C CA . THR A 1 227 ? 34.587 28.581 19.863 1.00 19.83 ? 227 THR A CA 1 ATOM 1762 C C . THR A 1 227 ? 34.311 30.066 19.752 1.00 18.77 ? 227 THR A C 1 ATOM 1763 O O . THR A 1 227 ? 33.639 30.669 20.594 1.00 20.73 ? 227 THR A O 1 ATOM 1764 C CB . THR A 1 227 ? 33.304 27.901 19.357 1.00 18.89 ? 227 THR A CB 1 ATOM 1765 O OG1 . THR A 1 227 ? 33.559 26.497 19.379 1.00 19.89 ? 227 THR A OG1 1 ATOM 1766 C CG2 . THR A 1 227 ? 32.919 28.327 17.927 1.00 17.37 ? 227 THR A CG2 1 ATOM 1767 N N . TYR A 1 228 ? 34.889 30.678 18.731 1.00 17.52 ? 228 TYR A N 1 ATOM 1768 C CA . TYR A 1 228 ? 34.692 32.090 18.450 1.00 17.46 ? 228 TYR A CA 1 ATOM 1769 C C . TYR A 1 228 ? 33.957 32.256 17.109 1.00 16.52 ? 228 TYR A C 1 ATOM 1770 O O . TYR A 1 228 ? 34.340 31.669 16.092 1.00 17.76 ? 228 TYR A O 1 ATOM 1771 C CB . TYR A 1 228 ? 36.025 32.817 18.336 1.00 18.00 ? 228 TYR A CB 1 ATOM 1772 C CG . TYR A 1 228 ? 36.923 32.775 19.553 1.00 19.34 ? 228 TYR A CG 1 ATOM 1773 C CD1 . TYR A 1 228 ? 36.709 33.645 20.619 1.00 20.30 ? 228 TYR A CD1 1 ATOM 1774 C CD2 . TYR A 1 228 ? 37.925 31.840 19.591 1.00 19.46 ? 228 TYR A CD2 1 ATOM 1775 C CE1 . TYR A 1 228 ? 37.516 33.592 21.738 1.00 19.93 ? 228 TYR A CE1 1 ATOM 1776 C CE2 . TYR A 1 228 ? 38.729 31.791 20.711 1.00 21.95 ? 228 TYR A CE2 1 ATOM 1777 C CZ . TYR A 1 228 ? 38.514 32.651 21.775 1.00 19.10 ? 228 TYR A CZ 1 ATOM 1778 O OH . TYR A 1 228 ? 39.351 32.586 22.869 1.00 23.64 ? 228 TYR A OH 1 ATOM 1779 N N . ILE A 1 229 ? 32.853 32.974 17.022 1.00 16.95 ? 229 ILE A N 1 ATOM 1780 C CA . ILE A 1 229 ? 32.153 33.184 15.751 1.00 15.19 ? 229 ILE A CA 1 ATOM 1781 C C . ILE A 1 229 ? 32.744 34.515 15.231 1.00 17.56 ? 229 ILE A C 1 ATOM 1782 O O . ILE A 1 229 ? 32.701 35.575 15.892 1.00 14.32 ? 229 ILE A O 1 ATOM 1783 C CB . ILE A 1 229 ? 30.596 33.300 15.971 1.00 16.01 ? 229 ILE A CB 1 ATOM 1784 C CG1 . ILE A 1 229 ? 30.045 32.025 16.649 1.00 14.46 ? 229 ILE A CG1 1 ATOM 1785 C CG2 . ILE A 1 229 ? 29.918 33.605 14.613 1.00 14.27 ? 229 ILE A CG2 1 ATOM 1786 C CD1 . ILE A 1 229 ? 30.383 30.680 15.946 1.00 12.77 ? 229 ILE A CD1 1 ATOM 1787 N N . LEU A 1 230 ? 33.286 34.485 14.015 1.00 18.10 ? 230 LEU A N 1 ATOM 1788 C CA . LEU A 1 230 ? 33.912 35.676 13.456 1.00 15.96 ? 230 LEU A CA 1 ATOM 1789 C C . LEU A 1 230 ? 33.122 36.570 12.509 1.00 15.91 ? 230 LEU A C 1 ATOM 1790 O O . LEU A 1 230 ? 33.414 37.755 12.332 1.00 14.66 ? 230 LEU A O 1 ATOM 1791 C CB . LEU A 1 230 ? 35.182 35.214 12.808 1.00 15.63 ? 230 LEU A CB 1 ATOM 1792 C CG . LEU A 1 230 ? 36.111 34.316 13.601 1.00 22.19 ? 230 LEU A CG 1 ATOM 1793 C CD1 . LEU A 1 230 ? 37.348 33.999 12.767 1.00 23.21 ? 230 LEU A CD1 1 ATOM 1794 C CD2 . LEU A 1 230 ? 36.521 34.998 14.870 1.00 22.34 ? 230 LEU A CD2 1 ATOM 1795 N N . SER A 1 231 ? 32.076 36.035 11.903 1.00 15.94 ? 231 SER A N 1 ATOM 1796 C CA . SER A 1 231 ? 31.201 36.756 10.960 1.00 16.83 ? 231 SER A CA 1 ATOM 1797 C C . SER A 1 231 ? 29.897 35.999 10.838 1.00 17.03 ? 231 SER A C 1 ATOM 1798 O O . SER A 1 231 ? 29.823 34.806 11.159 1.00 17.85 ? 231 SER A O 1 ATOM 1799 C CB . SER A 1 231 ? 31.763 36.845 9.552 1.00 16.51 ? 231 SER A CB 1 ATOM 1800 O OG . SER A 1 231 ? 31.946 35.580 8.945 1.00 17.43 ? 231 SER A OG 1 ATOM 1801 N N . TRP A 1 232 ? 28.828 36.668 10.434 1.00 16.35 ? 232 TRP A N 1 ATOM 1802 C CA . TRP A 1 232 ? 27.530 36.009 10.320 1.00 15.17 ? 232 TRP A CA 1 ATOM 1803 C C . TRP A 1 232 ? 26.607 36.761 9.362 1.00 15.37 ? 232 TRP A C 1 ATOM 1804 O O . TRP A 1 232 ? 26.442 37.980 9.354 1.00 16.75 ? 232 TRP A O 1 ATOM 1805 C CB . TRP A 1 232 ? 26.856 35.902 11.732 1.00 11.29 ? 232 TRP A CB 1 ATOM 1806 C CG . TRP A 1 232 ? 25.567 35.064 11.897 1.00 15.49 ? 232 TRP A CG 1 ATOM 1807 C CD1 . TRP A 1 232 ? 25.184 34.086 11.017 1.00 17.80 ? 232 TRP A CD1 1 ATOM 1808 C CD2 . TRP A 1 232 ? 24.661 35.152 12.938 1.00 17.41 ? 232 TRP A CD2 1 ATOM 1809 N NE1 . TRP A 1 232 ? 24.063 33.567 11.480 1.00 18.10 ? 232 TRP A NE1 1 ATOM 1810 C CE2 . TRP A 1 232 ? 23.717 34.169 12.615 1.00 17.17 ? 232 TRP A CE2 1 ATOM 1811 C CE3 . TRP A 1 232 ? 24.510 35.920 14.086 1.00 18.37 ? 232 TRP A CE3 1 ATOM 1812 C CZ2 . TRP A 1 232 ? 22.620 33.906 13.406 1.00 17.84 ? 232 TRP A CZ2 1 ATOM 1813 C CZ3 . TRP A 1 232 ? 23.407 35.656 14.876 1.00 20.17 ? 232 TRP A CZ3 1 ATOM 1814 C CH2 . TRP A 1 232 ? 22.481 34.671 14.542 1.00 18.43 ? 232 TRP A CH2 1 ATOM 1815 N N . HIS A 1 233 ? 26.038 35.991 8.467 1.00 13.87 ? 233 HIS A N 1 ATOM 1816 C CA . HIS A 1 233 ? 25.093 36.484 7.503 1.00 13.46 ? 233 HIS A CA 1 ATOM 1817 C C . HIS A 1 233 ? 23.886 35.546 7.523 1.00 16.07 ? 233 HIS A C 1 ATOM 1818 O O . HIS A 1 233 ? 24.001 34.316 7.565 1.00 14.69 ? 233 HIS A O 1 ATOM 1819 C CB . HIS A 1 233 ? 25.727 36.487 6.106 1.00 14.28 ? 233 HIS A CB 1 ATOM 1820 C CG . HIS A 1 233 ? 24.689 36.732 5.014 1.00 16.49 ? 233 HIS A CG 1 ATOM 1821 N ND1 . HIS A 1 233 ? 23.992 37.858 4.799 1.00 19.66 ? 233 HIS A ND1 1 ATOM 1822 C CD2 . HIS A 1 233 ? 24.284 35.804 4.065 1.00 14.87 ? 233 HIS A CD2 1 ATOM 1823 C CE1 . HIS A 1 233 ? 23.196 37.675 3.783 1.00 17.92 ? 233 HIS A CE1 1 ATOM 1824 N NE2 . HIS A 1 233 ? 23.384 36.441 3.356 1.00 18.22 ? 233 HIS A NE2 1 ATOM 1825 N N . PHE A 1 234 ? 22.708 36.150 7.467 1.00 16.29 ? 234 PHE A N 1 ATOM 1826 C CA . PHE A 1 234 ? 21.453 35.407 7.410 1.00 17.03 ? 234 PHE A CA 1 ATOM 1827 C C . PHE A 1 234 ? 20.536 36.089 6.395 1.00 15.77 ? 234 PHE A C 1 ATOM 1828 O O . PHE A 1 234 ? 20.444 37.305 6.333 1.00 18.76 ? 234 PHE A O 1 ATOM 1829 C CB . PHE A 1 234 ? 20.711 35.366 8.780 1.00 13.54 ? 234 PHE A CB 1 ATOM 1830 C CG . PHE A 1 234 ? 19.459 34.479 8.784 1.00 16.67 ? 234 PHE A CG 1 ATOM 1831 C CD1 . PHE A 1 234 ? 19.572 33.120 9.047 1.00 17.66 ? 234 PHE A CD1 1 ATOM 1832 C CD2 . PHE A 1 234 ? 18.197 35.003 8.484 1.00 16.97 ? 234 PHE A CD2 1 ATOM 1833 C CE1 . PHE A 1 234 ? 18.459 32.298 9.005 1.00 17.15 ? 234 PHE A CE1 1 ATOM 1834 C CE2 . PHE A 1 234 ? 17.085 34.168 8.440 1.00 15.87 ? 234 PHE A CE2 1 ATOM 1835 C CZ . PHE A 1 234 ? 17.215 32.818 8.697 1.00 16.11 ? 234 PHE A CZ 1 ATOM 1836 N N . PHE A 1 235 ? 19.911 35.313 5.534 1.00 17.04 ? 235 PHE A N 1 ATOM 1837 C CA . PHE A 1 235 ? 18.973 35.831 4.559 1.00 15.56 ? 235 PHE A CA 1 ATOM 1838 C C . PHE A 1 235 ? 17.782 34.869 4.448 1.00 19.52 ? 235 PHE A C 1 ATOM 1839 O O . PHE A 1 235 ? 17.979 33.653 4.307 1.00 17.39 ? 235 PHE A O 1 ATOM 1840 C CB . PHE A 1 235 ? 19.632 35.975 3.171 1.00 15.29 ? 235 PHE A CB 1 ATOM 1841 C CG . PHE A 1 235 ? 18.617 36.270 2.051 1.00 18.90 ? 235 PHE A CG 1 ATOM 1842 C CD1 . PHE A 1 235 ? 17.962 35.232 1.391 1.00 17.54 ? 235 PHE A CD1 1 ATOM 1843 C CD2 . PHE A 1 235 ? 18.278 37.573 1.754 1.00 20.00 ? 235 PHE A CD2 1 ATOM 1844 C CE1 . PHE A 1 235 ? 16.976 35.481 0.475 1.00 17.45 ? 235 PHE A CE1 1 ATOM 1845 C CE2 . PHE A 1 235 ? 17.293 37.820 0.832 1.00 18.05 ? 235 PHE A CE2 1 ATOM 1846 C CZ . PHE A 1 235 ? 16.649 36.782 0.203 1.00 17.98 ? 235 PHE A CZ 1 ATOM 1847 N N . SER A 1 236 ? 16.522 35.318 4.569 1.00 19.63 ? 236 SER A N 1 ATOM 1848 C CA . SER A 1 236 ? 15.380 34.417 4.354 1.00 20.11 ? 236 SER A CA 1 ATOM 1849 C C . SER A 1 236 ? 14.471 35.031 3.295 1.00 19.86 ? 236 SER A C 1 ATOM 1850 O O . SER A 1 236 ? 14.468 36.218 2.975 1.00 20.28 ? 236 SER A O 1 ATOM 1851 C CB . SER A 1 236 ? 14.482 34.136 5.560 1.00 18.20 ? 236 SER A CB 1 ATOM 1852 O OG . SER A 1 236 ? 14.006 35.321 6.124 1.00 18.88 ? 236 SER A OG 1 ATOM 1853 N N . THR A 1 237 ? 13.814 34.149 2.580 1.00 20.37 ? 237 THR A N 1 ATOM 1854 C CA . THR A 1 237 ? 12.914 34.514 1.498 1.00 21.72 ? 237 THR A CA 1 ATOM 1855 C C . THR A 1 237 ? 11.629 33.694 1.528 1.00 23.23 ? 237 THR A C 1 ATOM 1856 O O . THR A 1 237 ? 11.666 32.519 1.918 1.00 24.59 ? 237 THR A O 1 ATOM 1857 C CB . THR A 1 237 ? 13.583 34.282 0.116 1.00 20.10 ? 237 THR A CB 1 ATOM 1858 O OG1 . THR A 1 237 ? 12.626 34.765 -0.831 1.00 22.20 ? 237 THR A OG1 1 ATOM 1859 C CG2 . THR A 1 237 ? 13.957 32.808 -0.196 1.00 13.70 ? 237 THR A CG2 1 ATOM 1860 N N . LEU A 1 238 ? 10.483 34.256 1.169 1.00 23.51 ? 238 LEU A N 1 ATOM 1861 C CA . LEU A 1 238 ? 9.228 33.488 1.106 1.00 24.63 ? 238 LEU A CA 1 ATOM 1862 C C . LEU A 1 238 ? 8.967 32.925 -0.310 1.00 24.12 ? 238 LEU A C 1 ATOM 1863 O O . LEU A 1 238 ? 7.986 32.233 -0.565 1.00 22.32 ? 238 LEU A O 1 ATOM 1864 C CB . LEU A 1 238 ? 8.098 34.416 1.561 1.00 27.70 ? 238 LEU A CB 1 ATOM 1865 C CG . LEU A 1 238 ? 7.704 34.448 3.054 1.00 29.16 ? 238 LEU A CG 1 ATOM 1866 C CD1 . LEU A 1 238 ? 8.839 34.158 3.997 1.00 29.74 ? 238 LEU A CD1 1 ATOM 1867 C CD2 . LEU A 1 238 ? 7.196 35.817 3.337 1.00 30.06 ? 238 LEU A CD2 1 ATOM 1868 N N . ASP A 1 239 ? 9.873 33.200 -1.257 1.00 23.62 ? 239 ASP A N 1 ATOM 1869 C CA . ASP A 1 239 ? 9.821 32.733 -2.629 1.00 27.50 ? 239 ASP A CA 1 ATOM 1870 C C . ASP A 1 239 ? 9.262 31.351 -2.886 1.00 31.45 ? 239 ASP A C 1 ATOM 1871 O O . ASP A 1 239 ? 9.684 30.357 -2.283 1.00 30.01 ? 239 ASP A O 1 ATOM 1872 C CB . ASP A 1 239 ? 11.199 32.724 -3.296 1.00 27.34 ? 239 ASP A CB 1 ATOM 1873 C CG . ASP A 1 239 ? 11.628 34.078 -3.838 1.00 30.30 ? 239 ASP A CG 1 ATOM 1874 O OD1 . ASP A 1 239 ? 10.862 35.031 -3.724 1.00 33.36 ? 239 ASP A OD1 1 ATOM 1875 O OD2 . ASP A 1 239 ? 12.736 34.204 -4.362 1.00 32.17 ? 239 ASP A OD2 1 ATOM 1876 N N . GLY A 1 240 ? 8.272 31.269 -3.772 1.00 34.16 ? 240 GLY A N 1 ATOM 1877 C CA . GLY A 1 240 ? 7.644 29.988 -4.097 1.00 37.82 ? 240 GLY A CA 1 ATOM 1878 C C . GLY A 1 240 ? 6.584 29.506 -3.076 1.00 39.77 ? 240 GLY A C 1 ATOM 1879 O O . GLY A 1 240 ? 6.017 28.442 -3.302 1.00 38.55 ? 240 GLY A O 1 ATOM 1880 N N . THR A 1 241 ? 6.257 30.172 -1.946 1.00 43.42 ? 241 THR A N 1 ATOM 1881 C CA . THR A 1 241 ? 5.227 29.663 -1.023 1.00 48.98 ? 241 THR A CA 1 ATOM 1882 C C . THR A 1 241 ? 3.986 30.568 -1.009 1.00 56.81 ? 241 THR A C 1 ATOM 1883 O O . THR A 1 241 ? 3.307 30.914 -0.043 1.00 56.67 ? 241 THR A O 1 ATOM 1884 C CB . THR A 1 241 ? 5.807 29.531 0.401 1.00 44.31 ? 241 THR A CB 1 ATOM 1885 O OG1 . THR A 1 241 ? 6.185 30.836 0.859 1.00 39.12 ? 241 THR A OG1 1 ATOM 1886 C CG2 . THR A 1 241 ? 6.952 28.523 0.413 1.00 40.41 ? 241 THR A CG2 1 ATOM 1887 N N . ASN A 1 242 ? 3.659 30.817 -2.279 1.00 66.93 ? 242 ASN A N 1 ATOM 1888 C CA . ASN A 1 242 ? 2.567 31.649 -2.810 1.00 76.04 ? 242 ASN A CA 1 ATOM 1889 C C . ASN A 1 242 ? 2.726 33.150 -2.674 1.00 79.79 ? 242 ASN A C 1 ATOM 1890 O O . ASN A 1 242 ? 1.913 33.943 -3.161 1.00 80.44 ? 242 ASN A O 1 ATOM 1891 C CB . ASN A 1 242 ? 1.205 31.327 -2.209 1.00 81.26 ? 242 ASN A CB 1 ATOM 1892 C CG . ASN A 1 242 ? 0.468 30.347 -3.110 1.00 85.98 ? 242 ASN A CG 1 ATOM 1893 O OD1 . ASN A 1 242 ? 0.062 30.632 -4.233 1.00 88.17 ? 242 ASN A OD1 1 ATOM 1894 N ND2 . ASN A 1 242 ? 0.266 29.113 -2.699 1.00 87.82 ? 242 ASN A ND2 1 ATOM 1895 N N . LYS A 1 243 ? 3.807 33.458 -1.969 1.00 83.68 ? 243 LYS A N 1 ATOM 1896 C CA . LYS A 1 243 ? 4.300 34.786 -1.701 1.00 87.47 ? 243 LYS A CA 1 ATOM 1897 C C . LYS A 1 243 ? 5.736 34.716 -2.312 1.00 89.09 ? 243 LYS A C 1 ATOM 1898 O O . LYS A 1 243 ? 6.321 33.633 -2.478 1.00 90.93 ? 243 LYS A O 1 ATOM 1899 C CB . LYS A 1 243 ? 4.290 35.030 -0.180 1.00 88.09 ? 243 LYS A CB 1 ATOM 1900 C CG . LYS A 1 243 ? 4.334 36.517 0.211 1.00 89.22 ? 243 LYS A CG 1 ATOM 1901 C CD . LYS A 1 243 ? 5.787 36.973 0.334 1.00 89.85 ? 243 LYS A CD 1 ATOM 1902 C CE . LYS A 1 243 ? 6.032 38.374 0.886 1.00 89.32 ? 243 LYS A CE 1 ATOM 1903 N NZ . LYS A 1 243 ? 7.453 38.554 1.151 1.00 88.63 ? 243 LYS A NZ 1 ATOM 1904 O OXT . LYS A 1 243 ? 6.263 35.746 -2.722 1.00 91.52 ? 243 LYS A OXT 1 HETATM 1905 C C1 . FUC B 2 . ? 28.103 14.571 29.030 1.00 27.44 ? 252 FUC A C1 1 HETATM 1906 C C2 . FUC B 2 . ? 26.888 13.612 28.735 1.00 28.39 ? 252 FUC A C2 1 HETATM 1907 C C3 . FUC B 2 . ? 26.613 12.717 29.981 1.00 29.16 ? 252 FUC A C3 1 HETATM 1908 C C4 . FUC B 2 . ? 26.586 13.559 31.303 1.00 30.76 ? 252 FUC A C4 1 HETATM 1909 C C5 . FUC B 2 . ? 27.959 14.331 31.417 1.00 29.78 ? 252 FUC A C5 1 HETATM 1910 C C6 . FUC B 2 . ? 28.159 15.125 32.685 1.00 30.26 ? 252 FUC A C6 1 HETATM 1911 O O2 . FUC B 2 . ? 27.145 12.801 27.534 1.00 28.36 ? 252 FUC A O2 1 HETATM 1912 O O3 . FUC B 2 . ? 25.351 12.080 29.809 1.00 33.72 ? 252 FUC A O3 1 HETATM 1913 O O4 . FUC B 2 . ? 25.462 14.448 31.383 1.00 31.04 ? 252 FUC A O4 1 HETATM 1914 O O5 . FUC B 2 . ? 28.087 15.246 30.283 1.00 30.19 ? 252 FUC A O5 1 HETATM 1915 C C1 . GAL C 3 . ? 31.577 13.911 29.864 1.00 32.30 ? 253 GAL A C1 1 HETATM 1916 C C2 . GAL C 3 . ? 30.558 14.590 28.956 1.00 30.75 ? 253 GAL A C2 1 HETATM 1917 C C3 . GAL C 3 . ? 31.077 14.658 27.488 1.00 30.43 ? 253 GAL A C3 1 HETATM 1918 C C4 . GAL C 3 . ? 32.503 15.289 27.441 1.00 29.28 ? 253 GAL A C4 1 HETATM 1919 C C5 . GAL C 3 . ? 33.426 14.462 28.351 1.00 31.83 ? 253 GAL A C5 1 HETATM 1920 C C6 . GAL C 3 . ? 34.857 15.084 28.357 1.00 32.99 ? 253 GAL A C6 1 HETATM 1921 O O2 . GAL C 3 . ? 29.312 13.845 28.975 1.00 28.77 ? 253 GAL A O2 1 HETATM 1922 O O3 . GAL C 3 . ? 30.178 15.445 26.698 1.00 26.90 ? 253 GAL A O3 1 HETATM 1923 O O4 . GAL C 3 . ? 32.497 16.667 27.836 1.00 28.32 ? 253 GAL A O4 1 HETATM 1924 O O5 . GAL C 3 . ? 32.863 14.491 29.681 1.00 32.46 ? 253 GAL A O5 1 HETATM 1925 O O6 . GAL C 3 . ? 35.792 14.261 29.042 1.00 34.12 ? 253 GAL A O6 1 HETATM 1926 C C1 . FUC D 2 . ? 33.090 16.801 33.402 1.00 32.96 ? 254 FUC A C1 1 HETATM 1927 C C2 . FUC D 2 . ? 34.312 17.505 32.839 1.00 36.46 ? 254 FUC A C2 1 HETATM 1928 C C3 . FUC D 2 . ? 34.258 17.541 31.298 1.00 34.09 ? 254 FUC A C3 1 HETATM 1929 C C4 . FUC D 2 . ? 32.945 18.192 30.849 1.00 29.35 ? 254 FUC A C4 1 HETATM 1930 C C5 . FUC D 2 . ? 31.752 17.415 31.486 1.00 30.95 ? 254 FUC A C5 1 HETATM 1931 C C6 . FUC D 2 . ? 30.393 18.011 31.149 1.00 29.63 ? 254 FUC A C6 1 HETATM 1932 O O2 . FUC D 2 . ? 35.502 16.815 33.236 1.00 39.38 ? 254 FUC A O2 1 HETATM 1933 O O3 . FUC D 2 . ? 35.356 18.262 30.770 1.00 33.71 ? 254 FUC A O3 1 HETATM 1934 O O4 . FUC D 2 . ? 32.929 19.576 31.217 1.00 27.16 ? 254 FUC A O4 1 HETATM 1935 O O5 . FUC D 2 . ? 31.871 17.411 32.937 1.00 33.84 ? 254 FUC A O5 1 HETATM 1936 C C1 . MAG E 4 . ? 32.058 11.673 33.948 1.00 47.35 ? 255 MAG A C1 1 HETATM 1937 C C2 . MAG E 4 . ? 31.235 12.207 32.728 1.00 43.14 ? 255 MAG A C2 1 HETATM 1938 C C3 . MAG E 4 . ? 31.957 13.475 32.265 1.00 39.11 ? 255 MAG A C3 1 HETATM 1939 C C4 . MAG E 4 . ? 32.147 14.494 33.455 1.00 40.08 ? 255 MAG A C4 1 HETATM 1940 C C5 . MAG E 4 . ? 32.695 13.885 34.845 1.00 41.91 ? 255 MAG A C5 1 HETATM 1941 C C6 . MAG E 4 . ? 32.390 14.735 36.176 1.00 40.00 ? 255 MAG A C6 1 HETATM 1942 C C7 . MAG E 4 . ? 29.999 10.558 31.351 1.00 39.27 ? 255 MAG A C7 1 HETATM 1943 C C8 . MAG E 4 . ? 29.980 9.467 30.292 1.00 40.47 ? 255 MAG A C8 1 HETATM 1944 N N2 . MAG E 4 . ? 31.149 11.165 31.670 1.00 40.36 ? 255 MAG A N2 1 HETATM 1945 O O1 . MAG E 4 . ? 30.978 10.748 34.330 1.00 50.24 ? 255 MAG A O1 1 HETATM 1946 O O3 . MAG E 4 . ? 31.160 14.114 31.215 1.00 35.90 ? 255 MAG A O3 1 HETATM 1947 O O4 . MAG E 4 . ? 33.146 15.409 32.973 1.00 36.89 ? 255 MAG A O4 1 HETATM 1948 O O5 . MAG E 4 . ? 32.115 12.599 35.069 1.00 45.64 ? 255 MAG A O5 1 HETATM 1949 O O6 . MAG E 4 . ? 31.001 14.798 36.464 1.00 40.90 ? 255 MAG A O6 1 HETATM 1950 O O7 . MAG E 4 . ? 28.922 10.948 31.795 1.00 39.37 ? 255 MAG A O7 1 HETATM 1951 C CM . MAG E 4 . ? 31.373 9.610 35.103 1.00 54.59 ? 255 MAG A CM 1 HETATM 1952 C C1 . NAG F 5 . ? 18.618 36.643 31.113 1.00 41.72 ? 256 NAG A C1 1 HETATM 1953 C C2 . NAG F 5 . ? 17.857 35.347 31.055 1.00 42.54 ? 256 NAG A C2 1 HETATM 1954 C C3 . NAG F 5 . ? 16.922 35.324 32.276 1.00 44.39 ? 256 NAG A C3 1 HETATM 1955 C C4 . NAG F 5 . ? 17.778 35.384 33.554 1.00 46.99 ? 256 NAG A C4 1 HETATM 1956 C C5 . NAG F 5 . ? 18.694 36.653 33.540 1.00 48.73 ? 256 NAG A C5 1 HETATM 1957 C C6 . NAG F 5 . ? 19.753 36.639 34.683 1.00 47.58 ? 256 NAG A C6 1 HETATM 1958 C C7 . NAG F 5 . ? 17.107 34.062 29.081 1.00 33.61 ? 256 NAG A C7 1 HETATM 1959 C C8 . NAG F 5 . ? 16.307 33.998 27.803 1.00 29.08 ? 256 NAG A C8 1 HETATM 1960 N N2 . NAG F 5 . ? 17.123 35.202 29.776 1.00 38.64 ? 256 NAG A N2 1 HETATM 1961 O O3 . NAG F 5 . ? 16.141 34.144 32.243 1.00 44.47 ? 256 NAG A O3 1 HETATM 1962 O O4 . NAG F 5 . ? 16.956 35.403 34.726 1.00 53.00 ? 256 NAG A O4 1 HETATM 1963 O O5 . NAG F 5 . ? 19.416 36.731 32.279 1.00 43.95 ? 256 NAG A O5 1 HETATM 1964 O O6 . NAG F 5 . ? 20.406 37.901 34.730 1.00 49.13 ? 256 NAG A O6 1 HETATM 1965 O O7 . NAG F 5 . ? 17.727 33.085 29.497 1.00 31.26 ? 256 NAG A O7 1 HETATM 1966 C C1 . NAG G 5 . ? 21.786 39.372 27.911 1.00 31.15 ? 257 NAG A C1 1 HETATM 1967 C C2 . NAG G 5 . ? 22.367 38.745 29.130 1.00 31.32 ? 257 NAG A C2 1 HETATM 1968 C C3 . NAG G 5 . ? 21.558 37.475 29.468 1.00 31.88 ? 257 NAG A C3 1 HETATM 1969 C C4 . NAG G 5 . ? 20.151 37.822 29.688 1.00 35.49 ? 257 NAG A C4 1 HETATM 1970 C C5 . NAG G 5 . ? 19.572 38.491 28.475 1.00 38.08 ? 257 NAG A C5 1 HETATM 1971 C C6 . NAG G 5 . ? 18.115 38.927 28.704 1.00 39.01 ? 257 NAG A C6 1 HETATM 1972 C C7 . NAG G 5 . ? 24.743 39.212 29.385 1.00 37.12 ? 257 NAG A C7 1 HETATM 1973 C C8 . NAG G 5 . ? 26.189 38.873 29.128 1.00 39.22 ? 257 NAG A C8 1 HETATM 1974 N N2 . NAG G 5 . ? 23.775 38.451 28.904 1.00 33.26 ? 257 NAG A N2 1 HETATM 1975 O O3 . NAG G 5 . ? 22.051 36.884 30.646 1.00 30.47 ? 257 NAG A O3 1 HETATM 1976 O O4 . NAG G 5 . ? 19.426 36.634 29.946 1.00 38.21 ? 257 NAG A O4 1 HETATM 1977 O O5 . NAG G 5 . ? 20.403 39.658 28.144 1.00 35.50 ? 257 NAG A O5 1 HETATM 1978 O O6 . NAG G 5 . ? 17.500 39.077 27.438 1.00 52.99 ? 257 NAG A O6 1 HETATM 1979 O O7 . NAG G 5 . ? 24.472 40.242 29.989 1.00 40.84 ? 257 NAG A O7 1 HETATM 1980 C C1 . FUC H 2 . ? 23.028 35.856 30.490 1.00 33.84 ? 262 FUC A C1 1 HETATM 1981 C C2 . FUC H 2 . ? 23.888 35.858 31.742 1.00 35.24 ? 262 FUC A C2 1 HETATM 1982 C C3 . FUC H 2 . ? 23.072 35.328 32.928 1.00 36.91 ? 262 FUC A C3 1 HETATM 1983 C C4 . FUC H 2 . ? 22.330 33.996 32.618 1.00 35.61 ? 262 FUC A C4 1 HETATM 1984 C C5 . FUC H 2 . ? 21.516 34.173 31.308 1.00 35.32 ? 262 FUC A C5 1 HETATM 1985 C C6 . FUC H 2 . ? 20.806 32.918 30.821 1.00 34.76 ? 262 FUC A C6 1 HETATM 1986 O O2 . FUC H 2 . ? 24.370 37.185 32.046 1.00 35.94 ? 262 FUC A O2 1 HETATM 1987 O O3 . FUC H 2 . ? 23.982 35.080 34.001 1.00 41.47 ? 262 FUC A O3 1 HETATM 1988 O O4 . FUC H 2 . ? 23.267 32.922 32.516 1.00 35.53 ? 262 FUC A O4 1 HETATM 1989 O O5 . FUC H 2 . ? 22.380 34.597 30.255 1.00 33.33 ? 262 FUC A O5 1 HETATM 1990 MN MN . MN I 6 . ? 26.916 14.133 17.707 1.00 21.11 ? 250 MN A MN 1 HETATM 1991 CA CA . CA J 7 . ? 29.279 14.504 21.108 1.00 20.35 ? 251 CA A CA 1 HETATM 1992 S S . SO4 K 8 . ? 27.606 44.099 16.152 0.56 63.30 ? 500 SO4 A S 1 HETATM 1993 O O1 . SO4 K 8 . ? 27.198 44.904 15.027 0.56 61.48 ? 500 SO4 A O1 1 HETATM 1994 O O2 . SO4 K 8 . ? 29.030 43.885 16.109 0.56 58.82 ? 500 SO4 A O2 1 HETATM 1995 O O3 . SO4 K 8 . ? 27.249 44.817 17.328 0.56 61.91 ? 500 SO4 A O3 1 HETATM 1996 O O4 . SO4 K 8 . ? 26.910 42.840 16.155 0.56 60.04 ? 500 SO4 A O4 1 HETATM 1997 O O . HOH L 9 . ? 18.944 23.471 1.147 1.00 14.95 ? 301 HOH A O 1 HETATM 1998 O O . HOH L 9 . ? 31.337 15.464 3.390 1.00 15.87 ? 302 HOH A O 1 HETATM 1999 O O . HOH L 9 . ? 25.289 11.062 5.838 0.85 34.87 ? 303 HOH A O 1 HETATM 2000 O O . HOH L 9 . ? 24.006 43.070 20.750 0.99 31.76 ? 304 HOH A O 1 HETATM 2001 O O . HOH L 9 . ? 25.434 13.082 16.742 1.00 19.52 ? 305 HOH A O 1 HETATM 2002 O O . HOH L 9 . ? 9.245 24.795 6.464 1.00 24.87 ? 306 HOH A O 1 HETATM 2003 O O . HOH L 9 . ? 35.324 39.268 13.307 1.00 19.92 ? 307 HOH A O 1 HETATM 2004 O O . HOH L 9 . ? 10.168 27.373 6.821 1.00 20.99 ? 308 HOH A O 1 HETATM 2005 O O . HOH L 9 . ? 32.871 24.886 21.813 1.00 23.59 ? 309 HOH A O 1 HETATM 2006 O O . HOH L 9 . ? 32.950 27.371 22.962 1.00 16.84 ? 310 HOH A O 1 HETATM 2007 O O . HOH L 9 . ? 37.384 23.679 12.660 1.00 24.42 ? 311 HOH A O 1 HETATM 2008 O O . HOH L 9 . ? 39.390 23.517 14.973 0.99 20.06 ? 312 HOH A O 1 HETATM 2009 O O . HOH L 9 . ? 37.336 26.400 13.077 1.00 19.50 ? 313 HOH A O 1 HETATM 2010 O O . HOH L 9 . ? 39.530 23.035 29.664 0.93 29.35 ? 314 HOH A O 1 HETATM 2011 O O . HOH L 9 . ? 32.192 13.819 5.565 1.00 20.01 ? 315 HOH A O 1 HETATM 2012 O O . HOH L 9 . ? 16.902 12.823 3.693 0.86 20.33 ? 316 HOH A O 1 HETATM 2013 O O . HOH L 9 . ? 12.196 23.292 -4.352 1.00 29.48 ? 317 HOH A O 1 HETATM 2014 O O . HOH L 9 . ? 35.065 27.230 27.667 1.00 32.43 ? 318 HOH A O 1 HETATM 2015 O O . HOH L 9 . ? 10.505 29.688 0.326 0.98 24.15 ? 319 HOH A O 1 HETATM 2016 O O . HOH L 9 . ? 36.746 23.679 27.121 0.95 34.59 ? 320 HOH A O 1 HETATM 2017 O O . HOH L 9 . ? 16.244 18.553 26.487 0.84 27.17 ? 321 HOH A O 1 HETATM 2018 O O . HOH L 9 . ? 16.285 35.191 16.689 1.00 24.88 ? 322 HOH A O 1 HETATM 2019 O O . HOH L 9 . ? 12.004 34.959 7.888 1.00 24.32 ? 323 HOH A O 1 HETATM 2020 O O . HOH L 9 . ? 17.966 14.496 16.176 1.00 24.91 ? 324 HOH A O 1 HETATM 2021 O O . HOH L 9 . ? 24.072 10.767 17.096 1.00 32.52 ? 325 HOH A O 1 HETATM 2022 O O . HOH L 9 . ? 15.632 21.265 24.019 1.00 29.80 ? 326 HOH A O 1 HETATM 2023 O O . HOH L 9 . ? 6.721 16.188 16.354 1.00 84.06 ? 327 HOH A O 1 HETATM 2024 O O . HOH L 9 . ? 43.189 17.757 24.731 0.88 33.53 ? 328 HOH A O 1 HETATM 2025 O O . HOH L 9 . ? 30.033 16.296 22.158 1.00 19.06 ? 329 HOH A O 1 HETATM 2026 O O . HOH L 9 . ? 30.982 10.159 6.642 0.98 28.57 ? 330 HOH A O 1 HETATM 2027 O O . HOH L 9 . ? 18.185 26.630 23.736 1.00 29.22 ? 331 HOH A O 1 HETATM 2028 O O . HOH L 9 . ? 25.393 14.729 19.153 0.87 19.06 ? 332 HOH A O 1 HETATM 2029 O O . HOH L 9 . ? 26.912 15.419 21.367 0.97 20.94 ? 333 HOH A O 1 HETATM 2030 O O . HOH L 9 . ? 29.699 35.124 6.942 1.00 26.86 ? 334 HOH A O 1 HETATM 2031 O O . HOH L 9 . ? 34.929 33.886 29.460 0.72 24.45 ? 335 HOH A O 1 HETATM 2032 O O . HOH L 9 . ? 39.195 34.337 25.110 0.99 34.92 ? 336 HOH A O 1 HETATM 2033 O O . HOH L 9 . ? 8.374 13.214 17.867 0.88 58.77 ? 337 HOH A O 1 HETATM 2034 O O . HOH L 9 . ? 40.660 23.369 11.796 1.00 23.82 ? 338 HOH A O 1 HETATM 2035 O O . HOH L 9 . ? 8.761 30.618 19.378 0.90 29.37 ? 339 HOH A O 1 HETATM 2036 O O . HOH L 9 . ? 41.872 22.601 9.231 1.00 36.22 ? 340 HOH A O 1 HETATM 2037 O O . HOH L 9 . ? 40.980 20.809 5.340 0.82 25.02 ? 341 HOH A O 1 HETATM 2038 O O . HOH L 9 . ? 21.034 48.400 16.658 0.89 50.12 ? 342 HOH A O 1 HETATM 2039 O O . HOH L 9 . ? 17.116 24.125 22.874 0.96 32.92 ? 343 HOH A O 1 HETATM 2040 O O . HOH L 9 . ? 44.945 21.407 19.258 0.81 37.72 ? 344 HOH A O 1 HETATM 2041 O O . HOH L 9 . ? 24.027 9.543 8.722 1.00 42.78 ? 345 HOH A O 1 HETATM 2042 O O . HOH L 9 . ? 12.474 22.455 23.477 0.75 35.15 ? 346 HOH A O 1 HETATM 2043 O O . HOH L 9 . ? 37.611 39.344 11.524 1.00 36.41 ? 347 HOH A O 1 HETATM 2044 O O . HOH L 9 . ? 42.991 25.010 28.450 1.00 43.21 ? 348 HOH A O 1 HETATM 2045 O O . HOH L 9 . ? 8.147 19.551 17.590 1.00 37.53 ? 349 HOH A O 1 HETATM 2046 O O . HOH L 9 . ? 31.794 42.120 18.918 1.00 34.11 ? 350 HOH A O 1 HETATM 2047 O O . HOH L 9 . ? 31.399 26.648 3.124 0.91 33.83 ? 351 HOH A O 1 HETATM 2048 O O . HOH L 9 . ? 11.839 25.915 24.365 1.00 69.54 ? 352 HOH A O 1 HETATM 2049 O O . HOH L 9 . ? 27.340 27.440 31.534 1.00 42.74 ? 353 HOH A O 1 HETATM 2050 O O . HOH L 9 . ? 37.703 12.167 18.791 0.84 47.77 ? 354 HOH A O 1 HETATM 2051 O O . HOH L 9 . ? 37.957 29.387 5.823 0.92 36.27 ? 355 HOH A O 1 HETATM 2052 O O . HOH L 9 . ? 7.172 23.931 5.047 1.00 35.34 ? 356 HOH A O 1 HETATM 2053 O O . HOH L 9 . ? 10.088 15.204 16.471 1.00 42.87 ? 357 HOH A O 1 HETATM 2054 O O . HOH L 9 . ? 17.504 36.130 20.950 0.84 38.41 ? 358 HOH A O 1 HETATM 2055 O O . HOH L 9 . ? 25.179 45.505 27.253 0.91 45.97 ? 359 HOH A O 1 HETATM 2056 O O . HOH L 9 . ? 6.082 13.970 25.836 1.00 34.02 ? 360 HOH A O 1 HETATM 2057 O O . HOH L 9 . ? 12.281 16.730 -1.080 0.82 24.91 ? 361 HOH A O 1 HETATM 2058 O O . HOH L 9 . ? 8.635 17.693 19.658 1.00 35.10 ? 362 HOH A O 1 HETATM 2059 O O . HOH L 9 . ? 28.992 40.026 26.516 0.86 29.57 ? 363 HOH A O 1 HETATM 2060 O O . HOH L 9 . ? 11.137 37.487 10.273 0.88 31.88 ? 364 HOH A O 1 HETATM 2061 O O . HOH L 9 . ? 15.308 33.728 24.740 1.00 47.51 ? 365 HOH A O 1 HETATM 2062 O O . HOH L 9 . ? 25.789 35.646 28.689 1.00 41.43 ? 366 HOH A O 1 HETATM 2063 O O . HOH L 9 . ? 28.561 9.698 9.894 1.00 33.94 ? 367 HOH A O 1 HETATM 2064 O O . HOH L 9 . ? 26.804 41.770 25.749 0.91 53.15 ? 368 HOH A O 1 HETATM 2065 O O . HOH L 9 . ? 24.641 9.020 12.686 1.00 31.72 ? 369 HOH A O 1 HETATM 2066 O O . HOH L 9 . ? 29.384 37.967 6.675 0.92 44.21 ? 370 HOH A O 1 HETATM 2067 O O . HOH L 9 . ? 35.781 41.988 26.388 1.00 41.67 ? 371 HOH A O 1 HETATM 2068 O O . HOH L 9 . ? 42.431 20.181 31.506 1.00 59.68 ? 372 HOH A O 1 HETATM 2069 O O . HOH L 9 . ? 13.355 13.314 15.663 0.94 51.62 ? 373 HOH A O 1 HETATM 2070 O O . HOH L 9 . ? 22.972 9.510 14.947 1.00 42.53 ? 374 HOH A O 1 HETATM 2071 O O . HOH L 9 . ? 5.052 23.190 14.698 1.00 52.90 ? 375 HOH A O 1 HETATM 2072 O O . HOH L 9 . ? 37.344 11.932 12.020 1.00 36.01 ? 376 HOH A O 1 HETATM 2073 O O . HOH L 9 . ? 42.523 25.387 6.495 1.00 41.68 ? 377 HOH A O 1 HETATM 2074 O O . HOH L 9 . ? 24.442 24.988 1.979 0.85 28.90 ? 378 HOH A O 1 HETATM 2075 O O . HOH L 9 . ? 3.619 28.478 16.261 0.98 55.92 ? 379 HOH A O 1 HETATM 2076 O O . HOH L 9 . ? 3.315 25.611 15.939 1.00 63.15 ? 380 HOH A O 1 HETATM 2077 O O . HOH L 9 . ? 14.360 24.550 22.568 0.72 26.21 ? 381 HOH A O 1 HETATM 2078 O O . HOH L 9 . ? 29.116 11.468 27.915 1.00 43.64 ? 382 HOH A O 1 HETATM 2079 O O . HOH L 9 . ? 13.985 29.652 -1.983 0.99 31.38 ? 383 HOH A O 1 HETATM 2080 O O . HOH L 9 . ? 3.273 33.983 12.740 1.00 65.41 ? 384 HOH A O 1 HETATM 2081 O O . HOH L 9 . ? 36.022 12.110 21.714 0.95 38.20 ? 385 HOH A O 1 HETATM 2082 O O . HOH L 9 . ? 21.098 30.025 32.564 0.83 52.85 ? 386 HOH A O 1 HETATM 2083 O O . HOH L 9 . ? 14.300 27.531 27.934 0.91 63.31 ? 387 HOH A O 1 HETATM 2084 O O . HOH L 9 . ? 40.636 11.555 10.254 1.00 33.21 ? 388 HOH A O 1 HETATM 2085 O O . HOH L 9 . ? 44.427 30.581 12.832 1.00 67.26 ? 389 HOH A O 1 HETATM 2086 O O . HOH L 9 . ? 10.043 37.100 0.403 0.88 31.03 ? 390 HOH A O 1 HETATM 2087 O O . HOH L 9 . ? 8.815 36.365 -1.973 0.89 39.82 ? 391 HOH A O 1 HETATM 2088 O O . HOH L 9 . ? -0.996 31.909 10.998 1.00 60.09 ? 392 HOH A O 1 HETATM 2089 O O . HOH L 9 . ? 42.427 13.778 9.663 0.93 36.97 ? 393 HOH A O 1 HETATM 2090 O O . HOH L 9 . ? 24.949 21.031 32.563 1.00 46.39 ? 394 HOH A O 1 HETATM 2091 O O . HOH L 9 . ? 13.878 24.023 29.665 1.00 63.16 ? 395 HOH A O 1 HETATM 2092 O O . HOH L 9 . ? 23.077 44.077 7.483 0.91 50.30 ? 396 HOH A O 1 HETATM 2093 O O . HOH L 9 . ? 36.032 35.819 8.067 0.98 41.98 ? 397 HOH A O 1 HETATM 2094 O O . HOH L 9 . ? 37.825 24.349 0.330 0.85 40.01 ? 398 HOH A O 1 HETATM 2095 O O . HOH L 9 . ? 16.517 11.442 27.083 0.84 24.70 ? 399 HOH A O 1 HETATM 2096 O O . HOH L 9 . ? 46.683 30.670 25.587 1.00 67.33 ? 400 HOH A O 1 HETATM 2097 O O . HOH L 9 . ? 36.835 28.586 3.160 0.90 34.19 ? 401 HOH A O 1 HETATM 2098 O O . HOH L 9 . ? 28.210 9.566 6.440 0.84 32.73 ? 402 HOH A O 1 HETATM 2099 O O . HOH L 9 . ? 39.450 39.450 21.346 0.71 14.93 ? 403 HOH A O 1 HETATM 2100 O O . HOH L 9 . ? 39.450 39.450 23.688 0.43 9.47 ? 404 HOH A O 1 HETATM 2101 O O . HOH L 9 . ? 13.806 12.122 0.769 0.95 55.72 ? 405 HOH A O 1 HETATM 2102 O O . HOH L 9 . ? 21.194 43.523 12.362 1.00 49.40 ? 406 HOH A O 1 HETATM 2103 O O . HOH L 9 . ? 35.732 38.254 9.369 0.91 37.36 ? 407 HOH A O 1 HETATM 2104 O O . HOH L 9 . ? 44.467 15.438 14.087 1.00 61.05 ? 408 HOH A O 1 HETATM 2105 O O . HOH L 9 . ? 31.552 8.598 25.791 1.00 37.66 ? 409 HOH A O 1 HETATM 2106 O O . HOH L 9 . ? 29.030 5.856 20.228 1.00 53.31 ? 410 HOH A O 1 HETATM 2107 O O . HOH L 9 . ? 35.553 26.013 -0.600 0.77 68.82 ? 411 HOH A O 1 HETATM 2108 O O . HOH L 9 . ? 44.125 29.377 15.398 0.86 38.10 ? 412 HOH A O 1 HETATM 2109 O O . HOH L 9 . ? 41.030 27.801 6.475 0.85 39.70 ? 413 HOH A O 1 HETATM 2110 O O . HOH L 9 . ? 24.304 3.485 26.476 1.00 67.23 ? 414 HOH A O 1 HETATM 2111 O O . HOH L 9 . ? 28.018 33.150 0.070 1.00 53.41 ? 415 HOH A O 1 HETATM 2112 O O . HOH L 9 . ? 13.939 14.148 10.235 0.99 61.09 ? 416 HOH A O 1 HETATM 2113 O O . HOH L 9 . ? 14.928 11.547 8.983 0.85 71.60 ? 417 HOH A O 1 HETATM 2114 O O . HOH L 9 . ? 6.200 28.707 20.928 0.80 88.59 ? 418 HOH A O 1 HETATM 2115 O O . HOH L 9 . ? 42.817 30.039 9.867 0.78 37.61 ? 419 HOH A O 1 HETATM 2116 O O . HOH L 9 . ? 31.693 11.084 26.970 1.00 39.85 ? 420 HOH A O 1 HETATM 2117 O O . HOH L 9 . ? 41.994 18.325 4.662 0.81 62.23 ? 421 HOH A O 1 HETATM 2118 O O . HOH L 9 . ? 32.754 38.545 6.416 1.00 59.36 ? 422 HOH A O 1 HETATM 2119 O O . HOH L 9 . ? 32.003 31.292 1.172 1.00 32.66 ? 423 HOH A O 1 HETATM 2120 O O . HOH L 9 . ? 25.767 29.582 32.608 1.00 74.76 ? 424 HOH A O 1 HETATM 2121 O O . HOH L 9 . ? 22.625 42.331 29.943 0.76 43.49 ? 425 HOH A O 1 HETATM 2122 O O . HOH L 9 . ? 43.048 22.785 6.013 1.00 57.28 ? 426 HOH A O 1 HETATM 2123 O O . HOH L 9 . ? 27.990 44.570 5.824 0.74 44.42 ? 427 HOH A O 1 HETATM 2124 O O . HOH L 9 . ? 21.202 7.555 26.978 1.00 57.72 ? 428 HOH A O 1 HETATM 2125 O O . HOH L 9 . ? 14.762 39.283 2.036 1.00 44.73 ? 429 HOH A O 1 HETATM 2126 O O . HOH L 9 . ? 12.388 21.644 26.135 0.61 54.94 ? 430 HOH A O 1 HETATM 2127 O O . HOH L 9 . ? 19.339 19.789 33.357 0.89 49.27 ? 431 HOH A O 1 HETATM 2128 O O . HOH L 9 . ? 12.989 37.732 -0.804 0.94 50.20 ? 432 HOH A O 1 HETATM 2129 O O . HOH L 9 . ? 3.969 27.095 5.898 1.00 62.66 ? 433 HOH A O 1 HETATM 2130 O O . HOH L 9 . ? 33.298 6.319 5.378 1.00 37.61 ? 434 HOH A O 1 HETATM 2131 O O . HOH L 9 . ? 34.598 6.505 7.855 0.59 56.50 ? 435 HOH A O 1 HETATM 2132 O O . HOH L 9 . ? 26.561 17.416 30.649 0.87 32.69 ? 450 HOH A O 1 HETATM 2133 O O . HOH L 9 . ? 34.542 8.952 24.661 1.00 63.43 ? 451 HOH A O 1 HETATM 2134 O O . HOH L 9 . ? 25.525 13.682 23.209 0.90 38.35 ? 452 HOH A O 1 HETATM 2135 O O . HOH L 9 . ? 33.467 10.731 29.801 1.00 72.07 ? 453 HOH A O 1 HETATM 2136 O O . HOH L 9 . ? 25.761 14.484 25.964 1.00 37.84 ? 454 HOH A O 1 HETATM 2137 O O . HOH L 9 . ? 34.452 12.792 36.992 0.95 16.92 ? 455 HOH A O 1 HETATM 2138 O O . HOH L 9 . ? 35.795 17.168 36.105 0.86 63.06 ? 456 HOH A O 1 HETATM 2139 O O . HOH L 9 . ? 29.860 18.205 34.443 1.00 60.41 ? 457 HOH A O 1 HETATM 2140 O O . HOH L 9 . ? 27.949 11.432 34.542 1.00 45.38 ? 458 HOH A O 1 # loop_ _pdbx_poly_seq_scheme.asym_id _pdbx_poly_seq_scheme.entity_id _pdbx_poly_seq_scheme.seq_id _pdbx_poly_seq_scheme.mon_id _pdbx_poly_seq_scheme.ndb_seq_num _pdbx_poly_seq_scheme.pdb_seq_num _pdbx_poly_seq_scheme.auth_seq_num _pdbx_poly_seq_scheme.pdb_mon_id _pdbx_poly_seq_scheme.auth_mon_id _pdbx_poly_seq_scheme.pdb_strand_id _pdbx_poly_seq_scheme.pdb_ins_code _pdbx_poly_seq_scheme.hetero A 1 1 PCA 1 1 1 PCA PCA A . n A 1 2 ASN 2 2 2 ASN ASN A . n A 1 3 THR 3 3 3 THR THR A . n A 1 4 VAL 4 4 4 VAL VAL A . n A 1 5 ASN 5 5 5 ASN ASN A . n A 1 6 PHE 6 6 6 PHE PHE A . n A 1 7 THR 7 7 7 THR THR A . n A 1 8 TYR 8 8 8 TYR TYR A . n A 1 9 PRO 9 9 9 PRO PRO A . n A 1 10 ASP 10 10 10 ASP ASP A . n A 1 11 PHE 11 11 11 PHE PHE A . n A 1 12 TRP 12 12 12 TRP TRP A . n A 1 13 SER 13 13 13 SER SER A . n A 1 14 TYR 14 14 14 TYR TYR A . n A 1 15 SER 15 15 15 SER SER A . n A 1 16 LEU 16 16 16 LEU LEU A . n A 1 17 LYS 17 17 17 LYS LYS A . n A 1 18 ASN 18 18 18 ASN ASN A . n A 1 19 GLY 19 19 19 GLY GLY A . n A 1 20 THR 20 20 20 THR THR A . n A 1 21 GLU 21 21 21 GLU GLU A . n A 1 22 ILE 22 22 22 ILE ILE A . n A 1 23 THR 23 23 23 THR THR A . n A 1 24 PHE 24 24 24 PHE PHE A . n A 1 25 LEU 25 25 25 LEU LEU A . n A 1 26 GLY 26 26 26 GLY GLY A . n A 1 27 ASP 27 27 27 ASP ASP A . n A 1 28 ALA 28 28 28 ALA ALA A . n A 1 29 THR 29 29 29 THR THR A . n A 1 30 ARG 30 30 30 ARG ARG A . n A 1 31 ILE 31 31 31 ILE ILE A . n A 1 32 PRO 32 32 32 PRO PRO A . n A 1 33 GLY 33 33 33 GLY GLY A . n A 1 34 ALA 34 34 34 ALA ALA A . n A 1 35 LEU 35 35 35 LEU LEU A . n A 1 36 GLN 36 36 36 GLN GLN 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 LYS 39 39 39 LYS LYS A . n A 1 40 THR 40 40 40 THR THR A . n A 1 41 ASP 41 41 41 ASP ASP A . n A 1 42 ALA 42 42 42 ALA ALA A . n A 1 43 ASN 43 43 43 ASN ASN A . n A 1 44 GLY 44 44 44 GLY GLY A . n A 1 45 ASN 45 45 45 ASN ASN A . n A 1 46 PRO 46 46 46 PRO PRO A . n A 1 47 VAL 47 47 47 VAL VAL A . n A 1 48 ARG 48 48 48 ARG ARG A . n A 1 49 SER 49 49 49 SER SER A . n A 1 50 SER 50 50 50 SER SER A . n A 1 51 ALA 51 51 51 ALA ALA A . n A 1 52 GLY 52 52 52 GLY GLY A . n A 1 53 GLN 53 53 53 GLN GLN A . n A 1 54 ALA 54 54 54 ALA ALA A . n A 1 55 SER 55 55 55 SER SER A . n A 1 56 TYR 56 56 56 TYR TYR A . n A 1 57 SER 57 57 57 SER SER A . n A 1 58 GLU 58 58 58 GLU GLU A . n A 1 59 PRO 59 59 59 PRO PRO A . n A 1 60 VAL 60 60 60 VAL VAL A . n A 1 61 PHE 61 61 61 PHE PHE A . n A 1 62 LEU 62 62 62 LEU LEU A . n A 1 63 TRP 63 63 63 TRP TRP A . n A 1 64 ASP 64 64 64 ASP ASP A . n A 1 65 SER 65 65 65 SER SER A . n A 1 66 THR 66 66 66 THR THR A . n A 1 67 GLY 67 67 67 GLY GLY A . n A 1 68 LYS 68 68 68 LYS LYS A . n A 1 69 ALA 69 69 69 ALA ALA A . n A 1 70 ALA 70 70 70 ALA ALA A . n A 1 71 SER 71 71 71 SER SER A . n A 1 72 PHE 72 72 72 PHE PHE A . n A 1 73 TYR 73 73 73 TYR TYR A . n A 1 74 THR 74 74 74 THR THR A . n A 1 75 SER 75 75 75 SER SER A . n A 1 76 PHE 76 76 76 PHE PHE A . n A 1 77 THR 77 77 77 THR THR A . n A 1 78 PHE 78 78 78 PHE PHE A . n A 1 79 LEU 79 79 79 LEU LEU A . n A 1 80 LEU 80 80 80 LEU LEU A . n A 1 81 LYS 81 81 81 LYS LYS A . n A 1 82 ASN 82 82 82 ASN ASN A . n A 1 83 TYR 83 83 83 TYR TYR A . n A 1 84 GLY 84 84 84 GLY GLY A . n A 1 85 ALA 85 85 85 ALA ALA A . n A 1 86 PRO 86 86 86 PRO PRO A . n A 1 87 THR 87 87 87 THR THR A . n A 1 88 ALA 88 88 88 ALA ALA A . n A 1 89 ASP 89 89 89 ASP ASP A . n A 1 90 GLY 90 90 90 GLY GLY A . n A 1 91 LEU 91 91 91 LEU LEU A . n A 1 92 ALA 92 92 92 ALA ALA A . n A 1 93 PHE 93 93 93 PHE PHE A . n A 1 94 PHE 94 94 94 PHE PHE A . n A 1 95 LEU 95 95 95 LEU LEU A . n A 1 96 ALA 96 96 96 ALA ALA A . n A 1 97 PRO 97 97 97 PRO PRO A . n A 1 98 VAL 98 98 98 VAL VAL A . n A 1 99 ASP 99 99 99 ASP ASP A . n A 1 100 SER 100 100 100 SER SER A . n A 1 101 SER 101 101 101 SER SER A . n A 1 102 VAL 102 102 102 VAL VAL A . n A 1 103 LYS 103 103 103 LYS LYS A . n A 1 104 ASP 104 104 104 ASP ASP A . n A 1 105 TYR 105 105 105 TYR TYR A . n A 1 106 GLY 106 106 106 GLY GLY A . n A 1 107 GLY 107 107 107 GLY GLY A . n A 1 108 PHE 108 108 108 PHE PHE A . n A 1 109 LEU 109 109 109 LEU LEU A . n A 1 110 GLY 110 110 110 GLY GLY A . n A 1 111 LEU 111 111 111 LEU LEU A . n A 1 112 PHE 112 112 112 PHE PHE A . n A 1 113 ARG 113 113 113 ARG ARG A . n A 1 114 HIS 114 114 114 HIS HIS A . n A 1 115 GLU 115 115 115 GLU GLU A . n A 1 116 THR 116 116 116 THR THR A . n A 1 117 ALA 117 117 117 ALA ALA A . n A 1 118 ALA 118 118 118 ALA ALA A . n A 1 119 ASP 119 119 119 ASP ASP A . n A 1 120 PRO 120 120 120 PRO PRO A . n A 1 121 SER 121 121 121 SER SER A . n A 1 122 LYS 122 122 122 LYS LYS A . n A 1 123 ASN 123 123 123 ASN ASN A . n A 1 124 GLN 124 124 124 GLN GLN A . n A 1 125 VAL 125 125 125 VAL VAL A . n A 1 126 VAL 126 126 126 VAL VAL A . n A 1 127 ALA 127 127 127 ALA ALA A . n A 1 128 VAL 128 128 128 VAL VAL A . n A 1 129 GLU 129 129 129 GLU GLU A . n A 1 130 PHE 130 130 130 PHE PHE A . n A 1 131 ASP 131 131 131 ASP ASP A . n A 1 132 THR 132 132 132 THR THR A . n A 1 133 TRP 133 133 133 TRP TRP A . n A 1 134 ILE 134 134 134 ILE ILE A . n A 1 135 ASN 135 135 135 ASN ASN A . n A 1 136 LYS 136 136 136 LYS LYS A . n A 1 137 ASP 137 137 137 ASP ASP A . n A 1 138 TRP 138 138 138 TRP TRP A . n A 1 139 ASN 139 139 139 ASN ASN A . n A 1 140 ASP 140 140 140 ASP ASP A . n A 1 141 PRO 141 141 141 PRO PRO A . n A 1 142 PRO 142 142 142 PRO PRO A . n A 1 143 TYR 143 143 143 TYR TYR A . n A 1 144 PRO 144 144 144 PRO PRO A . n A 1 145 HIS 145 145 145 HIS HIS A . n A 1 146 ILE 146 146 146 ILE ILE A . n A 1 147 GLY 147 147 147 GLY GLY A . n A 1 148 ILE 148 148 148 ILE ILE A . n A 1 149 ASP 149 149 149 ASP ASP A . n A 1 150 VAL 150 150 150 VAL VAL A . n A 1 151 ASN 151 151 151 ASN ASN A . n A 1 152 SER 152 152 152 SER SER A . n A 1 153 ILE 153 153 153 ILE ILE A . n A 1 154 VAL 154 154 154 VAL VAL A . n A 1 155 SER 155 155 155 SER SER A . n A 1 156 VAL 156 156 156 VAL VAL A . n A 1 157 ALA 157 157 157 ALA ALA A . n A 1 158 THR 158 158 158 THR THR A . n A 1 159 THR 159 159 159 THR THR A . n A 1 160 ARG 160 160 160 ARG ARG A . n A 1 161 TRP 161 161 161 TRP TRP A . n A 1 162 GLU 162 162 162 GLU GLU A . n A 1 163 ASN 163 163 163 ASN ASN A . n A 1 164 ASP 164 164 164 ASP ASP A . n A 1 165 ASP 165 165 165 ASP ASP A . n A 1 166 ALA 166 166 166 ALA ALA A . n A 1 167 TYR 167 167 167 TYR TYR A . n A 1 168 GLY 168 168 168 GLY GLY A . n A 1 169 SER 169 169 169 SER SER A . n A 1 170 SER 170 170 170 SER SER A . n A 1 171 ILE 171 171 171 ILE ILE A . n A 1 172 ALA 172 172 172 ALA ALA A . n A 1 173 THR 173 173 173 THR THR A . n A 1 174 ALA 174 174 174 ALA ALA A . n A 1 175 HIS 175 175 175 HIS HIS A . n A 1 176 ILE 176 176 176 ILE ILE A . n A 1 177 THR 177 177 177 THR THR A . n A 1 178 TYR 178 178 178 TYR TYR A . n A 1 179 ASP 179 179 179 ASP ASP A . n A 1 180 ALA 180 180 180 ALA ALA A . n A 1 181 ARG 181 181 181 ARG ARG A . n A 1 182 SER 182 182 182 SER SER A . n A 1 183 LYS 183 183 183 LYS LYS A . n A 1 184 ILE 184 184 184 ILE ILE A . n A 1 185 LEU 185 185 185 LEU LEU A . n A 1 186 THR 186 186 186 THR THR A . n A 1 187 VAL 187 187 187 VAL VAL A . n A 1 188 LEU 188 188 188 LEU LEU A . n A 1 189 LEU 189 189 189 LEU LEU A . n A 1 190 SER 190 190 190 SER SER A . n A 1 191 TYR 191 191 191 TYR TYR A . n A 1 192 GLU 192 192 192 GLU GLU A . n A 1 193 HIS 193 193 193 HIS HIS A . n A 1 194 GLY 194 194 194 GLY GLY A . n A 1 195 ARG 195 195 195 ARG ARG A . n A 1 196 ASP 196 196 196 ASP ASP A . n A 1 197 TYR 197 197 197 TYR TYR A . n A 1 198 ILE 198 198 198 ILE ILE A . n A 1 199 LEU 199 199 199 LEU LEU A . n A 1 200 SER 200 200 200 SER SER A . n A 1 201 HIS 201 201 201 HIS HIS A . n A 1 202 VAL 202 202 202 VAL VAL A . n A 1 203 VAL 203 203 203 VAL VAL A . n A 1 204 ASP 204 204 204 ASP ASP A . n A 1 205 LEU 205 205 205 LEU LEU A . n A 1 206 ALA 206 206 206 ALA ALA A . n A 1 207 LYS 207 207 207 LYS LYS A . n A 1 208 VAL 208 208 208 VAL VAL A . n A 1 209 LEU 209 209 209 LEU LEU A . n A 1 210 PRO 210 210 210 PRO PRO A . n A 1 211 GLN 211 211 211 GLN GLN A . n A 1 212 LYS 212 212 212 LYS LYS A . n A 1 213 VAL 213 213 213 VAL VAL A . n A 1 214 ARG 214 214 214 ARG ARG A . n A 1 215 ILE 215 215 215 ILE ILE A . n A 1 216 GLY 216 216 216 GLY GLY A . n A 1 217 PHE 217 217 217 PHE PHE A . n A 1 218 SER 218 218 218 SER SER A . n A 1 219 ALA 219 219 219 ALA ALA A . n A 1 220 GLY 220 220 220 GLY GLY A . n A 1 221 VAL 221 221 221 VAL VAL A . n A 1 222 GLY 222 222 222 GLY GLY A . n A 1 223 TYR 223 223 223 TYR TYR A . n A 1 224 ASP 224 224 224 ASP ASP A . n A 1 225 GLU 225 225 225 GLU GLU A . n A 1 226 VAL 226 226 226 VAL VAL A . n A 1 227 THR 227 227 227 THR THR A . n A 1 228 TYR 228 228 228 TYR TYR A . n A 1 229 ILE 229 229 229 ILE ILE A . n A 1 230 LEU 230 230 230 LEU LEU A . n A 1 231 SER 231 231 231 SER SER A . n A 1 232 TRP 232 232 232 TRP TRP A . n A 1 233 HIS 233 233 233 HIS HIS A . n A 1 234 PHE 234 234 234 PHE PHE A . n A 1 235 PHE 235 235 235 PHE PHE A . n A 1 236 SER 236 236 236 SER SER A . n A 1 237 THR 237 237 237 THR THR A . n A 1 238 LEU 238 238 238 LEU LEU A . n A 1 239 ASP 239 239 239 ASP ASP A . n A 1 240 GLY 240 240 240 GLY GLY A . n A 1 241 THR 241 241 241 THR THR A . n A 1 242 ASN 242 242 242 ASN ASN A . n A 1 243 LYS 243 243 243 LYS LYS A . n # loop_ _pdbx_nonpoly_scheme.asym_id _pdbx_nonpoly_scheme.entity_id _pdbx_nonpoly_scheme.mon_id _pdbx_nonpoly_scheme.ndb_seq_num _pdbx_nonpoly_scheme.pdb_seq_num _pdbx_nonpoly_scheme.auth_seq_num _pdbx_nonpoly_scheme.pdb_mon_id _pdbx_nonpoly_scheme.auth_mon_id _pdbx_nonpoly_scheme.pdb_strand_id _pdbx_nonpoly_scheme.pdb_ins_code B 2 FUC 1 252 252 FUC FUC A . C 3 GAL 2 253 253 GAL GAL A . D 2 FUC 3 254 254 FUC FUC A . E 4 MAG 4 255 255 MAG NAG A . F 5 NAG 1 256 256 NAG NAG A . G 5 NAG 2 257 257 NAG NAG A . H 2 FUC 3 262 262 FUC FUC A . I 6 MN 1 250 250 MN MN A . J 7 CA 1 251 251 CA CA A . K 8 SO4 1 500 500 SO4 SO4 A . L 9 HOH 1 301 301 HOH HOH A . L 9 HOH 2 302 302 HOH HOH A . L 9 HOH 3 303 303 HOH HOH A . L 9 HOH 4 304 304 HOH HOH A . L 9 HOH 5 305 305 HOH HOH A . L 9 HOH 6 306 306 HOH HOH A . L 9 HOH 7 307 307 HOH HOH A . L 9 HOH 8 308 308 HOH HOH A . L 9 HOH 9 309 309 HOH HOH A . L 9 HOH 10 310 310 HOH HOH A . L 9 HOH 11 311 311 HOH HOH A . L 9 HOH 12 312 312 HOH HOH A . L 9 HOH 13 313 313 HOH HOH A . L 9 HOH 14 314 314 HOH HOH A . L 9 HOH 15 315 315 HOH HOH A . L 9 HOH 16 316 316 HOH HOH A . L 9 HOH 17 317 317 HOH HOH A . L 9 HOH 18 318 318 HOH HOH A . L 9 HOH 19 319 319 HOH HOH A . L 9 HOH 20 320 320 HOH HOH A . L 9 HOH 21 321 321 HOH HOH A . L 9 HOH 22 322 322 HOH HOH A . L 9 HOH 23 323 323 HOH HOH A . L 9 HOH 24 324 324 HOH HOH A . L 9 HOH 25 325 325 HOH HOH A . L 9 HOH 26 326 326 HOH HOH A . L 9 HOH 27 327 327 HOH HOH A . L 9 HOH 28 328 328 HOH HOH A . L 9 HOH 29 329 329 HOH HOH A . L 9 HOH 30 330 330 HOH HOH A . L 9 HOH 31 331 331 HOH HOH A . L 9 HOH 32 332 332 HOH HOH A . L 9 HOH 33 333 333 HOH HOH A . L 9 HOH 34 334 334 HOH HOH A . L 9 HOH 35 335 335 HOH HOH A . L 9 HOH 36 336 336 HOH HOH A . L 9 HOH 37 337 337 HOH HOH A . L 9 HOH 38 338 338 HOH HOH A . L 9 HOH 39 339 339 HOH HOH A . L 9 HOH 40 340 340 HOH HOH A . L 9 HOH 41 341 341 HOH HOH A . L 9 HOH 42 342 342 HOH HOH A . L 9 HOH 43 343 343 HOH HOH A . L 9 HOH 44 344 344 HOH HOH A . L 9 HOH 45 345 345 HOH HOH A . L 9 HOH 46 346 346 HOH HOH A . L 9 HOH 47 347 347 HOH HOH A . L 9 HOH 48 348 348 HOH HOH A . L 9 HOH 49 349 349 HOH HOH A . L 9 HOH 50 350 350 HOH HOH A . L 9 HOH 51 351 351 HOH HOH A . L 9 HOH 52 352 352 HOH HOH A . L 9 HOH 53 353 353 HOH HOH A . L 9 HOH 54 354 354 HOH HOH A . L 9 HOH 55 355 355 HOH HOH A . L 9 HOH 56 356 356 HOH HOH A . L 9 HOH 57 357 357 HOH HOH A . L 9 HOH 58 358 358 HOH HOH A . L 9 HOH 59 359 359 HOH HOH A . L 9 HOH 60 360 360 HOH HOH A . L 9 HOH 61 361 361 HOH HOH A . L 9 HOH 62 362 362 HOH HOH A . L 9 HOH 63 363 363 HOH HOH A . L 9 HOH 64 364 364 HOH HOH A . L 9 HOH 65 365 365 HOH HOH A . L 9 HOH 66 366 366 HOH HOH A . L 9 HOH 67 367 367 HOH HOH A . L 9 HOH 68 368 368 HOH HOH A . L 9 HOH 69 369 369 HOH HOH A . L 9 HOH 70 370 370 HOH HOH A . L 9 HOH 71 371 371 HOH HOH A . L 9 HOH 72 372 372 HOH HOH A . L 9 HOH 73 373 373 HOH HOH A . L 9 HOH 74 374 374 HOH HOH A . L 9 HOH 75 375 375 HOH HOH A . L 9 HOH 76 376 376 HOH HOH A . L 9 HOH 77 377 377 HOH HOH A . L 9 HOH 78 378 378 HOH HOH A . L 9 HOH 79 379 379 HOH HOH A . L 9 HOH 80 380 380 HOH HOH A . L 9 HOH 81 381 381 HOH HOH A . L 9 HOH 82 382 382 HOH HOH A . L 9 HOH 83 383 383 HOH HOH A . L 9 HOH 84 384 384 HOH HOH A . L 9 HOH 85 385 385 HOH HOH A . L 9 HOH 86 386 386 HOH HOH A . L 9 HOH 87 387 387 HOH HOH A . L 9 HOH 88 388 388 HOH HOH A . L 9 HOH 89 389 389 HOH HOH A . L 9 HOH 90 390 390 HOH HOH A . L 9 HOH 91 391 391 HOH HOH A . L 9 HOH 92 392 392 HOH HOH A . L 9 HOH 93 393 393 HOH HOH A . L 9 HOH 94 394 394 HOH HOH A . L 9 HOH 95 395 395 HOH HOH A . L 9 HOH 96 396 396 HOH HOH A . L 9 HOH 97 397 397 HOH HOH A . L 9 HOH 98 398 398 HOH HOH A . L 9 HOH 99 399 399 HOH HOH A . L 9 HOH 100 400 400 HOH HOH A . L 9 HOH 101 401 401 HOH HOH A . L 9 HOH 102 402 402 HOH HOH A . L 9 HOH 103 403 403 HOH HOH A . L 9 HOH 104 404 404 HOH HOH A . L 9 HOH 105 405 405 HOH HOH A . L 9 HOH 106 406 406 HOH HOH A . L 9 HOH 107 407 407 HOH HOH A . L 9 HOH 108 408 408 HOH HOH A . L 9 HOH 109 409 409 HOH HOH A . L 9 HOH 110 410 410 HOH HOH A . L 9 HOH 111 411 411 HOH HOH A . L 9 HOH 112 412 412 HOH HOH A . L 9 HOH 113 413 413 HOH HOH A . L 9 HOH 114 414 414 HOH HOH A . L 9 HOH 115 415 415 HOH HOH A . L 9 HOH 116 416 416 HOH HOH A . L 9 HOH 117 417 417 HOH HOH A . L 9 HOH 118 418 418 HOH HOH A . L 9 HOH 119 419 419 HOH HOH A . L 9 HOH 120 420 420 HOH HOH A . L 9 HOH 121 421 421 HOH HOH A . L 9 HOH 122 422 422 HOH HOH A . L 9 HOH 123 423 423 HOH HOH A . L 9 HOH 124 424 424 HOH HOH A . L 9 HOH 125 425 425 HOH HOH A . L 9 HOH 126 426 426 HOH HOH A . L 9 HOH 127 427 427 HOH HOH A . L 9 HOH 128 428 428 HOH HOH A . L 9 HOH 129 429 429 HOH HOH A . L 9 HOH 130 430 430 HOH HOH A . L 9 HOH 131 431 431 HOH HOH A . L 9 HOH 132 432 432 HOH HOH A . L 9 HOH 133 433 433 HOH HOH A . L 9 HOH 134 434 434 HOH HOH A . L 9 HOH 135 435 435 HOH HOH A . L 9 HOH 136 450 450 HOH HOH A . L 9 HOH 137 451 451 HOH HOH A . L 9 HOH 138 452 452 HOH HOH A . L 9 HOH 139 453 453 HOH HOH A . L 9 HOH 140 454 454 HOH HOH A . L 9 HOH 141 455 455 HOH HOH A . L 9 HOH 142 456 456 HOH HOH A . L 9 HOH 143 457 457 HOH HOH A . L 9 HOH 144 458 458 HOH HOH A . # loop_ _pdbx_struct_mod_residue.id _pdbx_struct_mod_residue.label_asym_id _pdbx_struct_mod_residue.label_comp_id _pdbx_struct_mod_residue.label_seq_id _pdbx_struct_mod_residue.auth_asym_id _pdbx_struct_mod_residue.auth_comp_id _pdbx_struct_mod_residue.auth_seq_id _pdbx_struct_mod_residue.PDB_ins_code _pdbx_struct_mod_residue.parent_comp_id _pdbx_struct_mod_residue.details 1 A ASN 18 A ASN 18 ? ASN 'GLYCOSYLATION SITE' 2 A PCA 1 A PCA 1 ? GLU 'PYROGLUTAMIC ACID' # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details author_defined_assembly _pdbx_struct_assembly.method_details ? _pdbx_struct_assembly.oligomeric_details dimeric _pdbx_struct_assembly.oligomeric_count 2 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1,2 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E,F,G,H,I,J,K,L # loop_ _pdbx_struct_oper_list.id _pdbx_struct_oper_list.type _pdbx_struct_oper_list.name _pdbx_struct_oper_list.symmetry_operation _pdbx_struct_oper_list.matrix[1][1] _pdbx_struct_oper_list.matrix[1][2] _pdbx_struct_oper_list.matrix[1][3] _pdbx_struct_oper_list.vector[1] _pdbx_struct_oper_list.matrix[2][1] _pdbx_struct_oper_list.matrix[2][2] _pdbx_struct_oper_list.matrix[2][3] _pdbx_struct_oper_list.vector[2] _pdbx_struct_oper_list.matrix[3][1] _pdbx_struct_oper_list.matrix[3][2] _pdbx_struct_oper_list.matrix[3][3] _pdbx_struct_oper_list.vector[3] 1 'identity operation' 1_555 x,y,z 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 2 'crystal symmetry operation' 7_555 y,x,-z 0.0000000000 1.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 0.0000000000 # loop_ _pdbx_struct_special_symmetry.id _pdbx_struct_special_symmetry.PDB_model_num _pdbx_struct_special_symmetry.auth_asym_id _pdbx_struct_special_symmetry.auth_comp_id _pdbx_struct_special_symmetry.auth_seq_id _pdbx_struct_special_symmetry.PDB_ins_code _pdbx_struct_special_symmetry.label_asym_id _pdbx_struct_special_symmetry.label_comp_id _pdbx_struct_special_symmetry.label_seq_id 1 1 A HOH 403 ? L HOH . 2 1 A HOH 404 ? L HOH . # loop_ _pdbx_struct_conn_angle.id _pdbx_struct_conn_angle.ptnr1_label_atom_id _pdbx_struct_conn_angle.ptnr1_label_alt_id _pdbx_struct_conn_angle.ptnr1_label_asym_id _pdbx_struct_conn_angle.ptnr1_label_comp_id _pdbx_struct_conn_angle.ptnr1_label_seq_id _pdbx_struct_conn_angle.ptnr1_auth_atom_id _pdbx_struct_conn_angle.ptnr1_auth_asym_id _pdbx_struct_conn_angle.ptnr1_auth_comp_id _pdbx_struct_conn_angle.ptnr1_auth_seq_id _pdbx_struct_conn_angle.ptnr1_PDB_ins_code _pdbx_struct_conn_angle.ptnr1_symmetry _pdbx_struct_conn_angle.ptnr2_label_atom_id _pdbx_struct_conn_angle.ptnr2_label_alt_id _pdbx_struct_conn_angle.ptnr2_label_asym_id _pdbx_struct_conn_angle.ptnr2_label_comp_id _pdbx_struct_conn_angle.ptnr2_label_seq_id _pdbx_struct_conn_angle.ptnr2_auth_atom_id _pdbx_struct_conn_angle.ptnr2_auth_asym_id _pdbx_struct_conn_angle.ptnr2_auth_comp_id _pdbx_struct_conn_angle.ptnr2_auth_seq_id _pdbx_struct_conn_angle.ptnr2_PDB_ins_code _pdbx_struct_conn_angle.ptnr2_symmetry _pdbx_struct_conn_angle.ptnr3_label_atom_id _pdbx_struct_conn_angle.ptnr3_label_alt_id _pdbx_struct_conn_angle.ptnr3_label_asym_id _pdbx_struct_conn_angle.ptnr3_label_comp_id _pdbx_struct_conn_angle.ptnr3_label_seq_id _pdbx_struct_conn_angle.ptnr3_auth_atom_id _pdbx_struct_conn_angle.ptnr3_auth_asym_id _pdbx_struct_conn_angle.ptnr3_auth_comp_id _pdbx_struct_conn_angle.ptnr3_auth_seq_id _pdbx_struct_conn_angle.ptnr3_PDB_ins_code _pdbx_struct_conn_angle.ptnr3_symmetry _pdbx_struct_conn_angle.value _pdbx_struct_conn_angle.value_esd 1 NE2 ? A HIS 145 ? A HIS 145 ? 1_555 MN ? I MN . ? A MN 250 ? 1_555 OD2 ? A ASP 131 ? A ASP 131 ? 1_555 83.0 ? 2 NE2 ? A HIS 145 ? A HIS 145 ? 1_555 MN ? I MN . ? A MN 250 ? 1_555 OD1 ? A ASP 140 ? A ASP 140 ? 1_555 91.2 ? 3 OD2 ? A ASP 131 ? A ASP 131 ? 1_555 MN ? I MN . ? A MN 250 ? 1_555 OD1 ? A ASP 140 ? A ASP 140 ? 1_555 94.3 ? 4 NE2 ? A HIS 145 ? A HIS 145 ? 1_555 MN ? I MN . ? A MN 250 ? 1_555 O ? L HOH . ? A HOH 305 ? 1_555 95.1 ? 5 OD2 ? A ASP 131 ? A ASP 131 ? 1_555 MN ? I MN . ? A MN 250 ? 1_555 O ? L HOH . ? A HOH 305 ? 1_555 177.6 ? 6 OD1 ? A ASP 140 ? A ASP 140 ? 1_555 MN ? I MN . ? A MN 250 ? 1_555 O ? L HOH . ? A HOH 305 ? 1_555 84.2 ? 7 NE2 ? A HIS 145 ? A HIS 145 ? 1_555 MN ? I MN . ? A MN 250 ? 1_555 O ? L HOH . ? A HOH 332 ? 1_555 175.5 ? 8 OD2 ? A ASP 131 ? A ASP 131 ? 1_555 MN ? I MN . ? A MN 250 ? 1_555 O ? L HOH . ? A HOH 332 ? 1_555 94.7 ? 9 OD1 ? A ASP 140 ? A ASP 140 ? 1_555 MN ? I MN . ? A MN 250 ? 1_555 O ? L HOH . ? A HOH 332 ? 1_555 85.1 ? 10 O ? L HOH . ? A HOH 305 ? 1_555 MN ? I MN . ? A MN 250 ? 1_555 O ? L HOH . ? A HOH 332 ? 1_555 87.0 ? 11 NE2 ? A HIS 145 ? A HIS 145 ? 1_555 MN ? I MN . ? A MN 250 ? 1_555 OE2 ? A GLU 129 ? A GLU 129 ? 1_555 95.8 ? 12 OD2 ? A ASP 131 ? A ASP 131 ? 1_555 MN ? I MN . ? A MN 250 ? 1_555 OE2 ? A GLU 129 ? A GLU 129 ? 1_555 93.8 ? 13 OD1 ? A ASP 140 ? A ASP 140 ? 1_555 MN ? I MN . ? A MN 250 ? 1_555 OE2 ? A GLU 129 ? A GLU 129 ? 1_555 169.9 ? 14 O ? L HOH . ? A HOH 305 ? 1_555 MN ? I MN . ? A MN 250 ? 1_555 OE2 ? A GLU 129 ? A GLU 129 ? 1_555 87.8 ? 15 O ? L HOH . ? A HOH 332 ? 1_555 MN ? I MN . ? A MN 250 ? 1_555 OE2 ? A GLU 129 ? A GLU 129 ? 1_555 88.3 ? 16 O ? L HOH . ? A HOH 329 ? 1_555 CA ? J CA . ? A CA 251 ? 1_555 OD2 ? A ASP 131 ? A ASP 131 ? 1_555 111.0 ? 17 O ? L HOH . ? A HOH 329 ? 1_555 CA ? J CA . ? A CA 251 ? 1_555 O ? A TRP 133 ? A TRP 133 ? 1_555 96.0 ? 18 OD2 ? A ASP 131 ? A ASP 131 ? 1_555 CA ? J CA . ? A CA 251 ? 1_555 O ? A TRP 133 ? A TRP 133 ? 1_555 108.3 ? 19 O ? L HOH . ? A HOH 329 ? 1_555 CA ? J CA . ? A CA 251 ? 1_555 OD1 ? A ASN 135 ? A ASN 135 ? 1_555 80.6 ? 20 OD2 ? A ASP 131 ? A ASP 131 ? 1_555 CA ? J CA . ? A CA 251 ? 1_555 OD1 ? A ASN 135 ? A ASN 135 ? 1_555 162.9 ? 21 O ? A TRP 133 ? A TRP 133 ? 1_555 CA ? J CA . ? A CA 251 ? 1_555 OD1 ? A ASN 135 ? A ASN 135 ? 1_555 82.1 ? 22 O ? L HOH . ? A HOH 329 ? 1_555 CA ? J CA . ? A CA 251 ? 1_555 OD2 ? A ASP 140 ? A ASP 140 ? 1_555 167.6 ? 23 OD2 ? A ASP 131 ? A ASP 131 ? 1_555 CA ? J CA . ? A CA 251 ? 1_555 OD2 ? A ASP 140 ? A ASP 140 ? 1_555 79.8 ? 24 O ? A TRP 133 ? A TRP 133 ? 1_555 CA ? J CA . ? A CA 251 ? 1_555 OD2 ? A ASP 140 ? A ASP 140 ? 1_555 74.4 ? 25 OD1 ? A ASN 135 ? A ASN 135 ? 1_555 CA ? J CA . ? A CA 251 ? 1_555 OD2 ? A ASP 140 ? A ASP 140 ? 1_555 90.4 ? 26 O ? L HOH . ? A HOH 329 ? 1_555 CA ? J CA . ? A CA 251 ? 1_555 OD1 ? A ASP 131 ? A ASP 131 ? 1_555 74.6 ? 27 OD2 ? A ASP 131 ? A ASP 131 ? 1_555 CA ? J CA . ? A CA 251 ? 1_555 OD1 ? A ASP 131 ? A ASP 131 ? 1_555 49.7 ? 28 O ? A TRP 133 ? A TRP 133 ? 1_555 CA ? J CA . ? A CA 251 ? 1_555 OD1 ? A ASP 131 ? A ASP 131 ? 1_555 79.9 ? 29 OD1 ? A ASN 135 ? A ASN 135 ? 1_555 CA ? J CA . ? A CA 251 ? 1_555 OD1 ? A ASP 131 ? A ASP 131 ? 1_555 147.4 ? 30 OD2 ? A ASP 140 ? A ASP 140 ? 1_555 CA ? J CA . ? A CA 251 ? 1_555 OD1 ? A ASP 131 ? A ASP 131 ? 1_555 110.4 ? 31 O ? L HOH . ? A HOH 329 ? 1_555 CA ? J CA . ? A CA 251 ? 1_555 O ? L HOH . ? A HOH 333 ? 1_555 88.7 ? 32 OD2 ? A ASP 131 ? A ASP 131 ? 1_555 CA ? J CA . ? A CA 251 ? 1_555 O ? L HOH . ? A HOH 333 ? 1_555 73.8 ? 33 O ? A TRP 133 ? A TRP 133 ? 1_555 CA ? J CA . ? A CA 251 ? 1_555 O ? L HOH . ? A HOH 333 ? 1_555 173.7 ? 34 OD1 ? A ASN 135 ? A ASN 135 ? 1_555 CA ? J CA . ? A CA 251 ? 1_555 O ? L HOH . ? A HOH 333 ? 1_555 94.5 ? 35 OD2 ? A ASP 140 ? A ASP 140 ? 1_555 CA ? J CA . ? A CA 251 ? 1_555 O ? L HOH . ? A HOH 333 ? 1_555 100.4 ? 36 OD1 ? A ASP 131 ? A ASP 131 ? 1_555 CA ? J CA . ? A CA 251 ? 1_555 O ? L HOH . ? A HOH 333 ? 1_555 105.6 ? # loop_ _pdbx_audit_revision_history.ordinal _pdbx_audit_revision_history.data_content_type _pdbx_audit_revision_history.major_revision _pdbx_audit_revision_history.minor_revision _pdbx_audit_revision_history.revision_date 1 'Structure model' 1 0 1994-01-31 2 'Structure model' 1 1 2008-03-03 3 'Structure model' 1 2 2011-07-13 4 'Structure model' 1 3 2017-11-29 # _pdbx_audit_revision_details.ordinal 1 _pdbx_audit_revision_details.revision_ordinal 1 _pdbx_audit_revision_details.data_content_type 'Structure model' _pdbx_audit_revision_details.provider repository _pdbx_audit_revision_details.type 'Initial release' _pdbx_audit_revision_details.description ? # loop_ _pdbx_audit_revision_group.ordinal _pdbx_audit_revision_group.revision_ordinal _pdbx_audit_revision_group.data_content_type _pdbx_audit_revision_group.group 1 2 'Structure model' 'Version format compliance' 2 3 'Structure model' 'Non-polymer description' 3 3 'Structure model' 'Version format compliance' 4 4 'Structure model' 'Derived calculations' 5 4 'Structure model' Other # loop_ _pdbx_audit_revision_category.ordinal _pdbx_audit_revision_category.revision_ordinal _pdbx_audit_revision_category.data_content_type _pdbx_audit_revision_category.category 1 4 'Structure model' pdbx_database_status 2 4 'Structure model' struct_conf 3 4 'Structure model' struct_conf_type # _pdbx_audit_revision_item.ordinal 1 _pdbx_audit_revision_item.revision_ordinal 4 _pdbx_audit_revision_item.data_content_type 'Structure model' _pdbx_audit_revision_item.item '_pdbx_database_status.process_site' # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal X-PLOR 'model building' . ? 1 PROLSQ refinement . ? 2 X-PLOR refinement . ? 3 X-PLOR phasing . ? 4 # _pdbx_validate_rmsd_bond.id 1 _pdbx_validate_rmsd_bond.PDB_model_num 1 _pdbx_validate_rmsd_bond.auth_atom_id_1 NE2 _pdbx_validate_rmsd_bond.auth_asym_id_1 A _pdbx_validate_rmsd_bond.auth_comp_id_1 HIS _pdbx_validate_rmsd_bond.auth_seq_id_1 201 _pdbx_validate_rmsd_bond.PDB_ins_code_1 ? _pdbx_validate_rmsd_bond.label_alt_id_1 ? _pdbx_validate_rmsd_bond.auth_atom_id_2 CD2 _pdbx_validate_rmsd_bond.auth_asym_id_2 A _pdbx_validate_rmsd_bond.auth_comp_id_2 HIS _pdbx_validate_rmsd_bond.auth_seq_id_2 201 _pdbx_validate_rmsd_bond.PDB_ins_code_2 ? _pdbx_validate_rmsd_bond.label_alt_id_2 ? _pdbx_validate_rmsd_bond.bond_value 1.297 _pdbx_validate_rmsd_bond.bond_target_value 1.373 _pdbx_validate_rmsd_bond.bond_deviation -0.076 _pdbx_validate_rmsd_bond.bond_standard_deviation 0.011 _pdbx_validate_rmsd_bond.linker_flag N # loop_ _pdbx_validate_rmsd_angle.id _pdbx_validate_rmsd_angle.PDB_model_num _pdbx_validate_rmsd_angle.auth_atom_id_1 _pdbx_validate_rmsd_angle.auth_asym_id_1 _pdbx_validate_rmsd_angle.auth_comp_id_1 _pdbx_validate_rmsd_angle.auth_seq_id_1 _pdbx_validate_rmsd_angle.PDB_ins_code_1 _pdbx_validate_rmsd_angle.label_alt_id_1 _pdbx_validate_rmsd_angle.auth_atom_id_2 _pdbx_validate_rmsd_angle.auth_asym_id_2 _pdbx_validate_rmsd_angle.auth_comp_id_2 _pdbx_validate_rmsd_angle.auth_seq_id_2 _pdbx_validate_rmsd_angle.PDB_ins_code_2 _pdbx_validate_rmsd_angle.label_alt_id_2 _pdbx_validate_rmsd_angle.auth_atom_id_3 _pdbx_validate_rmsd_angle.auth_asym_id_3 _pdbx_validate_rmsd_angle.auth_comp_id_3 _pdbx_validate_rmsd_angle.auth_seq_id_3 _pdbx_validate_rmsd_angle.PDB_ins_code_3 _pdbx_validate_rmsd_angle.label_alt_id_3 _pdbx_validate_rmsd_angle.angle_value _pdbx_validate_rmsd_angle.angle_target_value _pdbx_validate_rmsd_angle.angle_deviation _pdbx_validate_rmsd_angle.angle_standard_deviation _pdbx_validate_rmsd_angle.linker_flag 1 1 CD1 A TRP 12 ? ? CG A TRP 12 ? ? CD2 A TRP 12 ? ? 111.99 106.30 5.69 0.80 N 2 1 CB A TRP 12 ? ? CG A TRP 12 ? ? CD1 A TRP 12 ? ? 119.04 127.00 -7.96 1.30 N 3 1 CE2 A TRP 12 ? ? CD2 A TRP 12 ? ? CG A TRP 12 ? ? 101.56 107.30 -5.74 0.80 N 4 1 CG A TRP 12 ? ? CD2 A TRP 12 ? ? CE3 A TRP 12 ? ? 139.57 133.90 5.67 0.90 N 5 1 NE A ARG 48 ? ? CZ A ARG 48 ? ? NH1 A ARG 48 ? ? 123.35 120.30 3.05 0.50 N 6 1 CD1 A TRP 63 ? ? CG A TRP 63 ? ? CD2 A TRP 63 ? ? 111.28 106.30 4.98 0.80 N 7 1 CE2 A TRP 63 ? ? CD2 A TRP 63 ? ? CG A TRP 63 ? ? 102.15 107.30 -5.15 0.80 N 8 1 CB A TYR 73 ? ? CG A TYR 73 ? ? CD2 A TYR 73 ? ? 115.62 121.00 -5.38 0.60 N 9 1 CD1 A TRP 133 ? ? CG A TRP 133 ? ? CD2 A TRP 133 ? ? 113.81 106.30 7.51 0.80 N 10 1 CG A TRP 133 ? ? CD1 A TRP 133 ? ? NE1 A TRP 133 ? ? 104.04 110.10 -6.06 1.00 N 11 1 CE2 A TRP 133 ? ? CD2 A TRP 133 ? ? CG A TRP 133 ? ? 101.29 107.30 -6.01 0.80 N 12 1 CD1 A TRP 138 ? ? CG A TRP 138 ? ? CD2 A TRP 138 ? ? 112.44 106.30 6.14 0.80 N 13 1 CE2 A TRP 138 ? ? CD2 A TRP 138 ? ? CG A TRP 138 ? ? 101.34 107.30 -5.96 0.80 N 14 1 CB A TYR 143 ? ? CG A TYR 143 ? ? CD2 A TYR 143 ? ? 116.32 121.00 -4.68 0.60 N 15 1 CD1 A TRP 161 ? ? CG A TRP 161 ? ? CD2 A TRP 161 ? ? 111.40 106.30 5.10 0.80 N 16 1 CE2 A TRP 161 ? ? CD2 A TRP 161 ? ? CG A TRP 161 ? ? 102.44 107.30 -4.86 0.80 N 17 1 NE A ARG 195 ? ? CZ A ARG 195 ? ? NH1 A ARG 195 ? ? 124.34 120.30 4.04 0.50 N 18 1 CB A TYR 197 ? ? CG A TYR 197 ? ? CD1 A TYR 197 ? ? 116.67 121.00 -4.33 0.60 N 19 1 NE A ARG 214 ? ? CZ A ARG 214 ? ? NH1 A ARG 214 ? ? 125.18 120.30 4.88 0.50 N 20 1 NE A ARG 214 ? ? CZ A ARG 214 ? ? NH2 A ARG 214 ? ? 114.87 120.30 -5.43 0.50 N # loop_ _pdbx_validate_torsion.id _pdbx_validate_torsion.PDB_model_num _pdbx_validate_torsion.auth_comp_id _pdbx_validate_torsion.auth_asym_id _pdbx_validate_torsion.auth_seq_id _pdbx_validate_torsion.PDB_ins_code _pdbx_validate_torsion.label_alt_id _pdbx_validate_torsion.phi _pdbx_validate_torsion.psi 1 1 TYR A 83 ? ? -108.07 41.59 2 1 LYS A 103 ? ? -111.85 -137.11 3 1 PRO A 142 ? ? -77.52 40.81 4 1 ASN A 151 ? ? 57.60 18.84 5 1 ASP A 239 ? ? -35.28 126.26 6 1 ASN A 242 ? ? 72.39 -5.71 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 ALPHA-L-FUCOSE FUC 3 BETA-D-GALACTOSE GAL 4 BETA-METHYL-N-ACETYL-D-GLUCOSAMINE MAG 5 N-ACETYL-D-GLUCOSAMINE NAG 6 'MANGANESE (II) ION' MN 7 'CALCIUM ION' CA 8 'SULFATE ION' SO4 9 water HOH #