data_3WCS # _entry.id 3WCS # _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 3WCS RCSB RCSB096172 WWPDB D_1000096172 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.details _pdbx_database_related.content_type PDB 3WCR . unspecified PDB 3WOG . unspecified # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 3WCS _pdbx_database_status.recvd_initial_deposition_date 2013-05-31 _pdbx_database_status.deposit_site PDBJ _pdbx_database_status.process_site PDBJ _pdbx_database_status.methods_development_category ? _pdbx_database_status.status_code_sf REL _pdbx_database_status.status_code_mr ? _pdbx_database_status.SG_entry ? _pdbx_database_status.status_code_cs ? _pdbx_database_status.pdb_format_compatible Y # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Nagae, M.' 1 'Yamaguchi, Y.' 2 # _citation.id primary _citation.title 'Phytohemagglutinin from Phaseolus vulgaris (PHA-E) displays a novel glycan recognition mode using a common legume lectin fold' _citation.journal_abbrev Glycobiology _citation.journal_volume 24 _citation.page_first 368 _citation.page_last 378 _citation.year 2014 _citation.journal_id_ASTM ? _citation.country UK _citation.journal_id_ISSN 0959-6658 _citation.journal_id_CSD 9999 _citation.book_publisher ? _citation.pdbx_database_id_PubMed 24436051 _citation.pdbx_database_id_DOI 10.1093/glycob/cwu004 # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Nagae, M.' 1 primary 'Soga, K.' 2 primary 'Morita-Matsumoto, K.' 3 primary 'Hanashima, S.' 4 primary 'Ikeda, A.' 5 primary 'Yamamoto, K.' 6 primary 'Yamaguchi, Y.' 7 # _cell.entry_id 3WCS _cell.length_a 76.579 _cell.length_b 196.193 _cell.length_c 98.655 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 90.00 _cell.Z_PDB 16 _cell.pdbx_unique_axis ? _cell.length_a_esd ? _cell.length_b_esd ? _cell.length_c_esd ? _cell.angle_alpha_esd ? _cell.angle_beta_esd ? _cell.angle_gamma_esd ? # _symmetry.entry_id 3WCS _symmetry.space_group_name_H-M 'C 2 2 21' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 20 _symmetry.space_group_name_Hall ? # loop_ _entity.id _entity.type _entity.src_method _entity.pdbx_description _entity.formula_weight _entity.pdbx_number_of_molecules _entity.pdbx_ec _entity.pdbx_mutation _entity.pdbx_fragment _entity.details 1 polymer nat Erythroagglutinin 27619.783 2 ? ? 'UNP residues 22-275' ? 2 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 4 ? ? ? ? 3 non-polymer syn 'MANGANESE (II) ION' 54.938 2 ? ? ? ? 4 non-polymer syn 'CALCIUM ION' 40.078 2 ? ? ? ? 5 non-polymer man ALPHA-D-MANNOSE 180.156 2 ? ? ? ? 6 non-polymer man BETA-D-GALACTOSE 180.156 1 ? ? ? ? 7 non-polymer syn 1,2-ETHANEDIOL 62.068 5 ? ? ? ? 8 water nat water 18.015 150 ? ? ? ? # _entity_name_com.entity_id 1 _entity_name_com.name Phytohemagglutinin # _entity_poly.entity_id 1 _entity_poly.type 'polypeptide(L)' _entity_poly.nstd_linkage no _entity_poly.nstd_monomer no _entity_poly.pdbx_seq_one_letter_code ;ASQTSFSFQRFNETNLILQRDATVSSKGQLRLTNVNDNGEPTLSSLGRAFYSAPIQIWDNTTGAVASFATSFTFNIDVPN NSGPADGLAFVLLPVGSQPKDKGGLLGLFNNYKYDSNAHTVAVEFDTLYNVHWDPKPRHIGIDVNSIKSIKTTTWDFVKG ENAEVLITYDSSTKLLVASLVYPSLKTSFIVSDTVDLKSVLPEWVIVGFTATTGITKGNVETNDILSWSFASKLSDGTTS EALNLANFALNQIL ; _entity_poly.pdbx_seq_one_letter_code_can ;ASQTSFSFQRFNETNLILQRDATVSSKGQLRLTNVNDNGEPTLSSLGRAFYSAPIQIWDNTTGAVASFATSFTFNIDVPN NSGPADGLAFVLLPVGSQPKDKGGLLGLFNNYKYDSNAHTVAVEFDTLYNVHWDPKPRHIGIDVNSIKSIKTTTWDFVKG ENAEVLITYDSSTKLLVASLVYPSLKTSFIVSDTVDLKSVLPEWVIVGFTATTGITKGNVETNDILSWSFASKLSDGTTS EALNLANFALNQIL ; _entity_poly.pdbx_strand_id A,B _entity_poly.pdbx_target_identifier ? # loop_ _entity_poly_seq.entity_id _entity_poly_seq.num _entity_poly_seq.mon_id _entity_poly_seq.hetero 1 1 ALA n 1 2 SER n 1 3 GLN n 1 4 THR n 1 5 SER n 1 6 PHE n 1 7 SER n 1 8 PHE n 1 9 GLN n 1 10 ARG n 1 11 PHE n 1 12 ASN n 1 13 GLU n 1 14 THR n 1 15 ASN n 1 16 LEU n 1 17 ILE n 1 18 LEU n 1 19 GLN n 1 20 ARG n 1 21 ASP n 1 22 ALA n 1 23 THR n 1 24 VAL n 1 25 SER n 1 26 SER n 1 27 LYS n 1 28 GLY n 1 29 GLN n 1 30 LEU n 1 31 ARG n 1 32 LEU n 1 33 THR n 1 34 ASN n 1 35 VAL n 1 36 ASN n 1 37 ASP n 1 38 ASN n 1 39 GLY n 1 40 GLU n 1 41 PRO n 1 42 THR n 1 43 LEU n 1 44 SER n 1 45 SER n 1 46 LEU n 1 47 GLY n 1 48 ARG n 1 49 ALA n 1 50 PHE n 1 51 TYR n 1 52 SER n 1 53 ALA n 1 54 PRO n 1 55 ILE n 1 56 GLN n 1 57 ILE n 1 58 TRP n 1 59 ASP n 1 60 ASN n 1 61 THR n 1 62 THR n 1 63 GLY n 1 64 ALA n 1 65 VAL n 1 66 ALA n 1 67 SER n 1 68 PHE n 1 69 ALA n 1 70 THR n 1 71 SER n 1 72 PHE n 1 73 THR n 1 74 PHE n 1 75 ASN n 1 76 ILE n 1 77 ASP n 1 78 VAL n 1 79 PRO n 1 80 ASN n 1 81 ASN n 1 82 SER n 1 83 GLY n 1 84 PRO n 1 85 ALA n 1 86 ASP n 1 87 GLY n 1 88 LEU n 1 89 ALA n 1 90 PHE n 1 91 VAL n 1 92 LEU n 1 93 LEU n 1 94 PRO n 1 95 VAL n 1 96 GLY n 1 97 SER n 1 98 GLN n 1 99 PRO n 1 100 LYS n 1 101 ASP n 1 102 LYS n 1 103 GLY n 1 104 GLY n 1 105 LEU n 1 106 LEU n 1 107 GLY n 1 108 LEU n 1 109 PHE n 1 110 ASN n 1 111 ASN n 1 112 TYR n 1 113 LYS n 1 114 TYR n 1 115 ASP n 1 116 SER n 1 117 ASN n 1 118 ALA n 1 119 HIS n 1 120 THR n 1 121 VAL n 1 122 ALA n 1 123 VAL n 1 124 GLU n 1 125 PHE n 1 126 ASP n 1 127 THR n 1 128 LEU n 1 129 TYR n 1 130 ASN n 1 131 VAL n 1 132 HIS n 1 133 TRP n 1 134 ASP n 1 135 PRO n 1 136 LYS n 1 137 PRO n 1 138 ARG n 1 139 HIS n 1 140 ILE n 1 141 GLY n 1 142 ILE n 1 143 ASP n 1 144 VAL n 1 145 ASN n 1 146 SER n 1 147 ILE n 1 148 LYS n 1 149 SER n 1 150 ILE n 1 151 LYS n 1 152 THR n 1 153 THR n 1 154 THR n 1 155 TRP n 1 156 ASP n 1 157 PHE n 1 158 VAL n 1 159 LYS n 1 160 GLY n 1 161 GLU n 1 162 ASN n 1 163 ALA n 1 164 GLU n 1 165 VAL n 1 166 LEU n 1 167 ILE n 1 168 THR n 1 169 TYR n 1 170 ASP n 1 171 SER n 1 172 SER n 1 173 THR n 1 174 LYS n 1 175 LEU n 1 176 LEU n 1 177 VAL n 1 178 ALA n 1 179 SER n 1 180 LEU n 1 181 VAL n 1 182 TYR n 1 183 PRO n 1 184 SER n 1 185 LEU n 1 186 LYS n 1 187 THR n 1 188 SER n 1 189 PHE n 1 190 ILE n 1 191 VAL n 1 192 SER n 1 193 ASP n 1 194 THR n 1 195 VAL n 1 196 ASP n 1 197 LEU n 1 198 LYS n 1 199 SER n 1 200 VAL n 1 201 LEU n 1 202 PRO n 1 203 GLU n 1 204 TRP n 1 205 VAL n 1 206 ILE n 1 207 VAL n 1 208 GLY n 1 209 PHE n 1 210 THR n 1 211 ALA n 1 212 THR n 1 213 THR n 1 214 GLY n 1 215 ILE n 1 216 THR n 1 217 LYS n 1 218 GLY n 1 219 ASN n 1 220 VAL n 1 221 GLU n 1 222 THR n 1 223 ASN n 1 224 ASP n 1 225 ILE n 1 226 LEU n 1 227 SER n 1 228 TRP n 1 229 SER n 1 230 PHE n 1 231 ALA n 1 232 SER n 1 233 LYS n 1 234 LEU n 1 235 SER n 1 236 ASP n 1 237 GLY n 1 238 THR n 1 239 THR n 1 240 SER n 1 241 GLU n 1 242 ALA n 1 243 LEU n 1 244 ASN n 1 245 LEU n 1 246 ALA n 1 247 ASN n 1 248 PHE n 1 249 ALA n 1 250 LEU n 1 251 ASN n 1 252 GLN n 1 253 ILE n 1 254 LEU n # _entity_src_nat.entity_id 1 _entity_src_nat.pdbx_src_id 1 _entity_src_nat.pdbx_alt_source_flag sample _entity_src_nat.pdbx_beg_seq_num ? _entity_src_nat.pdbx_end_seq_num ? _entity_src_nat.common_name 'Kidney bean' _entity_src_nat.pdbx_organism_scientific 'Phaseolus vulgaris' _entity_src_nat.pdbx_ncbi_taxonomy_id 3885 _entity_src_nat.genus ? _entity_src_nat.species ? _entity_src_nat.strain ? _entity_src_nat.tissue ? _entity_src_nat.tissue_fraction ? _entity_src_nat.pdbx_secretion ? _entity_src_nat.pdbx_fragment ? _entity_src_nat.pdbx_variant ? _entity_src_nat.pdbx_cell_line ? _entity_src_nat.pdbx_atcc ? _entity_src_nat.pdbx_cellular_location ? _entity_src_nat.pdbx_organ ? _entity_src_nat.pdbx_organelle ? _entity_src_nat.pdbx_cell ? _entity_src_nat.pdbx_plasmid_name ? _entity_src_nat.pdbx_plasmid_details ? _entity_src_nat.details ? # _struct_ref.id 1 _struct_ref.db_name UNP _struct_ref.db_code V5YN37_PHAVU _struct_ref.pdbx_db_accession V5YN37 _struct_ref.entity_id 1 _struct_ref.pdbx_seq_one_letter_code ;ASQTSFSFQRFNETNLILQRDATVSSKGQLRLTNVNDNGEPTLSSLGRAFYSAPIQIWDNTTGAVASFATSFTFNIDVPN NSGPADGLAFVLLPVGSQPKDKGGLLGLFNNYKYDSNAHTVAVEFDTLYNVHWDPKPRHIGIDVNSIKSIKTTTWDFVKG ENAEVLITYDSSTKLLVASLVYPSLKTSFIVSDTVDLKSVLPEWVIVGFTATTGITKGNVETNDILSWSFASKLSDGTTS EALNLANFALNQIL ; _struct_ref.pdbx_align_begin 22 _struct_ref.pdbx_db_isoform ? # loop_ _struct_ref_seq.align_id _struct_ref_seq.ref_id _struct_ref_seq.pdbx_PDB_id_code _struct_ref_seq.pdbx_strand_id _struct_ref_seq.seq_align_beg _struct_ref_seq.pdbx_seq_align_beg_ins_code _struct_ref_seq.seq_align_end _struct_ref_seq.pdbx_seq_align_end_ins_code _struct_ref_seq.pdbx_db_accession _struct_ref_seq.db_align_beg _struct_ref_seq.pdbx_db_align_beg_ins_code _struct_ref_seq.db_align_end _struct_ref_seq.pdbx_db_align_end_ins_code _struct_ref_seq.pdbx_auth_seq_align_beg _struct_ref_seq.pdbx_auth_seq_align_end 1 1 3WCS A 1 ? 254 ? V5YN37 22 ? 275 ? 22 275 2 1 3WCS B 1 ? 254 ? V5YN37 22 ? 275 ? 22 275 # 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 EDO non-polymer . 1,2-ETHANEDIOL 'ETHYLENE GLYCOL' 'C2 H6 O2' 62.068 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 MAN D-saccharide . ALPHA-D-MANNOSE ? 'C6 H12 O6' 180.156 MN non-polymer . 'MANGANESE (II) ION' ? 'Mn 2' 54.938 NAG D-saccharide . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6' 221.208 PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.189 PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.130 SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093 THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3' 119.119 TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2' 204.225 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 3WCS _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 3.35 _exptl_crystal.density_percent_sol 63.33 _exptl_crystal.description ? _exptl_crystal.F_000 ? _exptl_crystal.preparation ? # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method 'VAPOR DIFFUSION, SITTING DROP' _exptl_crystal_grow.temp 293 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH 5.5 _exptl_crystal_grow.pdbx_details '0.1M Bis-tris (pH 5.5), 2.0M ammonium sulfate, VAPOR DIFFUSION, SITTING DROP, temperature 293K' _exptl_crystal_grow.pdbx_pH_range . # _diffrn.id 1 _diffrn.ambient_temp 95 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector CCD _diffrn_detector.type 'ADSC QUANTUM 270' _diffrn_detector.pdbx_collection_date 2012-10-20 _diffrn_detector.details ? # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator 'Numerical link type Si(111) double crystal monochromator, liquid nitrogen cooling' _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 1.00000 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'PHOTON FACTORY BEAMLINE AR-NE3A' _diffrn_source.pdbx_synchrotron_site 'Photon Factory' _diffrn_source.pdbx_synchrotron_beamline AR-NE3A _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_wavelength_list 1.00000 # _reflns.entry_id 3WCS _reflns.observed_criterion_sigma_I -3 _reflns.observed_criterion_sigma_F ? _reflns.d_resolution_low 100 _reflns.d_resolution_high 1.7 _reflns.number_obs 74124 _reflns.number_all ? _reflns.percent_possible_obs 99 _reflns.pdbx_Rmerge_I_obs ? _reflns.pdbx_Rsym_value 0.07 _reflns.pdbx_netI_over_sigmaI 42.1 _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy 7.3 _reflns.R_free_details ? _reflns.limit_h_max ? _reflns.limit_h_min ? _reflns.limit_k_max ? _reflns.limit_k_min ? _reflns.limit_l_max ? _reflns.limit_l_min ? _reflns.observed_criterion_F_max ? _reflns.observed_criterion_F_min ? _reflns.pdbx_chi_squared ? _reflns.pdbx_scaling_rejects ? _reflns.pdbx_ordinal 1 _reflns.pdbx_diffrn_id 1 # _reflns_shell.d_res_high 1.75 _reflns_shell.d_res_low 1.78 _reflns_shell.percent_possible_all 100 _reflns_shell.Rmerge_I_obs ? _reflns_shell.pdbx_Rsym_value 0.4 _reflns_shell.meanI_over_sigI_obs 5.7 _reflns_shell.pdbx_redundancy 7.4 _reflns_shell.percent_possible_obs ? _reflns_shell.number_unique_all 3718 _reflns_shell.number_measured_all ? _reflns_shell.number_measured_obs ? _reflns_shell.number_unique_obs ? _reflns_shell.pdbx_chi_squared ? _reflns_shell.pdbx_rejects ? _reflns_shell.pdbx_netI_over_sigmaI_obs ? _reflns_shell.number_possible ? _reflns_shell.Rmerge_F_all ? _reflns_shell.Rmerge_F_obs ? _reflns_shell.Rmerge_I_all ? _reflns_shell.meanI_over_sigI_all ? _reflns_shell.pdbx_Rrim_I_all ? _reflns_shell.pdbx_Rpim_I_all ? _reflns_shell.pdbx_ordinal 1 _reflns_shell.pdbx_diffrn_id 1 # _refine.entry_id 3WCS _refine.ls_number_reflns_obs 70316 _refine.ls_number_reflns_all ? _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F 0 _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 98.10 _refine.ls_d_res_high 1.75 _refine.ls_percent_reflns_obs 98.57 _refine.ls_R_factor_obs 0.23754 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.23661 _refine.ls_R_factor_R_free 0.25462 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 5.0 _refine.ls_number_reflns_R_free 3735 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc 0.937 _refine.correlation_coeff_Fo_to_Fc_free 0.927 _refine.B_iso_mean 30.155 _refine.aniso_B[1][1] 1.56 _refine.aniso_B[2][2] 0.55 _refine.aniso_B[3][3] -2.11 _refine.aniso_B[1][2] -0.00 _refine.aniso_B[1][3] -0.00 _refine.aniso_B[2][3] 0.00 _refine.solvent_model_details MASK _refine.solvent_model_param_ksol ? _refine.solvent_model_param_bsol ? _refine.pdbx_solvent_vdw_probe_radii 1.20 _refine.pdbx_solvent_ion_probe_radii 0.80 _refine.pdbx_solvent_shrinkage_radii 0.80 _refine.pdbx_ls_cross_valid_method THROUGHOUT _refine.details ? _refine.pdbx_starting_model 3WCR _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_stereochemistry_target_values 'MAXIMUM LIKELIHOOD' _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details RANDOM _refine.pdbx_overall_ESU_R 0.114 _refine.pdbx_overall_ESU_R_Free 0.108 _refine.overall_SU_ML 0.076 _refine.pdbx_overall_phase_error ? _refine.overall_SU_B 2.368 _refine.overall_SU_R_Cruickshank_DPI ? _refine.ls_redundancy_reflns_obs ? _refine.B_iso_min ? _refine.B_iso_max ? _refine.overall_SU_R_free ? _refine.ls_wR_factor_R_free ? _refine.ls_wR_factor_R_work ? _refine.overall_FOM_free_R_set ? _refine.overall_FOM_work_R_set ? _refine.pdbx_diffrn_id 1 _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.pdbx_TLS_residual_ADP_flag ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 3686 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 115 _refine_hist.number_atoms_solvent 150 _refine_hist.number_atoms_total 3951 _refine_hist.d_res_high 1.75 _refine_hist.d_res_low 98.10 # loop_ _refine_ls_restr.type _refine_ls_restr.dev_ideal _refine_ls_restr.dev_ideal_target _refine_ls_restr.weight _refine_ls_restr.number _refine_ls_restr.pdbx_restraint_function _refine_ls_restr.pdbx_refine_id r_bond_refined_d 0.010 0.020 ? 3906 ? 'X-RAY DIFFRACTION' r_bond_other_d ? ? ? ? ? 'X-RAY DIFFRACTION' r_angle_refined_deg 1.332 1.971 ? 5292 ? 'X-RAY DIFFRACTION' r_angle_other_deg ? ? ? ? ? 'X-RAY DIFFRACTION' r_dihedral_angle_1_deg 6.751 5.000 ? 474 ? 'X-RAY DIFFRACTION' r_dihedral_angle_2_deg 36.404 25.127 ? 158 ? 'X-RAY DIFFRACTION' r_dihedral_angle_3_deg 13.072 15.000 ? 593 ? 'X-RAY DIFFRACTION' r_dihedral_angle_4_deg 15.682 15.000 ? 10 ? 'X-RAY DIFFRACTION' r_chiral_restr 0.091 0.200 ? 641 ? 'X-RAY DIFFRACTION' r_gen_planes_refined 0.005 0.021 ? 2855 ? 'X-RAY DIFFRACTION' r_gen_planes_other ? ? ? ? ? 'X-RAY DIFFRACTION' r_nbd_refined ? ? ? ? ? 'X-RAY DIFFRACTION' r_nbd_other ? ? ? ? ? 'X-RAY DIFFRACTION' r_nbtor_refined ? ? ? ? ? 'X-RAY DIFFRACTION' r_nbtor_other ? ? ? ? ? 'X-RAY DIFFRACTION' r_xyhbond_nbd_refined ? ? ? ? ? 'X-RAY DIFFRACTION' r_xyhbond_nbd_other ? ? ? ? ? 'X-RAY DIFFRACTION' r_metal_ion_refined ? ? ? ? ? 'X-RAY DIFFRACTION' r_metal_ion_other ? ? ? ? ? 'X-RAY DIFFRACTION' r_symmetry_vdw_refined ? ? ? ? ? 'X-RAY DIFFRACTION' r_symmetry_vdw_other ? ? ? ? ? 'X-RAY DIFFRACTION' r_symmetry_hbond_refined ? ? ? ? ? 'X-RAY DIFFRACTION' r_symmetry_hbond_other ? ? ? ? ? 'X-RAY DIFFRACTION' r_symmetry_metal_ion_refined ? ? ? ? ? 'X-RAY DIFFRACTION' r_symmetry_metal_ion_other ? ? ? ? ? 'X-RAY DIFFRACTION' r_mcbond_it ? ? ? ? ? 'X-RAY DIFFRACTION' r_mcbond_other ? ? ? ? ? 'X-RAY DIFFRACTION' r_mcangle_it ? ? ? ? ? 'X-RAY DIFFRACTION' r_scbond_it ? ? ? ? ? 'X-RAY DIFFRACTION' r_scangle_it ? ? ? ? ? 'X-RAY DIFFRACTION' r_rigid_bond_restr ? ? ? ? ? 'X-RAY DIFFRACTION' r_sphericity_free ? ? ? ? ? 'X-RAY DIFFRACTION' r_sphericity_bonded ? ? ? ? ? 'X-RAY DIFFRACTION' # _refine_ls_shell.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_ls_shell.pdbx_total_number_of_bins_used 20 _refine_ls_shell.d_res_high 1.750 _refine_ls_shell.d_res_low 1.795 _refine_ls_shell.number_reflns_R_work 4717 _refine_ls_shell.R_factor_R_work 0.286 _refine_ls_shell.percent_reflns_obs 94.94 _refine_ls_shell.R_factor_R_free 0.313 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free 250 _refine_ls_shell.number_reflns_all ? _refine_ls_shell.R_factor_all ? _refine_ls_shell.number_reflns_obs ? _refine_ls_shell.redundancy_reflns_obs ? # _struct.entry_id 3WCS _struct.title 'Crystal structure of plant lectin (ligand-bound form)' _struct.pdbx_descriptor Erythroagglutinin _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 3WCS _struct_keywords.pdbx_keywords 'SUGAR BINDING PROTEIN' _struct_keywords.text 'Legume lectin fold, Carbohydrate binding, N-glycan, SUGAR BINDING PROTEIN' # loop_ _struct_asym.id _struct_asym.pdbx_blank_PDB_chainid_flag _struct_asym.pdbx_modified _struct_asym.entity_id _struct_asym.details A N N 1 ? B N N 1 ? C N N 2 ? D N N 3 ? E N N 4 ? F N N 5 ? G N N 2 ? H N N 6 ? I N N 7 ? J N N 7 ? K N N 7 ? L N N 7 ? M N N 7 ? N N N 2 ? O N N 3 ? P N N 4 ? Q N N 5 ? R N N 2 ? S N N 8 ? T N N 8 ? # _struct_biol.id 1 _struct_biol.details ? # loop_ _struct_conf.conf_type_id _struct_conf.id _struct_conf.pdbx_PDB_helix_id _struct_conf.beg_label_comp_id _struct_conf.beg_label_asym_id _struct_conf.beg_label_seq_id _struct_conf.pdbx_beg_PDB_ins_code _struct_conf.end_label_comp_id _struct_conf.end_label_asym_id _struct_conf.end_label_seq_id _struct_conf.pdbx_end_PDB_ins_code _struct_conf.beg_auth_comp_id _struct_conf.beg_auth_asym_id _struct_conf.beg_auth_seq_id _struct_conf.end_auth_comp_id _struct_conf.end_auth_asym_id _struct_conf.end_auth_seq_id _struct_conf.pdbx_PDB_helix_class _struct_conf.details _struct_conf.pdbx_PDB_helix_length HELX_P HELX_P1 1 ASN A 12 ? THR A 14 ? ASN A 33 THR A 35 5 ? 3 HELX_P HELX_P2 2 LYS A 102 ? LEU A 106 ? LYS A 123 LEU A 127 5 ? 5 HELX_P HELX_P3 3 ASP A 196 ? LEU A 201 ? ASP A 217 LEU A 222 1 ? 6 HELX_P HELX_P4 4 ASN B 12 ? THR B 14 ? ASN B 33 THR B 35 5 ? 3 HELX_P HELX_P5 5 LYS B 102 ? LEU B 106 ? LYS B 123 LEU B 127 5 ? 5 HELX_P HELX_P6 6 ASP B 196 ? VAL B 200 ? ASP B 217 VAL B 221 5 ? 5 HELX_P HELX_P7 7 ASN B 244 ? LEU B 250 ? ASN B 265 LEU B 271 1 ? 7 # _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 ? ? G NAG . O4 ? ? ? 1_555 H GAL . C1 ? ? A NAG 1005 A GAL 1006 1_555 ? ? ? ? ? ? ? 1.424 ? covale2 covale ? ? Q MAN . O2 ? ? ? 1_555 R NAG . C1 ? ? B MAN 1004 B NAG 1005 1_555 ? ? ? ? ? ? ? 1.437 ? covale3 covale ? ? F MAN . O2 ? ? ? 1_555 G NAG . C1 ? ? A MAN 1004 A NAG 1005 1_555 ? ? ? ? ? ? ? 1.440 ? covale4 covale ? ? A ASN 12 ND2 ? ? ? 1_555 C NAG . C1 ? ? A ASN 33 A NAG 1001 1_555 ? ? ? ? ? ? ? 1.442 ? covale5 covale ? ? B ASN 12 ND2 ? ? ? 1_555 N NAG . C1 ? ? B ASN 33 B NAG 1001 1_555 ? ? ? ? ? ? ? 1.446 ? metalc1 metalc ? ? B HIS 139 NE2 ? ? ? 1_555 O MN . MN ? ? B HIS 160 B MN 1002 1_555 ? ? ? ? ? ? ? 1.952 ? metalc2 metalc ? ? B ASP 126 OD2 ? ? ? 1_555 O MN . MN ? ? B ASP 147 B MN 1002 1_555 ? ? ? ? ? ? ? 1.953 ? metalc3 metalc ? ? B GLU 124 OE2 ? ? ? 1_555 O MN . MN ? ? B GLU 145 B MN 1002 1_555 ? ? ? ? ? ? ? 1.975 ? metalc4 metalc ? ? B ASP 134 OD1 ? ? ? 1_555 O MN . MN ? ? B ASP 155 B MN 1002 1_555 ? ? ? ? ? ? ? 1.981 ? metalc5 metalc ? ? A ASP 134 OD1 ? ? ? 1_555 D MN . MN ? ? A ASP 155 A MN 1002 1_555 ? ? ? ? ? ? ? 2.020 ? metalc6 metalc ? ? A GLU 124 OE2 ? ? ? 1_555 D MN . MN ? ? A GLU 145 A MN 1002 1_555 ? ? ? ? ? ? ? 2.032 ? metalc7 metalc ? ? A HIS 139 NE2 ? ? ? 1_555 D MN . MN ? ? A HIS 160 A MN 1002 1_555 ? ? ? ? ? ? ? 2.034 ? metalc8 metalc ? ? A ASP 126 OD2 ? ? ? 1_555 D MN . MN ? ? A ASP 147 A MN 1002 1_555 ? ? ? ? ? ? ? 2.046 ? metalc9 metalc ? ? B ASP 134 OD2 ? ? ? 1_555 P CA . CA ? ? B ASP 155 B CA 1003 1_555 ? ? ? ? ? ? ? 2.312 ? metalc10 metalc ? ? A ASP 134 OD2 ? ? ? 1_555 E CA . CA ? ? A ASP 155 A CA 1003 1_555 ? ? ? ? ? ? ? 2.313 ? metalc11 metalc ? ? B LEU 128 O ? ? ? 1_555 P CA . CA ? ? B LEU 149 B CA 1003 1_555 ? ? ? ? ? ? ? 2.318 ? metalc12 metalc ? ? B ASP 126 OD1 ? ? ? 1_555 P CA . CA ? ? B ASP 147 B CA 1003 1_555 ? ? ? ? ? ? ? 2.335 ? metalc13 metalc ? ? B ASN 130 OD1 ? ? ? 1_555 P CA . CA ? ? B ASN 151 B CA 1003 1_555 ? ? ? ? ? ? ? 2.338 ? metalc14 metalc ? ? A ASN 130 OD1 ? ? ? 1_555 E CA . CA ? ? A ASN 151 A CA 1003 1_555 ? ? ? ? ? ? ? 2.347 ? metalc15 metalc ? ? A LEU 128 O ? ? ? 1_555 E CA . CA ? ? A LEU 149 A CA 1003 1_555 ? ? ? ? ? ? ? 2.349 ? metalc16 metalc ? ? A ASP 126 OD1 ? ? ? 1_555 E CA . CA ? ? A ASP 147 A CA 1003 1_555 ? ? ? ? ? ? ? 2.352 ? metalc17 metalc ? ? B ASP 126 OD2 ? ? ? 1_555 P CA . CA ? ? B ASP 147 B CA 1003 1_555 ? ? ? ? ? ? ? 2.361 ? metalc18 metalc ? ? A ASP 126 OD2 ? ? ? 1_555 E CA . CA ? ? A ASP 147 A CA 1003 1_555 ? ? ? ? ? ? ? 2.427 ? metalc19 metalc ? ? O MN . MN ? ? ? 1_555 T HOH . O ? ? B MN 1002 B HOH 1102 1_555 ? ? ? ? ? ? ? 1.910 ? metalc20 metalc ? ? O MN . MN ? ? ? 1_555 T HOH . O ? ? B MN 1002 B HOH 1101 1_555 ? ? ? ? ? ? ? 1.922 ? metalc21 metalc ? ? D MN . MN ? ? ? 1_555 S HOH . O ? ? A MN 1002 A HOH 1103 1_555 ? ? ? ? ? ? ? 1.958 ? metalc22 metalc ? ? D MN . MN ? ? ? 1_555 S HOH . O ? ? A MN 1002 A HOH 1102 1_555 ? ? ? ? ? ? ? 2.001 ? metalc23 metalc ? ? E CA . CA ? ? ? 1_555 S HOH . O ? ? A CA 1003 A HOH 1105 1_555 ? ? ? ? ? ? ? 2.305 ? metalc24 metalc ? ? P CA . CA ? ? ? 1_555 T HOH . O ? ? B CA 1003 B HOH 1105 1_555 ? ? ? ? ? ? ? 2.316 ? metalc25 metalc ? ? P CA . CA ? ? ? 1_555 T HOH . O ? ? B CA 1003 B HOH 1104 1_555 ? ? ? ? ? ? ? 2.321 ? metalc26 metalc ? ? E CA . CA ? ? ? 1_555 S HOH . O ? ? A CA 1003 A HOH 1104 1_555 ? ? ? ? ? ? ? 2.338 ? # 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 106 A ASP 86 A ? ASP 107 A 1 1.63 2 ALA 85 B . ? ALA 106 B ASP 86 B ? ASP 107 B 1 -4.76 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details A ? 4 ? B ? 6 ? C ? 4 ? D ? 7 ? E ? 4 ? F ? 6 ? G ? 4 ? H ? 7 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense A 1 2 ? anti-parallel A 2 3 ? anti-parallel A 3 4 ? anti-parallel B 1 2 ? anti-parallel B 2 3 ? anti-parallel B 3 4 ? anti-parallel B 4 5 ? anti-parallel B 5 6 ? anti-parallel C 1 2 ? anti-parallel C 2 3 ? anti-parallel C 3 4 ? anti-parallel D 1 2 ? anti-parallel D 2 3 ? anti-parallel D 3 4 ? anti-parallel D 4 5 ? anti-parallel D 5 6 ? anti-parallel D 6 7 ? anti-parallel E 1 2 ? anti-parallel E 2 3 ? anti-parallel E 3 4 ? anti-parallel F 1 2 ? anti-parallel F 2 3 ? anti-parallel F 3 4 ? anti-parallel F 4 5 ? anti-parallel F 5 6 ? anti-parallel G 1 2 ? anti-parallel G 2 3 ? anti-parallel G 3 4 ? anti-parallel H 1 2 ? anti-parallel H 2 3 ? anti-parallel H 3 4 ? anti-parallel H 4 5 ? anti-parallel H 5 6 ? anti-parallel H 6 7 ? anti-parallel # loop_ _struct_sheet_range.sheet_id _struct_sheet_range.id _struct_sheet_range.beg_label_comp_id _struct_sheet_range.beg_label_asym_id _struct_sheet_range.beg_label_seq_id _struct_sheet_range.pdbx_beg_PDB_ins_code _struct_sheet_range.end_label_comp_id _struct_sheet_range.end_label_asym_id _struct_sheet_range.end_label_seq_id _struct_sheet_range.pdbx_end_PDB_ins_code _struct_sheet_range.beg_auth_comp_id _struct_sheet_range.beg_auth_asym_id _struct_sheet_range.beg_auth_seq_id _struct_sheet_range.end_auth_comp_id _struct_sheet_range.end_auth_asym_id _struct_sheet_range.end_auth_seq_id A 1 SER A 2 ? PHE A 8 ? SER A 23 PHE A 29 A 2 ASP A 224 ? LEU A 234 ? ASP A 245 LEU A 255 A 3 LEU A 30 ? ARG A 31 ? LEU A 51 ARG A 52 A 4 THR A 23 ? VAL A 24 ? THR A 44 VAL A 45 B 1 SER A 2 ? PHE A 8 ? SER A 23 PHE A 29 B 2 ASP A 224 ? LEU A 234 ? ASP A 245 LEU A 255 B 3 SER A 67 ? ASN A 75 ? SER A 88 ASN A 96 B 4 ALA A 163 ? ASP A 170 ? ALA A 184 ASP A 191 B 5 LEU A 175 ? TYR A 182 ? LEU A 196 TYR A 203 B 6 THR A 187 ? THR A 194 ? THR A 208 THR A 215 C 1 LEU A 16 ? ARG A 20 ? LEU A 37 ARG A 41 C 2 LEU A 46 ? TYR A 51 ? LEU A 67 TYR A 72 C 3 TRP A 204 ? THR A 213 ? TRP A 225 THR A 234 C 4 ILE A 55 ? GLN A 56 ? ILE A 76 GLN A 77 D 1 LEU A 16 ? ARG A 20 ? LEU A 37 ARG A 41 D 2 LEU A 46 ? TYR A 51 ? LEU A 67 TYR A 72 D 3 TRP A 204 ? THR A 213 ? TRP A 225 THR A 234 D 4 ASP A 86 ? PRO A 94 ? ASP A 107 PRO A 115 D 5 VAL A 121 ? ASP A 126 ? VAL A 142 ASP A 147 D 6 HIS A 139 ? VAL A 144 ? HIS A 160 VAL A 165 D 7 LYS A 151 ? THR A 154 ? LYS A 172 THR A 175 E 1 SER B 2 ? PHE B 8 ? SER B 23 PHE B 29 E 2 ASP B 224 ? LEU B 234 ? ASP B 245 LEU B 255 E 3 LEU B 30 ? ARG B 31 ? LEU B 51 ARG B 52 E 4 THR B 23 ? VAL B 24 ? THR B 44 VAL B 45 F 1 SER B 2 ? PHE B 8 ? SER B 23 PHE B 29 F 2 ASP B 224 ? LEU B 234 ? ASP B 245 LEU B 255 F 3 SER B 67 ? ASN B 75 ? SER B 88 ASN B 96 F 4 ALA B 163 ? ASP B 170 ? ALA B 184 ASP B 191 F 5 LEU B 175 ? TYR B 182 ? LEU B 196 TYR B 203 F 6 THR B 187 ? THR B 194 ? THR B 208 THR B 215 G 1 LEU B 16 ? ARG B 20 ? LEU B 37 ARG B 41 G 2 LEU B 46 ? TYR B 51 ? LEU B 67 TYR B 72 G 3 TRP B 204 ? THR B 213 ? TRP B 225 THR B 234 G 4 ILE B 55 ? GLN B 56 ? ILE B 76 GLN B 77 H 1 LEU B 16 ? ARG B 20 ? LEU B 37 ARG B 41 H 2 LEU B 46 ? TYR B 51 ? LEU B 67 TYR B 72 H 3 TRP B 204 ? THR B 213 ? TRP B 225 THR B 234 H 4 ASP B 86 ? PRO B 94 ? ASP B 107 PRO B 115 H 5 VAL B 121 ? ASP B 126 ? VAL B 142 ASP B 147 H 6 HIS B 139 ? VAL B 144 ? HIS B 160 VAL B 165 H 7 LYS B 151 ? THR B 154 ? LYS B 172 THR B 175 # loop_ _pdbx_struct_sheet_hbond.sheet_id _pdbx_struct_sheet_hbond.range_id_1 _pdbx_struct_sheet_hbond.range_id_2 _pdbx_struct_sheet_hbond.range_1_label_atom_id _pdbx_struct_sheet_hbond.range_1_label_comp_id _pdbx_struct_sheet_hbond.range_1_label_asym_id _pdbx_struct_sheet_hbond.range_1_label_seq_id _pdbx_struct_sheet_hbond.range_1_PDB_ins_code _pdbx_struct_sheet_hbond.range_1_auth_atom_id _pdbx_struct_sheet_hbond.range_1_auth_comp_id _pdbx_struct_sheet_hbond.range_1_auth_asym_id _pdbx_struct_sheet_hbond.range_1_auth_seq_id _pdbx_struct_sheet_hbond.range_2_label_atom_id _pdbx_struct_sheet_hbond.range_2_label_comp_id _pdbx_struct_sheet_hbond.range_2_label_asym_id _pdbx_struct_sheet_hbond.range_2_label_seq_id _pdbx_struct_sheet_hbond.range_2_PDB_ins_code _pdbx_struct_sheet_hbond.range_2_auth_atom_id _pdbx_struct_sheet_hbond.range_2_auth_comp_id _pdbx_struct_sheet_hbond.range_2_auth_asym_id _pdbx_struct_sheet_hbond.range_2_auth_seq_id A 1 2 N PHE A 8 ? N PHE A 29 O TRP A 228 ? O TRP A 249 A 2 3 O ILE A 225 ? O ILE A 246 N LEU A 30 ? N LEU A 51 A 3 4 O ARG A 31 ? O ARG A 52 N THR A 23 ? N THR A 44 B 1 2 N PHE A 8 ? N PHE A 29 O TRP A 228 ? O TRP A 249 B 2 3 O LEU A 226 ? O LEU A 247 N THR A 73 ? N THR A 94 B 3 4 N PHE A 72 ? N PHE A 93 O VAL A 165 ? O VAL A 186 B 4 5 N GLU A 164 ? N GLU A 185 O VAL A 181 ? O VAL A 202 B 5 6 N LEU A 176 ? N LEU A 197 O ASP A 193 ? O ASP A 214 C 1 2 N GLN A 19 ? N GLN A 40 O ARG A 48 ? O ARG A 69 C 2 3 N ALA A 49 ? N ALA A 70 O PHE A 209 ? O PHE A 230 C 3 4 O VAL A 205 ? O VAL A 226 N ILE A 55 ? N ILE A 76 D 1 2 N GLN A 19 ? N GLN A 40 O ARG A 48 ? O ARG A 69 D 2 3 N ALA A 49 ? N ALA A 70 O PHE A 209 ? O PHE A 230 D 3 4 O GLY A 208 ? O GLY A 229 N VAL A 91 ? N VAL A 112 D 4 5 N LEU A 88 ? N LEU A 109 O PHE A 125 ? O PHE A 146 D 5 6 N ALA A 122 ? N ALA A 143 O ASP A 143 ? O ASP A 164 D 6 7 N ILE A 142 ? N ILE A 163 O LYS A 151 ? O LYS A 172 E 1 2 N PHE B 8 ? N PHE B 29 O TRP B 228 ? O TRP B 249 E 2 3 O ILE B 225 ? O ILE B 246 N LEU B 30 ? N LEU B 51 E 3 4 O ARG B 31 ? O ARG B 52 N THR B 23 ? N THR B 44 F 1 2 N PHE B 8 ? N PHE B 29 O TRP B 228 ? O TRP B 249 F 2 3 O SER B 229 ? O SER B 250 N SER B 71 ? N SER B 92 F 3 4 N PHE B 72 ? N PHE B 93 O VAL B 165 ? O VAL B 186 F 4 5 N GLU B 164 ? N GLU B 185 O VAL B 181 ? O VAL B 202 F 5 6 N LEU B 176 ? N LEU B 197 O ASP B 193 ? O ASP B 214 G 1 2 N ILE B 17 ? N ILE B 38 O PHE B 50 ? O PHE B 71 G 2 3 N ALA B 49 ? N ALA B 70 O PHE B 209 ? O PHE B 230 G 3 4 O VAL B 205 ? O VAL B 226 N ILE B 55 ? N ILE B 76 H 1 2 N ILE B 17 ? N ILE B 38 O PHE B 50 ? O PHE B 71 H 2 3 N ALA B 49 ? N ALA B 70 O PHE B 209 ? O PHE B 230 H 3 4 O GLY B 208 ? O GLY B 229 N VAL B 91 ? N VAL B 112 H 4 5 N LEU B 88 ? N LEU B 109 O PHE B 125 ? O PHE B 146 H 5 6 N ALA B 122 ? N ALA B 143 O ASP B 143 ? O ASP B 164 H 6 7 N ILE B 142 ? N ILE B 163 O LYS B 151 ? O LYS B 172 # loop_ _struct_site.id _struct_site.pdbx_evidence_code _struct_site.pdbx_auth_asym_id _struct_site.pdbx_auth_comp_id _struct_site.pdbx_auth_seq_id _struct_site.pdbx_auth_ins_code _struct_site.pdbx_num_residues _struct_site.details AC1 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE MN A 1002' AC2 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE CA A 1003' AC3 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE EDO A 1007' AC4 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE EDO A 1008' AC5 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE EDO A 1009' AC6 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE EDO A 1010' AC7 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE EDO A 1011' AC8 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE MN B 1002' AC9 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE CA B 1003' BC1 Software ? ? ? ? 5 'BINDING SITE FOR MONO-SACCHARIDE NAG A1001 BOUND TO ASN A 33' BC2 Software ? ? ? ? 21 'BINDING SITE FOR CHAIN A OF POLYSACCHARIDE RESIDUES 1004 TO 1006' BC3 Software ? ? ? ? 4 'BINDING SITE FOR MONO-SACCHARIDE NAG B1001 BOUND TO ASN B 33' BC4 Software ? ? ? ? 8 'BINDING SITE FOR DI-SACCHARIDE MAN B1004 AND NAG B1005' # loop_ _struct_site_gen.id _struct_site_gen.site_id _struct_site_gen.pdbx_num_res _struct_site_gen.label_comp_id _struct_site_gen.label_asym_id _struct_site_gen.label_seq_id _struct_site_gen.pdbx_auth_ins_code _struct_site_gen.auth_comp_id _struct_site_gen.auth_asym_id _struct_site_gen.auth_seq_id _struct_site_gen.label_atom_id _struct_site_gen.label_alt_id _struct_site_gen.symmetry _struct_site_gen.details 1 AC1 6 GLU A 124 ? GLU A 145 . ? 1_555 ? 2 AC1 6 ASP A 126 ? ASP A 147 . ? 1_555 ? 3 AC1 6 ASP A 134 ? ASP A 155 . ? 1_555 ? 4 AC1 6 HIS A 139 ? HIS A 160 . ? 1_555 ? 5 AC1 6 HOH S . ? HOH A 1102 . ? 1_555 ? 6 AC1 6 HOH S . ? HOH A 1103 . ? 1_555 ? 7 AC2 6 ASP A 126 ? ASP A 147 . ? 1_555 ? 8 AC2 6 LEU A 128 ? LEU A 149 . ? 1_555 ? 9 AC2 6 ASN A 130 ? ASN A 151 . ? 1_555 ? 10 AC2 6 ASP A 134 ? ASP A 155 . ? 1_555 ? 11 AC2 6 HOH S . ? HOH A 1104 . ? 1_555 ? 12 AC2 6 HOH S . ? HOH A 1105 . ? 1_555 ? 13 AC3 4 SER A 179 ? SER A 200 . ? 1_555 ? 14 AC3 4 HOH S . ? HOH A 1217 . ? 1_555 ? 15 AC3 4 THR B 168 ? THR B 189 . ? 1_555 ? 16 AC3 4 VAL B 177 ? VAL B 198 . ? 1_555 ? 17 AC4 5 THR A 168 ? THR A 189 . ? 1_555 ? 18 AC4 5 VAL A 177 ? VAL A 198 . ? 1_555 ? 19 AC4 5 HOH S . ? HOH A 1218 . ? 1_555 ? 20 AC4 5 LEU B 166 ? LEU B 187 . ? 1_555 ? 21 AC4 5 SER B 179 ? SER B 200 . ? 1_555 ? 22 AC5 8 SER A 2 ? SER A 23 . ? 1_555 ? 23 AC5 8 GLN A 3 ? GLN A 24 . ? 1_555 ? 24 AC5 8 THR A 4 ? THR A 25 . ? 1_555 ? 25 AC5 8 ILE A 55 ? ILE A 76 . ? 1_555 ? 26 AC5 8 GLN A 56 ? GLN A 77 . ? 1_555 ? 27 AC5 8 SER A 232 ? SER A 253 . ? 1_555 ? 28 AC5 8 LEU A 234 ? LEU A 255 . ? 1_555 ? 29 AC5 8 HOH S . ? HOH A 1193 . ? 1_555 ? 30 AC6 6 ILE A 17 ? ILE A 38 . ? 1_555 ? 31 AC6 6 GLN A 19 ? GLN A 40 . ? 1_555 ? 32 AC6 6 GLY A 96 ? GLY A 117 . ? 1_555 ? 33 AC6 6 SER A 97 ? SER A 118 . ? 1_555 ? 34 AC6 6 GLN A 98 ? GLN A 119 . ? 1_555 ? 35 AC6 6 ILE A 206 ? ILE A 227 . ? 1_555 ? 36 AC7 5 PHE A 8 ? PHE A 29 . ? 1_555 ? 37 AC7 5 ARG A 10 ? ARG A 31 . ? 1_555 ? 38 AC7 5 PHE A 11 ? PHE A 32 . ? 1_555 ? 39 AC7 5 ASN A 12 ? ASN A 33 . ? 1_555 ? 40 AC7 5 ASN A 15 ? ASN A 36 . ? 1_555 ? 41 AC8 6 GLU B 124 ? GLU B 145 . ? 1_555 ? 42 AC8 6 ASP B 126 ? ASP B 147 . ? 1_555 ? 43 AC8 6 ASP B 134 ? ASP B 155 . ? 1_555 ? 44 AC8 6 HIS B 139 ? HIS B 160 . ? 1_555 ? 45 AC8 6 HOH T . ? HOH B 1101 . ? 1_555 ? 46 AC8 6 HOH T . ? HOH B 1102 . ? 1_555 ? 47 AC9 6 ASP B 126 ? ASP B 147 . ? 1_555 ? 48 AC9 6 LEU B 128 ? LEU B 149 . ? 1_555 ? 49 AC9 6 ASN B 130 ? ASN B 151 . ? 1_555 ? 50 AC9 6 ASP B 134 ? ASP B 155 . ? 1_555 ? 51 AC9 6 HOH T . ? HOH B 1104 . ? 1_555 ? 52 AC9 6 HOH T . ? HOH B 1105 . ? 1_555 ? 53 BC1 5 ASN A 12 ? ASN A 33 . ? 1_555 ? 54 BC1 5 GLU A 13 ? GLU A 34 . ? 1_555 ? 55 BC1 5 SER A 25 ? SER A 46 . ? 1_555 ? 56 BC1 5 GLU A 203 ? GLU A 224 . ? 3_554 ? 57 BC1 5 TRP A 204 ? TRP A 225 . ? 3_554 ? 58 BC2 21 THR A 61 ? THR A 82 . ? 6_555 ? 59 BC2 21 THR A 62 ? THR A 83 . ? 6_555 ? 60 BC2 21 GLY A 103 ? GLY A 124 . ? 1_555 ? 61 BC2 21 GLY A 104 ? GLY A 125 . ? 1_555 ? 62 BC2 21 LEU A 105 ? LEU A 126 . ? 1_555 ? 63 BC2 21 TYR A 129 ? TYR A 150 . ? 1_555 ? 64 BC2 21 ASN A 130 ? ASN A 151 . ? 1_555 ? 65 BC2 21 HIS A 132 ? HIS A 153 . ? 1_555 ? 66 BC2 21 ILE A 215 ? ILE A 236 . ? 1_555 ? 67 BC2 21 THR A 216 ? THR A 237 . ? 1_555 ? 68 BC2 21 ASN A 219 ? ASN A 240 . ? 1_555 ? 69 BC2 21 HOH S . ? HOH A 1122 . ? 1_555 ? 70 BC2 21 HOH S . ? HOH A 1123 . ? 1_555 ? 71 BC2 21 HOH S . ? HOH A 1124 . ? 1_555 ? 72 BC2 21 HOH S . ? HOH A 1125 . ? 1_555 ? 73 BC2 21 HOH S . ? HOH A 1127 . ? 1_555 ? 74 BC2 21 HOH S . ? HOH A 1130 . ? 1_555 ? 75 BC2 21 HOH S . ? HOH A 1151 . ? 1_555 ? 76 BC2 21 HOH S . ? HOH A 1194 . ? 1_555 ? 77 BC2 21 HOH S . ? HOH A 1195 . ? 1_555 ? 78 BC2 21 HOH S . ? HOH A 1196 . ? 1_555 ? 79 BC3 4 ASN B 12 ? ASN B 33 . ? 1_555 ? 80 BC3 4 SER B 25 ? SER B 46 . ? 1_555 ? 81 BC3 4 GLU B 203 ? GLU B 224 . ? 3_554 ? 82 BC3 4 TRP B 204 ? TRP B 225 . ? 3_554 ? 83 BC4 8 GLY B 103 ? GLY B 124 . ? 1_555 ? 84 BC4 8 GLY B 104 ? GLY B 125 . ? 1_555 ? 85 BC4 8 LEU B 105 ? LEU B 126 . ? 1_555 ? 86 BC4 8 LEU B 128 ? LEU B 149 . ? 1_555 ? 87 BC4 8 ASN B 130 ? ASN B 151 . ? 1_555 ? 88 BC4 8 ILE B 215 ? ILE B 236 . ? 1_555 ? 89 BC4 8 THR B 216 ? THR B 237 . ? 1_555 ? 90 BC4 8 ASN B 219 ? ASN B 240 . ? 1_555 ? # _database_PDB_matrix.entry_id 3WCS _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 3WCS _atom_sites.fract_transf_matrix[1][1] 0.013058 _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] 0.005097 _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] 0.010136 _atom_sites.fract_transf_vector[1] 0.00000 _atom_sites.fract_transf_vector[2] 0.00000 _atom_sites.fract_transf_vector[3] 0.00000 # loop_ _atom_type.symbol C CA MN N O # loop_ _atom_site.group_PDB _atom_site.id _atom_site.type_symbol _atom_site.label_atom_id _atom_site.label_alt_id _atom_site.label_comp_id _atom_site.label_asym_id _atom_site.label_entity_id _atom_site.label_seq_id _atom_site.pdbx_PDB_ins_code _atom_site.Cartn_x _atom_site.Cartn_y _atom_site.Cartn_z _atom_site.occupancy _atom_site.B_iso_or_equiv _atom_site.pdbx_formal_charge _atom_site.auth_seq_id _atom_site.auth_comp_id _atom_site.auth_asym_id _atom_site.auth_atom_id _atom_site.pdbx_PDB_model_num ATOM 1 N N . ALA A 1 1 ? 9.241 59.200 -32.221 1.00 31.65 ? 22 ALA A N 1 ATOM 2 C CA . ALA A 1 1 ? 9.173 58.253 -33.369 1.00 30.59 ? 22 ALA A CA 1 ATOM 3 C C . ALA A 1 1 ? 8.277 57.034 -33.112 1.00 28.67 ? 22 ALA A C 1 ATOM 4 O O . ALA A 1 1 ? 7.202 56.926 -33.713 1.00 29.35 ? 22 ALA A O 1 ATOM 5 C CB . ALA A 1 1 ? 10.556 57.821 -33.734 1.00 34.70 ? 22 ALA A CB 1 ATOM 6 N N . SER A 1 2 ? 8.724 56.087 -32.281 1.00 25.42 ? 23 SER A N 1 ATOM 7 C CA . SER A 1 2 ? 7.786 55.149 -31.649 1.00 24.78 ? 23 SER A CA 1 ATOM 8 C C . SER A 1 2 ? 7.424 55.779 -30.303 1.00 24.40 ? 23 SER A C 1 ATOM 9 O O . SER A 1 2 ? 8.308 56.221 -29.580 1.00 22.39 ? 23 SER A O 1 ATOM 10 C CB . SER A 1 2 ? 8.412 53.789 -31.387 1.00 26.47 ? 23 SER A CB 1 ATOM 11 O OG . SER A 1 2 ? 8.511 52.999 -32.557 1.00 30.11 ? 23 SER A OG 1 ATOM 12 N N . GLN A 1 3 ? 6.138 55.835 -29.960 1.00 21.38 ? 24 GLN A N 1 ATOM 13 C CA . GLN A 1 3 ? 5.744 56.390 -28.664 1.00 24.09 ? 24 GLN A CA 1 ATOM 14 C C . GLN A 1 3 ? 4.698 55.496 -28.013 1.00 23.02 ? 24 GLN A C 1 ATOM 15 O O . GLN A 1 3 ? 3.823 54.965 -28.694 1.00 22.08 ? 24 GLN A O 1 ATOM 16 C CB . GLN A 1 3 ? 5.167 57.807 -28.823 1.00 26.89 ? 24 GLN A CB 1 ATOM 17 C CG . GLN A 1 3 ? 6.151 58.837 -29.341 1.00 31.57 ? 24 GLN A CG 1 ATOM 18 C CD . GLN A 1 3 ? 5.491 60.142 -29.737 1.00 34.75 ? 24 GLN A CD 1 ATOM 19 O OE1 . GLN A 1 3 ? 4.801 60.227 -30.754 1.00 39.10 ? 24 GLN A OE1 1 ATOM 20 N NE2 . GLN A 1 3 ? 5.718 61.175 -28.943 1.00 39.40 ? 24 GLN A NE2 1 ATOM 21 N N . THR A 1 4 ? 4.794 55.328 -26.695 1.00 22.89 ? 25 THR A N 1 ATOM 22 C CA . THR A 1 4 ? 3.794 54.563 -25.956 1.00 22.50 ? 25 THR A CA 1 ATOM 23 C C . THR A 1 4 ? 3.483 55.305 -24.675 1.00 22.65 ? 25 THR A C 1 ATOM 24 O O . THR A 1 4 ? 4.369 55.863 -24.045 1.00 20.90 ? 25 THR A O 1 ATOM 25 C CB . THR A 1 4 ? 4.301 53.157 -25.587 1.00 23.69 ? 25 THR A CB 1 ATOM 26 O OG1 . THR A 1 4 ? 4.641 52.442 -26.767 1.00 26.47 ? 25 THR A OG1 1 ATOM 27 C CG2 . THR A 1 4 ? 3.232 52.355 -24.816 1.00 27.00 ? 25 THR A CG2 1 ATOM 28 N N . SER A 1 5 ? 2.214 55.335 -24.273 1.00 19.39 ? 26 SER A N 1 ATOM 29 C CA . SER A 1 5 ? 1.923 55.843 -22.955 1.00 20.71 ? 26 SER A CA 1 ATOM 30 C C . SER A 1 5 ? 0.652 55.189 -22.433 1.00 20.21 ? 26 SER A C 1 ATOM 31 O O . SER A 1 5 ? -0.198 54.745 -23.204 1.00 21.81 ? 26 SER A O 1 ATOM 32 C CB . SER A 1 5 ? 1.775 57.363 -22.946 1.00 22.02 ? 26 SER A CB 1 ATOM 33 O OG . SER A 1 5 ? 0.735 57.764 -23.809 1.00 27.55 ? 26 SER A OG 1 ATOM 34 N N . PHE A 1 6 ? 0.539 55.133 -21.117 1.00 18.21 ? 27 PHE A N 1 ATOM 35 C CA . PHE A 1 6 ? -0.704 54.669 -20.502 1.00 17.39 ? 27 PHE A CA 1 ATOM 36 C C . PHE A 1 6 ? -0.793 55.270 -19.114 1.00 18.38 ? 27 PHE A C 1 ATOM 37 O O . PHE A 1 6 ? 0.201 55.652 -18.540 1.00 17.15 ? 27 PHE A O 1 ATOM 38 C CB . PHE A 1 6 ? -0.836 53.133 -20.467 1.00 18.07 ? 27 PHE A CB 1 ATOM 39 C CG . PHE A 1 6 ? 0.341 52.385 -19.851 1.00 18.51 ? 27 PHE A CG 1 ATOM 40 C CD1 . PHE A 1 6 ? 1.313 51.800 -20.670 1.00 19.79 ? 27 PHE A CD1 1 ATOM 41 C CD2 . PHE A 1 6 ? 0.450 52.220 -18.481 1.00 19.47 ? 27 PHE A CD2 1 ATOM 42 C CE1 . PHE A 1 6 ? 2.384 51.094 -20.114 1.00 19.55 ? 27 PHE A CE1 1 ATOM 43 C CE2 . PHE A 1 6 ? 1.520 51.502 -17.921 1.00 18.99 ? 27 PHE A CE2 1 ATOM 44 C CZ . PHE A 1 6 ? 2.476 50.943 -18.738 1.00 19.34 ? 27 PHE A CZ 1 ATOM 45 N N . SER A 1 7 ? -2.001 55.374 -18.571 1.00 16.63 ? 28 SER A N 1 ATOM 46 C CA . SER A 1 7 ? -2.133 55.915 -17.229 1.00 17.49 ? 28 SER A CA 1 ATOM 47 C C . SER A 1 7 ? -3.373 55.283 -16.625 1.00 18.31 ? 28 SER A C 1 ATOM 48 O O . SER A 1 7 ? -4.458 55.337 -17.237 1.00 18.56 ? 28 SER A O 1 ATOM 49 C CB . SER A 1 7 ? -2.275 57.444 -17.267 1.00 18.21 ? 28 SER A CB 1 ATOM 50 O OG . SER A 1 7 ? -2.363 57.981 -15.943 1.00 21.26 ? 28 SER A OG 1 ATOM 51 N N . PHE A 1 8 ? -3.224 54.687 -15.441 1.00 17.69 ? 29 PHE A N 1 ATOM 52 C CA . PHE A 1 8 ? -4.372 54.048 -14.779 1.00 18.53 ? 29 PHE A CA 1 ATOM 53 C C . PHE A 1 8 ? -4.508 54.545 -13.348 1.00 19.02 ? 29 PHE A C 1 ATOM 54 O O . PHE A 1 8 ? -3.530 54.596 -12.610 1.00 17.44 ? 29 PHE A O 1 ATOM 55 C CB . PHE A 1 8 ? -4.240 52.515 -14.793 1.00 19.51 ? 29 PHE A CB 1 ATOM 56 C CG . PHE A 1 8 ? -3.957 51.944 -16.158 1.00 21.55 ? 29 PHE A CG 1 ATOM 57 C CD1 . PHE A 1 8 ? -4.914 52.021 -17.165 1.00 22.41 ? 29 PHE A CD1 1 ATOM 58 C CD2 . PHE A 1 8 ? -2.716 51.344 -16.449 1.00 21.54 ? 29 PHE A CD2 1 ATOM 59 C CE1 . PHE A 1 8 ? -4.652 51.522 -18.442 1.00 23.38 ? 29 PHE A CE1 1 ATOM 60 C CE2 . PHE A 1 8 ? -2.458 50.832 -17.725 1.00 21.80 ? 29 PHE A CE2 1 ATOM 61 C CZ . PHE A 1 8 ? -3.425 50.928 -18.719 1.00 22.93 ? 29 PHE A CZ 1 ATOM 62 N N . GLN A 1 9 ? -5.725 54.930 -12.961 1.00 18.71 ? 30 GLN A N 1 ATOM 63 C CA . GLN A 1 9 ? -5.992 55.279 -11.554 1.00 19.87 ? 30 GLN A CA 1 ATOM 64 C C . GLN A 1 9 ? -6.563 54.087 -10.797 1.00 19.41 ? 30 GLN A C 1 ATOM 65 O O . GLN A 1 9 ? -6.513 54.051 -9.558 1.00 18.72 ? 30 GLN A O 1 ATOM 66 C CB . GLN A 1 9 ? -6.937 56.488 -11.416 1.00 21.22 ? 30 GLN A CB 1 ATOM 67 C CG . GLN A 1 9 ? -6.377 57.780 -12.000 1.00 25.34 ? 30 GLN A CG 1 ATOM 68 C CD . GLN A 1 9 ? -4.997 58.118 -11.466 1.00 29.06 ? 30 GLN A CD 1 ATOM 69 O OE1 . GLN A 1 9 ? -4.040 58.219 -12.233 1.00 31.98 ? 30 GLN A OE1 1 ATOM 70 N NE2 . GLN A 1 9 ? -4.885 58.276 -10.147 1.00 28.24 ? 30 GLN A NE2 1 ATOM 71 N N . ARG A 1 10 ? -7.101 53.134 -11.557 1.00 18.66 ? 31 ARG A N 1 ATOM 72 C CA . ARG A 1 10 ? -7.594 51.870 -11.052 1.00 18.09 ? 31 ARG A CA 1 ATOM 73 C C . ARG A 1 10 ? -7.161 50.776 -11.997 1.00 17.39 ? 31 ARG A C 1 ATOM 74 O O . ARG A 1 10 ? -7.095 51.000 -13.223 1.00 18.40 ? 31 ARG A O 1 ATOM 75 C CB . ARG A 1 10 ? -9.136 51.894 -10.993 1.00 17.70 ? 31 ARG A CB 1 ATOM 76 C CG . ARG A 1 10 ? -9.707 52.830 -9.933 1.00 18.96 ? 31 ARG A CG 1 ATOM 77 C CD . ARG A 1 10 ? -9.259 52.467 -8.514 1.00 20.25 ? 31 ARG A CD 1 ATOM 78 N NE . ARG A 1 10 ? -9.921 53.330 -7.537 1.00 19.50 ? 31 ARG A NE 1 ATOM 79 C CZ . ARG A 1 10 ? -9.472 54.511 -7.120 1.00 21.90 ? 31 ARG A CZ 1 ATOM 80 N NH1 . ARG A 1 10 ? -8.308 55.003 -7.579 1.00 21.55 ? 31 ARG A NH1 1 ATOM 81 N NH2 . ARG A 1 10 ? -10.183 55.203 -6.233 1.00 22.11 ? 31 ARG A NH2 1 ATOM 82 N N . PHE A 1 11 ? -6.934 49.592 -11.454 1.00 17.66 ? 32 PHE A N 1 ATOM 83 C CA . PHE A 1 11 ? -6.370 48.473 -12.202 1.00 18.60 ? 32 PHE A CA 1 ATOM 84 C C . PHE A 1 11 ? -7.383 47.384 -12.490 1.00 19.30 ? 32 PHE A C 1 ATOM 85 O O . PHE A 1 11 ? -8.414 47.256 -11.802 1.00 18.79 ? 32 PHE A O 1 ATOM 86 C CB . PHE A 1 11 ? -5.144 47.872 -11.488 1.00 18.31 ? 32 PHE A CB 1 ATOM 87 C CG . PHE A 1 11 ? -3.992 48.827 -11.346 1.00 18.49 ? 32 PHE A CG 1 ATOM 88 C CD1 . PHE A 1 11 ? -3.122 49.049 -12.413 1.00 18.73 ? 32 PHE A CD1 1 ATOM 89 C CD2 . PHE A 1 11 ? -3.778 49.522 -10.150 1.00 18.34 ? 32 PHE A CD2 1 ATOM 90 C CE1 . PHE A 1 11 ? -2.048 49.945 -12.282 1.00 19.52 ? 32 PHE A CE1 1 ATOM 91 C CE2 . PHE A 1 11 ? -2.722 50.420 -10.013 1.00 19.33 ? 32 PHE A CE2 1 ATOM 92 C CZ . PHE A 1 11 ? -1.853 50.637 -11.083 1.00 19.20 ? 32 PHE A CZ 1 ATOM 93 N N . ASN A 1 12 ? -7.081 46.622 -13.532 1.00 18.86 ? 33 ASN A N 1 ATOM 94 C CA . ASN A 1 12 ? -7.795 45.422 -13.878 1.00 20.60 ? 33 ASN A CA 1 ATOM 95 C C . ASN A 1 12 ? -6.834 44.426 -14.489 1.00 20.77 ? 33 ASN A C 1 ATOM 96 O O . ASN A 1 12 ? -5.920 44.812 -15.208 1.00 20.73 ? 33 ASN A O 1 ATOM 97 C CB . ASN A 1 12 ? -8.927 45.763 -14.868 1.00 22.36 ? 33 ASN A CB 1 ATOM 98 C CG . ASN A 1 12 ? -9.793 44.553 -15.179 1.00 23.80 ? 33 ASN A CG 1 ATOM 99 O OD1 . ASN A 1 12 ? -9.436 43.726 -16.009 1.00 22.53 ? 33 ASN A OD1 1 ATOM 100 N ND2 . ASN A 1 12 ? -10.926 44.431 -14.483 1.00 26.98 ? 33 ASN A ND2 1 ATOM 101 N N . GLU A 1 13 ? -7.048 43.137 -14.237 1.00 20.81 ? 34 GLU A N 1 ATOM 102 C CA . GLU A 1 13 ? -6.116 42.101 -14.691 1.00 22.80 ? 34 GLU A CA 1 ATOM 103 C C . GLU A 1 13 ? -6.036 41.938 -16.221 1.00 20.89 ? 34 GLU A C 1 ATOM 104 O O . GLU A 1 13 ? -5.063 41.406 -16.735 1.00 20.37 ? 34 GLU A O 1 ATOM 105 C CB . GLU A 1 13 ? -6.443 40.755 -14.014 1.00 26.08 ? 34 GLU A CB 1 ATOM 106 C CG . GLU A 1 13 ? -7.836 40.198 -14.298 1.00 32.05 ? 34 GLU A CG 1 ATOM 107 C CD . GLU A 1 13 ? -8.959 40.766 -13.421 1.00 35.54 ? 34 GLU A CD 1 ATOM 108 O OE1 . GLU A 1 13 ? -8.768 41.768 -12.685 1.00 34.53 ? 34 GLU A OE1 1 ATOM 109 O OE2 . GLU A 1 13 ? -10.087 40.207 -13.498 1.00 39.84 ? 34 GLU A OE2 1 ATOM 110 N N . THR A 1 14 ? -7.061 42.408 -16.936 1.00 18.96 ? 35 THR A N 1 ATOM 111 C CA . THR A 1 14 ? -7.166 42.141 -18.386 1.00 19.41 ? 35 THR A CA 1 ATOM 112 C C . THR A 1 14 ? -5.966 42.605 -19.218 1.00 19.27 ? 35 THR A C 1 ATOM 113 O O . THR A 1 14 ? -5.581 41.917 -20.157 1.00 20.46 ? 35 THR A O 1 ATOM 114 C CB . THR A 1 14 ? -8.454 42.723 -18.977 1.00 20.15 ? 35 THR A CB 1 ATOM 115 O OG1 . THR A 1 14 ? -9.547 42.219 -18.211 1.00 21.40 ? 35 THR A OG1 1 ATOM 116 C CG2 . THR A 1 14 ? -8.644 42.267 -20.435 1.00 21.27 ? 35 THR A CG2 1 ATOM 117 N N . ASN A 1 15 ? -5.385 43.755 -18.866 1.00 18.16 ? 36 ASN A N 1 ATOM 118 C CA . ASN A 1 15 ? -4.242 44.301 -19.612 1.00 17.87 ? 36 ASN A CA 1 ATOM 119 C C . ASN A 1 15 ? -2.915 44.181 -18.853 1.00 17.98 ? 36 ASN A C 1 ATOM 120 O O . ASN A 1 15 ? -1.944 44.854 -19.194 1.00 19.85 ? 36 ASN A O 1 ATOM 121 C CB . ASN A 1 15 ? -4.491 45.759 -20.061 1.00 17.53 ? 36 ASN A CB 1 ATOM 122 C CG . ASN A 1 15 ? -4.657 46.730 -18.898 1.00 17.50 ? 36 ASN A CG 1 ATOM 123 O OD1 . ASN A 1 15 ? -4.684 46.330 -17.722 1.00 18.59 ? 36 ASN A OD1 1 ATOM 124 N ND2 . ASN A 1 15 ? -4.776 48.023 -19.221 1.00 18.38 ? 36 ASN A ND2 1 ATOM 125 N N . LEU A 1 16 ? -2.905 43.347 -17.818 1.00 17.03 ? 37 LEU A N 1 ATOM 126 C CA . LEU A 1 16 ? -1.698 43.094 -17.017 1.00 17.60 ? 37 LEU A CA 1 ATOM 127 C C . LEU A 1 16 ? -1.268 41.638 -17.125 1.00 18.41 ? 37 LEU A C 1 ATOM 128 O O . LEU A 1 16 ? -2.077 40.760 -17.368 1.00 18.55 ? 37 LEU A O 1 ATOM 129 C CB . LEU A 1 16 ? -1.920 43.447 -15.537 1.00 17.15 ? 37 LEU A CB 1 ATOM 130 C CG . LEU A 1 16 ? -2.358 44.876 -15.239 1.00 17.63 ? 37 LEU A CG 1 ATOM 131 C CD1 . LEU A 1 16 ? -2.611 45.025 -13.740 1.00 18.08 ? 37 LEU A CD1 1 ATOM 132 C CD2 . LEU A 1 16 ? -1.381 45.933 -15.722 1.00 17.88 ? 37 LEU A CD2 1 ATOM 133 N N . ILE A 1 17 ? 0.035 41.393 -16.976 1.00 17.84 ? 38 ILE A N 1 ATOM 134 C CA . ILE A 1 17 ? 0.551 40.052 -16.790 1.00 19.09 ? 38 ILE A CA 1 ATOM 135 C C . ILE A 1 17 ? 0.880 39.928 -15.307 1.00 19.80 ? 38 ILE A C 1 ATOM 136 O O . ILE A 1 17 ? 1.771 40.616 -14.812 1.00 20.10 ? 38 ILE A O 1 ATOM 137 C CB . ILE A 1 17 ? 1.824 39.818 -17.641 1.00 20.81 ? 38 ILE A CB 1 ATOM 138 C CG1 . ILE A 1 17 ? 1.477 39.975 -19.132 1.00 22.89 ? 38 ILE A CG1 1 ATOM 139 C CG2 . ILE A 1 17 ? 2.420 38.435 -17.347 1.00 21.11 ? 38 ILE A CG2 1 ATOM 140 C CD1 . ILE A 1 17 ? 2.667 40.368 -19.996 1.00 25.02 ? 38 ILE A CD1 1 ATOM 141 N N . LEU A 1 18 ? 0.148 39.064 -14.601 1.00 19.32 ? 39 LEU A N 1 ATOM 142 C CA . LEU A 1 18 ? 0.351 38.886 -13.170 1.00 19.30 ? 39 LEU A CA 1 ATOM 143 C C . LEU A 1 18 ? 1.058 37.588 -12.878 1.00 19.40 ? 39 LEU A C 1 ATOM 144 O O . LEU A 1 18 ? 0.706 36.526 -13.425 1.00 19.93 ? 39 LEU A O 1 ATOM 145 C CB . LEU A 1 18 ? -0.990 38.906 -12.422 1.00 18.89 ? 39 LEU A CB 1 ATOM 146 C CG . LEU A 1 18 ? -1.866 40.131 -12.641 1.00 19.31 ? 39 LEU A CG 1 ATOM 147 C CD1 . LEU A 1 18 ? -3.194 39.950 -11.898 1.00 19.78 ? 39 LEU A CD1 1 ATOM 148 C CD2 . LEU A 1 18 ? -1.153 41.380 -12.166 1.00 19.77 ? 39 LEU A CD2 1 ATOM 149 N N . GLN A 1 19 ? 2.069 37.675 -12.016 1.00 19.15 ? 40 GLN A N 1 ATOM 150 C CA . GLN A 1 19 ? 2.860 36.518 -11.647 1.00 18.49 ? 40 GLN A CA 1 ATOM 151 C C . GLN A 1 19 ? 2.821 36.234 -10.153 1.00 18.34 ? 40 GLN A C 1 ATOM 152 O O . GLN A 1 19 ? 2.880 37.152 -9.331 1.00 18.08 ? 40 GLN A O 1 ATOM 153 C CB . GLN A 1 19 ? 4.312 36.730 -12.071 1.00 19.00 ? 40 GLN A CB 1 ATOM 154 C CG . GLN A 1 19 ? 4.449 36.903 -13.581 1.00 18.89 ? 40 GLN A CG 1 ATOM 155 C CD . GLN A 1 19 ? 5.898 36.968 -14.042 1.00 19.64 ? 40 GLN A CD 1 ATOM 156 O OE1 . GLN A 1 19 ? 6.780 37.424 -13.316 1.00 19.27 ? 40 GLN A OE1 1 ATOM 157 N NE2 . GLN A 1 19 ? 6.140 36.520 -15.264 1.00 20.29 ? 40 GLN A NE2 1 ATOM 158 N N . ARG A 1 20 ? 2.743 34.946 -9.824 1.00 18.91 ? 41 ARG A N 1 ATOM 159 C CA . ARG A 1 20 ? 2.793 34.474 -8.439 1.00 21.16 ? 41 ARG A CA 1 ATOM 160 C C . ARG A 1 20 ? 1.685 35.058 -7.592 1.00 20.58 ? 41 ARG A C 1 ATOM 161 O O . ARG A 1 20 ? 0.508 34.866 -7.928 1.00 20.63 ? 41 ARG A O 1 ATOM 162 C CB . ARG A 1 20 ? 4.181 34.683 -7.833 1.00 23.21 ? 41 ARG A CB 1 ATOM 163 C CG . ARG A 1 20 ? 5.222 33.779 -8.437 1.00 28.75 ? 41 ARG A CG 1 ATOM 164 C CD . ARG A 1 20 ? 5.309 32.432 -7.718 1.00 29.93 ? 41 ARG A CD 1 ATOM 165 N NE . ARG A 1 20 ? 6.707 32.027 -7.791 1.00 34.66 ? 41 ARG A NE 1 ATOM 166 C CZ . ARG A 1 20 ? 7.575 32.074 -6.788 1.00 34.84 ? 41 ARG A CZ 1 ATOM 167 N NH1 . ARG A 1 20 ? 7.211 32.439 -5.554 1.00 38.83 ? 41 ARG A NH1 1 ATOM 168 N NH2 . ARG A 1 20 ? 8.822 31.698 -7.016 1.00 40.31 ? 41 ARG A NH2 1 ATOM 169 N N . ASP A 1 21 ? 2.016 35.776 -6.515 1.00 19.74 ? 42 ASP A N 1 ATOM 170 C CA . ASP A 1 21 ? 0.963 36.261 -5.600 1.00 20.38 ? 42 ASP A CA 1 ATOM 171 C C . ASP A 1 21 ? 0.236 37.546 -5.997 1.00 20.02 ? 42 ASP A C 1 ATOM 172 O O . ASP A 1 21 ? -0.681 37.951 -5.299 1.00 20.15 ? 42 ASP A O 1 ATOM 173 C CB . ASP A 1 21 ? 1.509 36.433 -4.171 1.00 20.85 ? 42 ASP A CB 1 ATOM 174 C CG . ASP A 1 21 ? 2.085 35.158 -3.614 1.00 22.02 ? 42 ASP A CG 1 ATOM 175 O OD1 . ASP A 1 21 ? 1.759 34.068 -4.150 1.00 22.08 ? 42 ASP A OD1 1 ATOM 176 O OD2 . ASP A 1 21 ? 2.874 35.245 -2.648 1.00 22.26 ? 42 ASP A OD2 1 ATOM 177 N N . ALA A 1 22 ? 0.632 38.187 -7.102 1.00 19.09 ? 43 ALA A N 1 ATOM 178 C CA . ALA A 1 22 ? 0.055 39.463 -7.488 1.00 17.84 ? 43 ALA A CA 1 ATOM 179 C C . ALA A 1 22 ? -1.424 39.316 -7.828 1.00 17.91 ? 43 ALA A C 1 ATOM 180 O O . ALA A 1 22 ? -1.788 38.394 -8.549 1.00 19.35 ? 43 ALA A O 1 ATOM 181 C CB . ALA A 1 22 ? 0.807 40.032 -8.688 1.00 17.05 ? 43 ALA A CB 1 ATOM 182 N N . THR A 1 23 ? -2.244 40.217 -7.304 1.00 17.61 ? 44 THR A N 1 ATOM 183 C CA . THR A 1 23 ? -3.689 40.236 -7.620 1.00 18.22 ? 44 THR A CA 1 ATOM 184 C C . THR A 1 23 ? -4.164 41.648 -7.890 1.00 18.11 ? 44 THR A C 1 ATOM 185 O O . THR A 1 23 ? -3.492 42.612 -7.539 1.00 19.44 ? 44 THR A O 1 ATOM 186 C CB . THR A 1 23 ? -4.548 39.679 -6.460 1.00 18.43 ? 44 THR A CB 1 ATOM 187 O OG1 . THR A 1 23 ? -4.336 40.462 -5.286 1.00 20.97 ? 44 THR A OG1 1 ATOM 188 C CG2 . THR A 1 23 ? -4.254 38.213 -6.173 1.00 20.27 ? 44 THR A CG2 1 ATOM 189 N N . VAL A 1 24 ? -5.349 41.774 -8.500 1.00 17.97 ? 45 VAL A N 1 ATOM 190 C CA . VAL A 1 24 ? -6.027 43.044 -8.547 1.00 17.35 ? 45 VAL A CA 1 ATOM 191 C C . VAL A 1 24 ? -7.266 42.886 -7.653 1.00 17.66 ? 45 VAL A C 1 ATOM 192 O O . VAL A 1 24 ? -8.031 41.925 -7.831 1.00 17.26 ? 45 VAL A O 1 ATOM 193 C CB . VAL A 1 24 ? -6.448 43.430 -9.982 1.00 17.80 ? 45 VAL A CB 1 ATOM 194 C CG1 . VAL A 1 24 ? -7.273 44.694 -9.960 1.00 16.91 ? 45 VAL A CG1 1 ATOM 195 C CG2 . VAL A 1 24 ? -5.200 43.644 -10.865 1.00 18.35 ? 45 VAL A CG2 1 ATOM 196 N N . SER A 1 25 ? -7.414 43.793 -6.682 1.00 17.19 ? 46 SER A N 1 ATOM 197 C CA . SER A 1 25 ? -8.515 43.716 -5.684 1.00 17.63 ? 46 SER A CA 1 ATOM 198 C C . SER A 1 25 ? -9.826 44.222 -6.248 1.00 18.57 ? 46 SER A C 1 ATOM 199 O O . SER A 1 25 ? -9.865 44.839 -7.299 1.00 18.18 ? 46 SER A O 1 ATOM 200 C CB . SER A 1 25 ? -8.196 44.546 -4.449 1.00 16.67 ? 46 SER A CB 1 ATOM 201 O OG . SER A 1 25 ? -8.351 45.955 -4.675 1.00 16.78 ? 46 SER A OG 1 ATOM 202 N N . SER A 1 26 ? -10.896 44.022 -5.485 1.00 19.72 ? 47 SER A N 1 ATOM 203 C CA . SER A 1 26 ? -12.207 44.507 -5.914 1.00 19.78 ? 47 SER A CA 1 ATOM 204 C C . SER A 1 26 ? -12.307 46.045 -5.907 1.00 19.15 ? 47 SER A C 1 ATOM 205 O O . SER A 1 26 ? -13.262 46.618 -6.466 1.00 20.10 ? 47 SER A O 1 ATOM 206 C CB . SER A 1 26 ? -13.293 43.854 -5.056 1.00 21.39 ? 47 SER A CB 1 ATOM 207 O OG . SER A 1 26 ? -13.134 44.265 -3.722 1.00 24.07 ? 47 SER A OG 1 ATOM 208 N N . LYS A 1 27 ? -11.311 46.708 -5.297 1.00 17.16 ? 48 LYS A N 1 ATOM 209 C CA . LYS A 1 27 ? -11.205 48.158 -5.303 1.00 17.03 ? 48 LYS A CA 1 ATOM 210 C C . LYS A 1 27 ? -10.269 48.646 -6.425 1.00 17.49 ? 48 LYS A C 1 ATOM 211 O O . LYS A 1 27 ? -10.016 49.845 -6.527 1.00 18.40 ? 48 LYS A O 1 ATOM 212 C CB . LYS A 1 27 ? -10.664 48.662 -3.972 1.00 19.40 ? 48 LYS A CB 1 ATOM 213 C CG . LYS A 1 27 ? -11.576 48.349 -2.805 1.00 19.32 ? 48 LYS A CG 1 ATOM 214 C CD . LYS A 1 27 ? -11.090 48.981 -1.521 1.00 20.20 ? 48 LYS A CD 1 ATOM 215 C CE . LYS A 1 27 ? -12.057 48.650 -0.394 1.00 21.70 ? 48 LYS A CE 1 ATOM 216 N NZ . LYS A 1 27 ? -11.612 49.293 0.893 1.00 24.33 ? 48 LYS A NZ 1 ATOM 217 N N . GLY A 1 28 ? -9.751 47.709 -7.215 1.00 18.16 ? 49 GLY A N 1 ATOM 218 C CA . GLY A 1 28 ? -8.958 48.053 -8.399 1.00 18.10 ? 49 GLY A CA 1 ATOM 219 C C . GLY A 1 28 ? -7.557 48.444 -7.950 1.00 18.79 ? 49 GLY A C 1 ATOM 220 O O . GLY A 1 28 ? -6.905 49.276 -8.585 1.00 18.65 ? 49 GLY A O 1 ATOM 221 N N . GLN A 1 29 ? -7.137 47.914 -6.805 1.00 18.28 ? 50 GLN A N 1 ATOM 222 C CA . GLN A 1 29 ? -5.747 48.115 -6.353 1.00 17.37 ? 50 GLN A CA 1 ATOM 223 C C . GLN A 1 29 ? -4.876 46.962 -6.816 1.00 16.95 ? 50 GLN A C 1 ATOM 224 O O . GLN A 1 29 ? -5.274 45.800 -6.800 1.00 17.04 ? 50 GLN A O 1 ATOM 225 C CB . GLN A 1 29 ? -5.728 48.248 -4.828 1.00 19.16 ? 50 GLN A CB 1 ATOM 226 C CG . GLN A 1 29 ? -6.502 49.459 -4.343 1.00 22.26 ? 50 GLN A CG 1 ATOM 227 C CD . GLN A 1 29 ? -6.395 49.676 -2.850 1.00 24.80 ? 50 GLN A CD 1 ATOM 228 O OE1 . GLN A 1 29 ? -5.883 48.834 -2.127 1.00 26.38 ? 50 GLN A OE1 1 ATOM 229 N NE2 . GLN A 1 29 ? -6.865 50.825 -2.386 1.00 25.70 ? 50 GLN A NE2 1 ATOM 230 N N . LEU A 1 30 ? -3.654 47.268 -7.265 1.00 17.23 ? 51 LEU A N 1 ATOM 231 C CA . LEU A 1 30 ? -2.741 46.222 -7.666 1.00 15.98 ? 51 LEU A CA 1 ATOM 232 C C . LEU A 1 30 ? -1.949 45.768 -6.445 1.00 17.79 ? 51 LEU A C 1 ATOM 233 O O . LEU A 1 30 ? -1.037 46.463 -6.002 1.00 16.23 ? 51 LEU A O 1 ATOM 234 C CB . LEU A 1 30 ? -1.834 46.721 -8.805 1.00 16.36 ? 51 LEU A CB 1 ATOM 235 C CG . LEU A 1 30 ? -0.681 45.835 -9.312 1.00 16.18 ? 51 LEU A CG 1 ATOM 236 C CD1 . LEU A 1 30 ? -1.157 44.471 -9.812 1.00 16.17 ? 51 LEU A CD1 1 ATOM 237 C CD2 . LEU A 1 30 ? 0.041 46.582 -10.418 1.00 16.97 ? 51 LEU A CD2 1 ATOM 238 N N . ARG A 1 31 ? -2.332 44.620 -5.887 1.00 17.04 ? 52 ARG A N 1 ATOM 239 C CA . ARG A 1 31 ? -1.748 44.149 -4.623 1.00 16.79 ? 52 ARG A CA 1 ATOM 240 C C . ARG A 1 31 ? -0.656 43.156 -4.989 1.00 16.44 ? 52 ARG A C 1 ATOM 241 O O . ARG A 1 31 ? -0.904 41.994 -5.313 1.00 16.05 ? 52 ARG A O 1 ATOM 242 C CB . ARG A 1 31 ? -2.816 43.513 -3.729 1.00 16.63 ? 52 ARG A CB 1 ATOM 243 C CG . ARG A 1 31 ? -4.030 44.412 -3.557 1.00 17.36 ? 52 ARG A CG 1 ATOM 244 C CD . ARG A 1 31 ? -4.767 44.104 -2.256 1.00 18.29 ? 52 ARG A CD 1 ATOM 245 N NE . ARG A 1 31 ? -4.103 44.760 -1.123 1.00 19.81 ? 52 ARG A NE 1 ATOM 246 C CZ . ARG A 1 31 ? -4.605 44.810 0.108 1.00 20.98 ? 52 ARG A CZ 1 ATOM 247 N NH1 . ARG A 1 31 ? -5.767 44.210 0.363 1.00 21.94 ? 52 ARG A NH1 1 ATOM 248 N NH2 . ARG A 1 31 ? -3.959 45.466 1.068 1.00 20.80 ? 52 ARG A NH2 1 ATOM 249 N N . LEU A 1 32 ? 0.586 43.616 -4.974 1.00 17.07 ? 53 LEU A N 1 ATOM 250 C CA . LEU A 1 32 ? 1.639 42.765 -5.477 1.00 17.53 ? 53 LEU A CA 1 ATOM 251 C C . LEU A 1 32 ? 1.897 41.529 -4.628 1.00 18.69 ? 53 LEU A C 1 ATOM 252 O O . LEU A 1 32 ? 2.221 40.476 -5.159 1.00 18.61 ? 53 LEU A O 1 ATOM 253 C CB . LEU A 1 32 ? 2.934 43.562 -5.635 1.00 17.07 ? 53 LEU A CB 1 ATOM 254 C CG . LEU A 1 32 ? 2.847 44.768 -6.585 1.00 17.41 ? 53 LEU A CG 1 ATOM 255 C CD1 . LEU A 1 32 ? 4.102 45.617 -6.432 1.00 16.87 ? 53 LEU A CD1 1 ATOM 256 C CD2 . LEU A 1 32 ? 2.667 44.329 -8.042 1.00 17.32 ? 53 LEU A CD2 1 ATOM 257 N N . THR A 1 33 ? 1.769 41.668 -3.312 1.00 17.63 ? 54 THR A N 1 ATOM 258 C CA . THR A 1 33 ? 1.989 40.538 -2.420 1.00 17.74 ? 54 THR A CA 1 ATOM 259 C C . THR A 1 33 ? 0.707 40.164 -1.691 1.00 18.41 ? 54 THR A C 1 ATOM 260 O O . THR A 1 33 ? -0.247 40.932 -1.669 1.00 19.54 ? 54 THR A O 1 ATOM 261 C CB . THR A 1 33 ? 3.127 40.804 -1.425 1.00 16.85 ? 54 THR A CB 1 ATOM 262 O OG1 . THR A 1 33 ? 2.992 42.123 -0.864 1.00 17.48 ? 54 THR A OG1 1 ATOM 263 C CG2 . THR A 1 33 ? 4.467 40.715 -2.164 1.00 17.74 ? 54 THR A CG2 1 ATOM 264 N N . ASN A 1 34 ? 0.699 38.969 -1.119 1.00 19.15 ? 55 ASN A N 1 ATOM 265 C CA . ASN A 1 34 ? -0.523 38.387 -0.563 1.00 20.99 ? 55 ASN A CA 1 ATOM 266 C C . ASN A 1 34 ? -1.053 39.092 0.681 1.00 21.08 ? 55 ASN A C 1 ATOM 267 O O . ASN A 1 34 ? -0.295 39.467 1.570 1.00 20.02 ? 55 ASN A O 1 ATOM 268 C CB . ASN A 1 34 ? -0.300 36.890 -0.268 1.00 21.49 ? 55 ASN A CB 1 ATOM 269 C CG . ASN A 1 34 ? -1.591 36.183 0.069 1.00 23.52 ? 55 ASN A CG 1 ATOM 270 O OD1 . ASN A 1 34 ? -2.438 35.977 -0.801 1.00 25.04 ? 55 ASN A OD1 1 ATOM 271 N ND2 . ASN A 1 34 ? -1.770 35.843 1.345 1.00 23.55 ? 55 ASN A ND2 1 ATOM 272 N N . VAL A 1 35 ? -2.377 39.262 0.738 1.00 20.84 ? 56 VAL A N 1 ATOM 273 C CA . VAL A 1 35 ? -3.030 39.827 1.908 1.00 23.27 ? 56 VAL A CA 1 ATOM 274 C C . VAL A 1 35 ? -4.173 38.853 2.227 1.00 25.36 ? 56 VAL A C 1 ATOM 275 O O . VAL A 1 35 ? -4.912 38.460 1.326 1.00 26.29 ? 56 VAL A O 1 ATOM 276 C CB . VAL A 1 35 ? -3.541 41.273 1.640 1.00 24.13 ? 56 VAL A CB 1 ATOM 277 C CG1 . VAL A 1 35 ? -4.279 41.840 2.847 1.00 25.51 ? 56 VAL A CG1 1 ATOM 278 C CG2 . VAL A 1 35 ? -2.392 42.206 1.239 1.00 23.84 ? 56 VAL A CG2 1 ATOM 279 N N . ASN A 1 36 ? -4.292 38.414 3.481 1.00 25.87 ? 57 ASN A N 1 ATOM 280 C CA . ASN A 1 36 ? -5.303 37.387 3.790 1.00 26.96 ? 57 ASN A CA 1 ATOM 281 C C . ASN A 1 36 ? -6.682 38.022 3.953 1.00 28.68 ? 57 ASN A C 1 ATOM 282 O O . ASN A 1 36 ? -6.816 39.235 3.796 1.00 25.83 ? 57 ASN A O 1 ATOM 283 C CB . ASN A 1 36 ? -4.900 36.541 5.009 1.00 27.42 ? 57 ASN A CB 1 ATOM 284 C CG . ASN A 1 36 ? -4.841 37.342 6.300 1.00 27.36 ? 57 ASN A CG 1 ATOM 285 O OD1 . ASN A 1 36 ? -5.486 38.382 6.448 1.00 27.42 ? 57 ASN A OD1 1 ATOM 286 N ND2 . ASN A 1 36 ? -4.075 36.834 7.263 1.00 29.34 ? 57 ASN A ND2 1 ATOM 287 N N . ASP A 1 37 ? -7.693 37.209 4.265 1.00 31.10 ? 58 ASP A N 1 ATOM 288 C CA . ASP A 1 37 ? -9.064 37.712 4.397 1.00 34.62 ? 58 ASP A CA 1 ATOM 289 C C . ASP A 1 37 ? -9.263 38.658 5.574 1.00 34.94 ? 58 ASP A C 1 ATOM 290 O O . ASP A 1 37 ? -10.270 39.375 5.622 1.00 35.55 ? 58 ASP A O 1 ATOM 291 C CB . ASP A 1 37 ? -10.071 36.561 4.457 1.00 39.92 ? 58 ASP A CB 1 ATOM 292 C CG . ASP A 1 37 ? -10.222 35.843 3.125 1.00 46.86 ? 58 ASP A CG 1 ATOM 293 O OD1 . ASP A 1 37 ? -10.006 36.474 2.065 1.00 50.00 ? 58 ASP A OD1 1 ATOM 294 O OD2 . ASP A 1 37 ? -10.563 34.640 3.135 1.00 51.95 ? 58 ASP A OD2 1 ATOM 295 N N . ASN A 1 38 ? -8.301 38.682 6.505 1.00 33.44 ? 59 ASN A N 1 ATOM 296 C CA . ASN A 1 38 ? -8.320 39.633 7.629 1.00 32.87 ? 59 ASN A CA 1 ATOM 297 C C . ASN A 1 38 ? -7.702 40.984 7.306 1.00 33.22 ? 59 ASN A C 1 ATOM 298 O O . ASN A 1 38 ? -7.662 41.878 8.158 1.00 34.58 ? 59 ASN A O 1 ATOM 299 C CB . ASN A 1 38 ? -7.614 39.041 8.846 1.00 34.70 ? 59 ASN A CB 1 ATOM 300 C CG . ASN A 1 38 ? -8.266 37.778 9.335 1.00 36.84 ? 59 ASN A CG 1 ATOM 301 O OD1 . ASN A 1 38 ? -7.587 36.850 9.766 1.00 40.91 ? 59 ASN A OD1 1 ATOM 302 N ND2 . ASN A 1 38 ? -9.594 37.730 9.271 1.00 34.15 ? 59 ASN A ND2 1 ATOM 303 N N . GLY A 1 39 ? -7.214 41.124 6.078 1.00 31.24 ? 60 GLY A N 1 ATOM 304 C CA . GLY A 1 39 ? -6.568 42.347 5.632 1.00 29.37 ? 60 GLY A CA 1 ATOM 305 C C . GLY A 1 39 ? -5.107 42.379 6.059 1.00 28.34 ? 60 GLY A C 1 ATOM 306 O O . GLY A 1 39 ? -4.493 43.440 6.052 1.00 30.85 ? 60 GLY A O 1 ATOM 307 N N . GLU A 1 40 ? -4.556 41.227 6.438 1.00 25.96 ? 61 GLU A N 1 ATOM 308 C CA . GLU A 1 40 ? -3.178 41.188 6.965 1.00 27.47 ? 61 GLU A CA 1 ATOM 309 C C . GLU A 1 40 ? -2.227 40.577 5.959 1.00 23.38 ? 61 GLU A C 1 ATOM 310 O O . GLU A 1 40 ? -2.535 39.542 5.376 1.00 23.72 ? 61 GLU A O 1 ATOM 311 C CB . GLU A 1 40 ? -3.094 40.421 8.299 1.00 30.60 ? 61 GLU A CB 1 ATOM 312 C CG . GLU A 1 40 ? -3.799 41.090 9.485 1.00 34.55 ? 61 GLU A CG 1 ATOM 313 C CD . GLU A 1 40 ? -3.392 42.544 9.713 1.00 38.99 ? 61 GLU A CD 1 ATOM 314 O OE1 . GLU A 1 40 ? -2.210 42.906 9.498 1.00 39.89 ? 61 GLU A OE1 1 ATOM 315 O OE2 . GLU A 1 40 ? -4.264 43.341 10.121 1.00 42.65 ? 61 GLU A OE2 1 ATOM 316 N N . PRO A 1 41 ? -1.048 41.211 5.764 1.00 22.36 ? 62 PRO A N 1 ATOM 317 C CA . PRO A 1 41 ? -0.086 40.683 4.809 1.00 21.79 ? 62 PRO A CA 1 ATOM 318 C C . PRO A 1 41 ? 0.568 39.409 5.360 1.00 22.04 ? 62 PRO A C 1 ATOM 319 O O . PRO A 1 41 ? 0.723 39.264 6.577 1.00 21.40 ? 62 PRO A O 1 ATOM 320 C CB . PRO A 1 41 ? 0.931 41.828 4.682 1.00 20.45 ? 62 PRO A CB 1 ATOM 321 C CG . PRO A 1 41 ? 0.896 42.513 6.013 1.00 19.66 ? 62 PRO A CG 1 ATOM 322 C CD . PRO A 1 41 ? -0.578 42.462 6.390 1.00 20.93 ? 62 PRO A CD 1 ATOM 323 N N . THR A 1 42 ? 0.938 38.493 4.476 1.00 21.99 ? 63 THR A N 1 ATOM 324 C CA . THR A 1 42 ? 1.462 37.215 4.902 1.00 22.37 ? 63 THR A CA 1 ATOM 325 C C . THR A 1 42 ? 2.941 37.068 4.532 1.00 22.64 ? 63 THR A C 1 ATOM 326 O O . THR A 1 42 ? 3.444 37.793 3.658 1.00 22.84 ? 63 THR A O 1 ATOM 327 C CB . THR A 1 42 ? 0.612 36.046 4.370 1.00 23.29 ? 63 THR A CB 1 ATOM 328 O OG1 . THR A 1 42 ? 0.586 36.076 2.940 1.00 23.80 ? 63 THR A OG1 1 ATOM 329 C CG2 . THR A 1 42 ? -0.849 36.158 4.914 1.00 23.93 ? 63 THR A CG2 1 ATOM 330 N N . LEU A 1 43 ? 3.616 36.138 5.203 1.00 22.13 ? 64 LEU A N 1 ATOM 331 C CA . LEU A 1 43 ? 5.072 35.950 5.046 1.00 22.21 ? 64 LEU A CA 1 ATOM 332 C C . LEU A 1 43 ? 5.427 35.184 3.790 1.00 21.16 ? 64 LEU A C 1 ATOM 333 O O . LEU A 1 43 ? 4.623 34.429 3.265 1.00 20.35 ? 64 LEU A O 1 ATOM 334 C CB . LEU A 1 43 ? 5.662 35.207 6.268 1.00 23.57 ? 64 LEU A CB 1 ATOM 335 C CG . LEU A 1 43 ? 5.512 35.903 7.620 1.00 25.44 ? 64 LEU A CG 1 ATOM 336 C CD1 . LEU A 1 43 ? 5.765 34.894 8.728 1.00 25.80 ? 64 LEU A CD1 1 ATOM 337 C CD2 . LEU A 1 43 ? 6.432 37.117 7.759 1.00 24.72 ? 64 LEU A CD2 1 ATOM 338 N N . SER A 1 44 ? 6.671 35.351 3.341 1.00 20.62 ? 65 SER A N 1 ATOM 339 C CA . SER A 1 44 ? 7.213 34.631 2.203 1.00 20.88 ? 65 SER A CA 1 ATOM 340 C C . SER A 1 44 ? 6.390 34.800 0.922 1.00 20.53 ? 65 SER A C 1 ATOM 341 O O . SER A 1 44 ? 6.324 33.891 0.109 1.00 20.79 ? 65 SER A O 1 ATOM 342 C CB . SER A 1 44 ? 7.431 33.153 2.548 1.00 23.27 ? 65 SER A CB 1 ATOM 343 O OG . SER A 1 44 ? 8.431 33.070 3.570 1.00 24.14 ? 65 SER A OG 1 ATOM 344 N N . SER A 1 45 ? 5.825 35.994 0.749 1.00 19.94 ? 66 SER A N 1 ATOM 345 C CA . SER A 1 45 ? 5.050 36.316 -0.444 1.00 19.97 ? 66 SER A CA 1 ATOM 346 C C . SER A 1 45 ? 5.941 36.950 -1.523 1.00 20.40 ? 66 SER A C 1 ATOM 347 O O . SER A 1 45 ? 6.924 37.620 -1.217 1.00 18.94 ? 66 SER A O 1 ATOM 348 C CB . SER A 1 45 ? 3.887 37.235 -0.095 1.00 20.45 ? 66 SER A CB 1 ATOM 349 O OG . SER A 1 45 ? 3.076 37.461 -1.248 1.00 20.00 ? 66 SER A OG 1 ATOM 350 N N . LEU A 1 46 ? 5.597 36.700 -2.782 1.00 19.47 ? 67 LEU A N 1 ATOM 351 C CA . LEU A 1 46 ? 6.299 37.292 -3.923 1.00 19.39 ? 67 LEU A CA 1 ATOM 352 C C . LEU A 1 46 ? 5.241 37.465 -4.998 1.00 18.55 ? 67 LEU A C 1 ATOM 353 O O . LEU A 1 46 ? 4.512 36.529 -5.281 1.00 19.66 ? 67 LEU A O 1 ATOM 354 C CB . LEU A 1 46 ? 7.365 36.344 -4.460 1.00 20.04 ? 67 LEU A CB 1 ATOM 355 C CG . LEU A 1 46 ? 8.079 36.596 -5.800 1.00 22.20 ? 67 LEU A CG 1 ATOM 356 C CD1 . LEU A 1 46 ? 8.443 38.050 -5.981 1.00 24.22 ? 67 LEU A CD1 1 ATOM 357 C CD2 . LEU A 1 46 ? 9.327 35.720 -5.922 1.00 22.41 ? 67 LEU A CD2 1 ATOM 358 N N . GLY A 1 47 ? 5.165 38.654 -5.587 1.00 17.41 ? 68 GLY A N 1 ATOM 359 C CA . GLY A 1 47 ? 4.333 38.825 -6.792 1.00 16.85 ? 68 GLY A CA 1 ATOM 360 C C . GLY A 1 47 ? 4.965 39.832 -7.739 1.00 17.01 ? 68 GLY A C 1 ATOM 361 O O . GLY A 1 47 ? 5.724 40.709 -7.307 1.00 15.53 ? 68 GLY A O 1 ATOM 362 N N . ARG A 1 48 ? 4.619 39.736 -9.028 1.00 16.40 ? 69 ARG A N 1 ATOM 363 C CA . ARG A 1 48 ? 5.109 40.692 -10.016 1.00 15.24 ? 69 ARG A CA 1 ATOM 364 C C . ARG A 1 48 ? 3.966 40.990 -10.961 1.00 15.28 ? 69 ARG A C 1 ATOM 365 O O . ARG A 1 48 ? 3.041 40.183 -11.090 1.00 15.45 ? 69 ARG A O 1 ATOM 366 C CB . ARG A 1 48 ? 6.340 40.134 -10.781 1.00 15.92 ? 69 ARG A CB 1 ATOM 367 C CG . ARG A 1 48 ? 7.284 39.353 -9.879 1.00 16.06 ? 69 ARG A CG 1 ATOM 368 C CD . ARG A 1 48 ? 8.702 39.209 -10.446 1.00 15.49 ? 69 ARG A CD 1 ATOM 369 N NE . ARG A 1 48 ? 8.711 38.649 -11.804 1.00 15.80 ? 69 ARG A NE 1 ATOM 370 C CZ . ARG A 1 48 ? 9.812 38.531 -12.543 1.00 16.26 ? 69 ARG A CZ 1 ATOM 371 N NH1 . ARG A 1 48 ? 11.000 38.891 -12.032 1.00 16.79 ? 69 ARG A NH1 1 ATOM 372 N NH2 . ARG A 1 48 ? 9.735 38.039 -13.785 1.00 16.54 ? 69 ARG A NH2 1 ATOM 373 N N . ALA A 1 49 ? 3.986 42.170 -11.565 1.00 15.56 ? 70 ALA A N 1 ATOM 374 C CA . ALA A 1 49 ? 2.909 42.579 -12.470 1.00 16.17 ? 70 ALA A CA 1 ATOM 375 C C . ALA A 1 49 ? 3.488 43.446 -13.560 1.00 15.73 ? 70 ALA A C 1 ATOM 376 O O . ALA A 1 49 ? 4.204 44.397 -13.269 1.00 17.03 ? 70 ALA A O 1 ATOM 377 C CB . ALA A 1 49 ? 1.862 43.375 -11.703 1.00 16.99 ? 70 ALA A CB 1 ATOM 378 N N . PHE A 1 50 ? 3.126 43.165 -14.817 1.00 16.27 ? 71 PHE A N 1 ATOM 379 C CA . PHE A 1 50 ? 3.630 43.957 -15.929 1.00 16.34 ? 71 PHE A CA 1 ATOM 380 C C . PHE A 1 50 ? 2.537 44.415 -16.865 1.00 16.47 ? 71 PHE A C 1 ATOM 381 O O . PHE A 1 50 ? 1.492 43.771 -16.963 1.00 16.34 ? 71 PHE A O 1 ATOM 382 C CB . PHE A 1 50 ? 4.622 43.138 -16.744 1.00 16.82 ? 71 PHE A CB 1 ATOM 383 C CG . PHE A 1 50 ? 5.671 42.509 -15.912 1.00 17.92 ? 71 PHE A CG 1 ATOM 384 C CD1 . PHE A 1 50 ? 6.826 43.219 -15.620 1.00 17.73 ? 71 PHE A CD1 1 ATOM 385 C CD2 . PHE A 1 50 ? 5.509 41.208 -15.410 1.00 17.39 ? 71 PHE A CD2 1 ATOM 386 C CE1 . PHE A 1 50 ? 7.808 42.639 -14.818 1.00 17.88 ? 71 PHE A CE1 1 ATOM 387 C CE2 . PHE A 1 50 ? 6.488 40.621 -14.618 1.00 18.97 ? 71 PHE A CE2 1 ATOM 388 C CZ . PHE A 1 50 ? 7.636 41.346 -14.320 1.00 18.84 ? 71 PHE A CZ 1 ATOM 389 N N . TYR A 1 51 ? 2.802 45.504 -17.581 1.00 15.61 ? 72 TYR A N 1 ATOM 390 C CA . TYR A 1 51 ? 1.891 45.893 -18.686 1.00 17.36 ? 72 TYR A CA 1 ATOM 391 C C . TYR A 1 51 ? 1.892 44.837 -19.791 1.00 18.64 ? 72 TYR A C 1 ATOM 392 O O . TYR A 1 51 ? 2.934 44.287 -20.118 1.00 18.01 ? 72 TYR A O 1 ATOM 393 C CB . TYR A 1 51 ? 2.302 47.244 -19.224 1.00 17.63 ? 72 TYR A CB 1 ATOM 394 C CG . TYR A 1 51 ? 1.398 47.810 -20.282 1.00 18.37 ? 72 TYR A CG 1 ATOM 395 C CD1 . TYR A 1 51 ? 0.035 48.056 -20.023 1.00 19.60 ? 72 TYR A CD1 1 ATOM 396 C CD2 . TYR A 1 51 ? 1.908 48.141 -21.526 1.00 20.11 ? 72 TYR A CD2 1 ATOM 397 C CE1 . TYR A 1 51 ? -0.779 48.616 -21.001 1.00 21.06 ? 72 TYR A CE1 1 ATOM 398 C CE2 . TYR A 1 51 ? 1.110 48.699 -22.496 1.00 21.32 ? 72 TYR A CE2 1 ATOM 399 C CZ . TYR A 1 51 ? -0.228 48.928 -22.237 1.00 22.68 ? 72 TYR A CZ 1 ATOM 400 O OH . TYR A 1 51 ? -0.987 49.491 -23.235 1.00 25.50 ? 72 TYR A OH 1 ATOM 401 N N . SER A 1 52 ? 0.729 44.539 -20.376 1.00 17.83 ? 73 SER A N 1 ATOM 402 C CA . SER A 1 52 ? 0.689 43.394 -21.289 1.00 19.38 ? 73 SER A CA 1 ATOM 403 C C . SER A 1 52 ? 1.476 43.575 -22.607 1.00 19.54 ? 73 SER A C 1 ATOM 404 O O . SER A 1 52 ? 1.888 42.570 -23.184 1.00 23.65 ? 73 SER A O 1 ATOM 405 C CB . SER A 1 52 ? -0.739 42.921 -21.561 1.00 21.97 ? 73 SER A CB 1 ATOM 406 O OG . SER A 1 52 ? -1.526 44.035 -21.819 1.00 24.31 ? 73 SER A OG 1 ATOM 407 N N . ALA A 1 53 ? 1.719 44.808 -23.055 1.00 17.34 ? 74 ALA A N 1 ATOM 408 C CA . ALA A 1 53 ? 2.485 45.023 -24.306 1.00 17.38 ? 74 ALA A CA 1 ATOM 409 C C . ALA A 1 53 ? 3.974 45.245 -24.016 1.00 17.21 ? 74 ALA A C 1 ATOM 410 O O . ALA A 1 53 ? 4.301 46.078 -23.177 1.00 17.05 ? 74 ALA A O 1 ATOM 411 C CB . ALA A 1 53 ? 1.950 46.223 -25.053 1.00 17.89 ? 74 ALA A CB 1 ATOM 412 N N . PRO A 1 54 ? 4.864 44.541 -24.743 1.00 18.02 ? 75 PRO A N 1 ATOM 413 C CA . PRO A 1 54 ? 6.301 44.868 -24.625 1.00 18.20 ? 75 PRO A CA 1 ATOM 414 C C . PRO A 1 54 ? 6.593 46.278 -25.096 1.00 18.09 ? 75 PRO A C 1 ATOM 415 O O . PRO A 1 54 ? 5.878 46.817 -25.952 1.00 17.61 ? 75 PRO A O 1 ATOM 416 C CB . PRO A 1 54 ? 6.971 43.858 -25.551 1.00 18.79 ? 75 PRO A CB 1 ATOM 417 C CG . PRO A 1 54 ? 5.992 42.753 -25.737 1.00 21.66 ? 75 PRO A CG 1 ATOM 418 C CD . PRO A 1 54 ? 4.630 43.403 -25.642 1.00 18.10 ? 75 PRO A CD 1 ATOM 419 N N . ILE A 1 55 ? 7.666 46.859 -24.566 1.00 17.88 ? 76 ILE A N 1 ATOM 420 C CA . ILE A 1 55 ? 8.042 48.232 -24.848 1.00 18.03 ? 76 ILE A CA 1 ATOM 421 C C . ILE A 1 55 ? 9.432 48.172 -25.480 1.00 17.69 ? 76 ILE A C 1 ATOM 422 O O . ILE A 1 55 ? 10.293 47.496 -24.939 1.00 17.25 ? 76 ILE A O 1 ATOM 423 C CB . ILE A 1 55 ? 8.144 49.029 -23.528 1.00 19.46 ? 76 ILE A CB 1 ATOM 424 C CG1 . ILE A 1 55 ? 6.775 49.095 -22.830 1.00 21.07 ? 76 ILE A CG1 1 ATOM 425 C CG2 . ILE A 1 55 ? 8.678 50.428 -23.768 1.00 19.84 ? 76 ILE A CG2 1 ATOM 426 C CD1 . ILE A 1 55 ? 5.690 49.751 -23.654 1.00 22.07 ? 76 ILE A CD1 1 ATOM 427 N N . GLN A 1 56 ? 9.629 48.839 -26.614 1.00 17.45 ? 77 GLN A N 1 ATOM 428 C CA . GLN A 1 56 ? 10.969 48.897 -27.209 1.00 17.59 ? 77 GLN A CA 1 ATOM 429 C C . GLN A 1 56 ? 11.845 49.944 -26.506 1.00 17.34 ? 77 GLN A C 1 ATOM 430 O O . GLN A 1 56 ? 11.538 51.149 -26.478 1.00 16.59 ? 77 GLN A O 1 ATOM 431 C CB . GLN A 1 56 ? 10.923 49.145 -28.728 1.00 18.43 ? 77 GLN A CB 1 ATOM 432 C CG . GLN A 1 56 ? 12.295 48.921 -29.359 1.00 18.89 ? 77 GLN A CG 1 ATOM 433 C CD . GLN A 1 56 ? 12.297 49.018 -30.865 1.00 20.81 ? 77 GLN A CD 1 ATOM 434 O OE1 . GLN A 1 56 ? 11.305 49.411 -31.477 1.00 21.21 ? 77 GLN A OE1 1 ATOM 435 N NE2 . GLN A 1 56 ? 13.442 48.694 -31.471 1.00 21.87 ? 77 GLN A NE2 1 ATOM 436 N N . ILE A 1 57 ? 12.981 49.462 -25.988 1.00 18.81 ? 78 ILE A N 1 ATOM 437 C CA . ILE A 1 57 ? 13.903 50.264 -25.194 1.00 20.13 ? 78 ILE A CA 1 ATOM 438 C C . ILE A 1 57 ? 15.061 50.760 -26.063 1.00 18.72 ? 78 ILE A C 1 ATOM 439 O O . ILE A 1 57 ? 15.517 51.885 -25.905 1.00 18.96 ? 78 ILE A O 1 ATOM 440 C CB . ILE A 1 57 ? 14.439 49.453 -23.980 1.00 22.23 ? 78 ILE A CB 1 ATOM 441 C CG1 . ILE A 1 57 ? 13.432 49.512 -22.827 1.00 24.65 ? 78 ILE A CG1 1 ATOM 442 C CG2 . ILE A 1 57 ? 15.791 49.968 -23.485 1.00 25.03 ? 78 ILE A CG2 1 ATOM 443 C CD1 . ILE A 1 57 ? 12.979 50.915 -22.446 1.00 25.56 ? 78 ILE A CD1 1 ATOM 444 N N . TRP A 1 58 ? 15.487 49.935 -27.007 1.00 18.26 ? 79 TRP A N 1 ATOM 445 C CA . TRP A 1 58 ? 16.509 50.372 -27.963 1.00 19.87 ? 79 TRP A CA 1 ATOM 446 C C . TRP A 1 58 ? 16.421 49.642 -29.260 1.00 19.94 ? 79 TRP A C 1 ATOM 447 O O . TRP A 1 58 ? 15.690 48.652 -29.379 1.00 19.33 ? 79 TRP A O 1 ATOM 448 C CB . TRP A 1 58 ? 17.913 50.347 -27.349 1.00 20.75 ? 79 TRP A CB 1 ATOM 449 C CG . TRP A 1 58 ? 18.470 48.996 -27.011 1.00 22.53 ? 79 TRP A CG 1 ATOM 450 C CD1 . TRP A 1 58 ? 18.177 48.197 -25.904 1.00 21.68 ? 79 TRP A CD1 1 ATOM 451 C CD2 . TRP A 1 58 ? 19.474 48.257 -27.763 1.00 23.23 ? 79 TRP A CD2 1 ATOM 452 N NE1 . TRP A 1 58 ? 18.896 47.039 -25.936 1.00 21.81 ? 79 TRP A NE1 1 ATOM 453 C CE2 . TRP A 1 58 ? 19.707 47.016 -27.026 1.00 23.07 ? 79 TRP A CE2 1 ATOM 454 C CE3 . TRP A 1 58 ? 20.186 48.495 -28.947 1.00 25.60 ? 79 TRP A CE3 1 ATOM 455 C CZ2 . TRP A 1 58 ? 20.615 46.058 -27.464 1.00 25.16 ? 79 TRP A CZ2 1 ATOM 456 C CZ3 . TRP A 1 58 ? 21.114 47.525 -29.372 1.00 26.92 ? 79 TRP A CZ3 1 ATOM 457 C CH2 . TRP A 1 58 ? 21.312 46.336 -28.653 1.00 26.18 ? 79 TRP A CH2 1 ATOM 458 N N . ASP A 1 59 ? 17.140 50.140 -30.261 1.00 22.51 ? 80 ASP A N 1 ATOM 459 C CA . ASP A 1 59 ? 17.097 49.576 -31.617 1.00 23.54 ? 80 ASP A CA 1 ATOM 460 C C . ASP A 1 59 ? 18.513 49.311 -32.096 1.00 24.39 ? 80 ASP A C 1 ATOM 461 O O . ASP A 1 59 ? 19.279 50.237 -32.169 1.00 22.66 ? 80 ASP A O 1 ATOM 462 C CB . ASP A 1 59 ? 16.456 50.565 -32.585 1.00 25.38 ? 80 ASP A CB 1 ATOM 463 C CG . ASP A 1 59 ? 16.236 49.967 -33.949 1.00 29.03 ? 80 ASP A CG 1 ATOM 464 O OD1 . ASP A 1 59 ? 15.147 49.411 -34.186 1.00 34.02 ? 80 ASP A OD1 1 ATOM 465 O OD2 . ASP A 1 59 ? 17.165 50.007 -34.765 1.00 30.22 ? 80 ASP A OD2 1 ATOM 466 N N . ASN A 1 60 ? 18.811 48.068 -32.464 1.00 27.50 ? 81 ASN A N 1 ATOM 467 C CA . ASN A 1 60 ? 20.180 47.655 -32.835 1.00 31.92 ? 81 ASN A CA 1 ATOM 468 C C . ASN A 1 60 ? 20.584 48.111 -34.250 1.00 34.39 ? 81 ASN A C 1 ATOM 469 O O . ASN A 1 60 ? 21.774 48.130 -34.569 1.00 37.58 ? 81 ASN A O 1 ATOM 470 C CB . ASN A 1 60 ? 20.353 46.132 -32.651 1.00 35.82 ? 81 ASN A CB 1 ATOM 471 C CG . ASN A 1 60 ? 21.817 45.674 -32.653 1.00 39.47 ? 81 ASN A CG 1 ATOM 472 O OD1 . ASN A 1 60 ? 22.736 46.406 -32.259 1.00 40.42 ? 81 ASN A OD1 1 ATOM 473 N ND2 . ASN A 1 60 ? 22.030 44.430 -33.075 1.00 42.48 ? 81 ASN A ND2 1 ATOM 474 N N . THR A 1 61 ? 19.608 48.491 -35.081 1.00 31.87 ? 82 THR A N 1 ATOM 475 C CA . THR A 1 61 ? 19.891 49.074 -36.412 1.00 31.45 ? 82 THR A CA 1 ATOM 476 C C . THR A 1 61 ? 20.321 50.533 -36.298 1.00 30.43 ? 82 THR A C 1 ATOM 477 O O . THR A 1 61 ? 21.381 50.910 -36.788 1.00 31.00 ? 82 THR A O 1 ATOM 478 C CB . THR A 1 61 ? 18.677 49.008 -37.370 1.00 31.39 ? 82 THR A CB 1 ATOM 479 O OG1 . THR A 1 61 ? 18.213 47.659 -37.482 1.00 35.42 ? 82 THR A OG1 1 ATOM 480 C CG2 . THR A 1 61 ? 19.057 49.513 -38.779 1.00 33.87 ? 82 THR A CG2 1 ATOM 481 N N . THR A 1 62 ? 19.495 51.355 -35.653 1.00 27.06 ? 83 THR A N 1 ATOM 482 C CA . THR A 1 62 ? 19.739 52.795 -35.602 1.00 25.36 ? 83 THR A CA 1 ATOM 483 C C . THR A 1 62 ? 20.628 53.190 -34.431 1.00 24.51 ? 83 THR A C 1 ATOM 484 O O . THR A 1 62 ? 21.175 54.285 -34.414 1.00 24.85 ? 83 THR A O 1 ATOM 485 C CB . THR A 1 62 ? 18.448 53.600 -35.471 1.00 26.53 ? 83 THR A CB 1 ATOM 486 O OG1 . THR A 1 62 ? 17.844 53.311 -34.209 1.00 24.55 ? 83 THR A OG1 1 ATOM 487 C CG2 . THR A 1 62 ? 17.461 53.269 -36.617 1.00 27.35 ? 83 THR A CG2 1 ATOM 488 N N . GLY A 1 63 ? 20.730 52.305 -33.447 1.00 23.63 ? 84 GLY A N 1 ATOM 489 C CA . GLY A 1 63 ? 21.438 52.620 -32.208 1.00 24.19 ? 84 GLY A CA 1 ATOM 490 C C . GLY A 1 63 ? 20.646 53.509 -31.261 1.00 23.28 ? 84 GLY A C 1 ATOM 491 O O . GLY A 1 63 ? 21.144 53.869 -30.191 1.00 24.24 ? 84 GLY A O 1 ATOM 492 N N . ALA A 1 64 ? 19.408 53.867 -31.621 1.00 20.34 ? 85 ALA A N 1 ATOM 493 C CA . ALA A 1 64 ? 18.628 54.767 -30.774 1.00 19.42 ? 85 ALA A CA 1 ATOM 494 C C . ALA A 1 64 ? 18.259 54.058 -29.477 1.00 17.48 ? 85 ALA A C 1 ATOM 495 O O . ALA A 1 64 ? 18.057 52.836 -29.470 1.00 17.25 ? 85 ALA A O 1 ATOM 496 C CB . ALA A 1 64 ? 17.356 55.221 -31.488 1.00 20.28 ? 85 ALA A CB 1 ATOM 497 N N . VAL A 1 65 ? 18.167 54.844 -28.410 1.00 17.18 ? 86 VAL A N 1 ATOM 498 C CA . VAL A 1 65 ? 17.742 54.363 -27.073 1.00 18.28 ? 86 VAL A CA 1 ATOM 499 C C . VAL A 1 65 ? 16.585 55.242 -26.625 1.00 17.48 ? 86 VAL A C 1 ATOM 500 O O . VAL A 1 65 ? 16.632 56.459 -26.767 1.00 18.12 ? 86 VAL A O 1 ATOM 501 C CB . VAL A 1 65 ? 18.898 54.423 -26.028 1.00 19.34 ? 86 VAL A CB 1 ATOM 502 C CG1 . VAL A 1 65 ? 18.401 53.916 -24.686 1.00 19.09 ? 86 VAL A CG1 1 ATOM 503 C CG2 . VAL A 1 65 ? 20.065 53.571 -26.489 1.00 19.20 ? 86 VAL A CG2 1 ATOM 504 N N . ALA A 1 66 ? 15.540 54.613 -26.078 1.00 18.13 ? 87 ALA A N 1 ATOM 505 C CA . ALA A 1 66 ? 14.373 55.347 -25.620 1.00 17.71 ? 87 ALA A CA 1 ATOM 506 C C . ALA A 1 66 ? 14.642 56.218 -24.408 1.00 17.56 ? 87 ALA A C 1 ATOM 507 O O . ALA A 1 66 ? 15.483 55.890 -23.561 1.00 18.30 ? 87 ALA A O 1 ATOM 508 C CB . ALA A 1 66 ? 13.244 54.362 -25.311 1.00 17.07 ? 87 ALA A CB 1 ATOM 509 N N . SER A 1 67 ? 13.893 57.309 -24.308 1.00 17.55 ? 88 SER A N 1 ATOM 510 C CA . SER A 1 67 ? 13.753 58.010 -23.045 1.00 17.00 ? 88 SER A CA 1 ATOM 511 C C . SER A 1 67 ? 12.405 57.563 -22.483 1.00 18.00 ? 88 SER A C 1 ATOM 512 O O . SER A 1 67 ? 11.490 57.254 -23.235 1.00 17.23 ? 88 SER A O 1 ATOM 513 C CB . SER A 1 67 ? 13.764 59.513 -23.260 1.00 18.29 ? 88 SER A CB 1 ATOM 514 O OG . SER A 1 67 ? 15.063 59.954 -23.623 1.00 20.30 ? 88 SER A OG 1 ATOM 515 N N . PHE A 1 68 ? 12.298 57.471 -21.165 1.00 17.21 ? 89 PHE A N 1 ATOM 516 C CA . PHE A 1 68 ? 10.996 57.086 -20.584 1.00 17.02 ? 89 PHE A CA 1 ATOM 517 C C . PHE A 1 68 ? 10.787 57.779 -19.257 1.00 17.26 ? 89 PHE A C 1 ATOM 518 O O . PHE A 1 68 ? 11.722 58.335 -18.660 1.00 17.64 ? 89 PHE A O 1 ATOM 519 C CB . PHE A 1 68 ? 10.823 55.554 -20.447 1.00 17.90 ? 89 PHE A CB 1 ATOM 520 C CG . PHE A 1 68 ? 11.740 54.902 -19.436 1.00 18.48 ? 89 PHE A CG 1 ATOM 521 C CD1 . PHE A 1 68 ? 11.391 54.850 -18.081 1.00 19.88 ? 89 PHE A CD1 1 ATOM 522 C CD2 . PHE A 1 68 ? 12.950 54.333 -19.844 1.00 19.29 ? 89 PHE A CD2 1 ATOM 523 C CE1 . PHE A 1 68 ? 12.239 54.249 -17.148 1.00 21.34 ? 89 PHE A CE1 1 ATOM 524 C CE2 . PHE A 1 68 ? 13.792 53.729 -18.915 1.00 19.65 ? 89 PHE A CE2 1 ATOM 525 C CZ . PHE A 1 68 ? 13.440 53.691 -17.572 1.00 19.49 ? 89 PHE A CZ 1 ATOM 526 N N . ALA A 1 69 ? 9.546 57.750 -18.793 1.00 15.79 ? 90 ALA A N 1 ATOM 527 C CA . ALA A 1 69 ? 9.272 58.242 -17.457 1.00 15.99 ? 90 ALA A CA 1 ATOM 528 C C . ALA A 1 69 ? 8.113 57.428 -16.923 1.00 16.06 ? 90 ALA A C 1 ATOM 529 O O . ALA A 1 69 ? 7.239 57.017 -17.671 1.00 17.75 ? 90 ALA A O 1 ATOM 530 C CB . ALA A 1 69 ? 8.891 59.709 -17.504 1.00 15.83 ? 90 ALA A CB 1 ATOM 531 N N . THR A 1 70 ? 8.114 57.200 -15.619 1.00 15.51 ? 91 THR A N 1 ATOM 532 C CA . THR A 1 70 ? 6.966 56.522 -15.009 1.00 15.82 ? 91 THR A CA 1 ATOM 533 C C . THR A 1 70 ? 6.632 57.175 -13.670 1.00 15.84 ? 91 THR A C 1 ATOM 534 O O . THR A 1 70 ? 7.505 57.644 -12.950 1.00 15.46 ? 91 THR A O 1 ATOM 535 C CB . THR A 1 70 ? 7.208 54.989 -14.911 1.00 16.22 ? 91 THR A CB 1 ATOM 536 O OG1 . THR A 1 70 ? 5.997 54.332 -14.550 1.00 16.04 ? 91 THR A OG1 1 ATOM 537 C CG2 . THR A 1 70 ? 8.327 54.619 -13.877 1.00 16.42 ? 91 THR A CG2 1 ATOM 538 N N . SER A 1 71 ? 5.348 57.251 -13.358 1.00 15.69 ? 92 SER A N 1 ATOM 539 C CA . SER A 1 71 ? 4.950 57.713 -12.028 1.00 16.26 ? 92 SER A CA 1 ATOM 540 C C . SER A 1 71 ? 4.017 56.664 -11.443 1.00 16.41 ? 92 SER A C 1 ATOM 541 O O . SER A 1 71 ? 3.349 55.960 -12.179 1.00 17.08 ? 92 SER A O 1 ATOM 542 C CB . SER A 1 71 ? 4.307 59.085 -12.089 1.00 17.60 ? 92 SER A CB 1 ATOM 543 O OG . SER A 1 71 ? 3.095 59.064 -12.857 1.00 18.72 ? 92 SER A OG 1 ATOM 544 N N . PHE A 1 72 ? 3.996 56.535 -10.124 1.00 15.21 ? 93 PHE A N 1 ATOM 545 C CA . PHE A 1 72 ? 3.030 55.646 -9.484 1.00 15.68 ? 93 PHE A CA 1 ATOM 546 C C . PHE A 1 72 ? 2.869 56.020 -8.025 1.00 15.88 ? 93 PHE A C 1 ATOM 547 O O . PHE A 1 72 ? 3.781 56.598 -7.405 1.00 16.39 ? 93 PHE A O 1 ATOM 548 C CB . PHE A 1 72 ? 3.395 54.142 -9.634 1.00 15.55 ? 93 PHE A CB 1 ATOM 549 C CG . PHE A 1 72 ? 4.834 53.793 -9.251 1.00 15.17 ? 93 PHE A CG 1 ATOM 550 C CD1 . PHE A 1 72 ? 5.131 53.350 -7.969 1.00 15.91 ? 93 PHE A CD1 1 ATOM 551 C CD2 . PHE A 1 72 ? 5.856 53.860 -10.190 1.00 16.61 ? 93 PHE A CD2 1 ATOM 552 C CE1 . PHE A 1 72 ? 6.441 53.012 -7.613 1.00 15.93 ? 93 PHE A CE1 1 ATOM 553 C CE2 . PHE A 1 72 ? 7.164 53.526 -9.839 1.00 16.10 ? 93 PHE A CE2 1 ATOM 554 C CZ . PHE A 1 72 ? 7.449 53.104 -8.557 1.00 15.68 ? 93 PHE A CZ 1 ATOM 555 N N . THR A 1 73 ? 1.688 55.721 -7.497 1.00 15.50 ? 94 THR A N 1 ATOM 556 C CA . THR A 1 73 ? 1.430 55.842 -6.071 1.00 15.84 ? 94 THR A CA 1 ATOM 557 C C . THR A 1 73 ? 1.419 54.453 -5.456 1.00 15.49 ? 94 THR A C 1 ATOM 558 O O . THR A 1 73 ? 0.859 53.526 -6.001 1.00 15.28 ? 94 THR A O 1 ATOM 559 C CB . THR A 1 73 ? 0.085 56.554 -5.841 1.00 15.48 ? 94 THR A CB 1 ATOM 560 O OG1 . THR A 1 73 ? 0.174 57.871 -6.397 1.00 17.42 ? 94 THR A OG1 1 ATOM 561 C CG2 . THR A 1 73 ? -0.212 56.669 -4.331 1.00 16.45 ? 94 THR A CG2 1 ATOM 562 N N . PHE A 1 74 ? 2.120 54.286 -4.336 1.00 16.85 ? 95 PHE A N 1 ATOM 563 C CA . PHE A 1 74 ? 2.111 52.999 -3.645 1.00 16.10 ? 95 PHE A CA 1 ATOM 564 C C . PHE A 1 74 ? 1.835 53.182 -2.169 1.00 16.12 ? 95 PHE A C 1 ATOM 565 O O . PHE A 1 74 ? 2.045 54.270 -1.606 1.00 17.22 ? 95 PHE A O 1 ATOM 566 C CB . PHE A 1 74 ? 3.393 52.148 -3.888 1.00 16.44 ? 95 PHE A CB 1 ATOM 567 C CG . PHE A 1 74 ? 4.643 52.632 -3.180 1.00 16.81 ? 95 PHE A CG 1 ATOM 568 C CD1 . PHE A 1 74 ? 4.848 52.400 -1.816 1.00 16.77 ? 95 PHE A CD1 1 ATOM 569 C CD2 . PHE A 1 74 ? 5.663 53.251 -3.900 1.00 17.34 ? 95 PHE A CD2 1 ATOM 570 C CE1 . PHE A 1 74 ? 6.017 52.812 -1.183 1.00 17.27 ? 95 PHE A CE1 1 ATOM 571 C CE2 . PHE A 1 74 ? 6.835 53.669 -3.275 1.00 17.11 ? 95 PHE A CE2 1 ATOM 572 C CZ . PHE A 1 74 ? 7.019 53.449 -1.915 1.00 16.06 ? 95 PHE A CZ 1 ATOM 573 N N . ASN A 1 75 ? 1.326 52.119 -1.569 1.00 15.67 ? 96 ASN A N 1 ATOM 574 C CA . ASN A 1 75 ? 1.071 52.132 -0.139 1.00 15.69 ? 96 ASN A CA 1 ATOM 575 C C . ASN A 1 75 ? 1.656 50.868 0.448 1.00 15.74 ? 96 ASN A C 1 ATOM 576 O O . ASN A 1 75 ? 1.229 49.776 0.116 1.00 16.52 ? 96 ASN A O 1 ATOM 577 C CB . ASN A 1 75 ? -0.447 52.232 0.132 1.00 16.14 ? 96 ASN A CB 1 ATOM 578 C CG . ASN A 1 75 ? -0.747 52.533 1.589 1.00 16.98 ? 96 ASN A CG 1 ATOM 579 O OD1 . ASN A 1 75 ? -0.731 51.636 2.422 1.00 18.97 ? 96 ASN A OD1 1 ATOM 580 N ND2 . ASN A 1 75 ? -0.932 53.810 1.909 1.00 16.93 ? 96 ASN A ND2 1 ATOM 581 N N . ILE A 1 76 ? 2.657 51.026 1.308 1.00 16.29 ? 97 ILE A N 1 ATOM 582 C CA . ILE A 1 76 ? 3.232 49.923 2.042 1.00 15.51 ? 97 ILE A CA 1 ATOM 583 C C . ILE A 1 76 ? 2.813 50.127 3.484 1.00 16.54 ? 97 ILE A C 1 ATOM 584 O O . ILE A 1 76 ? 3.070 51.183 4.063 1.00 18.03 ? 97 ILE A O 1 ATOM 585 C CB . ILE A 1 76 ? 4.788 49.939 1.966 1.00 15.55 ? 97 ILE A CB 1 ATOM 586 C CG1 . ILE A 1 76 ? 5.263 49.591 0.554 1.00 15.71 ? 97 ILE A CG1 1 ATOM 587 C CG2 . ILE A 1 76 ? 5.359 48.930 2.962 1.00 15.90 ? 97 ILE A CG2 1 ATOM 588 C CD1 . ILE A 1 76 ? 6.783 49.714 0.353 1.00 16.26 ? 97 ILE A CD1 1 ATOM 589 N N . ASP A 1 77 ? 2.126 49.143 4.033 1.00 18.61 ? 98 ASP A N 1 ATOM 590 C CA . ASP A 1 77 ? 1.617 49.241 5.402 1.00 19.36 ? 98 ASP A CA 1 ATOM 591 C C . ASP A 1 77 ? 2.045 48.000 6.171 1.00 19.05 ? 98 ASP A C 1 ATOM 592 O O . ASP A 1 77 ? 2.322 46.955 5.577 1.00 18.71 ? 98 ASP A O 1 ATOM 593 C CB . ASP A 1 77 ? 0.085 49.415 5.405 1.00 20.80 ? 98 ASP A CB 1 ATOM 594 C CG . ASP A 1 77 ? -0.455 50.067 6.699 1.00 24.17 ? 98 ASP A CG 1 ATOM 595 O OD1 . ASP A 1 77 ? 0.321 50.478 7.581 1.00 22.75 ? 98 ASP A OD1 1 ATOM 596 O OD2 . ASP A 1 77 ? -1.698 50.189 6.814 1.00 26.98 ? 98 ASP A OD2 1 ATOM 597 N N . VAL A 1 78 ? 2.082 48.122 7.502 1.00 19.33 ? 99 VAL A N 1 ATOM 598 C CA . VAL A 1 78 ? 2.718 47.138 8.362 1.00 19.96 ? 99 VAL A CA 1 ATOM 599 C C . VAL A 1 78 ? 1.812 46.916 9.573 1.00 19.89 ? 99 VAL A C 1 ATOM 600 O O . VAL A 1 78 ? 1.356 47.889 10.160 1.00 20.63 ? 99 VAL A O 1 ATOM 601 C CB . VAL A 1 78 ? 4.082 47.670 8.873 1.00 19.81 ? 99 VAL A CB 1 ATOM 602 C CG1 . VAL A 1 78 ? 4.767 46.641 9.748 1.00 21.68 ? 99 VAL A CG1 1 ATOM 603 C CG2 . VAL A 1 78 ? 4.985 48.044 7.694 1.00 19.98 ? 99 VAL A CG2 1 ATOM 604 N N . PRO A 1 79 ? 1.588 45.656 9.956 1.00 21.45 ? 100 PRO A N 1 ATOM 605 C CA . PRO A 1 79 ? 0.774 45.419 11.164 1.00 24.76 ? 100 PRO A CA 1 ATOM 606 C C . PRO A 1 79 ? 1.494 45.880 12.420 1.00 28.98 ? 100 PRO A C 1 ATOM 607 O O . PRO A 1 79 ? 2.724 45.897 12.453 1.00 28.04 ? 100 PRO A O 1 ATOM 608 C CB . PRO A 1 79 ? 0.598 43.896 11.204 1.00 25.83 ? 100 PRO A CB 1 ATOM 609 C CG . PRO A 1 79 ? 1.488 43.317 10.157 1.00 24.54 ? 100 PRO A CG 1 ATOM 610 C CD . PRO A 1 79 ? 1.923 44.415 9.232 1.00 22.30 ? 100 PRO A CD 1 ATOM 611 N N . ASN A 1 80 ? 0.738 46.248 13.453 1.00 31.58 ? 101 ASN A N 1 ATOM 612 C CA . ASN A 1 80 ? 1.349 46.575 14.739 1.00 35.39 ? 101 ASN A CA 1 ATOM 613 C C . ASN A 1 80 ? 2.140 45.352 15.242 1.00 35.22 ? 101 ASN A C 1 ATOM 614 O O . ASN A 1 80 ? 1.755 44.210 14.989 1.00 34.86 ? 101 ASN A O 1 ATOM 615 C CB . ASN A 1 80 ? 0.283 47.006 15.757 1.00 38.52 ? 101 ASN A CB 1 ATOM 616 C CG . ASN A 1 80 ? -0.428 48.300 15.369 1.00 41.31 ? 101 ASN A CG 1 ATOM 617 O OD1 . ASN A 1 80 ? 0.046 49.080 14.533 1.00 43.62 ? 101 ASN A OD1 1 ATOM 618 N ND2 . ASN A 1 80 ? -1.572 48.542 15.996 1.00 42.54 ? 101 ASN A ND2 1 ATOM 619 N N . ASN A 1 81 ? 3.264 45.594 15.908 1.00 38.10 ? 102 ASN A N 1 ATOM 620 C CA . ASN A 1 81 ? 4.137 44.504 16.389 1.00 38.93 ? 102 ASN A CA 1 ATOM 621 C C . ASN A 1 81 ? 4.935 43.757 15.316 1.00 35.85 ? 102 ASN A C 1 ATOM 622 O O . ASN A 1 81 ? 5.546 42.714 15.592 1.00 34.83 ? 102 ASN A O 1 ATOM 623 C CB . ASN A 1 81 ? 3.361 43.520 17.278 1.00 44.47 ? 102 ASN A CB 1 ATOM 624 C CG . ASN A 1 81 ? 3.118 44.070 18.669 1.00 48.70 ? 102 ASN A CG 1 ATOM 625 O OD1 . ASN A 1 81 ? 2.018 44.525 18.988 1.00 51.38 ? 102 ASN A OD1 1 ATOM 626 N ND2 . ASN A 1 81 ? 4.159 44.056 19.499 1.00 50.09 ? 102 ASN A ND2 1 ATOM 627 N N . SER A 1 82 ? 4.914 44.282 14.093 1.00 31.09 ? 103 SER A N 1 ATOM 628 C CA . SER A 1 82 ? 5.870 43.869 13.053 1.00 27.64 ? 103 SER A CA 1 ATOM 629 C C . SER A 1 82 ? 6.659 45.089 12.579 1.00 23.53 ? 103 SER A C 1 ATOM 630 O O . SER A 1 82 ? 6.249 46.235 12.793 1.00 22.86 ? 103 SER A O 1 ATOM 631 C CB . SER A 1 82 ? 5.156 43.213 11.849 1.00 27.77 ? 103 SER A CB 1 ATOM 632 O OG . SER A 1 82 ? 4.842 41.842 12.077 1.00 32.44 ? 103 SER A OG 1 ATOM 633 N N . GLY A 1 83 ? 7.816 44.841 11.961 1.00 22.70 ? 104 GLY A N 1 ATOM 634 C CA . GLY A 1 83 ? 8.470 45.850 11.146 1.00 20.56 ? 104 GLY A CA 1 ATOM 635 C C . GLY A 1 83 ? 8.222 45.475 9.683 1.00 20.43 ? 104 GLY A C 1 ATOM 636 O O . GLY A 1 83 ? 7.733 44.367 9.398 1.00 19.97 ? 104 GLY A O 1 ATOM 637 N N . PRO A 1 84 ? 8.582 46.370 8.751 1.00 20.10 ? 105 PRO A N 1 ATOM 638 C CA . PRO A 1 84 ? 8.343 46.085 7.334 1.00 19.90 ? 105 PRO A CA 1 ATOM 639 C C . PRO A 1 84 ? 9.382 45.144 6.721 1.00 19.75 ? 105 PRO A C 1 ATOM 640 O O . PRO A 1 84 ? 10.540 45.115 7.160 1.00 20.15 ? 105 PRO A O 1 ATOM 641 C CB . PRO A 1 84 ? 8.478 47.467 6.685 1.00 19.17 ? 105 PRO A CB 1 ATOM 642 C CG . PRO A 1 84 ? 9.450 48.211 7.560 1.00 18.42 ? 105 PRO A CG 1 ATOM 643 C CD . PRO A 1 84 ? 9.185 47.705 8.958 1.00 19.02 ? 105 PRO A CD 1 ATOM 644 N N . ALA A 1 85 ? 8.976 44.387 5.701 1.00 18.10 ? 106 ALA A N 1 ATOM 645 C CA . ALA A 1 85 ? 9.900 43.704 4.774 1.00 16.99 ? 106 ALA A CA 1 ATOM 646 C C . ALA A 1 85 ? 9.085 43.209 3.581 1.00 17.06 ? 106 ALA A C 1 ATOM 647 O O . ALA A 1 85 ? 7.899 42.880 3.750 1.00 17.63 ? 106 ALA A O 1 ATOM 648 C CB . ALA A 1 85 ? 10.602 42.519 5.445 1.00 17.47 ? 106 ALA A CB 1 ATOM 649 N N . ASP A 1 86 ? 9.660 43.128 2.379 1.00 17.27 ? 107 ASP A N 1 ATOM 650 C CA . ASP A 1 86 ? 11.079 43.451 2.070 1.00 16.93 ? 107 ASP A CA 1 ATOM 651 C C . ASP A 1 86 ? 11.192 44.665 1.163 1.00 17.28 ? 107 ASP A C 1 ATOM 652 O O . ASP A 1 86 ? 12.267 45.276 1.045 1.00 18.14 ? 107 ASP A O 1 ATOM 653 C CB . ASP A 1 86 ? 11.718 42.265 1.352 1.00 17.84 ? 107 ASP A CB 1 ATOM 654 C CG . ASP A 1 86 ? 12.402 41.321 2.291 1.00 19.66 ? 107 ASP A CG 1 ATOM 655 O OD1 . ASP A 1 86 ? 13.532 41.662 2.736 1.00 18.70 ? 107 ASP A OD1 1 ATOM 656 O OD2 . ASP A 1 86 ? 11.853 40.219 2.546 1.00 18.89 ? 107 ASP A OD2 1 ATOM 657 N N . GLY A 1 87 ? 10.101 44.966 0.452 1.00 17.23 ? 108 GLY A N 1 ATOM 658 C CA . GLY A 1 87 ? 10.046 46.171 -0.367 1.00 15.99 ? 108 GLY A CA 1 ATOM 659 C C . GLY A 1 87 ? 9.427 45.898 -1.716 1.00 14.82 ? 108 GLY A C 1 ATOM 660 O O . GLY A 1 87 ? 8.920 44.797 -1.967 1.00 16.79 ? 108 GLY A O 1 ATOM 661 N N . LEU A 1 88 ? 9.445 46.914 -2.567 1.00 13.88 ? 109 LEU A N 1 ATOM 662 C CA . LEU A 1 88 ? 8.954 46.776 -3.938 1.00 15.33 ? 109 LEU A CA 1 ATOM 663 C C . LEU A 1 88 ? 9.858 47.506 -4.922 1.00 15.30 ? 109 LEU A C 1 ATOM 664 O O . LEU A 1 88 ? 10.663 48.359 -4.532 1.00 15.49 ? 109 LEU A O 1 ATOM 665 C CB . LEU A 1 88 ? 7.494 47.286 -4.028 1.00 14.48 ? 109 LEU A CB 1 ATOM 666 C CG . LEU A 1 88 ? 7.155 48.737 -3.691 1.00 14.76 ? 109 LEU A CG 1 ATOM 667 C CD1 . LEU A 1 88 ? 7.414 49.682 -4.883 1.00 15.94 ? 109 LEU A CD1 1 ATOM 668 C CD2 . LEU A 1 88 ? 5.683 48.845 -3.237 1.00 15.07 ? 109 LEU A CD2 1 ATOM 669 N N . ALA A 1 89 ? 9.714 47.196 -6.208 1.00 15.23 ? 110 ALA A N 1 ATOM 670 C CA . ALA A 1 89 ? 10.540 47.849 -7.207 1.00 14.59 ? 110 ALA A CA 1 ATOM 671 C C . ALA A 1 89 ? 9.788 47.985 -8.517 1.00 14.43 ? 110 ALA A C 1 ATOM 672 O O . ALA A 1 89 ? 8.962 47.126 -8.863 1.00 14.10 ? 110 ALA A O 1 ATOM 673 C CB . ALA A 1 89 ? 11.818 47.044 -7.426 1.00 14.34 ? 110 ALA A CB 1 ATOM 674 N N . PHE A 1 90 ? 10.062 49.089 -9.202 1.00 14.32 ? 111 PHE A N 1 ATOM 675 C CA . PHE A 1 90 ? 9.728 49.249 -10.602 1.00 14.44 ? 111 PHE A CA 1 ATOM 676 C C . PHE A 1 90 ? 10.838 48.635 -11.450 1.00 14.89 ? 111 PHE A C 1 ATOM 677 O O . PHE A 1 90 ? 12.043 48.859 -11.157 1.00 15.94 ? 111 PHE A O 1 ATOM 678 C CB . PHE A 1 90 ? 9.593 50.731 -10.968 1.00 14.49 ? 111 PHE A CB 1 ATOM 679 C CG . PHE A 1 90 ? 9.341 50.931 -12.430 1.00 14.71 ? 111 PHE A CG 1 ATOM 680 C CD1 . PHE A 1 90 ? 8.080 50.674 -12.962 1.00 15.62 ? 111 PHE A CD1 1 ATOM 681 C CD2 . PHE A 1 90 ? 10.387 51.287 -13.289 1.00 14.76 ? 111 PHE A CD2 1 ATOM 682 C CE1 . PHE A 1 90 ? 7.865 50.805 -14.325 1.00 15.79 ? 111 PHE A CE1 1 ATOM 683 C CE2 . PHE A 1 90 ? 10.165 51.418 -14.654 1.00 15.44 ? 111 PHE A CE2 1 ATOM 684 C CZ . PHE A 1 90 ? 8.899 51.179 -15.169 1.00 16.68 ? 111 PHE A CZ 1 ATOM 685 N N . VAL A 1 91 ? 10.463 47.850 -12.466 1.00 14.96 ? 112 VAL A N 1 ATOM 686 C CA . VAL A 1 91 ? 11.452 47.049 -13.209 1.00 15.36 ? 112 VAL A CA 1 ATOM 687 C C . VAL A 1 91 ? 11.299 47.107 -14.724 1.00 17.05 ? 112 VAL A C 1 ATOM 688 O O . VAL A 1 91 ? 10.188 47.289 -15.250 1.00 16.67 ? 112 VAL A O 1 ATOM 689 C CB . VAL A 1 91 ? 11.459 45.556 -12.770 1.00 15.82 ? 112 VAL A CB 1 ATOM 690 C CG1 . VAL A 1 91 ? 11.584 45.455 -11.262 1.00 16.73 ? 112 VAL A CG1 1 ATOM 691 C CG2 . VAL A 1 91 ? 10.158 44.868 -13.183 1.00 16.70 ? 112 VAL A CG2 1 ATOM 692 N N . LEU A 1 92 ? 12.440 46.980 -15.404 1.00 16.73 ? 113 LEU A N 1 ATOM 693 C CA . LEU A 1 92 ? 12.474 46.669 -16.835 1.00 17.37 ? 113 LEU A CA 1 ATOM 694 C C . LEU A 1 92 ? 13.166 45.319 -16.988 1.00 17.13 ? 113 LEU A C 1 ATOM 695 O O . LEU A 1 92 ? 14.288 45.128 -16.495 1.00 16.56 ? 113 LEU A O 1 ATOM 696 C CB . LEU A 1 92 ? 13.209 47.754 -17.627 1.00 18.48 ? 113 LEU A CB 1 ATOM 697 C CG . LEU A 1 92 ? 12.569 49.164 -17.651 1.00 19.60 ? 113 LEU A CG 1 ATOM 698 C CD1 . LEU A 1 92 ? 13.052 49.967 -16.457 1.00 22.71 ? 113 LEU A CD1 1 ATOM 699 C CD2 . LEU A 1 92 ? 12.932 49.901 -18.929 1.00 24.10 ? 113 LEU A CD2 1 ATOM 700 N N . LEU A 1 93 ? 12.497 44.380 -17.656 1.00 16.52 ? 114 LEU A N 1 ATOM 701 C CA . LEU A 1 93 ? 12.944 42.978 -17.722 1.00 17.64 ? 114 LEU A CA 1 ATOM 702 C C . LEU A 1 93 ? 12.741 42.402 -19.115 1.00 19.45 ? 114 LEU A C 1 ATOM 703 O O . LEU A 1 93 ? 11.914 42.929 -19.866 1.00 18.22 ? 114 LEU A O 1 ATOM 704 C CB . LEU A 1 93 ? 12.183 42.101 -16.724 1.00 17.64 ? 114 LEU A CB 1 ATOM 705 C CG . LEU A 1 93 ? 12.362 42.354 -15.236 1.00 17.09 ? 114 LEU A CG 1 ATOM 706 C CD1 . LEU A 1 93 ? 11.414 41.432 -14.465 1.00 16.65 ? 114 LEU A CD1 1 ATOM 707 C CD2 . LEU A 1 93 ? 13.813 42.074 -14.871 1.00 18.96 ? 114 LEU A CD2 1 ATOM 708 N N . PRO A 1 94 ? 13.466 41.310 -19.462 1.00 19.82 ? 115 PRO A N 1 ATOM 709 C CA . PRO A 1 94 ? 13.203 40.667 -20.758 1.00 19.45 ? 115 PRO A CA 1 ATOM 710 C C . PRO A 1 94 ? 11.767 40.193 -20.888 1.00 19.54 ? 115 PRO A C 1 ATOM 711 O O . PRO A 1 94 ? 11.160 39.740 -19.905 1.00 18.41 ? 115 PRO A O 1 ATOM 712 C CB . PRO A 1 94 ? 14.107 39.450 -20.720 1.00 20.93 ? 115 PRO A CB 1 ATOM 713 C CG . PRO A 1 94 ? 15.284 39.921 -19.927 1.00 21.40 ? 115 PRO A CG 1 ATOM 714 C CD . PRO A 1 94 ? 14.664 40.727 -18.811 1.00 20.74 ? 115 PRO A CD 1 ATOM 715 N N . VAL A 1 95 ? 11.248 40.249 -22.108 1.00 19.63 ? 116 VAL A N 1 ATOM 716 C CA . VAL A 1 95 ? 9.951 39.629 -22.385 1.00 19.70 ? 116 VAL A CA 1 ATOM 717 C C . VAL A 1 95 ? 10.017 38.148 -21.967 1.00 20.49 ? 116 VAL A C 1 ATOM 718 O O . VAL A 1 95 ? 11.015 37.467 -22.229 1.00 22.40 ? 116 VAL A O 1 ATOM 719 C CB . VAL A 1 95 ? 9.573 39.763 -23.887 1.00 19.22 ? 116 VAL A CB 1 ATOM 720 C CG1 . VAL A 1 95 ? 8.248 39.059 -24.177 1.00 22.13 ? 116 VAL A CG1 1 ATOM 721 C CG2 . VAL A 1 95 ? 9.491 41.230 -24.296 1.00 19.19 ? 116 VAL A CG2 1 ATOM 722 N N . GLY A 1 96 ? 8.991 37.669 -21.272 1.00 20.77 ? 117 GLY A N 1 ATOM 723 C CA . GLY A 1 96 ? 8.954 36.273 -20.820 1.00 21.68 ? 117 GLY A CA 1 ATOM 724 C C . GLY A 1 96 ? 9.606 36.021 -19.464 1.00 22.97 ? 117 GLY A C 1 ATOM 725 O O . GLY A 1 96 ? 9.593 34.894 -18.966 1.00 22.17 ? 117 GLY A O 1 ATOM 726 N N . SER A 1 97 ? 10.168 37.071 -18.861 1.00 21.73 ? 118 SER A N 1 ATOM 727 C CA . SER A 1 97 ? 10.855 36.940 -17.573 1.00 22.15 ? 118 SER A CA 1 ATOM 728 C C . SER A 1 97 ? 9.960 36.304 -16.517 1.00 21.96 ? 118 SER A C 1 ATOM 729 O O . SER A 1 97 ? 8.789 36.695 -16.378 1.00 20.53 ? 118 SER A O 1 ATOM 730 C CB . SER A 1 97 ? 11.330 38.307 -17.073 1.00 22.67 ? 118 SER A CB 1 ATOM 731 O OG . SER A 1 97 ? 12.049 38.167 -15.857 1.00 23.66 ? 118 SER A OG 1 ATOM 732 N N . GLN A 1 98 ? 10.520 35.334 -15.783 1.00 21.90 ? 119 GLN A N 1 ATOM 733 C CA . GLN A 1 98 ? 9.833 34.647 -14.679 1.00 22.66 ? 119 GLN A CA 1 ATOM 734 C C . GLN A 1 98 ? 10.454 35.035 -13.323 1.00 21.89 ? 119 GLN A C 1 ATOM 735 O O . GLN A 1 98 ? 11.616 35.446 -13.275 1.00 21.64 ? 119 GLN A O 1 ATOM 736 C CB . GLN A 1 98 ? 9.905 33.116 -14.868 1.00 25.61 ? 119 GLN A CB 1 ATOM 737 C CG . GLN A 1 98 ? 9.272 32.614 -16.162 1.00 27.44 ? 119 GLN A CG 1 ATOM 738 C CD . GLN A 1 98 ? 7.810 32.994 -16.289 1.00 29.24 ? 119 GLN A CD 1 ATOM 739 O OE1 . GLN A 1 98 ? 7.394 33.578 -17.296 1.00 33.79 ? 119 GLN A OE1 1 ATOM 740 N NE2 . GLN A 1 98 ? 7.022 32.693 -15.262 1.00 30.72 ? 119 GLN A NE2 1 ATOM 741 N N . PRO A 1 99 ? 9.679 34.913 -12.222 1.00 21.26 ? 120 PRO A N 1 ATOM 742 C CA . PRO A 1 99 ? 10.189 35.327 -10.911 1.00 21.20 ? 120 PRO A CA 1 ATOM 743 C C . PRO A 1 99 ? 11.439 34.551 -10.464 1.00 22.23 ? 120 PRO A C 1 ATOM 744 O O . PRO A 1 99 ? 11.571 33.349 -10.753 1.00 22.70 ? 120 PRO A O 1 ATOM 745 C CB . PRO A 1 99 ? 9.031 35.010 -9.963 1.00 20.90 ? 120 PRO A CB 1 ATOM 746 C CG . PRO A 1 99 ? 7.812 35.041 -10.822 1.00 20.22 ? 120 PRO A CG 1 ATOM 747 C CD . PRO A 1 99 ? 8.250 34.529 -12.162 1.00 20.85 ? 120 PRO A CD 1 ATOM 748 N N . LYS A 1 100 ? 12.324 35.257 -9.769 1.00 22.95 ? 121 LYS A N 1 ATOM 749 C CA . LYS A 1 100 ? 13.523 34.668 -9.169 1.00 23.80 ? 121 LYS A CA 1 ATOM 750 C C . LYS A 1 100 ? 13.279 34.507 -7.661 1.00 24.42 ? 121 LYS A C 1 ATOM 751 O O . LYS A 1 100 ? 12.142 34.296 -7.237 1.00 24.08 ? 121 LYS A O 1 ATOM 752 C CB . LYS A 1 100 ? 14.765 35.520 -9.468 1.00 24.33 ? 121 LYS A CB 1 ATOM 753 C CG . LYS A 1 100 ? 14.951 35.918 -10.928 1.00 27.35 ? 121 LYS A CG 1 ATOM 754 C CD . LYS A 1 100 ? 15.264 34.728 -11.810 1.00 29.54 ? 121 LYS A CD 1 ATOM 755 C CE . LYS A 1 100 ? 15.547 35.156 -13.256 1.00 32.72 ? 121 LYS A CE 1 ATOM 756 N NZ . LYS A 1 100 ? 14.293 35.561 -13.973 1.00 33.34 ? 121 LYS A NZ 1 ATOM 757 N N . ASP A 1 101 ? 14.327 34.595 -6.849 1.00 24.74 ? 122 ASP A N 1 ATOM 758 C CA . ASP A 1 101 ? 14.184 34.328 -5.421 1.00 25.61 ? 122 ASP A CA 1 ATOM 759 C C . ASP A 1 101 ? 13.429 35.421 -4.642 1.00 24.64 ? 122 ASP A C 1 ATOM 760 O O . ASP A 1 101 ? 13.458 36.614 -5.004 1.00 22.26 ? 122 ASP A O 1 ATOM 761 C CB . ASP A 1 101 ? 15.550 34.067 -4.770 1.00 28.91 ? 122 ASP A CB 1 ATOM 762 C CG . ASP A 1 101 ? 16.116 32.685 -5.104 1.00 35.49 ? 122 ASP A CG 1 ATOM 763 O OD1 . ASP A 1 101 ? 15.345 31.757 -5.443 1.00 40.33 ? 122 ASP A OD1 1 ATOM 764 O OD2 . ASP A 1 101 ? 17.353 32.517 -5.017 1.00 39.42 ? 122 ASP A OD2 1 ATOM 765 N N . LYS A 1 102 ? 12.792 34.995 -3.551 1.00 23.19 ? 123 LYS A N 1 ATOM 766 C CA . LYS A 1 102 ? 11.929 35.866 -2.756 1.00 23.73 ? 123 LYS A CA 1 ATOM 767 C C . LYS A 1 102 ? 12.679 36.653 -1.670 1.00 21.66 ? 123 LYS A C 1 ATOM 768 O O . LYS A 1 102 ? 13.916 36.779 -1.705 1.00 21.09 ? 123 LYS A O 1 ATOM 769 C CB . LYS A 1 102 ? 10.781 35.046 -2.157 1.00 25.09 ? 123 LYS A CB 1 ATOM 770 C CG . LYS A 1 102 ? 11.231 33.992 -1.152 1.00 28.00 ? 123 LYS A CG 1 ATOM 771 C CD . LYS A 1 102 ? 10.044 33.283 -0.502 1.00 33.21 ? 123 LYS A CD 1 ATOM 772 C CE . LYS A 1 102 ? 9.585 32.085 -1.318 1.00 36.28 ? 123 LYS A CE 1 ATOM 773 N NZ . LYS A 1 102 ? 8.319 31.512 -0.781 1.00 39.52 ? 123 LYS A NZ 1 ATOM 774 N N . GLY A 1 103 ? 11.932 37.203 -0.719 1.00 20.77 ? 124 GLY A N 1 ATOM 775 C CA . GLY A 1 103 ? 12.547 37.964 0.378 1.00 18.97 ? 124 GLY A CA 1 ATOM 776 C C . GLY A 1 103 ? 13.394 39.146 -0.087 1.00 18.71 ? 124 GLY A C 1 ATOM 777 O O . GLY A 1 103 ? 12.980 39.928 -0.944 1.00 17.90 ? 124 GLY A O 1 ATOM 778 N N . GLY A 1 104 ? 14.606 39.262 0.456 1.00 17.73 ? 125 GLY A N 1 ATOM 779 C CA . GLY A 1 104 ? 15.451 40.411 0.164 1.00 18.25 ? 125 GLY A CA 1 ATOM 780 C C . GLY A 1 104 ? 15.937 40.487 -1.286 1.00 17.30 ? 125 GLY A C 1 ATOM 781 O O . GLY A 1 104 ? 16.466 41.491 -1.711 1.00 17.27 ? 125 GLY A O 1 ATOM 782 N N . LEU A 1 105 ? 15.779 39.415 -2.039 1.00 17.55 ? 126 LEU A N 1 ATOM 783 C CA . LEU A 1 105 ? 16.178 39.436 -3.438 1.00 17.59 ? 126 LEU A CA 1 ATOM 784 C C . LEU A 1 105 ? 15.054 39.952 -4.362 1.00 18.48 ? 126 LEU A C 1 ATOM 785 O O . LEU A 1 105 ? 15.241 40.087 -5.575 1.00 18.77 ? 126 LEU A O 1 ATOM 786 C CB . LEU A 1 105 ? 16.674 38.046 -3.852 1.00 18.42 ? 126 LEU A CB 1 ATOM 787 C CG . LEU A 1 105 ? 17.935 37.597 -3.072 1.00 18.34 ? 126 LEU A CG 1 ATOM 788 C CD1 . LEU A 1 105 ? 18.278 36.137 -3.351 1.00 20.84 ? 126 LEU A CD1 1 ATOM 789 C CD2 . LEU A 1 105 ? 19.106 38.532 -3.322 1.00 19.67 ? 126 LEU A CD2 1 ATOM 790 N N . LEU A 1 106 ? 13.897 40.244 -3.764 1.00 18.08 ? 127 LEU A N 1 ATOM 791 C CA . LEU A 1 106 ? 12.823 41.000 -4.440 1.00 18.88 ? 127 LEU A CA 1 ATOM 792 C C . LEU A 1 106 ? 12.204 40.325 -5.679 1.00 18.95 ? 127 LEU A C 1 ATOM 793 O O . LEU A 1 106 ? 11.518 40.976 -6.491 1.00 19.30 ? 127 LEU A O 1 ATOM 794 C CB . LEU A 1 106 ? 13.287 42.434 -4.764 1.00 18.22 ? 127 LEU A CB 1 ATOM 795 C CG . LEU A 1 106 ? 13.691 43.316 -3.575 1.00 18.35 ? 127 LEU A CG 1 ATOM 796 C CD1 . LEU A 1 106 ? 14.104 44.708 -4.017 1.00 19.35 ? 127 LEU A CD1 1 ATOM 797 C CD2 . LEU A 1 106 ? 12.595 43.411 -2.515 1.00 20.47 ? 127 LEU A CD2 1 ATOM 798 N N . GLY A 1 107 ? 12.397 39.025 -5.807 1.00 17.97 ? 128 GLY A N 1 ATOM 799 C CA . GLY A 1 107 ? 11.895 38.299 -6.983 1.00 18.32 ? 128 GLY A CA 1 ATOM 800 C C . GLY A 1 107 ? 12.690 38.587 -8.237 1.00 19.36 ? 128 GLY A C 1 ATOM 801 O O . GLY A 1 107 ? 12.248 38.254 -9.330 1.00 19.88 ? 128 GLY A O 1 ATOM 802 N N . LEU A 1 108 ? 13.885 39.164 -8.086 1.00 19.15 ? 129 LEU A N 1 ATOM 803 C CA . LEU A 1 108 ? 14.669 39.619 -9.239 1.00 18.96 ? 129 LEU A CA 1 ATOM 804 C C . LEU A 1 108 ? 16.025 38.928 -9.383 1.00 20.28 ? 129 LEU A C 1 ATOM 805 O O . LEU A 1 108 ? 16.600 38.897 -10.473 1.00 20.16 ? 129 LEU A O 1 ATOM 806 C CB . LEU A 1 108 ? 14.898 41.133 -9.181 1.00 18.15 ? 129 LEU A CB 1 ATOM 807 C CG . LEU A 1 108 ? 13.711 42.069 -9.347 1.00 17.82 ? 129 LEU A CG 1 ATOM 808 C CD1 . LEU A 1 108 ? 14.203 43.505 -9.202 1.00 17.35 ? 129 LEU A CD1 1 ATOM 809 C CD2 . LEU A 1 108 ? 13.091 41.799 -10.719 1.00 17.22 ? 129 LEU A CD2 1 ATOM 810 N N . PHE A 1 109 ? 16.518 38.368 -8.292 1.00 20.51 ? 130 PHE A N 1 ATOM 811 C CA . PHE A 1 109 ? 17.846 37.754 -8.306 1.00 22.14 ? 130 PHE A CA 1 ATOM 812 C C . PHE A 1 109 ? 17.854 36.423 -7.572 1.00 22.78 ? 130 PHE A C 1 ATOM 813 O O . PHE A 1 109 ? 16.927 36.123 -6.816 1.00 23.11 ? 130 PHE A O 1 ATOM 814 C CB . PHE A 1 109 ? 18.884 38.737 -7.752 1.00 21.61 ? 130 PHE A CB 1 ATOM 815 C CG . PHE A 1 109 ? 18.902 40.056 -8.473 1.00 21.72 ? 130 PHE A CG 1 ATOM 816 C CD1 . PHE A 1 109 ? 19.512 40.173 -9.726 1.00 23.34 ? 130 PHE A CD1 1 ATOM 817 C CD2 . PHE A 1 109 ? 18.285 41.174 -7.919 1.00 20.89 ? 130 PHE A CD2 1 ATOM 818 C CE1 . PHE A 1 109 ? 19.518 41.383 -10.403 1.00 23.18 ? 130 PHE A CE1 1 ATOM 819 C CE2 . PHE A 1 109 ? 18.296 42.390 -8.584 1.00 21.89 ? 130 PHE A CE2 1 ATOM 820 C CZ . PHE A 1 109 ? 18.906 42.489 -9.832 1.00 22.83 ? 130 PHE A CZ 1 ATOM 821 N N . ASN A 1 110 ? 18.900 35.620 -7.806 1.00 24.69 ? 131 ASN A N 1 ATOM 822 C CA . ASN A 1 110 ? 19.020 34.296 -7.192 1.00 26.55 ? 131 ASN A CA 1 ATOM 823 C C . ASN A 1 110 ? 20.036 34.283 -6.065 1.00 26.91 ? 131 ASN A C 1 ATOM 824 O O . ASN A 1 110 ? 20.064 33.357 -5.253 1.00 25.60 ? 131 ASN A O 1 ATOM 825 C CB . ASN A 1 110 ? 19.420 33.235 -8.226 1.00 28.81 ? 131 ASN A CB 1 ATOM 826 C CG . ASN A 1 110 ? 18.278 32.855 -9.159 1.00 31.68 ? 131 ASN A CG 1 ATOM 827 O OD1 . ASN A 1 110 ? 17.097 32.923 -8.800 1.00 33.31 ? 131 ASN A OD1 1 ATOM 828 N ND2 . ASN A 1 110 ? 18.631 32.428 -10.354 1.00 32.67 ? 131 ASN A ND2 1 ATOM 829 N N . ASN A 1 111 ? 20.880 35.301 -6.049 1.00 25.94 ? 132 ASN A N 1 ATOM 830 C CA . ASN A 1 111 ? 21.855 35.533 -4.991 1.00 28.59 ? 132 ASN A CA 1 ATOM 831 C C . ASN A 1 111 ? 22.186 37.013 -5.015 1.00 27.66 ? 132 ASN A C 1 ATOM 832 O O . ASN A 1 111 ? 21.543 37.761 -5.741 1.00 28.70 ? 132 ASN A O 1 ATOM 833 C CB . ASN A 1 111 ? 23.108 34.691 -5.232 1.00 30.11 ? 132 ASN A CB 1 ATOM 834 C CG . ASN A 1 111 ? 23.673 34.886 -6.619 1.00 29.62 ? 132 ASN A CG 1 ATOM 835 O OD1 . ASN A 1 111 ? 23.961 36.008 -7.043 1.00 31.60 ? 132 ASN A OD1 1 ATOM 836 N ND2 . ASN A 1 111 ? 23.820 33.795 -7.343 1.00 32.64 ? 132 ASN A ND2 1 ATOM 837 N N . TYR A 1 112 ? 23.190 37.439 -4.248 1.00 28.22 ? 133 TYR A N 1 ATOM 838 C CA . TYR A 1 112 ? 23.538 38.856 -4.199 1.00 27.55 ? 133 TYR A CA 1 ATOM 839 C C . TYR A 1 112 ? 24.811 39.247 -4.967 1.00 28.94 ? 133 TYR A C 1 ATOM 840 O O . TYR A 1 112 ? 25.384 40.310 -4.733 1.00 28.36 ? 133 TYR A O 1 ATOM 841 C CB . TYR A 1 112 ? 23.556 39.393 -2.759 1.00 28.59 ? 133 TYR A CB 1 ATOM 842 C CG . TYR A 1 112 ? 24.411 38.632 -1.746 1.00 29.76 ? 133 TYR A CG 1 ATOM 843 C CD1 . TYR A 1 112 ? 25.734 39.012 -1.483 1.00 30.73 ? 133 TYR A CD1 1 ATOM 844 C CD2 . TYR A 1 112 ? 23.869 37.573 -1.018 1.00 30.11 ? 133 TYR A CD2 1 ATOM 845 C CE1 . TYR A 1 112 ? 26.501 38.326 -0.533 1.00 31.14 ? 133 TYR A CE1 1 ATOM 846 C CE2 . TYR A 1 112 ? 24.617 36.892 -0.065 1.00 32.29 ? 133 TYR A CE2 1 ATOM 847 C CZ . TYR A 1 112 ? 25.927 37.267 0.168 1.00 31.99 ? 133 TYR A CZ 1 ATOM 848 O OH . TYR A 1 112 ? 26.643 36.576 1.126 1.00 35.69 ? 133 TYR A OH 1 ATOM 849 N N . LYS A 1 113 ? 25.228 38.403 -5.902 1.00 28.75 ? 134 LYS A N 1 ATOM 850 C CA . LYS A 1 113 ? 26.357 38.744 -6.771 1.00 30.91 ? 134 LYS A CA 1 ATOM 851 C C . LYS A 1 113 ? 25.885 39.449 -8.053 1.00 30.79 ? 134 LYS A C 1 ATOM 852 O O . LYS A 1 113 ? 24.700 39.365 -8.442 1.00 28.62 ? 134 LYS A O 1 ATOM 853 C CB . LYS A 1 113 ? 27.193 37.499 -7.101 1.00 34.21 ? 134 LYS A CB 1 ATOM 854 C CG . LYS A 1 113 ? 27.694 36.744 -5.875 1.00 38.17 ? 134 LYS A CG 1 ATOM 855 C CD . LYS A 1 113 ? 28.579 35.563 -6.252 1.00 43.73 ? 134 LYS A CD 1 ATOM 856 C CE . LYS A 1 113 ? 28.821 34.658 -5.044 1.00 47.05 ? 134 LYS A CE 1 ATOM 857 N NZ . LYS A 1 113 ? 30.052 33.824 -5.158 1.00 52.94 ? 134 LYS A NZ 1 ATOM 858 N N . TYR A 1 114 ? 26.804 40.167 -8.687 1.00 29.19 ? 135 TYR A N 1 ATOM 859 C CA . TYR A 1 114 ? 26.543 40.759 -9.980 1.00 30.00 ? 135 TYR A CA 1 ATOM 860 C C . TYR A 1 114 ? 26.321 39.630 -10.979 1.00 30.99 ? 135 TYR A C 1 ATOM 861 O O . TYR A 1 114 ? 27.036 38.634 -10.958 1.00 29.44 ? 135 TYR A O 1 ATOM 862 C CB . TYR A 1 114 ? 27.698 41.657 -10.432 1.00 30.56 ? 135 TYR A CB 1 ATOM 863 C CG . TYR A 1 114 ? 27.394 42.356 -11.743 1.00 31.69 ? 135 TYR A CG 1 ATOM 864 C CD1 . TYR A 1 114 ? 26.798 43.614 -11.760 1.00 29.53 ? 135 TYR A CD1 1 ATOM 865 C CD2 . TYR A 1 114 ? 27.684 41.746 -12.965 1.00 33.53 ? 135 TYR A CD2 1 ATOM 866 C CE1 . TYR A 1 114 ? 26.512 44.254 -12.952 1.00 32.23 ? 135 TYR A CE1 1 ATOM 867 C CE2 . TYR A 1 114 ? 27.397 42.378 -14.159 1.00 33.10 ? 135 TYR A CE2 1 ATOM 868 C CZ . TYR A 1 114 ? 26.808 43.626 -14.151 1.00 32.91 ? 135 TYR A CZ 1 ATOM 869 O OH . TYR A 1 114 ? 26.509 44.242 -15.347 1.00 33.60 ? 135 TYR A OH 1 ATOM 870 N N . ASP A 1 115 ? 25.312 39.780 -11.833 1.00 29.98 ? 136 ASP A N 1 ATOM 871 C CA . ASP A 1 115 ? 25.025 38.801 -12.872 1.00 31.66 ? 136 ASP A CA 1 ATOM 872 C C . ASP A 1 115 ? 24.830 39.527 -14.193 1.00 32.05 ? 136 ASP A C 1 ATOM 873 O O . ASP A 1 115 ? 23.762 40.088 -14.441 1.00 30.04 ? 136 ASP A O 1 ATOM 874 C CB . ASP A 1 115 ? 23.778 37.988 -12.516 1.00 32.50 ? 136 ASP A CB 1 ATOM 875 C CG . ASP A 1 115 ? 23.399 36.978 -13.594 1.00 33.03 ? 136 ASP A CG 1 ATOM 876 O OD1 . ASP A 1 115 ? 24.157 36.784 -14.569 1.00 34.36 ? 136 ASP A OD1 1 ATOM 877 O OD2 . ASP A 1 115 ? 22.327 36.369 -13.458 1.00 36.72 ? 136 ASP A OD2 1 ATOM 878 N N . SER A 1 116 ? 25.866 39.520 -15.033 1.00 33.78 ? 137 SER A N 1 ATOM 879 C CA . SER A 1 116 ? 25.837 40.221 -16.320 1.00 36.10 ? 137 SER A CA 1 ATOM 880 C C . SER A 1 116 ? 24.781 39.690 -17.300 1.00 35.60 ? 137 SER A C 1 ATOM 881 O O . SER A 1 116 ? 24.546 40.305 -18.337 1.00 39.37 ? 137 SER A O 1 ATOM 882 C CB . SER A 1 116 ? 27.225 40.197 -16.982 1.00 38.74 ? 137 SER A CB 1 ATOM 883 O OG . SER A 1 116 ? 27.537 38.890 -17.415 1.00 41.73 ? 137 SER A OG 1 ATOM 884 N N . ASN A 1 117 ? 24.167 38.551 -16.982 1.00 34.33 ? 138 ASN A N 1 ATOM 885 C CA . ASN A 1 117 ? 23.094 37.992 -17.813 1.00 35.48 ? 138 ASN A CA 1 ATOM 886 C C . ASN A 1 117 ? 21.704 38.124 -17.178 1.00 32.08 ? 138 ASN A C 1 ATOM 887 O O . ASN A 1 117 ? 20.747 37.478 -17.614 1.00 31.08 ? 138 ASN A O 1 ATOM 888 C CB . ASN A 1 117 ? 23.383 36.528 -18.186 1.00 39.38 ? 138 ASN A CB 1 ATOM 889 C CG . ASN A 1 117 ? 24.744 36.344 -18.839 1.00 42.54 ? 138 ASN A CG 1 ATOM 890 O OD1 . ASN A 1 117 ? 25.428 35.357 -18.578 1.00 47.36 ? 138 ASN A OD1 1 ATOM 891 N ND2 . ASN A 1 117 ? 25.152 37.301 -19.671 1.00 43.43 ? 138 ASN A ND2 1 ATOM 892 N N . ALA A 1 118 ? 21.597 38.964 -16.147 1.00 28.45 ? 139 ALA A N 1 ATOM 893 C CA . ALA A 1 118 ? 20.308 39.189 -15.486 1.00 27.47 ? 139 ALA A CA 1 ATOM 894 C C . ALA A 1 118 ? 19.395 40.078 -16.340 1.00 25.84 ? 139 ALA A C 1 ATOM 895 O O . ALA A 1 118 ? 18.164 39.996 -16.238 1.00 24.56 ? 139 ALA A O 1 ATOM 896 C CB . ALA A 1 118 ? 20.515 39.819 -14.113 1.00 26.84 ? 139 ALA A CB 1 ATOM 897 N N . HIS A 1 119 ? 20.011 40.923 -17.164 1.00 23.51 ? 140 HIS A N 1 ATOM 898 C CA . HIS A 1 119 ? 19.299 41.918 -17.999 1.00 24.26 ? 140 HIS A CA 1 ATOM 899 C C . HIS A 1 119 ? 18.216 42.613 -17.212 1.00 22.54 ? 140 HIS A C 1 ATOM 900 O O . HIS A 1 119 ? 17.058 42.620 -17.616 1.00 22.50 ? 140 HIS A O 1 ATOM 901 C CB . HIS A 1 119 ? 18.701 41.265 -19.246 1.00 26.07 ? 140 HIS A CB 1 ATOM 902 C CG . HIS A 1 119 ? 19.684 40.448 -20.047 1.00 29.46 ? 140 HIS A CG 1 ATOM 903 N ND1 . HIS A 1 119 ? 20.710 41.008 -20.729 1.00 33.15 ? 140 HIS A ND1 1 ATOM 904 C CD2 . HIS A 1 119 ? 19.769 39.079 -20.263 1.00 30.66 ? 140 HIS A CD2 1 ATOM 905 C CE1 . HIS A 1 119 ? 21.415 40.043 -21.351 1.00 33.45 ? 140 HIS A CE1 1 ATOM 906 N NE2 . HIS A 1 119 ? 20.842 38.863 -21.068 1.00 32.57 ? 140 HIS A NE2 1 ATOM 907 N N . THR A 1 120 ? 18.589 43.166 -16.060 1.00 20.31 ? 141 THR A N 1 ATOM 908 C CA . THR A 1 120 ? 17.631 43.737 -15.098 1.00 19.85 ? 141 THR A CA 1 ATOM 909 C C . THR A 1 120 ? 18.041 45.146 -14.751 1.00 19.23 ? 141 THR A C 1 ATOM 910 O O . THR A 1 120 ? 19.202 45.394 -14.349 1.00 19.58 ? 141 THR A O 1 ATOM 911 C CB . THR A 1 120 ? 17.585 42.904 -13.803 1.00 19.67 ? 141 THR A CB 1 ATOM 912 O OG1 . THR A 1 120 ? 17.141 41.590 -14.116 1.00 20.53 ? 141 THR A OG1 1 ATOM 913 C CG2 . THR A 1 120 ? 16.650 43.523 -12.741 1.00 21.03 ? 141 THR A CG2 1 ATOM 914 N N . VAL A 1 121 ? 17.115 46.078 -14.941 1.00 17.55 ? 142 VAL A N 1 ATOM 915 C CA . VAL A 1 121 ? 17.256 47.432 -14.406 1.00 17.05 ? 142 VAL A CA 1 ATOM 916 C C . VAL A 1 121 ? 16.028 47.667 -13.536 1.00 18.25 ? 142 VAL A C 1 ATOM 917 O O . VAL A 1 121 ? 14.907 47.428 -13.993 1.00 18.44 ? 142 VAL A O 1 ATOM 918 C CB . VAL A 1 121 ? 17.316 48.506 -15.512 1.00 18.34 ? 142 VAL A CB 1 ATOM 919 C CG1 . VAL A 1 121 ? 17.344 49.910 -14.897 1.00 18.57 ? 142 VAL A CG1 1 ATOM 920 C CG2 . VAL A 1 121 ? 18.547 48.322 -16.412 1.00 17.76 ? 142 VAL A CG2 1 ATOM 921 N N . ALA A 1 122 ? 16.227 48.140 -12.311 1.00 16.59 ? 143 ALA A N 1 ATOM 922 C CA . ALA A 1 122 ? 15.093 48.316 -11.382 1.00 16.58 ? 143 ALA A CA 1 ATOM 923 C C . ALA A 1 122 ? 15.322 49.525 -10.505 1.00 17.18 ? 143 ALA A C 1 ATOM 924 O O . ALA A 1 122 ? 16.467 49.885 -10.250 1.00 17.33 ? 143 ALA A O 1 ATOM 925 C CB . ALA A 1 122 ? 14.958 47.084 -10.515 1.00 16.68 ? 143 ALA A CB 1 ATOM 926 N N . VAL A 1 123 ? 14.241 50.127 -10.005 1.00 15.42 ? 144 VAL A N 1 ATOM 927 C CA . VAL A 1 123 ? 14.370 51.135 -8.953 1.00 15.10 ? 144 VAL A CA 1 ATOM 928 C C . VAL A 1 123 ? 13.652 50.564 -7.741 1.00 15.57 ? 144 VAL A C 1 ATOM 929 O O . VAL A 1 123 ? 12.429 50.363 -7.775 1.00 15.47 ? 144 VAL A O 1 ATOM 930 C CB . VAL A 1 123 ? 13.772 52.499 -9.332 1.00 14.72 ? 144 VAL A CB 1 ATOM 931 C CG1 . VAL A 1 123 ? 13.769 53.464 -8.144 1.00 13.94 ? 144 VAL A CG1 1 ATOM 932 C CG2 . VAL A 1 123 ? 14.468 53.101 -10.551 1.00 15.67 ? 144 VAL A CG2 1 ATOM 933 N N . GLU A 1 124 ? 14.412 50.327 -6.670 1.00 15.03 ? 145 GLU A N 1 ATOM 934 C CA . GLU A 1 124 ? 13.895 49.638 -5.488 1.00 16.01 ? 145 GLU A CA 1 ATOM 935 C C . GLU A 1 124 ? 13.572 50.574 -4.336 1.00 15.41 ? 145 GLU A C 1 ATOM 936 O O . GLU A 1 124 ? 14.199 51.624 -4.169 1.00 15.68 ? 145 GLU A O 1 ATOM 937 C CB . GLU A 1 124 ? 14.866 48.556 -4.998 1.00 15.35 ? 145 GLU A CB 1 ATOM 938 C CG . GLU A 1 124 ? 16.240 49.103 -4.521 1.00 15.86 ? 145 GLU A CG 1 ATOM 939 C CD . GLU A 1 124 ? 17.040 48.066 -3.711 1.00 16.46 ? 145 GLU A CD 1 ATOM 940 O OE1 . GLU A 1 124 ? 17.229 46.953 -4.257 1.00 16.54 ? 145 GLU A OE1 1 ATOM 941 O OE2 . GLU A 1 124 ? 17.480 48.331 -2.539 1.00 17.63 ? 145 GLU A OE2 1 ATOM 942 N N . PHE A 1 125 ? 12.514 50.202 -3.601 1.00 14.98 ? 146 PHE A N 1 ATOM 943 C CA . PHE A 1 125 ? 12.055 50.904 -2.413 1.00 15.72 ? 146 PHE A CA 1 ATOM 944 C C . PHE A 1 125 ? 12.168 49.846 -1.331 1.00 17.04 ? 146 PHE A C 1 ATOM 945 O O . PHE A 1 125 ? 11.313 48.988 -1.187 1.00 15.61 ? 146 PHE A O 1 ATOM 946 C CB . PHE A 1 125 ? 10.624 51.432 -2.667 1.00 15.81 ? 146 PHE A CB 1 ATOM 947 C CG . PHE A 1 125 ? 10.601 52.407 -3.792 1.00 14.46 ? 146 PHE A CG 1 ATOM 948 C CD1 . PHE A 1 125 ? 10.768 53.766 -3.546 1.00 14.98 ? 146 PHE A CD1 1 ATOM 949 C CD2 . PHE A 1 125 ? 10.525 51.966 -5.118 1.00 14.28 ? 146 PHE A CD2 1 ATOM 950 C CE1 . PHE A 1 125 ? 10.831 54.675 -4.581 1.00 15.13 ? 146 PHE A CE1 1 ATOM 951 C CE2 . PHE A 1 125 ? 10.592 52.879 -6.157 1.00 13.57 ? 146 PHE A CE2 1 ATOM 952 C CZ . PHE A 1 125 ? 10.729 54.224 -5.895 1.00 14.02 ? 146 PHE A CZ 1 ATOM 953 N N . ASP A 1 126 ? 13.321 49.872 -0.651 1.00 16.81 ? 147 ASP A N 1 ATOM 954 C CA . ASP A 1 126 ? 13.809 48.719 0.166 1.00 18.82 ? 147 ASP A CA 1 ATOM 955 C C . ASP A 1 126 ? 13.578 49.046 1.646 1.00 17.10 ? 147 ASP A C 1 ATOM 956 O O . ASP A 1 126 ? 14.121 50.026 2.174 1.00 16.87 ? 147 ASP A O 1 ATOM 957 C CB . ASP A 1 126 ? 15.324 48.505 -0.150 1.00 19.57 ? 147 ASP A CB 1 ATOM 958 C CG . ASP A 1 126 ? 15.923 47.212 0.456 1.00 19.07 ? 147 ASP A CG 1 ATOM 959 O OD1 . ASP A 1 126 ? 15.262 46.645 1.351 1.00 18.96 ? 147 ASP A OD1 1 ATOM 960 O OD2 . ASP A 1 126 ? 17.057 46.763 0.034 1.00 19.14 ? 147 ASP A OD2 1 ATOM 961 N N . THR A 1 127 ? 12.765 48.217 2.305 1.00 16.29 ? 148 THR A N 1 ATOM 962 C CA . THR A 1 127 ? 12.327 48.482 3.676 1.00 17.17 ? 148 THR A CA 1 ATOM 963 C C . THR A 1 127 ? 13.011 47.623 4.714 1.00 17.29 ? 148 THR A C 1 ATOM 964 O O . THR A 1 127 ? 12.678 47.723 5.910 1.00 16.68 ? 148 THR A O 1 ATOM 965 C CB . THR A 1 127 ? 10.807 48.234 3.817 1.00 16.57 ? 148 THR A CB 1 ATOM 966 O OG1 . THR A 1 127 ? 10.522 46.875 3.491 1.00 18.34 ? 148 THR A OG1 1 ATOM 967 C CG2 . THR A 1 127 ? 10.043 49.186 2.906 1.00 17.72 ? 148 THR A CG2 1 ATOM 968 N N . LEU A 1 128 ? 13.927 46.759 4.270 1.00 17.76 ? 149 LEU A N 1 ATOM 969 C CA . LEU A 1 128 ? 14.589 45.800 5.167 1.00 17.16 ? 149 LEU A CA 1 ATOM 970 C C . LEU A 1 128 ? 16.094 45.746 4.895 1.00 16.51 ? 149 LEU A C 1 ATOM 971 O O . LEU A 1 128 ? 16.534 45.440 3.788 1.00 16.38 ? 149 LEU A O 1 ATOM 972 C CB . LEU A 1 128 ? 13.985 44.402 5.029 1.00 17.87 ? 149 LEU A CB 1 ATOM 973 C CG . LEU A 1 128 ? 14.629 43.572 6.168 1.00 20.92 ? 149 LEU A CG 1 ATOM 974 C CD1 . LEU A 1 128 ? 13.705 43.066 7.269 1.00 21.71 ? 149 LEU A CD1 1 ATOM 975 C CD2 . LEU A 1 128 ? 15.691 42.582 5.673 1.00 19.95 ? 149 LEU A CD2 1 ATOM 976 N N . TYR A 1 129 ? 16.862 46.041 5.941 1.00 16.87 ? 150 TYR A N 1 ATOM 977 C CA . TYR A 1 129 ? 18.342 45.994 5.850 1.00 16.99 ? 150 TYR A CA 1 ATOM 978 C C . TYR A 1 129 ? 18.855 44.562 5.740 1.00 17.06 ? 150 TYR A C 1 ATOM 979 O O . TYR A 1 129 ? 18.712 43.765 6.684 1.00 17.58 ? 150 TYR A O 1 ATOM 980 C CB . TYR A 1 129 ? 18.891 46.672 7.094 1.00 17.75 ? 150 TYR A CB 1 ATOM 981 C CG . TYR A 1 129 ? 20.358 46.386 7.396 1.00 18.65 ? 150 TYR A CG 1 ATOM 982 C CD1 . TYR A 1 129 ? 21.344 46.705 6.493 1.00 19.88 ? 150 TYR A CD1 1 ATOM 983 C CD2 . TYR A 1 129 ? 20.717 45.780 8.593 1.00 19.95 ? 150 TYR A CD2 1 ATOM 984 C CE1 . TYR A 1 129 ? 22.686 46.451 6.795 1.00 21.83 ? 150 TYR A CE1 1 ATOM 985 C CE2 . TYR A 1 129 ? 22.050 45.518 8.908 1.00 21.39 ? 150 TYR A CE2 1 ATOM 986 C CZ . TYR A 1 129 ? 23.022 45.850 8.007 1.00 22.02 ? 150 TYR A CZ 1 ATOM 987 O OH . TYR A 1 129 ? 24.354 45.584 8.344 1.00 22.61 ? 150 TYR A OH 1 ATOM 988 N N . ASN A 1 130 ? 19.475 44.241 4.599 1.00 16.73 ? 151 ASN A N 1 ATOM 989 C CA . ASN A 1 130 ? 20.022 42.912 4.371 1.00 17.67 ? 151 ASN A CA 1 ATOM 990 C C . ASN A 1 130 ? 21.525 43.058 4.560 1.00 18.31 ? 151 ASN A C 1 ATOM 991 O O . ASN A 1 130 ? 22.188 43.722 3.780 1.00 19.19 ? 151 ASN A O 1 ATOM 992 C CB . ASN A 1 130 ? 19.684 42.411 2.958 1.00 17.84 ? 151 ASN A CB 1 ATOM 993 C CG . ASN A 1 130 ? 18.223 41.990 2.828 1.00 18.23 ? 151 ASN A CG 1 ATOM 994 O OD1 . ASN A 1 130 ? 17.390 42.717 2.253 1.00 18.68 ? 151 ASN A OD1 1 ATOM 995 N ND2 . ASN A 1 130 ? 17.908 40.795 3.360 1.00 18.40 ? 151 ASN A ND2 1 ATOM 996 N N . VAL A 1 131 ? 22.020 42.470 5.637 1.00 19.03 ? 152 VAL A N 1 ATOM 997 C CA . VAL A 1 131 ? 23.398 42.713 6.105 1.00 20.10 ? 152 VAL A CA 1 ATOM 998 C C . VAL A 1 131 ? 24.502 42.531 5.057 1.00 19.97 ? 152 VAL A C 1 ATOM 999 O O . VAL A 1 131 ? 25.534 43.224 5.102 1.00 19.86 ? 152 VAL A O 1 ATOM 1000 C CB . VAL A 1 131 ? 23.678 41.851 7.369 1.00 19.92 ? 152 VAL A CB 1 ATOM 1001 C CG1 . VAL A 1 131 ? 23.601 40.364 7.063 1.00 20.45 ? 152 VAL A CG1 1 ATOM 1002 C CG2 . VAL A 1 131 ? 25.019 42.214 7.990 1.00 22.15 ? 152 VAL A CG2 1 ATOM 1003 N N . HIS A 1 132 ? 24.305 41.615 4.116 1.00 21.15 ? 153 HIS A N 1 ATOM 1004 C CA . HIS A 1 132 ? 25.372 41.286 3.160 1.00 21.77 ? 153 HIS A CA 1 ATOM 1005 C C . HIS A 1 132 ? 25.507 42.245 1.998 1.00 22.05 ? 153 HIS A C 1 ATOM 1006 O O . HIS A 1 132 ? 26.491 42.182 1.244 1.00 21.91 ? 153 HIS A O 1 ATOM 1007 C CB . HIS A 1 132 ? 25.237 39.853 2.672 1.00 23.60 ? 153 HIS A CB 1 ATOM 1008 C CG . HIS A 1 132 ? 25.331 38.816 3.766 1.00 25.27 ? 153 HIS A CG 1 ATOM 1009 N ND1 . HIS A 1 132 ? 26.398 38.725 4.603 1.00 25.99 ? 153 HIS A ND1 1 ATOM 1010 C CD2 . HIS A 1 132 ? 24.458 37.779 4.124 1.00 26.01 ? 153 HIS A CD2 1 ATOM 1011 C CE1 . HIS A 1 132 ? 26.209 37.708 5.466 1.00 25.66 ? 153 HIS A CE1 1 ATOM 1012 N NE2 . HIS A 1 132 ? 25.020 37.125 5.178 1.00 27.71 ? 153 HIS A NE2 1 ATOM 1013 N N . TRP A 1 133 ? 24.539 43.149 1.819 1.00 19.92 ? 154 TRP A N 1 ATOM 1014 C CA . TRP A 1 133 ? 24.604 44.099 0.697 1.00 19.31 ? 154 TRP A CA 1 ATOM 1015 C C . TRP A 1 133 ? 24.006 45.480 0.859 1.00 17.83 ? 154 TRP A C 1 ATOM 1016 O O . TRP A 1 133 ? 24.376 46.384 0.135 1.00 17.00 ? 154 TRP A O 1 ATOM 1017 C CB . TRP A 1 133 ? 24.061 43.446 -0.577 1.00 18.79 ? 154 TRP A CB 1 ATOM 1018 C CG . TRP A 1 133 ? 22.569 43.189 -0.523 1.00 18.60 ? 154 TRP A CG 1 ATOM 1019 C CD1 . TRP A 1 133 ? 21.550 44.098 -0.758 1.00 20.33 ? 154 TRP A CD1 1 ATOM 1020 C CD2 . TRP A 1 133 ? 21.906 41.919 -0.258 1.00 19.16 ? 154 TRP A CD2 1 ATOM 1021 N NE1 . TRP A 1 133 ? 20.306 43.489 -0.619 1.00 18.83 ? 154 TRP A NE1 1 ATOM 1022 C CE2 . TRP A 1 133 ? 20.459 42.180 -0.340 1.00 18.24 ? 154 TRP A CE2 1 ATOM 1023 C CE3 . TRP A 1 133 ? 22.341 40.631 0.051 1.00 19.64 ? 154 TRP A CE3 1 ATOM 1024 C CZ2 . TRP A 1 133 ? 19.532 41.187 -0.130 1.00 19.84 ? 154 TRP A CZ2 1 ATOM 1025 C CZ3 . TRP A 1 133 ? 21.390 39.637 0.261 1.00 21.01 ? 154 TRP A CZ3 1 ATOM 1026 C CH2 . TRP A 1 133 ? 20.007 39.919 0.182 1.00 20.09 ? 154 TRP A CH2 1 ATOM 1027 N N . ASP A 1 134 ? 23.046 45.660 1.773 1.00 17.54 ? 155 ASP A N 1 ATOM 1028 C CA . ASP A 1 134 ? 22.341 46.943 1.902 1.00 17.96 ? 155 ASP A CA 1 ATOM 1029 C C . ASP A 1 134 ? 23.031 47.964 2.815 1.00 17.83 ? 155 ASP A C 1 ATOM 1030 O O . ASP A 1 134 ? 23.659 47.564 3.793 1.00 19.19 ? 155 ASP A O 1 ATOM 1031 C CB . ASP A 1 134 ? 20.938 46.699 2.497 1.00 17.11 ? 155 ASP A CB 1 ATOM 1032 C CG . ASP A 1 134 ? 19.891 46.279 1.450 1.00 17.40 ? 155 ASP A CG 1 ATOM 1033 O OD1 . ASP A 1 134 ? 19.911 46.738 0.265 1.00 17.68 ? 155 ASP A OD1 1 ATOM 1034 O OD2 . ASP A 1 134 ? 18.981 45.518 1.891 1.00 16.54 ? 155 ASP A OD2 1 ATOM 1035 N N . PRO A 1 135 ? 22.826 49.277 2.556 1.00 18.14 ? 156 PRO A N 1 ATOM 1036 C CA . PRO A 1 135 ? 23.055 50.299 3.582 1.00 18.28 ? 156 PRO A CA 1 ATOM 1037 C C . PRO A 1 135 ? 22.039 50.085 4.704 1.00 19.28 ? 156 PRO A C 1 ATOM 1038 O O . PRO A 1 135 ? 20.955 49.545 4.450 1.00 20.15 ? 156 PRO A O 1 ATOM 1039 C CB . PRO A 1 135 ? 22.805 51.625 2.852 1.00 19.52 ? 156 PRO A CB 1 ATOM 1040 C CG . PRO A 1 135 ? 21.906 51.274 1.699 1.00 19.25 ? 156 PRO A CG 1 ATOM 1041 C CD . PRO A 1 135 ? 22.181 49.837 1.339 1.00 18.12 ? 156 PRO A CD 1 ATOM 1042 N N . LYS A 1 136 ? 22.414 50.448 5.932 1.00 18.90 ? 157 LYS A N 1 ATOM 1043 C CA . LYS A 1 136 ? 21.548 50.238 7.104 1.00 21.20 ? 157 LYS A CA 1 ATOM 1044 C C . LYS A 1 136 ? 20.186 50.978 7.037 1.00 20.01 ? 157 LYS A C 1 ATOM 1045 O O . LYS A 1 136 ? 19.145 50.365 7.330 1.00 21.71 ? 157 LYS A O 1 ATOM 1046 C CB . LYS A 1 136 ? 22.306 50.536 8.410 1.00 23.54 ? 157 LYS A CB 1 ATOM 1047 C CG . LYS A 1 136 ? 23.390 49.504 8.722 1.00 26.18 ? 157 LYS A CG 1 ATOM 1048 C CD . LYS A 1 136 ? 23.972 49.711 10.121 1.00 29.38 ? 157 LYS A CD 1 ATOM 1049 C CE . LYS A 1 136 ? 23.286 48.818 11.153 1.00 32.94 ? 157 LYS A CE 1 ATOM 1050 N NZ . LYS A 1 136 ? 23.766 49.076 12.546 1.00 33.63 ? 157 LYS A NZ 1 ATOM 1051 N N . PRO A 1 137 ? 20.182 52.285 6.679 1.00 20.60 ? 158 PRO A N 1 ATOM 1052 C CA . PRO A 1 137 ? 18.891 52.977 6.583 1.00 19.08 ? 158 PRO A CA 1 ATOM 1053 C C . PRO A 1 137 ? 18.067 52.461 5.413 1.00 18.76 ? 158 PRO A C 1 ATOM 1054 O O . PRO A 1 137 ? 18.627 52.080 4.381 1.00 17.69 ? 158 PRO A O 1 ATOM 1055 C CB . PRO A 1 137 ? 19.273 54.445 6.332 1.00 19.83 ? 158 PRO A CB 1 ATOM 1056 C CG . PRO A 1 137 ? 20.729 54.549 6.765 1.00 20.90 ? 158 PRO A CG 1 ATOM 1057 C CD . PRO A 1 137 ? 21.308 53.208 6.432 1.00 20.09 ? 158 PRO A CD 1 ATOM 1058 N N . ARG A 1 138 ? 16.734 52.459 5.564 1.00 17.86 ? 159 ARG A N 1 ATOM 1059 C CA . ARG A 1 138 ? 15.864 52.149 4.431 1.00 17.26 ? 159 ARG A CA 1 ATOM 1060 C C . ARG A 1 138 ? 16.158 53.148 3.325 1.00 17.54 ? 159 ARG A C 1 ATOM 1061 O O . ARG A 1 138 ? 16.610 54.270 3.584 1.00 19.37 ? 159 ARG A O 1 ATOM 1062 C CB . ARG A 1 138 ? 14.376 52.182 4.864 1.00 16.60 ? 159 ARG A CB 1 ATOM 1063 C CG . ARG A 1 138 ? 14.076 51.135 5.931 1.00 16.81 ? 159 ARG A CG 1 ATOM 1064 C CD . ARG A 1 138 ? 12.612 51.141 6.382 1.00 16.84 ? 159 ARG A CD 1 ATOM 1065 N NE . ARG A 1 138 ? 12.445 50.129 7.428 1.00 16.95 ? 159 ARG A NE 1 ATOM 1066 C CZ . ARG A 1 138 ? 12.289 50.402 8.723 1.00 17.48 ? 159 ARG A CZ 1 ATOM 1067 N NH1 . ARG A 1 138 ? 12.221 51.656 9.164 1.00 19.69 ? 159 ARG A NH1 1 ATOM 1068 N NH2 . ARG A 1 138 ? 12.189 49.410 9.588 1.00 17.68 ? 159 ARG A NH2 1 ATOM 1069 N N . HIS A 1 139 ? 15.926 52.739 2.083 1.00 17.20 ? 160 HIS A N 1 ATOM 1070 C CA . HIS A 1 139 ? 16.548 53.445 0.959 1.00 17.05 ? 160 HIS A CA 1 ATOM 1071 C C . HIS A 1 139 ? 15.810 53.254 -0.337 1.00 16.64 ? 160 HIS A C 1 ATOM 1072 O O . HIS A 1 139 ? 15.080 52.265 -0.526 1.00 16.45 ? 160 HIS A O 1 ATOM 1073 C CB . HIS A 1 139 ? 18.034 52.985 0.802 1.00 17.12 ? 160 HIS A CB 1 ATOM 1074 C CG . HIS A 1 139 ? 18.217 51.482 0.689 1.00 17.69 ? 160 HIS A CG 1 ATOM 1075 N ND1 . HIS A 1 139 ? 18.264 50.668 1.768 1.00 17.63 ? 160 HIS A ND1 1 ATOM 1076 C CD2 . HIS A 1 139 ? 18.322 50.653 -0.438 1.00 17.32 ? 160 HIS A CD2 1 ATOM 1077 C CE1 . HIS A 1 139 ? 18.429 49.387 1.365 1.00 16.04 ? 160 HIS A CE1 1 ATOM 1078 N NE2 . HIS A 1 139 ? 18.455 49.357 -0.006 1.00 19.96 ? 160 HIS A NE2 1 ATOM 1079 N N . ILE A 1 140 ? 15.995 54.209 -1.238 1.00 17.17 ? 161 ILE A N 1 ATOM 1080 C CA . ILE A 1 140 ? 15.616 54.016 -2.639 1.00 17.53 ? 161 ILE A CA 1 ATOM 1081 C C . ILE A 1 140 ? 16.930 53.677 -3.316 1.00 17.79 ? 161 ILE A C 1 ATOM 1082 O O . ILE A 1 140 ? 17.949 54.305 -3.020 1.00 19.46 ? 161 ILE A O 1 ATOM 1083 C CB . ILE A 1 140 ? 15.042 55.304 -3.248 1.00 19.36 ? 161 ILE A CB 1 ATOM 1084 C CG1 . ILE A 1 140 ? 13.856 55.806 -2.411 1.00 20.21 ? 161 ILE A CG1 1 ATOM 1085 C CG2 . ILE A 1 140 ? 14.670 55.095 -4.723 1.00 18.38 ? 161 ILE A CG2 1 ATOM 1086 C CD1 . ILE A 1 140 ? 13.557 57.270 -2.669 1.00 21.51 ? 161 ILE A CD1 1 ATOM 1087 N N . GLY A 1 141 ? 16.925 52.649 -4.153 1.00 17.77 ? 162 GLY A N 1 ATOM 1088 C CA . GLY A 1 141 ? 18.157 52.237 -4.852 1.00 17.79 ? 162 GLY A CA 1 ATOM 1089 C C . GLY A 1 141 ? 17.941 52.028 -6.337 1.00 18.81 ? 162 GLY A C 1 ATOM 1090 O O . GLY A 1 141 ? 16.856 51.623 -6.760 1.00 18.08 ? 162 GLY A O 1 ATOM 1091 N N . ILE A 1 142 ? 18.981 52.325 -7.117 1.00 17.43 ? 163 ILE A N 1 ATOM 1092 C CA . ILE A 1 142 ? 19.026 51.998 -8.540 1.00 18.72 ? 163 ILE A CA 1 ATOM 1093 C C . ILE A 1 142 ? 19.791 50.677 -8.689 1.00 18.15 ? 163 ILE A C 1 ATOM 1094 O O . ILE A 1 142 ? 20.959 50.567 -8.258 1.00 18.67 ? 163 ILE A O 1 ATOM 1095 C CB . ILE A 1 142 ? 19.676 53.151 -9.373 1.00 18.04 ? 163 ILE A CB 1 ATOM 1096 C CG1 . ILE A 1 142 ? 18.887 54.455 -9.230 1.00 19.54 ? 163 ILE A CG1 1 ATOM 1097 C CG2 . ILE A 1 142 ? 19.811 52.754 -10.845 1.00 18.55 ? 163 ILE A CG2 1 ATOM 1098 C CD1 . ILE A 1 142 ? 19.524 55.703 -9.819 1.00 19.81 ? 163 ILE A CD1 1 ATOM 1099 N N . ASP A 1 143 ? 19.121 49.670 -9.247 1.00 17.59 ? 164 ASP A N 1 ATOM 1100 C CA . ASP A 1 143 ? 19.658 48.312 -9.366 1.00 18.37 ? 164 ASP A CA 1 ATOM 1101 C C . ASP A 1 143 ? 19.914 47.989 -10.820 1.00 19.28 ? 164 ASP A C 1 ATOM 1102 O O . ASP A 1 143 ? 18.981 48.027 -11.651 1.00 18.80 ? 164 ASP A O 1 ATOM 1103 C CB . ASP A 1 143 ? 18.678 47.265 -8.814 1.00 17.52 ? 164 ASP A CB 1 ATOM 1104 C CG . ASP A 1 143 ? 18.463 47.380 -7.315 1.00 18.05 ? 164 ASP A CG 1 ATOM 1105 O OD1 . ASP A 1 143 ? 19.112 48.236 -6.696 1.00 18.91 ? 164 ASP A OD1 1 ATOM 1106 O OD2 . ASP A 1 143 ? 17.613 46.619 -6.777 1.00 18.01 ? 164 ASP A OD2 1 ATOM 1107 N N . VAL A 1 144 ? 21.175 47.688 -11.133 1.00 18.49 ? 165 VAL A N 1 ATOM 1108 C CA . VAL A 1 144 ? 21.547 47.231 -12.483 1.00 19.91 ? 165 VAL A CA 1 ATOM 1109 C C . VAL A 1 144 ? 22.205 45.854 -12.383 1.00 20.55 ? 165 VAL A C 1 ATOM 1110 O O . VAL A 1 144 ? 23.378 45.748 -11.957 1.00 19.85 ? 165 VAL A O 1 ATOM 1111 C CB . VAL A 1 144 ? 22.511 48.238 -13.172 1.00 19.50 ? 165 VAL A CB 1 ATOM 1112 C CG1 . VAL A 1 144 ? 22.939 47.743 -14.552 1.00 20.47 ? 165 VAL A CG1 1 ATOM 1113 C CG2 . VAL A 1 144 ? 21.884 49.621 -13.291 1.00 21.18 ? 165 VAL A CG2 1 ATOM 1114 N N . ASN A 1 145 ? 21.459 44.803 -12.730 1.00 19.09 ? 166 ASN A N 1 ATOM 1115 C CA . ASN A 1 145 ? 21.984 43.416 -12.743 1.00 21.12 ? 166 ASN A CA 1 ATOM 1116 C C . ASN A 1 145 ? 22.493 42.871 -11.398 1.00 21.43 ? 166 ASN A C 1 ATOM 1117 O O . ASN A 1 145 ? 23.269 41.899 -11.367 1.00 22.82 ? 166 ASN A O 1 ATOM 1118 C CB . ASN A 1 145 ? 23.117 43.294 -13.780 1.00 20.25 ? 166 ASN A CB 1 ATOM 1119 C CG . ASN A 1 145 ? 22.604 43.205 -15.203 1.00 22.70 ? 166 ASN A CG 1 ATOM 1120 O OD1 . ASN A 1 145 ? 21.452 42.832 -15.436 1.00 22.62 ? 166 ASN A OD1 1 ATOM 1121 N ND2 . ASN A 1 145 ? 23.474 43.511 -16.166 1.00 22.99 ? 166 ASN A ND2 1 ATOM 1122 N N . SER A 1 146 ? 22.075 43.513 -10.307 1.00 19.82 ? 167 SER A N 1 ATOM 1123 C CA . SER A 1 146 ? 22.449 43.088 -8.975 1.00 19.22 ? 167 SER A CA 1 ATOM 1124 C C . SER A 1 146 ? 21.500 43.681 -7.934 1.00 19.05 ? 167 SER A C 1 ATOM 1125 O O . SER A 1 146 ? 20.995 44.809 -8.101 1.00 18.27 ? 167 SER A O 1 ATOM 1126 C CB . SER A 1 146 ? 23.862 43.543 -8.649 1.00 19.98 ? 167 SER A CB 1 ATOM 1127 O OG . SER A 1 146 ? 24.219 43.073 -7.363 1.00 20.19 ? 167 SER A OG 1 ATOM 1128 N N . ILE A 1 147 ? 21.288 42.918 -6.862 1.00 19.30 ? 168 ILE A N 1 ATOM 1129 C CA . ILE A 1 147 ? 20.559 43.441 -5.691 1.00 19.53 ? 168 ILE A CA 1 ATOM 1130 C C . ILE A 1 147 ? 21.414 44.469 -4.927 1.00 20.43 ? 168 ILE A C 1 ATOM 1131 O O . ILE A 1 147 ? 20.887 45.251 -4.134 1.00 20.00 ? 168 ILE A O 1 ATOM 1132 C CB . ILE A 1 147 ? 20.047 42.308 -4.758 1.00 20.50 ? 168 ILE A CB 1 ATOM 1133 C CG1 . ILE A 1 147 ? 18.920 42.805 -3.840 1.00 20.35 ? 168 ILE A CG1 1 ATOM 1134 C CG2 . ILE A 1 147 ? 21.188 41.775 -3.885 1.00 20.25 ? 168 ILE A CG2 1 ATOM 1135 C CD1 . ILE A 1 147 ? 17.610 43.130 -4.557 1.00 19.65 ? 168 ILE A CD1 1 ATOM 1136 N N . LYS A 1 148 ? 22.739 44.480 -5.165 1.00 19.19 ? 169 LYS A N 1 ATOM 1137 C CA . LYS A 1 148 ? 23.588 45.508 -4.569 1.00 20.29 ? 169 LYS A CA 1 ATOM 1138 C C . LYS A 1 148 ? 23.499 46.765 -5.424 1.00 20.16 ? 169 LYS A C 1 ATOM 1139 O O . LYS A 1 148 ? 24.149 46.843 -6.492 1.00 20.37 ? 169 LYS A O 1 ATOM 1140 C CB . LYS A 1 148 ? 25.066 45.035 -4.475 1.00 21.23 ? 169 LYS A CB 1 ATOM 1141 C CG . LYS A 1 148 ? 25.951 46.037 -3.740 1.00 25.22 ? 169 LYS A CG 1 ATOM 1142 C CD . LYS A 1 148 ? 27.439 45.795 -4.005 1.00 27.92 ? 169 LYS A CD 1 ATOM 1143 C CE . LYS A 1 148 ? 28.211 47.060 -3.664 1.00 32.30 ? 169 LYS A CE 1 ATOM 1144 N NZ . LYS A 1 148 ? 29.623 47.057 -4.166 1.00 36.36 ? 169 LYS A NZ 1 ATOM 1145 N N . SER A 1 149 ? 22.731 47.752 -4.964 1.00 19.24 ? 170 SER A N 1 ATOM 1146 C CA . SER A 1 149 ? 22.379 48.927 -5.788 1.00 19.04 ? 170 SER A CA 1 ATOM 1147 C C . SER A 1 149 ? 23.621 49.667 -6.217 1.00 19.75 ? 170 SER A C 1 ATOM 1148 O O . SER A 1 149 ? 24.542 49.801 -5.423 1.00 19.67 ? 170 SER A O 1 ATOM 1149 C CB . SER A 1 149 ? 21.490 49.889 -5.013 1.00 19.27 ? 170 SER A CB 1 ATOM 1150 O OG . SER A 1 149 ? 20.324 49.209 -4.578 1.00 18.35 ? 170 SER A OG 1 ATOM 1151 N N . ILE A 1 150 ? 23.640 50.180 -7.448 1.00 19.12 ? 171 ILE A N 1 ATOM 1152 C CA . ILE A 1 150 ? 24.762 51.045 -7.873 1.00 19.57 ? 171 ILE A CA 1 ATOM 1153 C C . ILE A 1 150 ? 24.756 52.390 -7.153 1.00 21.60 ? 171 ILE A C 1 ATOM 1154 O O . ILE A 1 150 ? 25.796 53.056 -6.998 1.00 22.05 ? 171 ILE A O 1 ATOM 1155 C CB . ILE A 1 150 ? 24.820 51.251 -9.405 1.00 19.56 ? 171 ILE A CB 1 ATOM 1156 C CG1 . ILE A 1 150 ? 23.569 51.992 -9.927 1.00 19.36 ? 171 ILE A CG1 1 ATOM 1157 C CG2 . ILE A 1 150 ? 24.998 49.898 -10.067 1.00 20.19 ? 171 ILE A CG2 1 ATOM 1158 C CD1 . ILE A 1 150 ? 23.672 52.421 -11.384 1.00 20.28 ? 171 ILE A CD1 1 ATOM 1159 N N . LYS A 1 151 ? 23.583 52.791 -6.679 1.00 20.27 ? 172 LYS A N 1 ATOM 1160 C CA . LYS A 1 151 ? 23.475 54.034 -5.967 1.00 21.10 ? 172 LYS A CA 1 ATOM 1161 C C . LYS A 1 151 ? 22.208 54.019 -5.125 1.00 21.29 ? 172 LYS A C 1 ATOM 1162 O O . LYS A 1 151 ? 21.182 53.485 -5.554 1.00 21.19 ? 172 LYS A O 1 ATOM 1163 C CB . LYS A 1 151 ? 23.454 55.206 -6.925 1.00 21.50 ? 172 LYS A CB 1 ATOM 1164 C CG . LYS A 1 151 ? 23.822 56.508 -6.238 1.00 24.93 ? 172 LYS A CG 1 ATOM 1165 C CD . LYS A 1 151 ? 24.394 57.487 -7.222 1.00 25.20 ? 172 LYS A CD 1 ATOM 1166 C CE . LYS A 1 151 ? 24.708 58.800 -6.543 1.00 24.46 ? 172 LYS A CE 1 ATOM 1167 N NZ . LYS A 1 151 ? 24.738 59.819 -7.626 1.00 25.19 ? 172 LYS A NZ 1 ATOM 1168 N N . THR A 1 152 ? 22.299 54.599 -3.928 1.00 20.71 ? 173 THR A N 1 ATOM 1169 C CA . THR A 1 152 ? 21.132 54.696 -3.034 1.00 20.61 ? 173 THR A CA 1 ATOM 1170 C C . THR A 1 152 ? 21.011 56.086 -2.420 1.00 21.49 ? 173 THR A C 1 ATOM 1171 O O . THR A 1 152 ? 21.971 56.865 -2.403 1.00 21.12 ? 173 THR A O 1 ATOM 1172 C CB . THR A 1 152 ? 21.177 53.656 -1.882 1.00 21.10 ? 173 THR A CB 1 ATOM 1173 O OG1 . THR A 1 152 ? 22.358 53.870 -1.075 1.00 20.85 ? 173 THR A OG1 1 ATOM 1174 C CG2 . THR A 1 152 ? 21.154 52.210 -2.412 1.00 19.90 ? 173 THR A CG2 1 ATOM 1175 N N . THR A 1 153 ? 19.806 56.411 -1.950 1.00 20.12 ? 174 THR A N 1 ATOM 1176 C CA . THR A 1 153 ? 19.583 57.543 -1.071 1.00 19.79 ? 174 THR A CA 1 ATOM 1177 C C . THR A 1 153 ? 18.735 57.081 0.105 1.00 19.67 ? 174 THR A C 1 ATOM 1178 O O . THR A 1 153 ? 17.907 56.172 -0.045 1.00 17.86 ? 174 THR A O 1 ATOM 1179 C CB . THR A 1 153 ? 18.955 58.765 -1.785 1.00 20.86 ? 174 THR A CB 1 ATOM 1180 O OG1 . THR A 1 153 ? 19.088 59.923 -0.948 1.00 22.68 ? 174 THR A OG1 1 ATOM 1181 C CG2 . THR A 1 153 ? 17.459 58.558 -2.106 1.00 19.74 ? 174 THR A CG2 1 ATOM 1182 N N . THR A 1 154 ? 18.938 57.706 1.270 1.00 18.67 ? 175 THR A N 1 ATOM 1183 C CA . THR A 1 154 ? 18.127 57.381 2.448 1.00 19.52 ? 175 THR A CA 1 ATOM 1184 C C . THR A 1 154 ? 16.649 57.702 2.194 1.00 18.27 ? 175 THR A C 1 ATOM 1185 O O . THR A 1 154 ? 16.315 58.763 1.640 1.00 18.75 ? 175 THR A O 1 ATOM 1186 C CB . THR A 1 154 ? 18.626 58.118 3.703 1.00 22.24 ? 175 THR A CB 1 ATOM 1187 O OG1 . THR A 1 154 ? 19.896 57.572 4.052 1.00 24.02 ? 175 THR A OG1 1 ATOM 1188 C CG2 . THR A 1 154 ? 17.658 57.899 4.883 1.00 21.80 ? 175 THR A CG2 1 ATOM 1189 N N . TRP A 1 155 ? 15.790 56.769 2.594 1.00 17.73 ? 176 TRP A N 1 ATOM 1190 C CA . TRP A 1 155 ? 14.338 56.950 2.486 1.00 17.48 ? 176 TRP A CA 1 ATOM 1191 C C . TRP A 1 155 ? 13.737 56.860 3.870 1.00 18.49 ? 176 TRP A C 1 ATOM 1192 O O . TRP A 1 155 ? 13.844 55.819 4.528 1.00 19.87 ? 176 TRP A O 1 ATOM 1193 C CB . TRP A 1 155 ? 13.773 55.876 1.558 1.00 16.90 ? 176 TRP A CB 1 ATOM 1194 C CG . TRP A 1 155 ? 12.254 55.718 1.527 1.00 16.41 ? 176 TRP A CG 1 ATOM 1195 C CD1 . TRP A 1 155 ? 11.272 56.703 1.597 1.00 17.54 ? 176 TRP A CD1 1 ATOM 1196 C CD2 . TRP A 1 155 ? 11.529 54.468 1.340 1.00 15.59 ? 176 TRP A CD2 1 ATOM 1197 N NE1 . TRP A 1 155 ? 10.007 56.138 1.513 1.00 16.43 ? 176 TRP A NE1 1 ATOM 1198 C CE2 . TRP A 1 155 ? 10.105 54.805 1.346 1.00 15.48 ? 176 TRP A CE2 1 ATOM 1199 C CE3 . TRP A 1 155 ? 11.909 53.133 1.198 1.00 15.58 ? 176 TRP A CE3 1 ATOM 1200 C CZ2 . TRP A 1 155 ? 9.129 53.837 1.205 1.00 15.33 ? 176 TRP A CZ2 1 ATOM 1201 C CZ3 . TRP A 1 155 ? 10.915 52.163 1.048 1.00 15.78 ? 176 TRP A CZ3 1 ATOM 1202 C CH2 . TRP A 1 155 ? 9.544 52.517 1.074 1.00 15.51 ? 176 TRP A CH2 1 ATOM 1203 N N . ASP A 1 156 ? 13.135 57.961 4.324 1.00 19.32 ? 177 ASP A N 1 ATOM 1204 C CA . ASP A 1 156 ? 12.476 57.981 5.636 1.00 20.59 ? 177 ASP A CA 1 ATOM 1205 C C . ASP A 1 156 ? 11.106 57.351 5.505 1.00 20.22 ? 177 ASP A C 1 ATOM 1206 O O . ASP A 1 156 ? 10.094 58.057 5.450 1.00 21.50 ? 177 ASP A O 1 ATOM 1207 C CB . ASP A 1 156 ? 12.401 59.408 6.197 1.00 23.07 ? 177 ASP A CB 1 ATOM 1208 C CG . ASP A 1 156 ? 13.785 60.000 6.451 1.00 25.98 ? 177 ASP A CG 1 ATOM 1209 O OD1 . ASP A 1 156 ? 14.678 59.221 6.849 1.00 28.57 ? 177 ASP A OD1 1 ATOM 1210 O OD2 . ASP A 1 156 ? 13.981 61.220 6.224 1.00 27.31 ? 177 ASP A OD2 1 ATOM 1211 N N . PHE A 1 157 ? 11.095 56.020 5.445 1.00 20.88 ? 178 PHE A N 1 ATOM 1212 C CA . PHE A 1 157 ? 9.859 55.238 5.273 1.00 19.29 ? 178 PHE A CA 1 ATOM 1213 C C . PHE A 1 157 ? 8.868 55.473 6.412 1.00 19.84 ? 178 PHE A C 1 ATOM 1214 O O . PHE A 1 157 ? 9.235 55.505 7.584 1.00 20.44 ? 178 PHE A O 1 ATOM 1215 C CB . PHE A 1 157 ? 10.220 53.750 5.175 1.00 20.07 ? 178 PHE A CB 1 ATOM 1216 C CG . PHE A 1 157 ? 9.090 52.824 5.447 1.00 19.78 ? 178 PHE A CG 1 ATOM 1217 C CD1 . PHE A 1 157 ? 8.148 52.540 4.458 1.00 19.62 ? 178 PHE A CD1 1 ATOM 1218 C CD2 . PHE A 1 157 ? 8.978 52.182 6.683 1.00 20.15 ? 178 PHE A CD2 1 ATOM 1219 C CE1 . PHE A 1 157 ? 7.090 51.664 4.716 1.00 20.21 ? 178 PHE A CE1 1 ATOM 1220 C CE2 . PHE A 1 157 ? 7.934 51.300 6.937 1.00 20.03 ? 178 PHE A CE2 1 ATOM 1221 C CZ . PHE A 1 157 ? 6.982 51.041 5.954 1.00 19.99 ? 178 PHE A CZ 1 ATOM 1222 N N . VAL A 1 158 ? 7.601 55.637 6.060 1.00 19.69 ? 179 VAL A N 1 ATOM 1223 C CA . VAL A 1 158 ? 6.531 55.745 7.069 1.00 19.89 ? 179 VAL A CA 1 ATOM 1224 C C . VAL A 1 158 ? 5.404 54.819 6.609 1.00 20.99 ? 179 VAL A C 1 ATOM 1225 O O . VAL A 1 158 ? 4.919 54.950 5.463 1.00 20.44 ? 179 VAL A O 1 ATOM 1226 C CB . VAL A 1 158 ? 6.035 57.206 7.225 1.00 19.63 ? 179 VAL A CB 1 ATOM 1227 C CG1 . VAL A 1 158 ? 4.846 57.278 8.175 1.00 20.72 ? 179 VAL A CG1 1 ATOM 1228 C CG2 . VAL A 1 158 ? 7.144 58.130 7.739 1.00 19.34 ? 179 VAL A CG2 1 ATOM 1229 N N . LYS A 1 159 ? 5.004 53.874 7.470 1.00 20.14 ? 180 LYS A N 1 ATOM 1230 C CA . LYS A 1 159 ? 4.008 52.873 7.091 1.00 20.47 ? 180 LYS A CA 1 ATOM 1231 C C . LYS A 1 159 ? 2.645 53.519 6.838 1.00 20.14 ? 180 LYS A C 1 ATOM 1232 O O . LYS A 1 159 ? 2.270 54.499 7.507 1.00 20.47 ? 180 LYS A O 1 ATOM 1233 C CB . LYS A 1 159 ? 3.869 51.751 8.138 1.00 20.77 ? 180 LYS A CB 1 ATOM 1234 C CG . LYS A 1 159 ? 3.282 52.201 9.480 1.00 23.01 ? 180 LYS A CG 1 ATOM 1235 C CD . LYS A 1 159 ? 2.912 51.002 10.334 1.00 25.53 ? 180 LYS A CD 1 ATOM 1236 C CE . LYS A 1 159 ? 2.399 51.410 11.715 1.00 28.16 ? 180 LYS A CE 1 ATOM 1237 N NZ . LYS A 1 159 ? 1.890 50.215 12.458 1.00 31.27 ? 180 LYS A NZ 1 ATOM 1238 N N . GLY A 1 160 ? 1.966 52.995 5.825 1.00 19.68 ? 181 GLY A N 1 ATOM 1239 C CA . GLY A 1 160 ? 0.556 53.325 5.540 1.00 19.74 ? 181 GLY A CA 1 ATOM 1240 C C . GLY A 1 160 ? 0.329 54.694 4.925 1.00 20.56 ? 181 GLY A C 1 ATOM 1241 O O . GLY A 1 160 ? -0.813 55.076 4.711 1.00 22.52 ? 181 GLY A O 1 ATOM 1242 N N . GLU A 1 161 ? 1.394 55.450 4.650 1.00 20.08 ? 182 GLU A N 1 ATOM 1243 C CA . GLU A 1 161 ? 1.246 56.735 3.983 1.00 20.42 ? 182 GLU A CA 1 ATOM 1244 C C . GLU A 1 161 ? 1.463 56.563 2.480 1.00 20.23 ? 182 GLU A C 1 ATOM 1245 O O . GLU A 1 161 ? 2.487 55.989 2.078 1.00 21.03 ? 182 GLU A O 1 ATOM 1246 C CB . GLU A 1 161 ? 2.246 57.762 4.510 1.00 23.18 ? 182 GLU A CB 1 ATOM 1247 C CG . GLU A 1 161 ? 2.053 58.151 5.973 1.00 26.16 ? 182 GLU A CG 1 ATOM 1248 C CD . GLU A 1 161 ? 0.917 59.140 6.181 1.00 30.96 ? 182 GLU A CD 1 ATOM 1249 O OE1 . GLU A 1 161 ? 0.409 59.714 5.198 1.00 33.14 ? 182 GLU A OE1 1 ATOM 1250 O OE2 . GLU A 1 161 ? 0.519 59.339 7.339 1.00 33.52 ? 182 GLU A OE2 1 ATOM 1251 N N . ASN A 1 162 ? 0.548 57.082 1.660 1.00 19.50 ? 183 ASN A N 1 ATOM 1252 C CA . ASN A 1 162 ? 0.743 57.009 0.191 1.00 18.35 ? 183 ASN A CA 1 ATOM 1253 C C . ASN A 1 162 ? 2.029 57.707 -0.238 1.00 18.59 ? 183 ASN A C 1 ATOM 1254 O O . ASN A 1 162 ? 2.268 58.865 0.140 1.00 18.27 ? 183 ASN A O 1 ATOM 1255 C CB . ASN A 1 162 ? -0.401 57.672 -0.574 1.00 18.91 ? 183 ASN A CB 1 ATOM 1256 C CG . ASN A 1 162 ? -1.686 56.863 -0.549 1.00 19.05 ? 183 ASN A CG 1 ATOM 1257 O OD1 . ASN A 1 162 ? -1.735 55.749 -0.050 1.00 19.91 ? 183 ASN A OD1 1 ATOM 1258 N ND2 . ASN A 1 162 ? -2.736 57.429 -1.120 1.00 20.09 ? 183 ASN A ND2 1 ATOM 1259 N N . ALA A 1 163 ? 2.813 57.008 -1.061 1.00 16.58 ? 184 ALA A N 1 ATOM 1260 C CA . ALA A 1 163 ? 4.071 57.538 -1.610 1.00 16.74 ? 184 ALA A CA 1 ATOM 1261 C C . ALA A 1 163 ? 3.893 57.731 -3.105 1.00 16.98 ? 184 ALA A C 1 ATOM 1262 O O . ALA A 1 163 ? 3.418 56.820 -3.786 1.00 18.14 ? 184 ALA A O 1 ATOM 1263 C CB . ALA A 1 163 ? 5.188 56.551 -1.360 1.00 16.71 ? 184 ALA A CB 1 ATOM 1264 N N . GLU A 1 164 ? 4.281 58.898 -3.607 1.00 17.10 ? 185 GLU A N 1 ATOM 1265 C CA . GLU A 1 164 ? 4.196 59.188 -5.048 1.00 17.08 ? 185 GLU A CA 1 ATOM 1266 C C . GLU A 1 164 ? 5.609 59.197 -5.633 1.00 17.02 ? 185 GLU A C 1 ATOM 1267 O O . GLU A 1 164 ? 6.460 60.000 -5.222 1.00 16.66 ? 185 GLU A O 1 ATOM 1268 C CB . GLU A 1 164 ? 3.511 60.525 -5.275 1.00 20.61 ? 185 GLU A CB 1 ATOM 1269 C CG . GLU A 1 164 ? 2.060 60.536 -4.807 1.00 23.34 ? 185 GLU A CG 1 ATOM 1270 C CD . GLU A 1 164 ? 1.414 61.906 -4.895 1.00 28.00 ? 185 GLU A CD 1 ATOM 1271 O OE1 . GLU A 1 164 ? 2.128 62.891 -5.180 1.00 32.77 ? 185 GLU A OE1 1 ATOM 1272 O OE2 . GLU A 1 164 ? 0.191 62.008 -4.652 1.00 30.29 ? 185 GLU A OE2 1 ATOM 1273 N N . VAL A 1 165 ? 5.848 58.294 -6.574 1.00 16.25 ? 186 VAL A N 1 ATOM 1274 C CA . VAL A 1 165 ? 7.186 58.134 -7.199 1.00 15.37 ? 186 VAL A CA 1 ATOM 1275 C C . VAL A 1 165 ? 7.177 58.691 -8.612 1.00 16.37 ? 186 VAL A C 1 ATOM 1276 O O . VAL A 1 165 ? 6.171 58.585 -9.323 1.00 15.86 ? 186 VAL A O 1 ATOM 1277 C CB . VAL A 1 165 ? 7.529 56.626 -7.281 1.00 15.02 ? 186 VAL A CB 1 ATOM 1278 C CG1 . VAL A 1 165 ? 8.831 56.364 -8.059 1.00 15.60 ? 186 VAL A CG1 1 ATOM 1279 C CG2 . VAL A 1 165 ? 7.599 56.052 -5.868 1.00 16.18 ? 186 VAL A CG2 1 ATOM 1280 N N . LEU A 1 166 ? 8.305 59.268 -9.017 1.00 15.87 ? 187 LEU A N 1 ATOM 1281 C CA . LEU A 1 166 ? 8.545 59.615 -10.415 1.00 15.82 ? 187 LEU A CA 1 ATOM 1282 C C . LEU A 1 166 ? 9.930 59.117 -10.772 1.00 16.35 ? 187 LEU A C 1 ATOM 1283 O O . LEU A 1 166 ? 10.890 59.399 -10.066 1.00 17.83 ? 187 LEU A O 1 ATOM 1284 C CB . LEU A 1 166 ? 8.466 61.132 -10.646 1.00 15.56 ? 187 LEU A CB 1 ATOM 1285 C CG . LEU A 1 166 ? 8.891 61.597 -12.060 1.00 16.54 ? 187 LEU A CG 1 ATOM 1286 C CD1 . LEU A 1 166 ? 7.867 61.160 -13.111 1.00 16.53 ? 187 LEU A CD1 1 ATOM 1287 C CD2 . LEU A 1 166 ? 9.025 63.113 -12.092 1.00 17.51 ? 187 LEU A CD2 1 ATOM 1288 N N . ILE A 1 167 ? 10.024 58.341 -11.849 1.00 16.11 ? 188 ILE A N 1 ATOM 1289 C CA . ILE A 1 167 ? 11.297 57.826 -12.331 1.00 15.59 ? 188 ILE A CA 1 ATOM 1290 C C . ILE A 1 167 ? 11.432 58.306 -13.773 1.00 16.48 ? 188 ILE A C 1 ATOM 1291 O O . ILE A 1 167 ? 10.497 58.193 -14.573 1.00 16.51 ? 188 ILE A O 1 ATOM 1292 C CB . ILE A 1 167 ? 11.324 56.285 -12.288 1.00 14.57 ? 188 ILE A CB 1 ATOM 1293 C CG1 . ILE A 1 167 ? 11.209 55.784 -10.833 1.00 14.27 ? 188 ILE A CG1 1 ATOM 1294 C CG2 . ILE A 1 167 ? 12.577 55.752 -12.990 1.00 14.65 ? 188 ILE A CG2 1 ATOM 1295 C CD1 . ILE A 1 167 ? 10.907 54.298 -10.719 1.00 14.67 ? 188 ILE A CD1 1 ATOM 1296 N N . THR A 1 168 ? 12.586 58.847 -14.131 1.00 16.68 ? 189 THR A N 1 ATOM 1297 C CA . THR A 1 168 ? 12.762 59.347 -15.499 1.00 16.99 ? 189 THR A CA 1 ATOM 1298 C C . THR A 1 168 ? 14.079 58.810 -16.031 1.00 18.34 ? 189 THR A C 1 ATOM 1299 O O . THR A 1 168 ? 15.012 58.562 -15.259 1.00 18.30 ? 189 THR A O 1 ATOM 1300 C CB . THR A 1 168 ? 12.776 60.896 -15.571 1.00 17.78 ? 189 THR A CB 1 ATOM 1301 O OG1 . THR A 1 168 ? 13.844 61.424 -14.761 1.00 18.03 ? 189 THR A OG1 1 ATOM 1302 C CG2 . THR A 1 168 ? 11.458 61.480 -15.057 1.00 17.68 ? 189 THR A CG2 1 ATOM 1303 N N . TYR A 1 169 ? 14.133 58.601 -17.337 1.00 17.70 ? 190 TYR A N 1 ATOM 1304 C CA . TYR A 1 169 ? 15.374 58.194 -17.978 1.00 18.24 ? 190 TYR A CA 1 ATOM 1305 C C . TYR A 1 169 ? 15.537 59.034 -19.231 1.00 19.06 ? 190 TYR A C 1 ATOM 1306 O O . TYR A 1 169 ? 14.633 59.076 -20.094 1.00 18.78 ? 190 TYR A O 1 ATOM 1307 C CB . TYR A 1 169 ? 15.358 56.707 -18.331 1.00 17.83 ? 190 TYR A CB 1 ATOM 1308 C CG . TYR A 1 169 ? 16.665 56.282 -18.975 1.00 18.82 ? 190 TYR A CG 1 ATOM 1309 C CD1 . TYR A 1 169 ? 17.812 56.123 -18.189 1.00 19.31 ? 190 TYR A CD1 1 ATOM 1310 C CD2 . TYR A 1 169 ? 16.776 56.118 -20.362 1.00 18.46 ? 190 TYR A CD2 1 ATOM 1311 C CE1 . TYR A 1 169 ? 19.020 55.768 -18.758 1.00 19.81 ? 190 TYR A CE1 1 ATOM 1312 C CE2 . TYR A 1 169 ? 17.994 55.775 -20.943 1.00 19.79 ? 190 TYR A CE2 1 ATOM 1313 C CZ . TYR A 1 169 ? 19.106 55.592 -20.124 1.00 20.63 ? 190 TYR A CZ 1 ATOM 1314 O OH . TYR A 1 169 ? 20.329 55.248 -20.666 1.00 21.17 ? 190 TYR A OH 1 ATOM 1315 N N . ASP A 1 170 ? 16.681 59.699 -19.336 1.00 19.37 ? 191 ASP A N 1 ATOM 1316 C CA . ASP A 1 170 ? 16.973 60.551 -20.477 1.00 21.05 ? 191 ASP A CA 1 ATOM 1317 C C . ASP A 1 170 ? 18.090 59.859 -21.259 1.00 21.51 ? 191 ASP A C 1 ATOM 1318 O O . ASP A 1 170 ? 19.225 59.802 -20.805 1.00 23.02 ? 191 ASP A O 1 ATOM 1319 C CB . ASP A 1 170 ? 17.402 61.952 -19.987 1.00 22.22 ? 191 ASP A CB 1 ATOM 1320 C CG . ASP A 1 170 ? 17.758 62.902 -21.120 1.00 23.14 ? 191 ASP A CG 1 ATOM 1321 O OD1 . ASP A 1 170 ? 18.081 62.447 -22.229 1.00 26.11 ? 191 ASP A OD1 1 ATOM 1322 O OD2 . ASP A 1 170 ? 17.727 64.120 -20.901 1.00 25.90 ? 191 ASP A OD2 1 ATOM 1323 N N . SER A 1 171 ? 17.779 59.335 -22.436 1.00 20.94 ? 192 SER A N 1 ATOM 1324 C CA . SER A 1 171 ? 18.766 58.544 -23.150 1.00 23.33 ? 192 SER A CA 1 ATOM 1325 C C . SER A 1 171 ? 19.918 59.388 -23.715 1.00 23.67 ? 192 SER A C 1 ATOM 1326 O O . SER A 1 171 ? 20.987 58.836 -24.022 1.00 24.31 ? 192 SER A O 1 ATOM 1327 C CB . SER A 1 171 ? 18.124 57.705 -24.243 1.00 22.49 ? 192 SER A CB 1 ATOM 1328 O OG . SER A 1 171 ? 17.682 58.549 -25.272 1.00 22.61 ? 192 SER A OG 1 ATOM 1329 N N . SER A 1 172 ? 19.725 60.701 -23.829 1.00 23.36 ? 193 SER A N 1 ATOM 1330 C CA . SER A 1 172 ? 20.829 61.556 -24.306 1.00 25.26 ? 193 SER A CA 1 ATOM 1331 C C . SER A 1 172 ? 21.950 61.689 -23.271 1.00 25.70 ? 193 SER A C 1 ATOM 1332 O O . SER A 1 172 ? 23.125 61.752 -23.646 1.00 27.49 ? 193 SER A O 1 ATOM 1333 C CB . SER A 1 172 ? 20.361 62.930 -24.794 1.00 25.84 ? 193 SER A CB 1 ATOM 1334 O OG . SER A 1 172 ? 19.951 63.781 -23.740 1.00 28.37 ? 193 SER A OG 1 ATOM 1335 N N . THR A 1 173 ? 21.581 61.725 -21.989 1.00 23.33 ? 194 THR A N 1 ATOM 1336 C CA . THR A 1 173 ? 22.547 61.859 -20.877 1.00 23.53 ? 194 THR A CA 1 ATOM 1337 C C . THR A 1 173 ? 22.773 60.519 -20.159 1.00 23.95 ? 194 THR A C 1 ATOM 1338 O O . THR A 1 173 ? 23.700 60.379 -19.330 1.00 23.86 ? 194 THR A O 1 ATOM 1339 C CB . THR A 1 173 ? 22.049 62.872 -19.831 1.00 23.27 ? 194 THR A CB 1 ATOM 1340 O OG1 . THR A 1 173 ? 20.821 62.386 -19.250 1.00 22.04 ? 194 THR A OG1 1 ATOM 1341 C CG2 . THR A 1 173 ? 21.819 64.241 -20.445 1.00 24.33 ? 194 THR A CG2 1 ATOM 1342 N N . LYS A 1 174 ? 21.923 59.537 -20.478 1.00 22.30 ? 195 LYS A N 1 ATOM 1343 C CA . LYS A 1 174 ? 21.871 58.222 -19.806 1.00 22.89 ? 195 LYS A CA 1 ATOM 1344 C C . LYS A 1 174 ? 21.507 58.309 -18.320 1.00 20.34 ? 195 LYS A C 1 ATOM 1345 O O . LYS A 1 174 ? 21.645 57.332 -17.573 1.00 20.80 ? 195 LYS A O 1 ATOM 1346 C CB . LYS A 1 174 ? 23.183 57.435 -19.982 1.00 24.78 ? 195 LYS A CB 1 ATOM 1347 C CG . LYS A 1 174 ? 23.569 57.238 -21.438 1.00 27.37 ? 195 LYS A CG 1 ATOM 1348 C CD . LYS A 1 174 ? 24.885 56.501 -21.589 1.00 29.90 ? 195 LYS A CD 1 ATOM 1349 C CE . LYS A 1 174 ? 25.404 56.692 -23.009 1.00 31.29 ? 195 LYS A CE 1 ATOM 1350 N NZ . LYS A 1 174 ? 25.926 55.402 -23.525 1.00 35.23 ? 195 LYS A NZ 1 ATOM 1351 N N . LEU A 1 175 ? 21.015 59.461 -17.889 1.00 20.21 ? 196 LEU A N 1 ATOM 1352 C CA . LEU A 1 175 ? 20.668 59.627 -16.473 1.00 19.17 ? 196 LEU A CA 1 ATOM 1353 C C . LEU A 1 175 ? 19.312 59.025 -16.106 1.00 19.13 ? 196 LEU A C 1 ATOM 1354 O O . LEU A 1 175 ? 18.289 59.342 -16.737 1.00 18.97 ? 196 LEU A O 1 ATOM 1355 C CB . LEU A 1 175 ? 20.705 61.094 -16.077 1.00 19.33 ? 196 LEU A CB 1 ATOM 1356 C CG . LEU A 1 175 ? 20.746 61.372 -14.571 1.00 19.45 ? 196 LEU A CG 1 ATOM 1357 C CD1 . LEU A 1 175 ? 22.117 61.010 -13.983 1.00 20.97 ? 196 LEU A CD1 1 ATOM 1358 C CD2 . LEU A 1 175 ? 20.401 62.839 -14.324 1.00 20.56 ? 196 LEU A CD2 1 ATOM 1359 N N . LEU A 1 176 ? 19.339 58.158 -15.094 1.00 17.46 ? 197 LEU A N 1 ATOM 1360 C CA . LEU A 1 176 ? 18.115 57.634 -14.480 1.00 17.91 ? 197 LEU A CA 1 ATOM 1361 C C . LEU A 1 176 ? 17.929 58.366 -13.165 1.00 18.24 ? 197 LEU A C 1 ATOM 1362 O O . LEU A 1 176 ? 18.845 58.412 -12.317 1.00 19.19 ? 197 LEU A O 1 ATOM 1363 C CB . LEU A 1 176 ? 18.228 56.126 -14.259 1.00 17.28 ? 197 LEU A CB 1 ATOM 1364 C CG . LEU A 1 176 ? 17.013 55.351 -13.727 1.00 18.86 ? 197 LEU A CG 1 ATOM 1365 C CD1 . LEU A 1 176 ? 15.854 55.408 -14.698 1.00 20.02 ? 197 LEU A CD1 1 ATOM 1366 C CD2 . LEU A 1 176 ? 17.405 53.899 -13.553 1.00 20.52 ? 197 LEU A CD2 1 ATOM 1367 N N . VAL A 1 177 ? 16.746 58.944 -12.971 1.00 17.32 ? 198 VAL A N 1 ATOM 1368 C CA . VAL A 1 177 ? 16.497 59.707 -11.755 1.00 16.51 ? 198 VAL A CA 1 ATOM 1369 C C . VAL A 1 177 ? 15.248 59.127 -11.101 1.00 17.26 ? 198 VAL A C 1 ATOM 1370 O O . VAL A 1 177 ? 14.244 58.918 -11.791 1.00 17.24 ? 198 VAL A O 1 ATOM 1371 C CB . VAL A 1 177 ? 16.276 61.201 -12.056 1.00 16.98 ? 198 VAL A CB 1 ATOM 1372 C CG1 . VAL A 1 177 ? 15.960 61.992 -10.787 1.00 17.56 ? 198 VAL A CG1 1 ATOM 1373 C CG2 . VAL A 1 177 ? 17.483 61.812 -12.762 1.00 17.46 ? 198 VAL A CG2 1 ATOM 1374 N N . ALA A 1 178 ? 15.324 58.872 -9.797 1.00 16.71 ? 199 ALA A N 1 ATOM 1375 C CA . ALA A 1 178 ? 14.144 58.385 -9.053 1.00 16.80 ? 199 ALA A CA 1 ATOM 1376 C C . ALA A 1 178 ? 13.865 59.304 -7.879 1.00 16.90 ? 199 ALA A C 1 ATOM 1377 O O . ALA A 1 178 ? 14.776 59.638 -7.108 1.00 17.16 ? 199 ALA A O 1 ATOM 1378 C CB . ALA A 1 178 ? 14.362 56.971 -8.554 1.00 15.80 ? 199 ALA A CB 1 ATOM 1379 N N . SER A 1 179 ? 12.597 59.655 -7.694 1.00 16.90 ? 200 SER A N 1 ATOM 1380 C CA . SER A 1 179 ? 12.210 60.484 -6.569 1.00 17.56 ? 200 SER A CA 1 ATOM 1381 C C . SER A 1 179 ? 10.924 59.962 -5.949 1.00 18.16 ? 200 SER A C 1 ATOM 1382 O O . SER A 1 179 ? 10.094 59.357 -6.628 1.00 17.78 ? 200 SER A O 1 ATOM 1383 C CB . SER A 1 179 ? 12.060 61.944 -6.991 1.00 19.11 ? 200 SER A CB 1 ATOM 1384 O OG . SER A 1 179 ? 11.028 62.103 -7.960 1.00 21.33 ? 200 SER A OG 1 ATOM 1385 N N . LEU A 1 180 ? 10.781 60.199 -4.651 1.00 17.59 ? 201 LEU A N 1 ATOM 1386 C CA . LEU A 1 180 ? 9.598 59.798 -3.904 1.00 17.91 ? 201 LEU A CA 1 ATOM 1387 C C . LEU A 1 180 ? 9.169 60.973 -3.057 1.00 18.05 ? 201 LEU A C 1 ATOM 1388 O O . LEU A 1 180 ? 9.990 61.643 -2.440 1.00 19.29 ? 201 LEU A O 1 ATOM 1389 C CB . LEU A 1 180 ? 9.907 58.595 -2.993 1.00 16.89 ? 201 LEU A CB 1 ATOM 1390 C CG . LEU A 1 180 ? 8.773 58.005 -2.152 1.00 17.46 ? 201 LEU A CG 1 ATOM 1391 C CD1 . LEU A 1 180 ? 9.000 56.499 -1.975 1.00 16.98 ? 201 LEU A CD1 1 ATOM 1392 C CD2 . LEU A 1 180 ? 8.603 58.696 -0.798 1.00 18.13 ? 201 LEU A CD2 1 ATOM 1393 N N . VAL A 1 181 ? 7.869 61.219 -3.019 1.00 18.57 ? 202 VAL A N 1 ATOM 1394 C CA . VAL A 1 181 ? 7.328 62.222 -2.120 1.00 20.09 ? 202 VAL A CA 1 ATOM 1395 C C . VAL A 1 181 ? 6.199 61.596 -1.305 1.00 19.94 ? 202 VAL A C 1 ATOM 1396 O O . VAL A 1 181 ? 5.476 60.735 -1.809 1.00 19.38 ? 202 VAL A O 1 ATOM 1397 C CB . VAL A 1 181 ? 6.860 63.521 -2.849 1.00 21.24 ? 202 VAL A CB 1 ATOM 1398 C CG1 . VAL A 1 181 ? 7.984 64.128 -3.688 1.00 22.41 ? 202 VAL A CG1 1 ATOM 1399 C CG2 . VAL A 1 181 ? 5.636 63.293 -3.707 1.00 23.09 ? 202 VAL A CG2 1 ATOM 1400 N N . TYR A 1 182 ? 6.099 61.983 -0.035 1.00 19.35 ? 203 TYR A N 1 ATOM 1401 C CA . TYR A 1 182 ? 4.936 61.671 0.772 1.00 19.66 ? 203 TYR A CA 1 ATOM 1402 C C . TYR A 1 182 ? 4.124 62.963 0.881 1.00 20.53 ? 203 TYR A C 1 ATOM 1403 O O . TYR A 1 182 ? 4.498 63.844 1.657 1.00 20.29 ? 203 TYR A O 1 ATOM 1404 C CB . TYR A 1 182 ? 5.362 61.232 2.173 1.00 18.70 ? 203 TYR A CB 1 ATOM 1405 C CG . TYR A 1 182 ? 5.883 59.829 2.349 1.00 17.37 ? 203 TYR A CG 1 ATOM 1406 C CD1 . TYR A 1 182 ? 5.069 58.718 2.165 1.00 17.75 ? 203 TYR A CD1 1 ATOM 1407 C CD2 . TYR A 1 182 ? 7.213 59.613 2.757 1.00 16.77 ? 203 TYR A CD2 1 ATOM 1408 C CE1 . TYR A 1 182 ? 5.534 57.431 2.358 1.00 16.69 ? 203 TYR A CE1 1 ATOM 1409 C CE2 . TYR A 1 182 ? 7.690 58.325 2.968 1.00 17.88 ? 203 TYR A CE2 1 ATOM 1410 C CZ . TYR A 1 182 ? 6.861 57.245 2.786 1.00 17.38 ? 203 TYR A CZ 1 ATOM 1411 O OH . TYR A 1 182 ? 7.335 55.977 2.994 1.00 18.09 ? 203 TYR A OH 1 ATOM 1412 N N . PRO A 1 183 ? 3.009 63.088 0.111 1.00 21.19 ? 204 PRO A N 1 ATOM 1413 C CA . PRO A 1 183 ? 2.325 64.387 0.118 1.00 22.33 ? 204 PRO A CA 1 ATOM 1414 C C . PRO A 1 183 ? 1.814 64.779 1.506 1.00 23.43 ? 204 PRO A C 1 ATOM 1415 O O . PRO A 1 183 ? 1.865 65.955 1.858 1.00 25.00 ? 204 PRO A O 1 ATOM 1416 C CB . PRO A 1 183 ? 1.136 64.191 -0.833 1.00 23.58 ? 204 PRO A CB 1 ATOM 1417 C CG . PRO A 1 183 ? 1.463 62.982 -1.653 1.00 24.45 ? 204 PRO A CG 1 ATOM 1418 C CD . PRO A 1 183 ? 2.444 62.148 -0.879 1.00 22.08 ? 204 PRO A CD 1 ATOM 1419 N N . SER A 1 184 ? 1.330 63.807 2.275 1.00 24.85 ? 205 SER A N 1 ATOM 1420 C CA . SER A 1 184 ? 0.746 64.093 3.597 1.00 25.85 ? 205 SER A CA 1 ATOM 1421 C C . SER A 1 184 ? 1.806 64.469 4.641 1.00 25.48 ? 205 SER A C 1 ATOM 1422 O O . SER A 1 184 ? 1.496 65.139 5.626 1.00 26.52 ? 205 SER A O 1 ATOM 1423 C CB . SER A 1 184 ? -0.086 62.920 4.087 1.00 27.84 ? 205 SER A CB 1 ATOM 1424 O OG . SER A 1 184 ? 0.745 61.795 4.318 1.00 34.25 ? 205 SER A OG 1 ATOM 1425 N N . LEU A 1 185 ? 3.053 64.069 4.408 1.00 24.09 ? 206 LEU A N 1 ATOM 1426 C CA . LEU A 1 185 ? 4.158 64.408 5.310 1.00 24.42 ? 206 LEU A CA 1 ATOM 1427 C C . LEU A 1 185 ? 5.032 65.552 4.798 1.00 23.78 ? 206 LEU A C 1 ATOM 1428 O O . LEU A 1 185 ? 5.862 66.079 5.547 1.00 23.21 ? 206 LEU A O 1 ATOM 1429 C CB . LEU A 1 185 ? 5.025 63.174 5.577 1.00 24.26 ? 206 LEU A CB 1 ATOM 1430 C CG . LEU A 1 185 ? 4.312 61.912 6.056 1.00 23.64 ? 206 LEU A CG 1 ATOM 1431 C CD1 . LEU A 1 185 ? 5.314 60.784 6.168 1.00 24.22 ? 206 LEU A CD1 1 ATOM 1432 C CD2 . LEU A 1 185 ? 3.610 62.134 7.397 1.00 25.46 ? 206 LEU A CD2 1 ATOM 1433 N N . LYS A 1 186 ? 4.863 65.893 3.516 1.00 22.97 ? 207 LYS A N 1 ATOM 1434 C CA . LYS A 1 186 ? 5.601 66.959 2.832 1.00 23.00 ? 207 LYS A CA 1 ATOM 1435 C C . LYS A 1 186 ? 7.100 66.637 2.691 1.00 22.28 ? 207 LYS A C 1 ATOM 1436 O O . LYS A 1 186 ? 7.928 67.531 2.532 1.00 23.25 ? 207 LYS A O 1 ATOM 1437 C CB . LYS A 1 186 ? 5.368 68.324 3.508 1.00 24.83 ? 207 LYS A CB 1 ATOM 1438 C CG . LYS A 1 186 ? 3.897 68.643 3.792 1.00 25.86 ? 207 LYS A CG 1 ATOM 1439 C CD . LYS A 1 186 ? 3.794 69.934 4.588 1.00 29.81 ? 207 LYS A CD 1 ATOM 1440 C CE . LYS A 1 186 ? 2.630 69.916 5.560 1.00 34.24 ? 207 LYS A CE 1 ATOM 1441 N NZ . LYS A 1 186 ? 1.467 70.681 5.029 1.00 39.44 ? 207 LYS A NZ 1 ATOM 1442 N N . THR A 1 187 ? 7.439 65.351 2.731 1.00 22.09 ? 208 THR A N 1 ATOM 1443 C CA . THR A 1 187 ? 8.844 64.934 2.641 1.00 21.08 ? 208 THR A CA 1 ATOM 1444 C C . THR A 1 187 ? 9.173 64.404 1.243 1.00 21.78 ? 208 THR A C 1 ATOM 1445 O O . THR A 1 187 ? 8.301 63.917 0.534 1.00 20.28 ? 208 THR A O 1 ATOM 1446 C CB . THR A 1 187 ? 9.211 63.883 3.709 1.00 21.75 ? 208 THR A CB 1 ATOM 1447 O OG1 . THR A 1 187 ? 8.355 62.746 3.576 1.00 20.05 ? 208 THR A OG1 1 ATOM 1448 C CG2 . THR A 1 187 ? 9.078 64.472 5.137 1.00 21.99 ? 208 THR A CG2 1 ATOM 1449 N N . SER A 1 188 ? 10.444 64.474 0.861 1.00 20.37 ? 209 SER A N 1 ATOM 1450 C CA . SER A 1 188 ? 10.828 64.138 -0.513 1.00 19.74 ? 209 SER A CA 1 ATOM 1451 C C . SER A 1 188 ? 12.250 63.642 -0.536 1.00 20.54 ? 209 SER A C 1 ATOM 1452 O O . SER A 1 188 ? 13.066 64.079 0.274 1.00 20.60 ? 209 SER A O 1 ATOM 1453 C CB . SER A 1 188 ? 10.676 65.370 -1.407 1.00 20.17 ? 209 SER A CB 1 ATOM 1454 O OG . SER A 1 188 ? 11.430 66.468 -0.879 1.00 20.74 ? 209 SER A OG 1 ATOM 1455 N N . PHE A 1 189 ? 12.529 62.716 -1.458 1.00 19.95 ? 210 PHE A N 1 ATOM 1456 C CA . PHE A 1 189 ? 13.799 61.995 -1.562 1.00 19.07 ? 210 PHE A CA 1 ATOM 1457 C C . PHE A 1 189 ? 14.130 61.827 -3.041 1.00 19.13 ? 210 PHE A C 1 ATOM 1458 O O . PHE A 1 189 ? 13.224 61.741 -3.867 1.00 19.64 ? 210 PHE A O 1 ATOM 1459 C CB . PHE A 1 189 ? 13.693 60.628 -0.859 1.00 19.21 ? 210 PHE A CB 1 ATOM 1460 C CG . PHE A 1 189 ? 13.010 60.707 0.479 1.00 19.08 ? 210 PHE A CG 1 ATOM 1461 C CD1 . PHE A 1 189 ? 13.737 60.972 1.629 1.00 20.01 ? 210 PHE A CD1 1 ATOM 1462 C CD2 . PHE A 1 189 ? 11.616 60.545 0.583 1.00 19.54 ? 210 PHE A CD2 1 ATOM 1463 C CE1 . PHE A 1 189 ? 13.102 61.088 2.865 1.00 20.32 ? 210 PHE A CE1 1 ATOM 1464 C CE2 . PHE A 1 189 ? 10.975 60.653 1.819 1.00 20.61 ? 210 PHE A CE2 1 ATOM 1465 C CZ . PHE A 1 189 ? 11.722 60.931 2.959 1.00 20.67 ? 210 PHE A CZ 1 ATOM 1466 N N . ILE A 1 190 ? 15.418 61.820 -3.380 1.00 18.95 ? 211 ILE A N 1 ATOM 1467 C CA . ILE A 1 190 ? 15.833 61.713 -4.786 1.00 18.12 ? 211 ILE A CA 1 ATOM 1468 C C . ILE A 1 190 ? 17.176 61.031 -4.915 1.00 19.60 ? 211 ILE A C 1 ATOM 1469 O O . ILE A 1 190 ? 18.048 61.240 -4.071 1.00 18.43 ? 211 ILE A O 1 ATOM 1470 C CB . ILE A 1 190 ? 15.848 63.105 -5.494 1.00 18.56 ? 211 ILE A CB 1 ATOM 1471 C CG1 . ILE A 1 190 ? 16.018 62.953 -7.023 1.00 18.36 ? 211 ILE A CG1 1 ATOM 1472 C CG2 . ILE A 1 190 ? 16.891 64.059 -4.879 1.00 18.77 ? 211 ILE A CG2 1 ATOM 1473 C CD1 . ILE A 1 190 ? 15.637 64.194 -7.805 1.00 18.75 ? 211 ILE A CD1 1 ATOM 1474 N N . VAL A 1 191 ? 17.327 60.221 -5.964 1.00 19.06 ? 212 VAL A N 1 ATOM 1475 C CA . VAL A 1 191 ? 18.586 59.543 -6.285 1.00 18.56 ? 212 VAL A CA 1 ATOM 1476 C C . VAL A 1 191 ? 18.788 59.553 -7.800 1.00 19.27 ? 212 VAL A C 1 ATOM 1477 O O . VAL A 1 191 ? 17.817 59.512 -8.561 1.00 18.62 ? 212 VAL A O 1 ATOM 1478 C CB . VAL A 1 191 ? 18.651 58.104 -5.682 1.00 18.72 ? 212 VAL A CB 1 ATOM 1479 C CG1 . VAL A 1 191 ? 17.572 57.202 -6.264 1.00 19.14 ? 212 VAL A CG1 1 ATOM 1480 C CG2 . VAL A 1 191 ? 20.037 57.480 -5.839 1.00 19.46 ? 212 VAL A CG2 1 ATOM 1481 N N . SER A 1 192 ? 20.042 59.634 -8.251 1.00 18.85 ? 213 SER A N 1 ATOM 1482 C CA . SER A 1 192 ? 20.290 59.699 -9.681 1.00 19.99 ? 213 SER A CA 1 ATOM 1483 C C . SER A 1 192 ? 21.616 59.058 -10.003 1.00 20.69 ? 213 SER A C 1 ATOM 1484 O O . SER A 1 192 ? 22.583 59.215 -9.243 1.00 19.91 ? 213 SER A O 1 ATOM 1485 C CB . SER A 1 192 ? 20.279 61.159 -10.173 1.00 20.57 ? 213 SER A CB 1 ATOM 1486 O OG . SER A 1 192 ? 21.208 61.962 -9.441 1.00 23.59 ? 213 SER A OG 1 ATOM 1487 N N . ASP A 1 193 ? 21.653 58.331 -11.118 1.00 20.43 ? 214 ASP A N 1 ATOM 1488 C CA . ASP A 1 193 ? 22.905 57.742 -11.635 1.00 20.38 ? 214 ASP A CA 1 ATOM 1489 C C . ASP A 1 193 ? 22.743 57.458 -13.117 1.00 21.74 ? 214 ASP A C 1 ATOM 1490 O O . ASP A 1 193 ? 21.615 57.387 -13.639 1.00 21.83 ? 214 ASP A O 1 ATOM 1491 C CB . ASP A 1 193 ? 23.236 56.429 -10.916 1.00 20.30 ? 214 ASP A CB 1 ATOM 1492 C CG . ASP A 1 193 ? 24.743 56.138 -10.877 1.00 22.98 ? 214 ASP A CG 1 ATOM 1493 O OD1 . ASP A 1 193 ? 25.506 56.868 -11.563 1.00 22.29 ? 214 ASP A OD1 1 ATOM 1494 O OD2 . ASP A 1 193 ? 25.126 55.190 -10.152 1.00 23.45 ? 214 ASP A OD2 1 ATOM 1495 N N . THR A 1 194 ? 23.858 57.300 -13.822 1.00 19.95 ? 215 THR A N 1 ATOM 1496 C CA . THR A 1 194 ? 23.771 56.904 -15.232 1.00 20.92 ? 215 THR A CA 1 ATOM 1497 C C . THR A 1 194 ? 23.667 55.388 -15.384 1.00 20.92 ? 215 THR A C 1 ATOM 1498 O O . THR A 1 194 ? 24.252 54.619 -14.600 1.00 21.13 ? 215 THR A O 1 ATOM 1499 C CB . THR A 1 194 ? 24.963 57.441 -16.041 1.00 21.61 ? 215 THR A CB 1 ATOM 1500 O OG1 . THR A 1 194 ? 26.150 57.130 -15.322 1.00 23.32 ? 215 THR A OG1 1 ATOM 1501 C CG2 . THR A 1 194 ? 24.855 58.952 -16.215 1.00 22.35 ? 215 THR A CG2 1 ATOM 1502 N N . VAL A 1 195 ? 22.879 54.956 -16.375 1.00 19.74 ? 216 VAL A N 1 ATOM 1503 C CA . VAL A 1 195 ? 22.696 53.539 -16.712 1.00 19.88 ? 216 VAL A CA 1 ATOM 1504 C C . VAL A 1 195 ? 22.742 53.420 -18.238 1.00 21.30 ? 216 VAL A C 1 ATOM 1505 O O . VAL A 1 195 ? 22.097 54.194 -18.944 1.00 21.77 ? 216 VAL A O 1 ATOM 1506 C CB . VAL A 1 195 ? 21.313 53.006 -16.216 1.00 19.57 ? 216 VAL A CB 1 ATOM 1507 C CG1 . VAL A 1 195 ? 21.158 51.526 -16.543 1.00 20.18 ? 216 VAL A CG1 1 ATOM 1508 C CG2 . VAL A 1 195 ? 21.157 53.225 -14.717 1.00 20.39 ? 216 VAL A CG2 1 ATOM 1509 N N . ASP A 1 196 ? 23.535 52.481 -18.729 1.00 24.27 ? 217 ASP A N 1 ATOM 1510 C CA . ASP A 1 196 ? 23.638 52.210 -20.156 1.00 25.69 ? 217 ASP A CA 1 ATOM 1511 C C . ASP A 1 196 ? 22.659 51.099 -20.508 1.00 22.89 ? 217 ASP A C 1 ATOM 1512 O O . ASP A 1 196 ? 22.969 49.912 -20.423 1.00 23.08 ? 217 ASP A O 1 ATOM 1513 C CB . ASP A 1 196 ? 25.077 51.808 -20.488 1.00 27.92 ? 217 ASP A CB 1 ATOM 1514 C CG . ASP A 1 196 ? 25.344 51.704 -21.982 1.00 31.99 ? 217 ASP A CG 1 ATOM 1515 O OD1 . ASP A 1 196 ? 24.405 51.718 -22.814 1.00 33.99 ? 217 ASP A OD1 1 ATOM 1516 O OD2 . ASP A 1 196 ? 26.537 51.614 -22.322 1.00 34.39 ? 217 ASP A OD2 1 ATOM 1517 N N . LEU A 1 197 ? 21.441 51.491 -20.888 1.00 25.37 ? 218 LEU A N 1 ATOM 1518 C CA . LEU A 1 197 ? 20.406 50.506 -21.173 1.00 23.97 ? 218 LEU A CA 1 ATOM 1519 C C . LEU A 1 197 ? 20.800 49.545 -22.284 1.00 24.17 ? 218 LEU A C 1 ATOM 1520 O O . LEU A 1 197 ? 20.517 48.350 -22.210 1.00 24.50 ? 218 LEU A O 1 ATOM 1521 C CB . LEU A 1 197 ? 19.085 51.203 -21.523 1.00 22.93 ? 218 LEU A CB 1 ATOM 1522 C CG . LEU A 1 197 ? 18.472 52.145 -20.488 1.00 23.30 ? 218 LEU A CG 1 ATOM 1523 C CD1 . LEU A 1 197 ? 17.049 52.457 -20.941 1.00 24.23 ? 218 LEU A CD1 1 ATOM 1524 C CD2 . LEU A 1 197 ? 18.433 51.503 -19.105 1.00 24.00 ? 218 LEU A CD2 1 ATOM 1525 N N . LYS A 1 198 ? 21.453 50.079 -23.310 1.00 24.83 ? 219 LYS A N 1 ATOM 1526 C CA . LYS A 1 198 ? 21.823 49.299 -24.484 1.00 27.03 ? 219 LYS A CA 1 ATOM 1527 C C . LYS A 1 198 ? 22.764 48.144 -24.133 1.00 27.00 ? 219 LYS A C 1 ATOM 1528 O O . LYS A 1 198 ? 22.706 47.084 -24.752 1.00 28.11 ? 219 LYS A O 1 ATOM 1529 C CB . LYS A 1 198 ? 22.422 50.243 -25.535 1.00 29.05 ? 219 LYS A CB 1 ATOM 1530 C CG . LYS A 1 198 ? 22.754 49.626 -26.880 1.00 31.84 ? 219 LYS A CG 1 ATOM 1531 C CD . LYS A 1 198 ? 22.661 50.660 -28.003 1.00 33.40 ? 219 LYS A CD 1 ATOM 1532 C CE . LYS A 1 198 ? 23.450 51.934 -27.737 1.00 35.99 ? 219 LYS A CE 1 ATOM 1533 N NZ . LYS A 1 198 ? 23.655 52.686 -29.012 1.00 37.07 ? 219 LYS A NZ 1 ATOM 1534 N N . SER A 1 199 ? 23.612 48.334 -23.122 1.00 27.17 ? 220 SER A N 1 ATOM 1535 C CA . SER A 1 199 ? 24.512 47.261 -22.675 1.00 26.66 ? 220 SER A CA 1 ATOM 1536 C C . SER A 1 199 ? 23.898 46.267 -21.682 1.00 27.13 ? 220 SER A C 1 ATOM 1537 O O . SER A 1 199 ? 24.466 45.203 -21.444 1.00 28.56 ? 220 SER A O 1 ATOM 1538 C CB . SER A 1 199 ? 25.802 47.863 -22.092 1.00 28.19 ? 220 SER A CB 1 ATOM 1539 O OG . SER A 1 199 ? 25.550 48.491 -20.843 1.00 33.71 ? 220 SER A OG 1 ATOM 1540 N N . VAL A 1 200 ? 22.732 46.591 -21.112 1.00 23.34 ? 221 VAL A N 1 ATOM 1541 C CA . VAL A 1 200 ? 22.153 45.760 -20.063 1.00 22.62 ? 221 VAL A CA 1 ATOM 1542 C C . VAL A 1 200 ? 20.914 45.025 -20.529 1.00 21.08 ? 221 VAL A C 1 ATOM 1543 O O . VAL A 1 200 ? 20.762 43.827 -20.285 1.00 21.42 ? 221 VAL A O 1 ATOM 1544 C CB . VAL A 1 200 ? 21.841 46.596 -18.792 1.00 22.42 ? 221 VAL A CB 1 ATOM 1545 C CG1 . VAL A 1 200 ? 21.004 45.785 -17.797 1.00 22.58 ? 221 VAL A CG1 1 ATOM 1546 C CG2 . VAL A 1 200 ? 23.152 47.022 -18.147 1.00 23.54 ? 221 VAL A CG2 1 ATOM 1547 N N . LEU A 1 201 ? 20.049 45.749 -21.226 1.00 20.83 ? 222 LEU A N 1 ATOM 1548 C CA . LEU A 1 201 ? 18.703 45.252 -21.547 1.00 20.74 ? 222 LEU A CA 1 ATOM 1549 C C . LEU A 1 201 ? 18.596 44.738 -22.984 1.00 20.65 ? 222 LEU A C 1 ATOM 1550 O O . LEU A 1 201 ? 19.354 45.186 -23.856 1.00 21.29 ? 222 LEU A O 1 ATOM 1551 C CB . LEU A 1 201 ? 17.680 46.361 -21.319 1.00 19.26 ? 222 LEU A CB 1 ATOM 1552 C CG . LEU A 1 201 ? 17.420 46.851 -19.878 1.00 19.84 ? 222 LEU A CG 1 ATOM 1553 C CD1 . LEU A 1 201 ? 16.469 48.047 -19.899 1.00 17.91 ? 222 LEU A CD1 1 ATOM 1554 C CD2 . LEU A 1 201 ? 16.918 45.692 -19.005 1.00 19.65 ? 222 LEU A CD2 1 ATOM 1555 N N . PRO A 1 202 ? 17.686 43.778 -23.232 1.00 20.23 ? 223 PRO A N 1 ATOM 1556 C CA . PRO A 1 202 ? 17.318 43.453 -24.628 1.00 19.33 ? 223 PRO A CA 1 ATOM 1557 C C . PRO A 1 202 ? 16.629 44.658 -25.299 1.00 19.17 ? 223 PRO A C 1 ATOM 1558 O O . PRO A 1 202 ? 16.304 45.645 -24.630 1.00 18.22 ? 223 PRO A O 1 ATOM 1559 C CB . PRO A 1 202 ? 16.356 42.268 -24.469 1.00 20.37 ? 223 PRO A CB 1 ATOM 1560 C CG . PRO A 1 202 ? 15.781 42.431 -23.088 1.00 20.47 ? 223 PRO A CG 1 ATOM 1561 C CD . PRO A 1 202 ? 16.930 42.967 -22.260 1.00 19.83 ? 223 PRO A CD 1 ATOM 1562 N N . GLU A 1 203 ? 16.448 44.599 -26.619 1.00 17.56 ? 224 GLU A N 1 ATOM 1563 C CA . GLU A 1 203 ? 15.860 45.701 -27.350 1.00 18.54 ? 224 GLU A CA 1 ATOM 1564 C C . GLU A 1 203 ? 14.419 45.936 -26.902 1.00 17.78 ? 224 GLU A C 1 ATOM 1565 O O . GLU A 1 203 ? 13.959 47.072 -26.842 1.00 19.05 ? 224 GLU A O 1 ATOM 1566 C CB . GLU A 1 203 ? 15.881 45.407 -28.845 1.00 19.52 ? 224 GLU A CB 1 ATOM 1567 C CG . GLU A 1 203 ? 17.263 45.588 -29.459 1.00 21.68 ? 224 GLU A CG 1 ATOM 1568 C CD . GLU A 1 203 ? 17.239 45.208 -30.921 1.00 25.40 ? 224 GLU A CD 1 ATOM 1569 O OE1 . GLU A 1 203 ? 17.136 46.115 -31.761 1.00 29.45 ? 224 GLU A OE1 1 ATOM 1570 O OE2 . GLU A 1 203 ? 17.258 43.999 -31.213 1.00 29.23 ? 224 GLU A OE2 1 ATOM 1571 N N . TRP A 1 204 ? 13.742 44.847 -26.601 1.00 17.86 ? 225 TRP A N 1 ATOM 1572 C CA . TRP A 1 204 ? 12.365 44.918 -26.075 1.00 18.04 ? 225 TRP A CA 1 ATOM 1573 C C . TRP A 1 204 ? 12.289 44.424 -24.670 1.00 17.79 ? 225 TRP A C 1 ATOM 1574 O O . TRP A 1 204 ? 12.921 43.434 -24.314 1.00 20.11 ? 225 TRP A O 1 ATOM 1575 C CB . TRP A 1 204 ? 11.440 44.109 -26.950 1.00 18.69 ? 225 TRP A CB 1 ATOM 1576 C CG . TRP A 1 204 ? 11.315 44.686 -28.329 1.00 19.64 ? 225 TRP A CG 1 ATOM 1577 C CD1 . TRP A 1 204 ? 12.220 44.591 -29.384 1.00 19.97 ? 225 TRP A CD1 1 ATOM 1578 C CD2 . TRP A 1 204 ? 10.191 45.476 -28.846 1.00 19.73 ? 225 TRP A CD2 1 ATOM 1579 N NE1 . TRP A 1 204 ? 11.758 45.271 -30.489 1.00 19.58 ? 225 TRP A NE1 1 ATOM 1580 C CE2 . TRP A 1 204 ? 10.530 45.810 -30.238 1.00 19.29 ? 225 TRP A CE2 1 ATOM 1581 C CE3 . TRP A 1 204 ? 8.983 45.909 -28.320 1.00 18.77 ? 225 TRP A CE3 1 ATOM 1582 C CZ2 . TRP A 1 204 ? 9.691 46.572 -31.040 1.00 19.63 ? 225 TRP A CZ2 1 ATOM 1583 C CZ3 . TRP A 1 204 ? 8.140 46.671 -29.137 1.00 19.05 ? 225 TRP A CZ3 1 ATOM 1584 C CH2 . TRP A 1 204 ? 8.477 46.987 -30.466 1.00 18.93 ? 225 TRP A CH2 1 ATOM 1585 N N . VAL A 1 205 ? 11.487 45.105 -23.858 1.00 18.00 ? 226 VAL A N 1 ATOM 1586 C CA . VAL A 1 205 ? 11.325 44.724 -22.452 1.00 16.58 ? 226 VAL A CA 1 ATOM 1587 C C . VAL A 1 205 ? 9.855 44.737 -22.027 1.00 16.89 ? 226 VAL A C 1 ATOM 1588 O O . VAL A 1 205 ? 8.998 45.270 -22.731 1.00 18.52 ? 226 VAL A O 1 ATOM 1589 C CB . VAL A 1 205 ? 12.112 45.646 -21.495 1.00 16.81 ? 226 VAL A CB 1 ATOM 1590 C CG1 . VAL A 1 205 ? 13.615 45.648 -21.844 1.00 16.51 ? 226 VAL A CG1 1 ATOM 1591 C CG2 . VAL A 1 205 ? 11.563 47.066 -21.499 1.00 17.10 ? 226 VAL A CG2 1 ATOM 1592 N N . ILE A 1 206 ? 9.597 44.156 -20.862 1.00 17.03 ? 227 ILE A N 1 ATOM 1593 C CA . ILE A 1 206 ? 8.313 44.363 -20.157 1.00 16.99 ? 227 ILE A CA 1 ATOM 1594 C C . ILE A 1 206 ? 8.585 45.330 -19.016 1.00 17.46 ? 227 ILE A C 1 ATOM 1595 O O . ILE A 1 206 ? 9.702 45.357 -18.457 1.00 17.50 ? 227 ILE A O 1 ATOM 1596 C CB . ILE A 1 206 ? 7.686 43.049 -19.662 1.00 17.52 ? 227 ILE A CB 1 ATOM 1597 C CG1 . ILE A 1 206 ? 8.688 42.246 -18.796 1.00 19.29 ? 227 ILE A CG1 1 ATOM 1598 C CG2 . ILE A 1 206 ? 7.216 42.259 -20.875 1.00 19.98 ? 227 ILE A CG2 1 ATOM 1599 C CD1 . ILE A 1 206 ? 8.181 40.957 -18.199 1.00 20.73 ? 227 ILE A CD1 1 ATOM 1600 N N . VAL A 1 207 ? 7.603 46.173 -18.715 1.00 16.10 ? 228 VAL A N 1 ATOM 1601 C CA . VAL A 1 207 ? 7.746 47.136 -17.634 1.00 15.36 ? 228 VAL A CA 1 ATOM 1602 C C . VAL A 1 207 ? 6.687 46.834 -16.574 1.00 15.14 ? 228 VAL A C 1 ATOM 1603 O O . VAL A 1 207 ? 5.566 46.402 -16.914 1.00 14.76 ? 228 VAL A O 1 ATOM 1604 C CB . VAL A 1 207 ? 7.635 48.613 -18.105 1.00 14.92 ? 228 VAL A CB 1 ATOM 1605 C CG1 . VAL A 1 207 ? 8.761 48.959 -19.074 1.00 15.43 ? 228 VAL A CG1 1 ATOM 1606 C CG2 . VAL A 1 207 ? 6.278 48.897 -18.777 1.00 15.44 ? 228 VAL A CG2 1 ATOM 1607 N N . GLY A 1 208 ? 7.042 47.062 -15.308 1.00 15.08 ? 229 GLY A N 1 ATOM 1608 C CA . GLY A 1 208 ? 6.071 46.807 -14.228 1.00 15.16 ? 229 GLY A CA 1 ATOM 1609 C C . GLY A 1 208 ? 6.764 46.757 -12.880 1.00 15.10 ? 229 GLY A C 1 ATOM 1610 O O . GLY A 1 208 ? 7.757 47.478 -12.640 1.00 16.13 ? 229 GLY A O 1 ATOM 1611 N N . PHE A 1 209 ? 6.255 45.875 -12.025 1.00 14.64 ? 230 PHE A N 1 ATOM 1612 C CA . PHE A 1 209 ? 6.619 45.881 -10.607 1.00 14.83 ? 230 PHE A CA 1 ATOM 1613 C C . PHE A 1 209 ? 6.926 44.498 -10.088 1.00 14.50 ? 230 PHE A C 1 ATOM 1614 O O . PHE A 1 209 ? 6.430 43.500 -10.623 1.00 16.18 ? 230 PHE A O 1 ATOM 1615 C CB . PHE A 1 209 ? 5.466 46.477 -9.765 1.00 14.37 ? 230 PHE A CB 1 ATOM 1616 C CG . PHE A 1 209 ? 5.071 47.868 -10.173 1.00 14.55 ? 230 PHE A CG 1 ATOM 1617 C CD1 . PHE A 1 209 ? 5.737 48.974 -9.668 1.00 14.91 ? 230 PHE A CD1 1 ATOM 1618 C CD2 . PHE A 1 209 ? 4.044 48.071 -11.109 1.00 14.43 ? 230 PHE A CD2 1 ATOM 1619 C CE1 . PHE A 1 209 ? 5.409 50.273 -10.059 1.00 14.49 ? 230 PHE A CE1 1 ATOM 1620 C CE2 . PHE A 1 209 ? 3.690 49.358 -11.487 1.00 14.74 ? 230 PHE A CE2 1 ATOM 1621 C CZ . PHE A 1 209 ? 4.353 50.466 -10.983 1.00 14.79 ? 230 PHE A CZ 1 ATOM 1622 N N . THR A 1 210 ? 7.721 44.447 -9.019 1.00 14.62 ? 231 THR A N 1 ATOM 1623 C CA . THR A 1 210 ? 7.932 43.225 -8.255 1.00 14.24 ? 231 THR A CA 1 ATOM 1624 C C . THR A 1 210 ? 7.915 43.616 -6.786 1.00 13.93 ? 231 THR A C 1 ATOM 1625 O O . THR A 1 210 ? 8.201 44.785 -6.457 1.00 13.74 ? 231 THR A O 1 ATOM 1626 C CB . THR A 1 210 ? 9.272 42.552 -8.616 1.00 14.48 ? 231 THR A CB 1 ATOM 1627 O OG1 . THR A 1 210 ? 9.355 41.278 -7.961 1.00 15.12 ? 231 THR A OG1 1 ATOM 1628 C CG2 . THR A 1 210 ? 10.416 43.452 -8.206 1.00 15.35 ? 231 THR A CG2 1 ATOM 1629 N N . ALA A 1 211 ? 7.512 42.683 -5.921 1.00 14.33 ? 232 ALA A N 1 ATOM 1630 C CA . ALA A 1 211 ? 7.496 42.926 -4.461 1.00 15.13 ? 232 ALA A CA 1 ATOM 1631 C C . ALA A 1 211 ? 7.559 41.611 -3.711 1.00 15.21 ? 232 ALA A C 1 ATOM 1632 O O . ALA A 1 211 ? 7.144 40.554 -4.220 1.00 15.31 ? 232 ALA A O 1 ATOM 1633 C CB . ALA A 1 211 ? 6.265 43.725 -4.032 1.00 15.85 ? 232 ALA A CB 1 ATOM 1634 N N . THR A 1 212 ? 8.089 41.681 -2.489 1.00 15.64 ? 233 THR A N 1 ATOM 1635 C CA . THR A 1 212 ? 8.154 40.510 -1.632 1.00 16.31 ? 233 THR A CA 1 ATOM 1636 C C . THR A 1 212 ? 7.862 40.944 -0.200 1.00 17.47 ? 233 THR A C 1 ATOM 1637 O O . THR A 1 212 ? 8.002 42.113 0.159 1.00 17.93 ? 233 THR A O 1 ATOM 1638 C CB . THR A 1 212 ? 9.550 39.856 -1.630 1.00 17.95 ? 233 THR A CB 1 ATOM 1639 O OG1 . THR A 1 212 ? 10.493 40.890 -1.424 1.00 18.14 ? 233 THR A OG1 1 ATOM 1640 C CG2 . THR A 1 212 ? 9.854 39.119 -2.971 1.00 17.59 ? 233 THR A CG2 1 ATOM 1641 N N . THR A 1 213 ? 7.450 39.977 0.605 1.00 17.56 ? 234 THR A N 1 ATOM 1642 C CA . THR A 1 213 ? 7.342 40.188 2.042 1.00 17.90 ? 234 THR A CA 1 ATOM 1643 C C . THR A 1 213 ? 8.428 39.371 2.755 1.00 19.26 ? 234 THR A C 1 ATOM 1644 O O . THR A 1 213 ? 9.050 38.474 2.166 1.00 19.70 ? 234 THR A O 1 ATOM 1645 C CB . THR A 1 213 ? 5.949 39.775 2.577 1.00 18.02 ? 234 THR A CB 1 ATOM 1646 O OG1 . THR A 1 213 ? 5.770 38.367 2.379 1.00 19.15 ? 234 THR A OG1 1 ATOM 1647 C CG2 . THR A 1 213 ? 4.811 40.563 1.877 1.00 18.60 ? 234 THR A CG2 1 ATOM 1648 N N . GLY A 1 214 ? 8.641 39.682 4.028 1.00 19.38 ? 235 GLY A N 1 ATOM 1649 C CA . GLY A 1 214 ? 9.699 39.038 4.797 1.00 21.00 ? 235 GLY A CA 1 ATOM 1650 C C . GLY A 1 214 ? 9.456 37.550 4.962 1.00 20.87 ? 235 GLY A C 1 ATOM 1651 O O . GLY A 1 214 ? 8.314 37.087 4.952 1.00 20.85 ? 235 GLY A O 1 ATOM 1652 N N . ILE A 1 215 ? 10.534 36.788 5.101 1.00 20.57 ? 236 ILE A N 1 ATOM 1653 C CA . ILE A 1 215 ? 10.380 35.347 5.289 1.00 22.58 ? 236 ILE A CA 1 ATOM 1654 C C . ILE A 1 215 ? 10.304 34.960 6.771 1.00 24.99 ? 236 ILE A C 1 ATOM 1655 O O . ILE A 1 215 ? 9.922 33.842 7.096 1.00 26.79 ? 236 ILE A O 1 ATOM 1656 C CB . ILE A 1 215 ? 11.454 34.527 4.541 1.00 22.94 ? 236 ILE A CB 1 ATOM 1657 C CG1 . ILE A 1 215 ? 12.867 34.789 5.095 1.00 23.17 ? 236 ILE A CG1 1 ATOM 1658 C CG2 . ILE A 1 215 ? 11.411 34.830 3.049 1.00 22.34 ? 236 ILE A CG2 1 ATOM 1659 C CD1 . ILE A 1 215 ? 13.887 33.755 4.643 1.00 25.12 ? 236 ILE A CD1 1 ATOM 1660 N N . THR A 1 216 ? 10.651 35.898 7.647 1.00 25.88 ? 237 THR A N 1 ATOM 1661 C CA . THR A 1 216 ? 10.719 35.660 9.094 1.00 26.85 ? 237 THR A CA 1 ATOM 1662 C C . THR A 1 216 ? 9.616 36.433 9.811 1.00 26.11 ? 237 THR A C 1 ATOM 1663 O O . THR A 1 216 ? 9.452 37.635 9.583 1.00 26.40 ? 237 THR A O 1 ATOM 1664 C CB . THR A 1 216 ? 12.076 36.117 9.647 1.00 28.22 ? 237 THR A CB 1 ATOM 1665 O OG1 . THR A 1 216 ? 13.118 35.406 8.974 1.00 30.78 ? 237 THR A OG1 1 ATOM 1666 C CG2 . THR A 1 216 ? 12.179 35.847 11.144 1.00 29.93 ? 237 THR A CG2 1 ATOM 1667 N N . LYS A 1 217 ? 8.872 35.752 10.681 1.00 26.63 ? 238 LYS A N 1 ATOM 1668 C CA . LYS A 1 217 ? 7.828 36.409 11.492 1.00 28.11 ? 238 LYS A CA 1 ATOM 1669 C C . LYS A 1 217 ? 8.323 37.738 12.078 1.00 26.69 ? 238 LYS A C 1 ATOM 1670 O O . LYS A 1 217 ? 9.474 37.830 12.549 1.00 27.20 ? 238 LYS A O 1 ATOM 1671 C CB . LYS A 1 217 ? 7.333 35.469 12.613 1.00 30.41 ? 238 LYS A CB 1 ATOM 1672 C CG . LYS A 1 217 ? 6.103 35.958 13.370 1.00 35.02 ? 238 LYS A CG 1 ATOM 1673 C CD . LYS A 1 217 ? 5.922 35.186 14.676 1.00 37.76 ? 238 LYS A CD 1 ATOM 1674 C CE . LYS A 1 217 ? 4.615 35.554 15.372 1.00 40.45 ? 238 LYS A CE 1 ATOM 1675 N NZ . LYS A 1 217 ? 4.433 34.792 16.643 1.00 41.18 ? 238 LYS A NZ 1 ATOM 1676 N N . GLY A 1 218 ? 7.462 38.758 12.043 1.00 24.59 ? 239 GLY A N 1 ATOM 1677 C CA . GLY A 1 218 ? 7.822 40.114 12.488 1.00 23.77 ? 239 GLY A CA 1 ATOM 1678 C C . GLY A 1 218 ? 8.391 41.048 11.416 1.00 21.64 ? 239 GLY A C 1 ATOM 1679 O O . GLY A 1 218 ? 8.762 42.189 11.711 1.00 22.31 ? 239 GLY A O 1 ATOM 1680 N N . ASN A 1 219 ? 8.463 40.563 10.172 1.00 21.76 ? 240 ASN A N 1 ATOM 1681 C CA . ASN A 1 219 ? 8.958 41.355 9.039 1.00 21.12 ? 240 ASN A CA 1 ATOM 1682 C C . ASN A 1 219 ? 8.028 41.145 7.854 1.00 20.05 ? 240 ASN A C 1 ATOM 1683 O O . ASN A 1 219 ? 8.150 40.157 7.129 1.00 20.39 ? 240 ASN A O 1 ATOM 1684 C CB . ASN A 1 219 ? 10.375 40.922 8.654 1.00 21.26 ? 240 ASN A CB 1 ATOM 1685 C CG . ASN A 1 219 ? 11.336 40.974 9.828 1.00 22.00 ? 240 ASN A CG 1 ATOM 1686 O OD1 . ASN A 1 219 ? 11.910 42.020 10.122 1.00 21.47 ? 240 ASN A OD1 1 ATOM 1687 N ND2 . ASN A 1 219 ? 11.492 39.848 10.516 1.00 22.78 ? 240 ASN A ND2 1 ATOM 1688 N N . VAL A 1 220 ? 7.072 42.052 7.691 1.00 20.93 ? 241 VAL A N 1 ATOM 1689 C CA . VAL A 1 220 ? 5.995 41.837 6.711 1.00 20.30 ? 241 VAL A CA 1 ATOM 1690 C C . VAL A 1 220 ? 5.355 43.174 6.352 1.00 18.09 ? 241 VAL A C 1 ATOM 1691 O O . VAL A 1 220 ? 5.382 44.140 7.133 1.00 19.08 ? 241 VAL A O 1 ATOM 1692 C CB . VAL A 1 220 ? 4.955 40.801 7.241 1.00 20.84 ? 241 VAL A CB 1 ATOM 1693 C CG1 . VAL A 1 220 ? 4.058 41.412 8.306 1.00 21.99 ? 241 VAL A CG1 1 ATOM 1694 C CG2 . VAL A 1 220 ? 4.138 40.181 6.108 1.00 22.06 ? 241 VAL A CG2 1 ATOM 1695 N N . GLU A 1 221 ? 4.766 43.243 5.160 1.00 18.05 ? 242 GLU A N 1 ATOM 1696 C CA . GLU A 1 221 ? 4.136 44.490 4.731 1.00 16.88 ? 242 GLU A CA 1 ATOM 1697 C C . GLU A 1 221 ? 3.184 44.199 3.584 1.00 17.33 ? 242 GLU A C 1 ATOM 1698 O O . GLU A 1 221 ? 3.341 43.191 2.903 1.00 16.48 ? 242 GLU A O 1 ATOM 1699 C CB . GLU A 1 221 ? 5.201 45.502 4.268 1.00 17.32 ? 242 GLU A CB 1 ATOM 1700 C CG . GLU A 1 221 ? 5.795 45.169 2.888 1.00 17.51 ? 242 GLU A CG 1 ATOM 1701 C CD . GLU A 1 221 ? 7.089 45.892 2.592 1.00 17.99 ? 242 GLU A CD 1 ATOM 1702 O OE1 . GLU A 1 221 ? 7.787 46.250 3.555 1.00 19.79 ? 242 GLU A OE1 1 ATOM 1703 O OE2 . GLU A 1 221 ? 7.416 46.130 1.391 1.00 16.70 ? 242 GLU A OE2 1 ATOM 1704 N N . THR A 1 222 ? 2.194 45.071 3.396 1.00 17.37 ? 243 THR A N 1 ATOM 1705 C CA . THR A 1 222 ? 1.501 45.143 2.108 1.00 18.26 ? 243 THR A CA 1 ATOM 1706 C C . THR A 1 222 ? 2.379 45.845 1.068 1.00 17.76 ? 243 THR A C 1 ATOM 1707 O O . THR A 1 222 ? 3.287 46.612 1.407 1.00 16.99 ? 243 THR A O 1 ATOM 1708 C CB . THR A 1 222 ? 0.170 45.900 2.234 1.00 18.22 ? 243 THR A CB 1 ATOM 1709 O OG1 . THR A 1 222 ? 0.415 47.234 2.691 1.00 18.10 ? 243 THR A OG1 1 ATOM 1710 C CG2 . THR A 1 222 ? -0.731 45.180 3.228 1.00 20.26 ? 243 THR A CG2 1 ATOM 1711 N N . ASN A 1 223 ? 2.116 45.576 -0.207 1.00 16.56 ? 244 ASN A N 1 ATOM 1712 C CA . ASN A 1 223 ? 2.847 46.234 -1.295 1.00 16.52 ? 244 ASN A CA 1 ATOM 1713 C C . ASN A 1 223 ? 1.852 46.565 -2.400 1.00 16.62 ? 244 ASN A C 1 ATOM 1714 O O . ASN A 1 223 ? 1.767 45.860 -3.406 1.00 16.25 ? 244 ASN A O 1 ATOM 1715 C CB . ASN A 1 223 ? 3.917 45.291 -1.834 1.00 16.80 ? 244 ASN A CB 1 ATOM 1716 C CG . ASN A 1 223 ? 5.073 45.110 -0.857 1.00 16.10 ? 244 ASN A CG 1 ATOM 1717 O OD1 . ASN A 1 223 ? 5.781 46.062 -0.533 1.00 16.31 ? 244 ASN A OD1 1 ATOM 1718 N ND2 . ASN A 1 223 ? 5.262 43.897 -0.405 1.00 16.56 ? 244 ASN A ND2 1 ATOM 1719 N N . ASP A 1 224 ? 1.111 47.640 -2.187 1.00 16.24 ? 245 ASP A N 1 ATOM 1720 C CA . ASP A 1 224 ? -0.040 47.970 -3.041 1.00 15.30 ? 245 ASP A CA 1 ATOM 1721 C C . ASP A 1 224 ? 0.303 49.128 -3.957 1.00 15.62 ? 245 ASP A C 1 ATOM 1722 O O . ASP A 1 224 ? 0.730 50.184 -3.494 1.00 16.26 ? 245 ASP A O 1 ATOM 1723 C CB . ASP A 1 224 ? -1.246 48.327 -2.158 1.00 15.57 ? 245 ASP A CB 1 ATOM 1724 C CG . ASP A 1 224 ? -1.685 47.180 -1.285 1.00 15.00 ? 245 ASP A CG 1 ATOM 1725 O OD1 . ASP A 1 224 ? -1.593 46.003 -1.701 1.00 16.16 ? 245 ASP A OD1 1 ATOM 1726 O OD2 . ASP A 1 224 ? -2.158 47.475 -0.159 1.00 17.89 ? 245 ASP A OD2 1 ATOM 1727 N N . ILE A 1 225 ? 0.107 48.922 -5.258 1.00 15.45 ? 246 ILE A N 1 ATOM 1728 C CA . ILE A 1 225 ? 0.203 49.999 -6.242 1.00 15.35 ? 246 ILE A CA 1 ATOM 1729 C C . ILE A 1 225 ? -1.193 50.556 -6.488 1.00 15.57 ? 246 ILE A C 1 ATOM 1730 O O . ILE A 1 225 ? -2.109 49.796 -6.775 1.00 15.91 ? 246 ILE A O 1 ATOM 1731 C CB . ILE A 1 225 ? 0.820 49.517 -7.575 1.00 15.83 ? 246 ILE A CB 1 ATOM 1732 C CG1 . ILE A 1 225 ? 2.170 48.784 -7.351 1.00 15.16 ? 246 ILE A CG1 1 ATOM 1733 C CG2 . ILE A 1 225 ? 0.957 50.689 -8.558 1.00 15.04 ? 246 ILE A CG2 1 ATOM 1734 C CD1 . ILE A 1 225 ? 3.251 49.614 -6.672 1.00 16.91 ? 246 ILE A CD1 1 ATOM 1735 N N . LEU A 1 226 ? -1.360 51.871 -6.362 1.00 15.44 ? 247 LEU A N 1 ATOM 1736 C CA . LEU A 1 226 ? -2.710 52.454 -6.427 1.00 16.74 ? 247 LEU A CA 1 ATOM 1737 C C . LEU A 1 226 ? -2.974 53.199 -7.737 1.00 16.43 ? 247 LEU A C 1 ATOM 1738 O O . LEU A 1 226 ? -4.114 53.436 -8.104 1.00 16.69 ? 247 LEU A O 1 ATOM 1739 C CB . LEU A 1 226 ? -2.957 53.378 -5.232 1.00 17.90 ? 247 LEU A CB 1 ATOM 1740 C CG . LEU A 1 226 ? -2.708 52.765 -3.845 1.00 19.78 ? 247 LEU A CG 1 ATOM 1741 C CD1 . LEU A 1 226 ? -2.923 53.803 -2.739 1.00 21.06 ? 247 LEU A CD1 1 ATOM 1742 C CD2 . LEU A 1 226 ? -3.545 51.516 -3.633 1.00 21.31 ? 247 LEU A CD2 1 ATOM 1743 N N . SER A 1 227 ? -1.916 53.593 -8.431 1.00 15.39 ? 248 SER A N 1 ATOM 1744 C CA . SER A 1 227 ? -2.031 54.260 -9.716 1.00 15.37 ? 248 SER A CA 1 ATOM 1745 C C . SER A 1 227 ? -0.678 54.150 -10.417 1.00 16.03 ? 248 SER A C 1 ATOM 1746 O O . SER A 1 227 ? 0.355 53.993 -9.774 1.00 15.11 ? 248 SER A O 1 ATOM 1747 C CB . SER A 1 227 ? -2.435 55.734 -9.581 1.00 16.89 ? 248 SER A CB 1 ATOM 1748 O OG . SER A 1 227 ? -1.403 56.497 -8.948 1.00 19.95 ? 248 SER A OG 1 ATOM 1749 N N . TRP A 1 228 ? -0.702 54.245 -11.737 1.00 15.13 ? 249 TRP A N 1 ATOM 1750 C CA . TRP A 1 228 ? 0.526 54.040 -12.534 1.00 14.67 ? 249 TRP A CA 1 ATOM 1751 C C . TRP A 1 228 ? 0.379 54.740 -13.860 1.00 14.74 ? 249 TRP A C 1 ATOM 1752 O O . TRP A 1 228 ? -0.613 54.548 -14.576 1.00 15.54 ? 249 TRP A O 1 ATOM 1753 C CB . TRP A 1 228 ? 0.753 52.548 -12.749 1.00 14.84 ? 249 TRP A CB 1 ATOM 1754 C CG . TRP A 1 228 ? 2.046 52.161 -13.478 1.00 14.61 ? 249 TRP A CG 1 ATOM 1755 C CD1 . TRP A 1 228 ? 3.250 52.860 -13.545 1.00 15.98 ? 249 TRP A CD1 1 ATOM 1756 C CD2 . TRP A 1 228 ? 2.280 50.916 -14.225 1.00 14.20 ? 249 TRP A CD2 1 ATOM 1757 N NE1 . TRP A 1 228 ? 4.177 52.154 -14.303 1.00 14.06 ? 249 TRP A NE1 1 ATOM 1758 C CE2 . TRP A 1 228 ? 3.671 50.967 -14.702 1.00 14.66 ? 249 TRP A CE2 1 ATOM 1759 C CE3 . TRP A 1 228 ? 1.509 49.780 -14.507 1.00 14.66 ? 249 TRP A CE3 1 ATOM 1760 C CZ2 . TRP A 1 228 ? 4.225 49.933 -15.464 1.00 14.65 ? 249 TRP A CZ2 1 ATOM 1761 C CZ3 . TRP A 1 228 ? 2.077 48.748 -15.265 1.00 14.18 ? 249 TRP A CZ3 1 ATOM 1762 C CH2 . TRP A 1 228 ? 3.420 48.826 -15.729 1.00 14.07 ? 249 TRP A CH2 1 ATOM 1763 N N . SER A 1 229 ? 1.384 55.523 -14.225 1.00 14.99 ? 250 SER A N 1 ATOM 1764 C CA . SER A 1 229 ? 1.433 56.186 -15.538 1.00 14.77 ? 250 SER A CA 1 ATOM 1765 C C . SER A 1 229 ? 2.811 55.888 -16.089 1.00 15.16 ? 250 SER A C 1 ATOM 1766 O O . SER A 1 229 ? 3.785 55.891 -15.330 1.00 16.01 ? 250 SER A O 1 ATOM 1767 C CB . SER A 1 229 ? 1.257 57.703 -15.412 1.00 16.37 ? 250 SER A CB 1 ATOM 1768 O OG . SER A 1 229 ? -0.077 58.062 -14.965 1.00 18.42 ? 250 SER A OG 1 ATOM 1769 N N . PHE A 1 230 ? 2.876 55.578 -17.383 1.00 15.04 ? 251 PHE A N 1 ATOM 1770 C CA . PHE A 1 230 ? 4.165 55.271 -18.048 1.00 14.38 ? 251 PHE A CA 1 ATOM 1771 C C . PHE A 1 230 ? 4.177 55.961 -19.407 1.00 15.22 ? 251 PHE A C 1 ATOM 1772 O O . PHE A 1 230 ? 3.161 56.048 -20.106 1.00 15.71 ? 251 PHE A O 1 ATOM 1773 C CB . PHE A 1 230 ? 4.321 53.737 -18.214 1.00 14.78 ? 251 PHE A CB 1 ATOM 1774 C CG . PHE A 1 230 ? 5.593 53.321 -18.924 1.00 15.53 ? 251 PHE A CG 1 ATOM 1775 C CD1 . PHE A 1 230 ? 6.760 53.100 -18.199 1.00 15.98 ? 251 PHE A CD1 1 ATOM 1776 C CD2 . PHE A 1 230 ? 5.628 53.219 -20.318 1.00 15.30 ? 251 PHE A CD2 1 ATOM 1777 C CE1 . PHE A 1 230 ? 7.932 52.734 -18.840 1.00 15.70 ? 251 PHE A CE1 1 ATOM 1778 C CE2 . PHE A 1 230 ? 6.818 52.881 -20.973 1.00 16.00 ? 251 PHE A CE2 1 ATOM 1779 C CZ . PHE A 1 230 ? 7.969 52.628 -20.223 1.00 16.01 ? 251 PHE A CZ 1 ATOM 1780 N N . ALA A 1 231 ? 5.338 56.451 -19.826 1.00 14.47 ? 252 ALA A N 1 ATOM 1781 C CA . ALA A 1 231 ? 5.434 56.969 -21.182 1.00 15.34 ? 252 ALA A CA 1 ATOM 1782 C C . ALA A 1 231 ? 6.848 56.695 -21.659 1.00 17.16 ? 252 ALA A C 1 ATOM 1783 O O . ALA A 1 231 ? 7.796 56.826 -20.878 1.00 18.01 ? 252 ALA A O 1 ATOM 1784 C CB . ALA A 1 231 ? 5.155 58.456 -21.223 1.00 16.14 ? 252 ALA A CB 1 ATOM 1785 N N . SER A 1 232 ? 6.972 56.322 -22.930 1.00 17.59 ? 253 SER A N 1 ATOM 1786 C CA . SER A 1 232 ? 8.304 56.152 -23.558 1.00 16.99 ? 253 SER A CA 1 ATOM 1787 C C . SER A 1 232 ? 8.321 56.692 -24.989 1.00 17.28 ? 253 SER A C 1 ATOM 1788 O O . SER A 1 232 ? 7.272 56.776 -25.642 1.00 16.47 ? 253 SER A O 1 ATOM 1789 C CB . SER A 1 232 ? 8.743 54.686 -23.522 1.00 18.24 ? 253 SER A CB 1 ATOM 1790 O OG . SER A 1 232 ? 7.855 53.849 -24.255 1.00 20.42 ? 253 SER A OG 1 ATOM 1791 N N . LYS A 1 233 ? 9.510 57.057 -25.481 1.00 17.16 ? 254 LYS A N 1 ATOM 1792 C CA . LYS A 1 233 ? 9.634 57.582 -26.831 1.00 18.89 ? 254 LYS A CA 1 ATOM 1793 C C . LYS A 1 233 ? 10.964 57.094 -27.343 1.00 18.81 ? 254 LYS A C 1 ATOM 1794 O O . LYS A 1 233 ? 11.961 57.209 -26.642 1.00 17.81 ? 254 LYS A O 1 ATOM 1795 C CB . LYS A 1 233 ? 9.639 59.109 -26.803 1.00 21.21 ? 254 LYS A CB 1 ATOM 1796 C CG . LYS A 1 233 ? 9.588 59.795 -28.161 1.00 26.40 ? 254 LYS A CG 1 ATOM 1797 C CD . LYS A 1 233 ? 9.752 61.312 -27.996 1.00 31.04 ? 254 LYS A CD 1 ATOM 1798 C CE . LYS A 1 233 ? 11.231 61.708 -28.038 1.00 33.36 ? 254 LYS A CE 1 ATOM 1799 N NZ . LYS A 1 233 ? 11.524 63.131 -27.669 1.00 37.28 ? 254 LYS A NZ 1 ATOM 1800 N N . LEU A 1 234 ? 10.961 56.546 -28.553 1.00 19.00 ? 255 LEU A N 1 ATOM 1801 C CA . LEU A 1 234 ? 12.187 56.024 -29.196 1.00 19.17 ? 255 LEU A CA 1 ATOM 1802 C C . LEU A 1 234 ? 12.280 56.616 -30.588 1.00 20.83 ? 255 LEU A C 1 ATOM 1803 O O . LEU A 1 234 ? 11.352 56.487 -31.387 1.00 19.68 ? 255 LEU A O 1 ATOM 1804 C CB . LEU A 1 234 ? 12.127 54.497 -29.282 1.00 19.11 ? 255 LEU A CB 1 ATOM 1805 C CG . LEU A 1 234 ? 13.259 53.774 -30.018 1.00 19.20 ? 255 LEU A CG 1 ATOM 1806 C CD1 . LEU A 1 234 ? 14.551 54.010 -29.248 1.00 20.01 ? 255 LEU A CD1 1 ATOM 1807 C CD2 . LEU A 1 234 ? 12.977 52.295 -30.159 1.00 19.65 ? 255 LEU A CD2 1 ATOM 1808 N N . SER A 1 235 ? 13.403 57.254 -30.903 1.00 22.46 ? 256 SER A N 1 ATOM 1809 C CA . SER A 1 235 ? 13.509 57.893 -32.218 1.00 26.24 ? 256 SER A CA 1 ATOM 1810 C C . SER A 1 235 ? 13.703 56.837 -33.324 1.00 28.29 ? 256 SER A C 1 ATOM 1811 O O . SER A 1 235 ? 14.303 55.785 -33.089 1.00 27.42 ? 256 SER A O 1 ATOM 1812 C CB . SER A 1 235 ? 14.602 58.954 -32.210 1.00 29.34 ? 256 SER A CB 1 ATOM 1813 O OG . SER A 1 235 ? 15.835 58.343 -31.931 1.00 32.88 ? 256 SER A OG 1 ATOM 1814 N N . ASP A 1 236 ? 13.129 57.085 -34.513 1.00 30.80 ? 257 ASP A N 1 ATOM 1815 C CA . ASP A 1 236 ? 13.285 56.158 -35.663 1.00 32.42 ? 257 ASP A CA 1 ATOM 1816 C C . ASP A 1 236 ? 14.019 56.776 -36.860 1.00 35.01 ? 257 ASP A C 1 ATOM 1817 O O . ASP A 1 236 ? 14.403 56.063 -37.795 1.00 35.61 ? 257 ASP A O 1 ATOM 1818 C CB . ASP A 1 236 ? 11.941 55.539 -36.108 1.00 34.36 ? 257 ASP A CB 1 ATOM 1819 C CG . ASP A 1 236 ? 10.838 56.579 -36.312 1.00 36.42 ? 257 ASP A CG 1 ATOM 1820 O OD1 . ASP A 1 236 ? 11.130 57.741 -36.704 1.00 38.34 ? 257 ASP A OD1 1 ATOM 1821 O OD2 . ASP A 1 236 ? 9.660 56.233 -36.060 1.00 37.30 ? 257 ASP A OD2 1 ATOM 1822 N N . GLY A 1 237 ? 14.225 58.091 -36.817 1.00 35.26 ? 258 GLY A N 1 ATOM 1823 C CA . GLY A 1 237 ? 14.917 58.808 -37.894 1.00 36.07 ? 258 GLY A CA 1 ATOM 1824 C C . GLY A 1 237 ? 13.935 59.425 -38.867 1.00 37.20 ? 258 GLY A C 1 ATOM 1825 O O . GLY A 1 237 ? 14.345 60.089 -39.828 1.00 36.27 ? 258 GLY A O 1 ATOM 1826 N N . THR A 1 238 ? 12.646 59.183 -38.596 1.00 37.28 ? 259 THR A N 1 ATOM 1827 C CA . THR A 1 238 ? 11.465 59.728 -39.302 1.00 42.62 ? 259 THR A CA 1 ATOM 1828 C C . THR A 1 238 ? 10.840 58.709 -40.256 1.00 43.31 ? 259 THR A C 1 ATOM 1829 O O . THR A 1 238 ? 10.173 57.771 -39.811 1.00 45.17 ? 259 THR A O 1 ATOM 1830 C CB . THR A 1 238 ? 11.693 61.116 -39.958 1.00 44.19 ? 259 THR A CB 1 ATOM 1831 O OG1 . THR A 1 238 ? 11.820 62.101 -38.925 1.00 47.51 ? 259 THR A OG1 1 ATOM 1832 C CG2 . THR A 1 238 ? 10.518 61.505 -40.857 1.00 43.66 ? 259 THR A CG2 1 ATOM 1833 N N . ALA B 1 1 ? -11.598 71.947 -18.021 1.00 49.31 ? 22 ALA B N 1 ATOM 1834 C CA . ALA B 1 1 ? -12.204 73.254 -18.418 1.00 50.17 ? 22 ALA B CA 1 ATOM 1835 C C . ALA B 1 1 ? -11.149 74.260 -18.905 1.00 48.22 ? 22 ALA B C 1 ATOM 1836 O O . ALA B 1 1 ? -11.491 75.260 -19.551 1.00 49.43 ? 22 ALA B O 1 ATOM 1837 C CB . ALA B 1 1 ? -13.031 73.837 -17.273 1.00 51.34 ? 22 ALA B CB 1 ATOM 1838 N N . SER B 1 2 ? -9.879 73.986 -18.590 1.00 42.64 ? 23 SER B N 1 ATOM 1839 C CA . SER B 1 2 ? -8.750 74.798 -19.056 1.00 39.82 ? 23 SER B CA 1 ATOM 1840 C C . SER B 1 2 ? -7.427 74.046 -19.020 1.00 37.96 ? 23 SER B C 1 ATOM 1841 O O . SER B 1 2 ? -7.040 73.521 -17.972 1.00 34.91 ? 23 SER B O 1 ATOM 1842 C CB . SER B 1 2 ? -8.600 76.067 -18.211 1.00 41.35 ? 23 SER B CB 1 ATOM 1843 O OG . SER B 1 2 ? -8.873 77.210 -18.981 1.00 46.23 ? 23 SER B OG 1 ATOM 1844 N N . GLN B 1 3 ? -6.728 74.025 -20.154 1.00 33.72 ? 24 GLN B N 1 ATOM 1845 C CA . GLN B 1 3 ? -5.375 73.469 -20.224 1.00 35.17 ? 24 GLN B CA 1 ATOM 1846 C C . GLN B 1 3 ? -4.473 74.380 -21.032 1.00 32.35 ? 24 GLN B C 1 ATOM 1847 O O . GLN B 1 3 ? -4.902 74.960 -22.023 1.00 32.63 ? 24 GLN B O 1 ATOM 1848 C CB . GLN B 1 3 ? -5.378 72.064 -20.845 1.00 36.32 ? 24 GLN B CB 1 ATOM 1849 C CG . GLN B 1 3 ? -6.007 71.000 -19.959 1.00 42.26 ? 24 GLN B CG 1 ATOM 1850 C CD . GLN B 1 3 ? -6.327 69.722 -20.707 1.00 45.92 ? 24 GLN B CD 1 ATOM 1851 O OE1 . GLN B 1 3 ? -7.491 69.339 -20.826 1.00 51.03 ? 24 GLN B OE1 1 ATOM 1852 N NE2 . GLN B 1 3 ? -5.298 69.059 -21.224 1.00 47.57 ? 24 GLN B NE2 1 ATOM 1853 N N . THR B 1 4 ? -3.224 74.500 -20.605 1.00 30.83 ? 25 THR B N 1 ATOM 1854 C CA . THR B 1 4 ? -2.232 75.270 -21.336 1.00 32.03 ? 25 THR B CA 1 ATOM 1855 C C . THR B 1 4 ? -0.904 74.564 -21.237 1.00 31.99 ? 25 THR B C 1 ATOM 1856 O O . THR B 1 4 ? -0.535 74.089 -20.168 1.00 31.32 ? 25 THR B O 1 ATOM 1857 C CB . THR B 1 4 ? -2.097 76.702 -20.771 1.00 32.99 ? 25 THR B CB 1 ATOM 1858 O OG1 . THR B 1 4 ? -3.319 77.410 -20.985 1.00 35.50 ? 25 THR B OG1 1 ATOM 1859 C CG2 . THR B 1 4 ? -0.962 77.461 -21.453 1.00 34.09 ? 25 THR B CG2 1 ATOM 1860 N N . SER B 1 5 ? -0.191 74.481 -22.356 1.00 30.06 ? 26 SER B N 1 ATOM 1861 C CA . SER B 1 5 ? 1.175 73.996 -22.339 1.00 30.14 ? 26 SER B CA 1 ATOM 1862 C C . SER B 1 5 ? 1.986 74.643 -23.446 1.00 29.38 ? 26 SER B C 1 ATOM 1863 O O . SER B 1 5 ? 1.447 75.043 -24.481 1.00 30.23 ? 26 SER B O 1 ATOM 1864 C CB . SER B 1 5 ? 1.235 72.466 -22.426 1.00 31.83 ? 26 SER B CB 1 ATOM 1865 O OG . SER B 1 5 ? 0.851 72.023 -23.705 1.00 35.24 ? 26 SER B OG 1 ATOM 1866 N N . PHE B 1 6 ? 3.275 74.797 -23.186 1.00 28.38 ? 27 PHE B N 1 ATOM 1867 C CA . PHE B 1 6 ? 4.231 75.202 -24.192 1.00 27.99 ? 27 PHE B CA 1 ATOM 1868 C C . PHE B 1 6 ? 5.563 74.591 -23.852 1.00 27.26 ? 27 PHE B C 1 ATOM 1869 O O . PHE B 1 6 ? 5.821 74.212 -22.705 1.00 27.88 ? 27 PHE B O 1 ATOM 1870 C CB . PHE B 1 6 ? 4.366 76.731 -24.322 1.00 28.95 ? 27 PHE B CB 1 ATOM 1871 C CG . PHE B 1 6 ? 4.612 77.458 -23.022 1.00 27.61 ? 27 PHE B CG 1 ATOM 1872 C CD1 . PHE B 1 6 ? 3.546 78.010 -22.315 1.00 27.99 ? 27 PHE B CD1 1 ATOM 1873 C CD2 . PHE B 1 6 ? 5.903 77.633 -22.529 1.00 28.52 ? 27 PHE B CD2 1 ATOM 1874 C CE1 . PHE B 1 6 ? 3.763 78.706 -21.131 1.00 28.17 ? 27 PHE B CE1 1 ATOM 1875 C CE2 . PHE B 1 6 ? 6.125 78.330 -21.340 1.00 27.01 ? 27 PHE B CE2 1 ATOM 1876 C CZ . PHE B 1 6 ? 5.050 78.864 -20.647 1.00 27.16 ? 27 PHE B CZ 1 ATOM 1877 N N . SER B 1 7 ? 6.407 74.490 -24.861 1.00 27.84 ? 28 SER B N 1 ATOM 1878 C CA . SER B 1 7 ? 7.746 73.996 -24.676 1.00 29.40 ? 28 SER B CA 1 ATOM 1879 C C . SER B 1 7 ? 8.659 74.632 -25.712 1.00 31.55 ? 28 SER B C 1 ATOM 1880 O O . SER B 1 7 ? 8.377 74.583 -26.921 1.00 30.81 ? 28 SER B O 1 ATOM 1881 C CB . SER B 1 7 ? 7.758 72.473 -24.800 1.00 29.01 ? 28 SER B CB 1 ATOM 1882 O OG . SER B 1 7 ? 9.078 71.982 -24.767 1.00 30.76 ? 28 SER B OG 1 ATOM 1883 N N . PHE B 1 8 ? 9.757 75.213 -25.234 1.00 31.33 ? 29 PHE B N 1 ATOM 1884 C CA . PHE B 1 8 ? 10.733 75.872 -26.114 1.00 33.85 ? 29 PHE B CA 1 ATOM 1885 C C . PHE B 1 8 ? 12.129 75.308 -25.895 1.00 35.88 ? 29 PHE B C 1 ATOM 1886 O O . PHE B 1 8 ? 12.598 75.200 -24.757 1.00 35.25 ? 29 PHE B O 1 ATOM 1887 C CB . PHE B 1 8 ? 10.718 77.398 -25.917 1.00 33.88 ? 29 PHE B CB 1 ATOM 1888 C CG . PHE B 1 8 ? 9.344 78.003 -25.965 1.00 35.02 ? 29 PHE B CG 1 ATOM 1889 C CD1 . PHE B 1 8 ? 8.553 77.890 -27.108 1.00 35.15 ? 29 PHE B CD1 1 ATOM 1890 C CD2 . PHE B 1 8 ? 8.833 78.690 -24.871 1.00 35.82 ? 29 PHE B CD2 1 ATOM 1891 C CE1 . PHE B 1 8 ? 7.283 78.443 -27.149 1.00 36.44 ? 29 PHE B CE1 1 ATOM 1892 C CE2 . PHE B 1 8 ? 7.563 79.247 -24.910 1.00 36.29 ? 29 PHE B CE2 1 ATOM 1893 C CZ . PHE B 1 8 ? 6.785 79.121 -26.050 1.00 36.42 ? 29 PHE B CZ 1 ATOM 1894 N N . GLN B 1 9 ? 12.772 74.909 -26.991 1.00 37.27 ? 30 GLN B N 1 ATOM 1895 C CA . GLN B 1 9 ? 14.177 74.508 -26.973 1.00 39.72 ? 30 GLN B CA 1 ATOM 1896 C C . GLN B 1 9 ? 15.057 75.683 -27.396 1.00 40.63 ? 30 GLN B C 1 ATOM 1897 O O . GLN B 1 9 ? 16.264 75.673 -27.164 1.00 41.81 ? 30 GLN B O 1 ATOM 1898 C CB . GLN B 1 9 ? 14.424 73.296 -27.879 1.00 43.64 ? 30 GLN B CB 1 ATOM 1899 C CG . GLN B 1 9 ? 13.878 71.971 -27.344 1.00 48.00 ? 30 GLN B CG 1 ATOM 1900 C CD . GLN B 1 9 ? 14.662 71.424 -26.154 1.00 53.18 ? 30 GLN B CD 1 ATOM 1901 O OE1 . GLN B 1 9 ? 14.077 70.923 -25.190 1.00 56.51 ? 30 GLN B OE1 1 ATOM 1902 N NE2 . GLN B 1 9 ? 15.992 71.510 -26.219 1.00 54.33 ? 30 GLN B NE2 1 ATOM 1903 N N . ARG B 1 10 ? 14.431 76.679 -28.024 1.00 40.79 ? 31 ARG B N 1 ATOM 1904 C CA . ARG B 1 10 ? 15.074 77.925 -28.431 1.00 40.35 ? 31 ARG B CA 1 ATOM 1905 C C . ARG B 1 10 ? 14.090 79.060 -28.200 1.00 39.09 ? 31 ARG B C 1 ATOM 1906 O O . ARG B 1 10 ? 12.885 78.903 -28.426 1.00 39.01 ? 31 ARG B O 1 ATOM 1907 C CB . ARG B 1 10 ? 15.489 77.873 -29.909 1.00 42.53 ? 31 ARG B CB 1 ATOM 1908 C CG . ARG B 1 10 ? 16.592 76.873 -30.244 1.00 44.47 ? 31 ARG B CG 1 ATOM 1909 C CD . ARG B 1 10 ? 17.915 77.211 -29.568 1.00 48.01 ? 31 ARG B CD 1 ATOM 1910 N NE . ARG B 1 10 ? 19.007 76.352 -30.029 1.00 50.98 ? 31 ARG B NE 1 ATOM 1911 C CZ . ARG B 1 10 ? 19.475 75.293 -29.371 1.00 52.49 ? 31 ARG B CZ 1 ATOM 1912 N NH1 . ARG B 1 10 ? 18.958 74.942 -28.202 1.00 55.14 ? 31 ARG B NH1 1 ATOM 1913 N NH2 . ARG B 1 10 ? 20.469 74.581 -29.883 1.00 53.26 ? 31 ARG B NH2 1 ATOM 1914 N N . PHE B 1 11 ? 14.590 80.210 -27.755 1.00 35.83 ? 32 PHE B N 1 ATOM 1915 C CA . PHE B 1 11 ? 13.707 81.311 -27.397 1.00 35.80 ? 32 PHE B CA 1 ATOM 1916 C C . PHE B 1 11 ? 13.647 82.417 -28.448 1.00 37.06 ? 32 PHE B C 1 ATOM 1917 O O . PHE B 1 11 ? 14.584 82.607 -29.227 1.00 35.31 ? 32 PHE B O 1 ATOM 1918 C CB . PHE B 1 11 ? 14.092 81.903 -26.034 1.00 35.56 ? 32 PHE B CB 1 ATOM 1919 C CG . PHE B 1 11 ? 13.896 80.955 -24.883 1.00 34.92 ? 32 PHE B CG 1 ATOM 1920 C CD1 . PHE B 1 11 ? 12.660 80.851 -24.257 1.00 34.35 ? 32 PHE B CD1 1 ATOM 1921 C CD2 . PHE B 1 11 ? 14.949 80.167 -24.429 1.00 34.52 ? 32 PHE B CD2 1 ATOM 1922 C CE1 . PHE B 1 11 ? 12.474 79.973 -23.201 1.00 34.76 ? 32 PHE B CE1 1 ATOM 1923 C CE2 . PHE B 1 11 ? 14.770 79.286 -23.369 1.00 34.46 ? 32 PHE B CE2 1 ATOM 1924 C CZ . PHE B 1 11 ? 13.532 79.195 -22.758 1.00 32.96 ? 32 PHE B CZ 1 ATOM 1925 N N . ASN B 1 12 ? 12.524 83.128 -28.444 1.00 39.13 ? 33 ASN B N 1 ATOM 1926 C CA . ASN B 1 12 ? 12.335 84.336 -29.237 1.00 41.03 ? 33 ASN B CA 1 ATOM 1927 C C . ASN B 1 12 ? 11.526 85.372 -28.461 1.00 41.44 ? 33 ASN B C 1 ATOM 1928 O O . ASN B 1 12 ? 10.642 85.022 -27.670 1.00 42.51 ? 33 ASN B O 1 ATOM 1929 C CB . ASN B 1 12 ? 11.653 84.012 -30.569 1.00 41.36 ? 33 ASN B CB 1 ATOM 1930 C CG . ASN B 1 12 ? 11.714 85.173 -31.544 1.00 41.76 ? 33 ASN B CG 1 ATOM 1931 O OD1 . ASN B 1 12 ? 10.953 86.134 -31.425 1.00 42.10 ? 33 ASN B OD1 1 ATOM 1932 N ND2 . ASN B 1 12 ? 12.626 85.088 -32.509 1.00 45.78 ? 33 ASN B ND2 1 ATOM 1933 N N . GLU B 1 13 ? 11.824 86.647 -28.707 1.00 42.09 ? 34 GLU B N 1 ATOM 1934 C CA . GLU B 1 13 ? 11.218 87.762 -27.976 1.00 41.48 ? 34 GLU B CA 1 ATOM 1935 C C . GLU B 1 13 ? 9.721 87.896 -28.201 1.00 39.31 ? 34 GLU B C 1 ATOM 1936 O O . GLU B 1 13 ? 9.011 88.408 -27.341 1.00 39.45 ? 34 GLU B O 1 ATOM 1937 C CB . GLU B 1 13 ? 11.886 89.093 -28.365 1.00 46.08 ? 34 GLU B CB 1 ATOM 1938 C CG . GLU B 1 13 ? 13.408 89.068 -28.377 1.00 51.54 ? 34 GLU B CG 1 ATOM 1939 C CD . GLU B 1 13 ? 14.026 90.456 -28.475 1.00 55.01 ? 34 GLU B CD 1 ATOM 1940 O OE1 . GLU B 1 13 ? 13.366 91.442 -28.072 1.00 55.67 ? 34 GLU B OE1 1 ATOM 1941 O OE2 . GLU B 1 13 ? 15.179 90.557 -28.950 1.00 55.26 ? 34 GLU B OE2 1 ATOM 1942 N N . THR B 1 14 ? 9.241 87.439 -29.357 1.00 37.30 ? 35 THR B N 1 ATOM 1943 C CA . THR B 1 14 ? 7.883 87.753 -29.793 1.00 36.42 ? 35 THR B CA 1 ATOM 1944 C C . THR B 1 14 ? 6.784 87.278 -28.837 1.00 35.84 ? 35 THR B C 1 ATOM 1945 O O . THR B 1 14 ? 5.770 87.956 -28.685 1.00 35.44 ? 35 THR B O 1 ATOM 1946 C CB . THR B 1 14 ? 7.621 87.250 -31.230 1.00 37.21 ? 35 THR B CB 1 ATOM 1947 O OG1 . THR B 1 14 ? 8.735 87.594 -32.064 1.00 37.10 ? 35 THR B OG1 1 ATOM 1948 C CG2 . THR B 1 14 ? 6.368 87.869 -31.794 1.00 37.56 ? 35 THR B CG2 1 ATOM 1949 N N . ASN B 1 15 ? 6.987 86.129 -28.188 1.00 35.40 ? 36 ASN B N 1 ATOM 1950 C CA . ASN B 1 15 ? 5.981 85.590 -27.255 1.00 35.79 ? 36 ASN B CA 1 ATOM 1951 C C . ASN B 1 15 ? 6.416 85.669 -25.790 1.00 37.09 ? 36 ASN B C 1 ATOM 1952 O O . ASN B 1 15 ? 5.875 84.966 -24.925 1.00 34.93 ? 36 ASN B O 1 ATOM 1953 C CB . ASN B 1 15 ? 5.590 84.149 -27.625 1.00 34.66 ? 36 ASN B CB 1 ATOM 1954 C CG . ASN B 1 15 ? 6.748 83.177 -27.519 1.00 36.57 ? 36 ASN B CG 1 ATOM 1955 O OD1 . ASN B 1 15 ? 7.877 83.554 -27.192 1.00 35.60 ? 36 ASN B OD1 1 ATOM 1956 N ND2 . ASN B 1 15 ? 6.476 81.910 -27.816 1.00 36.08 ? 36 ASN B ND2 1 ATOM 1957 N N . LEU B 1 16 ? 7.408 86.517 -25.529 1.00 37.41 ? 37 LEU B N 1 ATOM 1958 C CA . LEU B 1 16 ? 7.880 86.753 -24.172 1.00 37.40 ? 37 LEU B CA 1 ATOM 1959 C C . LEU B 1 16 ? 7.687 88.214 -23.764 1.00 39.23 ? 37 LEU B C 1 ATOM 1960 O O . LEU B 1 16 ? 7.699 89.114 -24.609 1.00 37.66 ? 37 LEU B O 1 ATOM 1961 C CB . LEU B 1 16 ? 9.352 86.342 -24.038 1.00 36.22 ? 37 LEU B CB 1 ATOM 1962 C CG . LEU B 1 16 ? 9.717 84.879 -24.322 1.00 36.13 ? 37 LEU B CG 1 ATOM 1963 C CD1 . LEU B 1 16 ? 11.217 84.675 -24.179 1.00 35.79 ? 37 LEU B CD1 1 ATOM 1964 C CD2 . LEU B 1 16 ? 8.957 83.932 -23.399 1.00 35.46 ? 37 LEU B CD2 1 ATOM 1965 N N . ILE B 1 17 ? 7.478 88.438 -22.473 1.00 39.76 ? 38 ILE B N 1 ATOM 1966 C CA . ILE B 1 17 ? 7.536 89.776 -21.903 1.00 40.08 ? 38 ILE B CA 1 ATOM 1967 C C . ILE B 1 17 ? 8.872 89.882 -21.190 1.00 41.60 ? 38 ILE B C 1 ATOM 1968 O O . ILE B 1 17 ? 9.076 89.246 -20.152 1.00 43.23 ? 38 ILE B O 1 ATOM 1969 C CB . ILE B 1 17 ? 6.378 90.037 -20.923 1.00 40.95 ? 38 ILE B CB 1 ATOM 1970 C CG1 . ILE B 1 17 ? 5.039 89.905 -21.645 1.00 40.86 ? 38 ILE B CG1 1 ATOM 1971 C CG2 . ILE B 1 17 ? 6.514 91.415 -20.273 1.00 41.17 ? 38 ILE B CG2 1 ATOM 1972 C CD1 . ILE B 1 17 ? 3.852 89.719 -20.721 1.00 42.97 ? 38 ILE B CD1 1 ATOM 1973 N N . LEU B 1 18 ? 9.786 90.663 -21.766 1.00 41.95 ? 39 LEU B N 1 ATOM 1974 C CA . LEU B 1 18 ? 11.125 90.835 -21.211 1.00 42.89 ? 39 LEU B CA 1 ATOM 1975 C C . LEU B 1 18 ? 11.199 92.142 -20.418 1.00 44.76 ? 39 LEU B C 1 ATOM 1976 O O . LEU B 1 18 ? 10.684 93.176 -20.859 1.00 44.46 ? 39 LEU B O 1 ATOM 1977 C CB . LEU B 1 18 ? 12.192 90.802 -22.312 1.00 43.79 ? 39 LEU B CB 1 ATOM 1978 C CG . LEU B 1 18 ? 12.283 89.589 -23.248 1.00 46.93 ? 39 LEU B CG 1 ATOM 1979 C CD1 . LEU B 1 18 ? 13.290 89.829 -24.362 1.00 47.69 ? 39 LEU B CD1 1 ATOM 1980 C CD2 . LEU B 1 18 ? 12.634 88.312 -22.493 1.00 46.21 ? 39 LEU B CD2 1 ATOM 1981 N N . GLN B 1 19 ? 11.815 92.079 -19.240 1.00 44.73 ? 40 GLN B N 1 ATOM 1982 C CA . GLN B 1 19 ? 11.932 93.234 -18.355 1.00 43.82 ? 40 GLN B CA 1 ATOM 1983 C C . GLN B 1 19 ? 13.390 93.471 -17.974 1.00 45.31 ? 40 GLN B C 1 ATOM 1984 O O . GLN B 1 19 ? 14.174 92.525 -17.865 1.00 44.99 ? 40 GLN B O 1 ATOM 1985 C CB . GLN B 1 19 ? 11.069 93.057 -17.104 1.00 42.64 ? 40 GLN B CB 1 ATOM 1986 C CG . GLN B 1 19 ? 9.567 93.069 -17.359 1.00 41.33 ? 40 GLN B CG 1 ATOM 1987 C CD . GLN B 1 19 ? 8.753 92.909 -16.093 1.00 42.00 ? 40 GLN B CD 1 ATOM 1988 O OE1 . GLN B 1 19 ? 9.250 92.412 -15.081 1.00 43.85 ? 40 GLN B OE1 1 ATOM 1989 N NE2 . GLN B 1 19 ? 7.492 93.328 -16.138 1.00 41.41 ? 40 GLN B NE2 1 ATOM 1990 N N . ARG B 1 20 ? 13.747 94.746 -17.800 1.00 46.49 ? 41 ARG B N 1 ATOM 1991 C CA . ARG B 1 20 ? 15.097 95.161 -17.403 1.00 44.76 ? 41 ARG B CA 1 ATOM 1992 C C . ARG B 1 20 ? 16.184 94.539 -18.305 1.00 44.12 ? 41 ARG B C 1 ATOM 1993 O O . ARG B 1 20 ? 16.104 94.676 -19.523 1.00 46.06 ? 41 ARG B O 1 ATOM 1994 C CB . ARG B 1 20 ? 15.312 94.922 -15.898 1.00 45.73 ? 41 ARG B CB 1 ATOM 1995 C CG . ARG B 1 20 ? 16.274 95.880 -15.195 1.00 48.74 ? 41 ARG B CG 1 ATOM 1996 C CD . ARG B 1 20 ? 15.852 97.352 -15.238 1.00 49.08 ? 41 ARG B CD 1 ATOM 1997 N NE . ARG B 1 20 ? 14.467 97.602 -14.823 1.00 47.90 ? 41 ARG B NE 1 ATOM 1998 C CZ . ARG B 1 20 ? 14.054 97.737 -13.563 1.00 47.95 ? 41 ARG B CZ 1 ATOM 1999 N NH1 . ARG B 1 20 ? 14.912 97.632 -12.551 1.00 46.48 ? 41 ARG B NH1 1 ATOM 2000 N NH2 . ARG B 1 20 ? 12.769 97.971 -13.313 1.00 48.55 ? 41 ARG B NH2 1 ATOM 2001 N N . ASP B 1 21 ? 17.174 93.851 -17.735 1.00 42.92 ? 42 ASP B N 1 ATOM 2002 C CA . ASP B 1 21 ? 18.341 93.380 -18.508 1.00 42.81 ? 42 ASP B CA 1 ATOM 2003 C C . ASP B 1 21 ? 18.165 92.086 -19.309 1.00 42.76 ? 42 ASP B C 1 ATOM 2004 O O . ASP B 1 21 ? 19.111 91.624 -19.953 1.00 41.22 ? 42 ASP B O 1 ATOM 2005 C CB . ASP B 1 21 ? 19.561 93.208 -17.598 1.00 45.31 ? 42 ASP B CB 1 ATOM 2006 C CG . ASP B 1 21 ? 20.033 94.512 -16.982 1.00 47.83 ? 42 ASP B CG 1 ATOM 2007 O OD1 . ASP B 1 21 ? 19.253 95.491 -16.958 1.00 48.16 ? 42 ASP B OD1 1 ATOM 2008 O OD2 . ASP B 1 21 ? 21.191 94.537 -16.511 1.00 49.01 ? 42 ASP B OD2 1 ATOM 2009 N N . ALA B 1 22 ? 16.974 91.498 -19.267 1.00 44.46 ? 43 ALA B N 1 ATOM 2010 C CA . ALA B 1 22 ? 16.749 90.198 -19.910 1.00 44.86 ? 43 ALA B CA 1 ATOM 2011 C C . ALA B 1 22 ? 16.702 90.308 -21.433 1.00 44.37 ? 43 ALA B C 1 ATOM 2012 O O . ALA B 1 22 ? 15.921 91.089 -21.982 1.00 44.32 ? 43 ALA B O 1 ATOM 2013 C CB . ALA B 1 22 ? 15.485 89.546 -19.371 1.00 44.15 ? 43 ALA B CB 1 ATOM 2014 N N . THR B 1 23 ? 17.557 89.531 -22.096 1.00 44.33 ? 44 THR B N 1 ATOM 2015 C CA . THR B 1 23 ? 17.630 89.492 -23.560 1.00 46.50 ? 44 THR B CA 1 ATOM 2016 C C . THR B 1 23 ? 17.467 88.063 -24.089 1.00 47.76 ? 44 THR B C 1 ATOM 2017 O O . THR B 1 23 ? 17.696 87.093 -23.365 1.00 46.42 ? 44 THR B O 1 ATOM 2018 C CB . THR B 1 23 ? 18.987 90.014 -24.084 1.00 45.85 ? 44 THR B CB 1 ATOM 2019 O OG1 . THR B 1 23 ? 20.035 89.118 -23.690 1.00 45.77 ? 44 THR B OG1 1 ATOM 2020 C CG2 . THR B 1 23 ? 19.291 91.418 -23.569 1.00 47.26 ? 44 THR B CG2 1 ATOM 2021 N N . VAL B 1 24 ? 17.078 87.944 -25.356 1.00 46.31 ? 45 VAL B N 1 ATOM 2022 C CA . VAL B 1 24 ? 17.196 86.681 -26.074 1.00 45.71 ? 45 VAL B CA 1 ATOM 2023 C C . VAL B 1 24 ? 18.407 86.787 -26.994 1.00 47.68 ? 45 VAL B C 1 ATOM 2024 O O . VAL B 1 24 ? 18.451 87.659 -27.866 1.00 47.39 ? 45 VAL B O 1 ATOM 2025 C CB . VAL B 1 24 ? 15.924 86.358 -26.891 1.00 44.67 ? 45 VAL B CB 1 ATOM 2026 C CG1 . VAL B 1 24 ? 16.124 85.106 -27.735 1.00 43.28 ? 45 VAL B CG1 1 ATOM 2027 C CG2 . VAL B 1 24 ? 14.722 86.196 -25.973 1.00 43.42 ? 45 VAL B CG2 1 ATOM 2028 N N . SER B 1 25 ? 19.390 85.909 -26.797 1.00 47.52 ? 46 SER B N 1 ATOM 2029 C CA . SER B 1 25 ? 20.610 85.937 -27.601 1.00 50.01 ? 46 SER B CA 1 ATOM 2030 C C . SER B 1 25 ? 20.305 85.542 -29.045 1.00 52.85 ? 46 SER B C 1 ATOM 2031 O O . SER B 1 25 ? 19.198 85.085 -29.341 1.00 52.66 ? 46 SER B O 1 ATOM 2032 C CB . SER B 1 25 ? 21.700 85.047 -26.993 1.00 48.71 ? 46 SER B CB 1 ATOM 2033 O OG . SER B 1 25 ? 21.513 83.679 -27.309 1.00 49.28 ? 46 SER B OG 1 ATOM 2034 N N . SER B 1 26 ? 21.268 85.733 -29.944 1.00 54.65 ? 47 SER B N 1 ATOM 2035 C CA . SER B 1 26 ? 21.070 85.360 -31.349 1.00 55.84 ? 47 SER B CA 1 ATOM 2036 C C . SER B 1 26 ? 21.173 83.840 -31.554 1.00 55.85 ? 47 SER B C 1 ATOM 2037 O O . SER B 1 26 ? 20.823 83.322 -32.618 1.00 56.43 ? 47 SER B O 1 ATOM 2038 C CB . SER B 1 26 ? 22.035 86.118 -32.266 1.00 55.15 ? 47 SER B CB 1 ATOM 2039 O OG . SER B 1 26 ? 23.378 85.823 -31.936 1.00 57.05 ? 47 SER B OG 1 ATOM 2040 N N . LYS B 1 27 ? 21.637 83.133 -30.524 1.00 56.11 ? 48 LYS B N 1 ATOM 2041 C CA . LYS B 1 27 ? 21.702 81.668 -30.550 1.00 54.84 ? 48 LYS B CA 1 ATOM 2042 C C . LYS B 1 27 ? 20.483 81.025 -29.867 1.00 51.78 ? 48 LYS B C 1 ATOM 2043 O O . LYS B 1 27 ? 20.402 79.801 -29.729 1.00 53.38 ? 48 LYS B O 1 ATOM 2044 C CB . LYS B 1 27 ? 23.026 81.180 -29.955 1.00 56.50 ? 48 LYS B CB 1 ATOM 2045 C CG . LYS B 1 27 ? 24.225 81.520 -30.836 1.00 60.46 ? 48 LYS B CG 1 ATOM 2046 C CD . LYS B 1 27 ? 25.555 81.191 -30.175 1.00 62.29 ? 48 LYS B CD 1 ATOM 2047 C CE . LYS B 1 27 ? 26.720 81.623 -31.057 1.00 62.68 ? 48 LYS B CE 1 ATOM 2048 N NZ . LYS B 1 27 ? 28.040 81.340 -30.427 1.00 62.44 ? 48 LYS B NZ 1 ATOM 2049 N N . GLY B 1 28 ? 19.536 81.863 -29.455 1.00 49.64 ? 49 GLY B N 1 ATOM 2050 C CA . GLY B 1 28 ? 18.246 81.398 -28.943 1.00 49.88 ? 49 GLY B CA 1 ATOM 2051 C C . GLY B 1 28 ? 18.184 81.156 -27.445 1.00 48.08 ? 49 GLY B C 1 ATOM 2052 O O . GLY B 1 28 ? 17.225 80.560 -26.948 1.00 46.71 ? 49 GLY B O 1 ATOM 2053 N N . GLN B 1 29 ? 19.203 81.624 -26.727 1.00 45.59 ? 50 GLN B N 1 ATOM 2054 C CA . GLN B 1 29 ? 19.240 81.511 -25.270 1.00 44.22 ? 50 GLN B CA 1 ATOM 2055 C C . GLN B 1 29 ? 18.601 82.715 -24.582 1.00 42.96 ? 50 GLN B C 1 ATOM 2056 O O . GLN B 1 29 ? 18.742 83.851 -25.036 1.00 44.65 ? 50 GLN B O 1 ATOM 2057 C CB . GLN B 1 29 ? 20.673 81.328 -24.782 1.00 44.39 ? 50 GLN B CB 1 ATOM 2058 C CG . GLN B 1 29 ? 21.360 80.093 -25.330 1.00 46.21 ? 50 GLN B CG 1 ATOM 2059 C CD . GLN B 1 29 ? 22.768 79.923 -24.801 1.00 47.75 ? 50 GLN B CD 1 ATOM 2060 O OE1 . GLN B 1 29 ? 23.271 80.759 -24.051 1.00 49.41 ? 50 GLN B OE1 1 ATOM 2061 N NE2 . GLN B 1 29 ? 23.414 78.831 -25.188 1.00 47.32 ? 50 GLN B NE2 1 ATOM 2062 N N . LEU B 1 30 ? 17.892 82.450 -23.489 1.00 39.80 ? 51 LEU B N 1 ATOM 2063 C CA . LEU B 1 30 ? 17.310 83.487 -22.662 1.00 39.24 ? 51 LEU B CA 1 ATOM 2064 C C . LEU B 1 30 ? 18.316 83.881 -21.573 1.00 41.98 ? 51 LEU B C 1 ATOM 2065 O O . LEU B 1 30 ? 18.415 83.222 -20.527 1.00 40.90 ? 51 LEU B O 1 ATOM 2066 C CB . LEU B 1 30 ? 15.988 83.003 -22.056 1.00 37.20 ? 51 LEU B CB 1 ATOM 2067 C CG . LEU B 1 30 ? 15.189 83.913 -21.120 1.00 37.64 ? 51 LEU B CG 1 ATOM 2068 C CD1 . LEU B 1 30 ? 14.711 85.184 -21.807 1.00 36.66 ? 51 LEU B CD1 1 ATOM 2069 C CD2 . LEU B 1 30 ? 14.003 83.170 -20.524 1.00 35.79 ? 51 LEU B CD2 1 ATOM 2070 N N . ARG B 1 31 ? 19.075 84.944 -21.840 1.00 41.37 ? 52 ARG B N 1 ATOM 2071 C CA . ARG B 1 31 ? 20.075 85.452 -20.897 1.00 41.70 ? 52 ARG B CA 1 ATOM 2072 C C . ARG B 1 31 ? 19.403 86.469 -19.985 1.00 40.59 ? 52 ARG B C 1 ATOM 2073 O O . ARG B 1 31 ? 19.143 87.610 -20.382 1.00 39.92 ? 52 ARG B O 1 ATOM 2074 C CB . ARG B 1 31 ? 21.275 86.061 -21.636 1.00 42.32 ? 52 ARG B CB 1 ATOM 2075 C CG . ARG B 1 31 ? 21.801 85.210 -22.786 1.00 43.98 ? 52 ARG B CG 1 ATOM 2076 C CD . ARG B 1 31 ? 23.271 85.471 -23.080 1.00 45.97 ? 52 ARG B CD 1 ATOM 2077 N NE . ARG B 1 31 ? 24.130 84.751 -22.142 1.00 47.88 ? 52 ARG B NE 1 ATOM 2078 C CZ . ARG B 1 31 ? 25.435 84.540 -22.299 1.00 48.68 ? 52 ARG B CZ 1 ATOM 2079 N NH1 . ARG B 1 31 ? 26.078 84.996 -23.368 1.00 50.42 ? 52 ARG B NH1 1 ATOM 2080 N NH2 . ARG B 1 31 ? 26.104 83.864 -21.376 1.00 48.23 ? 52 ARG B NH2 1 ATOM 2081 N N . LEU B 1 32 ? 19.089 86.041 -18.764 1.00 38.91 ? 53 LEU B N 1 ATOM 2082 C CA . LEU B 1 32 ? 18.280 86.850 -17.865 1.00 39.76 ? 53 LEU B CA 1 ATOM 2083 C C . LEU B 1 32 ? 19.034 88.066 -17.329 1.00 40.61 ? 53 LEU B C 1 ATOM 2084 O O . LEU B 1 32 ? 18.438 89.107 -17.117 1.00 42.86 ? 53 LEU B O 1 ATOM 2085 C CB . LEU B 1 32 ? 17.740 86.014 -16.710 1.00 38.61 ? 53 LEU B CB 1 ATOM 2086 C CG . LEU B 1 32 ? 16.716 84.919 -17.042 1.00 36.95 ? 53 LEU B CG 1 ATOM 2087 C CD1 . LEU B 1 32 ? 16.622 83.946 -15.880 1.00 35.39 ? 53 LEU B CD1 1 ATOM 2088 C CD2 . LEU B 1 32 ? 15.349 85.496 -17.364 1.00 35.47 ? 53 LEU B CD2 1 ATOM 2089 N N . THR B 1 33 ? 20.335 87.918 -17.113 1.00 41.99 ? 54 THR B N 1 ATOM 2090 C CA . THR B 1 33 ? 21.169 89.031 -16.650 1.00 45.36 ? 54 THR B CA 1 ATOM 2091 C C . THR B 1 33 ? 22.218 89.396 -17.697 1.00 47.36 ? 54 THR B C 1 ATOM 2092 O O . THR B 1 33 ? 22.491 88.618 -18.617 1.00 48.86 ? 54 THR B O 1 ATOM 2093 C CB . THR B 1 33 ? 21.831 88.728 -15.287 1.00 42.89 ? 54 THR B CB 1 ATOM 2094 O OG1 . THR B 1 33 ? 22.521 87.473 -15.341 1.00 42.06 ? 54 THR B OG1 1 ATOM 2095 C CG2 . THR B 1 33 ? 20.781 88.692 -14.193 1.00 41.73 ? 54 THR B CG2 1 ATOM 2096 N N . ASN B 1 34 ? 22.811 90.577 -17.553 1.00 49.79 ? 55 ASN B N 1 ATOM 2097 C CA . ASN B 1 34 ? 23.652 91.125 -18.612 1.00 50.77 ? 55 ASN B CA 1 ATOM 2098 C C . ASN B 1 34 ? 25.023 90.464 -18.753 1.00 50.82 ? 55 ASN B C 1 ATOM 2099 O O . ASN B 1 34 ? 25.674 90.118 -17.764 1.00 52.48 ? 55 ASN B O 1 ATOM 2100 C CB . ASN B 1 34 ? 23.778 92.649 -18.475 1.00 52.35 ? 55 ASN B CB 1 ATOM 2101 C CG . ASN B 1 34 ? 23.730 93.355 -19.820 1.00 53.36 ? 55 ASN B CG 1 ATOM 2102 O OD1 . ASN B 1 34 ? 22.715 93.946 -20.186 1.00 55.23 ? 55 ASN B OD1 1 ATOM 2103 N ND2 . ASN B 1 34 ? 24.817 93.263 -20.578 1.00 50.76 ? 55 ASN B ND2 1 ATOM 2104 N N . VAL B 1 35 ? 25.424 90.268 -20.006 1.00 53.60 ? 56 VAL B N 1 ATOM 2105 C CA . VAL B 1 35 ? 26.776 89.856 -20.378 1.00 56.52 ? 56 VAL B CA 1 ATOM 2106 C C . VAL B 1 35 ? 27.303 90.921 -21.353 1.00 61.75 ? 56 VAL B C 1 ATOM 2107 O O . VAL B 1 35 ? 26.626 91.261 -22.330 1.00 62.39 ? 56 VAL B O 1 ATOM 2108 C CB . VAL B 1 35 ? 26.790 88.458 -21.045 1.00 56.03 ? 56 VAL B CB 1 ATOM 2109 C CG1 . VAL B 1 35 ? 28.212 88.005 -21.345 1.00 55.07 ? 56 VAL B CG1 1 ATOM 2110 C CG2 . VAL B 1 35 ? 26.089 87.428 -20.171 1.00 56.71 ? 56 VAL B CG2 1 ATOM 2111 N N . ASN B 1 36 ? 28.496 91.453 -21.082 1.00 66.37 ? 57 ASN B N 1 ATOM 2112 C CA . ASN B 1 36 ? 29.056 92.570 -21.865 1.00 66.97 ? 57 ASN B CA 1 ATOM 2113 C C . ASN B 1 36 ? 29.305 92.266 -23.347 1.00 68.18 ? 57 ASN B C 1 ATOM 2114 O O . ASN B 1 36 ? 29.622 91.134 -23.717 1.00 69.49 ? 57 ASN B O 1 ATOM 2115 C CB . ASN B 1 36 ? 30.327 93.131 -21.203 1.00 65.72 ? 57 ASN B CB 1 ATOM 2116 C CG . ASN B 1 36 ? 31.454 92.107 -21.093 1.00 64.36 ? 57 ASN B CG 1 ATOM 2117 O OD1 . ASN B 1 36 ? 31.547 91.154 -21.871 1.00 64.49 ? 57 ASN B OD1 1 ATOM 2118 N ND2 . ASN B 1 36 ? 32.335 92.321 -20.124 1.00 65.07 ? 57 ASN B ND2 1 ATOM 2119 N N . GLU B 1 40 ? 31.490 87.920 -20.620 1.00 60.05 ? 61 GLU B N 1 ATOM 2120 C CA . GLU B 1 40 ? 31.689 88.217 -19.204 1.00 59.13 ? 61 GLU B CA 1 ATOM 2121 C C . GLU B 1 40 ? 30.447 88.849 -18.583 1.00 55.81 ? 61 GLU B C 1 ATOM 2122 O O . GLU B 1 40 ? 29.976 89.885 -19.059 1.00 57.19 ? 61 GLU B O 1 ATOM 2123 C CB . GLU B 1 40 ? 32.891 89.150 -19.005 1.00 63.41 ? 61 GLU B CB 1 ATOM 2124 C CG . GLU B 1 40 ? 34.244 88.538 -19.342 1.00 65.94 ? 61 GLU B CG 1 ATOM 2125 C CD . GLU B 1 40 ? 34.741 87.559 -18.293 1.00 68.57 ? 61 GLU B CD 1 ATOM 2126 O OE1 . GLU B 1 40 ? 34.014 87.288 -17.312 1.00 68.52 ? 61 GLU B OE1 1 ATOM 2127 O OE2 . GLU B 1 40 ? 35.873 87.057 -18.451 1.00 70.03 ? 61 GLU B OE2 1 ATOM 2128 N N . PRO B 1 41 ? 29.907 88.232 -17.512 1.00 53.75 ? 62 PRO B N 1 ATOM 2129 C CA . PRO B 1 41 ? 28.757 88.833 -16.835 1.00 52.54 ? 62 PRO B CA 1 ATOM 2130 C C . PRO B 1 41 ? 29.174 90.061 -16.037 1.00 51.79 ? 62 PRO B C 1 ATOM 2131 O O . PRO B 1 41 ? 30.325 90.151 -15.607 1.00 51.66 ? 62 PRO B O 1 ATOM 2132 C CB . PRO B 1 41 ? 28.286 87.726 -15.890 1.00 51.78 ? 62 PRO B CB 1 ATOM 2133 C CG . PRO B 1 41 ? 29.507 86.915 -15.617 1.00 50.62 ? 62 PRO B CG 1 ATOM 2134 C CD . PRO B 1 41 ? 30.338 86.976 -16.869 1.00 52.38 ? 62 PRO B CD 1 ATOM 2135 N N . THR B 1 42 ? 28.241 90.989 -15.846 1.00 53.37 ? 63 THR B N 1 ATOM 2136 C CA . THR B 1 42 ? 28.509 92.240 -15.131 1.00 54.29 ? 63 THR B CA 1 ATOM 2137 C C . THR B 1 42 ? 27.717 92.333 -13.823 1.00 54.58 ? 63 THR B C 1 ATOM 2138 O O . THR B 1 42 ? 26.803 91.542 -13.585 1.00 54.83 ? 63 THR B O 1 ATOM 2139 C CB . THR B 1 42 ? 28.201 93.475 -16.008 1.00 54.03 ? 63 THR B CB 1 ATOM 2140 O OG1 . THR B 1 42 ? 26.821 93.459 -16.397 1.00 52.40 ? 63 THR B OG1 1 ATOM 2141 C CG2 . THR B 1 42 ? 29.092 93.499 -17.253 1.00 54.90 ? 63 THR B CG2 1 ATOM 2142 N N . LEU B 1 43 ? 28.063 93.317 -12.994 1.00 53.00 ? 64 LEU B N 1 ATOM 2143 C CA . LEU B 1 43 ? 27.497 93.462 -11.653 1.00 49.98 ? 64 LEU B CA 1 ATOM 2144 C C . LEU B 1 43 ? 26.200 94.273 -11.653 1.00 49.33 ? 64 LEU B C 1 ATOM 2145 O O . LEU B 1 43 ? 25.883 94.953 -12.630 1.00 48.73 ? 64 LEU B O 1 ATOM 2146 C CB . LEU B 1 43 ? 28.532 94.099 -10.715 1.00 50.95 ? 64 LEU B CB 1 ATOM 2147 C CG . LEU B 1 43 ? 30.005 93.674 -10.838 1.00 52.66 ? 64 LEU B CG 1 ATOM 2148 C CD1 . LEU B 1 43 ? 30.912 94.773 -10.298 1.00 54.75 ? 64 LEU B CD1 1 ATOM 2149 C CD2 . LEU B 1 43 ? 30.303 92.346 -10.147 1.00 52.38 ? 64 LEU B CD2 1 ATOM 2150 N N . SER B 1 44 ? 25.453 94.180 -10.553 1.00 48.98 ? 65 SER B N 1 ATOM 2151 C CA . SER B 1 44 ? 24.200 94.918 -10.346 1.00 49.85 ? 65 SER B CA 1 ATOM 2152 C C . SER B 1 44 ? 23.118 94.709 -11.417 1.00 51.28 ? 65 SER B C 1 ATOM 2153 O O . SER B 1 44 ? 22.247 95.566 -11.599 1.00 53.38 ? 65 SER B O 1 ATOM 2154 C CB . SER B 1 44 ? 24.472 96.418 -10.143 1.00 51.30 ? 65 SER B CB 1 ATOM 2155 O OG . SER B 1 44 ? 24.923 96.684 -8.830 1.00 52.15 ? 65 SER B OG 1 ATOM 2156 N N . SER B 1 45 ? 23.156 93.566 -12.103 1.00 50.86 ? 66 SER B N 1 ATOM 2157 C CA . SER B 1 45 ? 22.152 93.247 -13.127 1.00 47.66 ? 66 SER B CA 1 ATOM 2158 C C . SER B 1 45 ? 20.888 92.609 -12.555 1.00 46.65 ? 66 SER B C 1 ATOM 2159 O O . SER B 1 45 ? 20.948 91.813 -11.616 1.00 43.90 ? 66 SER B O 1 ATOM 2160 C CB . SER B 1 45 ? 22.735 92.345 -14.215 1.00 48.90 ? 66 SER B CB 1 ATOM 2161 O OG . SER B 1 45 ? 21.796 92.168 -15.263 1.00 44.97 ? 66 SER B OG 1 ATOM 2162 N N . LEU B 1 46 ? 19.749 92.989 -13.131 1.00 45.58 ? 67 LEU B N 1 ATOM 2163 C CA . LEU B 1 46 ? 18.453 92.381 -12.851 1.00 45.55 ? 67 LEU B CA 1 ATOM 2164 C C . LEU B 1 46 ? 17.734 92.153 -14.184 1.00 47.11 ? 67 LEU B C 1 ATOM 2165 O O . LEU B 1 46 ? 17.718 93.033 -15.044 1.00 43.92 ? 67 LEU B O 1 ATOM 2166 C CB . LEU B 1 46 ? 17.618 93.272 -11.917 1.00 44.75 ? 67 LEU B CB 1 ATOM 2167 C CG . LEU B 1 46 ? 16.094 93.106 -11.806 1.00 45.35 ? 67 LEU B CG 1 ATOM 2168 C CD1 . LEU B 1 46 ? 15.693 91.703 -11.366 1.00 45.80 ? 67 LEU B CD1 1 ATOM 2169 C CD2 . LEU B 1 46 ? 15.504 94.139 -10.856 1.00 47.01 ? 67 LEU B CD2 1 ATOM 2170 N N . GLY B 1 47 ? 17.163 90.964 -14.359 1.00 45.83 ? 68 GLY B N 1 ATOM 2171 C CA . GLY B 1 47 ? 16.376 90.664 -15.551 1.00 44.85 ? 68 GLY B CA 1 ATOM 2172 C C . GLY B 1 47 ? 15.255 89.697 -15.239 1.00 44.82 ? 68 GLY B C 1 ATOM 2173 O O . GLY B 1 47 ? 15.428 88.781 -14.434 1.00 44.08 ? 68 GLY B O 1 ATOM 2174 N N . ARG B 1 48 ? 14.103 89.927 -15.862 1.00 42.58 ? 69 ARG B N 1 ATOM 2175 C CA . ARG B 1 48 ? 12.948 89.045 -15.743 1.00 39.99 ? 69 ARG B CA 1 ATOM 2176 C C . ARG B 1 48 ? 12.423 88.695 -17.134 1.00 41.16 ? 69 ARG B C 1 ATOM 2177 O O . ARG B 1 48 ? 12.581 89.478 -18.080 1.00 39.42 ? 69 ARG B O 1 ATOM 2178 C CB . ARG B 1 48 ? 11.830 89.711 -14.953 1.00 38.66 ? 69 ARG B CB 1 ATOM 2179 C CG . ARG B 1 48 ? 12.128 90.044 -13.498 1.00 38.29 ? 69 ARG B CG 1 ATOM 2180 C CD . ARG B 1 48 ? 11.088 91.043 -13.062 1.00 36.88 ? 69 ARG B CD 1 ATOM 2181 N NE . ARG B 1 48 ? 10.528 90.784 -11.752 1.00 38.07 ? 69 ARG B NE 1 ATOM 2182 C CZ . ARG B 1 48 ? 9.283 91.087 -11.405 1.00 37.89 ? 69 ARG B CZ 1 ATOM 2183 N NH1 . ARG B 1 48 ? 8.445 91.633 -12.280 1.00 36.64 ? 69 ARG B NH1 1 ATOM 2184 N NH2 . ARG B 1 48 ? 8.867 90.818 -10.179 1.00 39.26 ? 69 ARG B NH2 1 ATOM 2185 N N . ALA B 1 49 ? 11.799 87.522 -17.257 1.00 38.59 ? 70 ALA B N 1 ATOM 2186 C CA . ALA B 1 49 ? 11.191 87.086 -18.519 1.00 37.40 ? 70 ALA B CA 1 ATOM 2187 C C . ALA B 1 49 ? 9.948 86.248 -18.261 1.00 37.20 ? 70 ALA B C 1 ATOM 2188 O O . ALA B 1 49 ? 9.964 85.346 -17.422 1.00 35.98 ? 70 ALA B O 1 ATOM 2189 C CB . ALA B 1 49 ? 12.189 86.308 -19.345 1.00 36.47 ? 70 ALA B CB 1 ATOM 2190 N N . PHE B 1 50 ? 8.872 86.556 -18.979 1.00 36.08 ? 71 PHE B N 1 ATOM 2191 C CA . PHE B 1 50 ? 7.593 85.876 -18.789 1.00 36.99 ? 71 PHE B CA 1 ATOM 2192 C C . PHE B 1 50 ? 6.981 85.408 -20.109 1.00 37.71 ? 71 PHE B C 1 ATOM 2193 O O . PHE B 1 50 ? 7.240 85.985 -21.164 1.00 35.81 ? 71 PHE B O 1 ATOM 2194 C CB . PHE B 1 50 ? 6.596 86.785 -18.062 1.00 38.61 ? 71 PHE B CB 1 ATOM 2195 C CG . PHE B 1 50 ? 7.103 87.318 -16.748 1.00 40.72 ? 71 PHE B CG 1 ATOM 2196 C CD1 . PHE B 1 50 ? 6.858 86.633 -15.561 1.00 40.83 ? 71 PHE B CD1 1 ATOM 2197 C CD2 . PHE B 1 50 ? 7.836 88.504 -16.699 1.00 40.15 ? 71 PHE B CD2 1 ATOM 2198 C CE1 . PHE B 1 50 ? 7.327 87.125 -14.347 1.00 41.28 ? 71 PHE B CE1 1 ATOM 2199 C CE2 . PHE B 1 50 ? 8.310 88.995 -15.491 1.00 41.06 ? 71 PHE B CE2 1 ATOM 2200 C CZ . PHE B 1 50 ? 8.055 88.304 -14.314 1.00 40.14 ? 71 PHE B CZ 1 ATOM 2201 N N . TYR B 1 51 ? 6.176 84.351 -20.043 1.00 36.00 ? 72 TYR B N 1 ATOM 2202 C CA . TYR B 1 51 ? 5.334 83.968 -21.171 1.00 34.82 ? 72 TYR B CA 1 ATOM 2203 C C . TYR B 1 51 ? 4.293 85.068 -21.382 1.00 36.47 ? 72 TYR B C 1 ATOM 2204 O O . TYR B 1 51 ? 3.764 85.611 -20.407 1.00 35.47 ? 72 TYR B O 1 ATOM 2205 C CB . TYR B 1 51 ? 4.662 82.617 -20.889 1.00 33.68 ? 72 TYR B CB 1 ATOM 2206 C CG . TYR B 1 51 ? 3.812 82.078 -22.019 1.00 32.53 ? 72 TYR B CG 1 ATOM 2207 C CD1 . TYR B 1 51 ? 4.364 81.798 -23.271 1.00 33.73 ? 72 TYR B CD1 1 ATOM 2208 C CD2 . TYR B 1 51 ? 2.458 81.833 -21.827 1.00 34.13 ? 72 TYR B CD2 1 ATOM 2209 C CE1 . TYR B 1 51 ? 3.579 81.292 -24.305 1.00 34.34 ? 72 TYR B CE1 1 ATOM 2210 C CE2 . TYR B 1 51 ? 1.669 81.327 -22.849 1.00 35.46 ? 72 TYR B CE2 1 ATOM 2211 C CZ . TYR B 1 51 ? 2.235 81.063 -24.082 1.00 34.77 ? 72 TYR B CZ 1 ATOM 2212 O OH . TYR B 1 51 ? 1.432 80.561 -25.076 1.00 38.84 ? 72 TYR B OH 1 ATOM 2213 N N . SER B 1 52 ? 4.001 85.410 -22.639 1.00 38.26 ? 73 SER B N 1 ATOM 2214 C CA . SER B 1 52 ? 3.137 86.574 -22.916 1.00 39.62 ? 73 SER B CA 1 ATOM 2215 C C . SER B 1 52 ? 1.636 86.411 -22.624 1.00 39.46 ? 73 SER B C 1 ATOM 2216 O O . SER B 1 52 ? 0.924 87.404 -22.529 1.00 41.81 ? 73 SER B O 1 ATOM 2217 C CB . SER B 1 52 ? 3.370 87.132 -24.330 1.00 41.49 ? 73 SER B CB 1 ATOM 2218 O OG . SER B 1 52 ? 3.170 86.140 -25.309 1.00 45.81 ? 73 SER B OG 1 ATOM 2219 N N . ALA B 1 53 ? 1.156 85.179 -22.462 1.00 37.45 ? 74 ALA B N 1 ATOM 2220 C CA . ALA B 1 53 ? -0.249 84.946 -22.121 1.00 38.46 ? 74 ALA B CA 1 ATOM 2221 C C . ALA B 1 53 ? -0.440 84.675 -20.622 1.00 38.76 ? 74 ALA B C 1 ATOM 2222 O O . ALA B 1 53 ? 0.301 83.880 -20.043 1.00 37.51 ? 74 ALA B O 1 ATOM 2223 C CB . ALA B 1 53 ? -0.818 83.797 -22.945 1.00 37.94 ? 74 ALA B CB 1 ATOM 2224 N N . PRO B 1 54 ? -1.438 85.331 -19.996 1.00 39.15 ? 75 PRO B N 1 ATOM 2225 C CA . PRO B 1 54 ? -1.736 85.069 -18.585 1.00 38.52 ? 75 PRO B CA 1 ATOM 2226 C C . PRO B 1 54 ? -2.243 83.640 -18.380 1.00 38.70 ? 75 PRO B C 1 ATOM 2227 O O . PRO B 1 54 ? -2.956 83.109 -19.236 1.00 37.51 ? 75 PRO B O 1 ATOM 2228 C CB . PRO B 1 54 ? -2.861 86.065 -18.266 1.00 39.49 ? 75 PRO B CB 1 ATOM 2229 C CG . PRO B 1 54 ? -2.800 87.095 -19.344 1.00 40.93 ? 75 PRO B CG 1 ATOM 2230 C CD . PRO B 1 54 ? -2.337 86.354 -20.560 1.00 40.04 ? 75 PRO B CD 1 ATOM 2231 N N . ILE B 1 55 ? -1.872 83.042 -17.249 1.00 36.20 ? 76 ILE B N 1 ATOM 2232 C CA . ILE B 1 55 ? -2.277 81.687 -16.893 1.00 34.87 ? 76 ILE B CA 1 ATOM 2233 C C . ILE B 1 55 ? -3.227 81.756 -15.712 1.00 35.01 ? 76 ILE B C 1 ATOM 2234 O O . ILE B 1 55 ? -2.930 82.399 -14.697 1.00 36.34 ? 76 ILE B O 1 ATOM 2235 C CB . ILE B 1 55 ? -1.060 80.814 -16.504 1.00 34.63 ? 76 ILE B CB 1 ATOM 2236 C CG1 . ILE B 1 55 ? 0.047 80.865 -17.578 1.00 35.12 ? 76 ILE B CG1 1 ATOM 2237 C CG2 . ILE B 1 55 ? -1.487 79.387 -16.179 1.00 34.77 ? 76 ILE B CG2 1 ATOM 2238 C CD1 . ILE B 1 55 ? -0.347 80.360 -18.953 1.00 34.27 ? 76 ILE B CD1 1 ATOM 2239 N N . GLN B 1 56 ? -4.371 81.101 -15.842 1.00 32.98 ? 77 GLN B N 1 ATOM 2240 C CA . GLN B 1 56 ? -5.331 81.050 -14.763 1.00 34.51 ? 77 GLN B CA 1 ATOM 2241 C C . GLN B 1 56 ? -4.931 79.953 -13.775 1.00 35.79 ? 77 GLN B C 1 ATOM 2242 O O . GLN B 1 56 ? -4.887 78.778 -14.144 1.00 32.26 ? 77 GLN B O 1 ATOM 2243 C CB . GLN B 1 56 ? -6.741 80.800 -15.293 1.00 34.48 ? 77 GLN B CB 1 ATOM 2244 C CG . GLN B 1 56 ? -7.798 80.995 -14.214 1.00 35.65 ? 77 GLN B CG 1 ATOM 2245 C CD . GLN B 1 56 ? -9.225 80.803 -14.686 1.00 37.14 ? 77 GLN B CD 1 ATOM 2246 O OE1 . GLN B 1 56 ? -9.486 80.443 -15.834 1.00 38.27 ? 77 GLN B OE1 1 ATOM 2247 N NE2 . GLN B 1 56 ? -10.164 81.030 -13.780 1.00 37.44 ? 77 GLN B NE2 1 ATOM 2248 N N . ILE B 1 57 ? -4.639 80.334 -12.529 1.00 35.70 ? 78 ILE B N 1 ATOM 2249 C CA . ILE B 1 57 ? -4.245 79.339 -11.519 1.00 37.11 ? 78 ILE B CA 1 ATOM 2250 C C . ILE B 1 57 ? -5.348 78.955 -10.538 1.00 35.91 ? 78 ILE B C 1 ATOM 2251 O O . ILE B 1 57 ? -5.309 77.876 -9.955 1.00 36.17 ? 78 ILE B O 1 ATOM 2252 C CB . ILE B 1 57 ? -2.922 79.667 -10.781 1.00 38.79 ? 78 ILE B CB 1 ATOM 2253 C CG1 . ILE B 1 57 ? -2.859 81.129 -10.372 1.00 40.66 ? 78 ILE B CG1 1 ATOM 2254 C CG2 . ILE B 1 57 ? -1.712 79.254 -11.613 1.00 40.41 ? 78 ILE B CG2 1 ATOM 2255 C CD1 . ILE B 1 57 ? -3.299 81.360 -8.952 1.00 43.53 ? 78 ILE B CD1 1 ATOM 2256 N N . TRP B 1 58 ? -6.334 79.830 -10.352 1.00 37.17 ? 79 TRP B N 1 ATOM 2257 C CA . TRP B 1 58 ? -7.559 79.447 -9.644 1.00 37.06 ? 79 TRP B CA 1 ATOM 2258 C C . TRP B 1 58 ? -8.740 80.281 -10.051 1.00 39.28 ? 79 TRP B C 1 ATOM 2259 O O . TRP B 1 58 ? -8.588 81.269 -10.784 1.00 37.71 ? 79 TRP B O 1 ATOM 2260 C CB . TRP B 1 58 ? -7.367 79.409 -8.118 1.00 38.47 ? 79 TRP B CB 1 ATOM 2261 C CG . TRP B 1 58 ? -7.238 80.753 -7.443 1.00 38.87 ? 79 TRP B CG 1 ATOM 2262 C CD1 . TRP B 1 58 ? -6.137 81.606 -7.442 1.00 38.46 ? 79 TRP B CD1 1 ATOM 2263 C CD2 . TRP B 1 58 ? -8.243 81.429 -6.615 1.00 39.70 ? 79 TRP B CD2 1 ATOM 2264 N NE1 . TRP B 1 58 ? -6.389 82.736 -6.708 1.00 38.88 ? 79 TRP B NE1 1 ATOM 2265 C CE2 . TRP B 1 58 ? -7.635 82.695 -6.184 1.00 39.95 ? 79 TRP B CE2 1 ATOM 2266 C CE3 . TRP B 1 58 ? -9.540 81.129 -6.209 1.00 41.17 ? 79 TRP B CE3 1 ATOM 2267 C CZ2 . TRP B 1 58 ? -8.318 83.604 -5.376 1.00 40.91 ? 79 TRP B CZ2 1 ATOM 2268 C CZ3 . TRP B 1 58 ? -10.215 82.053 -5.395 1.00 41.82 ? 79 TRP B CZ3 1 ATOM 2269 C CH2 . TRP B 1 58 ? -9.615 83.259 -4.992 1.00 39.85 ? 79 TRP B CH2 1 ATOM 2270 N N . ASP B 1 59 ? -9.923 79.871 -9.595 1.00 40.05 ? 80 ASP B N 1 ATOM 2271 C CA . ASP B 1 59 ? -11.183 80.478 -9.998 1.00 43.70 ? 80 ASP B CA 1 ATOM 2272 C C . ASP B 1 59 ? -12.106 80.605 -8.793 1.00 45.76 ? 80 ASP B C 1 ATOM 2273 O O . ASP B 1 59 ? -12.459 79.604 -8.164 1.00 45.98 ? 80 ASP B O 1 ATOM 2274 C CB . ASP B 1 59 ? -11.846 79.622 -11.079 1.00 44.83 ? 80 ASP B CB 1 ATOM 2275 C CG . ASP B 1 59 ? -13.039 80.306 -11.719 1.00 47.37 ? 80 ASP B CG 1 ATOM 2276 O OD1 . ASP B 1 59 ? -14.149 80.215 -11.156 1.00 47.45 ? 80 ASP B OD1 1 ATOM 2277 O OD2 . ASP B 1 59 ? -12.864 80.918 -12.792 1.00 48.73 ? 80 ASP B OD2 1 ATOM 2278 N N . ASN B 1 60 ? -12.510 81.836 -8.493 1.00 48.30 ? 81 ASN B N 1 ATOM 2279 C CA . ASN B 1 60 ? -13.308 82.120 -7.300 1.00 51.32 ? 81 ASN B CA 1 ATOM 2280 C C . ASN B 1 60 ? -14.771 81.671 -7.372 1.00 50.55 ? 81 ASN B C 1 ATOM 2281 O O . ASN B 1 60 ? -15.420 81.504 -6.340 1.00 51.44 ? 81 ASN B O 1 ATOM 2282 C CB . ASN B 1 60 ? -13.216 83.606 -6.929 1.00 54.58 ? 81 ASN B CB 1 ATOM 2283 C CG . ASN B 1 60 ? -13.571 83.871 -5.476 1.00 58.28 ? 81 ASN B CG 1 ATOM 2284 O OD1 . ASN B 1 60 ? -13.274 83.062 -4.595 1.00 59.35 ? 81 ASN B OD1 1 ATOM 2285 N ND2 . ASN B 1 60 ? -14.205 85.013 -5.217 1.00 61.46 ? 81 ASN B ND2 1 ATOM 2286 N N . THR B 1 61 ? -15.282 81.460 -8.583 1.00 49.14 ? 82 THR B N 1 ATOM 2287 C CA . THR B 1 61 ? -16.668 81.011 -8.766 1.00 49.36 ? 82 THR B CA 1 ATOM 2288 C C . THR B 1 61 ? -16.819 79.513 -8.475 1.00 49.30 ? 82 THR B C 1 ATOM 2289 O O . THR B 1 61 ? -17.835 79.078 -7.932 1.00 49.29 ? 82 THR B O 1 ATOM 2290 C CB . THR B 1 61 ? -17.194 81.333 -10.187 1.00 50.07 ? 82 THR B CB 1 ATOM 2291 O OG1 . THR B 1 61 ? -16.834 82.673 -10.540 1.00 53.86 ? 82 THR B OG1 1 ATOM 2292 C CG2 . THR B 1 61 ? -18.708 81.191 -10.265 1.00 50.91 ? 82 THR B CG2 1 ATOM 2293 N N . THR B 1 62 ? -15.802 78.733 -8.837 1.00 47.58 ? 83 THR B N 1 ATOM 2294 C CA . THR B 1 62 ? -15.846 77.277 -8.679 1.00 45.76 ? 83 THR B CA 1 ATOM 2295 C C . THR B 1 62 ? -15.048 76.803 -7.462 1.00 44.86 ? 83 THR B C 1 ATOM 2296 O O . THR B 1 62 ? -15.337 75.745 -6.896 1.00 45.76 ? 83 THR B O 1 ATOM 2297 C CB . THR B 1 62 ? -15.318 76.549 -9.941 1.00 43.79 ? 83 THR B CB 1 ATOM 2298 O OG1 . THR B 1 62 ? -13.952 76.917 -10.172 1.00 41.52 ? 83 THR B OG1 1 ATOM 2299 C CG2 . THR B 1 62 ? -16.147 76.916 -11.174 1.00 44.19 ? 83 THR B CG2 1 ATOM 2300 N N . GLY B 1 63 ? -14.042 77.584 -7.070 1.00 44.01 ? 84 GLY B N 1 ATOM 2301 C CA . GLY B 1 63 ? -13.128 77.190 -5.994 1.00 45.07 ? 84 GLY B CA 1 ATOM 2302 C C . GLY B 1 63 ? -11.920 76.396 -6.484 1.00 44.30 ? 84 GLY B C 1 ATOM 2303 O O . GLY B 1 63 ? -10.936 76.238 -5.756 1.00 43.64 ? 84 GLY B O 1 ATOM 2304 N N . ALA B 1 64 ? -11.995 75.909 -7.724 1.00 42.08 ? 85 ALA B N 1 ATOM 2305 C CA . ALA B 1 64 ? -10.938 75.091 -8.326 1.00 39.09 ? 85 ALA B CA 1 ATOM 2306 C C . ALA B 1 64 ? -9.588 75.794 -8.365 1.00 37.80 ? 85 ALA B C 1 ATOM 2307 O O . ALA B 1 64 ? -9.505 77.004 -8.600 1.00 37.75 ? 85 ALA B O 1 ATOM 2308 C CB . ALA B 1 64 ? -11.346 74.657 -9.731 1.00 40.52 ? 85 ALA B CB 1 ATOM 2309 N N . VAL B 1 65 ? -8.531 75.021 -8.130 1.00 34.11 ? 86 VAL B N 1 ATOM 2310 C CA . VAL B 1 65 ? -7.156 75.514 -8.181 1.00 32.40 ? 86 VAL B CA 1 ATOM 2311 C C . VAL B 1 65 ? -6.415 74.658 -9.201 1.00 31.30 ? 86 VAL B C 1 ATOM 2312 O O . VAL B 1 65 ? -6.653 73.452 -9.285 1.00 31.87 ? 86 VAL B O 1 ATOM 2313 C CB . VAL B 1 65 ? -6.456 75.416 -6.802 1.00 32.23 ? 86 VAL B CB 1 ATOM 2314 C CG1 . VAL B 1 65 ? -5.044 75.979 -6.867 1.00 31.09 ? 86 VAL B CG1 1 ATOM 2315 C CG2 . VAL B 1 65 ? -7.264 76.143 -5.728 1.00 32.22 ? 86 VAL B CG2 1 ATOM 2316 N N . ALA B 1 66 ? -5.529 75.285 -9.967 1.00 30.84 ? 87 ALA B N 1 ATOM 2317 C CA . ALA B 1 66 ? -4.797 74.595 -11.026 1.00 29.85 ? 87 ALA B CA 1 ATOM 2318 C C . ALA B 1 66 ? -3.725 73.684 -10.460 1.00 29.91 ? 87 ALA B C 1 ATOM 2319 O O . ALA B 1 66 ? -3.159 73.958 -9.398 1.00 29.67 ? 87 ALA B O 1 ATOM 2320 C CB . ALA B 1 66 ? -4.153 75.596 -11.971 1.00 30.26 ? 87 ALA B CB 1 ATOM 2321 N N . SER B 1 67 ? -3.469 72.588 -11.169 1.00 29.08 ? 88 SER B N 1 ATOM 2322 C CA . SER B 1 67 ? -2.213 71.866 -11.023 1.00 27.65 ? 88 SER B CA 1 ATOM 2323 C C . SER B 1 67 ? -1.326 72.292 -12.187 1.00 26.80 ? 88 SER B C 1 ATOM 2324 O O . SER B 1 67 ? -1.821 72.572 -13.279 1.00 27.96 ? 88 SER B O 1 ATOM 2325 C CB . SER B 1 67 ? -2.447 70.358 -11.033 1.00 27.80 ? 88 SER B CB 1 ATOM 2326 O OG . SER B 1 67 ? -3.115 69.974 -9.848 1.00 28.50 ? 88 SER B OG 1 ATOM 2327 N N . PHE B 1 68 ? -0.025 72.376 -11.951 1.00 25.82 ? 89 PHE B N 1 ATOM 2328 C CA . PHE B 1 68 ? 0.896 72.752 -13.003 1.00 25.22 ? 89 PHE B CA 1 ATOM 2329 C C . PHE B 1 68 ? 2.249 72.066 -12.834 1.00 25.38 ? 89 PHE B C 1 ATOM 2330 O O . PHE B 1 68 ? 2.584 71.539 -11.763 1.00 24.55 ? 89 PHE B O 1 ATOM 2331 C CB . PHE B 1 68 ? 1.057 74.294 -13.092 1.00 25.62 ? 89 PHE B CB 1 ATOM 2332 C CG . PHE B 1 68 ? 1.748 74.917 -11.897 1.00 26.06 ? 89 PHE B CG 1 ATOM 2333 C CD1 . PHE B 1 68 ? 3.139 74.981 -11.827 1.00 26.45 ? 89 PHE B CD1 1 ATOM 2334 C CD2 . PHE B 1 68 ? 1.004 75.452 -10.850 1.00 27.15 ? 89 PHE B CD2 1 ATOM 2335 C CE1 . PHE B 1 68 ? 3.771 75.559 -10.720 1.00 28.15 ? 89 PHE B CE1 1 ATOM 2336 C CE2 . PHE B 1 68 ? 1.627 76.035 -9.750 1.00 26.05 ? 89 PHE B CE2 1 ATOM 2337 C CZ . PHE B 1 68 ? 3.010 76.090 -9.689 1.00 26.15 ? 89 PHE B CZ 1 ATOM 2338 N N . ALA B 1 69 ? 3.032 72.100 -13.898 1.00 23.63 ? 90 ALA B N 1 ATOM 2339 C CA . ALA B 1 69 ? 4.397 71.638 -13.849 1.00 24.33 ? 90 ALA B CA 1 ATOM 2340 C C . ALA B 1 69 ? 5.224 72.469 -14.804 1.00 24.48 ? 90 ALA B C 1 ATOM 2341 O O . ALA B 1 69 ? 4.724 72.926 -15.833 1.00 24.57 ? 90 ALA B O 1 ATOM 2342 C CB . ALA B 1 69 ? 4.473 70.160 -14.227 1.00 25.54 ? 90 ALA B CB 1 ATOM 2343 N N . THR B 1 70 ? 6.494 72.655 -14.464 1.00 22.93 ? 91 THR B N 1 ATOM 2344 C CA . THR B 1 70 ? 7.418 73.305 -15.360 1.00 23.67 ? 91 THR B CA 1 ATOM 2345 C C . THR B 1 70 ? 8.789 72.640 -15.274 1.00 23.60 ? 91 THR B C 1 ATOM 2346 O O . THR B 1 70 ? 9.222 72.215 -14.198 1.00 24.47 ? 91 THR B O 1 ATOM 2347 C CB . THR B 1 70 ? 7.496 74.834 -15.099 1.00 24.38 ? 91 THR B CB 1 ATOM 2348 O OG1 . THR B 1 70 ? 8.290 75.443 -16.124 1.00 25.58 ? 91 THR B OG1 1 ATOM 2349 C CG2 . THR B 1 70 ? 8.113 75.121 -13.726 1.00 24.35 ? 91 THR B CG2 1 ATOM 2350 N N . SER B 1 71 ? 9.444 72.511 -16.420 1.00 24.31 ? 92 SER B N 1 ATOM 2351 C CA . SER B 1 71 ? 10.815 72.047 -16.478 1.00 24.79 ? 92 SER B CA 1 ATOM 2352 C C . SER B 1 71 ? 11.628 73.075 -17.229 1.00 25.81 ? 92 SER B C 1 ATOM 2353 O O . SER B 1 71 ? 11.114 73.762 -18.112 1.00 26.59 ? 92 SER B O 1 ATOM 2354 C CB . SER B 1 71 ? 10.929 70.691 -17.176 1.00 27.36 ? 92 SER B CB 1 ATOM 2355 O OG . SER B 1 71 ? 10.333 70.757 -18.461 1.00 27.97 ? 92 SER B OG 1 ATOM 2356 N N . PHE B 1 72 ? 12.893 73.183 -16.855 1.00 25.45 ? 93 PHE B N 1 ATOM 2357 C CA . PHE B 1 72 ? 13.814 74.051 -17.565 1.00 26.80 ? 93 PHE B CA 1 ATOM 2358 C C . PHE B 1 72 ? 15.253 73.644 -17.337 1.00 26.71 ? 93 PHE B C 1 ATOM 2359 O O . PHE B 1 72 ? 15.592 73.043 -16.319 1.00 26.21 ? 93 PHE B O 1 ATOM 2360 C CB . PHE B 1 72 ? 13.571 75.548 -17.265 1.00 27.13 ? 93 PHE B CB 1 ATOM 2361 C CG . PHE B 1 72 ? 13.536 75.913 -15.797 1.00 27.43 ? 93 PHE B CG 1 ATOM 2362 C CD1 . PHE B 1 72 ? 14.699 76.321 -15.135 1.00 27.45 ? 93 PHE B CD1 1 ATOM 2363 C CD2 . PHE B 1 72 ? 12.330 75.927 -15.098 1.00 27.31 ? 93 PHE B CD2 1 ATOM 2364 C CE1 . PHE B 1 72 ? 14.656 76.685 -13.791 1.00 27.33 ? 93 PHE B CE1 1 ATOM 2365 C CE2 . PHE B 1 72 ? 12.284 76.301 -13.758 1.00 27.73 ? 93 PHE B CE2 1 ATOM 2366 C CZ . PHE B 1 72 ? 13.449 76.678 -13.106 1.00 27.72 ? 93 PHE B CZ 1 ATOM 2367 N N . THR B 1 73 ? 16.088 73.928 -18.332 1.00 26.68 ? 94 THR B N 1 ATOM 2368 C CA . THR B 1 73 ? 17.520 73.757 -18.224 1.00 28.02 ? 94 THR B CA 1 ATOM 2369 C C . THR B 1 73 ? 18.142 75.146 -18.080 1.00 28.43 ? 94 THR B C 1 ATOM 2370 O O . THR B 1 73 ? 17.783 76.076 -18.810 1.00 30.66 ? 94 THR B O 1 ATOM 2371 C CB . THR B 1 73 ? 18.092 73.017 -19.458 1.00 28.53 ? 94 THR B CB 1 ATOM 2372 O OG1 . THR B 1 73 ? 17.469 71.728 -19.576 1.00 27.74 ? 94 THR B OG1 1 ATOM 2373 C CG2 . THR B 1 73 ? 19.589 72.812 -19.327 1.00 28.42 ? 94 THR B CG2 1 ATOM 2374 N N . PHE B 1 74 ? 19.038 75.299 -17.108 1.00 29.70 ? 95 PHE B N 1 ATOM 2375 C CA . PHE B 1 74 ? 19.744 76.574 -16.935 1.00 29.25 ? 95 PHE B CA 1 ATOM 2376 C C . PHE B 1 74 ? 21.246 76.379 -16.814 1.00 29.39 ? 95 PHE B C 1 ATOM 2377 O O . PHE B 1 74 ? 21.717 75.309 -16.444 1.00 28.67 ? 95 PHE B O 1 ATOM 2378 C CB . PHE B 1 74 ? 19.155 77.433 -15.793 1.00 28.68 ? 95 PHE B CB 1 ATOM 2379 C CG . PHE B 1 74 ? 19.470 76.943 -14.388 1.00 28.83 ? 95 PHE B CG 1 ATOM 2380 C CD1 . PHE B 1 74 ? 20.732 77.131 -13.827 1.00 28.95 ? 95 PHE B CD1 1 ATOM 2381 C CD2 . PHE B 1 74 ? 18.480 76.343 -13.603 1.00 28.12 ? 95 PHE B CD2 1 ATOM 2382 C CE1 . PHE B 1 74 ? 21.013 76.701 -12.534 1.00 28.95 ? 95 PHE B CE1 1 ATOM 2383 C CE2 . PHE B 1 74 ? 18.754 75.911 -12.311 1.00 28.08 ? 95 PHE B CE2 1 ATOM 2384 C CZ . PHE B 1 74 ? 20.023 76.094 -11.772 1.00 29.11 ? 95 PHE B CZ 1 ATOM 2385 N N . ASN B 1 75 ? 22.001 77.419 -17.163 1.00 32.27 ? 96 ASN B N 1 ATOM 2386 C CA . ASN B 1 75 ? 23.440 77.401 -16.973 1.00 33.75 ? 96 ASN B CA 1 ATOM 2387 C C . ASN B 1 75 ? 23.837 78.677 -16.245 1.00 35.43 ? 96 ASN B C 1 ATOM 2388 O O . ASN B 1 75 ? 23.598 79.782 -16.740 1.00 35.92 ? 96 ASN B O 1 ATOM 2389 C CB . ASN B 1 75 ? 24.171 77.290 -18.319 1.00 34.69 ? 96 ASN B CB 1 ATOM 2390 C CG . ASN B 1 75 ? 25.652 77.009 -18.160 1.00 35.60 ? 96 ASN B CG 1 ATOM 2391 O OD1 . ASN B 1 75 ? 26.440 77.914 -17.873 1.00 37.84 ? 96 ASN B OD1 1 ATOM 2392 N ND2 . ASN B 1 75 ? 26.041 75.756 -18.350 1.00 32.37 ? 96 ASN B ND2 1 ATOM 2393 N N . ILE B 1 76 ? 24.384 78.510 -15.043 1.00 35.92 ? 97 ILE B N 1 ATOM 2394 C CA . ILE B 1 76 ? 24.977 79.606 -14.289 1.00 35.23 ? 97 ILE B CA 1 ATOM 2395 C C . ILE B 1 76 ? 26.477 79.390 -14.324 1.00 35.94 ? 97 ILE B C 1 ATOM 2396 O O . ILE B 1 76 ? 26.974 78.358 -13.874 1.00 36.94 ? 97 ILE B O 1 ATOM 2397 C CB . ILE B 1 76 ? 24.485 79.644 -12.827 1.00 34.63 ? 97 ILE B CB 1 ATOM 2398 C CG1 . ILE B 1 76 ? 22.999 79.988 -12.751 1.00 32.55 ? 97 ILE B CG1 1 ATOM 2399 C CG2 . ILE B 1 76 ? 25.298 80.645 -12.010 1.00 33.97 ? 97 ILE B CG2 1 ATOM 2400 C CD1 . ILE B 1 76 ? 22.414 79.840 -11.359 1.00 32.66 ? 97 ILE B CD1 1 ATOM 2401 N N . ASP B 1 77 ? 27.195 80.359 -14.884 1.00 37.78 ? 98 ASP B N 1 ATOM 2402 C CA . ASP B 1 77 ? 28.642 80.286 -14.984 1.00 39.85 ? 98 ASP B CA 1 ATOM 2403 C C . ASP B 1 77 ? 29.275 81.473 -14.261 1.00 39.00 ? 98 ASP B C 1 ATOM 2404 O O . ASP B 1 77 ? 28.635 82.502 -14.078 1.00 37.61 ? 98 ASP B O 1 ATOM 2405 C CB . ASP B 1 77 ? 29.080 80.265 -16.449 1.00 42.27 ? 98 ASP B CB 1 ATOM 2406 C CG . ASP B 1 77 ? 30.367 79.493 -16.664 1.00 43.73 ? 98 ASP B CG 1 ATOM 2407 O OD1 . ASP B 1 77 ? 30.998 79.054 -15.676 1.00 46.93 ? 98 ASP B OD1 1 ATOM 2408 O OD2 . ASP B 1 77 ? 30.750 79.310 -17.836 1.00 48.03 ? 98 ASP B OD2 1 ATOM 2409 N N . VAL B 1 78 ? 30.529 81.313 -13.857 1.00 43.13 ? 99 VAL B N 1 ATOM 2410 C CA . VAL B 1 78 ? 31.221 82.308 -13.036 1.00 44.61 ? 99 VAL B CA 1 ATOM 2411 C C . VAL B 1 78 ? 32.626 82.559 -13.594 1.00 45.12 ? 99 VAL B C 1 ATOM 2412 O O . VAL B 1 78 ? 33.342 81.609 -13.907 1.00 45.90 ? 99 VAL B O 1 ATOM 2413 C CB . VAL B 1 78 ? 31.323 81.852 -11.559 1.00 45.51 ? 99 VAL B CB 1 ATOM 2414 C CG1 . VAL B 1 78 ? 31.932 82.943 -10.689 1.00 45.29 ? 99 VAL B CG1 1 ATOM 2415 C CG2 . VAL B 1 78 ? 29.958 81.458 -11.010 1.00 44.95 ? 99 VAL B CG2 1 ATOM 2416 N N . PRO B 1 79 ? 33.017 83.842 -13.736 1.00 47.77 ? 100 PRO B N 1 ATOM 2417 C CA . PRO B 1 79 ? 34.388 84.179 -14.136 1.00 51.23 ? 100 PRO B CA 1 ATOM 2418 C C . PRO B 1 79 ? 35.406 83.754 -13.087 1.00 54.17 ? 100 PRO B C 1 ATOM 2419 O O . PRO B 1 79 ? 35.084 83.710 -11.894 1.00 55.81 ? 100 PRO B O 1 ATOM 2420 C CB . PRO B 1 79 ? 34.368 85.706 -14.225 1.00 49.73 ? 100 PRO B CB 1 ATOM 2421 C CG . PRO B 1 79 ? 32.941 86.071 -14.390 1.00 50.75 ? 100 PRO B CG 1 ATOM 2422 C CD . PRO B 1 79 ? 32.167 85.038 -13.627 1.00 48.43 ? 100 PRO B CD 1 ATOM 2423 N N . ASN B 1 80 ? 36.623 83.446 -13.530 1.00 57.85 ? 101 ASN B N 1 ATOM 2424 C CA . ASN B 1 80 ? 37.717 83.126 -12.616 1.00 61.72 ? 101 ASN B CA 1 ATOM 2425 C C . ASN B 1 80 ? 38.035 84.296 -11.682 1.00 61.66 ? 101 ASN B C 1 ATOM 2426 O O . ASN B 1 80 ? 37.844 85.462 -12.042 1.00 61.57 ? 101 ASN B O 1 ATOM 2427 C CB . ASN B 1 80 ? 38.964 82.680 -13.388 1.00 64.15 ? 101 ASN B CB 1 ATOM 2428 C CG . ASN B 1 80 ? 38.726 81.424 -14.215 1.00 66.10 ? 101 ASN B CG 1 ATOM 2429 O OD1 . ASN B 1 80 ? 39.287 81.267 -15.300 1.00 66.66 ? 101 ASN B OD1 1 ATOM 2430 N ND2 . ASN B 1 80 ? 37.892 80.523 -13.704 1.00 66.10 ? 101 ASN B ND2 1 ATOM 2431 N N . ASN B 1 81 ? 38.497 83.965 -10.476 1.00 63.31 ? 102 ASN B N 1 ATOM 2432 C CA . ASN B 1 81 ? 38.719 84.939 -9.394 1.00 62.41 ? 102 ASN B CA 1 ATOM 2433 C C . ASN B 1 81 ? 37.444 85.653 -8.930 1.00 58.54 ? 102 ASN B C 1 ATOM 2434 O O . ASN B 1 81 ? 37.502 86.732 -8.341 1.00 56.67 ? 102 ASN B O 1 ATOM 2435 C CB . ASN B 1 81 ? 39.833 85.938 -9.751 1.00 64.55 ? 102 ASN B CB 1 ATOM 2436 C CG . ASN B 1 81 ? 41.164 85.256 -10.003 1.00 66.24 ? 102 ASN B CG 1 ATOM 2437 O OD1 . ASN B 1 81 ? 41.313 84.497 -10.960 1.00 68.79 ? 102 ASN B OD1 1 ATOM 2438 N ND2 . ASN B 1 81 ? 42.138 85.520 -9.141 1.00 66.17 ? 102 ASN B ND2 1 ATOM 2439 N N . SER B 1 82 ? 36.299 85.033 -9.204 1.00 54.96 ? 103 SER B N 1 ATOM 2440 C CA . SER B 1 82 ? 35.010 85.490 -8.699 1.00 51.60 ? 103 SER B CA 1 ATOM 2441 C C . SER B 1 82 ? 34.233 84.313 -8.124 1.00 48.55 ? 103 SER B C 1 ATOM 2442 O O . SER B 1 82 ? 34.526 83.155 -8.434 1.00 45.85 ? 103 SER B O 1 ATOM 2443 C CB . SER B 1 82 ? 34.189 86.162 -9.805 1.00 52.52 ? 103 SER B CB 1 ATOM 2444 O OG . SER B 1 82 ? 34.316 87.574 -9.773 1.00 55.57 ? 103 SER B OG 1 ATOM 2445 N N . GLY B 1 83 ? 33.262 84.628 -7.274 1.00 46.90 ? 104 GLY B N 1 ATOM 2446 C CA . GLY B 1 83 ? 32.280 83.660 -6.798 1.00 47.24 ? 104 GLY B CA 1 ATOM 2447 C C . GLY B 1 83 ? 30.903 84.017 -7.338 1.00 46.66 ? 104 GLY B C 1 ATOM 2448 O O . GLY B 1 83 ? 30.699 85.128 -7.840 1.00 46.30 ? 104 GLY B O 1 ATOM 2449 N N . PRO B 1 84 ? 29.941 83.083 -7.239 1.00 45.60 ? 105 PRO B N 1 ATOM 2450 C CA . PRO B 1 84 ? 28.607 83.337 -7.771 1.00 43.64 ? 105 PRO B CA 1 ATOM 2451 C C . PRO B 1 84 ? 27.757 84.273 -6.907 1.00 42.21 ? 105 PRO B C 1 ATOM 2452 O O . PRO B 1 84 ? 27.958 84.347 -5.690 1.00 42.86 ? 105 PRO B O 1 ATOM 2453 C CB . PRO B 1 84 ? 27.981 81.938 -7.809 1.00 44.00 ? 105 PRO B CB 1 ATOM 2454 C CG . PRO B 1 84 ? 28.654 81.201 -6.703 1.00 45.16 ? 105 PRO B CG 1 ATOM 2455 C CD . PRO B 1 84 ? 30.062 81.731 -6.658 1.00 46.03 ? 105 PRO B CD 1 ATOM 2456 N N . ALA B 1 85 ? 26.834 84.979 -7.565 1.00 39.87 ? 106 ALA B N 1 ATOM 2457 C CA . ALA B 1 85 ? 25.738 85.746 -6.955 1.00 40.69 ? 106 ALA B CA 1 ATOM 2458 C C . ALA B 1 85 ? 24.857 86.313 -8.077 1.00 39.33 ? 106 ALA B C 1 ATOM 2459 O O . ALA B 1 85 ? 25.362 86.571 -9.166 1.00 41.63 ? 106 ALA B O 1 ATOM 2460 C CB . ALA B 1 85 ? 26.265 86.881 -6.082 1.00 40.92 ? 106 ALA B CB 1 ATOM 2461 N N . ASP B 1 86 ? 23.559 86.511 -7.844 1.00 39.98 ? 107 ASP B N 1 ATOM 2462 C CA . ASP B 1 86 ? 22.870 86.131 -6.605 1.00 40.85 ? 107 ASP B CA 1 ATOM 2463 C C . ASP B 1 86 ? 21.981 84.893 -6.781 1.00 41.74 ? 107 ASP B C 1 ATOM 2464 O O . ASP B 1 86 ? 21.545 84.293 -5.797 1.00 40.59 ? 107 ASP B O 1 ATOM 2465 C CB . ASP B 1 86 ? 22.034 87.297 -6.082 1.00 40.80 ? 107 ASP B CB 1 ATOM 2466 C CG . ASP B 1 86 ? 22.809 88.191 -5.113 1.00 44.00 ? 107 ASP B CG 1 ATOM 2467 O OD1 . ASP B 1 86 ? 22.945 87.813 -3.927 1.00 39.98 ? 107 ASP B OD1 1 ATOM 2468 O OD2 . ASP B 1 86 ? 23.262 89.281 -5.542 1.00 43.14 ? 107 ASP B OD2 1 ATOM 2469 N N . GLY B 1 87 ? 21.717 84.527 -8.034 1.00 40.71 ? 108 GLY B N 1 ATOM 2470 C CA . GLY B 1 87 ? 20.884 83.372 -8.358 1.00 40.23 ? 108 GLY B CA 1 ATOM 2471 C C . GLY B 1 87 ? 19.736 83.698 -9.293 1.00 39.73 ? 108 GLY B C 1 ATOM 2472 O O . GLY B 1 87 ? 19.621 84.822 -9.790 1.00 39.22 ? 108 GLY B O 1 ATOM 2473 N N . LEU B 1 88 ? 18.878 82.708 -9.532 1.00 37.52 ? 109 LEU B N 1 ATOM 2474 C CA . LEU B 1 88 ? 17.696 82.893 -10.369 1.00 35.93 ? 109 LEU B CA 1 ATOM 2475 C C . LEU B 1 88 ? 16.508 82.137 -9.792 1.00 34.79 ? 109 LEU B C 1 ATOM 2476 O O . LEU B 1 88 ? 16.680 81.228 -8.969 1.00 33.89 ? 109 LEU B O 1 ATOM 2477 C CB . LEU B 1 88 ? 17.971 82.505 -11.840 1.00 36.82 ? 109 LEU B CB 1 ATOM 2478 C CG . LEU B 1 88 ? 18.154 81.079 -12.400 1.00 38.20 ? 109 LEU B CG 1 ATOM 2479 C CD1 . LEU B 1 88 ? 19.247 80.308 -11.690 1.00 40.58 ? 109 LEU B CD1 1 ATOM 2480 C CD2 . LEU B 1 88 ? 16.857 80.276 -12.405 1.00 36.98 ? 109 LEU B CD2 1 ATOM 2481 N N . ALA B 1 89 ? 15.308 82.523 -10.208 1.00 33.12 ? 110 ALA B N 1 ATOM 2482 C CA . ALA B 1 89 ? 14.100 81.890 -9.703 1.00 32.34 ? 110 ALA B CA 1 ATOM 2483 C C . ALA B 1 89 ? 13.046 81.722 -10.778 1.00 33.50 ? 110 ALA B C 1 ATOM 2484 O O . ALA B 1 89 ? 12.925 82.552 -11.692 1.00 32.13 ? 110 ALA B O 1 ATOM 2485 C CB . ALA B 1 89 ? 13.525 82.684 -8.544 1.00 31.91 ? 110 ALA B CB 1 ATOM 2486 N N . PHE B 1 90 ? 12.286 80.635 -10.664 1.00 30.93 ? 111 PHE B N 1 ATOM 2487 C CA . PHE B 1 90 ? 11.051 80.503 -11.407 1.00 29.78 ? 111 PHE B CA 1 ATOM 2488 C C . PHE B 1 90 ? 9.928 81.103 -10.571 1.00 31.09 ? 111 PHE B C 1 ATOM 2489 O O . PHE B 1 90 ? 9.837 80.851 -9.366 1.00 32.24 ? 111 PHE B O 1 ATOM 2490 C CB . PHE B 1 90 ? 10.755 79.030 -11.767 1.00 28.70 ? 111 PHE B CB 1 ATOM 2491 C CG . PHE B 1 90 ? 9.387 78.836 -12.347 1.00 27.70 ? 111 PHE B CG 1 ATOM 2492 C CD1 . PHE B 1 90 ? 9.150 79.097 -13.694 1.00 28.13 ? 111 PHE B CD1 1 ATOM 2493 C CD2 . PHE B 1 90 ? 8.322 78.475 -11.541 1.00 27.36 ? 111 PHE B CD2 1 ATOM 2494 C CE1 . PHE B 1 90 ? 7.874 78.961 -14.225 1.00 27.21 ? 111 PHE B CE1 1 ATOM 2495 C CE2 . PHE B 1 90 ? 7.044 78.346 -12.064 1.00 28.13 ? 111 PHE B CE2 1 ATOM 2496 C CZ . PHE B 1 90 ? 6.822 78.587 -13.410 1.00 27.57 ? 111 PHE B CZ 1 ATOM 2497 N N . VAL B 1 91 ? 9.070 81.899 -11.201 1.00 30.65 ? 112 VAL B N 1 ATOM 2498 C CA . VAL B 1 91 ? 8.083 82.671 -10.455 1.00 31.04 ? 112 VAL B CA 1 ATOM 2499 C C . VAL B 1 91 ? 6.675 82.611 -11.023 1.00 31.42 ? 112 VAL B C 1 ATOM 2500 O O . VAL B 1 91 ? 6.491 82.438 -12.231 1.00 33.57 ? 112 VAL B O 1 ATOM 2501 C CB . VAL B 1 91 ? 8.511 84.166 -10.352 1.00 31.72 ? 112 VAL B CB 1 ATOM 2502 C CG1 . VAL B 1 91 ? 9.925 84.283 -9.810 1.00 32.03 ? 112 VAL B CG1 1 ATOM 2503 C CG2 . VAL B 1 91 ? 8.420 84.857 -11.710 1.00 30.60 ? 112 VAL B CG2 1 ATOM 2504 N N . LEU B 1 92 ? 5.700 82.773 -10.132 1.00 32.56 ? 113 LEU B N 1 ATOM 2505 C CA . LEU B 1 92 ? 4.315 83.072 -10.476 1.00 34.22 ? 113 LEU B CA 1 ATOM 2506 C C . LEU B 1 92 ? 3.952 84.448 -9.877 1.00 37.48 ? 113 LEU B C 1 ATOM 2507 O O . LEU B 1 92 ? 3.989 84.626 -8.652 1.00 36.79 ? 113 LEU B O 1 ATOM 2508 C CB . LEU B 1 92 ? 3.384 82.005 -9.906 1.00 34.71 ? 113 LEU B CB 1 ATOM 2509 C CG . LEU B 1 92 ? 3.534 80.532 -10.318 1.00 35.46 ? 113 LEU B CG 1 ATOM 2510 C CD1 . LEU B 1 92 ? 3.468 79.652 -9.081 1.00 37.21 ? 113 LEU B CD1 1 ATOM 2511 C CD2 . LEU B 1 92 ? 2.468 80.107 -11.311 1.00 35.91 ? 113 LEU B CD2 1 ATOM 2512 N N . LEU B 1 93 ? 3.594 85.407 -10.736 1.00 39.11 ? 114 LEU B N 1 ATOM 2513 C CA . LEU B 1 93 ? 3.357 86.805 -10.314 1.00 38.38 ? 114 LEU B CA 1 ATOM 2514 C C . LEU B 1 93 ? 2.050 87.390 -10.872 1.00 39.45 ? 114 LEU B C 1 ATOM 2515 O O . LEU B 1 93 ? 1.540 86.897 -11.884 1.00 37.69 ? 114 LEU B O 1 ATOM 2516 C CB . LEU B 1 93 ? 4.531 87.685 -10.747 1.00 37.19 ? 114 LEU B CB 1 ATOM 2517 C CG . LEU B 1 93 ? 5.910 87.404 -10.154 1.00 38.84 ? 114 LEU B CG 1 ATOM 2518 C CD1 . LEU B 1 93 ? 6.939 88.310 -10.804 1.00 36.64 ? 114 LEU B CD1 1 ATOM 2519 C CD2 . LEU B 1 93 ? 5.914 87.565 -8.638 1.00 37.92 ? 114 LEU B CD2 1 ATOM 2520 N N . PRO B 1 94 ? 1.497 88.444 -10.221 1.00 39.84 ? 115 PRO B N 1 ATOM 2521 C CA . PRO B 1 94 ? 0.313 89.111 -10.791 1.00 39.23 ? 115 PRO B CA 1 ATOM 2522 C C . PRO B 1 94 ? 0.580 89.655 -12.196 1.00 36.52 ? 115 PRO B C 1 ATOM 2523 O O . PRO B 1 94 ? 1.715 90.019 -12.516 1.00 34.80 ? 115 PRO B O 1 ATOM 2524 C CB . PRO B 1 94 ? 0.056 90.271 -9.821 1.00 40.05 ? 115 PRO B CB 1 ATOM 2525 C CG . PRO B 1 94 ? 0.662 89.830 -8.534 1.00 40.17 ? 115 PRO B CG 1 ATOM 2526 C CD . PRO B 1 94 ? 1.879 89.036 -8.921 1.00 40.65 ? 115 PRO B CD 1 ATOM 2527 N N . VAL B 1 95 ? -0.458 89.675 -13.026 1.00 36.48 ? 116 VAL B N 1 ATOM 2528 C CA . VAL B 1 95 ? -0.370 90.250 -14.376 1.00 39.41 ? 116 VAL B CA 1 ATOM 2529 C C . VAL B 1 95 ? 0.059 91.715 -14.274 1.00 40.31 ? 116 VAL B C 1 ATOM 2530 O O . VAL B 1 95 ? -0.529 92.472 -13.509 1.00 41.40 ? 116 VAL B O 1 ATOM 2531 C CB . VAL B 1 95 ? -1.720 90.143 -15.129 1.00 39.22 ? 116 VAL B CB 1 ATOM 2532 C CG1 . VAL B 1 95 ? -1.608 90.727 -16.534 1.00 39.27 ? 116 VAL B CG1 1 ATOM 2533 C CG2 . VAL B 1 95 ? -2.193 88.692 -15.193 1.00 39.76 ? 116 VAL B CG2 1 ATOM 2534 N N . GLY B 1 96 ? 1.104 92.091 -15.012 1.00 42.80 ? 117 GLY B N 1 ATOM 2535 C CA . GLY B 1 96 ? 1.611 93.472 -15.009 1.00 43.35 ? 117 GLY B CA 1 ATOM 2536 C C . GLY B 1 96 ? 2.745 93.775 -14.039 1.00 44.61 ? 117 GLY B C 1 ATOM 2537 O O . GLY B 1 96 ? 3.256 94.900 -14.008 1.00 42.17 ? 117 GLY B O 1 ATOM 2538 N N . SER B 1 97 ? 3.153 92.775 -13.256 1.00 43.03 ? 118 SER B N 1 ATOM 2539 C CA . SER B 1 97 ? 4.168 92.960 -12.215 1.00 42.47 ? 118 SER B CA 1 ATOM 2540 C C . SER B 1 97 ? 5.468 93.562 -12.745 1.00 43.05 ? 118 SER B C 1 ATOM 2541 O O . SER B 1 97 ? 5.941 93.208 -13.834 1.00 41.34 ? 118 SER B O 1 ATOM 2542 C CB . SER B 1 97 ? 4.432 91.645 -11.452 1.00 43.07 ? 118 SER B CB 1 ATOM 2543 O OG . SER B 1 97 ? 5.767 91.579 -10.960 1.00 43.49 ? 118 SER B OG 1 ATOM 2544 N N . GLN B 1 98 ? 6.021 94.486 -11.958 1.00 43.53 ? 119 GLN B N 1 ATOM 2545 C CA . GLN B 1 98 ? 7.257 95.190 -12.287 1.00 44.07 ? 119 GLN B CA 1 ATOM 2546 C C . GLN B 1 98 ? 8.398 94.788 -11.349 1.00 43.45 ? 119 GLN B C 1 ATOM 2547 O O . GLN B 1 98 ? 8.145 94.417 -10.198 1.00 45.95 ? 119 GLN B O 1 ATOM 2548 C CB . GLN B 1 98 ? 7.032 96.713 -12.229 1.00 45.12 ? 119 GLN B CB 1 ATOM 2549 C CG . GLN B 1 98 ? 6.143 97.265 -13.338 1.00 45.33 ? 119 GLN B CG 1 ATOM 2550 C CD . GLN B 1 98 ? 6.663 96.974 -14.740 1.00 45.35 ? 119 GLN B CD 1 ATOM 2551 O OE1 . GLN B 1 98 ? 5.892 96.636 -15.629 1.00 48.12 ? 119 GLN B OE1 1 ATOM 2552 N NE2 . GLN B 1 98 ? 7.969 97.108 -14.942 1.00 46.52 ? 119 GLN B NE2 1 ATOM 2553 N N . PRO B 1 99 ? 9.654 94.854 -11.836 1.00 41.95 ? 120 PRO B N 1 ATOM 2554 C CA . PRO B 1 99 ? 10.798 94.425 -11.029 1.00 43.52 ? 120 PRO B CA 1 ATOM 2555 C C . PRO B 1 99 ? 10.946 95.234 -9.741 1.00 46.57 ? 120 PRO B C 1 ATOM 2556 O O . PRO B 1 99 ? 10.819 96.459 -9.761 1.00 44.94 ? 120 PRO B O 1 ATOM 2557 C CB . PRO B 1 99 ? 11.998 94.676 -11.946 1.00 41.80 ? 120 PRO B CB 1 ATOM 2558 C CG . PRO B 1 99 ? 11.439 94.693 -13.324 1.00 41.82 ? 120 PRO B CG 1 ATOM 2559 C CD . PRO B 1 99 ? 10.062 95.270 -13.188 1.00 41.87 ? 120 PRO B CD 1 ATOM 2560 N N . LYS B 1 100 ? 11.177 94.538 -8.631 1.00 47.96 ? 121 LYS B N 1 ATOM 2561 C CA . LYS B 1 100 ? 11.469 95.192 -7.365 1.00 47.36 ? 121 LYS B CA 1 ATOM 2562 C C . LYS B 1 100 ? 12.981 95.214 -7.188 1.00 46.65 ? 121 LYS B C 1 ATOM 2563 O O . LYS B 1 100 ? 13.706 95.313 -8.174 1.00 47.87 ? 121 LYS B O 1 ATOM 2564 C CB . LYS B 1 100 ? 10.748 94.513 -6.200 1.00 48.12 ? 121 LYS B CB 1 ATOM 2565 C CG . LYS B 1 100 ? 9.227 94.550 -6.295 1.00 50.76 ? 121 LYS B CG 1 ATOM 2566 C CD . LYS B 1 100 ? 8.597 94.335 -4.926 1.00 54.02 ? 121 LYS B CD 1 ATOM 2567 C CE . LYS B 1 100 ? 7.132 93.929 -5.015 1.00 55.76 ? 121 LYS B CE 1 ATOM 2568 N NZ . LYS B 1 100 ? 6.256 95.027 -5.502 1.00 56.92 ? 121 LYS B NZ 1 ATOM 2569 N N . ASP B 1 101 ? 13.468 95.112 -5.955 1.00 48.40 ? 122 ASP B N 1 ATOM 2570 C CA . ASP B 1 101 ? 14.891 95.362 -5.699 1.00 49.77 ? 122 ASP B CA 1 ATOM 2571 C C . ASP B 1 101 ? 15.883 94.301 -6.165 1.00 49.57 ? 122 ASP B C 1 ATOM 2572 O O . ASP B 1 101 ? 15.591 93.106 -6.179 1.00 50.87 ? 122 ASP B O 1 ATOM 2573 C CB . ASP B 1 101 ? 15.132 95.762 -4.242 1.00 53.19 ? 122 ASP B CB 1 ATOM 2574 C CG . ASP B 1 101 ? 14.816 97.222 -3.994 1.00 56.18 ? 122 ASP B CG 1 ATOM 2575 O OD1 . ASP B 1 101 ? 15.299 98.067 -4.781 1.00 57.47 ? 122 ASP B OD1 1 ATOM 2576 O OD2 . ASP B 1 101 ? 14.077 97.523 -3.030 1.00 57.72 ? 122 ASP B OD2 1 ATOM 2577 N N . LYS B 1 102 ? 17.060 94.786 -6.539 1.00 48.24 ? 123 LYS B N 1 ATOM 2578 C CA . LYS B 1 102 ? 18.162 94.027 -7.121 1.00 48.03 ? 123 LYS B CA 1 ATOM 2579 C C . LYS B 1 102 ? 18.790 93.003 -6.162 1.00 45.85 ? 123 LYS B C 1 ATOM 2580 O O . LYS B 1 102 ? 18.271 92.748 -5.072 1.00 46.72 ? 123 LYS B O 1 ATOM 2581 C CB . LYS B 1 102 ? 19.241 95.046 -7.508 1.00 52.36 ? 123 LYS B CB 1 ATOM 2582 C CG . LYS B 1 102 ? 19.703 95.009 -8.953 1.00 55.88 ? 123 LYS B CG 1 ATOM 2583 C CD . LYS B 1 102 ? 20.018 96.424 -9.437 1.00 57.42 ? 123 LYS B CD 1 ATOM 2584 C CE . LYS B 1 102 ? 18.776 97.310 -9.418 1.00 57.95 ? 123 LYS B CE 1 ATOM 2585 N NZ . LYS B 1 102 ? 19.007 98.632 -10.061 1.00 59.35 ? 123 LYS B NZ 1 ATOM 2586 N N . GLY B 1 103 ? 19.922 92.440 -6.580 1.00 43.16 ? 124 GLY B N 1 ATOM 2587 C CA . GLY B 1 103 ? 20.775 91.617 -5.722 1.00 44.10 ? 124 GLY B CA 1 ATOM 2588 C C . GLY B 1 103 ? 20.091 90.423 -5.071 1.00 44.52 ? 124 GLY B C 1 ATOM 2589 O O . GLY B 1 103 ? 19.369 89.671 -5.735 1.00 44.60 ? 124 GLY B O 1 ATOM 2590 N N . GLY B 1 104 ? 20.307 90.267 -3.765 1.00 40.46 ? 125 GLY B N 1 ATOM 2591 C CA . GLY B 1 104 ? 19.795 89.126 -3.012 1.00 38.57 ? 125 GLY B CA 1 ATOM 2592 C C . GLY B 1 104 ? 18.288 89.070 -2.915 1.00 38.54 ? 125 GLY B C 1 ATOM 2593 O O . GLY B 1 104 ? 17.723 88.076 -2.458 1.00 38.20 ? 125 GLY B O 1 ATOM 2594 N N . LEU B 1 105 ? 17.618 90.133 -3.340 1.00 37.86 ? 126 LEU B N 1 ATOM 2595 C CA . LEU B 1 105 ? 16.166 90.148 -3.288 1.00 38.20 ? 126 LEU B CA 1 ATOM 2596 C C . LEU B 1 105 ? 15.589 89.651 -4.617 1.00 35.01 ? 126 LEU B C 1 ATOM 2597 O O . LEU B 1 105 ? 14.379 89.629 -4.801 1.00 36.90 ? 126 LEU B O 1 ATOM 2598 C CB . LEU B 1 105 ? 15.646 91.537 -2.902 1.00 39.57 ? 126 LEU B CB 1 ATOM 2599 C CG . LEU B 1 105 ? 16.100 91.986 -1.503 1.00 39.74 ? 126 LEU B CG 1 ATOM 2600 C CD1 . LEU B 1 105 ? 15.931 93.484 -1.325 1.00 40.35 ? 126 LEU B CD1 1 ATOM 2601 C CD2 . LEU B 1 105 ? 15.361 91.226 -0.409 1.00 39.75 ? 126 LEU B CD2 1 ATOM 2602 N N . LEU B 1 106 ? 16.495 89.271 -5.519 1.00 38.06 ? 127 LEU B N 1 ATOM 2603 C CA . LEU B 1 106 ? 16.198 88.584 -6.790 1.00 38.24 ? 127 LEU B CA 1 ATOM 2604 C C . LEU B 1 106 ? 15.219 89.315 -7.714 1.00 39.80 ? 127 LEU B C 1 ATOM 2605 O O . LEU B 1 106 ? 14.726 88.737 -8.684 1.00 40.10 ? 127 LEU B O 1 ATOM 2606 C CB . LEU B 1 106 ? 15.759 87.125 -6.540 1.00 37.33 ? 127 LEU B CB 1 ATOM 2607 C CG . LEU B 1 106 ? 16.792 86.210 -5.869 1.00 36.17 ? 127 LEU B CG 1 ATOM 2608 C CD1 . LEU B 1 106 ? 16.150 84.903 -5.423 1.00 35.67 ? 127 LEU B CD1 1 ATOM 2609 C CD2 . LEU B 1 106 ? 17.995 85.946 -6.762 1.00 37.45 ? 127 LEU B CD2 1 ATOM 2610 N N . GLY B 1 107 ? 14.960 90.588 -7.427 1.00 39.88 ? 128 GLY B N 1 ATOM 2611 C CA . GLY B 1 107 ? 14.020 91.371 -8.217 1.00 37.80 ? 128 GLY B CA 1 ATOM 2612 C C . GLY B 1 107 ? 12.574 91.156 -7.837 1.00 37.42 ? 128 GLY B C 1 ATOM 2613 O O . GLY B 1 107 ? 11.682 91.505 -8.605 1.00 39.48 ? 128 GLY B O 1 ATOM 2614 N N . LEU B 1 108 ? 12.336 90.600 -6.648 1.00 38.00 ? 129 LEU B N 1 ATOM 2615 C CA . LEU B 1 108 ? 10.984 90.210 -6.215 1.00 37.42 ? 129 LEU B CA 1 ATOM 2616 C C . LEU B 1 108 ? 10.480 90.901 -4.952 1.00 37.31 ? 129 LEU B C 1 ATOM 2617 O O . LEU B 1 108 ? 9.281 90.890 -4.677 1.00 38.11 ? 129 LEU B O 1 ATOM 2618 C CB . LEU B 1 108 ? 10.908 88.693 -5.993 1.00 38.20 ? 129 LEU B CB 1 ATOM 2619 C CG . LEU B 1 108 ? 11.176 87.757 -7.175 1.00 38.60 ? 129 LEU B CG 1 ATOM 2620 C CD1 . LEU B 1 108 ? 11.373 86.325 -6.688 1.00 37.67 ? 129 LEU B CD1 1 ATOM 2621 C CD2 . LEU B 1 108 ? 10.034 87.841 -8.175 1.00 37.67 ? 129 LEU B CD2 1 ATOM 2622 N N . PHE B 1 109 ? 11.393 91.468 -4.168 1.00 40.88 ? 130 PHE B N 1 ATOM 2623 C CA . PHE B 1 109 ? 11.018 92.088 -2.893 1.00 41.42 ? 130 PHE B CA 1 ATOM 2624 C C . PHE B 1 109 ? 11.774 93.392 -2.642 1.00 42.93 ? 130 PHE B C 1 ATOM 2625 O O . PHE B 1 109 ? 12.830 93.637 -3.232 1.00 41.34 ? 130 PHE B O 1 ATOM 2626 C CB . PHE B 1 109 ? 11.235 91.109 -1.727 1.00 41.25 ? 130 PHE B CB 1 ATOM 2627 C CG . PHE B 1 109 ? 10.625 89.750 -1.953 1.00 39.62 ? 130 PHE B CG 1 ATOM 2628 C CD1 . PHE B 1 109 ? 9.274 89.530 -1.701 1.00 40.45 ? 130 PHE B CD1 1 ATOM 2629 C CD2 . PHE B 1 109 ? 11.403 88.691 -2.426 1.00 40.47 ? 130 PHE B CD2 1 ATOM 2630 C CE1 . PHE B 1 109 ? 8.701 88.283 -1.917 1.00 41.46 ? 130 PHE B CE1 1 ATOM 2631 C CE2 . PHE B 1 109 ? 10.833 87.444 -2.646 1.00 39.22 ? 130 PHE B CE2 1 ATOM 2632 C CZ . PHE B 1 109 ? 9.484 87.244 -2.391 1.00 39.43 ? 130 PHE B CZ 1 ATOM 2633 N N . ASN B 1 110 ? 11.215 94.216 -1.758 1.00 47.08 ? 131 ASN B N 1 ATOM 2634 C CA . ASN B 1 110 ? 11.841 95.472 -1.339 1.00 50.74 ? 131 ASN B CA 1 ATOM 2635 C C . ASN B 1 110 ? 12.760 95.287 -0.136 1.00 53.56 ? 131 ASN B C 1 ATOM 2636 O O . ASN B 1 110 ? 13.768 95.989 0.012 1.00 55.15 ? 131 ASN B O 1 ATOM 2637 C CB . ASN B 1 110 ? 10.765 96.505 -1.007 1.00 50.92 ? 131 ASN B CB 1 ATOM 2638 C CG . ASN B 1 110 ? 9.959 96.916 -2.218 1.00 49.45 ? 131 ASN B CG 1 ATOM 2639 O OD1 . ASN B 1 110 ? 10.514 97.226 -3.271 1.00 49.29 ? 131 ASN B OD1 1 ATOM 2640 N ND2 . ASN B 1 110 ? 8.640 96.923 -2.074 1.00 50.80 ? 131 ASN B ND2 1 ATOM 2641 N N . ASN B 1 111 ? 12.396 94.334 0.718 1.00 54.41 ? 132 ASN B N 1 ATOM 2642 C CA . ASN B 1 111 ? 13.134 94.024 1.937 1.00 56.55 ? 132 ASN B CA 1 ATOM 2643 C C . ASN B 1 111 ? 13.048 92.522 2.222 1.00 56.85 ? 132 ASN B C 1 ATOM 2644 O O . ASN B 1 111 ? 12.474 91.772 1.427 1.00 54.99 ? 132 ASN B O 1 ATOM 2645 C CB . ASN B 1 111 ? 12.579 94.845 3.110 1.00 56.54 ? 132 ASN B CB 1 ATOM 2646 C CG . ASN B 1 111 ? 11.068 94.744 3.231 1.00 58.17 ? 132 ASN B CG 1 ATOM 2647 O OD1 . ASN B 1 111 ? 10.530 93.716 3.652 1.00 59.95 ? 132 ASN B OD1 1 ATOM 2648 N ND2 . ASN B 1 111 ? 10.373 95.816 2.862 1.00 58.60 ? 132 ASN B ND2 1 ATOM 2649 N N . TYR B 1 112 ? 13.609 92.084 3.347 1.00 56.26 ? 133 TYR B N 1 ATOM 2650 C CA . TYR B 1 112 ? 13.600 90.658 3.690 1.00 55.60 ? 133 TYR B CA 1 ATOM 2651 C C . TYR B 1 112 ? 12.532 90.229 4.697 1.00 53.65 ? 133 TYR B C 1 ATOM 2652 O O . TYR B 1 112 ? 12.605 89.133 5.251 1.00 55.83 ? 133 TYR B O 1 ATOM 2653 C CB . TYR B 1 112 ? 14.991 90.176 4.120 1.00 57.58 ? 133 TYR B CB 1 ATOM 2654 C CG . TYR B 1 112 ? 15.564 90.819 5.366 1.00 60.00 ? 133 TYR B CG 1 ATOM 2655 C CD1 . TYR B 1 112 ? 15.457 90.191 6.610 1.00 59.71 ? 133 TYR B CD1 1 ATOM 2656 C CD2 . TYR B 1 112 ? 16.244 92.040 5.296 1.00 60.37 ? 133 TYR B CD2 1 ATOM 2657 C CE1 . TYR B 1 112 ? 15.993 90.768 7.754 1.00 61.14 ? 133 TYR B CE1 1 ATOM 2658 C CE2 . TYR B 1 112 ? 16.783 92.624 6.433 1.00 62.52 ? 133 TYR B CE2 1 ATOM 2659 C CZ . TYR B 1 112 ? 16.655 91.986 7.657 1.00 62.46 ? 133 TYR B CZ 1 ATOM 2660 O OH . TYR B 1 112 ? 17.191 92.564 8.785 1.00 61.41 ? 133 TYR B OH 1 ATOM 2661 N N . LYS B 1 113 ? 11.539 91.085 4.913 1.00 53.09 ? 134 LYS B N 1 ATOM 2662 C CA . LYS B 1 113 ? 10.407 90.757 5.775 1.00 53.60 ? 134 LYS B CA 1 ATOM 2663 C C . LYS B 1 113 ? 9.262 90.185 4.936 1.00 53.31 ? 134 LYS B C 1 ATOM 2664 O O . LYS B 1 113 ? 9.220 90.372 3.716 1.00 52.41 ? 134 LYS B O 1 ATOM 2665 C CB . LYS B 1 113 ? 9.956 92.000 6.568 1.00 56.33 ? 134 LYS B CB 1 ATOM 2666 C CG . LYS B 1 113 ? 8.914 91.758 7.669 1.00 58.31 ? 134 LYS B CG 1 ATOM 2667 C CD . LYS B 1 113 ? 9.510 91.425 9.043 1.00 58.71 ? 134 LYS B CD 1 ATOM 2668 C CE . LYS B 1 113 ? 9.742 89.933 9.260 1.00 57.46 ? 134 LYS B CE 1 ATOM 2669 N NZ . LYS B 1 113 ? 8.546 89.100 8.947 1.00 54.19 ? 134 LYS B NZ 1 ATOM 2670 N N . TYR B 1 114 ? 8.349 89.477 5.595 1.00 51.84 ? 135 TYR B N 1 ATOM 2671 C CA . TYR B 1 114 ? 7.162 88.935 4.954 1.00 52.21 ? 135 TYR B CA 1 ATOM 2672 C C . TYR B 1 114 ? 6.241 90.049 4.477 1.00 53.83 ? 135 TYR B C 1 ATOM 2673 O O . TYR B 1 114 ? 5.989 91.011 5.205 1.00 54.37 ? 135 TYR B O 1 ATOM 2674 C CB . TYR B 1 114 ? 6.412 88.020 5.922 1.00 51.04 ? 135 TYR B CB 1 ATOM 2675 C CG . TYR B 1 114 ? 5.209 87.327 5.316 1.00 51.69 ? 135 TYR B CG 1 ATOM 2676 C CD1 . TYR B 1 114 ? 5.363 86.201 4.496 1.00 50.00 ? 135 TYR B CD1 1 ATOM 2677 C CD2 . TYR B 1 114 ? 3.916 87.788 5.567 1.00 50.34 ? 135 TYR B CD2 1 ATOM 2678 C CE1 . TYR B 1 114 ? 4.262 85.563 3.943 1.00 50.33 ? 135 TYR B CE1 1 ATOM 2679 C CE2 . TYR B 1 114 ? 2.809 87.156 5.018 1.00 50.68 ? 135 TYR B CE2 1 ATOM 2680 C CZ . TYR B 1 114 ? 2.990 86.047 4.207 1.00 50.93 ? 135 TYR B CZ 1 ATOM 2681 O OH . TYR B 1 114 ? 1.894 85.424 3.663 1.00 52.20 ? 135 TYR B OH 1 ATOM 2682 N N . ASP B 1 115 ? 5.736 89.900 3.255 1.00 53.81 ? 136 ASP B N 1 ATOM 2683 C CA . ASP B 1 115 ? 4.827 90.873 2.654 1.00 52.40 ? 136 ASP B CA 1 ATOM 2684 C C . ASP B 1 115 ? 3.596 90.167 2.094 1.00 51.84 ? 136 ASP B C 1 ATOM 2685 O O . ASP B 1 115 ? 3.652 89.586 1.011 1.00 52.22 ? 136 ASP B O 1 ATOM 2686 C CB . ASP B 1 115 ? 5.553 91.654 1.545 1.00 51.89 ? 136 ASP B CB 1 ATOM 2687 C CG . ASP B 1 115 ? 4.693 92.763 0.923 1.00 51.98 ? 136 ASP B CG 1 ATOM 2688 O OD1 . ASP B 1 115 ? 3.488 92.882 1.244 1.00 51.40 ? 136 ASP B OD1 1 ATOM 2689 O OD2 . ASP B 1 115 ? 5.237 93.520 0.095 1.00 51.54 ? 136 ASP B OD2 1 ATOM 2690 N N . SER B 1 116 ? 2.483 90.230 2.818 1.00 51.83 ? 137 SER B N 1 ATOM 2691 C CA . SER B 1 116 ? 1.253 89.564 2.376 1.00 55.31 ? 137 SER B CA 1 ATOM 2692 C C . SER B 1 116 ? 0.553 90.247 1.187 1.00 57.64 ? 137 SER B C 1 ATOM 2693 O O . SER B 1 116 ? -0.591 89.914 0.859 1.00 57.67 ? 137 SER B O 1 ATOM 2694 C CB . SER B 1 116 ? 0.286 89.340 3.548 1.00 56.46 ? 137 SER B CB 1 ATOM 2695 O OG . SER B 1 116 ? 0.114 90.518 4.312 1.00 61.15 ? 137 SER B OG 1 ATOM 2696 N N . ASN B 1 117 ? 1.256 91.182 0.544 1.00 60.08 ? 138 ASN B N 1 ATOM 2697 C CA . ASN B 1 117 ? 0.768 91.878 -0.655 1.00 59.51 ? 138 ASN B CA 1 ATOM 2698 C C . ASN B 1 117 ? 1.715 91.715 -1.848 1.00 57.28 ? 138 ASN B C 1 ATOM 2699 O O . ASN B 1 117 ? 1.495 92.298 -2.917 1.00 55.17 ? 138 ASN B O 1 ATOM 2700 C CB . ASN B 1 117 ? 0.536 93.373 -0.372 1.00 64.01 ? 138 ASN B CB 1 ATOM 2701 C CG . ASN B 1 117 ? -0.657 93.628 0.538 1.00 65.99 ? 138 ASN B CG 1 ATOM 2702 O OD1 . ASN B 1 117 ? -1.619 92.858 0.568 1.00 67.02 ? 138 ASN B OD1 1 ATOM 2703 N ND2 . ASN B 1 117 ? -0.598 94.726 1.284 1.00 68.82 ? 138 ASN B ND2 1 ATOM 2704 N N . ALA B 1 118 ? 2.767 90.920 -1.656 1.00 52.24 ? 139 ALA B N 1 ATOM 2705 C CA . ALA B 1 118 ? 3.728 90.628 -2.716 1.00 49.84 ? 139 ALA B CA 1 ATOM 2706 C C . ALA B 1 118 ? 3.127 89.712 -3.781 1.00 46.63 ? 139 ALA B C 1 ATOM 2707 O O . ALA B 1 118 ? 3.595 89.698 -4.917 1.00 46.83 ? 139 ALA B O 1 ATOM 2708 C CB . ALA B 1 118 ? 4.995 90.012 -2.140 1.00 49.74 ? 139 ALA B CB 1 ATOM 2709 N N . HIS B 1 119 ? 2.089 88.966 -3.399 1.00 44.84 ? 140 HIS B N 1 ATOM 2710 C CA . HIS B 1 119 ? 1.426 87.989 -4.272 1.00 45.29 ? 140 HIS B CA 1 ATOM 2711 C C . HIS B 1 119 ? 2.426 87.188 -5.072 1.00 43.55 ? 140 HIS B C 1 ATOM 2712 O O . HIS B 1 119 ? 2.279 87.029 -6.286 1.00 42.00 ? 140 HIS B O 1 ATOM 2713 C CB . HIS B 1 119 ? 0.409 88.672 -5.193 1.00 46.77 ? 140 HIS B CB 1 ATOM 2714 C CG . HIS B 1 119 ? -0.743 89.331 -4.470 1.00 48.20 ? 140 HIS B CG 1 ATOM 2715 N ND1 . HIS B 1 119 ? -1.823 88.643 -4.043 1.00 49.53 ? 140 HIS B ND1 1 ATOM 2716 C CD2 . HIS B 1 119 ? -0.968 90.665 -4.132 1.00 48.60 ? 140 HIS B CD2 1 ATOM 2717 C CE1 . HIS B 1 119 ? -2.690 89.488 -3.450 1.00 50.92 ? 140 HIS B CE1 1 ATOM 2718 N NE2 . HIS B 1 119 ? -2.165 90.726 -3.506 1.00 51.13 ? 140 HIS B NE2 1 ATOM 2719 N N . THR B 1 120 ? 3.455 86.686 -4.385 1.00 41.54 ? 141 THR B N 1 ATOM 2720 C CA . THR B 1 120 ? 4.592 86.019 -5.018 1.00 39.81 ? 141 THR B CA 1 ATOM 2721 C C . THR B 1 120 ? 4.736 84.555 -4.564 1.00 40.57 ? 141 THR B C 1 ATOM 2722 O O . THR B 1 120 ? 4.782 84.266 -3.364 1.00 39.34 ? 141 THR B O 1 ATOM 2723 C CB . THR B 1 120 ? 5.907 86.785 -4.744 1.00 40.12 ? 141 THR B CB 1 ATOM 2724 O OG1 . THR B 1 120 ? 5.830 88.097 -5.321 1.00 41.55 ? 141 THR B OG1 1 ATOM 2725 C CG2 . THR B 1 120 ? 7.115 86.061 -5.330 1.00 39.08 ? 141 THR B CG2 1 ATOM 2726 N N . VAL B 1 121 ? 4.780 83.646 -5.539 1.00 37.54 ? 142 VAL B N 1 ATOM 2727 C CA . VAL B 1 121 ? 5.210 82.265 -5.309 1.00 35.32 ? 142 VAL B CA 1 ATOM 2728 C C . VAL B 1 121 ? 6.390 82.022 -6.239 1.00 35.67 ? 142 VAL B C 1 ATOM 2729 O O . VAL B 1 121 ? 6.279 82.217 -7.456 1.00 36.89 ? 142 VAL B O 1 ATOM 2730 C CB . VAL B 1 121 ? 4.097 81.234 -5.588 1.00 35.79 ? 142 VAL B CB 1 ATOM 2731 C CG1 . VAL B 1 121 ? 4.639 79.820 -5.450 1.00 37.33 ? 142 VAL B CG1 1 ATOM 2732 C CG2 . VAL B 1 121 ? 2.926 81.412 -4.636 1.00 35.01 ? 142 VAL B CG2 1 ATOM 2733 N N . ALA B 1 122 ? 7.521 81.618 -5.668 1.00 33.46 ? 143 ALA B N 1 ATOM 2734 C CA . ALA B 1 122 ? 8.740 81.410 -6.434 1.00 33.29 ? 143 ALA B CA 1 ATOM 2735 C C . ALA B 1 122 ? 9.533 80.199 -5.957 1.00 32.68 ? 143 ALA B C 1 ATOM 2736 O O . ALA B 1 122 ? 9.468 79.822 -4.783 1.00 33.70 ? 143 ALA B O 1 ATOM 2737 C CB . ALA B 1 122 ? 9.614 82.656 -6.386 1.00 34.60 ? 143 ALA B CB 1 ATOM 2738 N N . VAL B 1 123 ? 10.272 79.589 -6.878 1.00 30.50 ? 144 VAL B N 1 ATOM 2739 C CA . VAL B 1 123 ? 11.266 78.593 -6.520 1.00 28.95 ? 144 VAL B CA 1 ATOM 2740 C C . VAL B 1 123 ? 12.631 79.169 -6.872 1.00 29.42 ? 144 VAL B C 1 ATOM 2741 O O . VAL B 1 123 ? 12.934 79.394 -8.044 1.00 29.73 ? 144 VAL B O 1 ATOM 2742 C CB . VAL B 1 123 ? 11.031 77.245 -7.241 1.00 28.37 ? 144 VAL B CB 1 ATOM 2743 C CG1 . VAL B 1 123 ? 12.197 76.300 -7.004 1.00 28.26 ? 144 VAL B CG1 1 ATOM 2744 C CG2 . VAL B 1 123 ? 9.712 76.630 -6.797 1.00 27.93 ? 144 VAL B CG2 1 ATOM 2745 N N . GLU B 1 124 ? 13.443 79.409 -5.843 1.00 29.47 ? 145 GLU B N 1 ATOM 2746 C CA . GLU B 1 124 ? 14.740 80.072 -5.993 1.00 30.12 ? 145 GLU B CA 1 ATOM 2747 C C . GLU B 1 124 ? 15.909 79.109 -6.056 1.00 29.76 ? 145 GLU B C 1 ATOM 2748 O O . GLU B 1 124 ? 15.929 78.064 -5.396 1.00 32.73 ? 145 GLU B O 1 ATOM 2749 C CB . GLU B 1 124 ? 14.965 81.109 -4.863 1.00 30.08 ? 145 GLU B CB 1 ATOM 2750 C CG . GLU B 1 124 ? 15.185 80.522 -3.460 1.00 30.39 ? 145 GLU B CG 1 ATOM 2751 C CD . GLU B 1 124 ? 15.650 81.566 -2.440 1.00 31.28 ? 145 GLU B CD 1 ATOM 2752 O OE1 . GLU B 1 124 ? 15.012 82.638 -2.392 1.00 32.53 ? 145 GLU B OE1 1 ATOM 2753 O OE2 . GLU B 1 124 ? 16.628 81.317 -1.688 1.00 32.18 ? 145 GLU B OE2 1 ATOM 2754 N N . PHE B 1 125 ? 16.890 79.478 -6.861 1.00 29.42 ? 146 PHE B N 1 ATOM 2755 C CA . PHE B 1 125 ? 18.152 78.788 -6.913 1.00 29.24 ? 146 PHE B CA 1 ATOM 2756 C C . PHE B 1 125 ? 19.207 79.791 -6.475 1.00 32.29 ? 146 PHE B C 1 ATOM 2757 O O . PHE B 1 125 ? 19.749 80.553 -7.284 1.00 31.24 ? 146 PHE B O 1 ATOM 2758 C CB . PHE B 1 125 ? 18.368 78.194 -8.307 1.00 29.24 ? 146 PHE B CB 1 ATOM 2759 C CG . PHE B 1 125 ? 17.276 77.227 -8.683 1.00 27.63 ? 146 PHE B CG 1 ATOM 2760 C CD1 . PHE B 1 125 ? 17.424 75.871 -8.437 1.00 28.99 ? 146 PHE B CD1 1 ATOM 2761 C CD2 . PHE B 1 125 ? 16.067 77.692 -9.186 1.00 28.13 ? 146 PHE B CD2 1 ATOM 2762 C CE1 . PHE B 1 125 ? 16.401 74.985 -8.730 1.00 27.78 ? 146 PHE B CE1 1 ATOM 2763 C CE2 . PHE B 1 125 ? 15.035 76.815 -9.481 1.00 28.93 ? 146 PHE B CE2 1 ATOM 2764 C CZ . PHE B 1 125 ? 15.204 75.456 -9.246 1.00 28.07 ? 146 PHE B CZ 1 ATOM 2765 N N . ASP B 1 126 ? 19.448 79.786 -5.163 1.00 32.61 ? 147 ASP B N 1 ATOM 2766 C CA . ASP B 1 126 ? 20.160 80.858 -4.468 1.00 31.67 ? 147 ASP B CA 1 ATOM 2767 C C . ASP B 1 126 ? 21.649 80.530 -4.376 1.00 31.97 ? 147 ASP B C 1 ATOM 2768 O O . ASP B 1 126 ? 22.050 79.546 -3.760 1.00 31.07 ? 147 ASP B O 1 ATOM 2769 C CB . ASP B 1 126 ? 19.527 81.061 -3.086 1.00 31.32 ? 147 ASP B CB 1 ATOM 2770 C CG . ASP B 1 126 ? 19.986 82.354 -2.383 1.00 30.09 ? 147 ASP B CG 1 ATOM 2771 O OD1 . ASP B 1 126 ? 21.038 82.898 -2.762 1.00 33.27 ? 147 ASP B OD1 1 ATOM 2772 O OD2 . ASP B 1 126 ? 19.297 82.792 -1.431 1.00 32.13 ? 147 ASP B OD2 1 ATOM 2773 N N . THR B 1 127 ? 22.474 81.364 -5.001 1.00 33.74 ? 148 THR B N 1 ATOM 2774 C CA . THR B 1 127 ? 23.910 81.103 -5.076 1.00 34.24 ? 148 THR B CA 1 ATOM 2775 C C . THR B 1 127 ? 24.750 81.905 -4.061 1.00 34.50 ? 148 THR B C 1 ATOM 2776 O O . THR B 1 127 ? 25.978 81.772 -4.024 1.00 33.05 ? 148 THR B O 1 ATOM 2777 C CB . THR B 1 127 ? 24.455 81.374 -6.493 1.00 37.20 ? 148 THR B CB 1 ATOM 2778 O OG1 . THR B 1 127 ? 24.192 82.739 -6.851 1.00 37.98 ? 148 THR B OG1 1 ATOM 2779 C CG2 . THR B 1 127 ? 23.792 80.437 -7.517 1.00 34.82 ? 148 THR B CG2 1 ATOM 2780 N N . LEU B 1 128 ? 24.086 82.714 -3.242 1.00 35.18 ? 149 LEU B N 1 ATOM 2781 C CA . LEU B 1 128 ? 24.794 83.604 -2.324 1.00 36.82 ? 149 LEU B CA 1 ATOM 2782 C C . LEU B 1 128 ? 24.115 83.720 -0.967 1.00 34.45 ? 149 LEU B C 1 ATOM 2783 O O . LEU B 1 128 ? 22.931 84.092 -0.860 1.00 35.63 ? 149 LEU B O 1 ATOM 2784 C CB . LEU B 1 128 ? 24.995 84.997 -2.945 1.00 37.14 ? 149 LEU B CB 1 ATOM 2785 C CG . LEU B 1 128 ? 25.888 85.892 -2.067 1.00 37.68 ? 149 LEU B CG 1 ATOM 2786 C CD1 . LEU B 1 128 ? 27.336 85.855 -2.527 1.00 37.41 ? 149 LEU B CD1 1 ATOM 2787 C CD2 . LEU B 1 128 ? 25.350 87.307 -2.037 1.00 40.55 ? 149 LEU B CD2 1 ATOM 2788 N N . TYR B 1 129 ? 24.898 83.395 0.059 1.00 37.11 ? 150 TYR B N 1 ATOM 2789 C CA . TYR B 1 129 ? 24.480 83.473 1.443 1.00 38.01 ? 150 TYR B CA 1 ATOM 2790 C C . TYR B 1 129 ? 24.237 84.920 1.865 1.00 40.07 ? 150 TYR B C 1 ATOM 2791 O O . TYR B 1 129 ? 25.175 85.703 1.992 1.00 40.05 ? 150 TYR B O 1 ATOM 2792 C CB . TYR B 1 129 ? 25.545 82.825 2.336 1.00 37.59 ? 150 TYR B CB 1 ATOM 2793 C CG . TYR B 1 129 ? 25.360 83.058 3.824 1.00 38.86 ? 150 TYR B CG 1 ATOM 2794 C CD1 . TYR B 1 129 ? 24.118 82.872 4.440 1.00 38.93 ? 150 TYR B CD1 1 ATOM 2795 C CD2 . TYR B 1 129 ? 26.440 83.447 4.620 1.00 39.69 ? 150 TYR B CD2 1 ATOM 2796 C CE1 . TYR B 1 129 ? 23.952 83.080 5.803 1.00 41.54 ? 150 TYR B CE1 1 ATOM 2797 C CE2 . TYR B 1 129 ? 26.288 83.658 5.982 1.00 41.40 ? 150 TYR B CE2 1 ATOM 2798 C CZ . TYR B 1 129 ? 25.045 83.475 6.569 1.00 42.06 ? 150 TYR B CZ 1 ATOM 2799 O OH . TYR B 1 129 ? 24.897 83.676 7.922 1.00 41.77 ? 150 TYR B OH 1 ATOM 2800 N N . ASN B 1 130 ? 22.973 85.263 2.073 1.00 39.86 ? 151 ASN B N 1 ATOM 2801 C CA . ASN B 1 130 ? 22.623 86.552 2.644 1.00 41.27 ? 151 ASN B CA 1 ATOM 2802 C C . ASN B 1 130 ? 22.408 86.399 4.144 1.00 41.15 ? 151 ASN B C 1 ATOM 2803 O O . ASN B 1 130 ? 21.402 85.837 4.592 1.00 39.60 ? 151 ASN B O 1 ATOM 2804 C CB . ASN B 1 130 ? 21.403 87.157 1.944 1.00 41.58 ? 151 ASN B CB 1 ATOM 2805 C CG . ASN B 1 130 ? 21.671 87.474 0.480 1.00 44.06 ? 151 ASN B CG 1 ATOM 2806 O OD1 . ASN B 1 130 ? 21.151 86.804 -0.424 1.00 39.36 ? 151 ASN B OD1 1 ATOM 2807 N ND2 . ASN B 1 130 ? 22.505 88.489 0.235 1.00 43.12 ? 151 ASN B ND2 1 ATOM 2808 N N . VAL B 1 131 ? 23.383 86.898 4.904 1.00 42.05 ? 152 VAL B N 1 ATOM 2809 C CA . VAL B 1 131 ? 23.454 86.745 6.365 1.00 40.57 ? 152 VAL B CA 1 ATOM 2810 C C . VAL B 1 131 ? 22.112 86.916 7.098 1.00 39.54 ? 152 VAL B C 1 ATOM 2811 O O . VAL B 1 131 ? 21.839 86.187 8.047 1.00 41.02 ? 152 VAL B O 1 ATOM 2812 C CB . VAL B 1 131 ? 24.594 87.636 6.959 1.00 40.53 ? 152 VAL B CB 1 ATOM 2813 C CG1 . VAL B 1 131 ? 24.292 89.113 6.764 1.00 40.57 ? 152 VAL B CG1 1 ATOM 2814 C CG2 . VAL B 1 131 ? 24.872 87.310 8.421 1.00 39.77 ? 152 VAL B CG2 1 ATOM 2815 N N . HIS B 1 132 ? 21.260 87.831 6.632 1.00 41.12 ? 153 HIS B N 1 ATOM 2816 C CA . HIS B 1 132 ? 20.038 88.191 7.368 1.00 42.25 ? 153 HIS B CA 1 ATOM 2817 C C . HIS B 1 132 ? 18.825 87.303 7.197 1.00 41.97 ? 153 HIS B C 1 ATOM 2818 O O . HIS B 1 132 ? 17.844 87.469 7.932 1.00 41.47 ? 153 HIS B O 1 ATOM 2819 C CB . HIS B 1 132 ? 19.649 89.652 7.101 1.00 46.75 ? 153 HIS B CB 1 ATOM 2820 C CG . HIS B 1 132 ? 20.689 90.658 7.555 1.00 50.80 ? 153 HIS B CG 1 ATOM 2821 N ND1 . HIS B 1 132 ? 21.087 90.762 8.840 1.00 52.25 ? 153 HIS B ND1 1 ATOM 2822 C CD2 . HIS B 1 132 ? 21.411 91.615 6.841 1.00 52.28 ? 153 HIS B CD2 1 ATOM 2823 C CE1 . HIS B 1 132 ? 22.021 91.727 8.944 1.00 52.86 ? 153 HIS B CE1 1 ATOM 2824 N NE2 . HIS B 1 132 ? 22.216 92.252 7.722 1.00 53.39 ? 153 HIS B NE2 1 ATOM 2825 N N . TRP B 1 133 ? 18.863 86.360 6.246 1.00 41.77 ? 154 TRP B N 1 ATOM 2826 C CA . TRP B 1 133 ? 17.701 85.481 6.003 1.00 40.92 ? 154 TRP B CA 1 ATOM 2827 C C . TRP B 1 133 ? 17.961 84.083 5.463 1.00 39.03 ? 154 TRP B C 1 ATOM 2828 O O . TRP B 1 133 ? 17.124 83.208 5.644 1.00 40.17 ? 154 TRP B O 1 ATOM 2829 C CB . TRP B 1 133 ? 16.647 86.187 5.142 1.00 42.87 ? 154 TRP B CB 1 ATOM 2830 C CG . TRP B 1 133 ? 17.088 86.434 3.718 1.00 43.97 ? 154 TRP B CG 1 ATOM 2831 C CD1 . TRP B 1 133 ? 17.070 85.531 2.652 1.00 43.75 ? 154 TRP B CD1 1 ATOM 2832 C CD2 . TRP B 1 133 ? 17.627 87.681 3.151 1.00 45.39 ? 154 TRP B CD2 1 ATOM 2833 N NE1 . TRP B 1 133 ? 17.558 86.113 1.507 1.00 43.74 ? 154 TRP B NE1 1 ATOM 2834 C CE2 . TRP B 1 133 ? 17.905 87.403 1.735 1.00 44.83 ? 154 TRP B CE2 1 ATOM 2835 C CE3 . TRP B 1 133 ? 17.909 88.948 3.659 1.00 46.58 ? 154 TRP B CE3 1 ATOM 2836 C CZ2 . TRP B 1 133 ? 18.429 88.369 0.885 1.00 45.71 ? 154 TRP B CZ2 1 ATOM 2837 C CZ3 . TRP B 1 133 ? 18.435 89.915 2.789 1.00 47.05 ? 154 TRP B CZ3 1 ATOM 2838 C CH2 . TRP B 1 133 ? 18.693 89.629 1.438 1.00 46.48 ? 154 TRP B CH2 1 ATOM 2839 N N . ASP B 1 134 ? 19.095 83.867 4.796 1.00 38.28 ? 155 ASP B N 1 ATOM 2840 C CA . ASP B 1 134 ? 19.387 82.586 4.125 1.00 36.93 ? 155 ASP B CA 1 ATOM 2841 C C . ASP B 1 134 ? 20.019 81.564 5.072 1.00 38.74 ? 155 ASP B C 1 ATOM 2842 O O . ASP B 1 134 ? 20.629 81.945 6.071 1.00 38.38 ? 155 ASP B O 1 ATOM 2843 C CB . ASP B 1 134 ? 20.366 82.791 2.959 1.00 36.26 ? 155 ASP B CB 1 ATOM 2844 C CG . ASP B 1 134 ? 19.688 83.231 1.649 1.00 34.45 ? 155 ASP B CG 1 ATOM 2845 O OD1 . ASP B 1 134 ? 18.519 82.874 1.339 1.00 32.76 ? 155 ASP B OD1 1 ATOM 2846 O OD2 . ASP B 1 134 ? 20.393 83.928 0.895 1.00 36.58 ? 155 ASP B OD2 1 ATOM 2847 N N . PRO B 1 135 ? 19.887 80.255 4.750 1.00 37.13 ? 156 PRO B N 1 ATOM 2848 C CA . PRO B 1 135 ? 20.792 79.239 5.285 1.00 36.18 ? 156 PRO B CA 1 ATOM 2849 C C . PRO B 1 135 ? 22.180 79.428 4.684 1.00 37.42 ? 156 PRO B C 1 ATOM 2850 O O . PRO B 1 135 ? 22.301 79.990 3.592 1.00 38.69 ? 156 PRO B O 1 ATOM 2851 C CB . PRO B 1 135 ? 20.191 77.926 4.773 1.00 35.69 ? 156 PRO B CB 1 ATOM 2852 C CG . PRO B 1 135 ? 19.389 78.315 3.573 1.00 34.00 ? 156 PRO B CG 1 ATOM 2853 C CD . PRO B 1 135 ? 18.820 79.656 3.923 1.00 36.24 ? 156 PRO B CD 1 ATOM 2854 N N . LYS B 1 136 ? 23.210 78.956 5.377 1.00 36.22 ? 157 LYS B N 1 ATOM 2855 C CA . LYS B 1 136 ? 24.593 79.168 4.943 1.00 39.49 ? 157 LYS B CA 1 ATOM 2856 C C . LYS B 1 136 ? 25.000 78.487 3.623 1.00 38.53 ? 157 LYS B C 1 ATOM 2857 O O . LYS B 1 136 ? 25.666 79.115 2.791 1.00 38.53 ? 157 LYS B O 1 ATOM 2858 C CB . LYS B 1 136 ? 25.572 78.839 6.075 1.00 41.44 ? 157 LYS B CB 1 ATOM 2859 C CG . LYS B 1 136 ? 25.561 79.902 7.161 1.00 45.49 ? 157 LYS B CG 1 ATOM 2860 C CD . LYS B 1 136 ? 26.552 79.625 8.278 1.00 48.83 ? 157 LYS B CD 1 ATOM 2861 C CE . LYS B 1 136 ? 26.537 80.767 9.284 1.00 48.69 ? 157 LYS B CE 1 ATOM 2862 N NZ . LYS B 1 136 ? 27.378 80.454 10.472 1.00 53.30 ? 157 LYS B NZ 1 ATOM 2863 N N . PRO B 1 137 ? 24.608 77.210 3.421 1.00 37.31 ? 158 PRO B N 1 ATOM 2864 C CA . PRO B 1 137 ? 24.943 76.597 2.132 1.00 35.53 ? 158 PRO B CA 1 ATOM 2865 C C . PRO B 1 137 ? 24.049 77.122 1.007 1.00 32.48 ? 158 PRO B C 1 ATOM 2866 O O . PRO B 1 137 ? 22.912 77.526 1.258 1.00 32.08 ? 158 PRO B O 1 ATOM 2867 C CB . PRO B 1 137 ? 24.674 75.095 2.361 1.00 35.46 ? 158 PRO B CB 1 ATOM 2868 C CG . PRO B 1 137 ? 24.263 74.941 3.796 1.00 37.01 ? 158 PRO B CG 1 ATOM 2869 C CD . PRO B 1 137 ? 23.859 76.288 4.295 1.00 36.95 ? 158 PRO B CD 1 ATOM 2870 N N . ARG B 1 138 ? 24.567 77.113 -0.218 1.00 31.97 ? 159 ARG B N 1 ATOM 2871 C CA . ARG B 1 138 ? 23.758 77.416 -1.394 1.00 32.62 ? 159 ARG B CA 1 ATOM 2872 C C . ARG B 1 138 ? 22.575 76.438 -1.437 1.00 31.41 ? 159 ARG B C 1 ATOM 2873 O O . ARG B 1 138 ? 22.688 75.303 -0.957 1.00 31.71 ? 159 ARG B O 1 ATOM 2874 C CB . ARG B 1 138 ? 24.608 77.330 -2.654 1.00 33.45 ? 159 ARG B CB 1 ATOM 2875 C CG . ARG B 1 138 ? 25.602 78.478 -2.744 1.00 35.37 ? 159 ARG B CG 1 ATOM 2876 C CD . ARG B 1 138 ? 26.560 78.326 -3.902 1.00 38.17 ? 159 ARG B CD 1 ATOM 2877 N NE . ARG B 1 138 ? 27.593 79.359 -3.848 1.00 38.42 ? 159 ARG B NE 1 ATOM 2878 C CZ . ARG B 1 138 ? 28.876 79.130 -3.605 1.00 39.56 ? 159 ARG B CZ 1 ATOM 2879 N NH1 . ARG B 1 138 ? 29.318 77.898 -3.411 1.00 40.77 ? 159 ARG B NH1 1 ATOM 2880 N NH2 . ARG B 1 138 ? 29.727 80.146 -3.573 1.00 41.91 ? 159 ARG B NH2 1 ATOM 2881 N N . HIS B 1 139 ? 21.447 76.891 -1.981 1.00 31.80 ? 160 HIS B N 1 ATOM 2882 C CA . HIS B 1 139 ? 20.171 76.225 -1.731 1.00 31.09 ? 160 HIS B CA 1 ATOM 2883 C C . HIS B 1 139 ? 19.137 76.383 -2.813 1.00 31.67 ? 160 HIS B C 1 ATOM 2884 O O . HIS B 1 139 ? 19.151 77.347 -3.584 1.00 29.38 ? 160 HIS B O 1 ATOM 2885 C CB . HIS B 1 139 ? 19.586 76.675 -0.383 1.00 31.78 ? 160 HIS B CB 1 ATOM 2886 C CG . HIS B 1 139 ? 19.445 78.185 -0.234 1.00 32.70 ? 160 HIS B CG 1 ATOM 2887 N ND1 . HIS B 1 139 ? 20.472 78.967 0.140 1.00 33.24 ? 160 HIS B ND1 1 ATOM 2888 C CD2 . HIS B 1 139 ? 18.344 79.035 -0.401 1.00 32.82 ? 160 HIS B CD2 1 ATOM 2889 C CE1 . HIS B 1 139 ? 20.069 80.252 0.198 1.00 33.61 ? 160 HIS B CE1 1 ATOM 2890 N NE2 . HIS B 1 139 ? 18.763 80.302 -0.130 1.00 33.42 ? 160 HIS B NE2 1 ATOM 2891 N N . ILE B 1 140 ? 18.237 75.402 -2.883 1.00 29.61 ? 161 ILE B N 1 ATOM 2892 C CA . ILE B 1 140 ? 16.968 75.571 -3.567 1.00 30.07 ? 161 ILE B CA 1 ATOM 2893 C C . ILE B 1 140 ? 15.946 75.938 -2.500 1.00 29.98 ? 161 ILE B C 1 ATOM 2894 O O . ILE B 1 140 ? 15.901 75.308 -1.443 1.00 31.02 ? 161 ILE B O 1 ATOM 2895 C CB . ILE B 1 140 ? 16.509 74.269 -4.262 1.00 30.31 ? 161 ILE B CB 1 ATOM 2896 C CG1 . ILE B 1 140 ? 17.562 73.790 -5.268 1.00 32.23 ? 161 ILE B CG1 1 ATOM 2897 C CG2 . ILE B 1 140 ? 15.158 74.477 -4.928 1.00 30.89 ? 161 ILE B CG2 1 ATOM 2898 C CD1 . ILE B 1 140 ? 17.399 72.336 -5.683 1.00 34.82 ? 161 ILE B CD1 1 ATOM 2899 N N . GLY B 1 141 ? 15.134 76.956 -2.767 1.00 28.71 ? 162 GLY B N 1 ATOM 2900 C CA . GLY B 1 141 ? 14.123 77.386 -1.814 1.00 28.09 ? 162 GLY B CA 1 ATOM 2901 C C . GLY B 1 141 ? 12.760 77.615 -2.426 1.00 29.17 ? 162 GLY B C 1 ATOM 2902 O O . GLY B 1 141 ? 12.645 77.980 -3.603 1.00 29.53 ? 162 GLY B O 1 ATOM 2903 N N . ILE B 1 142 ? 11.729 77.401 -1.613 1.00 28.27 ? 163 ILE B N 1 ATOM 2904 C CA . ILE B 1 142 ? 10.354 77.726 -1.964 1.00 27.91 ? 163 ILE B CA 1 ATOM 2905 C C . ILE B 1 142 ? 10.013 79.040 -1.262 1.00 30.12 ? 163 ILE B C 1 ATOM 2906 O O . ILE B 1 142 ? 10.006 79.105 -0.021 1.00 28.30 ? 163 ILE B O 1 ATOM 2907 C CB . ILE B 1 142 ? 9.367 76.607 -1.550 1.00 27.63 ? 163 ILE B CB 1 ATOM 2908 C CG1 . ILE B 1 142 ? 9.641 75.332 -2.369 1.00 26.67 ? 163 ILE B CG1 1 ATOM 2909 C CG2 . ILE B 1 142 ? 7.919 77.036 -1.748 1.00 26.93 ? 163 ILE B CG2 1 ATOM 2910 C CD1 . ILE B 1 142 ? 8.957 74.095 -1.825 1.00 26.21 ? 163 ILE B CD1 1 ATOM 2911 N N . ASP B 1 143 ? 9.743 80.073 -2.066 1.00 31.50 ? 164 ASP B N 1 ATOM 2912 C CA . ASP B 1 143 ? 9.432 81.428 -1.563 1.00 32.55 ? 164 ASP B CA 1 ATOM 2913 C C . ASP B 1 143 ? 7.954 81.756 -1.716 1.00 34.47 ? 164 ASP B C 1 ATOM 2914 O O . ASP B 1 143 ? 7.388 81.653 -2.813 1.00 34.70 ? 164 ASP B O 1 ATOM 2915 C CB . ASP B 1 143 ? 10.274 82.488 -2.288 1.00 32.32 ? 164 ASP B CB 1 ATOM 2916 C CG . ASP B 1 143 ? 11.764 82.240 -2.174 1.00 33.52 ? 164 ASP B CG 1 ATOM 2917 O OD1 . ASP B 1 143 ? 12.180 81.384 -1.372 1.00 35.43 ? 164 ASP B OD1 1 ATOM 2918 O OD2 . ASP B 1 143 ? 12.544 82.897 -2.895 1.00 34.25 ? 164 ASP B OD2 1 ATOM 2919 N N . VAL B 1 144 ? 7.323 82.138 -0.608 1.00 32.57 ? 165 VAL B N 1 ATOM 2920 C CA . VAL B 1 144 ? 5.937 82.553 -0.613 1.00 33.40 ? 165 VAL B CA 1 ATOM 2921 C C . VAL B 1 144 ? 5.881 83.921 0.081 1.00 36.66 ? 165 VAL B C 1 ATOM 2922 O O . VAL B 1 144 ? 6.055 84.017 1.303 1.00 36.78 ? 165 VAL B O 1 ATOM 2923 C CB . VAL B 1 144 ? 5.025 81.543 0.105 1.00 32.81 ? 165 VAL B CB 1 ATOM 2924 C CG1 . VAL B 1 144 ? 3.593 82.042 0.149 1.00 33.05 ? 165 VAL B CG1 1 ATOM 2925 C CG2 . VAL B 1 144 ? 5.079 80.174 -0.580 1.00 34.47 ? 165 VAL B CG2 1 ATOM 2926 N N . ASN B 1 145 ? 5.675 84.968 -0.716 1.00 37.34 ? 166 ASN B N 1 ATOM 2927 C CA . ASN B 1 145 ? 5.543 86.339 -0.199 1.00 38.54 ? 166 ASN B CA 1 ATOM 2928 C C . ASN B 1 145 ? 6.723 86.847 0.659 1.00 40.01 ? 166 ASN B C 1 ATOM 2929 O O . ASN B 1 145 ? 6.583 87.833 1.390 1.00 42.37 ? 166 ASN B O 1 ATOM 2930 C CB . ASN B 1 145 ? 4.211 86.489 0.556 1.00 38.22 ? 166 ASN B CB 1 ATOM 2931 C CG . ASN B 1 145 ? 3.015 86.613 -0.374 1.00 37.44 ? 166 ASN B CG 1 ATOM 2932 O OD1 . ASN B 1 145 ? 3.149 86.984 -1.544 1.00 40.30 ? 166 ASN B OD1 1 ATOM 2933 N ND2 . ASN B 1 145 ? 1.837 86.323 0.148 1.00 36.20 ? 166 ASN B ND2 1 ATOM 2934 N N . SER B 1 146 ? 7.877 86.189 0.550 1.00 37.68 ? 167 SER B N 1 ATOM 2935 C CA . SER B 1 146 ? 9.087 86.575 1.280 1.00 38.40 ? 167 SER B CA 1 ATOM 2936 C C . SER B 1 146 ? 10.334 85.982 0.646 1.00 38.06 ? 167 SER B C 1 ATOM 2937 O O . SER B 1 146 ? 10.292 84.883 0.076 1.00 38.43 ? 167 SER B O 1 ATOM 2938 C CB . SER B 1 146 ? 8.999 86.132 2.744 1.00 38.62 ? 167 SER B CB 1 ATOM 2939 O OG . SER B 1 146 ? 10.226 86.369 3.408 1.00 38.80 ? 167 SER B OG 1 ATOM 2940 N N . ILE B 1 147 ? 11.446 86.707 0.743 1.00 36.07 ? 168 ILE B N 1 ATOM 2941 C CA . ILE B 1 147 ? 12.750 86.192 0.330 1.00 35.22 ? 168 ILE B CA 1 ATOM 2942 C C . ILE B 1 147 ? 13.276 85.157 1.337 1.00 34.99 ? 168 ILE B C 1 ATOM 2943 O O . ILE B 1 147 ? 14.248 84.455 1.061 1.00 33.66 ? 168 ILE B O 1 ATOM 2944 C CB . ILE B 1 147 ? 13.793 87.325 0.122 1.00 36.88 ? 168 ILE B CB 1 ATOM 2945 C CG1 . ILE B 1 147 ? 15.014 86.852 -0.688 1.00 35.86 ? 168 ILE B CG1 1 ATOM 2946 C CG2 . ILE B 1 147 ? 14.273 87.880 1.458 1.00 38.10 ? 168 ILE B CG2 1 ATOM 2947 C CD1 . ILE B 1 147 ? 14.741 86.562 -2.154 1.00 37.05 ? 168 ILE B CD1 1 ATOM 2948 N N . LYS B 1 148 ? 12.653 85.092 2.511 1.00 35.41 ? 169 LYS B N 1 ATOM 2949 C CA . LYS B 1 148 ? 13.013 84.077 3.493 1.00 37.45 ? 169 LYS B CA 1 ATOM 2950 C C . LYS B 1 148 ? 12.197 82.830 3.180 1.00 35.36 ? 169 LYS B C 1 ATOM 2951 O O . LYS B 1 148 ? 11.012 82.746 3.530 1.00 35.80 ? 169 LYS B O 1 ATOM 2952 C CB . LYS B 1 148 ? 12.770 84.549 4.933 1.00 38.54 ? 169 LYS B CB 1 ATOM 2953 C CG . LYS B 1 148 ? 13.517 83.692 5.946 1.00 40.59 ? 169 LYS B CG 1 ATOM 2954 C CD . LYS B 1 148 ? 13.003 83.858 7.368 1.00 41.94 ? 169 LYS B CD 1 ATOM 2955 C CE . LYS B 1 148 ? 13.814 82.986 8.313 1.00 44.48 ? 169 LYS B CE 1 ATOM 2956 N NZ . LYS B 1 148 ? 13.224 82.910 9.676 1.00 45.79 ? 169 LYS B NZ 1 ATOM 2957 N N . SER B 1 149 ? 12.835 81.883 2.493 1.00 33.92 ? 170 SER B N 1 ATOM 2958 C CA . SER B 1 149 ? 12.140 80.690 1.985 1.00 33.49 ? 170 SER B CA 1 ATOM 2959 C C . SER B 1 149 ? 11.389 79.972 3.092 1.00 33.42 ? 170 SER B C 1 ATOM 2960 O O . SER B 1 149 ? 11.887 79.878 4.211 1.00 35.68 ? 170 SER B O 1 ATOM 2961 C CB . SER B 1 149 ? 13.137 79.720 1.354 1.00 30.96 ? 170 SER B CB 1 ATOM 2962 O OG . SER B 1 149 ? 13.896 80.324 0.323 1.00 32.22 ? 170 SER B OG 1 ATOM 2963 N N . ILE B 1 150 ? 10.191 79.474 2.788 1.00 32.73 ? 171 ILE B N 1 ATOM 2964 C CA . ILE B 1 150 ? 9.458 78.626 3.736 1.00 32.93 ? 171 ILE B CA 1 ATOM 2965 C C . ILE B 1 150 ? 10.117 77.249 3.898 1.00 32.84 ? 171 ILE B C 1 ATOM 2966 O O . ILE B 1 150 ? 9.927 76.578 4.912 1.00 32.04 ? 171 ILE B O 1 ATOM 2967 C CB . ILE B 1 150 ? 7.964 78.459 3.372 1.00 33.50 ? 171 ILE B CB 1 ATOM 2968 C CG1 . ILE B 1 150 ? 7.785 77.678 2.061 1.00 32.10 ? 171 ILE B CG1 1 ATOM 2969 C CG2 . ILE B 1 150 ? 7.267 79.816 3.309 1.00 34.68 ? 171 ILE B CG2 1 ATOM 2970 C CD1 . ILE B 1 150 ? 6.342 77.306 1.784 1.00 31.92 ? 171 ILE B CD1 1 ATOM 2971 N N . LYS B 1 151 ? 10.890 76.836 2.898 1.00 31.11 ? 172 LYS B N 1 ATOM 2972 C CA . LYS B 1 151 ? 11.547 75.533 2.920 1.00 32.04 ? 172 LYS B CA 1 ATOM 2973 C C . LYS B 1 151 ? 12.735 75.577 1.981 1.00 30.30 ? 172 LYS B C 1 ATOM 2974 O O . LYS B 1 151 ? 12.644 76.125 0.884 1.00 29.44 ? 172 LYS B O 1 ATOM 2975 C CB . LYS B 1 151 ? 10.578 74.428 2.481 1.00 32.99 ? 172 LYS B CB 1 ATOM 2976 C CG . LYS B 1 151 ? 10.990 73.021 2.898 1.00 35.08 ? 172 LYS B CG 1 ATOM 2977 C CD . LYS B 1 151 ? 10.448 72.675 4.273 1.00 37.12 ? 172 LYS B CD 1 ATOM 2978 C CE . LYS B 1 151 ? 10.946 71.318 4.744 1.00 38.90 ? 172 LYS B CE 1 ATOM 2979 N NZ . LYS B 1 151 ? 10.334 70.213 3.952 1.00 41.28 ? 172 LYS B NZ 1 ATOM 2980 N N . THR B 1 152 ? 13.856 75.018 2.414 1.00 28.72 ? 173 THR B N 1 ATOM 2981 C CA . THR B 1 152 ? 15.030 74.941 1.555 1.00 29.03 ? 173 THR B CA 1 ATOM 2982 C C . THR B 1 152 ? 15.643 73.553 1.585 1.00 28.24 ? 173 THR B C 1 ATOM 2983 O O . THR B 1 152 ? 15.376 72.764 2.488 1.00 27.95 ? 173 THR B O 1 ATOM 2984 C CB . THR B 1 152 ? 16.133 75.958 1.947 1.00 31.15 ? 173 THR B CB 1 ATOM 2985 O OG1 . THR B 1 152 ? 16.537 75.728 3.295 1.00 31.95 ? 173 THR B OG1 1 ATOM 2986 C CG2 . THR B 1 152 ? 15.658 77.393 1.810 1.00 30.56 ? 173 THR B CG2 1 ATOM 2987 N N . THR B 1 153 ? 16.446 73.252 0.572 1.00 28.30 ? 174 THR B N 1 ATOM 2988 C CA . THR B 1 153 ? 17.347 72.125 0.635 1.00 27.35 ? 174 THR B CA 1 ATOM 2989 C C . THR B 1 153 ? 18.725 72.579 0.179 1.00 27.78 ? 174 THR B C 1 ATOM 2990 O O . THR B 1 153 ? 18.850 73.503 -0.633 1.00 27.64 ? 174 THR B O 1 ATOM 2991 C CB . THR B 1 153 ? 16.846 70.907 -0.188 1.00 27.52 ? 174 THR B CB 1 ATOM 2992 O OG1 . THR B 1 153 ? 17.554 69.730 0.231 1.00 27.64 ? 174 THR B OG1 1 ATOM 2993 C CG2 . THR B 1 153 ? 17.047 71.111 -1.695 1.00 26.59 ? 174 THR B CG2 1 ATOM 2994 N N . THR B 1 154 ? 19.756 71.923 0.691 1.00 28.50 ? 175 THR B N 1 ATOM 2995 C CA . THR B 1 154 ? 21.119 72.197 0.256 1.00 30.23 ? 175 THR B CA 1 ATOM 2996 C C . THR B 1 154 ? 21.291 71.878 -1.237 1.00 31.61 ? 175 THR B C 1 ATOM 2997 O O . THR B 1 154 ? 20.842 70.822 -1.722 1.00 29.77 ? 175 THR B O 1 ATOM 2998 C CB . THR B 1 154 ? 22.117 71.412 1.108 1.00 31.11 ? 175 THR B CB 1 ATOM 2999 O OG1 . THR B 1 154 ? 22.018 71.881 2.452 1.00 33.23 ? 175 THR B OG1 1 ATOM 3000 C CG2 . THR B 1 154 ? 23.562 71.601 0.611 1.00 31.46 ? 175 THR B CG2 1 ATOM 3001 N N . TRP B 1 155 ? 21.926 72.808 -1.949 1.00 29.96 ? 176 TRP B N 1 ATOM 3002 C CA . TRP B 1 155 ? 22.259 72.649 -3.361 1.00 30.00 ? 176 TRP B CA 1 ATOM 3003 C C . TRP B 1 155 ? 23.741 72.792 -3.533 1.00 32.82 ? 176 TRP B C 1 ATOM 3004 O O . TRP B 1 155 ? 24.315 73.850 -3.229 1.00 33.78 ? 176 TRP B O 1 ATOM 3005 C CB . TRP B 1 155 ? 21.487 73.674 -4.185 1.00 29.31 ? 176 TRP B CB 1 ATOM 3006 C CG . TRP B 1 155 ? 21.883 73.835 -5.643 1.00 28.64 ? 176 TRP B CG 1 ATOM 3007 C CD1 . TRP B 1 155 ? 22.246 72.839 -6.557 1.00 28.95 ? 176 TRP B CD1 1 ATOM 3008 C CD2 . TRP B 1 155 ? 21.896 75.083 -6.417 1.00 28.86 ? 176 TRP B CD2 1 ATOM 3009 N NE1 . TRP B 1 155 ? 22.495 73.378 -7.799 1.00 29.28 ? 176 TRP B NE1 1 ATOM 3010 C CE2 . TRP B 1 155 ? 22.314 74.719 -7.781 1.00 28.70 ? 176 TRP B CE2 1 ATOM 3011 C CE3 . TRP B 1 155 ? 21.640 76.420 -6.122 1.00 29.38 ? 176 TRP B CE3 1 ATOM 3012 C CZ2 . TRP B 1 155 ? 22.452 75.666 -8.781 1.00 29.15 ? 176 TRP B CZ2 1 ATOM 3013 C CZ3 . TRP B 1 155 ? 21.783 77.369 -7.147 1.00 30.82 ? 176 TRP B CZ3 1 ATOM 3014 C CH2 . TRP B 1 155 ? 22.178 76.996 -8.443 1.00 29.34 ? 176 TRP B CH2 1 ATOM 3015 N N . ASP B 1 156 ? 24.376 71.722 -4.002 1.00 32.19 ? 177 ASP B N 1 ATOM 3016 C CA . ASP B 1 156 ? 25.807 71.727 -4.280 1.00 33.80 ? 177 ASP B CA 1 ATOM 3017 C C . ASP B 1 156 ? 26.052 72.316 -5.666 1.00 34.43 ? 177 ASP B C 1 ATOM 3018 O O . ASP B 1 156 ? 26.341 71.595 -6.620 1.00 34.14 ? 177 ASP B O 1 ATOM 3019 C CB . ASP B 1 156 ? 26.423 70.330 -4.153 1.00 34.71 ? 177 ASP B CB 1 ATOM 3020 C CG . ASP B 1 156 ? 26.212 69.714 -2.779 1.00 37.10 ? 177 ASP B CG 1 ATOM 3021 O OD1 . ASP B 1 156 ? 26.243 70.444 -1.768 1.00 40.60 ? 177 ASP B OD1 1 ATOM 3022 O OD2 . ASP B 1 156 ? 26.009 68.492 -2.704 1.00 37.49 ? 177 ASP B OD2 1 ATOM 3023 N N . PHE B 1 157 ? 25.914 73.641 -5.749 1.00 35.52 ? 178 PHE B N 1 ATOM 3024 C CA . PHE B 1 157 ? 26.168 74.412 -6.968 1.00 35.65 ? 178 PHE B CA 1 ATOM 3025 C C . PHE B 1 157 ? 27.530 74.117 -7.583 1.00 34.69 ? 178 PHE B C 1 ATOM 3026 O O . PHE B 1 157 ? 28.545 74.052 -6.876 1.00 34.70 ? 178 PHE B O 1 ATOM 3027 C CB . PHE B 1 157 ? 26.047 75.915 -6.673 1.00 36.91 ? 178 PHE B CB 1 ATOM 3028 C CG . PHE B 1 157 ? 26.647 76.796 -7.741 1.00 38.34 ? 178 PHE B CG 1 ATOM 3029 C CD1 . PHE B 1 157 ? 25.907 77.144 -8.870 1.00 37.04 ? 178 PHE B CD1 1 ATOM 3030 C CD2 . PHE B 1 157 ? 27.961 77.271 -7.621 1.00 39.13 ? 178 PHE B CD2 1 ATOM 3031 C CE1 . PHE B 1 157 ? 26.460 77.945 -9.858 1.00 38.91 ? 178 PHE B CE1 1 ATOM 3032 C CE2 . PHE B 1 157 ? 28.520 78.071 -8.611 1.00 38.16 ? 178 PHE B CE2 1 ATOM 3033 C CZ . PHE B 1 157 ? 27.767 78.410 -9.728 1.00 38.93 ? 178 PHE B CZ 1 ATOM 3034 N N . VAL B 1 158 ? 27.546 73.928 -8.903 1.00 36.00 ? 179 VAL B N 1 ATOM 3035 C CA . VAL B 1 158 ? 28.797 73.804 -9.664 1.00 35.55 ? 179 VAL B CA 1 ATOM 3036 C C . VAL B 1 158 ? 28.700 74.707 -10.892 1.00 37.42 ? 179 VAL B C 1 ATOM 3037 O O . VAL B 1 158 ? 27.730 74.637 -11.652 1.00 37.55 ? 179 VAL B O 1 ATOM 3038 C CB . VAL B 1 158 ? 29.124 72.343 -10.054 1.00 34.64 ? 179 VAL B CB 1 ATOM 3039 C CG1 . VAL B 1 158 ? 30.437 72.262 -10.817 1.00 34.95 ? 179 VAL B CG1 1 ATOM 3040 C CG2 . VAL B 1 158 ? 29.202 71.457 -8.820 1.00 35.11 ? 179 VAL B CG2 1 ATOM 3041 N N . LYS B 1 159 ? 29.693 75.578 -11.065 1.00 37.58 ? 180 LYS B N 1 ATOM 3042 C CA . LYS B 1 159 ? 29.654 76.576 -12.138 1.00 37.14 ? 180 LYS B CA 1 ATOM 3043 C C . LYS B 1 159 ? 29.702 75.947 -13.536 1.00 35.38 ? 180 LYS B C 1 ATOM 3044 O O . LYS B 1 159 ? 30.381 74.947 -13.753 1.00 36.41 ? 180 LYS B O 1 ATOM 3045 C CB . LYS B 1 159 ? 30.765 77.633 -11.961 1.00 37.28 ? 180 LYS B CB 1 ATOM 3046 C CG . LYS B 1 159 ? 32.187 77.098 -12.023 1.00 40.89 ? 180 LYS B CG 1 ATOM 3047 C CD . LYS B 1 159 ? 33.220 78.224 -11.947 1.00 41.32 ? 180 LYS B CD 1 ATOM 3048 C CE . LYS B 1 159 ? 34.602 77.706 -12.328 1.00 43.57 ? 180 LYS B CE 1 ATOM 3049 N NZ . LYS B 1 159 ? 35.597 78.798 -12.540 1.00 44.66 ? 180 LYS B NZ 1 ATOM 3050 N N . GLY B 1 160 ? 28.937 76.531 -14.457 1.00 37.10 ? 181 GLY B N 1 ATOM 3051 C CA . GLY B 1 160 ? 28.999 76.183 -15.878 1.00 38.78 ? 181 GLY B CA 1 ATOM 3052 C C . GLY B 1 160 ? 28.433 74.825 -16.263 1.00 38.78 ? 181 GLY B C 1 ATOM 3053 O O . GLY B 1 160 ? 28.543 74.415 -17.415 1.00 38.17 ? 181 GLY B O 1 ATOM 3054 N N . GLU B 1 161 ? 27.828 74.128 -15.303 1.00 38.20 ? 182 GLU B N 1 ATOM 3055 C CA . GLU B 1 161 ? 27.228 72.822 -15.569 1.00 37.03 ? 182 GLU B CA 1 ATOM 3056 C C . GLU B 1 161 ? 25.743 73.000 -15.819 1.00 34.16 ? 182 GLU B C 1 ATOM 3057 O O . GLU B 1 161 ? 25.058 73.675 -15.037 1.00 31.29 ? 182 GLU B O 1 ATOM 3058 C CB . GLU B 1 161 ? 27.445 71.874 -14.391 1.00 39.35 ? 182 GLU B CB 1 ATOM 3059 C CG . GLU B 1 161 ? 28.896 71.497 -14.135 1.00 44.62 ? 182 GLU B CG 1 ATOM 3060 C CD . GLU B 1 161 ? 29.468 70.546 -15.170 1.00 48.99 ? 182 GLU B CD 1 ATOM 3061 O OE1 . GLU B 1 161 ? 28.698 69.969 -15.967 1.00 52.21 ? 182 GLU B OE1 1 ATOM 3062 O OE2 . GLU B 1 161 ? 30.703 70.372 -15.190 1.00 52.47 ? 182 GLU B OE2 1 ATOM 3063 N N . ASN B 1 162 ? 25.242 72.413 -16.908 1.00 30.39 ? 183 ASN B N 1 ATOM 3064 C CA . ASN B 1 162 ? 23.809 72.480 -17.194 1.00 30.03 ? 183 ASN B CA 1 ATOM 3065 C C . ASN B 1 162 ? 23.017 71.847 -16.045 1.00 26.99 ? 183 ASN B C 1 ATOM 3066 O O . ASN B 1 162 ? 23.349 70.754 -15.596 1.00 27.65 ? 183 ASN B O 1 ATOM 3067 C CB . ASN B 1 162 ? 23.473 71.795 -18.533 1.00 30.88 ? 183 ASN B CB 1 ATOM 3068 C CG . ASN B 1 162 ? 23.735 72.687 -19.746 1.00 34.23 ? 183 ASN B CG 1 ATOM 3069 O OD1 . ASN B 1 162 ? 24.261 73.800 -19.629 1.00 33.85 ? 183 ASN B OD1 1 ATOM 3070 N ND2 . ASN B 1 162 ? 23.354 72.200 -20.924 1.00 33.44 ? 183 ASN B ND2 1 ATOM 3071 N N . ALA B 1 163 ? 21.997 72.561 -15.580 1.00 27.16 ? 184 ALA B N 1 ATOM 3072 C CA . ALA B 1 163 ? 21.109 72.086 -14.513 1.00 26.55 ? 184 ALA B CA 1 ATOM 3073 C C . ALA B 1 163 ? 19.704 71.901 -15.058 1.00 26.04 ? 184 ALA B C 1 ATOM 3074 O O . ALA B 1 163 ? 19.171 72.791 -15.703 1.00 26.16 ? 184 ALA B O 1 ATOM 3075 C CB . ALA B 1 163 ? 21.078 73.078 -13.363 1.00 25.33 ? 184 ALA B CB 1 ATOM 3076 N N . GLU B 1 164 ? 19.096 70.755 -14.761 1.00 27.17 ? 185 GLU B N 1 ATOM 3077 C CA . GLU B 1 164 ? 17.731 70.477 -15.218 1.00 26.75 ? 185 GLU B CA 1 ATOM 3078 C C . GLU B 1 164 ? 16.762 70.497 -14.057 1.00 24.37 ? 185 GLU B C 1 ATOM 3079 O O . GLU B 1 164 ? 16.902 69.728 -13.112 1.00 24.91 ? 185 GLU B O 1 ATOM 3080 C CB . GLU B 1 164 ? 17.677 69.127 -15.933 1.00 29.26 ? 185 GLU B CB 1 ATOM 3081 C CG . GLU B 1 164 ? 18.380 69.146 -17.279 1.00 32.27 ? 185 GLU B CG 1 ATOM 3082 C CD . GLU B 1 164 ? 18.481 67.776 -17.910 1.00 35.03 ? 185 GLU B CD 1 ATOM 3083 O OE1 . GLU B 1 164 ? 17.919 66.807 -17.360 1.00 38.23 ? 185 GLU B OE1 1 ATOM 3084 O OE2 . GLU B 1 164 ? 19.140 67.668 -18.957 1.00 38.19 ? 185 GLU B OE2 1 ATOM 3085 N N . VAL B 1 165 ? 15.779 71.376 -14.139 1.00 24.05 ? 186 VAL B N 1 ATOM 3086 C CA . VAL B 1 165 ? 14.838 71.563 -13.054 1.00 23.22 ? 186 VAL B CA 1 ATOM 3087 C C . VAL B 1 165 ? 13.470 71.013 -13.401 1.00 23.17 ? 186 VAL B C 1 ATOM 3088 O O . VAL B 1 165 ? 13.018 71.146 -14.529 1.00 23.30 ? 186 VAL B O 1 ATOM 3089 C CB . VAL B 1 165 ? 14.725 73.062 -12.681 1.00 22.85 ? 186 VAL B CB 1 ATOM 3090 C CG1 . VAL B 1 165 ? 13.580 73.304 -11.705 1.00 22.68 ? 186 VAL B CG1 1 ATOM 3091 C CG2 . VAL B 1 165 ? 16.057 73.545 -12.106 1.00 24.66 ? 186 VAL B CG2 1 ATOM 3092 N N . LEU B 1 166 ? 12.810 70.409 -12.414 1.00 23.07 ? 187 LEU B N 1 ATOM 3093 C CA . LEU B 1 166 ? 11.400 70.075 -12.533 1.00 22.21 ? 187 LEU B CA 1 ATOM 3094 C C . LEU B 1 166 ? 10.663 70.629 -11.326 1.00 21.97 ? 187 LEU B C 1 ATOM 3095 O O . LEU B 1 166 ? 11.036 70.344 -10.179 1.00 23.50 ? 187 LEU B O 1 ATOM 3096 C CB . LEU B 1 166 ? 11.200 68.547 -12.614 1.00 22.17 ? 187 LEU B CB 1 ATOM 3097 C CG . LEU B 1 166 ? 9.734 68.089 -12.667 1.00 22.38 ? 187 LEU B CG 1 ATOM 3098 C CD1 . LEU B 1 166 ? 9.003 68.593 -13.918 1.00 22.73 ? 187 LEU B CD1 1 ATOM 3099 C CD2 . LEU B 1 166 ? 9.601 66.566 -12.559 1.00 22.07 ? 187 LEU B CD2 1 ATOM 3100 N N . ILE B 1 167 ? 9.618 71.407 -11.581 1.00 22.44 ? 188 ILE B N 1 ATOM 3101 C CA . ILE B 1 167 ? 8.768 71.908 -10.510 1.00 22.70 ? 188 ILE B CA 1 ATOM 3102 C C . ILE B 1 167 ? 7.347 71.464 -10.763 1.00 23.24 ? 188 ILE B C 1 ATOM 3103 O O . ILE B 1 167 ? 6.843 71.631 -11.866 1.00 23.65 ? 188 ILE B O 1 ATOM 3104 C CB . ILE B 1 167 ? 8.829 73.445 -10.413 1.00 22.59 ? 188 ILE B CB 1 ATOM 3105 C CG1 . ILE B 1 167 ? 10.233 73.878 -9.991 1.00 23.59 ? 188 ILE B CG1 1 ATOM 3106 C CG2 . ILE B 1 167 ? 7.791 73.957 -9.429 1.00 23.46 ? 188 ILE B CG2 1 ATOM 3107 C CD1 . ILE B 1 167 ? 10.583 75.299 -10.384 1.00 24.78 ? 188 ILE B CD1 1 ATOM 3108 N N . THR B 1 168 ? 6.701 70.911 -9.740 1.00 23.51 ? 189 THR B N 1 ATOM 3109 C CA . THR B 1 168 ? 5.334 70.436 -9.878 1.00 23.35 ? 189 THR B CA 1 ATOM 3110 C C . THR B 1 168 ? 4.456 70.955 -8.750 1.00 24.09 ? 189 THR B C 1 ATOM 3111 O O . THR B 1 168 ? 4.903 71.108 -7.607 1.00 24.10 ? 189 THR B O 1 ATOM 3112 C CB . THR B 1 168 ? 5.256 68.889 -9.918 1.00 23.54 ? 189 THR B CB 1 ATOM 3113 O OG1 . THR B 1 168 ? 5.759 68.365 -8.686 1.00 23.82 ? 189 THR B OG1 1 ATOM 3114 C CG2 . THR B 1 168 ? 6.090 68.334 -11.067 1.00 23.37 ? 189 THR B CG2 1 ATOM 3115 N N . TYR B 1 169 ? 3.213 71.259 -9.090 1.00 23.47 ? 190 TYR B N 1 ATOM 3116 C CA . TYR B 1 169 ? 2.233 71.638 -8.099 1.00 25.89 ? 190 TYR B CA 1 ATOM 3117 C C . TYR B 1 169 ? 0.973 70.814 -8.265 1.00 26.32 ? 190 TYR B C 1 ATOM 3118 O O . TYR B 1 169 ? 0.368 70.794 -9.337 1.00 26.19 ? 190 TYR B O 1 ATOM 3119 C CB . TYR B 1 169 ? 1.906 73.145 -8.155 1.00 27.26 ? 190 TYR B CB 1 ATOM 3120 C CG . TYR B 1 169 ? 0.919 73.535 -7.079 1.00 28.26 ? 190 TYR B CG 1 ATOM 3121 C CD1 . TYR B 1 169 ? 1.355 73.791 -5.776 1.00 29.51 ? 190 TYR B CD1 1 ATOM 3122 C CD2 . TYR B 1 169 ? -0.453 73.597 -7.344 1.00 29.68 ? 190 TYR B CD2 1 ATOM 3123 C CE1 . TYR B 1 169 ? 0.457 74.111 -4.774 1.00 29.25 ? 190 TYR B CE1 1 ATOM 3124 C CE2 . TYR B 1 169 ? -1.358 73.918 -6.345 1.00 31.00 ? 190 TYR B CE2 1 ATOM 3125 C CZ . TYR B 1 169 ? -0.887 74.176 -5.062 1.00 30.67 ? 190 TYR B CZ 1 ATOM 3126 O OH . TYR B 1 169 ? -1.778 74.504 -4.067 1.00 31.87 ? 190 TYR B OH 1 ATOM 3127 N N . ASP B 1 170 ? 0.588 70.132 -7.193 1.00 26.74 ? 191 ASP B N 1 ATOM 3128 C CA . ASP B 1 170 ? -0.584 69.276 -7.193 1.00 28.52 ? 191 ASP B CA 1 ATOM 3129 C C . ASP B 1 170 ? -1.649 69.949 -6.343 1.00 29.83 ? 191 ASP B C 1 ATOM 3130 O O . ASP B 1 170 ? -1.490 70.065 -5.129 1.00 29.55 ? 191 ASP B O 1 ATOM 3131 C CB . ASP B 1 170 ? -0.209 67.893 -6.629 1.00 29.32 ? 191 ASP B CB 1 ATOM 3132 C CG . ASP B 1 170 ? -1.381 66.918 -6.591 1.00 31.79 ? 191 ASP B CG 1 ATOM 3133 O OD1 . ASP B 1 170 ? -2.546 67.334 -6.740 1.00 34.84 ? 191 ASP B OD1 1 ATOM 3134 O OD2 . ASP B 1 170 ? -1.131 65.710 -6.401 1.00 33.84 ? 191 ASP B OD2 1 ATOM 3135 N N . SER B 1 171 ? -2.735 70.399 -6.974 1.00 31.37 ? 192 SER B N 1 ATOM 3136 C CA . SER B 1 171 ? -3.761 71.151 -6.242 1.00 33.24 ? 192 SER B CA 1 ATOM 3137 C C . SER B 1 171 ? -4.598 70.288 -5.294 1.00 34.02 ? 192 SER B C 1 ATOM 3138 O O . SER B 1 171 ? -5.249 70.822 -4.390 1.00 35.83 ? 192 SER B O 1 ATOM 3139 C CB . SER B 1 171 ? -4.673 71.923 -7.202 1.00 34.72 ? 192 SER B CB 1 ATOM 3140 O OG . SER B 1 171 ? -5.299 71.033 -8.099 1.00 34.16 ? 192 SER B OG 1 ATOM 3141 N N . SER B 1 172 ? -4.582 68.969 -5.487 1.00 33.26 ? 193 SER B N 1 ATOM 3142 C CA . SER B 1 172 ? -5.340 68.077 -4.608 1.00 33.81 ? 193 SER B CA 1 ATOM 3143 C C . SER B 1 172 ? -4.636 67.874 -3.258 1.00 33.71 ? 193 SER B C 1 ATOM 3144 O O . SER B 1 172 ? -5.289 67.639 -2.255 1.00 34.05 ? 193 SER B O 1 ATOM 3145 C CB . SER B 1 172 ? -5.649 66.741 -5.284 1.00 34.55 ? 193 SER B CB 1 ATOM 3146 O OG . SER B 1 172 ? -4.481 65.968 -5.470 1.00 37.27 ? 193 SER B OG 1 ATOM 3147 N N . THR B 1 173 ? -3.312 67.998 -3.241 1.00 33.06 ? 194 THR B N 1 ATOM 3148 C CA . THR B 1 173 ? -2.543 67.890 -1.999 1.00 31.28 ? 194 THR B CA 1 ATOM 3149 C C . THR B 1 173 ? -1.928 69.214 -1.549 1.00 32.00 ? 194 THR B C 1 ATOM 3150 O O . THR B 1 173 ? -1.394 69.297 -0.436 1.00 34.25 ? 194 THR B O 1 ATOM 3151 C CB . THR B 1 173 ? -1.418 66.857 -2.134 1.00 30.14 ? 194 THR B CB 1 ATOM 3152 O OG1 . THR B 1 173 ? -0.493 67.308 -3.124 1.00 29.20 ? 194 THR B OG1 1 ATOM 3153 C CG2 . THR B 1 173 ? -1.966 65.500 -2.527 1.00 30.48 ? 194 THR B CG2 1 ATOM 3154 N N . LYS B 1 174 ? -2.006 70.237 -2.409 1.00 30.49 ? 195 LYS B N 1 ATOM 3155 C CA . LYS B 1 174 ? -1.338 71.541 -2.231 1.00 31.40 ? 195 LYS B CA 1 ATOM 3156 C C . LYS B 1 174 ? 0.192 71.464 -2.213 1.00 29.33 ? 195 LYS B C 1 ATOM 3157 O O . LYS B 1 174 ? 0.851 72.410 -1.792 1.00 30.05 ? 195 LYS B O 1 ATOM 3158 C CB . LYS B 1 174 ? -1.832 72.303 -0.982 1.00 33.24 ? 195 LYS B CB 1 ATOM 3159 C CG . LYS B 1 174 ? -3.327 72.589 -0.957 1.00 36.32 ? 195 LYS B CG 1 ATOM 3160 C CD . LYS B 1 174 ? -3.663 73.710 0.019 1.00 38.43 ? 195 LYS B CD 1 ATOM 3161 C CE . LYS B 1 174 ? -5.055 73.546 0.614 1.00 40.81 ? 195 LYS B CE 1 ATOM 3162 N NZ . LYS B 1 174 ? -6.083 73.185 -0.401 1.00 40.80 ? 195 LYS B NZ 1 ATOM 3163 N N . LEU B 1 175 ? 0.758 70.351 -2.677 1.00 28.97 ? 196 LEU B N 1 ATOM 3164 C CA . LEU B 1 175 ? 2.196 70.149 -2.559 1.00 27.46 ? 196 LEU B CA 1 ATOM 3165 C C . LEU B 1 175 ? 2.980 70.722 -3.734 1.00 27.58 ? 196 LEU B C 1 ATOM 3166 O O . LEU B 1 175 ? 2.754 70.350 -4.890 1.00 27.58 ? 196 LEU B O 1 ATOM 3167 C CB . LEU B 1 175 ? 2.535 68.661 -2.386 1.00 28.05 ? 196 LEU B CB 1 ATOM 3168 C CG . LEU B 1 175 ? 3.964 68.391 -1.895 1.00 28.45 ? 196 LEU B CG 1 ATOM 3169 C CD1 . LEU B 1 175 ? 4.140 68.854 -0.452 1.00 28.35 ? 196 LEU B CD1 1 ATOM 3170 C CD2 . LEU B 1 175 ? 4.327 66.920 -2.027 1.00 28.49 ? 196 LEU B CD2 1 ATOM 3171 N N . LEU B 1 176 ? 3.907 71.620 -3.418 1.00 26.16 ? 197 LEU B N 1 ATOM 3172 C CA . LEU B 1 176 ? 4.845 72.133 -4.390 1.00 26.69 ? 197 LEU B CA 1 ATOM 3173 C C . LEU B 1 176 ? 6.158 71.392 -4.206 1.00 25.63 ? 197 LEU B C 1 ATOM 3174 O O . LEU B 1 176 ? 6.729 71.397 -3.112 1.00 25.96 ? 197 LEU B O 1 ATOM 3175 C CB . LEU B 1 176 ? 5.043 73.651 -4.228 1.00 26.31 ? 197 LEU B CB 1 ATOM 3176 C CG . LEU B 1 176 ? 5.945 74.360 -5.249 1.00 27.64 ? 197 LEU B CG 1 ATOM 3177 C CD1 . LEU B 1 176 ? 5.336 74.328 -6.637 1.00 29.31 ? 197 LEU B CD1 1 ATOM 3178 C CD2 . LEU B 1 176 ? 6.194 75.809 -4.850 1.00 29.67 ? 197 LEU B CD2 1 ATOM 3179 N N . VAL B 1 177 ? 6.620 70.756 -5.283 1.00 24.60 ? 198 VAL B N 1 ATOM 3180 C CA . VAL B 1 177 ? 7.881 70.015 -5.289 1.00 22.53 ? 198 VAL B CA 1 ATOM 3181 C C . VAL B 1 177 ? 8.853 70.550 -6.330 1.00 22.61 ? 198 VAL B C 1 ATOM 3182 O O . VAL B 1 177 ? 8.488 70.759 -7.497 1.00 22.47 ? 198 VAL B O 1 ATOM 3183 C CB . VAL B 1 177 ? 7.659 68.501 -5.559 1.00 22.92 ? 198 VAL B CB 1 ATOM 3184 C CG1 . VAL B 1 177 ? 8.966 67.746 -5.412 1.00 22.15 ? 198 VAL B CG1 1 ATOM 3185 C CG2 . VAL B 1 177 ? 6.624 67.922 -4.613 1.00 22.55 ? 198 VAL B CG2 1 ATOM 3186 N N . ALA B 1 178 ? 10.101 70.765 -5.913 1.00 21.54 ? 199 ALA B N 1 ATOM 3187 C CA . ALA B 1 178 ? 11.110 71.293 -6.803 1.00 23.15 ? 199 ALA B CA 1 ATOM 3188 C C . ALA B 1 178 ? 12.356 70.420 -6.741 1.00 23.32 ? 199 ALA B C 1 ATOM 3189 O O . ALA B 1 178 ? 12.878 70.121 -5.657 1.00 22.61 ? 199 ALA B O 1 ATOM 3190 C CB . ALA B 1 178 ? 11.450 72.738 -6.436 1.00 23.06 ? 199 ALA B CB 1 ATOM 3191 N N . SER B 1 179 ? 12.824 70.001 -7.912 1.00 24.12 ? 200 SER B N 1 ATOM 3192 C CA . SER B 1 179 ? 14.018 69.180 -8.001 1.00 22.85 ? 200 SER B CA 1 ATOM 3193 C C . SER B 1 179 ? 14.973 69.692 -9.060 1.00 23.13 ? 200 SER B C 1 ATOM 3194 O O . SER B 1 179 ? 14.562 70.295 -10.055 1.00 23.61 ? 200 SER B O 1 ATOM 3195 C CB . SER B 1 179 ? 13.661 67.705 -8.268 1.00 23.28 ? 200 SER B CB 1 ATOM 3196 O OG . SER B 1 179 ? 13.037 67.570 -9.525 1.00 24.97 ? 200 SER B OG 1 ATOM 3197 N N . LEU B 1 180 ? 16.254 69.455 -8.830 1.00 22.31 ? 201 LEU B N 1 ATOM 3198 C CA . LEU B 1 180 ? 17.302 69.856 -9.758 1.00 23.93 ? 201 LEU B CA 1 ATOM 3199 C C . LEU B 1 180 ? 18.267 68.703 -9.914 1.00 23.55 ? 201 LEU B C 1 ATOM 3200 O O . LEU B 1 180 ? 18.656 68.075 -8.920 1.00 23.96 ? 201 LEU B O 1 ATOM 3201 C CB . LEU B 1 180 ? 18.043 71.098 -9.236 1.00 25.76 ? 201 LEU B CB 1 ATOM 3202 C CG . LEU B 1 180 ? 19.181 71.666 -10.102 1.00 26.05 ? 201 LEU B CG 1 ATOM 3203 C CD1 . LEU B 1 180 ? 19.358 73.159 -9.836 1.00 26.41 ? 201 LEU B CD1 1 ATOM 3204 C CD2 . LEU B 1 180 ? 20.483 70.914 -9.881 1.00 26.03 ? 201 LEU B CD2 1 ATOM 3205 N N . VAL B 1 181 ? 18.657 68.417 -11.158 1.00 22.85 ? 202 VAL B N 1 ATOM 3206 C CA . VAL B 1 181 ? 19.707 67.441 -11.422 1.00 23.79 ? 202 VAL B CA 1 ATOM 3207 C C . VAL B 1 181 ? 20.803 68.070 -12.290 1.00 23.65 ? 202 VAL B C 1 ATOM 3208 O O . VAL B 1 181 ? 20.528 68.932 -13.111 1.00 23.68 ? 202 VAL B O 1 ATOM 3209 C CB . VAL B 1 181 ? 19.201 66.110 -12.064 1.00 25.85 ? 202 VAL B CB 1 ATOM 3210 C CG1 . VAL B 1 181 ? 18.064 65.492 -11.245 1.00 25.33 ? 202 VAL B CG1 1 ATOM 3211 C CG2 . VAL B 1 181 ? 18.761 66.311 -13.508 1.00 26.06 ? 202 VAL B CG2 1 ATOM 3212 N N . TYR B 1 182 ? 22.039 67.652 -12.051 1.00 25.26 ? 203 TYR B N 1 ATOM 3213 C CA . TYR B 1 182 ? 23.178 67.962 -12.923 1.00 26.31 ? 203 TYR B CA 1 ATOM 3214 C C . TYR B 1 182 ? 23.536 66.674 -13.652 1.00 25.65 ? 203 TYR B C 1 ATOM 3215 O O . TYR B 1 182 ? 24.233 65.838 -13.098 1.00 26.67 ? 203 TYR B O 1 ATOM 3216 C CB . TYR B 1 182 ? 24.396 68.362 -12.097 1.00 26.52 ? 203 TYR B CB 1 ATOM 3217 C CG . TYR B 1 182 ? 24.412 69.762 -11.568 1.00 26.66 ? 203 TYR B CG 1 ATOM 3218 C CD1 . TYR B 1 182 ? 24.470 70.861 -12.428 1.00 28.04 ? 203 TYR B CD1 1 ATOM 3219 C CD2 . TYR B 1 182 ? 24.442 69.993 -10.200 1.00 28.01 ? 203 TYR B CD2 1 ATOM 3220 C CE1 . TYR B 1 182 ? 24.517 72.157 -11.928 1.00 29.05 ? 203 TYR B CE1 1 ATOM 3221 C CE2 . TYR B 1 182 ? 24.489 71.281 -9.692 1.00 28.02 ? 203 TYR B CE2 1 ATOM 3222 C CZ . TYR B 1 182 ? 24.538 72.356 -10.552 1.00 29.70 ? 203 TYR B CZ 1 ATOM 3223 O OH . TYR B 1 182 ? 24.587 73.630 -10.021 1.00 30.98 ? 203 TYR B OH 1 ATOM 3224 N N . PRO B 1 183 ? 23.053 66.499 -14.894 1.00 26.56 ? 204 PRO B N 1 ATOM 3225 C CA . PRO B 1 183 ? 23.281 65.200 -15.535 1.00 28.12 ? 204 PRO B CA 1 ATOM 3226 C C . PRO B 1 183 ? 24.759 64.823 -15.703 1.00 27.74 ? 204 PRO B C 1 ATOM 3227 O O . PRO B 1 183 ? 25.104 63.654 -15.632 1.00 26.35 ? 204 PRO B O 1 ATOM 3228 C CB . PRO B 1 183 ? 22.582 65.346 -16.896 1.00 28.53 ? 204 PRO B CB 1 ATOM 3229 C CG . PRO B 1 183 ? 21.580 66.432 -16.692 1.00 29.59 ? 204 PRO B CG 1 ATOM 3230 C CD . PRO B 1 183 ? 22.226 67.389 -15.725 1.00 27.15 ? 204 PRO B CD 1 ATOM 3231 N N . SER B 1 184 ? 25.630 65.801 -15.899 1.00 29.64 ? 205 SER B N 1 ATOM 3232 C CA . SER B 1 184 ? 27.049 65.479 -16.077 1.00 31.40 ? 205 SER B CA 1 ATOM 3233 C C . SER B 1 184 ? 27.696 65.008 -14.767 1.00 31.83 ? 205 SER B C 1 ATOM 3234 O O . SER B 1 184 ? 28.640 64.223 -14.776 1.00 32.54 ? 205 SER B O 1 ATOM 3235 C CB . SER B 1 184 ? 27.802 66.681 -16.650 1.00 34.43 ? 205 SER B CB 1 ATOM 3236 O OG . SER B 1 184 ? 27.529 67.840 -15.875 1.00 39.20 ? 205 SER B OG 1 ATOM 3237 N N . LEU B 1 185 ? 27.160 65.474 -13.646 1.00 30.89 ? 206 LEU B N 1 ATOM 3238 C CA . LEU B 1 185 ? 27.734 65.183 -12.331 1.00 31.37 ? 206 LEU B CA 1 ATOM 3239 C C . LEU B 1 185 ? 26.988 64.047 -11.625 1.00 30.95 ? 206 LEU B C 1 ATOM 3240 O O . LEU B 1 185 ? 27.478 63.498 -10.635 1.00 28.88 ? 206 LEU B O 1 ATOM 3241 C CB . LEU B 1 185 ? 27.700 66.445 -11.465 1.00 31.06 ? 206 LEU B CB 1 ATOM 3242 C CG . LEU B 1 185 ? 28.297 67.742 -12.031 1.00 33.80 ? 206 LEU B CG 1 ATOM 3243 C CD1 . LEU B 1 185 ? 27.902 68.904 -11.136 1.00 33.86 ? 206 LEU B CD1 1 ATOM 3244 C CD2 . LEU B 1 185 ? 29.812 67.654 -12.170 1.00 34.26 ? 206 LEU B CD2 1 ATOM 3245 N N . LYS B 1 186 ? 25.800 63.714 -12.142 1.00 29.56 ? 207 LYS B N 1 ATOM 3246 C CA . LYS B 1 186 ? 24.940 62.661 -11.587 1.00 28.91 ? 207 LYS B CA 1 ATOM 3247 C C . LYS B 1 186 ? 24.398 63.011 -10.188 1.00 27.63 ? 207 LYS B C 1 ATOM 3248 O O . LYS B 1 186 ? 24.008 62.130 -9.407 1.00 27.31 ? 207 LYS B O 1 ATOM 3249 C CB . LYS B 1 186 ? 25.647 61.301 -11.611 1.00 28.95 ? 207 LYS B CB 1 ATOM 3250 C CG . LYS B 1 186 ? 26.123 60.904 -13.002 1.00 30.50 ? 207 LYS B CG 1 ATOM 3251 C CD . LYS B 1 186 ? 27.225 59.874 -12.944 1.00 33.58 ? 207 LYS B CD 1 ATOM 3252 C CE . LYS B 1 186 ? 28.043 59.883 -14.225 1.00 35.40 ? 207 LYS B CE 1 ATOM 3253 N NZ . LYS B 1 186 ? 28.912 58.679 -14.316 1.00 40.88 ? 207 LYS B NZ 1 ATOM 3254 N N . THR B 1 187 ? 24.363 64.304 -9.883 1.00 26.25 ? 208 THR B N 1 ATOM 3255 C CA . THR B 1 187 ? 23.866 64.759 -8.579 1.00 26.95 ? 208 THR B CA 1 ATOM 3256 C C . THR B 1 187 ? 22.435 65.264 -8.680 1.00 26.38 ? 208 THR B C 1 ATOM 3257 O O . THR B 1 187 ? 22.002 65.750 -9.729 1.00 27.23 ? 208 THR B O 1 ATOM 3258 C CB . THR B 1 187 ? 24.763 65.849 -7.965 1.00 28.45 ? 208 THR B CB 1 ATOM 3259 O OG1 . THR B 1 187 ? 24.823 66.983 -8.851 1.00 28.37 ? 208 THR B OG1 1 ATOM 3260 C CG2 . THR B 1 187 ? 26.165 65.295 -7.697 1.00 27.04 ? 208 THR B CG2 1 ATOM 3261 N N . SER B 1 188 ? 21.699 65.140 -7.577 1.00 24.58 ? 209 SER B N 1 ATOM 3262 C CA . SER B 1 188 ? 20.293 65.493 -7.569 1.00 24.17 ? 209 SER B CA 1 ATOM 3263 C C . SER B 1 188 ? 19.864 66.043 -6.211 1.00 22.85 ? 209 SER B C 1 ATOM 3264 O O . SER B 1 188 ? 20.441 65.685 -5.171 1.00 22.72 ? 209 SER B O 1 ATOM 3265 C CB . SER B 1 188 ? 19.452 64.275 -7.941 1.00 22.18 ? 209 SER B CB 1 ATOM 3266 O OG . SER B 1 188 ? 19.780 63.186 -7.110 1.00 22.21 ? 209 SER B OG 1 ATOM 3267 N N . PHE B 1 189 ? 18.852 66.905 -6.242 1.00 23.17 ? 210 PHE B N 1 ATOM 3268 C CA . PHE B 1 189 ? 18.384 67.634 -5.068 1.00 23.11 ? 210 PHE B CA 1 ATOM 3269 C C . PHE B 1 189 ? 16.884 67.821 -5.147 1.00 21.98 ? 210 PHE B C 1 ATOM 3270 O O . PHE B 1 189 ? 16.330 67.998 -6.227 1.00 22.55 ? 210 PHE B O 1 ATOM 3271 C CB . PHE B 1 189 ? 19.084 68.995 -4.979 1.00 24.96 ? 210 PHE B CB 1 ATOM 3272 C CG . PHE B 1 189 ? 20.563 68.913 -5.244 1.00 24.55 ? 210 PHE B CG 1 ATOM 3273 C CD1 . PHE B 1 189 ? 21.454 68.659 -4.203 1.00 25.22 ? 210 PHE B CD1 1 ATOM 3274 C CD2 . PHE B 1 189 ? 21.058 69.036 -6.545 1.00 25.98 ? 210 PHE B CD2 1 ATOM 3275 C CE1 . PHE B 1 189 ? 22.810 68.546 -4.450 1.00 24.90 ? 210 PHE B CE1 1 ATOM 3276 C CE2 . PHE B 1 189 ? 22.423 68.929 -6.798 1.00 25.76 ? 210 PHE B CE2 1 ATOM 3277 C CZ . PHE B 1 189 ? 23.297 68.682 -5.747 1.00 25.56 ? 210 PHE B CZ 1 ATOM 3278 N N . ILE B 1 190 ? 16.224 67.794 -4.000 1.00 21.36 ? 211 ILE B N 1 ATOM 3279 C CA . ILE B 1 190 ? 14.763 67.923 -3.993 1.00 22.15 ? 211 ILE B CA 1 ATOM 3280 C C . ILE B 1 190 ? 14.277 68.656 -2.736 1.00 22.51 ? 211 ILE B C 1 ATOM 3281 O O . ILE B 1 190 ? 14.849 68.482 -1.645 1.00 24.10 ? 211 ILE B O 1 ATOM 3282 C CB . ILE B 1 190 ? 14.088 66.536 -4.152 1.00 20.72 ? 211 ILE B CB 1 ATOM 3283 C CG1 . ILE B 1 190 ? 12.592 66.674 -4.450 1.00 19.80 ? 211 ILE B CG1 1 ATOM 3284 C CG2 . ILE B 1 190 ? 14.320 65.656 -2.931 1.00 20.33 ? 211 ILE B CG2 1 ATOM 3285 C CD1 . ILE B 1 190 ? 12.002 65.393 -5.041 1.00 20.61 ? 211 ILE B CD1 1 ATOM 3286 N N . VAL B 1 191 ? 13.251 69.487 -2.907 1.00 23.36 ? 212 VAL B N 1 ATOM 3287 C CA . VAL B 1 191 ? 12.593 70.173 -1.791 1.00 23.77 ? 212 VAL B CA 1 ATOM 3288 C C . VAL B 1 191 ? 11.082 70.166 -2.011 1.00 23.90 ? 212 VAL B C 1 ATOM 3289 O O . VAL B 1 191 ? 10.620 70.286 -3.140 1.00 24.61 ? 212 VAL B O 1 ATOM 3290 C CB . VAL B 1 191 ? 13.146 71.619 -1.623 1.00 25.30 ? 212 VAL B CB 1 ATOM 3291 C CG1 . VAL B 1 191 ? 12.860 72.484 -2.857 1.00 24.73 ? 212 VAL B CG1 1 ATOM 3292 C CG2 . VAL B 1 191 ? 12.609 72.270 -0.351 1.00 25.53 ? 212 VAL B CG2 1 ATOM 3293 N N . SER B 1 192 ? 10.310 70.019 -0.941 1.00 23.75 ? 213 SER B N 1 ATOM 3294 C CA . SER B 1 192 ? 8.856 69.968 -1.042 1.00 24.38 ? 213 SER B CA 1 ATOM 3295 C C . SER B 1 192 ? 8.203 70.637 0.151 1.00 26.54 ? 213 SER B C 1 ATOM 3296 O O . SER B 1 192 ? 8.717 70.558 1.268 1.00 26.81 ? 213 SER B O 1 ATOM 3297 C CB . SER B 1 192 ? 8.388 68.517 -1.104 1.00 24.70 ? 213 SER B CB 1 ATOM 3298 O OG . SER B 1 192 ? 9.018 67.754 -0.080 1.00 26.15 ? 213 SER B OG 1 ATOM 3299 N N . ASP B 1 193 ? 7.066 71.283 -0.097 1.00 27.80 ? 214 ASP B N 1 ATOM 3300 C CA . ASP B 1 193 ? 6.262 71.899 0.950 1.00 28.84 ? 214 ASP B CA 1 ATOM 3301 C C . ASP B 1 193 ? 4.888 72.248 0.384 1.00 30.01 ? 214 ASP B C 1 ATOM 3302 O O . ASP B 1 193 ? 4.720 72.355 -0.832 1.00 28.39 ? 214 ASP B O 1 ATOM 3303 C CB . ASP B 1 193 ? 6.963 73.150 1.503 1.00 29.96 ? 214 ASP B CB 1 ATOM 3304 C CG . ASP B 1 193 ? 6.480 73.530 2.899 1.00 32.11 ? 214 ASP B CG 1 ATOM 3305 O OD1 . ASP B 1 193 ? 5.555 72.872 3.429 1.00 30.23 ? 214 ASP B OD1 1 ATOM 3306 O OD2 . ASP B 1 193 ? 7.034 74.495 3.458 1.00 31.89 ? 214 ASP B OD2 1 ATOM 3307 N N . THR B 1 194 ? 3.896 72.405 1.256 1.00 30.87 ? 215 THR B N 1 ATOM 3308 C CA . THR B 1 194 ? 2.566 72.814 0.802 1.00 31.22 ? 215 THR B CA 1 ATOM 3309 C C . THR B 1 194 ? 2.500 74.336 0.635 1.00 32.36 ? 215 THR B C 1 ATOM 3310 O O . THR B 1 194 ? 3.108 75.079 1.400 1.00 32.39 ? 215 THR B O 1 ATOM 3311 C CB . THR B 1 194 ? 1.442 72.317 1.735 1.00 32.73 ? 215 THR B CB 1 ATOM 3312 O OG1 . THR B 1 194 ? 1.746 72.678 3.086 1.00 32.81 ? 215 THR B OG1 1 ATOM 3313 C CG2 . THR B 1 194 ? 1.287 70.798 1.644 1.00 31.66 ? 215 THR B CG2 1 ATOM 3314 N N . VAL B 1 195 ? 1.801 74.784 -0.405 1.00 32.87 ? 216 VAL B N 1 ATOM 3315 C CA . VAL B 1 195 ? 1.547 76.199 -0.640 1.00 34.14 ? 216 VAL B CA 1 ATOM 3316 C C . VAL B 1 195 ? 0.067 76.344 -0.950 1.00 36.70 ? 216 VAL B C 1 ATOM 3317 O O . VAL B 1 195 ? -0.488 75.594 -1.765 1.00 35.87 ? 216 VAL B O 1 ATOM 3318 C CB . VAL B 1 195 ? 2.378 76.779 -1.811 1.00 33.31 ? 216 VAL B CB 1 ATOM 3319 C CG1 . VAL B 1 195 ? 2.052 78.255 -2.021 1.00 34.24 ? 216 VAL B CG1 1 ATOM 3320 C CG2 . VAL B 1 195 ? 3.872 76.620 -1.565 1.00 33.13 ? 216 VAL B CG2 1 ATOM 3321 N N . ASP B 1 196 ? -0.578 77.292 -0.279 1.00 38.36 ? 217 ASP B N 1 ATOM 3322 C CA . ASP B 1 196 ? -1.978 77.567 -0.535 1.00 40.20 ? 217 ASP B CA 1 ATOM 3323 C C . ASP B 1 196 ? -2.065 78.696 -1.566 1.00 42.11 ? 217 ASP B C 1 ATOM 3324 O O . ASP B 1 196 ? -2.013 79.876 -1.206 1.00 41.50 ? 217 ASP B O 1 ATOM 3325 C CB . ASP B 1 196 ? -2.686 77.946 0.769 1.00 43.20 ? 217 ASP B CB 1 ATOM 3326 C CG . ASP B 1 196 ? -4.191 77.992 0.620 1.00 44.85 ? 217 ASP B CG 1 ATOM 3327 O OD1 . ASP B 1 196 ? -4.690 78.790 -0.194 1.00 47.62 ? 217 ASP B OD1 1 ATOM 3328 O OD2 . ASP B 1 196 ? -4.880 77.228 1.320 1.00 49.70 ? 217 ASP B OD2 1 ATOM 3329 N N . LEU B 1 197 ? -2.181 78.331 -2.846 1.00 41.69 ? 218 LEU B N 1 ATOM 3330 C CA . LEU B 1 197 ? -2.158 79.315 -3.939 1.00 42.50 ? 218 LEU B CA 1 ATOM 3331 C C . LEU B 1 197 ? -3.342 80.291 -3.889 1.00 43.11 ? 218 LEU B C 1 ATOM 3332 O O . LEU B 1 197 ? -3.193 81.476 -4.196 1.00 44.60 ? 218 LEU B O 1 ATOM 3333 C CB . LEU B 1 197 ? -2.099 78.619 -5.304 1.00 42.45 ? 218 LEU B CB 1 ATOM 3334 C CG . LEU B 1 197 ? -0.904 77.728 -5.669 1.00 41.14 ? 218 LEU B CG 1 ATOM 3335 C CD1 . LEU B 1 197 ? -1.018 77.332 -7.131 1.00 40.82 ? 218 LEU B CD1 1 ATOM 3336 C CD2 . LEU B 1 197 ? 0.442 78.390 -5.405 1.00 40.62 ? 218 LEU B CD2 1 ATOM 3337 N N . LYS B 1 198 ? -4.500 79.768 -3.496 1.00 43.75 ? 219 LYS B N 1 ATOM 3338 C CA . LYS B 1 198 ? -5.744 80.519 -3.329 1.00 45.22 ? 219 LYS B CA 1 ATOM 3339 C C . LYS B 1 198 ? -5.556 81.787 -2.487 1.00 47.27 ? 219 LYS B C 1 ATOM 3340 O O . LYS B 1 198 ? -6.090 82.844 -2.822 1.00 48.15 ? 219 LYS B O 1 ATOM 3341 C CB . LYS B 1 198 ? -6.763 79.612 -2.650 1.00 46.16 ? 219 LYS B CB 1 ATOM 3342 C CG . LYS B 1 198 ? -8.158 79.636 -3.231 1.00 47.83 ? 219 LYS B CG 1 ATOM 3343 C CD . LYS B 1 198 ? -8.877 78.355 -2.848 1.00 50.43 ? 219 LYS B CD 1 ATOM 3344 C CE . LYS B 1 198 ? -10.324 78.374 -3.300 1.00 51.38 ? 219 LYS B CE 1 ATOM 3345 N NZ . LYS B 1 198 ? -10.945 77.038 -3.097 1.00 53.91 ? 219 LYS B NZ 1 ATOM 3346 N N . SER B 1 199 ? -4.779 81.680 -1.411 1.00 44.94 ? 220 SER B N 1 ATOM 3347 C CA . SER B 1 199 ? -4.602 82.788 -0.474 1.00 44.57 ? 220 SER B CA 1 ATOM 3348 C C . SER B 1 199 ? -3.399 83.689 -0.769 1.00 44.00 ? 220 SER B C 1 ATOM 3349 O O . SER B 1 199 ? -3.196 84.683 -0.080 1.00 46.19 ? 220 SER B O 1 ATOM 3350 C CB . SER B 1 199 ? -4.514 82.253 0.958 1.00 45.73 ? 220 SER B CB 1 ATOM 3351 O OG . SER B 1 199 ? -3.271 81.611 1.174 1.00 47.03 ? 220 SER B OG 1 ATOM 3352 N N . VAL B 1 200 ? -2.605 83.348 -1.779 1.00 40.50 ? 221 VAL B N 1 ATOM 3353 C CA . VAL B 1 200 ? -1.386 84.105 -2.086 1.00 41.65 ? 221 VAL B CA 1 ATOM 3354 C C . VAL B 1 200 ? -1.437 84.827 -3.439 1.00 42.08 ? 221 VAL B C 1 ATOM 3355 O O . VAL B 1 200 ? -1.085 86.007 -3.538 1.00 42.71 ? 221 VAL B O 1 ATOM 3356 C CB . VAL B 1 200 ? -0.131 83.201 -2.028 1.00 40.03 ? 221 VAL B CB 1 ATOM 3357 C CG1 . VAL B 1 200 ? 1.105 83.943 -2.523 1.00 39.81 ? 221 VAL B CG1 1 ATOM 3358 C CG2 . VAL B 1 200 ? 0.083 82.691 -0.611 1.00 40.33 ? 221 VAL B CG2 1 ATOM 3359 N N . LEU B 1 201 ? -1.864 84.106 -4.473 1.00 41.28 ? 222 LEU B N 1 ATOM 3360 C CA . LEU B 1 201 ? -1.828 84.617 -5.838 1.00 39.64 ? 222 LEU B CA 1 ATOM 3361 C C . LEU B 1 201 ? -3.195 85.100 -6.287 1.00 38.15 ? 222 LEU B C 1 ATOM 3362 O O . LEU B 1 201 ? -4.213 84.592 -5.809 1.00 39.08 ? 222 LEU B O 1 ATOM 3363 C CB . LEU B 1 201 ? -1.327 83.526 -6.798 1.00 39.65 ? 222 LEU B CB 1 ATOM 3364 C CG . LEU B 1 201 ? 0.108 83.005 -6.658 1.00 38.46 ? 222 LEU B CG 1 ATOM 3365 C CD1 . LEU B 1 201 ? 0.317 81.819 -7.591 1.00 37.62 ? 222 LEU B CD1 1 ATOM 3366 C CD2 . LEU B 1 201 ? 1.148 84.085 -6.924 1.00 36.77 ? 222 LEU B CD2 1 ATOM 3367 N N . PRO B 1 202 ? -3.228 86.088 -7.211 1.00 37.54 ? 223 PRO B N 1 ATOM 3368 C CA . PRO B 1 202 ? -4.493 86.435 -7.852 1.00 37.68 ? 223 PRO B CA 1 ATOM 3369 C C . PRO B 1 202 ? -4.918 85.288 -8.761 1.00 39.79 ? 223 PRO B C 1 ATOM 3370 O O . PRO B 1 202 ? -4.078 84.451 -9.107 1.00 41.46 ? 223 PRO B O 1 ATOM 3371 C CB . PRO B 1 202 ? -4.143 87.665 -8.694 1.00 37.06 ? 223 PRO B CB 1 ATOM 3372 C CG . PRO B 1 202 ? -2.668 87.607 -8.908 1.00 36.13 ? 223 PRO B CG 1 ATOM 3373 C CD . PRO B 1 202 ? -2.108 86.926 -7.689 1.00 38.02 ? 223 PRO B CD 1 ATOM 3374 N N . GLU B 1 203 ? -6.194 85.255 -9.138 1.00 38.90 ? 224 GLU B N 1 ATOM 3375 C CA . GLU B 1 203 ? -6.738 84.208 -10.010 1.00 38.86 ? 224 GLU B CA 1 ATOM 3376 C C . GLU B 1 203 ? -5.948 83.991 -11.298 1.00 38.37 ? 224 GLU B C 1 ATOM 3377 O O . GLU B 1 203 ? -5.842 82.856 -11.769 1.00 37.48 ? 224 GLU B O 1 ATOM 3378 C CB . GLU B 1 203 ? -8.190 84.498 -10.356 1.00 40.14 ? 224 GLU B CB 1 ATOM 3379 C CG . GLU B 1 203 ? -9.165 84.113 -9.263 1.00 41.47 ? 224 GLU B CG 1 ATOM 3380 C CD . GLU B 1 203 ? -10.524 84.728 -9.481 1.00 43.07 ? 224 GLU B CD 1 ATOM 3381 O OE1 . GLU B 1 203 ? -10.635 85.963 -9.346 1.00 45.39 ? 224 GLU B OE1 1 ATOM 3382 O OE2 . GLU B 1 203 ? -11.475 83.982 -9.779 1.00 44.38 ? 224 GLU B OE2 1 ATOM 3383 N N . TRP B 1 204 ? -5.419 85.078 -11.864 1.00 37.13 ? 225 TRP B N 1 ATOM 3384 C CA . TRP B 1 204 ? -4.591 85.016 -13.069 1.00 36.41 ? 225 TRP B CA 1 ATOM 3385 C C . TRP B 1 204 ? -3.204 85.504 -12.815 1.00 37.30 ? 225 TRP B C 1 ATOM 3386 O O . TRP B 1 204 ? -2.996 86.532 -12.146 1.00 38.90 ? 225 TRP B O 1 ATOM 3387 C CB . TRP B 1 204 ? -5.222 85.823 -14.199 1.00 35.96 ? 225 TRP B CB 1 ATOM 3388 C CG . TRP B 1 204 ? -6.476 85.198 -14.740 1.00 35.15 ? 225 TRP B CG 1 ATOM 3389 C CD1 . TRP B 1 204 ? -7.741 85.190 -14.161 1.00 35.14 ? 225 TRP B CD1 1 ATOM 3390 C CD2 . TRP B 1 204 ? -6.628 84.455 -15.996 1.00 35.07 ? 225 TRP B CD2 1 ATOM 3391 N NE1 . TRP B 1 204 ? -8.636 84.517 -14.949 1.00 35.35 ? 225 TRP B NE1 1 ATOM 3392 C CE2 . TRP B 1 204 ? -8.037 84.055 -16.065 1.00 35.30 ? 225 TRP B CE2 1 ATOM 3393 C CE3 . TRP B 1 204 ? -5.773 84.100 -17.030 1.00 35.32 ? 225 TRP B CE3 1 ATOM 3394 C CZ2 . TRP B 1 204 ? -8.542 83.322 -17.129 1.00 35.88 ? 225 TRP B CZ2 1 ATOM 3395 C CZ3 . TRP B 1 204 ? -6.296 83.366 -18.101 1.00 34.99 ? 225 TRP B CZ3 1 ATOM 3396 C CH2 . TRP B 1 204 ? -7.645 82.987 -18.146 1.00 35.98 ? 225 TRP B CH2 1 ATOM 3397 N N . VAL B 1 205 ? -2.233 84.786 -13.371 1.00 34.65 ? 226 VAL B N 1 ATOM 3398 C CA . VAL B 1 205 ? -0.825 85.070 -13.144 1.00 34.11 ? 226 VAL B CA 1 ATOM 3399 C C . VAL B 1 205 ? -0.013 85.101 -14.428 1.00 34.33 ? 226 VAL B C 1 ATOM 3400 O O . VAL B 1 205 ? -0.468 84.645 -15.470 1.00 38.15 ? 226 VAL B O 1 ATOM 3401 C CB . VAL B 1 205 ? -0.182 84.040 -12.177 1.00 34.45 ? 226 VAL B CB 1 ATOM 3402 C CG1 . VAL B 1 205 ? -0.753 84.183 -10.774 1.00 33.40 ? 226 VAL B CG1 1 ATOM 3403 C CG2 . VAL B 1 205 ? -0.354 82.610 -12.695 1.00 32.66 ? 226 VAL B CG2 1 ATOM 3404 N N . ILE B 1 206 ? 1.190 85.653 -14.345 1.00 35.42 ? 227 ILE B N 1 ATOM 3405 C CA . ILE B 1 206 ? 2.185 85.459 -15.388 1.00 36.22 ? 227 ILE B CA 1 ATOM 3406 C C . ILE B 1 206 ? 3.248 84.524 -14.838 1.00 35.23 ? 227 ILE B C 1 ATOM 3407 O O . ILE B 1 206 ? 3.563 84.568 -13.642 1.00 36.38 ? 227 ILE B O 1 ATOM 3408 C CB . ILE B 1 206 ? 2.799 86.782 -15.927 1.00 37.66 ? 227 ILE B CB 1 ATOM 3409 C CG1 . ILE B 1 206 ? 3.298 87.688 -14.784 1.00 39.31 ? 227 ILE B CG1 1 ATOM 3410 C CG2 . ILE B 1 206 ? 1.785 87.507 -16.807 1.00 39.06 ? 227 ILE B CG2 1 ATOM 3411 C CD1 . ILE B 1 206 ? 4.206 88.822 -15.235 1.00 40.09 ? 227 ILE B CD1 1 ATOM 3412 N N . VAL B 1 207 ? 3.757 83.648 -15.700 1.00 31.98 ? 228 VAL B N 1 ATOM 3413 C CA . VAL B 1 207 ? 4.775 82.680 -15.308 1.00 30.15 ? 228 VAL B CA 1 ATOM 3414 C C . VAL B 1 207 ? 6.090 82.968 -16.016 1.00 29.70 ? 228 VAL B C 1 ATOM 3415 O O . VAL B 1 207 ? 6.105 83.416 -17.169 1.00 29.93 ? 228 VAL B O 1 ATOM 3416 C CB . VAL B 1 207 ? 4.331 81.206 -15.545 1.00 29.85 ? 228 VAL B CB 1 ATOM 3417 C CG1 . VAL B 1 207 ? 3.068 80.889 -14.760 1.00 30.20 ? 228 VAL B CG1 1 ATOM 3418 C CG2 . VAL B 1 207 ? 4.121 80.908 -17.028 1.00 29.68 ? 228 VAL B CG2 1 ATOM 3419 N N . GLY B 1 208 ? 7.196 82.728 -15.325 1.00 28.38 ? 229 GLY B N 1 ATOM 3420 C CA . GLY B 1 208 ? 8.494 82.952 -15.919 1.00 29.88 ? 229 GLY B CA 1 ATOM 3421 C C . GLY B 1 208 ? 9.627 82.983 -14.922 1.00 32.66 ? 229 GLY B C 1 ATOM 3422 O O . GLY B 1 208 ? 9.598 82.277 -13.911 1.00 31.60 ? 229 GLY B O 1 ATOM 3423 N N . PHE B 1 209 ? 10.627 83.813 -15.213 1.00 32.94 ? 230 PHE B N 1 ATOM 3424 C CA . PHE B 1 209 ? 11.879 83.796 -14.477 1.00 32.78 ? 230 PHE B CA 1 ATOM 3425 C C . PHE B 1 209 ? 12.294 85.178 -14.000 1.00 34.99 ? 230 PHE B C 1 ATOM 3426 O O . PHE B 1 209 ? 11.840 86.202 -14.531 1.00 35.17 ? 230 PHE B O 1 ATOM 3427 C CB . PHE B 1 209 ? 13.006 83.225 -15.334 1.00 33.69 ? 230 PHE B CB 1 ATOM 3428 C CG . PHE B 1 209 ? 12.735 81.850 -15.872 1.00 33.84 ? 230 PHE B CG 1 ATOM 3429 C CD1 . PHE B 1 209 ? 13.022 80.720 -15.111 1.00 34.31 ? 230 PHE B CD1 1 ATOM 3430 C CD2 . PHE B 1 209 ? 12.206 81.684 -17.148 1.00 34.34 ? 230 PHE B CD2 1 ATOM 3431 C CE1 . PHE B 1 209 ? 12.781 79.449 -15.613 1.00 33.63 ? 230 PHE B CE1 1 ATOM 3432 C CE2 . PHE B 1 209 ? 11.958 80.415 -17.652 1.00 34.98 ? 230 PHE B CE2 1 ATOM 3433 C CZ . PHE B 1 209 ? 12.245 79.300 -16.882 1.00 33.18 ? 230 PHE B CZ 1 ATOM 3434 N N . THR B 1 210 ? 13.156 85.179 -12.990 1.00 34.87 ? 231 THR B N 1 ATOM 3435 C CA . THR B 1 210 ? 13.829 86.383 -12.510 1.00 35.78 ? 231 THR B CA 1 ATOM 3436 C C . THR B 1 210 ? 15.258 85.998 -12.164 1.00 35.71 ? 231 THR B C 1 ATOM 3437 O O . THR B 1 210 ? 15.522 84.850 -11.794 1.00 36.46 ? 231 THR B O 1 ATOM 3438 C CB . THR B 1 210 ? 13.090 87.026 -11.307 1.00 38.58 ? 231 THR B CB 1 ATOM 3439 O OG1 . THR B 1 210 ? 13.617 88.342 -11.051 1.00 37.09 ? 231 THR B OG1 1 ATOM 3440 C CG2 . THR B 1 210 ? 13.220 86.173 -10.052 1.00 36.00 ? 231 THR B CG2 1 ATOM 3441 N N . ALA B 1 211 ? 16.191 86.932 -12.315 1.00 34.30 ? 232 ALA B N 1 ATOM 3442 C CA . ALA B 1 211 ? 17.584 86.672 -11.962 1.00 34.75 ? 232 ALA B CA 1 ATOM 3443 C C . ALA B 1 211 ? 18.324 87.963 -11.661 1.00 37.90 ? 232 ALA B C 1 ATOM 3444 O O . ALA B 1 211 ? 17.957 89.027 -12.156 1.00 39.68 ? 232 ALA B O 1 ATOM 3445 C CB . ALA B 1 211 ? 18.299 85.912 -13.059 1.00 33.78 ? 232 ALA B CB 1 ATOM 3446 N N . THR B 1 212 ? 19.372 87.844 -10.855 1.00 39.08 ? 233 THR B N 1 ATOM 3447 C CA . THR B 1 212 ? 20.198 88.987 -10.484 1.00 41.99 ? 233 THR B CA 1 ATOM 3448 C C . THR B 1 212 ? 21.655 88.577 -10.399 1.00 43.27 ? 233 THR B C 1 ATOM 3449 O O . THR B 1 212 ? 21.967 87.407 -10.159 1.00 43.07 ? 233 THR B O 1 ATOM 3450 C CB . THR B 1 212 ? 19.795 89.570 -9.115 1.00 41.03 ? 233 THR B CB 1 ATOM 3451 O OG1 . THR B 1 212 ? 19.699 88.513 -8.146 1.00 40.37 ? 233 THR B OG1 1 ATOM 3452 C CG2 . THR B 1 212 ? 18.479 90.333 -9.198 1.00 39.97 ? 233 THR B CG2 1 ATOM 3453 N N . THR B 1 213 ? 22.545 89.548 -10.603 1.00 43.48 ? 234 THR B N 1 ATOM 3454 C CA . THR B 1 213 ? 23.961 89.376 -10.304 1.00 44.20 ? 234 THR B CA 1 ATOM 3455 C C . THR B 1 213 ? 24.299 90.152 -9.022 1.00 44.67 ? 234 THR B C 1 ATOM 3456 O O . THR B 1 213 ? 23.547 91.047 -8.606 1.00 44.55 ? 234 THR B O 1 ATOM 3457 C CB . THR B 1 213 ? 24.862 89.852 -11.459 1.00 46.08 ? 234 THR B CB 1 ATOM 3458 O OG1 . THR B 1 213 ? 24.675 91.260 -11.669 1.00 46.07 ? 234 THR B OG1 1 ATOM 3459 C CG2 . THR B 1 213 ? 24.539 89.091 -12.744 1.00 45.63 ? 234 THR B CG2 1 ATOM 3460 N N . GLY B 1 214 ? 25.416 89.796 -8.395 1.00 45.19 ? 235 GLY B N 1 ATOM 3461 C CA . GLY B 1 214 ? 25.847 90.454 -7.159 1.00 48.17 ? 235 GLY B CA 1 ATOM 3462 C C . GLY B 1 214 ? 26.182 91.916 -7.394 1.00 49.93 ? 235 GLY B C 1 ATOM 3463 O O . GLY B 1 214 ? 26.681 92.281 -8.465 1.00 49.62 ? 235 GLY B O 1 ATOM 3464 N N . ILE B 1 215 ? 25.889 92.751 -6.399 1.00 51.40 ? 236 ILE B N 1 ATOM 3465 C CA . ILE B 1 215 ? 26.176 94.189 -6.480 1.00 51.31 ? 236 ILE B CA 1 ATOM 3466 C C . ILE B 1 215 ? 27.596 94.539 -6.018 1.00 52.91 ? 236 ILE B C 1 ATOM 3467 O O . ILE B 1 215 ? 27.971 95.712 -6.015 1.00 52.40 ? 236 ILE B O 1 ATOM 3468 C CB . ILE B 1 215 ? 25.135 95.037 -5.706 1.00 50.33 ? 236 ILE B CB 1 ATOM 3469 C CG1 . ILE B 1 215 ? 25.227 94.779 -4.196 1.00 50.06 ? 236 ILE B CG1 1 ATOM 3470 C CG2 . ILE B 1 215 ? 23.727 94.784 -6.239 1.00 50.74 ? 236 ILE B CG2 1 ATOM 3471 C CD1 . ILE B 1 215 ? 24.533 95.814 -3.338 1.00 51.45 ? 236 ILE B CD1 1 ATOM 3472 N N . THR B 1 216 ? 28.379 93.520 -5.652 1.00 54.64 ? 237 THR B N 1 ATOM 3473 C CA . THR B 1 216 ? 29.720 93.698 -5.074 1.00 55.93 ? 237 THR B CA 1 ATOM 3474 C C . THR B 1 216 ? 30.762 92.897 -5.849 1.00 56.87 ? 237 THR B C 1 ATOM 3475 O O . THR B 1 216 ? 30.569 91.707 -6.096 1.00 57.99 ? 237 THR B O 1 ATOM 3476 C CB . THR B 1 216 ? 29.751 93.258 -3.592 1.00 56.18 ? 237 THR B CB 1 ATOM 3477 O OG1 . THR B 1 216 ? 28.697 93.907 -2.872 1.00 56.67 ? 237 THR B OG1 1 ATOM 3478 C CG2 . THR B 1 216 ? 31.086 93.592 -2.940 1.00 56.23 ? 237 THR B CG2 1 ATOM 3479 N N . LYS B 1 217 ? 31.864 93.553 -6.214 1.00 57.30 ? 238 LYS B N 1 ATOM 3480 C CA . LYS B 1 217 ? 32.939 92.941 -7.009 1.00 57.26 ? 238 LYS B CA 1 ATOM 3481 C C . LYS B 1 217 ? 33.410 91.614 -6.446 1.00 56.26 ? 238 LYS B C 1 ATOM 3482 O O . LYS B 1 217 ? 33.697 91.503 -5.255 1.00 56.18 ? 238 LYS B O 1 ATOM 3483 C CB . LYS B 1 217 ? 34.139 93.887 -7.142 1.00 60.66 ? 238 LYS B CB 1 ATOM 3484 C CG . LYS B 1 217 ? 34.003 94.919 -8.251 1.00 64.01 ? 238 LYS B CG 1 ATOM 3485 C CD . LYS B 1 217 ? 35.143 95.923 -8.220 1.00 64.97 ? 238 LYS B CD 1 ATOM 3486 C CE . LYS B 1 217 ? 34.812 97.141 -9.068 1.00 66.50 ? 238 LYS B CE 1 ATOM 3487 N NZ . LYS B 1 217 ? 35.683 98.292 -8.708 1.00 66.60 ? 238 LYS B NZ 1 ATOM 3488 N N . GLY B 1 218 ? 33.494 90.616 -7.323 1.00 55.16 ? 239 GLY B N 1 ATOM 3489 C CA . GLY B 1 218 ? 33.880 89.262 -6.937 1.00 53.68 ? 239 GLY B CA 1 ATOM 3490 C C . GLY B 1 218 ? 32.692 88.324 -6.791 1.00 52.16 ? 239 GLY B C 1 ATOM 3491 O O . GLY B 1 218 ? 32.870 87.122 -6.611 1.00 53.59 ? 239 GLY B O 1 ATOM 3492 N N . ASN B 1 219 ? 31.483 88.884 -6.861 1.00 49.79 ? 240 ASN B N 1 ATOM 3493 C CA . ASN B 1 219 ? 30.243 88.111 -6.771 1.00 48.74 ? 240 ASN B CA 1 ATOM 3494 C C . ASN B 1 219 ? 29.380 88.313 -8.011 1.00 45.28 ? 240 ASN B C 1 ATOM 3495 O O . ASN B 1 219 ? 28.539 89.212 -8.059 1.00 46.14 ? 240 ASN B O 1 ATOM 3496 C CB . ASN B 1 219 ? 29.459 88.490 -5.512 1.00 48.54 ? 240 ASN B CB 1 ATOM 3497 C CG . ASN B 1 219 ? 30.308 88.439 -4.263 1.00 50.96 ? 240 ASN B CG 1 ATOM 3498 O OD1 . ASN B 1 219 ? 30.714 87.369 -3.815 1.00 51.04 ? 240 ASN B OD1 1 ATOM 3499 N ND2 . ASN B 1 219 ? 30.589 89.606 -3.696 1.00 50.51 ? 240 ASN B ND2 1 ATOM 3500 N N . VAL B 1 220 ? 29.595 87.471 -9.015 1.00 45.64 ? 241 VAL B N 1 ATOM 3501 C CA . VAL B 1 220 ? 28.937 87.642 -10.308 1.00 45.67 ? 241 VAL B CA 1 ATOM 3502 C C . VAL B 1 220 ? 28.721 86.293 -11.015 1.00 43.93 ? 241 VAL B C 1 ATOM 3503 O O . VAL B 1 220 ? 29.424 85.319 -10.730 1.00 44.08 ? 241 VAL B O 1 ATOM 3504 C CB . VAL B 1 220 ? 29.729 88.647 -11.191 1.00 43.84 ? 241 VAL B CB 1 ATOM 3505 C CG1 . VAL B 1 220 ? 30.859 87.967 -11.950 1.00 44.88 ? 241 VAL B CG1 1 ATOM 3506 C CG2 . VAL B 1 220 ? 28.801 89.402 -12.127 1.00 44.91 ? 241 VAL B CG2 1 ATOM 3507 N N . GLU B 1 221 ? 27.748 86.253 -11.926 1.00 43.27 ? 242 GLU B N 1 ATOM 3508 C CA . GLU B 1 221 ? 27.397 85.032 -12.663 1.00 42.14 ? 242 GLU B CA 1 ATOM 3509 C C . GLU B 1 221 ? 26.509 85.320 -13.881 1.00 39.85 ? 242 GLU B C 1 ATOM 3510 O O . GLU B 1 221 ? 25.796 86.321 -13.917 1.00 38.99 ? 242 GLU B O 1 ATOM 3511 C CB . GLU B 1 221 ? 26.668 84.039 -11.739 1.00 39.46 ? 242 GLU B CB 1 ATOM 3512 C CG . GLU B 1 221 ? 25.233 84.442 -11.410 1.00 40.18 ? 242 GLU B CG 1 ATOM 3513 C CD . GLU B 1 221 ? 24.602 83.609 -10.304 1.00 40.40 ? 242 GLU B CD 1 ATOM 3514 O OE1 . GLU B 1 221 ? 25.332 83.109 -9.424 1.00 40.13 ? 242 GLU B OE1 1 ATOM 3515 O OE2 . GLU B 1 221 ? 23.363 83.470 -10.313 1.00 39.39 ? 242 GLU B OE2 1 ATOM 3516 N N . THR B 1 222 ? 26.557 84.427 -14.870 1.00 41.02 ? 243 THR B N 1 ATOM 3517 C CA . THR B 1 222 ? 25.542 84.393 -15.925 1.00 40.11 ? 243 THR B CA 1 ATOM 3518 C C . THR B 1 222 ? 24.307 83.649 -15.402 1.00 39.96 ? 243 THR B C 1 ATOM 3519 O O . THR B 1 222 ? 24.425 82.784 -14.526 1.00 38.93 ? 243 THR B O 1 ATOM 3520 C CB . THR B 1 222 ? 26.066 83.716 -17.211 1.00 41.10 ? 243 THR B CB 1 ATOM 3521 O OG1 . THR B 1 222 ? 26.630 82.432 -16.900 1.00 40.10 ? 243 THR B OG1 1 ATOM 3522 C CG2 . THR B 1 222 ? 27.130 84.586 -17.884 1.00 40.22 ? 243 THR B CG2 1 ATOM 3523 N N . ASN B 1 223 ? 23.133 84.013 -15.919 1.00 38.02 ? 244 ASN B N 1 ATOM 3524 C CA . ASN B 1 223 ? 21.866 83.361 -15.572 1.00 37.83 ? 244 ASN B CA 1 ATOM 3525 C C . ASN B 1 223 ? 21.078 83.043 -16.837 1.00 34.84 ? 244 ASN B C 1 ATOM 3526 O O . ASN B 1 223 ? 20.106 83.727 -17.164 1.00 36.56 ? 244 ASN B O 1 ATOM 3527 C CB . ASN B 1 223 ? 21.037 84.246 -14.642 1.00 38.08 ? 244 ASN B CB 1 ATOM 3528 C CG . ASN B 1 223 ? 21.695 84.454 -13.287 1.00 40.97 ? 244 ASN B CG 1 ATOM 3529 O OD1 . ASN B 1 223 ? 21.885 83.508 -12.523 1.00 39.81 ? 244 ASN B OD1 1 ATOM 3530 N ND2 . ASN B 1 223 ? 22.050 85.698 -12.986 1.00 40.62 ? 244 ASN B ND2 1 ATOM 3531 N N . ASP B 1 224 ? 21.513 82.005 -17.539 1.00 36.08 ? 245 ASP B N 1 ATOM 3532 C CA . ASP B 1 224 ? 20.966 81.646 -18.848 1.00 35.00 ? 245 ASP B CA 1 ATOM 3533 C C . ASP B 1 224 ? 19.974 80.483 -18.765 1.00 35.18 ? 245 ASP B C 1 ATOM 3534 O O . ASP B 1 224 ? 20.292 79.430 -18.214 1.00 33.65 ? 245 ASP B O 1 ATOM 3535 C CB . ASP B 1 224 ? 22.111 81.280 -19.797 1.00 36.37 ? 245 ASP B CB 1 ATOM 3536 C CG . ASP B 1 224 ? 23.140 82.401 -19.939 1.00 35.04 ? 245 ASP B CG 1 ATOM 3537 O OD1 . ASP B 1 224 ? 22.738 83.582 -19.945 1.00 38.66 ? 245 ASP B OD1 1 ATOM 3538 O OD2 . ASP B 1 224 ? 24.340 82.094 -20.040 1.00 36.24 ? 245 ASP B OD2 1 ATOM 3539 N N . ILE B 1 225 ? 18.777 80.692 -19.308 1.00 33.54 ? 246 ILE B N 1 ATOM 3540 C CA . ILE B 1 225 ? 17.787 79.625 -19.463 1.00 34.11 ? 246 ILE B CA 1 ATOM 3541 C C . ILE B 1 225 ? 17.898 79.079 -20.889 1.00 34.08 ? 246 ILE B C 1 ATOM 3542 O O . ILE B 1 225 ? 17.737 79.838 -21.855 1.00 34.13 ? 246 ILE B O 1 ATOM 3543 C CB . ILE B 1 225 ? 16.357 80.141 -19.193 1.00 34.08 ? 246 ILE B CB 1 ATOM 3544 C CG1 . ILE B 1 225 ? 16.258 80.834 -17.814 1.00 34.75 ? 246 ILE B CG1 1 ATOM 3545 C CG2 . ILE B 1 225 ? 15.328 79.012 -19.335 1.00 34.74 ? 246 ILE B CG2 1 ATOM 3546 C CD1 . ILE B 1 225 ? 16.453 79.933 -16.601 1.00 34.27 ? 246 ILE B CD1 1 ATOM 3547 N N . LEU B 1 226 ? 18.182 77.778 -21.006 1.00 31.75 ? 247 LEU B N 1 ATOM 3548 C CA . LEU B 1 226 ? 18.450 77.109 -22.294 1.00 32.02 ? 247 LEU B CA 1 ATOM 3549 C C . LEU B 1 226 ? 17.206 76.431 -22.892 1.00 31.87 ? 247 LEU B C 1 ATOM 3550 O O . LEU B 1 226 ? 17.092 76.314 -24.108 1.00 31.36 ? 247 LEU B O 1 ATOM 3551 C CB . LEU B 1 226 ? 19.568 76.081 -22.144 1.00 33.05 ? 247 LEU B CB 1 ATOM 3552 C CG . LEU B 1 226 ? 21.051 76.486 -22.116 1.00 35.67 ? 247 LEU B CG 1 ATOM 3553 C CD1 . LEU B 1 226 ? 21.386 77.554 -21.090 1.00 37.82 ? 247 LEU B CD1 1 ATOM 3554 C CD2 . LEU B 1 226 ? 21.891 75.244 -21.877 1.00 35.82 ? 247 LEU B CD2 1 ATOM 3555 N N . SER B 1 227 ? 16.288 75.975 -22.041 1.00 29.70 ? 248 SER B N 1 ATOM 3556 C CA . SER B 1 227 ? 15.004 75.422 -22.515 1.00 29.98 ? 248 SER B CA 1 ATOM 3557 C C . SER B 1 227 ? 13.954 75.525 -21.420 1.00 28.42 ? 248 SER B C 1 ATOM 3558 O O . SER B 1 227 ? 14.304 75.603 -20.239 1.00 28.94 ? 248 SER B O 1 ATOM 3559 C CB . SER B 1 227 ? 15.160 73.970 -22.993 1.00 30.89 ? 248 SER B CB 1 ATOM 3560 O OG . SER B 1 227 ? 15.644 73.121 -21.966 1.00 32.81 ? 248 SER B OG 1 ATOM 3561 N N . TRP B 1 228 ? 12.683 75.544 -21.806 1.00 26.99 ? 249 TRP B N 1 ATOM 3562 C CA . TRP B 1 228 ? 11.591 75.709 -20.859 1.00 27.81 ? 249 TRP B CA 1 ATOM 3563 C C . TRP B 1 228 ? 10.314 75.075 -21.349 1.00 28.23 ? 249 TRP B C 1 ATOM 3564 O O . TRP B 1 228 ? 9.873 75.321 -22.474 1.00 27.44 ? 249 TRP B O 1 ATOM 3565 C CB . TRP B 1 228 ? 11.388 77.201 -20.581 1.00 27.42 ? 249 TRP B CB 1 ATOM 3566 C CG . TRP B 1 228 ? 10.308 77.585 -19.596 1.00 28.68 ? 249 TRP B CG 1 ATOM 3567 C CD1 . TRP B 1 228 ? 9.870 76.878 -18.474 1.00 28.10 ? 249 TRP B CD1 1 ATOM 3568 C CD2 . TRP B 1 228 ? 9.524 78.831 -19.588 1.00 28.71 ? 249 TRP B CD2 1 ATOM 3569 N NE1 . TRP B 1 228 ? 8.882 77.564 -17.817 1.00 27.05 ? 249 TRP B NE1 1 ATOM 3570 C CE2 . TRP B 1 228 ? 8.633 78.748 -18.427 1.00 28.91 ? 249 TRP B CE2 1 ATOM 3571 C CE3 . TRP B 1 228 ? 9.468 79.962 -20.405 1.00 27.70 ? 249 TRP B CE3 1 ATOM 3572 C CZ2 . TRP B 1 228 ? 7.732 79.761 -18.118 1.00 29.36 ? 249 TRP B CZ2 1 ATOM 3573 C CZ3 . TRP B 1 228 ? 8.562 80.974 -20.088 1.00 27.79 ? 249 TRP B CZ3 1 ATOM 3574 C CH2 . TRP B 1 228 ? 7.712 80.880 -18.974 1.00 29.24 ? 249 TRP B CH2 1 ATOM 3575 N N . SER B 1 229 ? 9.714 74.247 -20.495 1.00 27.60 ? 250 SER B N 1 ATOM 3576 C CA . SER B 1 229 ? 8.393 73.692 -20.750 1.00 26.66 ? 250 SER B CA 1 ATOM 3577 C C . SER B 1 229 ? 7.476 73.986 -19.568 1.00 26.05 ? 250 SER B C 1 ATOM 3578 O O . SER B 1 229 ? 7.913 73.966 -18.419 1.00 25.59 ? 250 SER B O 1 ATOM 3579 C CB . SER B 1 229 ? 8.481 72.182 -20.967 1.00 27.31 ? 250 SER B CB 1 ATOM 3580 O OG . SER B 1 229 ? 9.458 71.870 -21.944 1.00 29.11 ? 250 SER B OG 1 ATOM 3581 N N . PHE B 1 230 ? 6.210 74.243 -19.862 1.00 24.27 ? 251 PHE B N 1 ATOM 3582 C CA . PHE B 1 230 ? 5.211 74.549 -18.847 1.00 24.79 ? 251 PHE B CA 1 ATOM 3583 C C . PHE B 1 230 ? 3.910 73.875 -19.236 1.00 24.98 ? 251 PHE B C 1 ATOM 3584 O O . PHE B 1 230 ? 3.615 73.735 -20.422 1.00 27.08 ? 251 PHE B O 1 ATOM 3585 C CB . PHE B 1 230 ? 5.019 76.079 -18.713 1.00 24.02 ? 251 PHE B CB 1 ATOM 3586 C CG . PHE B 1 230 ? 3.993 76.484 -17.674 1.00 25.28 ? 251 PHE B CG 1 ATOM 3587 C CD1 . PHE B 1 230 ? 4.359 76.657 -16.339 1.00 25.00 ? 251 PHE B CD1 1 ATOM 3588 C CD2 . PHE B 1 230 ? 2.667 76.690 -18.025 1.00 25.06 ? 251 PHE B CD2 1 ATOM 3589 C CE1 . PHE B 1 230 ? 3.414 77.014 -15.379 1.00 24.87 ? 251 PHE B CE1 1 ATOM 3590 C CE2 . PHE B 1 230 ? 1.721 77.050 -17.071 1.00 26.32 ? 251 PHE B CE2 1 ATOM 3591 C CZ . PHE B 1 230 ? 2.095 77.212 -15.742 1.00 25.63 ? 251 PHE B CZ 1 ATOM 3592 N N . ALA B 1 231 ? 3.140 73.447 -18.235 1.00 24.00 ? 252 ALA B N 1 ATOM 3593 C CA . ALA B 1 231 ? 1.821 72.865 -18.452 1.00 24.53 ? 252 ALA B CA 1 ATOM 3594 C C . ALA B 1 231 ? 0.973 73.135 -17.224 1.00 25.13 ? 252 ALA B C 1 ATOM 3595 O O . ALA B 1 231 ? 1.481 73.074 -16.106 1.00 26.54 ? 252 ALA B O 1 ATOM 3596 C CB . ALA B 1 231 ? 1.920 71.363 -18.705 1.00 23.59 ? 252 ALA B CB 1 ATOM 3597 N N . SER B 1 232 ? -0.302 73.450 -17.427 1.00 24.63 ? 253 SER B N 1 ATOM 3598 C CA . SER B 1 232 ? -1.224 73.648 -16.322 1.00 26.44 ? 253 SER B CA 1 ATOM 3599 C C . SER B 1 232 ? -2.625 73.212 -16.716 1.00 27.18 ? 253 SER B C 1 ATOM 3600 O O . SER B 1 232 ? -2.997 73.225 -17.897 1.00 27.25 ? 253 SER B O 1 ATOM 3601 C CB . SER B 1 232 ? -1.241 75.114 -15.866 1.00 27.89 ? 253 SER B CB 1 ATOM 3602 O OG . SER B 1 232 ? -1.620 75.956 -16.939 1.00 32.34 ? 253 SER B OG 1 ATOM 3603 N N . LYS B 1 233 ? -3.400 72.824 -15.713 1.00 27.05 ? 254 LYS B N 1 ATOM 3604 C CA . LYS B 1 233 ? -4.720 72.254 -15.926 1.00 30.36 ? 254 LYS B CA 1 ATOM 3605 C C . LYS B 1 233 ? -5.635 72.766 -14.823 1.00 30.15 ? 254 LYS B C 1 ATOM 3606 O O . LYS B 1 233 ? -5.278 72.711 -13.642 1.00 30.02 ? 254 LYS B O 1 ATOM 3607 C CB . LYS B 1 233 ? -4.625 70.722 -15.874 1.00 32.57 ? 254 LYS B CB 1 ATOM 3608 C CG . LYS B 1 233 ? -5.882 69.966 -16.278 1.00 37.39 ? 254 LYS B CG 1 ATOM 3609 C CD . LYS B 1 233 ? -5.534 68.522 -16.633 1.00 39.97 ? 254 LYS B CD 1 ATOM 3610 C CE . LYS B 1 233 ? -6.554 67.905 -17.580 1.00 44.46 ? 254 LYS B CE 1 ATOM 3611 N NZ . LYS B 1 233 ? -7.937 67.882 -17.019 1.00 46.31 ? 254 LYS B NZ 1 ATOM 3612 N N . LEU B 1 234 ? -6.806 73.265 -15.205 1.00 30.71 ? 255 LEU B N 1 ATOM 3613 C CA . LEU B 1 234 ? -7.772 73.767 -14.230 1.00 32.40 ? 255 LEU B CA 1 ATOM 3614 C C . LEU B 1 234 ? -9.140 73.161 -14.511 1.00 33.94 ? 255 LEU B C 1 ATOM 3615 O O . LEU B 1 234 ? -9.656 73.271 -15.623 1.00 33.84 ? 255 LEU B O 1 ATOM 3616 C CB . LEU B 1 234 ? -7.812 75.308 -14.269 1.00 32.05 ? 255 LEU B CB 1 ATOM 3617 C CG . LEU B 1 234 ? -8.735 76.089 -13.327 1.00 32.66 ? 255 LEU B CG 1 ATOM 3618 C CD1 . LEU B 1 234 ? -8.250 76.046 -11.886 1.00 31.40 ? 255 LEU B CD1 1 ATOM 3619 C CD2 . LEU B 1 234 ? -8.813 77.533 -13.791 1.00 34.34 ? 255 LEU B CD2 1 ATOM 3620 N N . SER B 1 235 ? -9.729 72.499 -13.520 1.00 35.70 ? 256 SER B N 1 ATOM 3621 C CA . SER B 1 235 ? -11.043 71.887 -13.724 1.00 38.41 ? 256 SER B CA 1 ATOM 3622 C C . SER B 1 235 ? -12.175 72.898 -13.511 1.00 39.66 ? 256 SER B C 1 ATOM 3623 O O . SER B 1 235 ? -11.926 74.105 -13.395 1.00 41.01 ? 256 SER B O 1 ATOM 3624 C CB . SER B 1 235 ? -11.225 70.676 -12.822 1.00 40.07 ? 256 SER B CB 1 ATOM 3625 O OG . SER B 1 235 ? -11.063 71.047 -11.468 1.00 44.23 ? 256 SER B OG 1 ATOM 3626 N N . LEU B 1 243 ? -1.754 66.569 -12.661 1.00 40.12 ? 264 LEU B N 1 ATOM 3627 C CA . LEU B 1 243 ? -1.082 66.379 -13.954 1.00 40.15 ? 264 LEU B CA 1 ATOM 3628 C C . LEU B 1 243 ? -0.451 64.995 -14.096 1.00 38.69 ? 264 LEU B C 1 ATOM 3629 O O . LEU B 1 243 ? -0.083 64.365 -13.096 1.00 40.01 ? 264 LEU B O 1 ATOM 3630 C CB . LEU B 1 243 ? -0.014 67.459 -14.189 1.00 41.65 ? 264 LEU B CB 1 ATOM 3631 C CG . LEU B 1 243 ? -0.347 68.609 -15.145 1.00 42.79 ? 264 LEU B CG 1 ATOM 3632 C CD1 . LEU B 1 243 ? -1.393 69.535 -14.559 1.00 42.81 ? 264 LEU B CD1 1 ATOM 3633 C CD2 . LEU B 1 243 ? 0.907 69.384 -15.501 1.00 43.68 ? 264 LEU B CD2 1 ATOM 3634 N N . ASN B 1 244 ? -0.339 64.530 -15.343 1.00 36.09 ? 265 ASN B N 1 ATOM 3635 C CA . ASN B 1 244 ? 0.373 63.293 -15.660 1.00 33.68 ? 265 ASN B CA 1 ATOM 3636 C C . ASN B 1 244 ? 1.872 63.599 -15.763 1.00 33.57 ? 265 ASN B C 1 ATOM 3637 O O . ASN B 1 244 ? 2.358 64.098 -16.780 1.00 33.42 ? 265 ASN B O 1 ATOM 3638 C CB . ASN B 1 244 ? -0.180 62.653 -16.951 1.00 32.63 ? 265 ASN B CB 1 ATOM 3639 C CG . ASN B 1 244 ? 0.447 61.290 -17.259 1.00 33.27 ? 265 ASN B CG 1 ATOM 3640 O OD1 . ASN B 1 244 ? 1.606 61.015 -16.906 1.00 31.73 ? 265 ASN B OD1 1 ATOM 3641 N ND2 . ASN B 1 244 ? -0.307 60.438 -17.945 1.00 30.73 ? 265 ASN B ND2 1 ATOM 3642 N N . LEU B 1 245 ? 2.593 63.314 -14.686 1.00 33.25 ? 266 LEU B N 1 ATOM 3643 C CA . LEU B 1 245 ? 4.015 63.645 -14.610 1.00 33.60 ? 266 LEU B CA 1 ATOM 3644 C C . LEU B 1 245 ? 4.899 62.769 -15.500 1.00 33.05 ? 266 LEU B C 1 ATOM 3645 O O . LEU B 1 245 ? 5.954 63.219 -15.951 1.00 32.54 ? 266 LEU B O 1 ATOM 3646 C CB . LEU B 1 245 ? 4.507 63.622 -13.161 1.00 33.77 ? 266 LEU B CB 1 ATOM 3647 C CG . LEU B 1 245 ? 3.903 64.699 -12.258 1.00 34.46 ? 266 LEU B CG 1 ATOM 3648 C CD1 . LEU B 1 245 ? 4.546 64.663 -10.877 1.00 33.74 ? 266 LEU B CD1 1 ATOM 3649 C CD2 . LEU B 1 245 ? 4.046 66.074 -12.909 1.00 34.55 ? 266 LEU B CD2 1 ATOM 3650 N N . ALA B 1 246 ? 4.482 61.525 -15.745 1.00 31.87 ? 267 ALA B N 1 ATOM 3651 C CA . ALA B 1 246 ? 5.186 60.674 -16.699 1.00 31.20 ? 267 ALA B CA 1 ATOM 3652 C C . ALA B 1 246 ? 5.145 61.312 -18.089 1.00 31.59 ? 267 ALA B C 1 ATOM 3653 O O . ALA B 1 246 ? 6.175 61.414 -18.756 1.00 31.92 ? 267 ALA B O 1 ATOM 3654 C CB . ALA B 1 246 ? 4.590 59.269 -16.729 1.00 27.13 ? 267 ALA B CB 1 ATOM 3655 N N . ASN B 1 247 ? 3.962 61.750 -18.527 1.00 31.87 ? 268 ASN B N 1 ATOM 3656 C CA . ASN B 1 247 ? 3.843 62.502 -19.794 1.00 33.28 ? 268 ASN B CA 1 ATOM 3657 C C . ASN B 1 247 ? 4.612 63.815 -19.848 1.00 34.25 ? 268 ASN B C 1 ATOM 3658 O O . ASN B 1 247 ? 5.297 64.098 -20.845 1.00 32.41 ? 268 ASN B O 1 ATOM 3659 C CB . ASN B 1 247 ? 2.383 62.755 -20.173 1.00 35.10 ? 268 ASN B CB 1 ATOM 3660 C CG . ASN B 1 247 ? 1.716 61.524 -20.761 1.00 37.00 ? 268 ASN B CG 1 ATOM 3661 O OD1 . ASN B 1 247 ? 2.322 60.457 -20.848 1.00 35.50 ? 268 ASN B OD1 1 ATOM 3662 N ND2 . ASN B 1 247 ? 0.462 61.667 -21.162 1.00 35.47 ? 268 ASN B ND2 1 ATOM 3663 N N . PHE B 1 248 ? 4.489 64.619 -18.792 1.00 32.50 ? 269 PHE B N 1 ATOM 3664 C CA . PHE B 1 248 ? 5.161 65.900 -18.773 1.00 34.20 ? 269 PHE B CA 1 ATOM 3665 C C . PHE B 1 248 ? 6.701 65.769 -18.844 1.00 35.38 ? 269 PHE B C 1 ATOM 3666 O O . PHE B 1 248 ? 7.356 66.385 -19.696 1.00 33.69 ? 269 PHE B O 1 ATOM 3667 C CB . PHE B 1 248 ? 4.730 66.749 -17.571 1.00 34.86 ? 269 PHE B CB 1 ATOM 3668 C CG . PHE B 1 248 ? 5.348 68.113 -17.579 1.00 34.55 ? 269 PHE B CG 1 ATOM 3669 C CD1 . PHE B 1 248 ? 4.821 69.113 -18.371 1.00 36.31 ? 269 PHE B CD1 1 ATOM 3670 C CD2 . PHE B 1 248 ? 6.522 68.363 -16.874 1.00 34.38 ? 269 PHE B CD2 1 ATOM 3671 C CE1 . PHE B 1 248 ? 5.414 70.367 -18.418 1.00 33.02 ? 269 PHE B CE1 1 ATOM 3672 C CE2 . PHE B 1 248 ? 7.117 69.613 -16.910 1.00 34.50 ? 269 PHE B CE2 1 ATOM 3673 C CZ . PHE B 1 248 ? 6.561 70.615 -17.693 1.00 32.73 ? 269 PHE B CZ 1 ATOM 3674 N N . ALA B 1 249 ? 7.265 64.948 -17.960 1.00 36.01 ? 270 ALA B N 1 ATOM 3675 C CA . ALA B 1 249 ? 8.720 64.789 -17.862 1.00 38.22 ? 270 ALA B CA 1 ATOM 3676 C C . ALA B 1 249 ? 9.376 64.390 -19.187 1.00 40.18 ? 270 ALA B C 1 ATOM 3677 O O . ALA B 1 249 ? 10.521 64.758 -19.448 1.00 42.93 ? 270 ALA B O 1 ATOM 3678 C CB . ALA B 1 249 ? 9.064 63.779 -16.779 1.00 37.11 ? 270 ALA B CB 1 ATOM 3679 N N . LEU B 1 250 ? 8.647 63.650 -20.021 1.00 40.37 ? 271 LEU B N 1 ATOM 3680 C CA . LEU B 1 250 ? 9.205 63.117 -21.266 1.00 40.73 ? 271 LEU B CA 1 ATOM 3681 C C . LEU B 1 250 ? 9.385 64.173 -22.367 1.00 42.00 ? 271 LEU B C 1 ATOM 3682 O O . LEU B 1 250 ? 8.487 64.991 -22.616 1.00 44.47 ? 271 LEU B O 1 ATOM 3683 C CB . LEU B 1 250 ? 8.345 61.949 -21.763 1.00 39.15 ? 271 LEU B CB 1 ATOM 3684 C CG . LEU B 1 250 ? 9.054 60.961 -22.674 1.00 36.71 ? 271 LEU B CG 1 ATOM 3685 C CD1 . LEU B 1 250 ? 10.324 60.462 -22.012 1.00 34.49 ? 271 LEU B CD1 1 ATOM 3686 C CD2 . LEU B 1 250 ? 8.130 59.808 -23.018 1.00 37.20 ? 271 LEU B CD2 1 HETATM 3687 C C1 . NAG C 2 . ? -11.796 43.295 -14.658 1.00 32.89 ? 1001 NAG A C1 1 HETATM 3688 C C2 . NAG C 2 . ? -12.533 42.725 -13.442 1.00 38.67 ? 1001 NAG A C2 1 HETATM 3689 C C3 . NAG C 2 . ? -13.179 41.379 -13.770 1.00 39.72 ? 1001 NAG A C3 1 HETATM 3690 C C4 . NAG C 2 . ? -14.097 41.504 -14.986 1.00 38.18 ? 1001 NAG A C4 1 HETATM 3691 C C5 . NAG C 2 . ? -13.323 42.179 -16.137 1.00 37.24 ? 1001 NAG A C5 1 HETATM 3692 C C6 . NAG C 2 . ? -14.282 42.518 -17.272 1.00 37.06 ? 1001 NAG A C6 1 HETATM 3693 C C7 . NAG C 2 . ? -11.776 43.301 -11.201 1.00 43.65 ? 1001 NAG A C7 1 HETATM 3694 C C8 . NAG C 2 . ? -10.808 43.020 -10.081 1.00 42.43 ? 1001 NAG A C8 1 HETATM 3695 N N2 . NAG C 2 . ? -11.647 42.549 -12.293 1.00 41.19 ? 1001 NAG A N2 1 HETATM 3696 O O3 . NAG C 2 . ? -13.884 40.900 -12.641 1.00 42.03 ? 1001 NAG A O3 1 HETATM 3697 O O4 . NAG C 2 . ? -14.545 40.210 -15.355 1.00 38.32 ? 1001 NAG A O4 1 HETATM 3698 O O5 . NAG C 2 . ? -12.671 43.393 -15.771 1.00 32.89 ? 1001 NAG A O5 1 HETATM 3699 O O6 . NAG C 2 . ? -13.790 41.864 -18.411 1.00 45.68 ? 1001 NAG A O6 1 HETATM 3700 O O7 . NAG C 2 . ? -12.620 44.195 -11.109 1.00 42.52 ? 1001 NAG A O7 1 HETATM 3701 MN MN . MN D 3 . ? 18.604 47.597 -1.014 1.00 15.94 ? 1002 MN A MN 1 HETATM 3702 CA CA . CA E 4 . ? 16.792 44.867 1.525 1.00 17.37 ? 1003 CA A CA 1 HETATM 3703 C C1 . MAN F 5 . ? 17.753 35.370 4.286 1.00 23.42 ? 1004 MAN A C1 1 HETATM 3704 C C2 . MAN F 5 . ? 16.619 36.386 4.195 1.00 21.77 ? 1004 MAN A C2 1 HETATM 3705 C C3 . MAN F 5 . ? 16.257 36.622 2.724 1.00 22.75 ? 1004 MAN A C3 1 HETATM 3706 C C4 . MAN F 5 . ? 17.488 37.108 1.959 1.00 22.91 ? 1004 MAN A C4 1 HETATM 3707 C C5 . MAN F 5 . ? 18.585 36.047 2.105 1.00 23.18 ? 1004 MAN A C5 1 HETATM 3708 C C6 . MAN F 5 . ? 19.879 36.420 1.393 1.00 24.61 ? 1004 MAN A C6 1 HETATM 3709 O O1 . MAN F 5 . ? 17.300 34.095 3.864 1.00 24.27 ? 1004 MAN A O1 1 HETATM 3710 O O2 . MAN F 5 . ? 17.061 37.629 4.712 1.00 20.60 ? 1004 MAN A O2 1 HETATM 3711 O O3 . MAN F 5 . ? 15.243 37.603 2.656 1.00 22.47 ? 1004 MAN A O3 1 HETATM 3712 O O4 . MAN F 5 . ? 17.196 37.385 0.591 1.00 22.93 ? 1004 MAN A O4 1 HETATM 3713 O O5 . MAN F 5 . ? 18.853 35.828 3.494 1.00 23.60 ? 1004 MAN A O5 1 HETATM 3714 O O6 . MAN F 5 . ? 20.726 35.277 1.369 1.00 24.62 ? 1004 MAN A O6 1 HETATM 3715 C C1 . NAG G 2 . ? 16.723 37.802 6.101 1.00 22.48 ? 1005 NAG A C1 1 HETATM 3716 C C2 . NAG G 2 . ? 17.798 38.686 6.723 1.00 22.84 ? 1005 NAG A C2 1 HETATM 3717 C C3 . NAG G 2 . ? 17.461 38.959 8.184 1.00 22.89 ? 1005 NAG A C3 1 HETATM 3718 C C4 . NAG G 2 . ? 16.039 39.501 8.353 1.00 22.84 ? 1005 NAG A C4 1 HETATM 3719 C C5 . NAG G 2 . ? 15.041 38.591 7.618 1.00 21.75 ? 1005 NAG A C5 1 HETATM 3720 C C6 . NAG G 2 . ? 13.629 39.167 7.602 1.00 21.30 ? 1005 NAG A C6 1 HETATM 3721 C C7 . NAG G 2 . ? 20.039 38.362 5.775 1.00 23.76 ? 1005 NAG A C7 1 HETATM 3722 C C8 . NAG G 2 . ? 21.286 37.521 5.820 1.00 24.02 ? 1005 NAG A C8 1 HETATM 3723 N N2 . NAG G 2 . ? 19.075 37.999 6.622 1.00 22.88 ? 1005 NAG A N2 1 HETATM 3724 O O3 . NAG G 2 . ? 18.404 39.856 8.732 1.00 23.71 ? 1005 NAG A O3 1 HETATM 3725 O O4 . NAG G 2 . ? 15.793 39.491 9.752 1.00 22.97 ? 1005 NAG A O4 1 HETATM 3726 O O5 . NAG G 2 . ? 15.444 38.399 6.270 1.00 22.26 ? 1005 NAG A O5 1 HETATM 3727 O O6 . NAG G 2 . ? 12.778 38.242 6.943 1.00 21.65 ? 1005 NAG A O6 1 HETATM 3728 O O7 . NAG G 2 . ? 19.954 39.308 4.990 1.00 23.63 ? 1005 NAG A O7 1 HETATM 3729 C C1 . GAL H 6 . ? 15.334 40.751 10.230 1.00 22.08 ? 1006 GAL A C1 1 HETATM 3730 C C2 . GAL H 6 . ? 15.089 40.596 11.734 1.00 22.71 ? 1006 GAL A C2 1 HETATM 3731 C C3 . GAL H 6 . ? 14.728 41.958 12.321 1.00 22.93 ? 1006 GAL A C3 1 HETATM 3732 C C4 . GAL H 6 . ? 15.767 43.007 11.940 1.00 23.11 ? 1006 GAL A C4 1 HETATM 3733 C C5 . GAL H 6 . ? 15.968 43.058 10.419 1.00 22.28 ? 1006 GAL A C5 1 HETATM 3734 C C6 . GAL H 6 . ? 17.124 43.967 9.975 1.00 22.40 ? 1006 GAL A C6 1 HETATM 3735 O O2 . GAL H 6 . ? 14.087 39.621 11.970 1.00 22.13 ? 1006 GAL A O2 1 HETATM 3736 O O3 . GAL H 6 . ? 14.639 41.857 13.731 1.00 23.75 ? 1006 GAL A O3 1 HETATM 3737 O O4 . GAL H 6 . ? 17.008 42.651 12.534 1.00 23.15 ? 1006 GAL A O4 1 HETATM 3738 O O5 . GAL H 6 . ? 16.288 41.755 9.976 1.00 22.35 ? 1006 GAL A O5 1 HETATM 3739 O O6 . GAL H 6 . ? 16.898 45.324 10.284 1.00 22.69 ? 1006 GAL A O6 1 HETATM 3740 C C1 . EDO I 7 . ? 8.963 64.611 -8.038 1.00 30.18 ? 1007 EDO A C1 1 HETATM 3741 O O1 . EDO I 7 . ? 8.754 63.304 -7.498 1.00 30.03 ? 1007 EDO A O1 1 HETATM 3742 C C2 . EDO I 7 . ? 7.629 65.309 -8.273 1.00 29.98 ? 1007 EDO A C2 1 HETATM 3743 O O2 . EDO I 7 . ? 7.905 66.639 -8.720 1.00 31.89 ? 1007 EDO A O2 1 HETATM 3744 C C1 . EDO J 7 . ? 13.452 64.338 -12.760 1.00 27.48 ? 1008 EDO A C1 1 HETATM 3745 O O1 . EDO J 7 . ? 13.168 62.953 -12.610 1.00 28.55 ? 1008 EDO A O1 1 HETATM 3746 C C2 . EDO J 7 . ? 13.685 64.931 -11.375 1.00 28.53 ? 1008 EDO A C2 1 HETATM 3747 O O2 . EDO J 7 . ? 13.937 66.343 -11.476 1.00 30.20 ? 1008 EDO A O2 1 HETATM 3748 C C1 . EDO K 7 . ? 8.284 53.348 -28.053 1.00 34.49 ? 1009 EDO A C1 1 HETATM 3749 O O1 . EDO K 7 . ? 7.074 52.825 -27.492 1.00 34.07 ? 1009 EDO A O1 1 HETATM 3750 C C2 . EDO K 7 . ? 9.350 53.603 -27.007 1.00 30.98 ? 1009 EDO A C2 1 HETATM 3751 O O2 . EDO K 7 . ? 9.374 52.495 -26.106 1.00 31.03 ? 1009 EDO A O2 1 HETATM 3752 C C1 . EDO L 7 . ? 6.407 38.067 -18.607 1.00 31.04 ? 1010 EDO A C1 1 HETATM 3753 O O1 . EDO L 7 . ? 6.810 36.712 -18.455 1.00 36.99 ? 1010 EDO A O1 1 HETATM 3754 C C2 . EDO L 7 . ? 5.569 38.187 -19.871 1.00 32.95 ? 1010 EDO A C2 1 HETATM 3755 O O2 . EDO L 7 . ? 6.386 38.530 -20.997 1.00 27.28 ? 1010 EDO A O2 1 HETATM 3756 C C1 . EDO M 7 . ? -5.129 48.952 -15.644 1.00 24.21 ? 1011 EDO A C1 1 HETATM 3757 O O1 . EDO M 7 . ? -4.881 47.594 -15.332 1.00 21.07 ? 1011 EDO A O1 1 HETATM 3758 C C2 . EDO M 7 . ? -6.410 49.054 -16.464 1.00 25.36 ? 1011 EDO A C2 1 HETATM 3759 O O2 . EDO M 7 . ? -7.500 49.328 -15.584 1.00 28.78 ? 1011 EDO A O2 1 HETATM 3760 C C1 . NAG N 2 . ? 12.843 86.116 -33.503 1.00 50.49 ? 1001 NAG B C1 1 HETATM 3761 C C2 . NAG N 2 . ? 14.247 85.899 -34.047 1.00 54.84 ? 1001 NAG B C2 1 HETATM 3762 C C3 . NAG N 2 . ? 14.635 87.089 -34.924 1.00 56.10 ? 1001 NAG B C3 1 HETATM 3763 C C4 . NAG N 2 . ? 13.562 87.436 -35.965 1.00 55.40 ? 1001 NAG B C4 1 HETATM 3764 C C5 . NAG N 2 . ? 12.110 87.170 -35.536 1.00 54.43 ? 1001 NAG B C5 1 HETATM 3765 C C6 . NAG N 2 . ? 11.344 86.799 -36.800 1.00 53.22 ? 1001 NAG B C6 1 HETATM 3766 C C7 . NAG N 2 . ? 15.966 84.610 -32.848 1.00 56.18 ? 1001 NAG B C7 1 HETATM 3767 C C8 . NAG N 2 . ? 16.891 84.560 -31.665 1.00 55.64 ? 1001 NAG B C8 1 HETATM 3768 N N2 . NAG N 2 . ? 15.198 85.698 -32.963 1.00 55.55 ? 1001 NAG B N2 1 HETATM 3769 O O3 . NAG N 2 . ? 15.830 86.770 -35.599 1.00 58.40 ? 1001 NAG B O3 1 HETATM 3770 O O4 . NAG N 2 . ? 13.681 88.795 -36.354 1.00 56.77 ? 1001 NAG B O4 1 HETATM 3771 O O5 . NAG N 2 . ? 11.930 86.118 -34.583 1.00 52.44 ? 1001 NAG B O5 1 HETATM 3772 O O6 . NAG N 2 . ? 9.963 86.933 -36.579 1.00 54.22 ? 1001 NAG B O6 1 HETATM 3773 O O7 . NAG N 2 . ? 15.958 83.673 -33.648 1.00 55.47 ? 1001 NAG B O7 1 HETATM 3774 MN MN . MN O 3 . ? 17.875 82.028 -0.332 1.00 32.41 ? 1002 MN B MN 1 HETATM 3775 CA CA . CA P 4 . ? 20.723 84.667 -1.271 1.00 35.91 ? 1003 CA B CA 1 HETATM 3776 C C1 . MAN Q 5 . ? 23.369 93.934 0.323 1.00 44.03 ? 1004 MAN B C1 1 HETATM 3777 C C2 . MAN Q 5 . ? 23.582 92.853 -0.746 1.00 44.57 ? 1004 MAN B C2 1 HETATM 3778 C C3 . MAN Q 5 . ? 22.291 92.639 -1.541 1.00 44.39 ? 1004 MAN B C3 1 HETATM 3779 C C4 . MAN Q 5 . ? 21.136 92.314 -0.594 1.00 45.00 ? 1004 MAN B C4 1 HETATM 3780 C C5 . MAN Q 5 . ? 21.013 93.434 0.444 1.00 45.71 ? 1004 MAN B C5 1 HETATM 3781 C C6 . MAN Q 5 . ? 19.905 93.146 1.443 1.00 45.56 ? 1004 MAN B C6 1 HETATM 3782 O O1 . MAN Q 5 . ? 23.217 95.202 -0.288 1.00 43.79 ? 1004 MAN B O1 1 HETATM 3783 O O2 . MAN Q 5 . ? 23.966 91.636 -0.131 1.00 44.54 ? 1004 MAN B O2 1 HETATM 3784 O O3 . MAN Q 5 . ? 22.485 91.634 -2.513 1.00 44.35 ? 1004 MAN B O3 1 HETATM 3785 O O4 . MAN Q 5 . ? 19.912 92.177 -1.282 1.00 47.03 ? 1004 MAN B O4 1 HETATM 3786 O O5 . MAN Q 5 . ? 22.240 93.612 1.133 1.00 43.46 ? 1004 MAN B O5 1 HETATM 3787 O O6 . MAN Q 5 . ? 20.048 94.013 2.540 1.00 47.61 ? 1004 MAN B O6 1 HETATM 3788 C C1 . NAG R 2 . ? 25.394 91.475 -0.114 1.00 44.04 ? 1005 NAG B C1 1 HETATM 3789 C C2 . NAG R 2 . ? 25.801 90.641 1.108 1.00 44.89 ? 1005 NAG B C2 1 HETATM 3790 C C3 . NAG R 2 . ? 27.304 90.359 1.114 1.00 44.52 ? 1005 NAG B C3 1 HETATM 3791 C C4 . NAG R 2 . ? 27.727 89.743 -0.212 1.00 44.63 ? 1005 NAG B C4 1 HETATM 3792 C C5 . NAG R 2 . ? 27.288 90.700 -1.327 1.00 44.02 ? 1005 NAG B C5 1 HETATM 3793 C C6 . NAG R 2 . ? 27.662 90.233 -2.724 1.00 46.14 ? 1005 NAG B C6 1 HETATM 3794 C C7 . NAG R 2 . ? 24.239 91.130 2.945 1.00 47.87 ? 1005 NAG B C7 1 HETATM 3795 C C8 . NAG R 2 . ? 24.015 91.950 4.184 1.00 46.00 ? 1005 NAG B C8 1 HETATM 3796 N N2 . NAG R 2 . ? 25.404 91.326 2.318 1.00 45.99 ? 1005 NAG B N2 1 HETATM 3797 O O3 . NAG R 2 . ? 27.648 89.500 2.176 1.00 45.53 ? 1005 NAG B O3 1 HETATM 3798 O O4 . NAG R 2 . ? 29.118 89.481 -0.221 1.00 43.70 ? 1005 NAG B O4 1 HETATM 3799 O O5 . NAG R 2 . ? 25.883 90.889 -1.299 1.00 43.55 ? 1005 NAG B O5 1 HETATM 3800 O O6 . NAG R 2 . ? 27.012 91.055 -3.671 1.00 46.79 ? 1005 NAG B O6 1 HETATM 3801 O O7 . NAG R 2 . ? 23.369 90.338 2.572 1.00 46.48 ? 1005 NAG B O7 1 HETATM 3802 O O . HOH S 8 . ? 16.610 49.629 7.840 1.00 25.42 ? 1101 HOH A O 1 HETATM 3803 O O . HOH S 8 . ? 20.325 48.185 -1.849 1.00 19.30 ? 1102 HOH A O 1 HETATM 3804 O O . HOH S 8 . ? 18.613 46.029 -2.187 1.00 19.21 ? 1103 HOH A O 1 HETATM 3805 O O . HOH S 8 . ? 17.280 44.133 -0.641 1.00 19.80 ? 1104 HOH A O 1 HETATM 3806 O O . HOH S 8 . ? 14.662 43.990 1.429 1.00 17.59 ? 1105 HOH A O 1 HETATM 3807 O O . HOH S 8 . ? 18.112 49.010 4.650 1.00 16.40 ? 1106 HOH A O 1 HETATM 3808 O O . HOH S 8 . ? 22.873 47.723 -1.704 1.00 16.50 ? 1107 HOH A O 1 HETATM 3809 O O . HOH S 8 . ? 24.661 49.763 -2.647 1.00 25.63 ? 1108 HOH A O 1 HETATM 3810 O O . HOH S 8 . ? -2.249 39.790 -3.790 1.00 20.21 ? 1109 HOH A O 1 HETATM 3811 O O . HOH S 8 . ? 1.492 41.739 1.317 1.00 18.40 ? 1110 HOH A O 1 HETATM 3812 O O . HOH S 8 . ? 0.238 43.821 -1.371 1.00 19.49 ? 1111 HOH A O 1 HETATM 3813 O O . HOH S 8 . ? -3.843 39.015 -1.800 1.00 23.95 ? 1112 HOH A O 1 HETATM 3814 O O . HOH S 8 . ? 9.207 36.729 0.099 1.00 21.04 ? 1113 HOH A O 1 HETATM 3815 O O . HOH S 8 . ? 2.372 34.304 1.924 1.00 22.95 ? 1114 HOH A O 1 HETATM 3816 O O . HOH S 8 . ? 5.412 45.690 -20.544 1.00 19.15 ? 1115 HOH A O 1 HETATM 3817 O O . HOH S 8 . ? 22.344 40.225 -7.108 1.00 20.97 ? 1116 HOH A O 1 HETATM 3818 O O . HOH S 8 . ? 29.675 40.368 -7.370 1.00 43.43 ? 1117 HOH A O 1 HETATM 3819 O O . HOH S 8 . ? 27.004 43.787 -7.625 1.00 35.16 ? 1118 HOH A O 1 HETATM 3820 O O . HOH S 8 . ? 5.658 53.964 2.859 1.00 20.08 ? 1119 HOH A O 1 HETATM 3821 O O . HOH S 8 . ? 3.629 53.876 1.014 1.00 21.18 ? 1120 HOH A O 1 HETATM 3822 O O . HOH S 8 . ? 1.391 60.741 1.987 1.00 27.60 ? 1121 HOH A O 1 HETATM 3823 O O . HOH S 8 . ? 12.844 38.152 4.155 1.00 22.26 ? 1122 HOH A O 1 HETATM 3824 O O . HOH S 8 . ? 15.352 40.072 3.741 1.00 22.25 ? 1123 HOH A O 1 HETATM 3825 O O . HOH S 8 . ? 22.076 39.886 3.425 1.00 21.91 ? 1124 HOH A O 1 HETATM 3826 O O . HOH S 8 . ? 20.140 41.694 7.779 1.00 23.34 ? 1125 HOH A O 1 HETATM 3827 O O . HOH S 8 . ? 21.153 42.181 10.311 1.00 28.74 ? 1126 HOH A O 1 HETATM 3828 O O . HOH S 8 . ? 18.797 40.796 11.442 1.00 28.65 ? 1127 HOH A O 1 HETATM 3829 O O . HOH S 8 . ? 11.516 44.632 9.732 1.00 26.22 ? 1128 HOH A O 1 HETATM 3830 O O . HOH S 8 . ? 12.967 46.711 8.457 1.00 18.32 ? 1129 HOH A O 1 HETATM 3831 O O . HOH S 8 . ? 15.631 46.916 8.457 1.00 20.52 ? 1130 HOH A O 1 HETATM 3832 O O . HOH S 8 . ? -1.442 48.919 2.116 1.00 21.32 ? 1131 HOH A O 1 HETATM 3833 O O . HOH S 8 . ? -4.285 49.600 -0.064 1.00 33.79 ? 1132 HOH A O 1 HETATM 3834 O O . HOH S 8 . ? -7.608 46.797 -2.244 1.00 21.62 ? 1133 HOH A O 1 HETATM 3835 O O . HOH S 8 . ? -5.934 51.641 -7.151 1.00 17.70 ? 1134 HOH A O 1 HETATM 3836 O O . HOH S 8 . ? -10.587 41.897 -3.416 1.00 30.48 ? 1135 HOH A O 1 HETATM 3837 O O . HOH S 8 . ? -4.012 34.279 2.445 1.00 38.21 ? 1136 HOH A O 1 HETATM 3838 O O . HOH S 8 . ? 5.025 39.320 11.024 1.00 34.14 ? 1137 HOH A O 1 HETATM 3839 O O . HOH S 8 . ? -1.756 58.462 2.525 1.00 28.29 ? 1138 HOH A O 1 HETATM 3840 O O . HOH S 8 . ? 9.262 60.880 5.452 1.00 22.95 ? 1139 HOH A O 1 HETATM 3841 O O . HOH S 8 . ? 12.512 54.289 7.810 1.00 28.05 ? 1140 HOH A O 1 HETATM 3842 O O . HOH S 8 . ? 17.169 62.615 -1.147 1.00 20.59 ? 1141 HOH A O 1 HETATM 3843 O O . HOH S 8 . ? 22.375 59.419 -3.577 1.00 31.69 ? 1142 HOH A O 1 HETATM 3844 O O . HOH S 8 . ? 20.417 62.718 -4.118 1.00 28.43 ? 1143 HOH A O 1 HETATM 3845 O O . HOH S 8 . ? 21.865 60.622 -6.166 1.00 23.86 ? 1144 HOH A O 1 HETATM 3846 O O . HOH S 8 . ? 21.752 59.488 1.535 1.00 35.73 ? 1145 HOH A O 1 HETATM 3847 O O . HOH S 8 . ? 6.349 53.448 10.049 1.00 23.15 ? 1146 HOH A O 1 HETATM 3848 O O . HOH S 8 . ? 2.226 33.426 -0.747 1.00 28.33 ? 1147 HOH A O 1 HETATM 3849 O O . HOH S 8 . ? 5.966 33.274 -2.625 1.00 35.75 ? 1148 HOH A O 1 HETATM 3850 O O . HOH S 8 . ? 3.687 32.180 -3.666 1.00 35.02 ? 1149 HOH A O 1 HETATM 3851 O O . HOH S 8 . ? -2.053 36.237 -3.602 1.00 30.05 ? 1150 HOH A O 1 HETATM 3852 O O . HOH S 8 . ? 15.938 35.286 -0.591 1.00 24.85 ? 1151 HOH A O 1 HETATM 3853 O O . HOH S 8 . ? 22.672 47.042 -8.777 1.00 19.80 ? 1152 HOH A O 1 HETATM 3854 O O . HOH S 8 . ? 26.392 46.536 -7.945 1.00 33.57 ? 1153 HOH A O 1 HETATM 3855 O O . HOH S 8 . ? 25.659 46.774 -10.777 1.00 20.99 ? 1154 HOH A O 1 HETATM 3856 O O . HOH S 8 . ? 17.374 39.175 -22.613 1.00 34.34 ? 1155 HOH A O 1 HETATM 3857 O O . HOH S 8 . ? 17.000 36.779 -21.054 1.00 33.87 ? 1156 HOH A O 1 HETATM 3858 O O . HOH S 8 . ? 15.183 39.103 -24.327 1.00 22.96 ? 1157 HOH A O 1 HETATM 3859 O O . HOH S 8 . ? 12.933 40.745 -24.434 1.00 24.41 ? 1158 HOH A O 1 HETATM 3860 O O . HOH S 8 . ? 11.603 40.005 -26.873 1.00 31.66 ? 1159 HOH A O 1 HETATM 3861 O O . HOH S 8 . ? 14.339 42.136 -27.826 1.00 24.55 ? 1160 HOH A O 1 HETATM 3862 O O . HOH S 8 . ? 12.688 35.605 -20.933 1.00 31.10 ? 1161 HOH A O 1 HETATM 3863 O O . HOH S 8 . ? 14.409 36.174 -18.939 1.00 33.44 ? 1162 HOH A O 1 HETATM 3864 O O . HOH S 8 . ? 14.246 37.200 -16.341 1.00 29.50 ? 1163 HOH A O 1 HETATM 3865 O O . HOH S 8 . ? 13.424 38.389 -13.273 1.00 23.21 ? 1164 HOH A O 1 HETATM 3866 O O . HOH S 8 . ? 15.702 39.530 -12.881 1.00 29.11 ? 1165 HOH A O 1 HETATM 3867 O O . HOH S 8 . ? 20.664 36.370 -9.628 1.00 30.94 ? 1166 HOH A O 1 HETATM 3868 O O . HOH S 8 . ? -0.547 36.381 -10.028 1.00 26.45 ? 1167 HOH A O 1 HETATM 3869 O O . HOH S 8 . ? -1.810 37.512 -15.933 1.00 26.70 ? 1168 HOH A O 1 HETATM 3870 O O . HOH S 8 . ? -6.363 39.259 -9.441 1.00 24.71 ? 1169 HOH A O 1 HETATM 3871 O O . HOH S 8 . ? -6.589 41.477 -4.077 1.00 24.97 ? 1170 HOH A O 1 HETATM 3872 O O . HOH S 8 . ? 2.055 34.644 7.287 1.00 29.72 ? 1171 HOH A O 1 HETATM 3873 O O . HOH S 8 . ? 19.243 64.232 -18.211 1.00 28.35 ? 1172 HOH A O 1 HETATM 3874 O O . HOH S 8 . ? 16.167 61.353 -16.179 1.00 19.63 ? 1173 HOH A O 1 HETATM 3875 O O . HOH S 8 . ? -12.062 51.744 -6.601 1.00 19.71 ? 1174 HOH A O 1 HETATM 3876 O O . HOH S 8 . ? -12.659 52.345 -4.037 1.00 22.62 ? 1175 HOH A O 1 HETATM 3877 O O . HOH S 8 . ? -10.647 52.757 -2.470 1.00 30.98 ? 1176 HOH A O 1 HETATM 3878 O O . HOH S 8 . ? -10.456 52.054 0.242 1.00 27.54 ? 1177 HOH A O 1 HETATM 3879 O O . HOH S 8 . ? -13.649 45.963 1.307 1.00 28.40 ? 1178 HOH A O 1 HETATM 3880 O O . HOH S 8 . ? -5.510 56.256 -7.674 1.00 29.98 ? 1179 HOH A O 1 HETATM 3881 O O . HOH S 8 . ? -8.121 54.083 -14.203 1.00 26.66 ? 1180 HOH A O 1 HETATM 3882 O O . HOH S 8 . ? -6.480 39.765 -21.520 1.00 32.30 ? 1181 HOH A O 1 HETATM 3883 O O . HOH S 8 . ? 4.810 40.638 -22.996 1.00 34.35 ? 1182 HOH A O 1 HETATM 3884 O O . HOH S 8 . ? 5.119 48.941 -27.502 1.00 23.25 ? 1183 HOH A O 1 HETATM 3885 O O . HOH S 8 . ? 8.658 50.395 -31.037 1.00 27.24 ? 1184 HOH A O 1 HETATM 3886 O O . HOH S 8 . ? 15.499 57.815 -28.969 1.00 22.40 ? 1185 HOH A O 1 HETATM 3887 O O . HOH S 8 . ? 27.629 43.222 -1.266 1.00 30.58 ? 1186 HOH A O 1 HETATM 3888 O O . HOH S 8 . ? 21.616 55.610 0.898 1.00 32.34 ? 1187 HOH A O 1 HETATM 3889 O O . HOH S 8 . ? 25.053 55.342 -3.043 1.00 26.77 ? 1188 HOH A O 1 HETATM 3890 O O . HOH S 8 . ? 17.692 60.949 1.081 1.00 30.87 ? 1189 HOH A O 1 HETATM 3891 O O . HOH S 8 . ? 25.151 50.851 -16.984 1.00 28.04 ? 1190 HOH A O 1 HETATM 3892 O O . HOH S 8 . ? 21.761 53.586 -22.928 1.00 31.71 ? 1191 HOH A O 1 HETATM 3893 O O . HOH S 8 . ? 15.282 53.281 -33.817 1.00 34.39 ? 1192 HOH A O 1 HETATM 3894 O O . HOH S 8 . ? 7.542 50.259 -28.250 1.00 25.06 ? 1193 HOH A O 1 HETATM 3895 O O . HOH S 8 . ? 19.515 35.835 8.420 1.00 37.24 ? 1194 HOH A O 1 HETATM 3896 O O . HOH S 8 . ? 22.710 34.941 3.300 1.00 31.50 ? 1195 HOH A O 1 HETATM 3897 O O . HOH S 8 . ? 21.581 34.941 -1.292 1.00 30.92 ? 1196 HOH A O 1 HETATM 3898 O O . HOH S 8 . ? 22.439 30.662 -7.372 1.00 47.12 ? 1197 HOH A O 1 HETATM 3899 O O . HOH S 8 . ? -2.690 35.273 -14.346 1.00 36.04 ? 1198 HOH A O 1 HETATM 3900 O O . HOH S 8 . ? -4.072 38.733 -16.292 1.00 30.91 ? 1199 HOH A O 1 HETATM 3901 O O . HOH S 8 . ? 2.319 55.760 9.965 1.00 30.80 ? 1200 HOH A O 1 HETATM 3902 O O . HOH S 8 . ? 4.855 61.089 -9.090 1.00 27.93 ? 1201 HOH A O 1 HETATM 3903 O O . HOH S 8 . ? -1.536 59.698 -5.661 1.00 34.93 ? 1202 HOH A O 1 HETATM 3904 O O . HOH S 8 . ? 13.841 66.803 0.642 1.00 27.93 ? 1203 HOH A O 1 HETATM 3905 O O . HOH S 8 . ? 21.446 61.297 -1.564 1.00 39.65 ? 1204 HOH A O 1 HETATM 3906 O O . HOH S 8 . ? -3.135 34.033 6.918 1.00 33.97 ? 1205 HOH A O 1 HETATM 3907 O O . HOH S 8 . ? 13.184 34.225 -16.561 1.00 31.40 ? 1206 HOH A O 1 HETATM 3908 O O . HOH S 8 . ? 21.850 44.338 -24.200 1.00 34.53 ? 1207 HOH A O 1 HETATM 3909 O O . HOH S 8 . ? -4.724 57.962 -15.070 1.00 31.87 ? 1208 HOH A O 1 HETATM 3910 O O . HOH S 8 . ? 3.481 66.048 -5.450 1.00 34.20 ? 1209 HOH A O 1 HETATM 3911 O O . HOH S 8 . ? 12.953 61.816 -19.954 1.00 35.57 ? 1210 HOH A O 1 HETATM 3912 O O . HOH S 8 . ? 14.444 62.608 -18.222 1.00 31.35 ? 1211 HOH A O 1 HETATM 3913 O O . HOH S 8 . ? -4.928 45.402 3.693 1.00 34.32 ? 1212 HOH A O 1 HETATM 3914 O O . HOH S 8 . ? 22.559 42.076 -18.735 1.00 32.71 ? 1213 HOH A O 1 HETATM 3915 O O . HOH S 8 . ? 26.355 48.394 -17.660 1.00 37.75 ? 1214 HOH A O 1 HETATM 3916 O O . HOH S 8 . ? 17.833 42.585 -28.141 1.00 33.93 ? 1215 HOH A O 1 HETATM 3917 O O . HOH S 8 . ? 19.480 57.480 -28.669 1.00 37.92 ? 1216 HOH A O 1 HETATM 3918 O O . HOH S 8 . ? 10.254 67.959 -8.754 1.00 31.90 ? 1217 HOH A O 1 HETATM 3919 O O . HOH S 8 . ? 12.413 61.818 -10.382 1.00 28.48 ? 1218 HOH A O 1 HETATM 3920 O O . HOH S 8 . ? 24.957 44.654 10.966 1.00 31.01 ? 1219 HOH A O 1 HETATM 3921 O O . HOH S 8 . ? 23.435 37.076 -9.241 1.00 39.23 ? 1220 HOH A O 1 HETATM 3922 O O . HOH S 8 . ? 7.436 31.539 -10.005 1.00 31.60 ? 1221 HOH A O 1 HETATM 3923 O O . HOH S 8 . ? -8.946 48.231 1.895 1.00 44.80 ? 1222 HOH A O 1 HETATM 3924 O O . HOH S 8 . ? 0.481 57.624 -11.437 1.00 26.34 ? 1223 HOH A O 1 HETATM 3925 O O . HOH S 8 . ? 15.717 53.532 8.207 1.00 32.74 ? 1224 HOH A O 1 HETATM 3926 O O . HOH S 8 . ? 8.568 61.535 8.109 1.00 36.97 ? 1225 HOH A O 1 HETATM 3927 O O . HOH T 8 . ? 16.768 83.570 -0.633 1.00 36.11 ? 1101 HOH B O 1 HETATM 3928 O O . HOH T 8 . ? 16.471 81.512 0.856 1.00 31.29 ? 1102 HOH B O 1 HETATM 3929 O O . HOH T 8 . ? 18.829 70.458 3.837 1.00 34.42 ? 1103 HOH B O 1 HETATM 3930 O O . HOH T 8 . ? 20.999 85.740 -3.310 1.00 39.39 ? 1104 HOH B O 1 HETATM 3931 O O . HOH T 8 . ? 18.603 85.553 -1.564 1.00 36.81 ? 1105 HOH B O 1 HETATM 3932 O O . HOH T 8 . ? 1.034 65.433 -4.462 1.00 33.32 ? 1106 HOH B O 1 HETATM 3933 O O . HOH T 8 . ? 23.118 63.462 -5.483 1.00 28.16 ? 1107 HOH B O 1 HETATM 3934 O O . HOH T 8 . ? 17.862 67.213 -1.680 1.00 23.90 ? 1108 HOH B O 1 HETATM 3935 O O . HOH T 8 . ? 11.996 69.246 1.495 1.00 27.61 ? 1109 HOH B O 1 HETATM 3936 O O . HOH T 8 . ? 14.826 70.852 -19.136 1.00 37.45 ? 1110 HOH B O 1 HETATM 3937 O O . HOH T 8 . ? 15.816 77.335 5.424 1.00 36.53 ? 1111 HOH B O 1 HETATM 3938 O O . HOH T 8 . ? 14.275 70.284 2.756 1.00 27.94 ? 1112 HOH B O 1 HETATM 3939 O O . HOH T 8 . ? 18.529 74.078 3.462 1.00 37.65 ? 1113 HOH B O 1 HETATM 3940 O O . HOH T 8 . ? 13.730 74.440 5.260 1.00 36.85 ? 1114 HOH B O 1 HETATM 3941 O O . HOH T 8 . ? 24.929 75.640 -11.690 1.00 35.67 ? 1115 HOH B O 1 HETATM 3942 O O . HOH T 8 . ? 3.744 68.334 -6.758 1.00 24.92 ? 1116 HOH B O 1 HETATM 3943 O O . HOH T 8 . ? 23.179 80.528 0.992 1.00 35.77 ? 1117 HOH B O 1 HETATM 3944 O O . HOH T 8 . ? 12.464 97.297 -19.146 1.00 52.12 ? 1118 HOH B O 1 HETATM 3945 O O . HOH T 8 . ? 2.270 91.217 -17.373 1.00 41.38 ? 1119 HOH B O 1 HETATM 3946 O O . HOH T 8 . ? 2.389 67.241 -9.120 1.00 34.94 ? 1120 HOH B O 1 HETATM 3947 O O . HOH T 8 . ? 26.394 68.806 -7.506 1.00 31.74 ? 1121 HOH B O 1 HETATM 3948 O O . HOH T 8 . ? 1.211 58.416 -19.411 1.00 26.08 ? 1122 HOH B O 1 HETATM 3949 O O . HOH T 8 . ? 17.534 63.836 -16.052 1.00 30.63 ? 1123 HOH B O 1 HETATM 3950 O O . HOH T 8 . ? 25.258 68.778 -16.122 1.00 39.12 ? 1124 HOH B O 1 HETATM 3951 O O . HOH T 8 . ? 2.901 84.161 -18.410 1.00 34.24 ? 1125 HOH B O 1 # loop_ _pdbx_poly_seq_scheme.asym_id _pdbx_poly_seq_scheme.entity_id _pdbx_poly_seq_scheme.seq_id _pdbx_poly_seq_scheme.mon_id _pdbx_poly_seq_scheme.ndb_seq_num _pdbx_poly_seq_scheme.pdb_seq_num _pdbx_poly_seq_scheme.auth_seq_num _pdbx_poly_seq_scheme.pdb_mon_id _pdbx_poly_seq_scheme.auth_mon_id _pdbx_poly_seq_scheme.pdb_strand_id _pdbx_poly_seq_scheme.pdb_ins_code _pdbx_poly_seq_scheme.hetero A 1 1 ALA 1 22 22 ALA ALA A . n A 1 2 SER 2 23 23 SER SER A . n A 1 3 GLN 3 24 24 GLN GLN A . n A 1 4 THR 4 25 25 THR THR A . n A 1 5 SER 5 26 26 SER SER A . n A 1 6 PHE 6 27 27 PHE PHE A . n A 1 7 SER 7 28 28 SER SER A . n A 1 8 PHE 8 29 29 PHE PHE A . n A 1 9 GLN 9 30 30 GLN GLN A . n A 1 10 ARG 10 31 31 ARG ARG A . n A 1 11 PHE 11 32 32 PHE PHE A . n A 1 12 ASN 12 33 33 ASN ASN A . n A 1 13 GLU 13 34 34 GLU GLU A . n A 1 14 THR 14 35 35 THR THR A . n A 1 15 ASN 15 36 36 ASN ASN A . n A 1 16 LEU 16 37 37 LEU LEU A . n A 1 17 ILE 17 38 38 ILE ILE A . n A 1 18 LEU 18 39 39 LEU LEU A . n A 1 19 GLN 19 40 40 GLN GLN A . n A 1 20 ARG 20 41 41 ARG ARG A . n A 1 21 ASP 21 42 42 ASP ASP A . n A 1 22 ALA 22 43 43 ALA ALA A . n A 1 23 THR 23 44 44 THR THR A . n A 1 24 VAL 24 45 45 VAL VAL A . n A 1 25 SER 25 46 46 SER SER A . n A 1 26 SER 26 47 47 SER SER A . n A 1 27 LYS 27 48 48 LYS LYS A . n A 1 28 GLY 28 49 49 GLY GLY A . n A 1 29 GLN 29 50 50 GLN GLN A . n A 1 30 LEU 30 51 51 LEU LEU A . n A 1 31 ARG 31 52 52 ARG ARG A . n A 1 32 LEU 32 53 53 LEU LEU A . n A 1 33 THR 33 54 54 THR THR A . n A 1 34 ASN 34 55 55 ASN ASN A . n A 1 35 VAL 35 56 56 VAL VAL A . n A 1 36 ASN 36 57 57 ASN ASN A . n A 1 37 ASP 37 58 58 ASP ASP A . n A 1 38 ASN 38 59 59 ASN ASN A . n A 1 39 GLY 39 60 60 GLY GLY A . n A 1 40 GLU 40 61 61 GLU GLU A . n A 1 41 PRO 41 62 62 PRO PRO A . n A 1 42 THR 42 63 63 THR THR A . n A 1 43 LEU 43 64 64 LEU LEU A . n A 1 44 SER 44 65 65 SER SER A . n A 1 45 SER 45 66 66 SER SER A . n A 1 46 LEU 46 67 67 LEU LEU A . n A 1 47 GLY 47 68 68 GLY GLY A . n A 1 48 ARG 48 69 69 ARG ARG A . n A 1 49 ALA 49 70 70 ALA ALA A . n A 1 50 PHE 50 71 71 PHE PHE A . n A 1 51 TYR 51 72 72 TYR TYR A . n A 1 52 SER 52 73 73 SER SER A . n A 1 53 ALA 53 74 74 ALA ALA A . n A 1 54 PRO 54 75 75 PRO PRO A . n A 1 55 ILE 55 76 76 ILE ILE A . n A 1 56 GLN 56 77 77 GLN GLN A . n A 1 57 ILE 57 78 78 ILE ILE A . n A 1 58 TRP 58 79 79 TRP TRP A . n A 1 59 ASP 59 80 80 ASP ASP A . n A 1 60 ASN 60 81 81 ASN ASN A . n A 1 61 THR 61 82 82 THR THR A . n A 1 62 THR 62 83 83 THR THR A . n A 1 63 GLY 63 84 84 GLY GLY A . n A 1 64 ALA 64 85 85 ALA ALA A . n A 1 65 VAL 65 86 86 VAL VAL A . n A 1 66 ALA 66 87 87 ALA ALA A . n A 1 67 SER 67 88 88 SER SER A . n A 1 68 PHE 68 89 89 PHE PHE A . n A 1 69 ALA 69 90 90 ALA ALA A . n A 1 70 THR 70 91 91 THR THR A . n A 1 71 SER 71 92 92 SER SER A . n A 1 72 PHE 72 93 93 PHE PHE A . n A 1 73 THR 73 94 94 THR THR A . n A 1 74 PHE 74 95 95 PHE PHE A . n A 1 75 ASN 75 96 96 ASN ASN A . n A 1 76 ILE 76 97 97 ILE ILE A . n A 1 77 ASP 77 98 98 ASP ASP A . n A 1 78 VAL 78 99 99 VAL VAL A . n A 1 79 PRO 79 100 100 PRO PRO A . n A 1 80 ASN 80 101 101 ASN ASN A . n A 1 81 ASN 81 102 102 ASN ASN A . n A 1 82 SER 82 103 103 SER SER A . n A 1 83 GLY 83 104 104 GLY GLY A . n A 1 84 PRO 84 105 105 PRO PRO A . n A 1 85 ALA 85 106 106 ALA ALA A . n A 1 86 ASP 86 107 107 ASP ASP A . n A 1 87 GLY 87 108 108 GLY GLY A . n A 1 88 LEU 88 109 109 LEU LEU A . n A 1 89 ALA 89 110 110 ALA ALA A . n A 1 90 PHE 90 111 111 PHE PHE A . n A 1 91 VAL 91 112 112 VAL VAL A . n A 1 92 LEU 92 113 113 LEU LEU A . n A 1 93 LEU 93 114 114 LEU LEU A . n A 1 94 PRO 94 115 115 PRO PRO A . n A 1 95 VAL 95 116 116 VAL VAL A . n A 1 96 GLY 96 117 117 GLY GLY A . n A 1 97 SER 97 118 118 SER SER A . n A 1 98 GLN 98 119 119 GLN GLN A . n A 1 99 PRO 99 120 120 PRO PRO A . n A 1 100 LYS 100 121 121 LYS LYS A . n A 1 101 ASP 101 122 122 ASP ASP A . n A 1 102 LYS 102 123 123 LYS LYS A . n A 1 103 GLY 103 124 124 GLY GLY A . n A 1 104 GLY 104 125 125 GLY GLY A . n A 1 105 LEU 105 126 126 LEU LEU A . n A 1 106 LEU 106 127 127 LEU LEU A . n A 1 107 GLY 107 128 128 GLY GLY A . n A 1 108 LEU 108 129 129 LEU LEU A . n A 1 109 PHE 109 130 130 PHE PHE A . n A 1 110 ASN 110 131 131 ASN ASN A . n A 1 111 ASN 111 132 132 ASN ASN A . n A 1 112 TYR 112 133 133 TYR TYR A . n A 1 113 LYS 113 134 134 LYS LYS A . n A 1 114 TYR 114 135 135 TYR TYR A . n A 1 115 ASP 115 136 136 ASP ASP A . n A 1 116 SER 116 137 137 SER SER A . n A 1 117 ASN 117 138 138 ASN ASN A . n A 1 118 ALA 118 139 139 ALA ALA A . n A 1 119 HIS 119 140 140 HIS HIS A . n A 1 120 THR 120 141 141 THR THR A . n A 1 121 VAL 121 142 142 VAL VAL A . n A 1 122 ALA 122 143 143 ALA ALA A . n A 1 123 VAL 123 144 144 VAL VAL A . n A 1 124 GLU 124 145 145 GLU GLU A . n A 1 125 PHE 125 146 146 PHE PHE A . n A 1 126 ASP 126 147 147 ASP ASP A . n A 1 127 THR 127 148 148 THR THR A . n A 1 128 LEU 128 149 149 LEU LEU A . n A 1 129 TYR 129 150 150 TYR TYR A . n A 1 130 ASN 130 151 151 ASN ASN A . n A 1 131 VAL 131 152 152 VAL VAL A . n A 1 132 HIS 132 153 153 HIS HIS A . n A 1 133 TRP 133 154 154 TRP TRP A . n A 1 134 ASP 134 155 155 ASP ASP A . n A 1 135 PRO 135 156 156 PRO PRO A . n A 1 136 LYS 136 157 157 LYS LYS A . n A 1 137 PRO 137 158 158 PRO PRO A . n A 1 138 ARG 138 159 159 ARG ARG A . n A 1 139 HIS 139 160 160 HIS HIS A . n A 1 140 ILE 140 161 161 ILE ILE A . n A 1 141 GLY 141 162 162 GLY GLY A . n A 1 142 ILE 142 163 163 ILE ILE A . n A 1 143 ASP 143 164 164 ASP ASP A . n A 1 144 VAL 144 165 165 VAL VAL A . n A 1 145 ASN 145 166 166 ASN ASN A . n A 1 146 SER 146 167 167 SER SER A . n A 1 147 ILE 147 168 168 ILE ILE A . n A 1 148 LYS 148 169 169 LYS LYS A . n A 1 149 SER 149 170 170 SER SER A . n A 1 150 ILE 150 171 171 ILE ILE A . n A 1 151 LYS 151 172 172 LYS LYS A . n A 1 152 THR 152 173 173 THR THR A . n A 1 153 THR 153 174 174 THR THR A . n A 1 154 THR 154 175 175 THR THR A . n A 1 155 TRP 155 176 176 TRP TRP A . n A 1 156 ASP 156 177 177 ASP ASP A . n A 1 157 PHE 157 178 178 PHE PHE A . n A 1 158 VAL 158 179 179 VAL VAL A . n A 1 159 LYS 159 180 180 LYS LYS A . n A 1 160 GLY 160 181 181 GLY GLY A . n A 1 161 GLU 161 182 182 GLU GLU A . n A 1 162 ASN 162 183 183 ASN ASN A . n A 1 163 ALA 163 184 184 ALA ALA A . n A 1 164 GLU 164 185 185 GLU GLU A . n A 1 165 VAL 165 186 186 VAL VAL A . n A 1 166 LEU 166 187 187 LEU LEU A . n A 1 167 ILE 167 188 188 ILE ILE A . n A 1 168 THR 168 189 189 THR THR A . n A 1 169 TYR 169 190 190 TYR TYR A . n A 1 170 ASP 170 191 191 ASP ASP A . n A 1 171 SER 171 192 192 SER SER A . n A 1 172 SER 172 193 193 SER SER A . n A 1 173 THR 173 194 194 THR THR A . n A 1 174 LYS 174 195 195 LYS LYS A . n A 1 175 LEU 175 196 196 LEU LEU A . n A 1 176 LEU 176 197 197 LEU LEU A . n A 1 177 VAL 177 198 198 VAL VAL A . n A 1 178 ALA 178 199 199 ALA ALA A . n A 1 179 SER 179 200 200 SER SER A . n A 1 180 LEU 180 201 201 LEU LEU A . n A 1 181 VAL 181 202 202 VAL VAL A . n A 1 182 TYR 182 203 203 TYR TYR A . n A 1 183 PRO 183 204 204 PRO PRO A . n A 1 184 SER 184 205 205 SER SER A . n A 1 185 LEU 185 206 206 LEU LEU A . n A 1 186 LYS 186 207 207 LYS LYS A . n A 1 187 THR 187 208 208 THR THR A . n A 1 188 SER 188 209 209 SER SER A . n A 1 189 PHE 189 210 210 PHE PHE A . n A 1 190 ILE 190 211 211 ILE ILE A . n A 1 191 VAL 191 212 212 VAL VAL A . n A 1 192 SER 192 213 213 SER SER A . n A 1 193 ASP 193 214 214 ASP ASP A . n A 1 194 THR 194 215 215 THR THR A . n A 1 195 VAL 195 216 216 VAL VAL A . n A 1 196 ASP 196 217 217 ASP ASP A . n A 1 197 LEU 197 218 218 LEU LEU A . n A 1 198 LYS 198 219 219 LYS LYS A . n A 1 199 SER 199 220 220 SER SER A . n A 1 200 VAL 200 221 221 VAL VAL A . n A 1 201 LEU 201 222 222 LEU LEU A . n A 1 202 PRO 202 223 223 PRO PRO A . n A 1 203 GLU 203 224 224 GLU GLU A . n A 1 204 TRP 204 225 225 TRP TRP A . n A 1 205 VAL 205 226 226 VAL VAL A . n A 1 206 ILE 206 227 227 ILE ILE A . n A 1 207 VAL 207 228 228 VAL VAL A . n A 1 208 GLY 208 229 229 GLY GLY A . n A 1 209 PHE 209 230 230 PHE PHE A . n A 1 210 THR 210 231 231 THR THR A . n A 1 211 ALA 211 232 232 ALA ALA A . n A 1 212 THR 212 233 233 THR THR A . n A 1 213 THR 213 234 234 THR THR A . n A 1 214 GLY 214 235 235 GLY GLY A . n A 1 215 ILE 215 236 236 ILE ILE A . n A 1 216 THR 216 237 237 THR THR A . n A 1 217 LYS 217 238 238 LYS LYS A . n A 1 218 GLY 218 239 239 GLY GLY A . n A 1 219 ASN 219 240 240 ASN ASN A . n A 1 220 VAL 220 241 241 VAL VAL A . n A 1 221 GLU 221 242 242 GLU GLU A . n A 1 222 THR 222 243 243 THR THR A . n A 1 223 ASN 223 244 244 ASN ASN A . n A 1 224 ASP 224 245 245 ASP ASP A . n A 1 225 ILE 225 246 246 ILE ILE A . n A 1 226 LEU 226 247 247 LEU LEU A . n A 1 227 SER 227 248 248 SER SER A . n A 1 228 TRP 228 249 249 TRP TRP A . n A 1 229 SER 229 250 250 SER SER A . n A 1 230 PHE 230 251 251 PHE PHE A . n A 1 231 ALA 231 252 252 ALA ALA A . n A 1 232 SER 232 253 253 SER SER A . n A 1 233 LYS 233 254 254 LYS LYS A . n A 1 234 LEU 234 255 255 LEU LEU A . n A 1 235 SER 235 256 256 SER SER A . n A 1 236 ASP 236 257 257 ASP ASP A . n A 1 237 GLY 237 258 258 GLY GLY A . n A 1 238 THR 238 259 259 THR THR A . n A 1 239 THR 239 260 ? ? ? A . n A 1 240 SER 240 261 ? ? ? A . n A 1 241 GLU 241 262 ? ? ? A . n A 1 242 ALA 242 263 ? ? ? A . n A 1 243 LEU 243 264 ? ? ? A . n A 1 244 ASN 244 265 ? ? ? A . n A 1 245 LEU 245 266 ? ? ? A . n A 1 246 ALA 246 267 ? ? ? A . n A 1 247 ASN 247 268 ? ? ? A . n A 1 248 PHE 248 269 ? ? ? A . n A 1 249 ALA 249 270 ? ? ? A . n A 1 250 LEU 250 271 ? ? ? A . n A 1 251 ASN 251 272 ? ? ? A . n A 1 252 GLN 252 273 ? ? ? A . n A 1 253 ILE 253 274 ? ? ? A . n A 1 254 LEU 254 275 ? ? ? A . n B 1 1 ALA 1 22 22 ALA ALA B . n B 1 2 SER 2 23 23 SER SER B . n B 1 3 GLN 3 24 24 GLN GLN B . n B 1 4 THR 4 25 25 THR THR B . n B 1 5 SER 5 26 26 SER SER B . n B 1 6 PHE 6 27 27 PHE PHE B . n B 1 7 SER 7 28 28 SER SER B . n B 1 8 PHE 8 29 29 PHE PHE B . n B 1 9 GLN 9 30 30 GLN GLN B . n B 1 10 ARG 10 31 31 ARG ARG B . n B 1 11 PHE 11 32 32 PHE PHE B . n B 1 12 ASN 12 33 33 ASN ASN B . n B 1 13 GLU 13 34 34 GLU GLU B . n B 1 14 THR 14 35 35 THR THR B . n B 1 15 ASN 15 36 36 ASN ASN B . n B 1 16 LEU 16 37 37 LEU LEU B . n B 1 17 ILE 17 38 38 ILE ILE B . n B 1 18 LEU 18 39 39 LEU LEU B . n B 1 19 GLN 19 40 40 GLN GLN B . n B 1 20 ARG 20 41 41 ARG ARG B . n B 1 21 ASP 21 42 42 ASP ASP B . n B 1 22 ALA 22 43 43 ALA ALA B . n B 1 23 THR 23 44 44 THR THR B . n B 1 24 VAL 24 45 45 VAL VAL B . n B 1 25 SER 25 46 46 SER SER B . n B 1 26 SER 26 47 47 SER SER B . n B 1 27 LYS 27 48 48 LYS LYS B . n B 1 28 GLY 28 49 49 GLY GLY B . n B 1 29 GLN 29 50 50 GLN GLN B . n B 1 30 LEU 30 51 51 LEU LEU B . n B 1 31 ARG 31 52 52 ARG ARG B . n B 1 32 LEU 32 53 53 LEU LEU B . n B 1 33 THR 33 54 54 THR THR B . n B 1 34 ASN 34 55 55 ASN ASN B . n B 1 35 VAL 35 56 56 VAL VAL B . n B 1 36 ASN 36 57 57 ASN ASN B . n B 1 37 ASP 37 58 ? ? ? B . n B 1 38 ASN 38 59 ? ? ? B . n B 1 39 GLY 39 60 ? ? ? B . n B 1 40 GLU 40 61 61 GLU GLU B . n B 1 41 PRO 41 62 62 PRO PRO B . n B 1 42 THR 42 63 63 THR THR B . n B 1 43 LEU 43 64 64 LEU LEU B . n B 1 44 SER 44 65 65 SER SER B . n B 1 45 SER 45 66 66 SER SER B . n B 1 46 LEU 46 67 67 LEU LEU B . n B 1 47 GLY 47 68 68 GLY GLY B . n B 1 48 ARG 48 69 69 ARG ARG B . n B 1 49 ALA 49 70 70 ALA ALA B . n B 1 50 PHE 50 71 71 PHE PHE B . n B 1 51 TYR 51 72 72 TYR TYR B . n B 1 52 SER 52 73 73 SER SER B . n B 1 53 ALA 53 74 74 ALA ALA B . n B 1 54 PRO 54 75 75 PRO PRO B . n B 1 55 ILE 55 76 76 ILE ILE B . n B 1 56 GLN 56 77 77 GLN GLN B . n B 1 57 ILE 57 78 78 ILE ILE B . n B 1 58 TRP 58 79 79 TRP TRP B . n B 1 59 ASP 59 80 80 ASP ASP B . n B 1 60 ASN 60 81 81 ASN ASN B . n B 1 61 THR 61 82 82 THR THR B . n B 1 62 THR 62 83 83 THR THR B . n B 1 63 GLY 63 84 84 GLY GLY B . n B 1 64 ALA 64 85 85 ALA ALA B . n B 1 65 VAL 65 86 86 VAL VAL B . n B 1 66 ALA 66 87 87 ALA ALA B . n B 1 67 SER 67 88 88 SER SER B . n B 1 68 PHE 68 89 89 PHE PHE B . n B 1 69 ALA 69 90 90 ALA ALA B . n B 1 70 THR 70 91 91 THR THR B . n B 1 71 SER 71 92 92 SER SER B . n B 1 72 PHE 72 93 93 PHE PHE B . n B 1 73 THR 73 94 94 THR THR B . n B 1 74 PHE 74 95 95 PHE PHE B . n B 1 75 ASN 75 96 96 ASN ASN B . n B 1 76 ILE 76 97 97 ILE ILE B . n B 1 77 ASP 77 98 98 ASP ASP B . n B 1 78 VAL 78 99 99 VAL VAL B . n B 1 79 PRO 79 100 100 PRO PRO B . n B 1 80 ASN 80 101 101 ASN ASN B . n B 1 81 ASN 81 102 102 ASN ASN B . n B 1 82 SER 82 103 103 SER SER B . n B 1 83 GLY 83 104 104 GLY GLY B . n B 1 84 PRO 84 105 105 PRO PRO B . n B 1 85 ALA 85 106 106 ALA ALA B . n B 1 86 ASP 86 107 107 ASP ASP B . n B 1 87 GLY 87 108 108 GLY GLY B . n B 1 88 LEU 88 109 109 LEU LEU B . n B 1 89 ALA 89 110 110 ALA ALA B . n B 1 90 PHE 90 111 111 PHE PHE B . n B 1 91 VAL 91 112 112 VAL VAL B . n B 1 92 LEU 92 113 113 LEU LEU B . n B 1 93 LEU 93 114 114 LEU LEU B . n B 1 94 PRO 94 115 115 PRO PRO B . n B 1 95 VAL 95 116 116 VAL VAL B . n B 1 96 GLY 96 117 117 GLY GLY B . n B 1 97 SER 97 118 118 SER SER B . n B 1 98 GLN 98 119 119 GLN GLN B . n B 1 99 PRO 99 120 120 PRO PRO B . n B 1 100 LYS 100 121 121 LYS LYS B . n B 1 101 ASP 101 122 122 ASP ASP B . n B 1 102 LYS 102 123 123 LYS LYS B . n B 1 103 GLY 103 124 124 GLY GLY B . n B 1 104 GLY 104 125 125 GLY GLY B . n B 1 105 LEU 105 126 126 LEU LEU B . n B 1 106 LEU 106 127 127 LEU LEU B . n B 1 107 GLY 107 128 128 GLY GLY B . n B 1 108 LEU 108 129 129 LEU LEU B . n B 1 109 PHE 109 130 130 PHE PHE B . n B 1 110 ASN 110 131 131 ASN ASN B . n B 1 111 ASN 111 132 132 ASN ASN B . n B 1 112 TYR 112 133 133 TYR TYR B . n B 1 113 LYS 113 134 134 LYS LYS B . n B 1 114 TYR 114 135 135 TYR TYR B . n B 1 115 ASP 115 136 136 ASP ASP B . n B 1 116 SER 116 137 137 SER SER B . n B 1 117 ASN 117 138 138 ASN ASN B . n B 1 118 ALA 118 139 139 ALA ALA B . n B 1 119 HIS 119 140 140 HIS HIS B . n B 1 120 THR 120 141 141 THR THR B . n B 1 121 VAL 121 142 142 VAL VAL B . n B 1 122 ALA 122 143 143 ALA ALA B . n B 1 123 VAL 123 144 144 VAL VAL B . n B 1 124 GLU 124 145 145 GLU GLU B . n B 1 125 PHE 125 146 146 PHE PHE B . n B 1 126 ASP 126 147 147 ASP ASP B . n B 1 127 THR 127 148 148 THR THR B . n B 1 128 LEU 128 149 149 LEU LEU B . n B 1 129 TYR 129 150 150 TYR TYR B . n B 1 130 ASN 130 151 151 ASN ASN B . n B 1 131 VAL 131 152 152 VAL VAL B . n B 1 132 HIS 132 153 153 HIS HIS B . n B 1 133 TRP 133 154 154 TRP TRP B . n B 1 134 ASP 134 155 155 ASP ASP B . n B 1 135 PRO 135 156 156 PRO PRO B . n B 1 136 LYS 136 157 157 LYS LYS B . n B 1 137 PRO 137 158 158 PRO PRO B . n B 1 138 ARG 138 159 159 ARG ARG B . n B 1 139 HIS 139 160 160 HIS HIS B . n B 1 140 ILE 140 161 161 ILE ILE B . n B 1 141 GLY 141 162 162 GLY GLY B . n B 1 142 ILE 142 163 163 ILE ILE B . n B 1 143 ASP 143 164 164 ASP ASP B . n B 1 144 VAL 144 165 165 VAL VAL B . n B 1 145 ASN 145 166 166 ASN ASN B . n B 1 146 SER 146 167 167 SER SER B . n B 1 147 ILE 147 168 168 ILE ILE B . n B 1 148 LYS 148 169 169 LYS LYS B . n B 1 149 SER 149 170 170 SER SER B . n B 1 150 ILE 150 171 171 ILE ILE B . n B 1 151 LYS 151 172 172 LYS LYS B . n B 1 152 THR 152 173 173 THR THR B . n B 1 153 THR 153 174 174 THR THR B . n B 1 154 THR 154 175 175 THR THR B . n B 1 155 TRP 155 176 176 TRP TRP B . n B 1 156 ASP 156 177 177 ASP ASP B . n B 1 157 PHE 157 178 178 PHE PHE B . n B 1 158 VAL 158 179 179 VAL VAL B . n B 1 159 LYS 159 180 180 LYS LYS B . n B 1 160 GLY 160 181 181 GLY GLY B . n B 1 161 GLU 161 182 182 GLU GLU B . n B 1 162 ASN 162 183 183 ASN ASN B . n B 1 163 ALA 163 184 184 ALA ALA B . n B 1 164 GLU 164 185 185 GLU GLU B . n B 1 165 VAL 165 186 186 VAL VAL B . n B 1 166 LEU 166 187 187 LEU LEU B . n B 1 167 ILE 167 188 188 ILE ILE B . n B 1 168 THR 168 189 189 THR THR B . n B 1 169 TYR 169 190 190 TYR TYR B . n B 1 170 ASP 170 191 191 ASP ASP B . n B 1 171 SER 171 192 192 SER SER B . n B 1 172 SER 172 193 193 SER SER B . n B 1 173 THR 173 194 194 THR THR B . n B 1 174 LYS 174 195 195 LYS LYS B . n B 1 175 LEU 175 196 196 LEU LEU B . n B 1 176 LEU 176 197 197 LEU LEU B . n B 1 177 VAL 177 198 198 VAL VAL B . n B 1 178 ALA 178 199 199 ALA ALA B . n B 1 179 SER 179 200 200 SER SER B . n B 1 180 LEU 180 201 201 LEU LEU B . n B 1 181 VAL 181 202 202 VAL VAL B . n B 1 182 TYR 182 203 203 TYR TYR B . n B 1 183 PRO 183 204 204 PRO PRO B . n B 1 184 SER 184 205 205 SER SER B . n B 1 185 LEU 185 206 206 LEU LEU B . n B 1 186 LYS 186 207 207 LYS LYS B . n B 1 187 THR 187 208 208 THR THR B . n B 1 188 SER 188 209 209 SER SER B . n B 1 189 PHE 189 210 210 PHE PHE B . n B 1 190 ILE 190 211 211 ILE ILE B . n B 1 191 VAL 191 212 212 VAL VAL B . n B 1 192 SER 192 213 213 SER SER B . n B 1 193 ASP 193 214 214 ASP ASP B . n B 1 194 THR 194 215 215 THR THR B . n B 1 195 VAL 195 216 216 VAL VAL B . n B 1 196 ASP 196 217 217 ASP ASP B . n B 1 197 LEU 197 218 218 LEU LEU B . n B 1 198 LYS 198 219 219 LYS LYS B . n B 1 199 SER 199 220 220 SER SER B . n B 1 200 VAL 200 221 221 VAL VAL B . n B 1 201 LEU 201 222 222 LEU LEU B . n B 1 202 PRO 202 223 223 PRO PRO B . n B 1 203 GLU 203 224 224 GLU GLU B . n B 1 204 TRP 204 225 225 TRP TRP B . n B 1 205 VAL 205 226 226 VAL VAL B . n B 1 206 ILE 206 227 227 ILE ILE B . n B 1 207 VAL 207 228 228 VAL VAL B . n B 1 208 GLY 208 229 229 GLY GLY B . n B 1 209 PHE 209 230 230 PHE PHE B . n B 1 210 THR 210 231 231 THR THR B . n B 1 211 ALA 211 232 232 ALA ALA B . n B 1 212 THR 212 233 233 THR THR B . n B 1 213 THR 213 234 234 THR THR B . n B 1 214 GLY 214 235 235 GLY GLY B . n B 1 215 ILE 215 236 236 ILE ILE B . n B 1 216 THR 216 237 237 THR THR B . n B 1 217 LYS 217 238 238 LYS LYS B . n B 1 218 GLY 218 239 239 GLY GLY B . n B 1 219 ASN 219 240 240 ASN ASN B . n B 1 220 VAL 220 241 241 VAL VAL B . n B 1 221 GLU 221 242 242 GLU GLU B . n B 1 222 THR 222 243 243 THR THR B . n B 1 223 ASN 223 244 244 ASN ASN B . n B 1 224 ASP 224 245 245 ASP ASP B . n B 1 225 ILE 225 246 246 ILE ILE B . n B 1 226 LEU 226 247 247 LEU LEU B . n B 1 227 SER 227 248 248 SER SER B . n B 1 228 TRP 228 249 249 TRP TRP B . n B 1 229 SER 229 250 250 SER SER B . n B 1 230 PHE 230 251 251 PHE PHE B . n B 1 231 ALA 231 252 252 ALA ALA B . n B 1 232 SER 232 253 253 SER SER B . n B 1 233 LYS 233 254 254 LYS LYS B . n B 1 234 LEU 234 255 255 LEU LEU B . n B 1 235 SER 235 256 256 SER SER B . n B 1 236 ASP 236 257 ? ? ? B . n B 1 237 GLY 237 258 ? ? ? B . n B 1 238 THR 238 259 ? ? ? B . n B 1 239 THR 239 260 ? ? ? B . n B 1 240 SER 240 261 ? ? ? B . n B 1 241 GLU 241 262 ? ? ? B . n B 1 242 ALA 242 263 ? ? ? B . n B 1 243 LEU 243 264 264 LEU LEU B . n B 1 244 ASN 244 265 265 ASN ASN B . n B 1 245 LEU 245 266 266 LEU LEU B . n B 1 246 ALA 246 267 267 ALA ALA B . n B 1 247 ASN 247 268 268 ASN ASN B . n B 1 248 PHE 248 269 269 PHE PHE B . n B 1 249 ALA 249 270 270 ALA ALA B . n B 1 250 LEU 250 271 271 LEU LEU B . n B 1 251 ASN 251 272 ? ? ? B . n B 1 252 GLN 252 273 ? ? ? B . n B 1 253 ILE 253 274 ? ? ? B . n B 1 254 LEU 254 275 ? ? ? B . n # loop_ _pdbx_nonpoly_scheme.asym_id _pdbx_nonpoly_scheme.entity_id _pdbx_nonpoly_scheme.mon_id _pdbx_nonpoly_scheme.ndb_seq_num _pdbx_nonpoly_scheme.pdb_seq_num _pdbx_nonpoly_scheme.auth_seq_num _pdbx_nonpoly_scheme.pdb_mon_id _pdbx_nonpoly_scheme.auth_mon_id _pdbx_nonpoly_scheme.pdb_strand_id _pdbx_nonpoly_scheme.pdb_ins_code C 2 NAG 1 1001 1001 NAG NAG A . D 3 MN 1 1002 2001 MN MN A . E 4 CA 1 1003 2002 CA CA A . F 5 MAN 1 1004 3002 MAN MAN A . G 2 NAG 2 1005 3003 NAG NAG A . H 6 GAL 3 1006 3004 GAL GAL A . I 7 EDO 1 1007 1001 EDO EDO A . J 7 EDO 1 1008 1002 EDO EDO A . K 7 EDO 1 1009 1003 EDO EDO A . L 7 EDO 1 1010 1004 EDO EDO A . M 7 EDO 1 1011 1005 EDO EDO A . N 2 NAG 1 1001 1001 NAG NAG B . O 3 MN 1 1002 2001 MN MN B . P 4 CA 1 1003 2002 CA CA B . Q 5 MAN 1 1004 3002 MAN MAN B . R 2 NAG 2 1005 3003 NAG NAG B . S 8 HOH 1 1101 1 HOH HOH A . S 8 HOH 2 1102 2 HOH HOH A . S 8 HOH 3 1103 3 HOH HOH A . S 8 HOH 4 1104 4 HOH HOH A . S 8 HOH 5 1105 5 HOH HOH A . S 8 HOH 6 1106 6 HOH HOH A . S 8 HOH 7 1107 7 HOH HOH A . S 8 HOH 8 1108 8 HOH HOH A . S 8 HOH 9 1109 9 HOH HOH A . S 8 HOH 10 1110 10 HOH HOH A . S 8 HOH 11 1111 11 HOH HOH A . S 8 HOH 12 1112 12 HOH HOH A . S 8 HOH 13 1113 13 HOH HOH A . S 8 HOH 14 1114 14 HOH HOH A . S 8 HOH 15 1115 15 HOH HOH A . S 8 HOH 16 1116 21 HOH HOH A . S 8 HOH 17 1117 22 HOH HOH A . S 8 HOH 18 1118 23 HOH HOH A . S 8 HOH 19 1119 24 HOH HOH A . S 8 HOH 20 1120 25 HOH HOH A . S 8 HOH 21 1121 26 HOH HOH A . S 8 HOH 22 1122 28 HOH HOH A . S 8 HOH 23 1123 29 HOH HOH A . S 8 HOH 24 1124 30 HOH HOH A . S 8 HOH 25 1125 31 HOH HOH A . S 8 HOH 26 1126 32 HOH HOH A . S 8 HOH 27 1127 33 HOH HOH A . S 8 HOH 28 1128 34 HOH HOH A . S 8 HOH 29 1129 35 HOH HOH A . S 8 HOH 30 1130 36 HOH HOH A . S 8 HOH 31 1131 37 HOH HOH A . S 8 HOH 32 1132 38 HOH HOH A . S 8 HOH 33 1133 39 HOH HOH A . S 8 HOH 34 1134 40 HOH HOH A . S 8 HOH 35 1135 41 HOH HOH A . S 8 HOH 36 1136 42 HOH HOH A . S 8 HOH 37 1137 43 HOH HOH A . S 8 HOH 38 1138 44 HOH HOH A . S 8 HOH 39 1139 45 HOH HOH A . S 8 HOH 40 1140 46 HOH HOH A . S 8 HOH 41 1141 47 HOH HOH A . S 8 HOH 42 1142 48 HOH HOH A . S 8 HOH 43 1143 49 HOH HOH A . S 8 HOH 44 1144 50 HOH HOH A . S 8 HOH 45 1145 52 HOH HOH A . S 8 HOH 46 1146 55 HOH HOH A . S 8 HOH 47 1147 56 HOH HOH A . S 8 HOH 48 1148 57 HOH HOH A . S 8 HOH 49 1149 58 HOH HOH A . S 8 HOH 50 1150 59 HOH HOH A . S 8 HOH 51 1151 60 HOH HOH A . S 8 HOH 52 1152 61 HOH HOH A . S 8 HOH 53 1153 62 HOH HOH A . S 8 HOH 54 1154 63 HOH HOH A . S 8 HOH 55 1155 64 HOH HOH A . S 8 HOH 56 1156 65 HOH HOH A . S 8 HOH 57 1157 66 HOH HOH A . S 8 HOH 58 1158 67 HOH HOH A . S 8 HOH 59 1159 68 HOH HOH A . S 8 HOH 60 1160 69 HOH HOH A . S 8 HOH 61 1161 70 HOH HOH A . S 8 HOH 62 1162 71 HOH HOH A . S 8 HOH 63 1163 72 HOH HOH A . S 8 HOH 64 1164 73 HOH HOH A . S 8 HOH 65 1165 74 HOH HOH A . S 8 HOH 66 1166 75 HOH HOH A . S 8 HOH 67 1167 76 HOH HOH A . S 8 HOH 68 1168 77 HOH HOH A . S 8 HOH 69 1169 78 HOH HOH A . S 8 HOH 70 1170 79 HOH HOH A . S 8 HOH 71 1171 80 HOH HOH A . S 8 HOH 72 1172 82 HOH HOH A . S 8 HOH 73 1173 83 HOH HOH A . S 8 HOH 74 1174 84 HOH HOH A . S 8 HOH 75 1175 85 HOH HOH A . S 8 HOH 76 1176 86 HOH HOH A . S 8 HOH 77 1177 87 HOH HOH A . S 8 HOH 78 1178 88 HOH HOH A . S 8 HOH 79 1179 89 HOH HOH A . S 8 HOH 80 1180 90 HOH HOH A . S 8 HOH 81 1181 91 HOH HOH A . S 8 HOH 82 1182 92 HOH HOH A . S 8 HOH 83 1183 93 HOH HOH A . S 8 HOH 84 1184 94 HOH HOH A . S 8 HOH 85 1185 95 HOH HOH A . S 8 HOH 86 1186 101 HOH HOH A . S 8 HOH 87 1187 102 HOH HOH A . S 8 HOH 88 1188 103 HOH HOH A . S 8 HOH 89 1189 104 HOH HOH A . S 8 HOH 90 1190 105 HOH HOH A . S 8 HOH 91 1191 106 HOH HOH A . S 8 HOH 92 1192 107 HOH HOH A . S 8 HOH 93 1193 108 HOH HOH A . S 8 HOH 94 1194 109 HOH HOH A . S 8 HOH 95 1195 110 HOH HOH A . S 8 HOH 96 1196 111 HOH HOH A . S 8 HOH 97 1197 112 HOH HOH A . S 8 HOH 98 1198 113 HOH HOH A . S 8 HOH 99 1199 114 HOH HOH A . S 8 HOH 100 1200 115 HOH HOH A . S 8 HOH 101 1201 117 HOH HOH A . S 8 HOH 102 1202 118 HOH HOH A . S 8 HOH 103 1203 119 HOH HOH A . S 8 HOH 104 1204 123 HOH HOH A . S 8 HOH 105 1205 124 HOH HOH A . S 8 HOH 106 1206 127 HOH HOH A . S 8 HOH 107 1207 128 HOH HOH A . S 8 HOH 108 1208 130 HOH HOH A . S 8 HOH 109 1209 131 HOH HOH A . S 8 HOH 110 1210 133 HOH HOH A . S 8 HOH 111 1211 134 HOH HOH A . S 8 HOH 112 1212 135 HOH HOH A . S 8 HOH 113 1213 137 HOH HOH A . S 8 HOH 114 1214 138 HOH HOH A . S 8 HOH 115 1215 139 HOH HOH A . S 8 HOH 116 1216 140 HOH HOH A . S 8 HOH 117 1217 141 HOH HOH A . S 8 HOH 118 1218 142 HOH HOH A . S 8 HOH 119 1219 143 HOH HOH A . S 8 HOH 120 1220 144 HOH HOH A . S 8 HOH 121 1221 145 HOH HOH A . S 8 HOH 122 1222 146 HOH HOH A . S 8 HOH 123 1223 147 HOH HOH A . S 8 HOH 124 1224 148 HOH HOH A . S 8 HOH 125 1225 149 HOH HOH A . T 8 HOH 1 1101 16 HOH HOH B . T 8 HOH 2 1102 17 HOH HOH B . T 8 HOH 3 1103 18 HOH HOH B . T 8 HOH 4 1104 19 HOH HOH B . T 8 HOH 5 1105 20 HOH HOH B . T 8 HOH 6 1106 27 HOH HOH B . T 8 HOH 7 1107 51 HOH HOH B . T 8 HOH 8 1108 53 HOH HOH B . T 8 HOH 9 1109 54 HOH HOH B . T 8 HOH 10 1110 81 HOH HOH B . T 8 HOH 11 1111 96 HOH HOH B . T 8 HOH 12 1112 97 HOH HOH B . T 8 HOH 13 1113 98 HOH HOH B . T 8 HOH 14 1114 99 HOH HOH B . T 8 HOH 15 1115 100 HOH HOH B . T 8 HOH 16 1116 116 HOH HOH B . T 8 HOH 17 1117 120 HOH HOH B . T 8 HOH 18 1118 121 HOH HOH B . T 8 HOH 19 1119 122 HOH HOH B . T 8 HOH 20 1120 125 HOH HOH B . T 8 HOH 21 1121 126 HOH HOH B . T 8 HOH 22 1122 129 HOH HOH B . T 8 HOH 23 1123 132 HOH HOH B . T 8 HOH 24 1124 136 HOH HOH B . T 8 HOH 25 1125 150 HOH HOH B . # 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 12 A ASN 33 ? ASN 'GLYCOSYLATION SITE' 2 B ASN 12 B ASN 33 ? ASN 'GLYCOSYLATION SITE' # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details author_and_software_defined_assembly _pdbx_struct_assembly.method_details PISA _pdbx_struct_assembly.oligomeric_details tetrameric _pdbx_struct_assembly.oligomeric_count 4 # _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,M,N,O,P,Q,R,S,T # loop_ _pdbx_struct_assembly_prop.biol_id _pdbx_struct_assembly_prop.type _pdbx_struct_assembly_prop.value _pdbx_struct_assembly_prop.details 1 'ABSA (A^2)' 15930 ? 1 MORE -25 ? 1 'SSA (A^2)' 34290 ? # 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' 3_554 -x,y,-z-1/2 -1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 -49.3275000000 # 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 ? B HIS 139 ? B HIS 160 ? 1_555 MN ? O MN . ? B MN 1002 ? 1_555 OD2 ? B ASP 126 ? B ASP 147 ? 1_555 94.2 ? 2 NE2 ? B HIS 139 ? B HIS 160 ? 1_555 MN ? O MN . ? B MN 1002 ? 1_555 OE2 ? B GLU 124 ? B GLU 145 ? 1_555 92.3 ? 3 OD2 ? B ASP 126 ? B ASP 147 ? 1_555 MN ? O MN . ? B MN 1002 ? 1_555 OE2 ? B GLU 124 ? B GLU 145 ? 1_555 102.4 ? 4 NE2 ? B HIS 139 ? B HIS 160 ? 1_555 MN ? O MN . ? B MN 1002 ? 1_555 OD1 ? B ASP 134 ? B ASP 155 ? 1_555 98.2 ? 5 OD2 ? B ASP 126 ? B ASP 147 ? 1_555 MN ? O MN . ? B MN 1002 ? 1_555 OD1 ? B ASP 134 ? B ASP 155 ? 1_555 94.1 ? 6 OE2 ? B GLU 124 ? B GLU 145 ? 1_555 MN ? O MN . ? B MN 1002 ? 1_555 OD1 ? B ASP 134 ? B ASP 155 ? 1_555 159.8 ? 7 NE2 ? B HIS 139 ? B HIS 160 ? 1_555 MN ? O MN . ? B MN 1002 ? 1_555 O ? T HOH . ? B HOH 1102 ? 1_555 91.8 ? 8 OD2 ? B ASP 126 ? B ASP 147 ? 1_555 MN ? O MN . ? B MN 1002 ? 1_555 O ? T HOH . ? B HOH 1102 ? 1_555 172.3 ? 9 OE2 ? B GLU 124 ? B GLU 145 ? 1_555 MN ? O MN . ? B MN 1002 ? 1_555 O ? T HOH . ? B HOH 1102 ? 1_555 82.3 ? 10 OD1 ? B ASP 134 ? B ASP 155 ? 1_555 MN ? O MN . ? B MN 1002 ? 1_555 O ? T HOH . ? B HOH 1102 ? 1_555 80.2 ? 11 NE2 ? B HIS 139 ? B HIS 160 ? 1_555 MN ? O MN . ? B MN 1002 ? 1_555 O ? T HOH . ? B HOH 1101 ? 1_555 171.1 ? 12 OD2 ? B ASP 126 ? B ASP 147 ? 1_555 MN ? O MN . ? B MN 1002 ? 1_555 O ? T HOH . ? B HOH 1101 ? 1_555 91.0 ? 13 OE2 ? B GLU 124 ? B GLU 145 ? 1_555 MN ? O MN . ? B MN 1002 ? 1_555 O ? T HOH . ? B HOH 1101 ? 1_555 79.5 ? 14 OD1 ? B ASP 134 ? B ASP 155 ? 1_555 MN ? O MN . ? B MN 1002 ? 1_555 O ? T HOH . ? B HOH 1101 ? 1_555 88.7 ? 15 O ? T HOH . ? B HOH 1102 ? 1_555 MN ? O MN . ? B MN 1002 ? 1_555 O ? T HOH . ? B HOH 1101 ? 1_555 83.7 ? 16 OD1 ? A ASP 134 ? A ASP 155 ? 1_555 MN ? D MN . ? A MN 1002 ? 1_555 OE2 ? A GLU 124 ? A GLU 145 ? 1_555 170.6 ? 17 OD1 ? A ASP 134 ? A ASP 155 ? 1_555 MN ? D MN . ? A MN 1002 ? 1_555 NE2 ? A HIS 139 ? A HIS 160 ? 1_555 95.8 ? 18 OE2 ? A GLU 124 ? A GLU 145 ? 1_555 MN ? D MN . ? A MN 1002 ? 1_555 NE2 ? A HIS 139 ? A HIS 160 ? 1_555 91.1 ? 19 OD1 ? A ASP 134 ? A ASP 155 ? 1_555 MN ? D MN . ? A MN 1002 ? 1_555 OD2 ? A ASP 126 ? A ASP 147 ? 1_555 89.5 ? 20 OE2 ? A GLU 124 ? A GLU 145 ? 1_555 MN ? D MN . ? A MN 1002 ? 1_555 OD2 ? A ASP 126 ? A ASP 147 ? 1_555 96.5 ? 21 NE2 ? A HIS 139 ? A HIS 160 ? 1_555 MN ? D MN . ? A MN 1002 ? 1_555 OD2 ? A ASP 126 ? A ASP 147 ? 1_555 92.5 ? 22 OD1 ? A ASP 134 ? A ASP 155 ? 1_555 MN ? D MN . ? A MN 1002 ? 1_555 O ? S HOH . ? A HOH 1103 ? 1_555 92.1 ? 23 OE2 ? A GLU 124 ? A GLU 145 ? 1_555 MN ? D MN . ? A MN 1002 ? 1_555 O ? S HOH . ? A HOH 1103 ? 1_555 80.9 ? 24 NE2 ? A HIS 139 ? A HIS 160 ? 1_555 MN ? D MN . ? A MN 1002 ? 1_555 O ? S HOH . ? A HOH 1103 ? 1_555 172.0 ? 25 OD2 ? A ASP 126 ? A ASP 147 ? 1_555 MN ? D MN . ? A MN 1002 ? 1_555 O ? S HOH . ? A HOH 1103 ? 1_555 89.1 ? 26 OD1 ? A ASP 134 ? A ASP 155 ? 1_555 MN ? D MN . ? A MN 1002 ? 1_555 O ? S HOH . ? A HOH 1102 ? 1_555 80.4 ? 27 OE2 ? A GLU 124 ? A GLU 145 ? 1_555 MN ? D MN . ? A MN 1002 ? 1_555 O ? S HOH . ? A HOH 1102 ? 1_555 93.2 ? 28 NE2 ? A HIS 139 ? A HIS 160 ? 1_555 MN ? D MN . ? A MN 1002 ? 1_555 O ? S HOH . ? A HOH 1102 ? 1_555 90.9 ? 29 OD2 ? A ASP 126 ? A ASP 147 ? 1_555 MN ? D MN . ? A MN 1002 ? 1_555 O ? S HOH . ? A HOH 1102 ? 1_555 169.6 ? 30 O ? S HOH . ? A HOH 1103 ? 1_555 MN ? D MN . ? A MN 1002 ? 1_555 O ? S HOH . ? A HOH 1102 ? 1_555 88.9 ? 31 OD2 ? B ASP 134 ? B ASP 155 ? 1_555 CA ? P CA . ? B CA 1003 ? 1_555 O ? B LEU 128 ? B LEU 149 ? 1_555 83.7 ? 32 OD2 ? B ASP 134 ? B ASP 155 ? 1_555 CA ? P CA . ? B CA 1003 ? 1_555 OD1 ? B ASP 126 ? B ASP 147 ? 1_555 112.0 ? 33 O ? B LEU 128 ? B LEU 149 ? 1_555 CA ? P CA . ? B CA 1003 ? 1_555 OD1 ? B ASP 126 ? B ASP 147 ? 1_555 78.3 ? 34 OD2 ? B ASP 134 ? B ASP 155 ? 1_555 CA ? P CA . ? B CA 1003 ? 1_555 OD1 ? B ASN 130 ? B ASN 151 ? 1_555 88.8 ? 35 O ? B LEU 128 ? B LEU 149 ? 1_555 CA ? P CA . ? B CA 1003 ? 1_555 OD1 ? B ASN 130 ? B ASN 151 ? 1_555 89.3 ? 36 OD1 ? B ASP 126 ? B ASP 147 ? 1_555 CA ? P CA . ? B CA 1003 ? 1_555 OD1 ? B ASN 130 ? B ASN 151 ? 1_555 154.0 ? 37 OD2 ? B ASP 134 ? B ASP 155 ? 1_555 CA ? P CA . ? B CA 1003 ? 1_555 OD2 ? B ASP 126 ? B ASP 147 ? 1_555 73.9 ? 38 O ? B LEU 128 ? B LEU 149 ? 1_555 CA ? P CA . ? B CA 1003 ? 1_555 OD2 ? B ASP 126 ? B ASP 147 ? 1_555 113.0 ? 39 OD1 ? B ASP 126 ? B ASP 147 ? 1_555 CA ? P CA . ? B CA 1003 ? 1_555 OD2 ? B ASP 126 ? B ASP 147 ? 1_555 55.7 ? 40 OD1 ? B ASN 130 ? B ASN 151 ? 1_555 CA ? P CA . ? B CA 1003 ? 1_555 OD2 ? B ASP 126 ? B ASP 147 ? 1_555 149.4 ? 41 OD2 ? B ASP 134 ? B ASP 155 ? 1_555 CA ? P CA . ? B CA 1003 ? 1_555 O ? T HOH . ? B HOH 1105 ? 1_555 96.3 ? 42 O ? B LEU 128 ? B LEU 149 ? 1_555 CA ? P CA . ? B CA 1003 ? 1_555 O ? T HOH . ? B HOH 1105 ? 1_555 171.5 ? 43 OD1 ? B ASP 126 ? B ASP 147 ? 1_555 CA ? P CA . ? B CA 1003 ? 1_555 O ? T HOH . ? B HOH 1105 ? 1_555 109.4 ? 44 OD1 ? B ASN 130 ? B ASN 151 ? 1_555 CA ? P CA . ? B CA 1003 ? 1_555 O ? T HOH . ? B HOH 1105 ? 1_555 82.2 ? 45 OD2 ? B ASP 126 ? B ASP 147 ? 1_555 CA ? P CA . ? B CA 1003 ? 1_555 O ? T HOH . ? B HOH 1105 ? 1_555 75.1 ? 46 OD2 ? B ASP 134 ? B ASP 155 ? 1_555 CA ? P CA . ? B CA 1003 ? 1_555 O ? T HOH . ? B HOH 1104 ? 1_555 171.1 ? 47 O ? B LEU 128 ? B LEU 149 ? 1_555 CA ? P CA . ? B CA 1003 ? 1_555 O ? T HOH . ? B HOH 1104 ? 1_555 99.0 ? 48 OD1 ? B ASP 126 ? B ASP 147 ? 1_555 CA ? P CA . ? B CA 1003 ? 1_555 O ? T HOH . ? B HOH 1104 ? 1_555 76.9 ? 49 OD1 ? B ASN 130 ? B ASN 151 ? 1_555 CA ? P CA . ? B CA 1003 ? 1_555 O ? T HOH . ? B HOH 1104 ? 1_555 82.8 ? 50 OD2 ? B ASP 126 ? B ASP 147 ? 1_555 CA ? P CA . ? B CA 1003 ? 1_555 O ? T HOH . ? B HOH 1104 ? 1_555 112.3 ? 51 O ? T HOH . ? B HOH 1105 ? 1_555 CA ? P CA . ? B CA 1003 ? 1_555 O ? T HOH . ? B HOH 1104 ? 1_555 79.7 ? 52 OD2 ? A ASP 134 ? A ASP 155 ? 1_555 CA ? E CA . ? A CA 1003 ? 1_555 OD1 ? A ASN 130 ? A ASN 151 ? 1_555 88.1 ? 53 OD2 ? A ASP 134 ? A ASP 155 ? 1_555 CA ? E CA . ? A CA 1003 ? 1_555 O ? A LEU 128 ? A LEU 149 ? 1_555 83.3 ? 54 OD1 ? A ASN 130 ? A ASN 151 ? 1_555 CA ? E CA . ? A CA 1003 ? 1_555 O ? A LEU 128 ? A LEU 149 ? 1_555 87.3 ? 55 OD2 ? A ASP 134 ? A ASP 155 ? 1_555 CA ? E CA . ? A CA 1003 ? 1_555 OD1 ? A ASP 126 ? A ASP 147 ? 1_555 114.5 ? 56 OD1 ? A ASN 130 ? A ASN 151 ? 1_555 CA ? E CA . ? A CA 1003 ? 1_555 OD1 ? A ASP 126 ? A ASP 147 ? 1_555 151.8 ? 57 O ? A LEU 128 ? A LEU 149 ? 1_555 CA ? E CA . ? A CA 1003 ? 1_555 OD1 ? A ASP 126 ? A ASP 147 ? 1_555 79.4 ? 58 OD2 ? A ASP 134 ? A ASP 155 ? 1_555 CA ? E CA . ? A CA 1003 ? 1_555 OD2 ? A ASP 126 ? A ASP 147 ? 1_555 76.9 ? 59 OD1 ? A ASN 130 ? A ASN 151 ? 1_555 CA ? E CA . ? A CA 1003 ? 1_555 OD2 ? A ASP 126 ? A ASP 147 ? 1_555 151.5 ? 60 O ? A LEU 128 ? A LEU 149 ? 1_555 CA ? E CA . ? A CA 1003 ? 1_555 OD2 ? A ASP 126 ? A ASP 147 ? 1_555 114.4 ? 61 OD1 ? A ASP 126 ? A ASP 147 ? 1_555 CA ? E CA . ? A CA 1003 ? 1_555 OD2 ? A ASP 126 ? A ASP 147 ? 1_555 55.6 ? 62 OD2 ? A ASP 134 ? A ASP 155 ? 1_555 CA ? E CA . ? A CA 1003 ? 1_555 O ? S HOH . ? A HOH 1105 ? 1_555 171.1 ? 63 OD1 ? A ASN 130 ? A ASN 151 ? 1_555 CA ? E CA . ? A CA 1003 ? 1_555 O ? S HOH . ? A HOH 1105 ? 1_555 84.3 ? 64 O ? A LEU 128 ? A LEU 149 ? 1_555 CA ? E CA . ? A CA 1003 ? 1_555 O ? S HOH . ? A HOH 1105 ? 1_555 91.8 ? 65 OD1 ? A ASP 126 ? A ASP 147 ? 1_555 CA ? E CA . ? A CA 1003 ? 1_555 O ? S HOH . ? A HOH 1105 ? 1_555 71.5 ? 66 OD2 ? A ASP 126 ? A ASP 147 ? 1_555 CA ? E CA . ? A CA 1003 ? 1_555 O ? S HOH . ? A HOH 1105 ? 1_555 111.9 ? 67 OD2 ? A ASP 134 ? A ASP 155 ? 1_555 CA ? E CA . ? A CA 1003 ? 1_555 O ? S HOH . ? A HOH 1104 ? 1_555 92.1 ? 68 OD1 ? A ASN 130 ? A ASN 151 ? 1_555 CA ? E CA . ? A CA 1003 ? 1_555 O ? S HOH . ? A HOH 1104 ? 1_555 86.9 ? 69 O ? A LEU 128 ? A LEU 149 ? 1_555 CA ? E CA . ? A CA 1003 ? 1_555 O ? S HOH . ? A HOH 1104 ? 1_555 172.7 ? 70 OD1 ? A ASP 126 ? A ASP 147 ? 1_555 CA ? E CA . ? A CA 1003 ? 1_555 O ? S HOH . ? A HOH 1104 ? 1_555 107.7 ? 71 OD2 ? A ASP 126 ? A ASP 147 ? 1_555 CA ? E CA . ? A CA 1003 ? 1_555 O ? S HOH . ? A HOH 1104 ? 1_555 69.7 ? 72 O ? S HOH . ? A HOH 1105 ? 1_555 CA ? E CA . ? A CA 1003 ? 1_555 O ? S HOH . ? A HOH 1104 ? 1_555 92.0 ? # 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 2014-04-09 2 'Structure model' 1 1 2017-11-22 # _pdbx_audit_revision_details.ordinal 1 _pdbx_audit_revision_details.revision_ordinal 1 _pdbx_audit_revision_details.data_content_type 'Structure model' _pdbx_audit_revision_details.provider repository _pdbx_audit_revision_details.type 'Initial release' _pdbx_audit_revision_details.description ? # _pdbx_audit_revision_group.ordinal 1 _pdbx_audit_revision_group.revision_ordinal 2 _pdbx_audit_revision_group.data_content_type 'Structure model' _pdbx_audit_revision_group.group 'Refinement description' # _pdbx_audit_revision_category.ordinal 1 _pdbx_audit_revision_category.revision_ordinal 2 _pdbx_audit_revision_category.data_content_type 'Structure model' _pdbx_audit_revision_category.category software # _pdbx_audit_revision_item.ordinal 1 _pdbx_audit_revision_item.revision_ordinal 2 _pdbx_audit_revision_item.data_content_type 'Structure model' _pdbx_audit_revision_item.item '_software.name' # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal SERGUI 'data collection' . ? 1 MOLREP phasing . ? 2 REFMAC refinement 5.6.0117 ? 3 HKL-2000 'data reduction' . ? 4 HKL-2000 'data scaling' . ? 5 # 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 ARG A 41 ? ? 59.07 -120.80 2 1 LYS A 121 ? ? -103.11 -149.44 3 1 TRP A 154 ? ? -148.48 -23.67 4 1 ARG B 41 ? ? 51.63 -125.52 5 1 LYS B 121 ? ? -97.13 -146.68 6 1 LYS B 123 ? ? -66.16 -170.04 7 1 LEU B 127 ? ? 56.35 13.69 8 1 TRP B 154 ? ? -150.98 -23.63 9 1 ASN B 166 ? ? 56.11 18.25 # loop_ _pdbx_unobs_or_zero_occ_residues.id _pdbx_unobs_or_zero_occ_residues.PDB_model_num _pdbx_unobs_or_zero_occ_residues.polymer_flag _pdbx_unobs_or_zero_occ_residues.occupancy_flag _pdbx_unobs_or_zero_occ_residues.auth_asym_id _pdbx_unobs_or_zero_occ_residues.auth_comp_id _pdbx_unobs_or_zero_occ_residues.auth_seq_id _pdbx_unobs_or_zero_occ_residues.PDB_ins_code _pdbx_unobs_or_zero_occ_residues.label_asym_id _pdbx_unobs_or_zero_occ_residues.label_comp_id _pdbx_unobs_or_zero_occ_residues.label_seq_id 1 1 Y 1 A THR 260 ? A THR 239 2 1 Y 1 A SER 261 ? A SER 240 3 1 Y 1 A GLU 262 ? A GLU 241 4 1 Y 1 A ALA 263 ? A ALA 242 5 1 Y 1 A LEU 264 ? A LEU 243 6 1 Y 1 A ASN 265 ? A ASN 244 7 1 Y 1 A LEU 266 ? A LEU 245 8 1 Y 1 A ALA 267 ? A ALA 246 9 1 Y 1 A ASN 268 ? A ASN 247 10 1 Y 1 A PHE 269 ? A PHE 248 11 1 Y 1 A ALA 270 ? A ALA 249 12 1 Y 1 A LEU 271 ? A LEU 250 13 1 Y 1 A ASN 272 ? A ASN 251 14 1 Y 1 A GLN 273 ? A GLN 252 15 1 Y 1 A ILE 274 ? A ILE 253 16 1 Y 1 A LEU 275 ? A LEU 254 17 1 Y 1 B ASP 58 ? B ASP 37 18 1 Y 1 B ASN 59 ? B ASN 38 19 1 Y 1 B GLY 60 ? B GLY 39 20 1 Y 1 B ASP 257 ? B ASP 236 21 1 Y 1 B GLY 258 ? B GLY 237 22 1 Y 1 B THR 259 ? B THR 238 23 1 Y 1 B THR 260 ? B THR 239 24 1 Y 1 B SER 261 ? B SER 240 25 1 Y 1 B GLU 262 ? B GLU 241 26 1 Y 1 B ALA 263 ? B ALA 242 27 1 Y 1 B ASN 272 ? B ASN 251 28 1 Y 1 B GLN 273 ? B GLN 252 29 1 Y 1 B ILE 274 ? B ILE 253 30 1 Y 1 B LEU 275 ? B LEU 254 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 2 N-ACETYL-D-GLUCOSAMINE NAG 3 'MANGANESE (II) ION' MN 4 'CALCIUM ION' CA 5 ALPHA-D-MANNOSE MAN 6 BETA-D-GALACTOSE GAL 7 1,2-ETHANEDIOL EDO 8 water HOH #