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*** pedro ***elNémo ID: 2309120951034067182Job options:ID = 2309120951034067182 JOBID = pedro USERID = pedro.murcia PRIVAT = 0 NMODES = 5 DQMIN = -100 DQMAX = 100 DQSTEP = 20 DOGRAPHS = on DOPROJMODS = 0 DORMSD = 0 NRBL = 0 CUTOFF = 0 CAONLY = 0 Input data for this run:HEADER pedro data_1DT3 # _entry.id 1DT3 # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.289 _audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic # loop_ _database_2.database_id _database_2.database_code PDB 1DT3 RCSB RCSB010343 WWPDB D_1000010343 # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 1DT3 _pdbx_database_status.recvd_initial_deposition_date 2000-01-11 _pdbx_database_status.deposit_site RCSB _pdbx_database_status.process_site RCSB _pdbx_database_status.SG_entry . _pdbx_database_status.pdb_format_compatible Y _pdbx_database_status.status_code_mr ? _pdbx_database_status.status_code_sf ? _pdbx_database_status.status_code_cs ? _pdbx_database_status.methods_development_category ? # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Brozozowski, A.M.' 1 'Savage, H.' 2 # _citation.id primary _citation.title 'Structural origins of the interfacial activation in Thermomyces (Humicola) lanuginosa lipase.' _citation.journal_abbrev Biochemistry _citation.journal_volume 39 _citation.page_first 15071 _citation.page_last 15082 _citation.year 2000 _citation.journal_id_ASTM BICHAW _citation.country US _citation.journal_id_ISSN 0006-2960 _citation.journal_id_CSD 0033 _citation.book_publisher ? _citation.pdbx_database_id_PubMed 11106485 _citation.pdbx_database_id_DOI 10.1021/bi0013905 # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Brzozowski, A.M.' 1 primary 'Savage, H.' 2 primary 'Verma, C.S.' 3 primary 'Turkenburg, J.P.' 4 primary 'Lawson, D.M.' 5 primary 'Svendsen, A.' 6 primary 'Patkar, S.' 7 # _cell.entry_id 1DT3 _cell.length_a 139.920 _cell.length_b 139.920 _cell.length_c 80.680 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 120.00 _cell.Z_PDB 12 _cell.pdbx_unique_axis ? # _symmetry.entry_id 1DT3 _symmetry.space_group_name_H-M 'P 61' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 169 # 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 LIPASE 29342.484 2 3.1.1.3 ? ? ? 2 water nat water 18.015 242 ? ? ? ? # _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 ;EVSQDLFNQFNLFAQYSAAAYCGKNNDAPAGTNITCTGNACPEVEKADATFLYSFEDSGVGDVTGFLALDNTNKLIVLSF RGSRSIENWIGNLNFDLKEINDICSGCRGHDGFTSSWRSVADTLRQKVEDAVREHPDYRVVFTGHSLGGALATVAGADLR GNGYDIDVFSYGAPRVGNRAFAEFLTVQTGGTLYRITHTNDIVPRLPPREFGYSHSSPEYWIKSGTLVPVTRNDIVKIEG IDATGGNNQPNIPDIPAHLWYFGLIGTCL ; _entity_poly.pdbx_seq_one_letter_code_can ;EVSQDLFNQFNLFAQYSAAAYCGKNNDAPAGTNITCTGNACPEVEKADATFLYSFEDSGVGDVTGFLALDNTNKLIVLSF RGSRSIENWIGNLNFDLKEINDICSGCRGHDGFTSSWRSVADTLRQKVEDAVREHPDYRVVFTGHSLGGALATVAGADLR GNGYDIDVFSYGAPRVGNRAFAEFLTVQTGGTLYRITHTNDIVPRLPPREFGYSHSSPEYWIKSGTLVPVTRNDIVKIEG IDATGGNNQPNIPDIPAHLWYFGLIGTCL ; _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 GLU n 1 2 VAL n 1 3 SER n 1 4 GLN n 1 5 ASP n 1 6 LEU n 1 7 PHE n 1 8 ASN n 1 9 GLN n 1 10 PHE n 1 11 ASN n 1 12 LEU n 1 13 PHE n 1 14 ALA n 1 15 GLN n 1 16 TYR n 1 17 SER n 1 18 ALA n 1 19 ALA n 1 20 ALA n 1 21 TYR n 1 22 CYS n 1 23 GLY n 1 24 LYS n 1 25 ASN n 1 26 ASN n 1 27 ASP n 1 28 ALA n 1 29 PRO n 1 30 ALA n 1 31 GLY n 1 32 THR n 1 33 ASN n 1 34 ILE n 1 35 THR n 1 36 CYS n 1 37 THR n 1 38 GLY n 1 39 ASN n 1 40 ALA n 1 41 CYS n 1 42 PRO n 1 43 GLU n 1 44 VAL n 1 45 GLU n 1 46 LYS n 1 47 ALA n 1 48 ASP n 1 49 ALA n 1 50 THR n 1 51 PHE n 1 52 LEU n 1 53 TYR n 1 54 SER n 1 55 PHE n 1 56 GLU n 1 57 ASP n 1 58 SER n 1 59 GLY n 1 60 VAL n 1 61 GLY n 1 62 ASP n 1 63 VAL n 1 64 THR n 1 65 GLY n 1 66 PHE n 1 67 LEU n 1 68 ALA n 1 69 LEU n 1 70 ASP n 1 71 ASN n 1 72 THR n 1 73 ASN n 1 74 LYS n 1 75 LEU n 1 76 ILE n 1 77 VAL n 1 78 LEU n 1 79 SER n 1 80 PHE n 1 81 ARG n 1 82 GLY n 1 83 SER n 1 84 ARG n 1 85 SER n 1 86 ILE n 1 87 GLU n 1 88 ASN n 1 89 TRP n 1 90 ILE n 1 91 GLY n 1 92 ASN n 1 93 LEU n 1 94 ASN n 1 95 PHE n 1 96 ASP n 1 97 LEU n 1 98 LYS n 1 99 GLU n 1 100 ILE n 1 101 ASN n 1 102 ASP n 1 103 ILE n 1 104 CYS n 1 105 SER n 1 106 GLY n 1 107 CYS n 1 108 ARG n 1 109 GLY n 1 110 HIS n 1 111 ASP n 1 112 GLY n 1 113 PHE n 1 114 THR n 1 115 SER n 1 116 SER n 1 117 TRP n 1 118 ARG n 1 119 SER n 1 120 VAL n 1 121 ALA n 1 122 ASP n 1 123 THR n 1 124 LEU n 1 125 ARG n 1 126 GLN n 1 127 LYS n 1 128 VAL n 1 129 GLU n 1 130 ASP n 1 131 ALA n 1 132 VAL n 1 133 ARG n 1 134 GLU n 1 135 HIS n 1 136 PRO n 1 137 ASP n 1 138 TYR n 1 139 ARG n 1 140 VAL n 1 141 VAL n 1 142 PHE n 1 143 THR n 1 144 GLY n 1 145 HIS n 1 146 SER n 1 147 LEU n 1 148 GLY n 1 149 GLY n 1 150 ALA n 1 151 LEU n 1 152 ALA n 1 153 THR n 1 154 VAL n 1 155 ALA n 1 156 GLY n 1 157 ALA n 1 158 ASP n 1 159 LEU n 1 160 ARG n 1 161 GLY n 1 162 ASN n 1 163 GLY n 1 164 TYR n 1 165 ASP n 1 166 ILE n 1 167 ASP n 1 168 VAL n 1 169 PHE n 1 170 SER n 1 171 TYR n 1 172 GLY n 1 173 ALA n 1 174 PRO n 1 175 ARG n 1 176 VAL n 1 177 GLY n 1 178 ASN n 1 179 ARG n 1 180 ALA n 1 181 PHE n 1 182 ALA n 1 183 GLU n 1 184 PHE n 1 185 LEU n 1 186 THR n 1 187 VAL n 1 188 GLN n 1 189 THR n 1 190 GLY n 1 191 GLY n 1 192 THR n 1 193 LEU n 1 194 TYR n 1 195 ARG n 1 196 ILE n 1 197 THR n 1 198 HIS n 1 199 THR n 1 200 ASN n 1 201 ASP n 1 202 ILE n 1 203 VAL n 1 204 PRO n 1 205 ARG n 1 206 LEU n 1 207 PRO n 1 208 PRO n 1 209 ARG n 1 210 GLU n 1 211 PHE n 1 212 GLY n 1 213 TYR n 1 214 SER n 1 215 HIS n 1 216 SER n 1 217 SER n 1 218 PRO n 1 219 GLU n 1 220 TYR n 1 221 TRP n 1 222 ILE n 1 223 LYS n 1 224 SER n 1 225 GLY n 1 226 THR n 1 227 LEU n 1 228 VAL n 1 229 PRO n 1 230 VAL n 1 231 THR n 1 232 ARG n 1 233 ASN n 1 234 ASP n 1 235 ILE n 1 236 VAL n 1 237 LYS n 1 238 ILE n 1 239 GLU n 1 240 GLY n 1 241 ILE n 1 242 ASP n 1 243 ALA n 1 244 THR n 1 245 GLY n 1 246 GLY n 1 247 ASN n 1 248 ASN n 1 249 GLN n 1 250 PRO n 1 251 ASN n 1 252 ILE n 1 253 PRO n 1 254 ASP n 1 255 ILE n 1 256 PRO n 1 257 ALA n 1 258 HIS n 1 259 LEU n 1 260 TRP n 1 261 TYR n 1 262 PHE n 1 263 GLY n 1 264 LEU n 1 265 ILE n 1 266 GLY n 1 267 THR n 1 268 CYS n 1 269 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 ? _entity_src_nat.pdbx_organism_scientific 'Thermomyces lanuginosus' _entity_src_nat.pdbx_ncbi_taxonomy_id 5541 _entity_src_nat.genus Thermomyces _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 LIP_THELA _struct_ref.entity_id 1 _struct_ref.pdbx_db_accession O59952 _struct_ref.pdbx_align_begin 23 _struct_ref.pdbx_seq_one_letter_code ;EVSQDLFNQFNLFAQYSAAAYCGKNNDAPAGTNITCTGNACPEVEKADATFLYSFEDSGVGDVTGFLALDNTNKLIVLSF RGSRSIENWIGNLNFDLKEINDICSGCRGHDGFTSSWRSVADTLRQKVEDAVREHPDYRVVFTGHSLGGALATVAGADLR GNGYDIDVFSYGAPRVGNRAFAEFLTVQTGGTLYRITHTNDIVPRLPPREFGYSHSSPEYWIKSGTLVPVTRNDIVKIEG IDATGGNNQPNIPDIPAHLWYFGLIGTCL ; _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 1DT3 A 1 ? 269 ? O59952 23 ? 291 ? 1 269 2 1 1DT3 B 1 ? 269 ? O59952 23 ? 291 ? 1 269 # 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 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.189 PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.130 SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093 THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3' 119.119 TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2' 204.225 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 1DT3 _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 3.88 _exptl_crystal.density_percent_sol 68.33 _exptl_crystal.description ? # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method 'VAPOR DIFFUSION, HANGING DROP' _exptl_crystal_grow.temp 279.0 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH 8.1 _exptl_crystal_grow.pdbx_details 'PEG 5000, magnesium chloride, , pH 8.1, VAPOR DIFFUSION, HANGING DROP, temperature 6K' _exptl_crystal_grow.pdbx_pH_range ? # _diffrn.id 1 _diffrn.ambient_temp 110 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector 'IMAGE PLATE' _diffrn_detector.type MARRESEARCH _diffrn_detector.pdbx_collection_date 1999-03-06 _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 ? _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 1.5418 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source 'ROTATING ANODE' _diffrn_source.type 'RIGAKU RU200' _diffrn_source.pdbx_synchrotron_site ? _diffrn_source.pdbx_synchrotron_beamline ? _diffrn_source.pdbx_wavelength 1.5418 _diffrn_source.pdbx_wavelength_list ? # _reflns.entry_id 1DT3 _reflns.observed_criterion_sigma_I 2.0 _reflns.observed_criterion_sigma_F 2.0 _reflns.d_resolution_low 20 _reflns.d_resolution_high 2.6 _reflns.number_obs 26160 _reflns.number_all 27814 _reflns.percent_possible_obs 94 _reflns.pdbx_Rmerge_I_obs 0.052 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI 26 _reflns.B_iso_Wilson_estimate 55 _reflns.pdbx_redundancy 5 _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_diffrn_id 1 _reflns.pdbx_ordinal 1 # _reflns_shell.d_res_high 2.6 _reflns_shell.d_res_low 20.0 _reflns_shell.percent_possible_all 99.6 _reflns_shell.Rmerge_I_obs 0.048 _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs ? _reflns_shell.pdbx_redundancy 26 _reflns_shell.percent_possible_obs ? _reflns_shell.number_unique_all 26160 _reflns_shell.pdbx_diffrn_id ? _reflns_shell.pdbx_ordinal 1 # _refine.entry_id 1DT3 _refine.ls_number_reflns_obs 26160 _refine.ls_number_reflns_all 27814 _refine.pdbx_ls_sigma_I 0.0 _refine.pdbx_ls_sigma_F 0.0 _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.ls_d_res_low 20.0 _refine.ls_d_res_high 2.6 _refine.ls_percent_reflns_obs 99.4 _refine.ls_R_factor_obs 0.228 _refine.ls_R_factor_all 0.228 _refine.ls_R_factor_R_work 0.228 _refine.ls_R_factor_R_free 0.288 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free ? _refine.ls_number_reflns_R_free 1390 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.B_iso_mean ? _refine.aniso_B[1][1] ? _refine.aniso_B[2][2] ? _refine.aniso_B[3][3] ? _refine.aniso_B[1][2] ? _refine.aniso_B[1][3] ? _refine.aniso_B[2][3] ? _refine.solvent_model_details ? _refine.solvent_model_param_ksol ? _refine.solvent_model_param_bsol ? _refine.pdbx_ls_cross_valid_method ? _refine.details ;rms bond = 0.013A rms angle = 0.041A ; _refine.pdbx_starting_model ? _refine.pdbx_method_to_determine_struct ? _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_stereochemistry_target_values ;rms bond = 0.02A rms angle = 0.06A ; _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details '5% of total data set used' _refine.pdbx_overall_ESU_R_Free ? _refine.overall_SU_B ? _refine.ls_redundancy_reflns_obs ? _refine.B_iso_min ? _refine.B_iso_max ? _refine.overall_SU_ML ? _refine.pdbx_overall_ESU_R ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.correlation_coeff_Fo_to_Fc ? _refine.correlation_coeff_Fo_to_Fc_free ? _refine.overall_SU_R_Cruickshank_DPI ? _refine.overall_SU_R_free ? _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.pdbx_solvent_vdw_probe_radii ? _refine.pdbx_solvent_ion_probe_radii ? _refine.pdbx_solvent_shrinkage_radii ? _refine.pdbx_overall_phase_error ? _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 4142 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 0 _refine_hist.number_atoms_solvent 242 _refine_hist.number_atoms_total 4384 _refine_hist.d_res_high 2.6 _refine_hist.d_res_low 20.0 # loop_ _refine_ls_restr.type _refine_ls_restr.dev_ideal _refine_ls_restr.dev_ideal_target _refine_ls_restr.weight _refine_ls_restr.number _refine_ls_restr.pdbx_refine_id _refine_ls_restr.pdbx_restraint_function x_bond_d 0.02 ? ? ? 'X-RAY DIFFRACTION' ? t_angle_deg 0.06 ? ? ? 'X-RAY DIFFRACTION' ? # _struct.entry_id 1DT3 _struct.title 'THE STRUCTURAL ORIGINS OF INTERFACIAL ACTIVATION IN THERMOMYCES (HUMICOLA) LANUGINOSA LIPASE' _struct.pdbx_descriptor 'LIPASE (E.C.3.1.1.3)' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 1DT3 _struct_keywords.pdbx_keywords HYDROLASE _struct_keywords.text 'lipase, thermomyces linuginosa, interfacial activation, HYDROLASE' # 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 2 ? # loop_ _struct_biol.id _struct_biol.details _struct_biol.pdbx_parent_biol_id 1 'The biological assembly is a monomer' ? 2 ? ? # 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 SER A 3 ? CYS A 22 ? SER A 3 CYS A 22 1 ? 20 HELX_P HELX_P2 2 CYS A 41 ? ALA A 47 ? CYS A 41 ALA A 47 1 ? 7 HELX_P HELX_P3 3 SER A 85 ? ASN A 92 ? SER A 85 ASN A 92 1 ? 8 HELX_P HELX_P4 4 ASP A 111 ? SER A 119 ? ASP A 111 SER A 119 1 ? 9 HELX_P HELX_P5 5 VAL A 120 ? HIS A 135 ? VAL A 120 HIS A 135 1 ? 16 HELX_P HELX_P6 6 SER A 146 ? ARG A 160 ? SER A 146 ARG A 160 1 ? 15 HELX_P HELX_P7 7 ASN A 178 ? GLN A 188 ? ASN A 178 GLN A 188 1 ? 11 HELX_P HELX_P8 8 ILE A 202 ? LEU A 206 ? ILE A 202 LEU A 206 5 ? 5 HELX_P HELX_P9 9 PRO A 208 ? GLY A 212 ? PRO A 208 GLY A 212 5 ? 5 HELX_P HELX_P10 10 THR A 231 ? ASN A 233 ? THR A 231 ASN A 233 5 ? 3 HELX_P HELX_P11 11 ASP A 254 ? LEU A 259 ? ASP A 254 LEU A 259 1 ? 6 HELX_P HELX_P12 12 SER B 3 ? ALA B 20 ? SER B 3 ALA B 20 1 ? 18 HELX_P HELX_P13 13 CYS B 41 ? ALA B 47 ? CYS B 41 ALA B 47 1 ? 7 HELX_P HELX_P14 14 SER B 85 ? ASN B 92 ? SER B 85 ASN B 92 1 ? 8 HELX_P HELX_P15 15 ASN B 101 ? CYS B 104 ? ASN B 101 CYS B 104 5 ? 4 HELX_P HELX_P16 16 ASP B 111 ? HIS B 135 ? ASP B 111 HIS B 135 1 ? 25 HELX_P HELX_P17 17 SER B 146 ? ARG B 160 ? SER B 146 ARG B 160 1 ? 15 HELX_P HELX_P18 18 ASN B 178 ? GLN B 188 ? ASN B 178 GLN B 188 1 ? 11 HELX_P HELX_P19 19 ILE B 202 ? LEU B 206 ? ILE B 202 LEU B 206 5 ? 5 HELX_P HELX_P20 20 PRO B 208 ? GLY B 212 ? PRO B 208 GLY B 212 5 ? 5 HELX_P HELX_P21 21 THR B 231 ? ASN B 233 ? THR B 231 ASN B 233 5 ? 3 HELX_P HELX_P22 22 ILE B 255 ? LEU B 259 ? ILE B 255 LEU B 259 5 ? 5 # _struct_conf_type.id HELX_P _struct_conf_type.criteria ? _struct_conf_type.reference ? # loop_ _struct_conn.id _struct_conn.conn_type_id _struct_conn.pdbx_leaving_atom_flag _struct_conn.pdbx_PDB_id _struct_conn.ptnr1_label_asym_id _struct_conn.ptnr1_label_comp_id _struct_conn.ptnr1_label_seq_id _struct_conn.ptnr1_label_atom_id _struct_conn.pdbx_ptnr1_label_alt_id _struct_conn.pdbx_ptnr1_PDB_ins_code _struct_conn.pdbx_ptnr1_standard_comp_id _struct_conn.ptnr1_symmetry _struct_conn.ptnr2_label_asym_id _struct_conn.ptnr2_label_comp_id _struct_conn.ptnr2_label_seq_id _struct_conn.ptnr2_label_atom_id _struct_conn.pdbx_ptnr2_label_alt_id _struct_conn.pdbx_ptnr2_PDB_ins_code _struct_conn.ptnr1_auth_asym_id _struct_conn.ptnr1_auth_comp_id _struct_conn.ptnr1_auth_seq_id _struct_conn.ptnr2_auth_asym_id _struct_conn.ptnr2_auth_comp_id _struct_conn.ptnr2_auth_seq_id _struct_conn.ptnr2_symmetry _struct_conn.pdbx_ptnr3_label_atom_id _struct_conn.pdbx_ptnr3_label_seq_id _struct_conn.pdbx_ptnr3_label_comp_id _struct_conn.pdbx_ptnr3_label_asym_id _struct_conn.pdbx_ptnr3_label_alt_id _struct_conn.pdbx_ptnr3_PDB_ins_code _struct_conn.details _struct_conn.pdbx_dist_value _struct_conn.pdbx_value_order disulf1 disulf ? ? A CYS 22 SG ? ? ? 1_555 A CYS 268 SG ? ? A CYS 22 A CYS 268 1_555 ? ? ? ? ? ? ? 2.009 ? disulf2 disulf ? ? A CYS 36 SG ? ? ? 1_555 A CYS 41 SG ? ? A CYS 36 A CYS 41 1_555 ? ? ? ? ? ? ? 2.056 ? disulf3 disulf ? ? A CYS 104 SG ? ? ? 1_555 A CYS 107 SG ? ? A CYS 104 A CYS 107 1_555 ? ? ? ? ? ? ? 2.036 ? disulf4 disulf ? ? B CYS 22 SG ? ? ? 1_555 B CYS 268 SG ? ? B CYS 22 B CYS 268 1_555 ? ? ? ? ? ? ? 1.970 ? disulf5 disulf ? ? B CYS 36 SG ? ? ? 1_555 B CYS 41 SG ? ? B CYS 36 B CYS 41 1_555 ? ? ? ? ? ? ? 2.055 ? disulf6 disulf ? ? B CYS 104 SG ? ? ? 1_555 B CYS 107 SG ? ? B CYS 104 B CYS 107 1_555 ? ? ? ? ? ? ? 2.044 ? # _struct_conn_type.id disulf _struct_conn_type.criteria ? _struct_conn_type.reference ? # 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 LEU 206 A . ? LEU 206 A PRO 207 A ? PRO 207 A 1 -8.75 2 SER 217 A . ? SER 217 A PRO 218 A ? PRO 218 A 1 4.21 3 LEU 206 B . ? LEU 206 B PRO 207 B ? PRO 207 B 1 -7.30 4 SER 217 B . ? SER 217 B PRO 218 B ? PRO 218 B 1 -2.31 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details A ? 8 ? B ? 2 ? C ? 8 ? D ? 2 ? # 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 ? parallel A 4 5 ? parallel A 5 6 ? parallel A 6 7 ? parallel A 7 8 ? anti-parallel B 1 2 ? anti-parallel C 1 2 ? anti-parallel C 2 3 ? anti-parallel C 3 4 ? parallel C 4 5 ? parallel C 5 6 ? parallel C 6 7 ? parallel C 7 8 ? anti-parallel D 1 2 ? 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 ALA A 49 ? SER A 58 ? ALA A 49 SER A 58 A 2 VAL A 63 ? ASP A 70 ? VAL A 63 ASP A 70 A 3 LEU A 75 ? PHE A 80 ? LEU A 75 PHE A 80 A 4 ARG A 139 ? HIS A 145 ? ARG A 139 HIS A 145 A 5 ASP A 167 ? TYR A 171 ? ASP A 167 TYR A 171 A 6 LEU A 193 ? HIS A 198 ? LEU A 193 HIS A 198 A 7 GLU A 219 ? ILE A 222 ? GLU A 219 ILE A 222 A 8 ILE A 235 ? ILE A 238 ? ILE A 235 ILE A 238 B 1 LEU A 97 ? GLU A 99 ? LEU A 97 GLU A 99 B 2 ARG A 108 ? HIS A 110 ? ARG A 108 HIS A 110 C 1 ALA B 49 ? SER B 58 ? ALA B 49 SER B 58 C 2 VAL B 63 ? ASP B 70 ? VAL B 63 ASP B 70 C 3 LEU B 75 ? PHE B 80 ? LEU B 75 PHE B 80 C 4 ARG B 139 ? HIS B 145 ? ARG B 139 HIS B 145 C 5 ILE B 166 ? TYR B 171 ? ILE B 166 TYR B 171 C 6 LEU B 193 ? HIS B 198 ? LEU B 193 HIS B 198 C 7 GLU B 219 ? ILE B 222 ? GLU B 219 ILE B 222 C 8 ILE B 235 ? ILE B 238 ? ILE B 235 ILE B 238 D 1 LEU B 97 ? GLU B 99 ? LEU B 97 GLU B 99 D 2 ARG B 108 ? HIS B 110 ? ARG B 108 HIS B 110 # 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 SER A 58 ? N SER A 58 O VAL A 63 ? O VAL A 63 A 2 3 N ASP A 70 ? N ASP A 70 O LEU A 75 ? O LEU A 75 A 3 4 N ILE A 76 ? N ILE A 76 O ARG A 139 ? O ARG A 139 A 4 5 N PHE A 142 ? N PHE A 142 O ASP A 167 ? O ASP A 167 A 5 6 O VAL A 168 ? O VAL A 168 N TYR A 194 ? N TYR A 194 A 6 7 N THR A 197 ? N THR A 197 O TYR A 220 ? O TYR A 220 A 7 8 N TRP A 221 ? N TRP A 221 O VAL A 236 ? O VAL A 236 B 1 2 O LYS A 98 ? O LYS A 98 N GLY A 109 ? N GLY A 109 C 1 2 N SER B 58 ? N SER B 58 O VAL B 63 ? O VAL B 63 C 2 3 N ASP B 70 ? N ASP B 70 O LEU B 75 ? O LEU B 75 C 3 4 N ILE B 76 ? N ILE B 76 O ARG B 139 ? O ARG B 139 C 4 5 N PHE B 142 ? N PHE B 142 O ASP B 167 ? O ASP B 167 C 5 6 O VAL B 168 ? O VAL B 168 N TYR B 194 ? N TYR B 194 C 6 7 O ARG B 195 ? O ARG B 195 N TYR B 220 ? N TYR B 220 C 7 8 O TRP B 221 ? O TRP B 221 N VAL B 236 ? N VAL B 236 D 1 2 O LYS B 98 ? O LYS B 98 N GLY B 109 ? N GLY B 109 # _database_PDB_matrix.entry_id 1DT3 _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 1DT3 _atom_sites.fract_transf_matrix[1][1] 0.007147 _atom_sites.fract_transf_matrix[1][2] 0.004126 _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] 0.008253 _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] 0.012395 _atom_sites.fract_transf_vector[1] 0.00000 _atom_sites.fract_transf_vector[2] 0.00000 _atom_sites.fract_transf_vector[3] 0.00000 # loop_ _atom_type.symbol C N O S # loop_ _atom_site.group_PDB _atom_site.id _atom_site.type_symbol _atom_site.label_atom_id _atom_site.label_alt_id _atom_site.label_comp_id _atom_site.label_asym_id _atom_site.label_entity_id _atom_site.label_seq_id _atom_site.pdbx_PDB_ins_code _atom_site.Cartn_x _atom_site.Cartn_y _atom_site.Cartn_z _atom_site.occupancy _atom_site.B_iso_or_equiv _atom_site.pdbx_formal_charge _atom_site.auth_seq_id _atom_site.auth_comp_id _atom_site.auth_asym_id _atom_site.auth_atom_id _atom_site.pdbx_PDB_model_num ATOM 1 N N . GLU A 1 1 ? 71.730 9.217 54.158 1.00 49.98 ? 1 GLU A N 1 ATOM 2 C CA . GLU A 1 1 ? 71.310 10.231 55.142 1.00 49.84 ? 1 GLU A CA 1 ATOM 3 C C . GLU A 1 1 ? 70.703 9.809 56.467 1.00 47.97 ? 1 GLU A C 1 ATOM 4 O O . GLU A 1 1 ? 70.713 10.725 57.317 1.00 49.31 ? 1 GLU A O 1 ATOM 5 C CB . GLU A 1 1 ? 70.505 11.362 54.526 1.00 54.70 ? 1 GLU A CB 1 ATOM 6 C CG . GLU A 1 1 ? 70.854 11.669 53.097 1.00 64.91 ? 1 GLU A CG 1 ATOM 7 C CD . GLU A 1 1 ? 72.326 11.852 52.782 1.00 69.62 ? 1 GLU A CD 1 ATOM 8 O OE1 . GLU A 1 1 ? 73.093 12.209 53.705 1.00 71.59 ? 1 GLU A OE1 1 ATOM 9 O OE2 . GLU A 1 1 ? 72.662 11.626 51.585 1.00 71.70 ? 1 GLU A OE2 1 ATOM 10 N N . VAL A 1 2 ? 70.267 8.630 56.824 1.00 45.27 ? 2 VAL A N 1 ATOM 11 C CA . VAL A 1 2 ? 70.037 8.340 58.244 1.00 43.07 ? 2 VAL A CA 1 ATOM 12 C C . VAL A 1 2 ? 70.957 7.142 58.579 1.00 42.30 ? 2 VAL A C 1 ATOM 13 O O . VAL A 1 2 ? 71.496 6.548 57.636 1.00 42.75 ? 2 VAL A O 1 ATOM 14 C CB . VAL A 1 2 ? 68.601 8.099 58.682 1.00 39.40 ? 2 VAL A CB 1 ATOM 15 C CG1 . VAL A 1 2 ? 67.713 9.259 58.282 1.00 40.78 ? 2 VAL A CG1 1 ATOM 16 C CG2 . VAL A 1 2 ? 67.951 6.795 58.219 1.00 36.28 ? 2 VAL A CG2 1 ATOM 17 N N . SER A 1 3 ? 70.992 6.662 59.802 1.00 39.75 ? 3 SER A N 1 ATOM 18 C CA . SER A 1 3 ? 71.811 5.533 60.127 1.00 39.24 ? 3 SER A CA 1 ATOM 19 C C . SER A 1 3 ? 71.130 4.202 59.830 1.00 39.51 ? 3 SER A C 1 ATOM 20 O O . SER A 1 3 ? 69.908 3.998 59.969 1.00 39.71 ? 3 SER A O 1 ATOM 21 C CB . SER A 1 3 ? 72.218 5.652 61.601 1.00 38.00 ? 3 SER A CB 1 ATOM 22 O OG . SER A 1 3 ? 71.130 5.216 62.424 1.00 41.99 ? 3 SER A OG 1 ATOM 23 N N . GLN A 1 4 ? 71.951 3.148 59.723 1.00 38.94 ? 4 GLN A N 1 ATOM 24 C CA . GLN A 1 4 ? 71.505 1.790 59.478 1.00 38.61 ? 4 GLN A CA 1 ATOM 25 C C . GLN A 1 4 ? 70.564 1.293 60.563 1.00 38.16 ? 4 GLN A C 1 ATOM 26 O O . GLN A 1 4 ? 69.542 0.618 60.389 1.00 37.18 ? 4 GLN A O 1 ATOM 27 C CB . GLN A 1 4 ? 72.730 0.885 59.308 1.00 38.34 ? 4 GLN A CB 1 ATOM 28 C CG . GLN A 1 4 ? 72.443 -0.529 58.876 1.00 39.64 ? 4 GLN A CG 1 ATOM 29 C CD . GLN A 1 4 ? 71.639 -0.720 57.617 1.00 41.25 ? 4 GLN A CD 1 ATOM 30 O OE1 . GLN A 1 4 ? 71.204 -1.837 57.335 1.00 42.74 ? 4 GLN A OE1 1 ATOM 31 N NE2 . GLN A 1 4 ? 71.422 0.252 56.735 1.00 40.11 ? 4 GLN A NE2 1 ATOM 32 N N . ASP A 1 5 ? 70.880 1.688 61.790 1.00 38.16 ? 5 ASP A N 1 ATOM 33 C CA . ASP A 1 5 ? 70.044 1.307 62.912 1.00 38.98 ? 5 ASP A CA 1 ATOM 34 C C . ASP A 1 5 ? 68.687 2.004 62.860 1.00 38.66 ? 5 ASP A C 1 ATOM 35 O O . ASP A 1 5 ? 67.620 1.386 62.970 1.00 38.26 ? 5 ASP A O 1 ATOM 36 C CB . ASP A 1 5 ? 70.774 1.557 64.213 1.00 42.89 ? 5 ASP A CB 1 ATOM 37 C CG . ASP A 1 5 ? 69.820 1.120 65.304 1.00 48.05 ? 5 ASP A CG 1 ATOM 38 O OD1 . ASP A 1 5 ? 69.623 -0.084 65.529 1.00 51.02 ? 5 ASP A OD1 1 ATOM 39 O OD2 . ASP A 1 5 ? 69.267 2.087 65.830 1.00 53.14 ? 5 ASP A OD2 1 ATOM 40 N N . LEU A 1 6 ? 68.728 3.274 62.448 1.00 37.65 ? 6 LEU A N 1 ATOM 41 C CA . LEU A 1 6 ? 67.399 3.891 62.287 1.00 37.21 ? 6 LEU A CA 1 ATOM 42 C C . LEU A 1 6 ? 66.701 3.276 61.090 1.00 36.39 ? 6 LEU A C 1 ATOM 43 O O . LEU A 1 6 ? 65.514 2.973 61.178 1.00 37.02 ? 6 LEU A O 1 ATOM 44 C CB . LEU A 1 6 ? 67.628 5.373 62.318 1.00 35.38 ? 6 LEU A CB 1 ATOM 45 C CG . LEU A 1 6 ? 66.658 6.264 63.049 1.00 35.84 ? 6 LEU A CG 1 ATOM 46 C CD1 . LEU A 1 6 ? 66.093 5.692 64.320 1.00 33.23 ? 6 LEU A CD1 1 ATOM 47 C CD2 . LEU A 1 6 ? 67.322 7.620 63.277 1.00 37.16 ? 6 LEU A CD2 1 ATOM 48 N N . PHE A 1 7 ? 67.341 3.072 59.962 1.00 35.12 ? 7 PHE A N 1 ATOM 49 C CA . PHE A 1 7 ? 66.736 2.446 58.801 1.00 35.09 ? 7 PHE A CA 1 ATOM 50 C C . PHE A 1 7 ? 66.067 1.134 59.125 1.00 34.48 ? 7 PHE A C 1 ATOM 51 O O . PHE A 1 7 ? 64.943 0.855 58.713 1.00 35.59 ? 7 PHE A O 1 ATOM 52 C CB . PHE A 1 7 ? 67.792 2.247 57.690 1.00 36.63 ? 7 PHE A CB 1 ATOM 53 C CG . PHE A 1 7 ? 67.345 1.388 56.562 1.00 39.60 ? 7 PHE A CG 1 ATOM 54 C CD1 . PHE A 1 7 ? 66.691 1.970 55.491 1.00 42.84 ? 7 PHE A CD1 1 ATOM 55 C CD2 . PHE A 1 7 ? 67.565 0.005 56.535 1.00 40.79 ? 7 PHE A CD2 1 ATOM 56 C CE1 . PHE A 1 7 ? 66.285 1.193 54.390 1.00 42.11 ? 7 PHE A CE1 1 ATOM 57 C CE2 . PHE A 1 7 ? 67.106 -0.771 55.470 1.00 39.02 ? 7 PHE A CE2 1 ATOM 58 C CZ . PHE A 1 7 ? 66.467 -0.174 54.418 1.00 39.95 ? 7 PHE A CZ 1 ATOM 59 N N . ASN A 1 8 ? 66.746 0.187 59.756 1.00 34.47 ? 8 ASN A N 1 ATOM 60 C CA . ASN A 1 8 ? 66.197 -1.069 60.199 1.00 32.74 ? 8 ASN A CA 1 ATOM 61 C C . ASN A 1 8 ? 64.965 -0.842 61.024 1.00 32.42 ? 8 ASN A C 1 ATOM 62 O O . ASN A 1 8 ? 63.973 -1.510 60.738 1.00 33.05 ? 8 ASN A O 1 ATOM 63 C CB . ASN A 1 8 ? 67.191 -1.916 60.970 1.00 35.40 ? 8 ASN A CB 1 ATOM 64 C CG . ASN A 1 8 ? 68.308 -2.451 60.091 1.00 36.24 ? 8 ASN A CG 1 ATOM 65 O OD1 . ASN A 1 8 ? 68.092 -2.633 58.882 1.00 40.15 ? 8 ASN A OD1 1 ATOM 66 N ND2 . ASN A 1 8 ? 69.487 -2.683 60.649 1.00 34.58 ? 8 ASN A ND2 1 ATOM 67 N N . GLN A 1 9 ? 64.956 0.140 61.927 1.00 32.33 ? 9 GLN A N 1 ATOM 68 C CA . GLN A 1 9 ? 63.737 0.358 62.714 1.00 32.26 ? 9 GLN A CA 1 ATOM 69 C C . GLN A 1 9 ? 62.583 0.832 61.845 1.00 31.97 ? 9 GLN A C 1 ATOM 70 O O . GLN A 1 9 ? 61.426 0.399 61.966 1.00 32.22 ? 9 GLN A O 1 ATOM 71 C CB . GLN A 1 9 ? 63.989 1.388 63.806 1.00 33.71 ? 9 GLN A CB 1 ATOM 72 C CG . GLN A 1 9 ? 64.795 0.874 64.964 1.00 37.50 ? 9 GLN A CG 1 ATOM 73 C CD . GLN A 1 9 ? 65.019 1.903 66.064 1.00 38.15 ? 9 GLN A CD 1 ATOM 74 O OE1 . GLN A 1 9 ? 64.086 2.169 66.838 1.00 36.50 ? 9 GLN A OE1 1 ATOM 75 N NE2 . GLN A 1 9 ? 66.274 2.373 66.126 1.00 36.79 ? 9 GLN A NE2 1 ATOM 76 N N . PHE A 1 10 ? 62.896 1.787 60.969 1.00 31.50 ? 10 PHE A N 1 ATOM 77 C CA . PHE A 1 10 ? 61.893 2.368 60.068 1.00 31.30 ? 10 PHE A CA 1 ATOM 78 C C . PHE A 1 10 ? 61.236 1.272 59.233 1.00 31.37 ? 10 PHE A C 1 ATOM 79 O O . PHE A 1 10 ? 60.009 1.241 59.208 1.00 30.34 ? 10 PHE A O 1 ATOM 80 C CB . PHE A 1 10 ? 62.514 3.439 59.206 1.00 30.24 ? 10 PHE A CB 1 ATOM 81 C CG . PHE A 1 10 ? 62.812 4.740 59.926 1.00 31.75 ? 10 PHE A CG 1 ATOM 82 C CD1 . PHE A 1 10 ? 62.489 4.962 61.238 1.00 30.00 ? 10 PHE A CD1 1 ATOM 83 C CD2 . PHE A 1 10 ? 63.392 5.780 59.226 1.00 28.32 ? 10 PHE A CD2 1 ATOM 84 C CE1 . PHE A 1 10 ? 62.827 6.131 61.861 1.00 34.27 ? 10 PHE A CE1 1 ATOM 85 C CE2 . PHE A 1 10 ? 63.678 6.970 59.841 1.00 32.13 ? 10 PHE A CE2 1 ATOM 86 C CZ . PHE A 1 10 ? 63.394 7.183 61.167 1.00 31.95 ? 10 PHE A CZ 1 ATOM 87 N N . ASN A 1 11 ? 62.042 0.290 58.839 1.00 31.08 ? 11 ASN A N 1 ATOM 88 C CA . ASN A 1 11 ? 61.632 -0.825 58.049 1.00 31.74 ? 11 ASN A CA 1 ATOM 89 C C . ASN A 1 11 ? 60.719 -1.841 58.721 1.00 31.51 ? 11 ASN A C 1 ATOM 90 O O . ASN A 1 11 ? 59.628 -2.163 58.218 1.00 31.26 ? 11 ASN A O 1 ATOM 91 C CB . ASN A 1 11 ? 62.920 -1.489 57.524 1.00 35.54 ? 11 ASN A CB 1 ATOM 92 C CG . ASN A 1 11 ? 62.574 -2.481 56.425 1.00 36.22 ? 11 ASN A CG 1 ATOM 93 O OD1 . ASN A 1 11 ? 61.552 -2.346 55.777 1.00 39.20 ? 11 ASN A OD1 1 ATOM 94 N ND2 . ASN A 1 11 ? 63.381 -3.491 56.209 1.00 38.01 ? 11 ASN A ND2 1 ATOM 95 N N . LEU A 1 12 ? 61.177 -2.358 59.847 1.00 30.11 ? 12 LEU A N 1 ATOM 96 C CA . LEU A 1 12 ? 60.347 -3.139 60.738 1.00 29.77 ? 12 LEU A CA 1 ATOM 97 C C . LEU A 1 12 ? 58.980 -2.515 60.971 1.00 30.07 ? 12 LEU A C 1 ATOM 98 O O . LEU A 1 12 ? 57.948 -3.068 60.567 1.00 28.81 ? 12 LEU A O 1 ATOM 99 C CB . LEU A 1 12 ? 61.136 -3.309 62.043 1.00 28.18 ? 12 LEU A CB 1 ATOM 100 C CG . LEU A 1 12 ? 60.610 -4.363 63.009 1.00 30.12 ? 12 LEU A CG 1 ATOM 101 C CD1 . LEU A 1 12 ? 60.790 -5.762 62.426 1.00 31.43 ? 12 LEU A CD1 1 ATOM 102 C CD2 . LEU A 1 12 ? 61.295 -4.367 64.363 1.00 27.85 ? 12 LEU A CD2 1 ATOM 103 N N . PHE A 1 13 ? 58.927 -1.266 61.476 1.00 30.79 ? 13 PHE A N 1 ATOM 104 C CA . PHE A 1 13 ? 57.623 -0.672 61.837 1.00 30.92 ? 13 PHE A CA 1 ATOM 105 C C . PHE A 1 13 ? 56.736 -0.367 60.642 1.00 30.33 ? 13 PHE A C 1 ATOM 106 O O . PHE A 1 13 ? 55.509 -0.523 60.738 1.00 28.41 ? 13 PHE A O 1 ATOM 107 C CB . PHE A 1 13 ? 57.801 0.442 62.876 1.00 32.24 ? 13 PHE A CB 1 ATOM 108 C CG . PHE A 1 13 ? 58.418 -0.068 64.166 1.00 34.02 ? 13 PHE A CG 1 ATOM 109 C CD1 . PHE A 1 13 ? 57.747 -1.050 64.900 1.00 32.34 ? 13 PHE A CD1 1 ATOM 110 C CD2 . PHE A 1 13 ? 59.657 0.394 64.602 1.00 32.37 ? 13 PHE A CD2 1 ATOM 111 C CE1 . PHE A 1 13 ? 58.350 -1.545 66.039 1.00 34.06 ? 13 PHE A CE1 1 ATOM 112 C CE2 . PHE A 1 13 ? 60.248 -0.083 65.733 1.00 30.83 ? 13 PHE A CE2 1 ATOM 113 C CZ . PHE A 1 13 ? 59.573 -1.050 66.466 1.00 33.25 ? 13 PHE A CZ 1 ATOM 114 N N . ALA A 1 14 ? 57.298 -0.152 59.440 1.00 29.91 ? 14 ALA A N 1 ATOM 115 C CA . ALA A 1 14 ? 56.450 -0.081 58.248 1.00 30.28 ? 14 ALA A CA 1 ATOM 116 C C . ALA A 1 14 ? 55.727 -1.426 58.091 1.00 31.85 ? 14 ALA A C 1 ATOM 117 O O . ALA A 1 14 ? 54.587 -1.462 57.646 1.00 30.90 ? 14 ALA A O 1 ATOM 118 C CB . ALA A 1 14 ? 57.257 0.190 57.006 1.00 31.09 ? 14 ALA A CB 1 ATOM 119 N N . GLN A 1 15 ? 56.470 -2.542 58.256 1.00 32.79 ? 15 GLN A N 1 ATOM 120 C CA . GLN A 1 15 ? 55.848 -3.839 58.184 1.00 34.01 ? 15 GLN A CA 1 ATOM 121 C C . GLN A 1 15 ? 54.870 -4.146 59.293 1.00 34.99 ? 15 GLN A C 1 ATOM 122 O O . GLN A 1 15 ? 53.762 -4.582 58.943 1.00 35.11 ? 15 GLN A O 1 ATOM 123 C CB . GLN A 1 15 ? 56.882 -4.949 58.035 1.00 35.96 ? 15 GLN A CB 1 ATOM 124 C CG . GLN A 1 15 ? 57.640 -4.674 56.750 1.00 33.29 ? 15 GLN A CG 1 ATOM 125 C CD . GLN A 1 15 ? 58.643 -5.748 56.438 1.00 33.50 ? 15 GLN A CD 1 ATOM 126 O OE1 . GLN A 1 15 ? 58.717 -6.804 57.027 1.00 34.65 ? 15 GLN A OE1 1 ATOM 127 N NE2 . GLN A 1 15 ? 59.463 -5.420 55.443 1.00 37.01 ? 15 GLN A NE2 1 ATOM 128 N N . TYR A 1 16 ? 55.126 -3.748 60.546 1.00 35.32 ? 16 TYR A N 1 ATOM 129 C CA . TYR A 1 16 ? 54.080 -3.850 61.555 1.00 35.65 ? 16 TYR A CA 1 ATOM 130 C C . TYR A 1 16 ? 52.884 -3.034 61.092 1.00 36.20 ? 16 TYR A C 1 ATOM 131 O O . TYR A 1 16 ? 51.770 -3.475 61.297 1.00 37.08 ? 16 TYR A O 1 ATOM 132 C CB . TYR A 1 16 ? 54.415 -3.394 62.985 1.00 35.71 ? 16 TYR A CB 1 ATOM 133 C CG . TYR A 1 16 ? 55.051 -4.504 63.807 1.00 32.62 ? 16 TYR A CG 1 ATOM 134 C CD1 . TYR A 1 16 ? 54.339 -5.547 64.394 1.00 32.22 ? 16 TYR A CD1 1 ATOM 135 C CD2 . TYR A 1 16 ? 56.423 -4.433 63.953 1.00 30.22 ? 16 TYR A CD2 1 ATOM 136 C CE1 . TYR A 1 16 ? 55.015 -6.559 65.082 1.00 31.50 ? 16 TYR A CE1 1 ATOM 137 C CE2 . TYR A 1 16 ? 57.086 -5.363 64.699 1.00 29.79 ? 16 TYR A CE2 1 ATOM 138 C CZ . TYR A 1 16 ? 56.389 -6.423 65.216 1.00 31.17 ? 16 TYR A CZ 1 ATOM 139 O OH . TYR A 1 16 ? 57.103 -7.356 65.900 1.00 30.39 ? 16 TYR A OH 1 ATOM 140 N N . SER A 1 17 ? 53.050 -1.840 60.579 1.00 37.07 ? 17 SER A N 1 ATOM 141 C CA . SER A 1 17 ? 52.006 -1.053 59.959 1.00 37.53 ? 17 SER A CA 1 ATOM 142 C C . SER A 1 17 ? 51.392 -1.740 58.756 1.00 38.13 ? 17 SER A C 1 ATOM 143 O O . SER A 1 17 ? 50.170 -1.935 58.655 1.00 38.96 ? 17 SER A O 1 ATOM 144 C CB . SER A 1 17 ? 52.564 0.327 59.558 1.00 37.59 ? 17 SER A CB 1 ATOM 145 O OG . SER A 1 17 ? 52.910 1.038 60.753 1.00 38.61 ? 17 SER A OG 1 ATOM 146 N N . ALA A 1 18 ? 52.181 -2.434 57.943 1.00 38.91 ? 18 ALA A N 1 ATOM 147 C CA . ALA A 1 18 ? 51.602 -3.119 56.774 1.00 39.36 ? 18 ALA A CA 1 ATOM 148 C C . ALA A 1 18 ? 50.818 -4.333 57.216 1.00 40.45 ? 18 ALA A C 1 ATOM 149 O O . ALA A 1 18 ? 49.661 -4.510 56.775 1.00 41.65 ? 18 ALA A O 1 ATOM 150 C CB . ALA A 1 18 ? 52.646 -3.408 55.727 1.00 37.65 ? 18 ALA A CB 1 ATOM 151 N N . ALA A 1 19 ? 51.228 -4.989 58.304 1.00 40.68 ? 19 ALA A N 1 ATOM 152 C CA . ALA A 1 19 ? 50.485 -6.106 58.862 1.00 40.68 ? 19 ALA A CA 1 ATOM 153 C C . ALA A 1 19 ? 49.141 -5.697 59.410 1.00 41.41 ? 19 ALA A C 1 ATOM 154 O O . ALA A 1 19 ? 48.215 -6.463 59.263 1.00 40.73 ? 19 ALA A O 1 ATOM 155 C CB . ALA A 1 19 ? 51.254 -6.814 59.957 1.00 39.56 ? 19 ALA A CB 1 ATOM 156 N N . ALA A 1 20 ? 48.881 -4.441 59.780 1.00 43.29 ? 20 ALA A N 1 ATOM 157 C CA . ALA A 1 20 ? 47.542 -4.034 60.217 1.00 44.52 ? 20 ALA A CA 1 ATOM 158 C C . ALA A 1 20 ? 46.506 -4.346 59.132 1.00 45.53 ? 20 ALA A C 1 ATOM 159 O O . ALA A 1 20 ? 45.301 -4.354 59.364 1.00 45.14 ? 20 ALA A O 1 ATOM 160 C CB . ALA A 1 20 ? 47.434 -2.558 60.541 1.00 37.28 ? 20 ALA A CB 1 ATOM 161 N N . TYR A 1 21 ? 46.913 -4.051 57.891 1.00 47.50 ? 21 TYR A N 1 ATOM 162 C CA . TYR A 1 21 ? 46.034 -4.337 56.771 1.00 49.03 ? 21 TYR A CA 1 ATOM 163 C C . TYR A 1 21 ? 46.080 -5.793 56.299 1.00 51.25 ? 21 TYR A C 1 ATOM 164 O O . TYR A 1 21 ? 45.080 -6.252 55.768 1.00 50.65 ? 21 TYR A O 1 ATOM 165 C CB . TYR A 1 21 ? 46.457 -3.523 55.544 1.00 45.16 ? 21 TYR A CB 1 ATOM 166 C CG . TYR A 1 21 ? 46.283 -2.030 55.631 1.00 40.21 ? 21 TYR A CG 1 ATOM 167 C CD1 . TYR A 1 21 ? 45.146 -1.266 55.362 1.00 36.28 ? 21 TYR A CD1 1 ATOM 168 C CD2 . TYR A 1 21 ? 47.452 -1.394 56.101 1.00 38.71 ? 21 TYR A CD2 1 ATOM 169 C CE1 . TYR A 1 21 ? 45.217 0.110 55.487 1.00 36.14 ? 21 TYR A CE1 1 ATOM 170 C CE2 . TYR A 1 21 ? 47.559 -0.016 56.228 1.00 35.86 ? 21 TYR A CE2 1 ATOM 171 C CZ . TYR A 1 21 ? 46.421 0.671 55.965 1.00 35.01 ? 21 TYR A CZ 1 ATOM 172 O OH . TYR A 1 21 ? 46.474 2.014 56.010 1.00 33.68 ? 21 TYR A OH 1 ATOM 173 N N . CYS A 1 22 ? 47.268 -6.421 56.338 1.00 54.64 ? 22 CYS A N 1 ATOM 174 C CA . CYS A 1 22 ? 47.437 -7.602 55.521 1.00 58.75 ? 22 CYS A CA 1 ATOM 175 C C . CYS A 1 22 ? 47.469 -8.988 56.161 1.00 63.51 ? 22 CYS A C 1 ATOM 176 O O . CYS A 1 22 ? 48.126 -9.955 55.742 1.00 63.22 ? 22 CYS A O 1 ATOM 177 C CB . CYS A 1 22 ? 48.457 -7.566 54.383 1.00 50.09 ? 22 CYS A CB 1 ATOM 178 S SG . CYS A 1 22 ? 48.282 -6.192 53.280 1.00 43.87 ? 22 CYS A SG 1 ATOM 179 N N . GLY A 1 23 ? 46.232 -9.107 56.654 1.00 68.53 ? 23 GLY A N 1 ATOM 180 C CA . GLY A 1 23 ? 45.465 -10.263 56.968 1.00 74.61 ? 23 GLY A CA 1 ATOM 181 C C . GLY A 1 23 ? 45.881 -11.081 58.149 1.00 78.80 ? 23 GLY A C 1 ATOM 182 O O . GLY A 1 23 ? 46.841 -10.808 58.849 1.00 78.31 ? 23 GLY A O 1 ATOM 183 N N . LYS A 1 24 ? 44.919 -11.900 58.581 1.00 83.70 ? 24 LYS A N 1 ATOM 184 C CA . LYS A 1 24 ? 44.983 -12.830 59.693 1.00 88.58 ? 24 LYS A CA 1 ATOM 185 C C . LYS A 1 24 ? 44.784 -12.145 61.040 1.00 91.63 ? 24 LYS A C 1 ATOM 186 O O . LYS A 1 24 ? 43.883 -12.474 61.818 1.00 91.83 ? 24 LYS A O 1 ATOM 187 C CB . LYS A 1 24 ? 46.252 -13.683 59.653 1.00 90.53 ? 24 LYS A CB 1 ATOM 188 C CG . LYS A 1 24 ? 46.214 -14.809 58.632 1.00 93.98 ? 24 LYS A CG 1 ATOM 189 C CD . LYS A 1 24 ? 46.363 -14.439 57.171 1.00 94.49 ? 24 LYS A CD 1 ATOM 190 C CE . LYS A 1 24 ? 47.756 -14.724 56.638 1.00 94.77 ? 24 LYS A CE 1 ATOM 191 N NZ . LYS A 1 24 ? 48.242 -16.058 57.096 1.00 96.25 ? 24 LYS A NZ 1 ATOM 192 N N . ASN A 1 25 ? 45.229 -10.900 61.116 1.00 94.64 ? 25 ASN A N 1 ATOM 193 C CA . ASN A 1 25 ? 45.343 -10.032 62.246 1.00 97.87 ? 25 ASN A CA 1 ATOM 194 C C . ASN A 1 25 ? 44.302 -8.931 62.399 1.00 99.64 ? 25 ASN A C 1 ATOM 195 O O . ASN A 1 25 ? 44.479 -8.055 63.261 1.00 99.53 ? 25 ASN A O 1 ATOM 196 C CB . ASN A 1 25 ? 46.704 -9.347 62.266 1.00 100.24 ? 25 ASN A CB 1 ATOM 197 C CG . ASN A 1 25 ? 47.194 -8.551 61.106 1.00 101.21 ? 25 ASN A CG 1 ATOM 198 O OD1 . ASN A 1 25 ? 48.185 -8.921 60.471 1.00 101.96 ? 25 ASN A OD1 1 ATOM 199 N ND2 . ASN A 1 25 ? 46.493 -7.446 60.861 1.00 102.65 ? 25 ASN A ND2 1 ATOM 200 N N . ASN A 1 26 ? 43.223 -9.015 61.607 1.00 101.23 ? 26 ASN A N 1 ATOM 201 C CA . ASN A 1 26 ? 42.143 -8.032 61.806 1.00 102.70 ? 26 ASN A CA 1 ATOM 202 C C . ASN A 1 26 ? 41.373 -8.526 63.041 1.00 103.35 ? 26 ASN A C 1 ATOM 203 O O . ASN A 1 26 ? 41.255 -7.726 63.972 1.00 103.58 ? 26 ASN A O 1 ATOM 204 C CB . ASN A 1 26 ? 41.305 -7.736 60.590 1.00 103.88 ? 26 ASN A CB 1 ATOM 205 C CG . ASN A 1 26 ? 42.021 -7.113 59.405 1.00 104.93 ? 26 ASN A CG 1 ATOM 206 O OD1 . ASN A 1 26 ? 42.543 -5.996 59.438 1.00 103.51 ? 26 ASN A OD1 1 ATOM 207 N ND2 . ASN A 1 26 ? 42.052 -7.806 58.261 1.00 105.60 ? 26 ASN A ND2 1 ATOM 208 N N . ASP A 1 27 ? 41.349 -9.855 63.211 1.00 103.88 ? 27 ASP A N 1 ATOM 209 C CA . ASP A 1 27 ? 40.932 -10.505 64.441 1.00 104.41 ? 27 ASP A CA 1 ATOM 210 C C . ASP A 1 27 ? 41.272 -11.997 64.499 1.00 103.96 ? 27 ASP A C 1 ATOM 211 O O . ASP A 1 27 ? 40.448 -12.842 64.153 1.00 104.02 ? 27 ASP A O 1 ATOM 212 C CB . ASP A 1 27 ? 39.440 -10.303 64.705 1.00 107.34 ? 27 ASP A CB 1 ATOM 213 C CG . ASP A 1 27 ? 39.090 -9.637 66.026 1.00 109.11 ? 27 ASP A CG 1 ATOM 214 O OD1 . ASP A 1 27 ? 39.094 -8.383 66.124 1.00 109.47 ? 27 ASP A OD1 1 ATOM 215 O OD2 . ASP A 1 27 ? 38.744 -10.369 66.981 1.00 110.38 ? 27 ASP A OD2 1 ATOM 216 N N . ALA A 1 28 ? 42.393 -12.342 65.134 1.00 103.36 ? 28 ALA A N 1 ATOM 217 C CA . ALA A 1 28 ? 42.842 -13.723 65.306 1.00 101.83 ? 28 ALA A CA 1 ATOM 218 C C . ALA A 1 28 ? 43.324 -13.967 66.727 1.00 100.49 ? 28 ALA A C 1 ATOM 219 O O . ALA A 1 28 ? 43.809 -13.059 67.399 1.00 100.77 ? 28 ALA A O 1 ATOM 220 C CB . ALA A 1 28 ? 43.909 -14.085 64.293 1.00 102.60 ? 28 ALA A CB 1 ATOM 221 N N . PRO A 1 29 ? 43.226 -15.208 67.174 1.00 99.12 ? 29 PRO A N 1 ATOM 222 C CA . PRO A 1 29 ? 43.463 -15.584 68.555 1.00 97.37 ? 29 PRO A CA 1 ATOM 223 C C . PRO A 1 29 ? 44.777 -15.138 69.158 1.00 95.25 ? 29 PRO A C 1 ATOM 224 O O . PRO A 1 29 ? 45.837 -15.215 68.543 1.00 95.07 ? 29 PRO A O 1 ATOM 225 C CB . PRO A 1 29 ? 43.322 -17.104 68.573 1.00 97.93 ? 29 PRO A CB 1 ATOM 226 C CG . PRO A 1 29 ? 43.380 -17.545 67.158 1.00 98.54 ? 29 PRO A CG 1 ATOM 227 C CD . PRO A 1 29 ? 42.914 -16.384 66.322 1.00 99.04 ? 29 PRO A CD 1 ATOM 228 N N . ALA A 1 30 ? 44.782 -14.814 70.451 1.00 92.58 ? 30 ALA A N 1 ATOM 229 C CA . ALA A 1 30 ? 45.971 -14.351 71.151 1.00 89.09 ? 30 ALA A CA 1 ATOM 230 C C . ALA A 1 30 ? 47.080 -15.388 71.236 1.00 86.67 ? 30 ALA A C 1 ATOM 231 O O . ALA A 1 30 ? 46.817 -16.555 71.511 1.00 86.44 ? 30 ALA A O 1 ATOM 232 C CB . ALA A 1 30 ? 45.543 -13.914 72.544 1.00 87.42 ? 30 ALA A CB 1 ATOM 233 N N . GLY A 1 31 ? 48.328 -14.995 70.981 1.00 83.85 ? 31 GLY A N 1 ATOM 234 C CA . GLY A 1 31 ? 49.460 -15.900 71.098 1.00 80.40 ? 31 GLY A CA 1 ATOM 235 C C . GLY A 1 31 ? 49.871 -16.556 69.789 1.00 77.65 ? 31 GLY A C 1 ATOM 236 O O . GLY A 1 31 ? 50.889 -17.207 69.593 1.00 77.22 ? 31 GLY A O 1 ATOM 237 N N . THR A 1 32 ? 49.026 -16.363 68.809 1.00 75.30 ? 32 THR A N 1 ATOM 238 C CA . THR A 1 32 ? 49.132 -16.808 67.436 1.00 72.76 ? 32 THR A CA 1 ATOM 239 C C . THR A 1 32 ? 50.251 -16.076 66.712 1.00 70.52 ? 32 THR A C 1 ATOM 240 O O . THR A 1 32 ? 50.682 -15.020 67.175 1.00 70.40 ? 32 THR A O 1 ATOM 241 C CB . THR A 1 32 ? 47.780 -16.438 66.791 1.00 73.23 ? 32 THR A CB 1 ATOM 242 O OG1 . THR A 1 32 ? 46.753 -17.232 67.411 1.00 73.97 ? 32 THR A OG1 1 ATOM 243 C CG2 . THR A 1 32 ? 47.821 -16.604 65.300 1.00 72.67 ? 32 THR A CG2 1 ATOM 244 N N . ASN A 1 33 ? 50.944 -16.747 65.815 1.00 68.07 ? 33 ASN A N 1 ATOM 245 C CA . ASN A 1 33 ? 52.077 -16.132 65.110 1.00 64.54 ? 33 ASN A CA 1 ATOM 246 C C . ASN A 1 33 ? 51.523 -15.060 64.189 1.00 61.50 ? 33 ASN A C 1 ATOM 247 O O . ASN A 1 33 ? 50.371 -15.151 63.768 1.00 60.81 ? 33 ASN A O 1 ATOM 248 C CB . ASN A 1 33 ? 52.844 -17.264 64.430 1.00 67.60 ? 33 ASN A CB 1 ATOM 249 C CG . ASN A 1 33 ? 53.783 -17.997 65.369 1.00 70.77 ? 33 ASN A CG 1 ATOM 250 O OD1 . ASN A 1 33 ? 54.450 -19.026 65.133 1.00 72.39 ? 33 ASN A OD1 1 ATOM 251 N ND2 . ASN A 1 33 ? 53.866 -17.381 66.543 1.00 72.01 ? 33 ASN A ND2 1 ATOM 252 N N . ILE A 1 34 ? 52.098 -13.857 64.173 1.00 58.72 ? 34 ILE A N 1 ATOM 253 C CA . ILE A 1 34 ? 51.636 -12.779 63.288 1.00 56.09 ? 34 ILE A CA 1 ATOM 254 C C . ILE A 1 34 ? 52.141 -13.019 61.857 1.00 53.67 ? 34 ILE A C 1 ATOM 255 O O . ILE A 1 34 ? 53.325 -13.300 61.713 1.00 51.14 ? 34 ILE A O 1 ATOM 256 C CB . ILE A 1 34 ? 52.092 -11.378 63.753 1.00 56.77 ? 34 ILE A CB 1 ATOM 257 C CG1 . ILE A 1 34 ? 51.346 -10.891 65.003 1.00 54.43 ? 34 ILE A CG1 1 ATOM 258 C CG2 . ILE A 1 34 ? 52.001 -10.347 62.632 1.00 52.63 ? 34 ILE A CG2 1 ATOM 259 C CD1 . ILE A 1 34 ? 51.848 -9.524 65.473 1.00 52.33 ? 34 ILE A CD1 1 ATOM 260 N N . THR A 1 35 ? 51.237 -13.086 60.868 1.00 52.77 ? 35 THR A N 1 ATOM 261 C CA . THR A 1 35 ? 51.643 -13.372 59.498 1.00 52.49 ? 35 THR A CA 1 ATOM 262 C C . THR A 1 35 ? 50.876 -12.537 58.471 1.00 51.59 ? 35 THR A C 1 ATOM 263 O O . THR A 1 35 ? 49.668 -12.393 58.629 1.00 52.69 ? 35 THR A O 1 ATOM 264 C CB . THR A 1 35 ? 51.448 -14.799 58.943 1.00 53.10 ? 35 THR A CB 1 ATOM 265 O OG1 . THR A 1 35 ? 50.048 -15.134 58.943 1.00 56.05 ? 35 THR A OG1 1 ATOM 266 C CG2 . THR A 1 35 ? 52.282 -15.834 59.649 1.00 52.24 ? 35 THR A CG2 1 ATOM 267 N N . CYS A 1 36 ? 51.495 -12.228 57.341 1.00 50.05 ? 36 CYS A N 1 ATOM 268 C CA . CYS A 1 36 ? 50.754 -11.488 56.321 1.00 49.17 ? 36 CYS A CA 1 ATOM 269 C C . CYS A 1 36 ? 50.569 -12.204 55.001 1.00 48.90 ? 36 CYS A C 1 ATOM 270 O O . CYS A 1 36 ? 51.324 -13.098 54.572 1.00 48.69 ? 36 CYS A O 1 ATOM 271 C CB . CYS A 1 36 ? 51.539 -10.178 56.031 1.00 44.85 ? 36 CYS A CB 1 ATOM 272 S SG . CYS A 1 36 ? 51.764 -9.133 57.479 1.00 45.88 ? 36 CYS A SG 1 ATOM 273 N N . THR A 1 37 ? 49.660 -11.666 54.175 1.00 48.59 ? 37 THR A N 1 ATOM 274 C CA . THR A 1 37 ? 49.641 -12.270 52.825 1.00 48.19 ? 37 THR A CA 1 ATOM 275 C C . THR A 1 37 ? 50.561 -11.460 51.936 1.00 47.61 ? 37 THR A C 1 ATOM 276 O O . THR A 1 37 ? 51.114 -10.428 52.332 1.00 47.12 ? 37 THR A O 1 ATOM 277 C CB . THR A 1 37 ? 48.216 -12.252 52.266 1.00 50.44 ? 37 THR A CB 1 ATOM 278 O OG1 . THR A 1 37 ? 47.642 -10.997 52.677 1.00 52.56 ? 37 THR A OG1 1 ATOM 279 C CG2 . THR A 1 37 ? 47.460 -13.402 52.899 1.00 47.64 ? 37 THR A CG2 1 ATOM 280 N N . GLY A 1 38 ? 50.956 -12.057 50.811 1.00 46.74 ? 38 GLY A N 1 ATOM 281 C CA . GLY A 1 38 ? 51.659 -11.392 49.755 1.00 45.18 ? 38 GLY A CA 1 ATOM 282 C C . GLY A 1 38 ? 52.918 -10.662 50.109 1.00 45.03 ? 38 GLY A C 1 ATOM 283 O O . GLY A 1 38 ? 53.204 -9.591 49.568 1.00 45.39 ? 38 GLY A O 1 ATOM 284 N N . ASN A 1 39 ? 53.667 -11.129 51.089 1.00 44.54 ? 39 ASN A N 1 ATOM 285 C CA . ASN A 1 39 ? 54.950 -10.602 51.476 1.00 43.87 ? 39 ASN A CA 1 ATOM 286 C C . ASN A 1 39 ? 54.979 -9.196 52.045 1.00 43.57 ? 39 ASN A C 1 ATOM 287 O O . ASN A 1 39 ? 56.079 -8.620 52.154 1.00 43.08 ? 39 ASN A O 1 ATOM 288 C CB . ASN A 1 39 ? 55.931 -10.829 50.316 1.00 44.37 ? 39 ASN A CB 1 ATOM 289 C CG . ASN A 1 39 ? 57.329 -11.074 50.842 1.00 47.78 ? 39 ASN A CG 1 ATOM 290 O OD1 . ASN A 1 39 ? 57.577 -11.775 51.833 1.00 51.93 ? 39 ASN A OD1 1 ATOM 291 N ND2 . ASN A 1 39 ? 58.338 -10.466 50.254 1.00 48.04 ? 39 ASN A ND2 1 ATOM 292 N N . ALA A 1 40 ? 53.897 -8.708 52.658 1.00 42.78 ? 40 ALA A N 1 ATOM 293 C CA . ALA A 1 40 ? 53.867 -7.440 53.353 1.00 42.79 ? 40 ALA A CA 1 ATOM 294 C C . ALA A 1 40 ? 54.743 -7.288 54.598 1.00 42.76 ? 40 ALA A C 1 ATOM 295 O O . ALA A 1 40 ? 55.317 -6.201 54.761 1.00 42.34 ? 40 ALA A O 1 ATOM 296 C CB . ALA A 1 40 ? 52.491 -6.969 53.826 1.00 40.92 ? 40 ALA A CB 1 ATOM 297 N N . CYS A 1 41 ? 54.898 -8.364 55.379 1.00 42.93 ? 41 CYS A N 1 ATOM 298 C CA . CYS A 1 41 ? 55.666 -8.252 56.600 1.00 42.56 ? 41 CYS A CA 1 ATOM 299 C C . CYS A 1 41 ? 56.660 -9.331 56.890 1.00 42.37 ? 41 CYS A C 1 ATOM 300 O O . CYS A 1 41 ? 56.565 -9.872 57.985 1.00 43.31 ? 41 CYS A O 1 ATOM 301 C CB . CYS A 1 41 ? 54.621 -8.135 57.709 1.00 43.77 ? 41 CYS A CB 1 ATOM 302 S SG . CYS A 1 41 ? 53.664 -9.580 58.125 1.00 42.61 ? 41 CYS A SG 1 ATOM 303 N N . PRO A 1 42 ? 57.646 -9.611 56.059 1.00 42.10 ? 42 PRO A N 1 ATOM 304 C CA . PRO A 1 42 ? 58.613 -10.640 56.261 1.00 41.79 ? 42 PRO A CA 1 ATOM 305 C C . PRO A 1 42 ? 59.542 -10.372 57.439 1.00 43.26 ? 42 PRO A C 1 ATOM 306 O O . PRO A 1 42 ? 60.004 -11.397 58.031 1.00 43.29 ? 42 PRO A O 1 ATOM 307 C CB . PRO A 1 42 ? 59.460 -10.769 55.002 1.00 41.85 ? 42 PRO A CB 1 ATOM 308 C CG . PRO A 1 42 ? 59.020 -9.699 54.058 1.00 41.62 ? 42 PRO A CG 1 ATOM 309 C CD . PRO A 1 42 ? 57.847 -8.985 54.710 1.00 42.12 ? 42 PRO A CD 1 ATOM 310 N N . GLU A 1 43 ? 59.815 -9.086 57.795 1.00 42.33 ? 43 GLU A N 1 ATOM 311 C CA . GLU A 1 43 ? 60.610 -8.963 59.036 1.00 42.71 ? 43 GLU A CA 1 ATOM 312 C C . GLU A 1 43 ? 59.785 -9.284 60.280 1.00 42.20 ? 43 GLU A C 1 ATOM 313 O O . GLU A 1 43 ? 60.379 -9.642 61.289 1.00 41.82 ? 43 GLU A O 1 ATOM 314 C CB . GLU A 1 43 ? 61.385 -7.682 59.204 1.00 42.46 ? 43 GLU A CB 1 ATOM 315 C CG . GLU A 1 43 ? 62.039 -7.211 57.929 1.00 47.03 ? 43 GLU A CG 1 ATOM 316 C CD . GLU A 1 43 ? 63.359 -7.877 57.605 1.00 49.67 ? 43 GLU A CD 1 ATOM 317 O OE1 . GLU A 1 43 ? 64.011 -8.392 58.544 1.00 47.76 ? 43 GLU A OE1 1 ATOM 318 O OE2 . GLU A 1 43 ? 63.719 -7.866 56.379 1.00 51.78 ? 43 GLU A OE2 1 ATOM 319 N N . VAL A 1 44 ? 58.467 -9.226 60.228 1.00 42.07 ? 44 VAL A N 1 ATOM 320 C CA . VAL A 1 44 ? 57.608 -9.561 61.345 1.00 43.07 ? 44 VAL A CA 1 ATOM 321 C C . VAL A 1 44 ? 57.479 -11.065 61.532 1.00 44.38 ? 44 VAL A C 1 ATOM 322 O O . VAL A 1 44 ? 57.974 -11.588 62.544 1.00 43.76 ? 44 VAL A O 1 ATOM 323 C CB . VAL A 1 44 ? 56.236 -8.921 61.140 1.00 41.83 ? 44 VAL A CB 1 ATOM 324 C CG1 . VAL A 1 44 ? 55.273 -9.312 62.234 1.00 40.68 ? 44 VAL A CG1 1 ATOM 325 C CG2 . VAL A 1 44 ? 56.449 -7.417 61.037 1.00 40.32 ? 44 VAL A CG2 1 ATOM 326 N N . GLU A 1 45 ? 57.358 -11.755 60.392 1.00 46.03 ? 45 GLU A N 1 ATOM 327 C CA . GLU A 1 45 ? 57.368 -13.220 60.424 1.00 47.86 ? 45 GLU A CA 1 ATOM 328 C C . GLU A 1 45 ? 58.711 -13.790 60.842 1.00 48.44 ? 45 GLU A C 1 ATOM 329 O O . GLU A 1 45 ? 58.768 -14.755 61.590 1.00 47.99 ? 45 GLU A O 1 ATOM 330 C CB . GLU A 1 45 ? 56.890 -13.787 59.100 1.00 46.45 ? 45 GLU A CB 1 ATOM 331 C CG . GLU A 1 45 ? 55.433 -13.480 58.829 1.00 49.87 ? 45 GLU A CG 1 ATOM 332 C CD . GLU A 1 45 ? 54.981 -13.879 57.440 1.00 52.46 ? 45 GLU A CD 1 ATOM 333 O OE1 . GLU A 1 45 ? 55.756 -14.496 56.684 1.00 52.86 ? 45 GLU A OE1 1 ATOM 334 O OE2 . GLU A 1 45 ? 53.827 -13.571 57.083 1.00 54.29 ? 45 GLU A OE2 1 ATOM 335 N N . LYS A 1 46 ? 59.825 -13.130 60.563 1.00 50.21 ? 46 LYS A N 1 ATOM 336 C CA . LYS A 1 46 ? 61.168 -13.613 60.913 1.00 51.19 ? 46 LYS A CA 1 ATOM 337 C C . LYS A 1 46 ? 61.264 -13.721 62.438 1.00 52.80 ? 46 LYS A C 1 ATOM 338 O O . LYS A 1 46 ? 61.704 -14.740 62.957 1.00 52.82 ? 46 LYS A O 1 ATOM 339 C CB . LYS A 1 46 ? 62.202 -12.669 60.361 1.00 51.36 ? 46 LYS A CB 1 ATOM 340 C CG . LYS A 1 46 ? 63.400 -13.080 59.573 1.00 54.27 ? 46 LYS A CG 1 ATOM 341 C CD . LYS A 1 46 ? 63.420 -12.451 58.180 1.00 60.10 ? 46 LYS A CD 1 ATOM 342 C CE . LYS A 1 46 ? 64.456 -11.386 57.917 1.00 63.57 ? 46 LYS A CE 1 ATOM 343 N NZ . LYS A 1 46 ? 64.179 -10.527 56.708 1.00 64.04 ? 46 LYS A NZ 1 ATOM 344 N N . ALA A 1 47 ? 60.685 -12.785 63.170 1.00 53.76 ? 47 ALA A N 1 ATOM 345 C CA . ALA A 1 47 ? 60.619 -12.748 64.602 1.00 54.73 ? 47 ALA A CA 1 ATOM 346 C C . ALA A 1 47 ? 59.638 -13.719 65.265 1.00 55.82 ? 47 ALA A C 1 ATOM 347 O O . ALA A 1 47 ? 58.546 -14.097 64.837 1.00 54.96 ? 47 ALA A O 1 ATOM 348 C CB . ALA A 1 47 ? 60.278 -11.317 65.014 1.00 54.09 ? 47 ALA A CB 1 ATOM 349 N N . ASP A 1 48 ? 59.797 -13.785 66.604 1.00 56.45 ? 48 ASP A N 1 ATOM 350 C CA . ASP A 1 48 ? 58.880 -14.553 67.452 1.00 57.38 ? 48 ASP A CA 1 ATOM 351 C C . ASP A 1 48 ? 57.821 -13.503 67.807 1.00 56.86 ? 48 ASP A C 1 ATOM 352 O O . ASP A 1 48 ? 58.016 -12.901 68.887 1.00 56.90 ? 48 ASP A O 1 ATOM 353 C CB . ASP A 1 48 ? 59.594 -15.074 68.707 1.00 59.92 ? 48 ASP A CB 1 ATOM 354 C CG . ASP A 1 48 ? 58.666 -15.743 69.715 1.00 62.06 ? 48 ASP A CG 1 ATOM 355 O OD1 . ASP A 1 48 ? 57.466 -15.908 69.393 1.00 61.14 ? 48 ASP A OD1 1 ATOM 356 O OD2 . ASP A 1 48 ? 59.096 -16.110 70.845 1.00 62.81 ? 48 ASP A OD2 1 ATOM 357 N N . ALA A 1 49 ? 56.967 -13.180 66.835 1.00 55.69 ? 49 ALA A N 1 ATOM 358 C CA . ALA A 1 49 ? 56.013 -12.092 67.132 1.00 55.22 ? 49 ALA A CA 1 ATOM 359 C C . ALA A 1 49 ? 54.582 -12.581 67.112 1.00 54.78 ? 49 ALA A C 1 ATOM 360 O O . ALA A 1 49 ? 54.163 -13.236 66.119 1.00 56.13 ? 49 ALA A O 1 ATOM 361 C CB . ALA A 1 49 ? 56.241 -10.939 66.168 1.00 52.80 ? 49 ALA A CB 1 ATOM 362 N N . THR A 1 50 ? 53.875 -12.397 68.208 1.00 53.77 ? 50 THR A N 1 ATOM 363 C CA . THR A 1 50 ? 52.513 -12.928 68.299 1.00 53.17 ? 50 THR A CA 1 ATOM 364 C C . THR A 1 50 ? 51.549 -11.843 68.782 1.00 53.30 ? 50 THR A C 1 ATOM 365 O O . THR A 1 50 ? 51.989 -10.790 69.245 1.00 51.95 ? 50 THR A O 1 ATOM 366 C CB . THR A 1 50 ? 52.490 -14.085 69.323 1.00 50.23 ? 50 THR A CB 1 ATOM 367 O OG1 . THR A 1 50 ? 52.967 -13.526 70.542 1.00 49.30 ? 50 THR A OG1 1 ATOM 368 C CG2 . THR A 1 50 ? 53.372 -15.265 68.962 1.00 45.07 ? 50 THR A CG2 1 ATOM 369 N N . PHE A 1 51 ? 50.254 -12.121 68.646 1.00 53.46 ? 51 PHE A N 1 ATOM 370 C CA . PHE A 1 51 ? 49.201 -11.233 69.050 1.00 54.00 ? 51 PHE A CA 1 ATOM 371 C C . PHE A 1 51 ? 48.925 -11.322 70.562 1.00 55.55 ? 51 PHE A C 1 ATOM 372 O O . PHE A 1 51 ? 48.475 -12.389 71.006 1.00 56.17 ? 51 PHE A O 1 ATOM 373 C CB . PHE A 1 51 ? 47.815 -11.660 68.500 1.00 53.40 ? 51 PHE A CB 1 ATOM 374 C CG . PHE A 1 51 ? 47.824 -11.526 67.017 1.00 52.56 ? 51 PHE A CG 1 ATOM 375 C CD1 . PHE A 1 51 ? 47.768 -10.267 66.442 1.00 52.03 ? 51 PHE A CD1 1 ATOM 376 C CD2 . PHE A 1 51 ? 48.025 -12.655 66.231 1.00 52.79 ? 51 PHE A CD2 1 ATOM 377 C CE1 . PHE A 1 51 ? 47.884 -10.120 65.080 1.00 52.39 ? 51 PHE A CE1 1 ATOM 378 C CE2 . PHE A 1 51 ? 48.072 -12.513 64.850 1.00 51.98 ? 51 PHE A CE2 1 ATOM 379 C CZ . PHE A 1 51 ? 48.036 -11.252 64.301 1.00 51.44 ? 51 PHE A CZ 1 ATOM 380 N N . LEU A 1 52 ? 48.573 -10.152 71.070 1.00 55.61 ? 52 LEU A N 1 ATOM 381 C CA . LEU A 1 52 ? 48.170 -10.001 72.441 1.00 55.98 ? 52 LEU A CA 1 ATOM 382 C C . LEU A 1 52 ? 46.682 -9.699 72.454 1.00 56.75 ? 52 LEU A C 1 ATOM 383 O O . LEU A 1 52 ? 45.953 -10.262 73.263 1.00 57.38 ? 52 LEU A O 1 ATOM 384 C CB . LEU A 1 52 ? 48.980 -8.890 73.117 1.00 54.29 ? 52 LEU A CB 1 ATOM 385 C CG . LEU A 1 52 ? 50.439 -9.253 73.437 1.00 54.37 ? 52 LEU A CG 1 ATOM 386 C CD1 . LEU A 1 52 ? 51.053 -8.257 74.402 1.00 52.04 ? 52 LEU A CD1 1 ATOM 387 C CD2 . LEU A 1 52 ? 50.611 -10.649 74.005 1.00 51.08 ? 52 LEU A CD2 1 ATOM 388 N N . TYR A 1 53 ? 46.260 -8.833 71.548 1.00 56.95 ? 53 TYR A N 1 ATOM 389 C CA . TYR A 1 53 ? 44.875 -8.393 71.460 1.00 56.81 ? 53 TYR A CA 1 ATOM 390 C C . TYR A 1 53 ? 44.653 -7.892 70.032 1.00 57.67 ? 53 TYR A C 1 ATOM 391 O O . TYR A 1 53 ? 45.651 -7.449 69.457 1.00 58.33 ? 53 TYR A O 1 ATOM 392 C CB . TYR A 1 53 ? 44.605 -7.268 72.451 1.00 56.05 ? 53 TYR A CB 1 ATOM 393 C CG . TYR A 1 53 ? 43.207 -6.697 72.406 1.00 56.05 ? 53 TYR A CG 1 ATOM 394 C CD1 . TYR A 1 53 ? 42.075 -7.495 72.526 1.00 56.09 ? 53 TYR A CD1 1 ATOM 395 C CD2 . TYR A 1 53 ? 43.020 -5.332 72.254 1.00 56.10 ? 53 TYR A CD2 1 ATOM 396 C CE1 . TYR A 1 53 ? 40.805 -6.960 72.458 1.00 56.97 ? 53 TYR A CE1 1 ATOM 397 C CE2 . TYR A 1 53 ? 41.763 -4.777 72.217 1.00 57.15 ? 53 TYR A CE2 1 ATOM 398 C CZ . TYR A 1 53 ? 40.648 -5.596 72.309 1.00 58.30 ? 53 TYR A CZ 1 ATOM 399 O OH . TYR A 1 53 ? 39.386 -5.019 72.236 1.00 58.77 ? 53 TYR A OH 1 ATOM 400 N N . SER A 1 54 ? 43.633 -8.397 69.361 1.00 57.96 ? 54 SER A N 1 ATOM 401 C CA . SER A 1 54 ? 43.238 -7.993 68.028 1.00 58.07 ? 54 SER A CA 1 ATOM 402 C C . SER A 1 54 ? 41.924 -7.215 68.162 1.00 58.66 ? 54 SER A C 1 ATOM 403 O O . SER A 1 54 ? 41.061 -7.628 68.943 1.00 59.38 ? 54 SER A O 1 ATOM 404 C CB . SER A 1 54 ? 42.938 -9.202 67.133 1.00 55.05 ? 54 SER A CB 1 ATOM 405 O OG . SER A 1 54 ? 43.907 -10.201 67.403 1.00 62.08 ? 54 SER A OG 1 ATOM 406 N N . PHE A 1 55 ? 41.750 -6.108 67.484 1.00 58.33 ? 55 PHE A N 1 ATOM 407 C CA . PHE A 1 55 ? 40.533 -5.320 67.516 1.00 58.29 ? 55 PHE A CA 1 ATOM 408 C C . PHE A 1 55 ? 40.080 -4.929 66.125 1.00 59.61 ? 55 PHE A C 1 ATOM 409 O O . PHE A 1 55 ? 40.851 -4.894 65.160 1.00 60.07 ? 55 PHE A O 1 ATOM 410 C CB . PHE A 1 55 ? 40.640 -4.136 68.466 1.00 51.80 ? 55 PHE A CB 1 ATOM 411 C CG . PHE A 1 55 ? 41.873 -3.291 68.332 1.00 46.41 ? 55 PHE A CG 1 ATOM 412 C CD1 . PHE A 1 55 ? 41.815 -2.086 67.672 1.00 42.14 ? 55 PHE A CD1 1 ATOM 413 C CD2 . PHE A 1 55 ? 43.092 -3.705 68.836 1.00 44.70 ? 55 PHE A CD2 1 ATOM 414 C CE1 . PHE A 1 55 ? 42.957 -1.329 67.547 1.00 43.00 ? 55 PHE A CE1 1 ATOM 415 C CE2 . PHE A 1 55 ? 44.224 -2.923 68.716 1.00 44.00 ? 55 PHE A CE2 1 ATOM 416 C CZ . PHE A 1 55 ? 44.183 -1.734 68.029 1.00 41.09 ? 55 PHE A CZ 1 ATOM 417 N N . GLU A 1 56 ? 38.796 -4.704 65.921 1.00 61.30 ? 56 GLU A N 1 ATOM 418 C CA . GLU A 1 56 ? 38.351 -4.442 64.548 1.00 63.52 ? 56 GLU A CA 1 ATOM 419 C C . GLU A 1 56 ? 37.049 -3.677 64.557 1.00 64.85 ? 56 GLU A C 1 ATOM 420 O O . GLU A 1 56 ? 36.095 -4.083 65.200 1.00 64.99 ? 56 GLU A O 1 ATOM 421 C CB . GLU A 1 56 ? 38.182 -5.760 63.809 1.00 63.34 ? 56 GLU A CB 1 ATOM 422 C CG . GLU A 1 56 ? 37.484 -5.498 62.485 1.00 64.91 ? 56 GLU A CG 1 ATOM 423 C CD . GLU A 1 56 ? 37.747 -6.639 61.526 1.00 67.47 ? 56 GLU A CD 1 ATOM 424 O OE1 . GLU A 1 56 ? 37.775 -7.778 62.030 1.00 67.00 ? 56 GLU A OE1 1 ATOM 425 O OE2 . GLU A 1 56 ? 37.915 -6.284 60.335 1.00 70.64 ? 56 GLU A OE2 1 ATOM 426 N N . ASP A 1 57 ? 37.050 -2.490 63.970 1.00 66.31 ? 57 ASP A N 1 ATOM 427 C CA . ASP A 1 57 ? 35.832 -1.678 64.057 1.00 68.32 ? 57 ASP A CA 1 ATOM 428 C C . ASP A 1 57 ? 35.450 -1.501 65.536 1.00 69.46 ? 57 ASP A C 1 ATOM 429 O O . ASP A 1 57 ? 34.350 -1.879 65.981 1.00 69.34 ? 57 ASP A O 1 ATOM 430 C CB . ASP A 1 57 ? 34.683 -2.356 63.338 1.00 70.02 ? 57 ASP A CB 1 ATOM 431 C CG . ASP A 1 57 ? 34.825 -2.494 61.842 1.00 74.31 ? 57 ASP A CG 1 ATOM 432 O OD1 . ASP A 1 57 ? 35.393 -1.594 61.178 1.00 76.24 ? 57 ASP A OD1 1 ATOM 433 O OD2 . ASP A 1 57 ? 34.304 -3.513 61.315 1.00 75.33 ? 57 ASP A OD2 1 ATOM 434 N N . SER A 1 58 ? 36.437 -1.077 66.330 1.00 70.12 ? 58 SER A N 1 ATOM 435 C CA . SER A 1 58 ? 36.222 -0.779 67.737 1.00 70.79 ? 58 SER A CA 1 ATOM 436 C C . SER A 1 58 ? 36.050 0.734 67.914 1.00 70.90 ? 58 SER A C 1 ATOM 437 O O . SER A 1 58 ? 36.269 1.520 66.980 1.00 70.78 ? 58 SER A O 1 ATOM 438 C CB . SER A 1 58 ? 37.371 -1.309 68.585 1.00 72.43 ? 58 SER A CB 1 ATOM 439 O OG . SER A 1 58 ? 37.210 -1.044 69.967 1.00 76.12 ? 58 SER A OG 1 ATOM 440 N N . GLY A 1 59 ? 35.299 1.097 68.958 1.00 70.62 ? 59 GLY A N 1 ATOM 441 C CA . GLY A 1 59 ? 35.166 2.504 69.292 1.00 70.63 ? 59 GLY A CA 1 ATOM 442 C C . GLY A 1 59 ? 34.266 3.255 68.335 1.00 70.40 ? 59 GLY A C 1 ATOM 443 O O . GLY A 1 59 ? 33.662 2.706 67.426 1.00 70.92 ? 59 GLY A O 1 ATOM 444 N N . VAL A 1 60 ? 34.175 4.552 68.587 1.00 70.04 ? 60 VAL A N 1 ATOM 445 C CA . VAL A 1 60 ? 33.257 5.417 67.868 1.00 69.36 ? 60 VAL A CA 1 ATOM 446 C C . VAL A 1 60 ? 33.682 5.573 66.423 1.00 69.39 ? 60 VAL A C 1 ATOM 447 O O . VAL A 1 60 ? 32.845 5.222 65.585 1.00 70.03 ? 60 VAL A O 1 ATOM 448 C CB . VAL A 1 60 ? 33.067 6.723 68.644 1.00 66.49 ? 60 VAL A CB 1 ATOM 449 C CG1 . VAL A 1 60 ? 33.805 7.910 68.054 1.00 64.25 ? 60 VAL A CG1 1 ATOM 450 C CG2 . VAL A 1 60 ? 31.583 7.032 68.771 1.00 67.33 ? 60 VAL A CG2 1 ATOM 451 N N . GLY A 1 61 ? 34.954 5.827 66.141 1.00 68.74 ? 61 GLY A N 1 ATOM 452 C CA . GLY A 1 61 ? 35.437 6.018 64.786 1.00 68.13 ? 61 GLY A CA 1 ATOM 453 C C . GLY A 1 61 ? 36.005 4.802 64.066 1.00 67.52 ? 61 GLY A C 1 ATOM 454 O O . GLY A 1 61 ? 36.778 4.885 63.117 1.00 67.54 ? 61 GLY A O 1 ATOM 455 N N . ASP A 1 62 ? 35.666 3.613 64.525 1.00 67.19 ? 62 ASP A N 1 ATOM 456 C CA . ASP A 1 62 ? 36.000 2.314 64.005 1.00 66.59 ? 62 ASP A CA 1 ATOM 457 C C . ASP A 1 62 ? 37.498 2.200 63.757 1.00 64.89 ? 62 ASP A C 1 ATOM 458 O O . ASP A 1 62 ? 38.026 2.673 62.761 1.00 65.65 ? 62 ASP A O 1 ATOM 459 C CB . ASP A 1 62 ? 35.227 1.947 62.730 1.00 72.12 ? 62 ASP A CB 1 ATOM 460 C CG . ASP A 1 62 ? 33.761 1.631 62.976 1.00 75.24 ? 62 ASP A CG 1 ATOM 461 O OD1 . ASP A 1 62 ? 32.939 2.551 63.208 1.00 77.61 ? 62 ASP A OD1 1 ATOM 462 O OD2 . ASP A 1 62 ? 33.348 0.450 62.935 1.00 75.75 ? 62 ASP A OD2 1 ATOM 463 N N . VAL A 1 63 ? 38.195 1.716 64.753 1.00 62.27 ? 63 VAL A N 1 ATOM 464 C CA . VAL A 1 63 ? 39.616 1.548 64.887 1.00 58.38 ? 63 VAL A CA 1 ATOM 465 C C . VAL A 1 63 ? 39.898 0.049 64.825 1.00 55.98 ? 63 VAL A C 1 ATOM 466 O O . VAL A 1 63 ? 39.303 -0.790 65.460 1.00 54.77 ? 63 VAL A O 1 ATOM 467 C CB . VAL A 1 63 ? 40.106 2.048 66.262 1.00 59.12 ? 63 VAL A CB 1 ATOM 468 C CG1 . VAL A 1 63 ? 41.567 1.757 66.543 1.00 60.50 ? 63 VAL A CG1 1 ATOM 469 C CG2 . VAL A 1 63 ? 39.772 3.531 66.387 1.00 59.19 ? 63 VAL A CG2 1 ATOM 470 N N . THR A 1 64 ? 40.853 -0.219 63.941 1.00 53.80 ? 64 THR A N 1 ATOM 471 C CA . THR A 1 64 ? 41.189 -1.608 63.617 1.00 50.58 ? 64 THR A CA 1 ATOM 472 C C . THR A 1 64 ? 42.680 -1.724 63.855 1.00 49.39 ? 64 THR A C 1 ATOM 473 O O . THR A 1 64 ? 43.344 -0.692 63.723 1.00 49.43 ? 64 THR A O 1 ATOM 474 C CB . THR A 1 64 ? 40.778 -1.829 62.144 1.00 45.67 ? 64 THR A CB 1 ATOM 475 O OG1 . THR A 1 64 ? 39.348 -1.705 62.043 1.00 41.56 ? 64 THR A OG1 1 ATOM 476 C CG2 . THR A 1 64 ? 41.214 -3.170 61.606 1.00 42.80 ? 64 THR A CG2 1 ATOM 477 N N . GLY A 1 65 ? 43.186 -2.809 64.426 1.00 47.80 ? 65 GLY A N 1 ATOM 478 C CA . GLY A 1 65 ? 44.598 -2.927 64.640 1.00 46.12 ? 65 GLY A CA 1 ATOM 479 C C . GLY A 1 65 ? 44.904 -4.183 65.426 1.00 45.34 ? 65 GLY A C 1 ATOM 480 O O . GLY A 1 65 ? 43.999 -4.898 65.805 1.00 44.42 ? 65 GLY A O 1 ATOM 481 N N . PHE A 1 66 ? 46.154 -4.198 65.896 1.00 44.99 ? 66 PHE A N 1 ATOM 482 C CA . PHE A 1 66 ? 46.536 -5.309 66.766 1.00 44.50 ? 66 PHE A CA 1 ATOM 483 C C . PHE A 1 66 ? 47.647 -4.804 67.696 1.00 44.26 ? 66 PHE A C 1 ATOM 484 O O . PHE A 1 66 ? 48.101 -3.675 67.547 1.00 44.40 ? 66 PHE A O 1 ATOM 485 C CB . PHE A 1 66 ? 46.856 -6.553 65.963 1.00 41.61 ? 66 PHE A CB 1 ATOM 486 C CG . PHE A 1 66 ? 48.077 -6.325 65.108 1.00 40.20 ? 66 PHE A CG 1 ATOM 487 C CD1 . PHE A 1 66 ? 49.314 -6.479 65.680 1.00 39.89 ? 66 PHE A CD1 1 ATOM 488 C CD2 . PHE A 1 66 ? 48.001 -5.929 63.794 1.00 38.94 ? 66 PHE A CD2 1 ATOM 489 C CE1 . PHE A 1 66 ? 50.467 -6.245 64.933 1.00 40.06 ? 66 PHE A CE1 1 ATOM 490 C CE2 . PHE A 1 66 ? 49.161 -5.690 63.070 1.00 38.12 ? 66 PHE A CE2 1 ATOM 491 C CZ . PHE A 1 66 ? 50.413 -5.876 63.610 1.00 36.02 ? 66 PHE A CZ 1 ATOM 492 N N . LEU A 1 67 ? 47.634 -5.345 68.908 1.00 43.57 ? 67 LEU A N 1 ATOM 493 C CA . LEU A 1 67 ? 48.671 -5.179 69.891 1.00 43.44 ? 67 LEU A CA 1 ATOM 494 C C . LEU A 1 67 ? 49.529 -6.454 69.881 1.00 43.29 ? 67 LEU A C 1 ATOM 495 O O . LEU A 1 67 ? 48.927 -7.501 70.072 1.00 43.29 ? 67 LEU A O 1 ATOM 496 C CB . LEU A 1 67 ? 48.156 -4.950 71.325 1.00 39.16 ? 67 LEU A CB 1 ATOM 497 C CG . LEU A 1 67 ? 49.283 -4.851 72.363 1.00 39.07 ? 67 LEU A CG 1 ATOM 498 C CD1 . LEU A 1 67 ? 50.048 -3.541 72.249 1.00 38.75 ? 67 LEU A CD1 1 ATOM 499 C CD2 . LEU A 1 67 ? 48.760 -4.975 73.777 1.00 41.17 ? 67 LEU A CD2 1 ATOM 500 N N . ALA A 1 68 ? 50.835 -6.343 69.693 1.00 43.18 ? 68 ALA A N 1 ATOM 501 C CA . ALA A 1 68 ? 51.706 -7.474 69.579 1.00 43.55 ? 68 ALA A CA 1 ATOM 502 C C . ALA A 1 68 ? 52.885 -7.579 70.551 1.00 44.71 ? 68 ALA A C 1 ATOM 503 O O . ALA A 1 68 ? 53.638 -6.647 70.861 1.00 44.19 ? 68 ALA A O 1 ATOM 504 C CB . ALA A 1 68 ? 52.410 -7.484 68.216 1.00 40.22 ? 68 ALA A CB 1 ATOM 505 N N . LEU A 1 69 ? 53.317 -8.855 70.601 1.00 45.37 ? 69 LEU A N 1 ATOM 506 C CA . LEU A 1 69 ? 54.451 -9.235 71.407 1.00 45.07 ? 69 LEU A CA 1 ATOM 507 C C . LEU A 1 69 ? 55.579 -9.674 70.494 1.00 45.57 ? 69 LEU A C 1 ATOM 508 O O . LEU A 1 69 ? 55.410 -10.552 69.648 1.00 45.84 ? 69 LEU A O 1 ATOM 509 C CB . LEU A 1 69 ? 54.152 -10.352 72.397 1.00 44.13 ? 69 LEU A CB 1 ATOM 510 C CG . LEU A 1 69 ? 55.300 -10.446 73.428 1.00 47.87 ? 69 LEU A CG 1 ATOM 511 C CD1 . LEU A 1 69 ? 55.247 -9.214 74.339 1.00 46.28 ? 69 LEU A CD1 1 ATOM 512 C CD2 . LEU A 1 69 ? 55.223 -11.756 74.191 1.00 45.52 ? 69 LEU A CD2 1 ATOM 513 N N . ASP A 1 70 ? 56.728 -9.017 70.650 1.00 45.85 ? 70 ASP A N 1 ATOM 514 C CA . ASP A 1 70 ? 57.831 -9.408 69.753 1.00 45.21 ? 70 ASP A CA 1 ATOM 515 C C . ASP A 1 70 ? 58.957 -9.746 70.712 1.00 45.67 ? 70 ASP A C 1 ATOM 516 O O . ASP A 1 70 ? 59.685 -8.832 71.068 1.00 45.88 ? 70 ASP A O 1 ATOM 517 C CB . ASP A 1 70 ? 58.130 -8.357 68.721 1.00 40.15 ? 70 ASP A CB 1 ATOM 518 C CG . ASP A 1 70 ? 59.314 -8.542 67.817 1.00 39.46 ? 70 ASP A CG 1 ATOM 519 O OD1 . ASP A 1 70 ? 60.205 -9.365 68.140 1.00 38.46 ? 70 ASP A OD1 1 ATOM 520 O OD2 . ASP A 1 70 ? 59.412 -7.864 66.751 1.00 39.03 ? 70 ASP A OD2 1 ATOM 521 N N . ASN A 1 71 ? 59.115 -11.039 71.009 1.00 45.89 ? 71 ASN A N 1 ATOM 522 C CA . ASN A 1 71 ? 60.226 -11.455 71.829 1.00 45.90 ? 71 ASN A CA 1 ATOM 523 C C . ASN A 1 71 ? 61.538 -11.406 71.081 1.00 46.42 ? 71 ASN A C 1 ATOM 524 O O . ASN A 1 71 ? 62.500 -11.600 71.831 1.00 48.02 ? 71 ASN A O 1 ATOM 525 C CB . ASN A 1 71 ? 60.113 -12.883 72.376 1.00 44.23 ? 71 ASN A CB 1 ATOM 526 C CG . ASN A 1 71 ? 58.818 -13.039 73.151 1.00 44.58 ? 71 ASN A CG 1 ATOM 527 O OD1 . ASN A 1 71 ? 58.500 -12.297 74.068 1.00 45.58 ? 71 ASN A OD1 1 ATOM 528 N ND2 . ASN A 1 71 ? 58.045 -14.023 72.745 1.00 45.03 ? 71 ASN A ND2 1 ATOM 529 N N . THR A 1 72 ? 61.667 -11.227 69.790 1.00 46.10 ? 72 THR A N 1 ATOM 530 C CA . THR A 1 72 ? 63.017 -11.303 69.199 1.00 46.17 ? 72 THR A CA 1 ATOM 531 C C . THR A 1 72 ? 63.696 -9.949 69.325 1.00 46.23 ? 72 THR A C 1 ATOM 532 O O . THR A 1 72 ? 64.832 -9.802 69.738 1.00 45.39 ? 72 THR A O 1 ATOM 533 C CB . THR A 1 72 ? 62.829 -11.715 67.730 1.00 47.44 ? 72 THR A CB 1 ATOM 534 O OG1 . THR A 1 72 ? 62.479 -13.109 67.745 1.00 50.22 ? 72 THR A OG1 1 ATOM 535 C CG2 . THR A 1 72 ? 63.998 -11.493 66.830 1.00 42.62 ? 72 THR A CG2 1 ATOM 536 N N . ASN A 1 73 ? 62.884 -8.932 69.052 1.00 46.11 ? 73 ASN A N 1 ATOM 537 C CA . ASN A 1 73 ? 63.250 -7.533 69.069 1.00 45.97 ? 73 ASN A CA 1 ATOM 538 C C . ASN A 1 73 ? 62.945 -6.916 70.445 1.00 46.28 ? 73 ASN A C 1 ATOM 539 O O . ASN A 1 73 ? 63.283 -5.762 70.750 1.00 45.68 ? 73 ASN A O 1 ATOM 540 C CB . ASN A 1 73 ? 62.448 -6.795 67.993 1.00 44.04 ? 73 ASN A CB 1 ATOM 541 C CG . ASN A 1 73 ? 62.923 -7.196 66.594 1.00 43.96 ? 73 ASN A CG 1 ATOM 542 O OD1 . ASN A 1 73 ? 64.018 -6.752 66.246 1.00 39.86 ? 73 ASN A OD1 1 ATOM 543 N ND2 . ASN A 1 73 ? 62.076 -7.957 65.901 1.00 40.72 ? 73 ASN A ND2 1 ATOM 544 N N . LYS A 1 74 ? 62.233 -7.693 71.257 1.00 45.47 ? 74 LYS A N 1 ATOM 545 C CA . LYS A 1 74 ? 61.962 -7.237 72.617 1.00 46.40 ? 74 LYS A CA 1 ATOM 546 C C . LYS A 1 74 ? 61.100 -5.976 72.560 1.00 45.28 ? 74 LYS A C 1 ATOM 547 O O . LYS A 1 74 ? 61.499 -4.919 73.031 1.00 45.24 ? 74 LYS A O 1 ATOM 548 C CB . LYS A 1 74 ? 63.268 -6.923 73.348 1.00 50.90 ? 74 LYS A CB 1 ATOM 549 C CG . LYS A 1 74 ? 63.998 -8.111 73.946 1.00 55.44 ? 74 LYS A CG 1 ATOM 550 C CD . LYS A 1 74 ? 65.435 -7.698 74.231 1.00 59.96 ? 74 LYS A CD 1 ATOM 551 C CE . LYS A 1 74 ? 65.947 -8.213 75.567 1.00 65.53 ? 74 LYS A CE 1 ATOM 552 N NZ . LYS A 1 74 ? 65.571 -7.313 76.712 1.00 67.27 ? 74 LYS A NZ 1 ATOM 553 N N . LEU A 1 75 ? 59.951 -6.106 71.920 1.00 43.87 ? 75 LEU A N 1 ATOM 554 C CA . LEU A 1 75 ? 59.000 -5.052 71.742 1.00 42.89 ? 75 LEU A CA 1 ATOM 555 C C . LEU A 1 75 ? 57.575 -5.395 72.183 1.00 42.03 ? 75 LEU A C 1 ATOM 556 O O . LEU A 1 75 ? 57.170 -6.551 72.130 1.00 40.44 ? 75 LEU A O 1 ATOM 557 C CB . LEU A 1 75 ? 58.849 -4.713 70.236 1.00 42.33 ? 75 LEU A CB 1 ATOM 558 C CG . LEU A 1 75 ? 60.162 -4.397 69.519 1.00 43.23 ? 75 LEU A CG 1 ATOM 559 C CD1 . LEU A 1 75 ? 59.895 -4.247 68.029 1.00 41.45 ? 75 LEU A CD1 1 ATOM 560 C CD2 . LEU A 1 75 ? 60.865 -3.162 70.084 1.00 39.65 ? 75 LEU A CD2 1 ATOM 561 N N . ILE A 1 76 ? 56.845 -4.311 72.446 1.00 41.47 ? 76 ILE A N 1 ATOM 562 C CA . ILE A 1 76 ? 55.422 -4.352 72.724 1.00 41.33 ? 76 ILE A CA 1 ATOM 563 C C . ILE A 1 76 ? 54.865 -3.267 71.776 1.00 42.27 ? 76 ILE A C 1 ATOM 564 O O . ILE A 1 76 ? 55.322 -2.127 71.887 1.00 42.51 ? 76 ILE A O 1 ATOM 565 C CB . ILE A 1 76 ? 55.027 -3.938 74.141 1.00 41.01 ? 76 ILE A CB 1 ATOM 566 C CG1 . ILE A 1 76 ? 55.613 -4.944 75.147 1.00 36.63 ? 76 ILE A CG1 1 ATOM 567 C CG2 . ILE A 1 76 ? 53.503 -3.800 74.257 1.00 40.27 ? 76 ILE A CG2 1 ATOM 568 C CD1 . ILE A 1 76 ? 55.484 -4.493 76.561 1.00 32.53 ? 76 ILE A CD1 1 ATOM 569 N N . VAL A 1 77 ? 54.279 -3.740 70.686 1.00 42.03 ? 77 VAL A N 1 ATOM 570 C CA . VAL A 1 77 ? 53.849 -2.968 69.566 1.00 41.42 ? 77 VAL A CA 1 ATOM 571 C C . VAL A 1 77 ? 52.328 -2.910 69.432 1.00 42.11 ? 77 VAL A C 1 ATOM 572 O O . VAL A 1 77 ? 51.679 -3.925 69.173 1.00 41.23 ? 77 VAL A O 1 ATOM 573 C CB . VAL A 1 77 ? 54.268 -3.612 68.219 1.00 40.45 ? 77 VAL A CB 1 ATOM 574 C CG1 . VAL A 1 77 ? 53.879 -2.639 67.095 1.00 40.65 ? 77 VAL A CG1 1 ATOM 575 C CG2 . VAL A 1 77 ? 55.722 -3.932 68.144 1.00 37.91 ? 77 VAL A CG2 1 ATOM 576 N N . LEU A 1 78 ? 51.843 -1.674 69.372 1.00 42.69 ? 78 LEU A N 1 ATOM 577 C CA . LEU A 1 78 ? 50.413 -1.424 69.191 1.00 42.61 ? 78 LEU A CA 1 ATOM 578 C C . LEU A 1 78 ? 50.231 -0.842 67.778 1.00 43.70 ? 78 LEU A C 1 ATOM 579 O O . LEU A 1 78 ? 50.556 0.334 67.556 1.00 43.21 ? 78 LEU A O 1 ATOM 580 C CB . LEU A 1 78 ? 49.898 -0.387 70.154 1.00 40.89 ? 78 LEU A CB 1 ATOM 581 C CG . LEU A 1 78 ? 48.429 -0.011 70.203 1.00 42.38 ? 78 LEU A CG 1 ATOM 582 C CD1 . LEU A 1 78 ? 47.623 -1.289 70.460 1.00 42.26 ? 78 LEU A CD1 1 ATOM 583 C CD2 . LEU A 1 78 ? 48.139 1.001 71.333 1.00 40.34 ? 78 LEU A CD2 1 ATOM 584 N N . SER A 1 79 ? 49.647 -1.663 66.889 1.00 43.53 ? 79 SER A N 1 ATOM 585 C CA . SER A 1 79 ? 49.519 -1.180 65.534 1.00 43.37 ? 79 SER A CA 1 ATOM 586 C C . SER A 1 79 ? 48.099 -0.851 65.151 1.00 43.44 ? 79 SER A C 1 ATOM 587 O O . SER A 1 79 ? 47.180 -1.660 65.145 1.00 43.75 ? 79 SER A O 1 ATOM 588 C CB . SER A 1 79 ? 50.248 -2.182 64.645 1.00 42.33 ? 79 SER A CB 1 ATOM 589 O OG . SER A 1 79 ? 50.107 -1.929 63.263 1.00 41.73 ? 79 SER A OG 1 ATOM 590 N N . PHE A 1 80 ? 47.946 0.256 64.451 1.00 43.82 ? 80 PHE A N 1 ATOM 591 C CA . PHE A 1 80 ? 46.699 0.730 63.901 1.00 43.94 ? 80 PHE A CA 1 ATOM 592 C C . PHE A 1 80 ? 46.708 0.682 62.379 1.00 44.89 ? 80 PHE A C 1 ATOM 593 O O . PHE A 1 80 ? 47.539 1.234 61.678 1.00 45.31 ? 80 PHE A O 1 ATOM 594 C CB . PHE A 1 80 ? 46.528 2.195 64.261 1.00 43.63 ? 80 PHE A CB 1 ATOM 595 C CG . PHE A 1 80 ? 46.480 2.451 65.720 1.00 43.82 ? 80 PHE A CG 1 ATOM 596 C CD1 . PHE A 1 80 ? 45.256 2.511 66.366 1.00 42.94 ? 80 PHE A CD1 1 ATOM 597 C CD2 . PHE A 1 80 ? 47.639 2.621 66.445 1.00 43.88 ? 80 PHE A CD2 1 ATOM 598 C CE1 . PHE A 1 80 ? 45.188 2.742 67.721 1.00 41.65 ? 80 PHE A CE1 1 ATOM 599 C CE2 . PHE A 1 80 ? 47.569 2.836 67.818 1.00 43.26 ? 80 PHE A CE2 1 ATOM 600 C CZ . PHE A 1 80 ? 46.350 2.911 68.455 1.00 43.04 ? 80 PHE A CZ 1 ATOM 601 N N . ARG A 1 81 ? 45.580 0.256 61.833 1.00 45.84 ? 81 ARG A N 1 ATOM 602 C CA . ARG A 1 81 ? 45.363 0.157 60.397 1.00 45.28 ? 81 ARG A CA 1 ATOM 603 C C . ARG A 1 81 ? 44.773 1.486 59.956 1.00 45.16 ? 81 ARG A C 1 ATOM 604 O O . ARG A 1 81 ? 44.006 2.079 60.697 1.00 43.93 ? 81 ARG A O 1 ATOM 605 C CB . ARG A 1 81 ? 44.344 -0.948 60.157 1.00 45.60 ? 81 ARG A CB 1 ATOM 606 C CG . ARG A 1 81 ? 44.316 -1.550 58.777 1.00 46.02 ? 81 ARG A CG 1 ATOM 607 C CD . ARG A 1 81 ? 42.987 -1.335 58.099 1.00 47.35 ? 81 ARG A CD 1 ATOM 608 N NE . ARG A 1 81 ? 41.985 -2.347 58.312 1.00 42.22 ? 81 ARG A NE 1 ATOM 609 C CZ . ARG A 1 81 ? 40.694 -2.112 58.454 1.00 43.03 ? 81 ARG A CZ 1 ATOM 610 N NH1 . ARG A 1 81 ? 40.078 -0.943 58.450 1.00 40.73 ? 81 ARG A NH1 1 ATOM 611 N NH2 . ARG A 1 81 ? 39.899 -3.160 58.662 1.00 46.53 ? 81 ARG A NH2 1 ATOM 612 N N . GLY A 1 82 ? 45.152 1.874 58.764 1.00 46.06 ? 82 GLY A N 1 ATOM 613 C CA . GLY A 1 82 ? 44.595 3.103 58.197 1.00 47.63 ? 82 GLY A CA 1 ATOM 614 C C . GLY A 1 82 ? 43.236 2.697 57.589 1.00 49.08 ? 82 GLY A C 1 ATOM 615 O O . GLY A 1 82 ? 42.763 1.585 57.865 1.00 48.10 ? 82 GLY A O 1 ATOM 616 N N . SER A 1 83 ? 42.649 3.594 56.797 1.00 50.45 ? 83 SER A N 1 ATOM 617 C CA . SER A 1 83 ? 41.343 3.230 56.275 1.00 52.96 ? 83 SER A CA 1 ATOM 618 C C . SER A 1 83 ? 41.398 2.108 55.252 1.00 55.27 ? 83 SER A C 1 ATOM 619 O O . SER A 1 83 ? 42.203 1.884 54.305 1.00 55.20 ? 83 SER A O 1 ATOM 620 C CB . SER A 1 83 ? 40.627 4.453 55.742 1.00 52.87 ? 83 SER A CB 1 ATOM 621 O OG . SER A 1 83 ? 40.068 4.051 54.514 1.00 54.69 ? 83 SER A OG 1 ATOM 622 N N . ARG A 1 84 ? 40.399 1.233 55.463 1.00 56.75 ? 84 ARG A N 1 ATOM 623 C CA . ARG A 1 84 ? 40.094 0.143 54.507 1.00 58.75 ? 84 ARG A CA 1 ATOM 624 C C . ARG A 1 84 ? 40.030 0.565 53.055 1.00 58.39 ? 84 ARG A C 1 ATOM 625 O O . ARG A 1 84 ? 40.258 -0.328 52.236 1.00 59.41 ? 84 ARG A O 1 ATOM 626 C CB . ARG A 1 84 ? 38.725 -0.507 54.794 1.00 63.72 ? 84 ARG A CB 1 ATOM 627 C CG . ARG A 1 84 ? 38.959 -2.001 55.002 1.00 68.52 ? 84 ARG A CG 1 ATOM 628 C CD . ARG A 1 84 ? 37.658 -2.678 54.586 1.00 75.79 ? 84 ARG A CD 1 ATOM 629 N NE . ARG A 1 84 ? 36.876 -3.061 55.753 1.00 80.90 ? 84 ARG A NE 1 ATOM 630 C CZ . ARG A 1 84 ? 36.336 -2.267 56.671 1.00 83.74 ? 84 ARG A CZ 1 ATOM 631 N NH1 . ARG A 1 84 ? 36.404 -0.936 56.680 1.00 84.74 ? 84 ARG A NH1 1 ATOM 632 N NH2 . ARG A 1 84 ? 35.674 -2.882 57.658 1.00 84.49 ? 84 ARG A NH2 1 ATOM 633 N N . SER A 1 85 ? 39.506 1.732 52.705 1.00 58.02 ? 85 SER A N 1 ATOM 634 C CA . SER A 1 85 ? 39.638 2.215 51.333 1.00 58.14 ? 85 SER A CA 1 ATOM 635 C C . SER A 1 85 ? 40.002 3.689 51.355 1.00 57.32 ? 85 SER A C 1 ATOM 636 O O . SER A 1 85 ? 39.171 4.578 51.482 1.00 57.78 ? 85 SER A O 1 ATOM 637 C CB . SER A 1 85 ? 38.397 1.911 50.499 1.00 60.61 ? 85 SER A CB 1 ATOM 638 O OG . SER A 1 85 ? 37.296 2.672 50.933 1.00 63.26 ? 85 SER A OG 1 ATOM 639 N N . ILE A 1 86 ? 41.269 3.987 51.219 1.00 56.89 ? 86 ILE A N 1 ATOM 640 C CA . ILE A 1 86 ? 41.901 5.268 51.455 1.00 57.22 ? 86 ILE A CA 1 ATOM 641 C C . ILE A 1 86 ? 41.510 6.404 50.563 1.00 58.19 ? 86 ILE A C 1 ATOM 642 O O . ILE A 1 86 ? 41.404 7.573 50.959 1.00 58.67 ? 86 ILE A O 1 ATOM 643 C CB . ILE A 1 86 ? 43.447 5.061 51.489 1.00 53.83 ? 86 ILE A CB 1 ATOM 644 C CG1 . ILE A 1 86 ? 43.708 4.169 52.711 1.00 50.54 ? 86 ILE A CG1 1 ATOM 645 C CG2 . ILE A 1 86 ? 44.258 6.329 51.531 1.00 48.00 ? 86 ILE A CG2 1 ATOM 646 C CD1 . ILE A 1 86 ? 45.002 3.440 52.794 1.00 49.34 ? 86 ILE A CD1 1 ATOM 647 N N . GLU A 1 87 ? 41.289 6.116 49.297 1.00 58.95 ? 87 GLU A N 1 ATOM 648 C CA . GLU A 1 87 ? 40.924 7.144 48.331 1.00 59.98 ? 87 GLU A CA 1 ATOM 649 C C . GLU A 1 87 ? 39.653 7.842 48.794 1.00 60.38 ? 87 GLU A C 1 ATOM 650 O O . GLU A 1 87 ? 39.520 9.069 48.774 1.00 59.89 ? 87 GLU A O 1 ATOM 651 C CB . GLU A 1 87 ? 40.759 6.443 46.982 1.00 63.08 ? 87 GLU A CB 1 ATOM 652 C CG . GLU A 1 87 ? 41.546 7.113 45.873 1.00 65.23 ? 87 GLU A CG 1 ATOM 653 C CD . GLU A 1 87 ? 40.688 7.448 44.671 1.00 66.40 ? 87 GLU A CD 1 ATOM 654 O OE1 . GLU A 1 87 ? 39.451 7.340 44.812 1.00 67.45 ? 87 GLU A OE1 1 ATOM 655 O OE2 . GLU A 1 87 ? 41.279 7.826 43.639 1.00 65.57 ? 87 GLU A OE2 1 ATOM 656 N N . ASN A 1 88 ? 38.678 7.041 49.224 1.00 60.80 ? 88 ASN A N 1 ATOM 657 C CA . ASN A 1 88 ? 37.446 7.595 49.764 1.00 61.75 ? 88 ASN A CA 1 ATOM 658 C C . ASN A 1 88 ? 37.684 8.401 51.036 1.00 60.97 ? 88 ASN A C 1 ATOM 659 O O . ASN A 1 88 ? 37.179 9.516 51.202 1.00 60.40 ? 88 ASN A O 1 ATOM 660 C CB . ASN A 1 88 ? 36.410 6.501 50.022 1.00 67.73 ? 88 ASN A CB 1 ATOM 661 C CG . ASN A 1 88 ? 35.839 5.950 48.730 1.00 70.50 ? 88 ASN A CG 1 ATOM 662 O OD1 . ASN A 1 88 ? 35.178 4.908 48.783 1.00 73.97 ? 88 ASN A OD1 1 ATOM 663 N ND2 . ASN A 1 88 ? 36.097 6.613 47.606 1.00 70.27 ? 88 ASN A ND2 1 ATOM 664 N N . TRP A 1 89 ? 38.432 7.834 51.965 1.00 60.16 ? 89 TRP A N 1 ATOM 665 C CA . TRP A 1 89 ? 38.776 8.523 53.218 1.00 58.58 ? 89 TRP A CA 1 ATOM 666 C C . TRP A 1 89 ? 39.341 9.912 52.952 1.00 57.75 ? 89 TRP A C 1 ATOM 667 O O . TRP A 1 89 ? 38.904 10.939 53.485 1.00 56.70 ? 89 TRP A O 1 ATOM 668 C CB . TRP A 1 89 ? 39.744 7.566 53.921 1.00 56.42 ? 89 TRP A CB 1 ATOM 669 C CG . TRP A 1 89 ? 40.313 8.176 55.147 1.00 55.76 ? 89 TRP A CG 1 ATOM 670 C CD1 . TRP A 1 89 ? 39.707 8.252 56.357 1.00 56.56 ? 89 TRP A CD1 1 ATOM 671 C CD2 . TRP A 1 89 ? 41.581 8.817 55.289 1.00 55.76 ? 89 TRP A CD2 1 ATOM 672 N NE1 . TRP A 1 89 ? 40.477 8.970 57.236 1.00 56.31 ? 89 TRP A NE1 1 ATOM 673 C CE2 . TRP A 1 89 ? 41.642 9.316 56.600 1.00 57.14 ? 89 TRP A CE2 1 ATOM 674 C CE3 . TRP A 1 89 ? 42.677 8.968 54.436 1.00 54.87 ? 89 TRP A CE3 1 ATOM 675 C CZ2 . TRP A 1 89 ? 42.774 9.957 57.125 1.00 56.14 ? 89 TRP A CZ2 1 ATOM 676 C CZ3 . TRP A 1 89 ? 43.760 9.655 54.927 1.00 55.77 ? 89 TRP A CZ3 1 ATOM 677 C CH2 . TRP A 1 89 ? 43.797 10.150 56.262 1.00 56.40 ? 89 TRP A CH2 1 ATOM 678 N N . ILE A 1 90 ? 40.352 10.025 52.100 1.00 57.75 ? 90 ILE A N 1 ATOM 679 C CA . ILE A 1 90 ? 40.954 11.299 51.768 1.00 58.78 ? 90 ILE A CA 1 ATOM 680 C C . ILE A 1 90 ? 39.886 12.295 51.329 1.00 60.24 ? 90 ILE A C 1 ATOM 681 O O . ILE A 1 90 ? 39.768 13.376 51.887 1.00 60.69 ? 90 ILE A O 1 ATOM 682 C CB . ILE A 1 90 ? 41.981 11.195 50.630 1.00 55.90 ? 90 ILE A CB 1 ATOM 683 C CG1 . ILE A 1 90 ? 43.264 10.546 51.131 1.00 56.34 ? 90 ILE A CG1 1 ATOM 684 C CG2 . ILE A 1 90 ? 42.262 12.549 50.010 1.00 54.67 ? 90 ILE A CG2 1 ATOM 685 C CD1 . ILE A 1 90 ? 43.815 9.458 50.233 1.00 57.09 ? 90 ILE A CD1 1 ATOM 686 N N . GLY A 1 91 ? 39.094 11.919 50.331 1.00 60.96 ? 91 GLY A N 1 ATOM 687 C CA . GLY A 1 91 ? 38.084 12.780 49.769 1.00 61.75 ? 91 GLY A CA 1 ATOM 688 C C . GLY A 1 91 ? 37.007 13.238 50.715 1.00 62.52 ? 91 GLY A C 1 ATOM 689 O O . GLY A 1 91 ? 36.547 14.376 50.684 1.00 63.10 ? 91 GLY A O 1 ATOM 690 N N . ASN A 1 92 ? 36.609 12.381 51.637 1.00 63.31 ? 92 ASN A N 1 ATOM 691 C CA . ASN A 1 92 ? 35.606 12.633 52.642 1.00 63.59 ? 92 ASN A CA 1 ATOM 692 C C . ASN A 1 92 ? 36.265 13.303 53.847 1.00 63.66 ? 92 ASN A C 1 ATOM 693 O O . ASN A 1 92 ? 35.569 13.484 54.852 1.00 63.89 ? 92 ASN A O 1 ATOM 694 C CB . ASN A 1 92 ? 35.007 11.322 53.133 1.00 68.04 ? 92 ASN A CB 1 ATOM 695 C CG . ASN A 1 92 ? 34.184 10.520 52.165 1.00 72.21 ? 92 ASN A CG 1 ATOM 696 O OD1 . ASN A 1 92 ? 32.995 10.289 52.426 1.00 74.48 ? 92 ASN A OD1 1 ATOM 697 N ND2 . ASN A 1 92 ? 34.738 10.058 51.053 1.00 76.33 ? 92 ASN A ND2 1 ATOM 698 N N . LEU A 1 93 ? 37.575 13.526 53.807 1.00 63.24 ? 93 LEU A N 1 ATOM 699 C CA . LEU A 1 93 ? 38.209 14.069 54.996 1.00 63.10 ? 93 LEU A CA 1 ATOM 700 C C . LEU A 1 93 ? 37.679 15.465 55.303 1.00 63.62 ? 93 LEU A C 1 ATOM 701 O O . LEU A 1 93 ? 38.178 16.395 54.678 1.00 63.91 ? 93 LEU A O 1 ATOM 702 C CB . LEU A 1 93 ? 39.727 14.061 54.865 1.00 59.29 ? 93 LEU A CB 1 ATOM 703 C CG . LEU A 1 93 ? 40.517 14.165 56.171 1.00 55.96 ? 93 LEU A CG 1 ATOM 704 C CD1 . LEU A 1 93 ? 40.193 13.002 57.075 1.00 57.16 ? 93 LEU A CD1 1 ATOM 705 C CD2 . LEU A 1 93 ? 42.006 14.235 55.862 1.00 55.33 ? 93 LEU A CD2 1 ATOM 706 N N . ASN A 1 94 ? 37.127 15.637 56.496 1.00 64.29 ? 94 ASN A N 1 ATOM 707 C CA . ASN A 1 94 ? 36.786 16.901 57.123 1.00 64.43 ? 94 ASN A CA 1 ATOM 708 C C . ASN A 1 94 ? 37.960 17.398 57.968 1.00 64.38 ? 94 ASN A C 1 ATOM 709 O O . ASN A 1 94 ? 38.767 16.672 58.548 1.00 63.54 ? 94 ASN A O 1 ATOM 710 C CB . ASN A 1 94 ? 35.491 16.804 57.896 1.00 68.37 ? 94 ASN A CB 1 ATOM 711 C CG . ASN A 1 94 ? 35.368 17.053 59.363 1.00 71.47 ? 94 ASN A CG 1 ATOM 712 O OD1 . ASN A 1 94 ? 36.005 16.453 60.234 1.00 76.07 ? 94 ASN A OD1 1 ATOM 713 N ND2 . ASN A 1 94 ? 34.486 17.988 59.727 1.00 72.43 ? 94 ASN A ND2 1 ATOM 714 N N . PHE A 1 95 ? 38.176 18.714 57.917 1.00 64.45 ? 95 PHE A N 1 ATOM 715 C CA . PHE A 1 95 ? 39.236 19.428 58.579 1.00 64.26 ? 95 PHE A CA 1 ATOM 716 C C . PHE A 1 95 ? 38.814 20.105 59.874 1.00 64.81 ? 95 PHE A C 1 ATOM 717 O O . PHE A 1 95 ? 39.626 20.854 60.434 1.00 64.61 ? 95 PHE A O 1 ATOM 718 C CB . PHE A 1 95 ? 39.823 20.521 57.683 1.00 61.27 ? 95 PHE A CB 1 ATOM 719 C CG . PHE A 1 95 ? 40.054 20.104 56.263 1.00 61.51 ? 95 PHE A CG 1 ATOM 720 C CD1 . PHE A 1 95 ? 40.498 18.817 55.954 1.00 61.20 ? 95 PHE A CD1 1 ATOM 721 C CD2 . PHE A 1 95 ? 39.881 21.004 55.233 1.00 59.31 ? 95 PHE A CD2 1 ATOM 722 C CE1 . PHE A 1 95 ? 40.753 18.423 54.674 1.00 60.13 ? 95 PHE A CE1 1 ATOM 723 C CE2 . PHE A 1 95 ? 40.120 20.604 53.949 1.00 60.54 ? 95 PHE A CE2 1 ATOM 724 C CZ . PHE A 1 95 ? 40.555 19.336 53.656 1.00 58.89 ? 95 PHE A CZ 1 ATOM 725 N N . ASP A 1 96 ? 37.755 19.612 60.505 1.00 65.93 ? 96 ASP A N 1 ATOM 726 C CA . ASP A 1 96 ? 37.350 20.234 61.759 1.00 67.01 ? 96 ASP A CA 1 ATOM 727 C C . ASP A 1 96 ? 38.274 19.997 62.934 1.00 66.94 ? 96 ASP A C 1 ATOM 728 O O . ASP A 1 96 ? 38.633 18.860 63.230 1.00 67.28 ? 96 ASP A O 1 ATOM 729 C CB . ASP A 1 96 ? 35.897 19.892 62.080 1.00 70.63 ? 96 ASP A CB 1 ATOM 730 C CG . ASP A 1 96 ? 34.988 20.891 61.372 1.00 74.38 ? 96 ASP A CG 1 ATOM 731 O OD1 . ASP A 1 96 ? 35.475 21.803 60.656 1.00 77.15 ? 96 ASP A OD1 1 ATOM 732 O OD2 . ASP A 1 96 ? 33.772 20.708 61.565 1.00 75.59 ? 96 ASP A OD2 1 ATOM 733 N N . LEU A 1 97 ? 38.683 21.087 63.593 1.00 66.58 ? 97 LEU A N 1 ATOM 734 C CA . LEU A 1 97 ? 39.385 21.021 64.854 1.00 66.93 ? 97 LEU A CA 1 ATOM 735 C C . LEU A 1 97 ? 38.369 20.942 66.016 1.00 67.67 ? 97 LEU A C 1 ATOM 736 O O . LEU A 1 97 ? 37.135 21.050 65.976 1.00 66.66 ? 97 LEU A O 1 ATOM 737 C CB . LEU A 1 97 ? 40.487 22.032 65.143 1.00 66.11 ? 97 LEU A CB 1 ATOM 738 C CG . LEU A 1 97 ? 41.627 22.265 64.161 1.00 68.06 ? 97 LEU A CG 1 ATOM 739 C CD1 . LEU A 1 97 ? 41.075 22.386 62.717 1.00 70.02 ? 97 LEU A CD1 1 ATOM 740 C CD2 . LEU A 1 97 ? 42.415 23.567 64.227 1.00 66.91 ? 97 LEU A CD2 1 ATOM 741 N N . LYS A 1 98 ? 38.972 20.493 67.114 1.00 68.61 ? 98 LYS A N 1 ATOM 742 C CA . LYS A 1 98 ? 38.296 20.303 68.406 1.00 69.59 ? 98 LYS A CA 1 ATOM 743 C C . LYS A 1 98 ? 39.351 20.302 69.494 1.00 69.61 ? 98 LYS A C 1 ATOM 744 O O . LYS A 1 98 ? 40.517 19.965 69.268 1.00 69.92 ? 98 LYS A O 1 ATOM 745 C CB . LYS A 1 98 ? 37.450 19.063 68.261 1.00 73.26 ? 98 LYS A CB 1 ATOM 746 C CG . LYS A 1 98 ? 36.599 18.653 69.427 1.00 77.20 ? 98 LYS A CG 1 ATOM 747 C CD . LYS A 1 98 ? 37.425 17.858 70.430 1.00 80.86 ? 98 LYS A CD 1 ATOM 748 C CE . LYS A 1 98 ? 37.272 16.356 70.259 1.00 83.24 ? 98 LYS A CE 1 ATOM 749 N NZ . LYS A 1 98 ? 37.708 15.602 71.478 1.00 85.02 ? 98 LYS A NZ 1 ATOM 750 N N . GLU A 1 99 ? 39.071 20.815 70.681 1.00 70.18 ? 99 GLU A N 1 ATOM 751 C CA . GLU A 1 99 ? 40.092 20.959 71.714 1.00 70.17 ? 99 GLU A CA 1 ATOM 752 C C . GLU A 1 99 ? 40.515 19.633 72.316 1.00 69.78 ? 99 GLU A C 1 ATOM 753 O O . GLU A 1 99 ? 39.723 18.712 72.489 1.00 69.42 ? 99 GLU A O 1 ATOM 754 C CB . GLU A 1 99 ? 39.725 21.971 72.791 1.00 69.56 ? 99 GLU A CB 1 ATOM 755 C CG . GLU A 1 99 ? 38.567 21.583 73.678 1.00 70.68 ? 99 GLU A CG 1 ATOM 756 C CD . GLU A 1 99 ? 38.863 20.559 74.752 1.00 72.43 ? 99 GLU A CD 1 ATOM 757 O OE1 . GLU A 1 99 ? 39.967 20.464 75.334 1.00 71.60 ? 99 GLU A OE1 1 ATOM 758 O OE2 . GLU A 1 99 ? 37.937 19.749 75.005 1.00 74.77 ? 99 GLU A OE2 1 ATOM 759 N N . ILE A 1 100 ? 41.763 19.598 72.757 1.00 69.77 ? 100 ILE A N 1 ATOM 760 C CA . ILE A 1 100 ? 42.327 18.427 73.410 1.00 70.07 ? 100 ILE A CA 1 ATOM 761 C C . ILE A 1 100 ? 43.238 18.888 74.539 1.00 70.66 ? 100 ILE A C 1 ATOM 762 O O . ILE A 1 100 ? 44.414 18.593 74.629 1.00 70.87 ? 100 ILE A O 1 ATOM 763 C CB . ILE A 1 100 ? 43.040 17.452 72.469 1.00 68.19 ? 100 ILE A CB 1 ATOM 764 C CG1 . ILE A 1 100 ? 43.788 18.175 71.358 1.00 68.68 ? 100 ILE A CG1 1 ATOM 765 C CG2 . ILE A 1 100 ? 42.086 16.438 71.849 1.00 65.34 ? 100 ILE A CG2 1 ATOM 766 C CD1 . ILE A 1 100 ? 45.108 17.567 70.939 1.00 68.88 ? 100 ILE A CD1 1 ATOM 767 N N . ASN A 1 101 ? 42.645 19.588 75.496 1.00 71.57 ? 101 ASN A N 1 ATOM 768 C CA . ASN A 1 101 ? 43.320 20.089 76.677 1.00 72.14 ? 101 ASN A CA 1 ATOM 769 C C . ASN A 1 101 ? 43.793 19.010 77.625 1.00 71.75 ? 101 ASN A C 1 ATOM 770 O O . ASN A 1 101 ? 44.913 19.092 78.144 1.00 71.70 ? 101 ASN A O 1 ATOM 771 C CB . ASN A 1 101 ? 42.438 21.176 77.306 1.00 75.86 ? 101 ASN A CB 1 ATOM 772 C CG . ASN A 1 101 ? 43.075 22.532 77.020 1.00 79.80 ? 101 ASN A CG 1 ATOM 773 O OD1 . ASN A 1 101 ? 43.834 22.985 77.890 1.00 83.27 ? 101 ASN A OD1 1 ATOM 774 N ND2 . ASN A 1 101 ? 42.897 23.115 75.841 1.00 79.56 ? 101 ASN A ND2 1 ATOM 775 N N . ASP A 1 102 ? 43.176 17.837 77.664 1.00 71.43 ? 102 ASP A N 1 ATOM 776 C CA . ASP A 1 102 ? 43.656 16.687 78.393 1.00 71.54 ? 102 ASP A CA 1 ATOM 777 C C . ASP A 1 102 ? 45.007 16.165 77.894 1.00 71.17 ? 102 ASP A C 1 ATOM 778 O O . ASP A 1 102 ? 45.711 15.474 78.632 1.00 70.97 ? 102 ASP A O 1 ATOM 779 C CB . ASP A 1 102 ? 42.751 15.460 78.313 1.00 76.30 ? 102 ASP A CB 1 ATOM 780 C CG . ASP A 1 102 ? 41.285 15.768 78.098 1.00 81.68 ? 102 ASP A CG 1 ATOM 781 O OD1 . ASP A 1 102 ? 40.628 16.109 79.113 1.00 81.03 ? 102 ASP A OD1 1 ATOM 782 O OD2 . ASP A 1 102 ? 40.873 15.646 76.914 1.00 84.74 ? 102 ASP A OD2 1 ATOM 783 N N . ILE A 1 103 ? 45.336 16.367 76.623 1.00 70.36 ? 103 ILE A N 1 ATOM 784 C CA . ILE A 1 103 ? 46.635 15.926 76.129 1.00 69.02 ? 103 ILE A CA 1 ATOM 785 C C . ILE A 1 103 ? 47.654 17.017 76.390 1.00 68.31 ? 103 ILE A C 1 ATOM 786 O O . ILE A 1 103 ? 48.655 16.766 77.061 1.00 67.77 ? 103 ILE A O 1 ATOM 787 C CB . ILE A 1 103 ? 46.531 15.490 74.657 1.00 68.70 ? 103 ILE A CB 1 ATOM 788 C CG1 . ILE A 1 103 ? 45.389 14.460 74.601 1.00 67.58 ? 103 ILE A CG1 1 ATOM 789 C CG2 . ILE A 1 103 ? 47.836 14.911 74.153 1.00 65.18 ? 103 ILE A CG2 1 ATOM 790 C CD1 . ILE A 1 103 ? 45.080 13.866 73.261 1.00 67.67 ? 103 ILE A CD1 1 ATOM 791 N N . CYS A 1 104 ? 47.312 18.267 76.090 1.00 67.83 ? 104 CYS A N 1 ATOM 792 C CA . CYS A 1 104 ? 48.269 19.366 76.233 1.00 67.14 ? 104 CYS A CA 1 ATOM 793 C C . CYS A 1 104 ? 47.547 20.704 76.170 1.00 66.75 ? 104 CYS A C 1 ATOM 794 O O . CYS A 1 104 ? 46.751 20.930 75.263 1.00 67.28 ? 104 CYS A O 1 ATOM 795 C CB . CYS A 1 104 ? 49.436 19.343 75.236 1.00 62.32 ? 104 CYS A CB 1 ATOM 796 S SG . CYS A 1 104 ? 49.077 19.140 73.479 1.00 57.88 ? 104 CYS A SG 1 ATOM 797 N N . SER A 1 105 ? 48.021 21.654 76.957 1.00 66.82 ? 105 SER A N 1 ATOM 798 C CA . SER A 1 105 ? 47.416 22.965 77.064 1.00 66.21 ? 105 SER A CA 1 ATOM 799 C C . SER A 1 105 ? 47.412 23.739 75.749 1.00 64.87 ? 105 SER A C 1 ATOM 800 O O . SER A 1 105 ? 48.419 24.090 75.152 1.00 63.73 ? 105 SER A O 1 ATOM 801 C CB . SER A 1 105 ? 48.005 23.861 78.158 1.00 67.48 ? 105 SER A CB 1 ATOM 802 O OG . SER A 1 105 ? 48.881 24.852 77.622 1.00 69.67 ? 105 SER A OG 1 ATOM 803 N N . GLY A 1 106 ? 46.177 24.132 75.442 1.00 64.33 ? 106 GLY A N 1 ATOM 804 C CA . GLY A 1 106 ? 45.964 24.952 74.248 1.00 64.25 ? 106 GLY A CA 1 ATOM 805 C C . GLY A 1 106 ? 46.159 24.155 72.962 1.00 62.89 ? 106 GLY A C 1 ATOM 806 O O . GLY A 1 106 ? 46.821 24.667 72.072 1.00 63.22 ? 106 GLY A O 1 ATOM 807 N N . CYS A 1 107 ? 45.887 22.864 72.988 1.00 61.84 ? 107 CYS A N 1 ATOM 808 C CA . CYS A 1 107 ? 46.113 22.033 71.830 1.00 60.53 ? 107 CYS A CA 1 ATOM 809 C C . CYS A 1 107 ? 44.724 21.647 71.299 1.00 59.54 ? 107 CYS A C 1 ATOM 810 O O . CYS A 1 107 ? 43.768 21.399 72.017 1.00 58.02 ? 107 CYS A O 1 ATOM 811 C CB . CYS A 1 107 ? 46.980 20.809 72.044 1.00 58.19 ? 107 CYS A CB 1 ATOM 812 S SG . CYS A 1 107 ? 48.606 20.987 72.764 1.00 57.20 ? 107 CYS A SG 1 ATOM 813 N N . ARG A 1 108 ? 44.639 21.877 69.984 1.00 59.31 ? 108 ARG A N 1 ATOM 814 C CA . ARG A 1 108 ? 43.476 21.414 69.226 1.00 58.15 ? 108 ARG A CA 1 ATOM 815 C C . ARG A 1 108 ? 43.990 20.328 68.266 1.00 56.71 ? 108 ARG A C 1 ATOM 816 O O . ARG A 1 108 ? 45.131 20.455 67.825 1.00 56.18 ? 108 ARG A O 1 ATOM 817 C CB . ARG A 1 108 ? 42.802 22.560 68.494 1.00 56.76 ? 108 ARG A CB 1 ATOM 818 C CG . ARG A 1 108 ? 42.697 23.830 69.318 1.00 59.87 ? 108 ARG A CG 1 ATOM 819 C CD . ARG A 1 108 ? 41.844 24.892 68.626 1.00 61.15 ? 108 ARG A CD 1 ATOM 820 N NE . ARG A 1 108 ? 40.444 24.481 68.792 1.00 62.03 ? 108 ARG A NE 1 ATOM 821 C CZ . ARG A 1 108 ? 39.519 24.713 67.874 1.00 65.07 ? 108 ARG A CZ 1 ATOM 822 N NH1 . ARG A 1 108 ? 39.803 25.336 66.713 1.00 68.15 ? 108 ARG A NH1 1 ATOM 823 N NH2 . ARG A 1 108 ? 38.302 24.258 68.156 1.00 65.89 ? 108 ARG A NH2 1 ATOM 824 N N . GLY A 1 109 ? 43.223 19.262 68.092 1.00 55.06 ? 109 GLY A N 1 ATOM 825 C CA . GLY A 1 109 ? 43.562 18.254 67.114 1.00 54.61 ? 109 GLY A CA 1 ATOM 826 C C . GLY A 1 109 ? 42.368 17.789 66.273 1.00 53.97 ? 109 GLY A C 1 ATOM 827 O O . GLY A 1 109 ? 41.249 18.160 66.593 1.00 53.68 ? 109 GLY A O 1 ATOM 828 N N . HIS A 1 110 ? 42.606 17.147 65.142 1.00 53.20 ? 110 HIS A N 1 ATOM 829 C CA . HIS A 1 110 ? 41.578 16.616 64.292 1.00 53.05 ? 110 HIS A CA 1 ATOM 830 C C . HIS A 1 110 ? 40.559 15.871 65.174 1.00 53.22 ? 110 HIS A C 1 ATOM 831 O O . HIS A 1 110 ? 40.700 14.806 65.750 1.00 52.55 ? 110 HIS A O 1 ATOM 832 C CB . HIS A 1 110 ? 42.097 15.633 63.247 1.00 49.39 ? 110 HIS A CB 1 ATOM 833 C CG . HIS A 1 110 ? 41.115 15.243 62.197 1.00 48.01 ? 110 HIS A CG 1 ATOM 834 N ND1 . HIS A 1 110 ? 40.298 14.134 62.272 1.00 47.44 ? 110 HIS A ND1 1 ATOM 835 C CD2 . HIS A 1 110 ? 40.844 15.810 60.985 1.00 48.20 ? 110 HIS A CD2 1 ATOM 836 C CE1 . HIS A 1 110 ? 39.566 14.038 61.179 1.00 45.38 ? 110 HIS A CE1 1 ATOM 837 N NE2 . HIS A 1 110 ? 39.891 15.044 60.373 1.00 45.23 ? 110 HIS A NE2 1 ATOM 838 N N . ASP A 1 111 ? 39.406 16.517 65.062 1.00 53.10 ? 111 ASP A N 1 ATOM 839 C CA . ASP A 1 111 ? 38.246 16.128 65.808 1.00 53.86 ? 111 ASP A CA 1 ATOM 840 C C . ASP A 1 111 ? 37.980 14.653 65.655 1.00 53.69 ? 111 ASP A C 1 ATOM 841 O O . ASP A 1 111 ? 37.823 13.975 66.678 1.00 54.09 ? 111 ASP A O 1 ATOM 842 C CB . ASP A 1 111 ? 37.117 17.088 65.468 1.00 56.87 ? 111 ASP A CB 1 ATOM 843 C CG . ASP A 1 111 ? 35.835 16.780 66.173 1.00 58.61 ? 111 ASP A CG 1 ATOM 844 O OD1 . ASP A 1 111 ? 35.761 15.750 66.870 1.00 60.75 ? 111 ASP A OD1 1 ATOM 845 O OD2 . ASP A 1 111 ? 34.850 17.534 66.077 1.00 63.15 ? 111 ASP A OD2 1 ATOM 846 N N . GLY A 1 112 ? 37.934 14.045 64.472 1.00 53.82 ? 112 GLY A N 1 ATOM 847 C CA . GLY A 1 112 ? 37.756 12.616 64.260 1.00 52.67 ? 112 GLY A CA 1 ATOM 848 C C . GLY A 1 112 ? 38.889 11.740 64.768 1.00 52.86 ? 112 GLY A C 1 ATOM 849 O O . GLY A 1 112 ? 38.702 10.762 65.497 1.00 52.08 ? 112 GLY A O 1 ATOM 850 N N . PHE A 1 113 ? 40.146 12.166 64.540 1.00 52.77 ? 113 PHE A N 1 ATOM 851 C CA . PHE A 1 113 ? 41.292 11.350 64.962 1.00 52.52 ? 113 PHE A CA 1 ATOM 852 C C . PHE A 1 113 ? 41.241 11.274 66.474 1.00 53.40 ? 113 PHE A C 1 ATOM 853 O O . PHE A 1 113 ? 41.088 10.238 67.103 1.00 53.64 ? 113 PHE A O 1 ATOM 854 C CB . PHE A 1 113 ? 42.629 11.856 64.443 1.00 46.49 ? 113 PHE A CB 1 ATOM 855 C CG . PHE A 1 113 ? 42.721 12.072 62.936 1.00 41.11 ? 113 PHE A CG 1 ATOM 856 C CD1 . PHE A 1 113 ? 41.915 11.433 62.005 1.00 36.34 ? 113 PHE A CD1 1 ATOM 857 C CD2 . PHE A 1 113 ? 43.685 12.947 62.458 1.00 35.99 ? 113 PHE A CD2 1 ATOM 858 C CE1 . PHE A 1 113 ? 42.103 11.702 60.660 1.00 36.57 ? 113 PHE A CE1 1 ATOM 859 C CE2 . PHE A 1 113 ? 43.871 13.209 61.131 1.00 33.34 ? 113 PHE A CE2 1 ATOM 860 C CZ . PHE A 1 113 ? 43.042 12.618 60.204 1.00 33.22 ? 113 PHE A CZ 1 ATOM 861 N N . THR A 1 114 ? 41.108 12.466 67.016 1.00 54.53 ? 114 THR A N 1 ATOM 862 C CA . THR A 1 114 ? 40.949 12.732 68.438 1.00 55.05 ? 114 THR A CA 1 ATOM 863 C C . THR A 1 114 ? 39.766 12.023 69.054 1.00 55.45 ? 114 THR A C 1 ATOM 864 O O . THR A 1 114 ? 39.968 11.361 70.074 1.00 55.21 ? 114 THR A O 1 ATOM 865 C CB . THR A 1 114 ? 40.778 14.259 68.528 1.00 55.30 ? 114 THR A CB 1 ATOM 866 O OG1 . THR A 1 114 ? 42.066 14.843 68.286 1.00 56.46 ? 114 THR A OG1 1 ATOM 867 C CG2 . THR A 1 114 ? 40.186 14.691 69.830 1.00 59.22 ? 114 THR A CG2 1 ATOM 868 N N . SER A 1 115 ? 38.569 11.987 68.455 1.00 55.97 ? 115 SER A N 1 ATOM 869 C CA . SER A 1 115 ? 37.467 11.263 69.099 1.00 56.09 ? 115 SER A CA 1 ATOM 870 C C . SER A 1 115 ? 37.556 9.740 68.957 1.00 56.49 ? 115 SER A C 1 ATOM 871 O O . SER A 1 115 ? 36.940 9.077 69.794 1.00 56.09 ? 115 SER A O 1 ATOM 872 C CB . SER A 1 115 ? 36.084 11.654 68.585 1.00 53.43 ? 115 SER A CB 1 ATOM 873 O OG . SER A 1 115 ? 36.043 12.983 68.150 1.00 54.03 ? 115 SER A OG 1 ATOM 874 N N . SER A 1 116 ? 38.154 9.229 67.880 1.00 56.28 ? 116 SER A N 1 ATOM 875 C CA . SER A 1 116 ? 38.248 7.799 67.677 1.00 56.89 ? 116 SER A CA 1 ATOM 876 C C . SER A 1 116 ? 39.169 7.192 68.726 1.00 57.00 ? 116 SER A C 1 ATOM 877 O O . SER A 1 116 ? 38.801 6.166 69.278 1.00 57.36 ? 116 SER A O 1 ATOM 878 C CB . SER A 1 116 ? 38.835 7.362 66.317 1.00 59.21 ? 116 SER A CB 1 ATOM 879 O OG . SER A 1 116 ? 37.983 7.852 65.294 1.00 60.81 ? 116 SER A OG 1 ATOM 880 N N . TRP A 1 117 ? 40.322 7.832 68.903 1.00 56.83 ? 117 TRP A N 1 ATOM 881 C CA . TRP A 1 117 ? 41.290 7.320 69.858 1.00 56.95 ? 117 TRP A CA 1 ATOM 882 C C . TRP A 1 117 ? 40.672 7.453 71.245 1.00 57.46 ? 117 TRP A C 1 ATOM 883 O O . TRP A 1 117 ? 40.383 6.457 71.887 1.00 56.81 ? 117 TRP A O 1 ATOM 884 C CB . TRP A 1 117 ? 42.614 8.102 69.871 1.00 53.72 ? 117 TRP A CB 1 ATOM 885 C CG . TRP A 1 117 ? 43.369 7.781 71.134 1.00 52.98 ? 117 TRP A CG 1 ATOM 886 C CD1 . TRP A 1 117 ? 43.644 8.633 72.162 1.00 52.11 ? 117 TRP A CD1 1 ATOM 887 C CD2 . TRP A 1 117 ? 43.838 6.488 71.540 1.00 51.49 ? 117 TRP A CD2 1 ATOM 888 N NE1 . TRP A 1 117 ? 44.271 7.943 73.178 1.00 52.17 ? 117 TRP A NE1 1 ATOM 889 C CE2 . TRP A 1 117 ? 44.431 6.637 72.809 1.00 50.43 ? 117 TRP A CE2 1 ATOM 890 C CE3 . TRP A 1 117 ? 43.844 5.229 70.944 1.00 51.35 ? 117 TRP A CE3 1 ATOM 891 C CZ2 . TRP A 1 117 ? 45.036 5.584 73.476 1.00 51.40 ? 117 TRP A CZ2 1 ATOM 892 C CZ3 . TRP A 1 117 ? 44.416 4.159 71.627 1.00 51.39 ? 117 TRP A CZ3 1 ATOM 893 C CH2 . TRP A 1 117 ? 45.011 4.341 72.887 1.00 51.50 ? 117 TRP A CH2 1 ATOM 894 N N . ARG A 1 118 ? 40.135 8.647 71.507 1.00 58.43 ? 118 ARG A N 1 ATOM 895 C CA . ARG A 1 118 ? 39.535 8.960 72.793 1.00 59.59 ? 118 ARG A CA 1 ATOM 896 C C . ARG A 1 118 ? 38.558 7.873 73.225 1.00 59.58 ? 118 ARG A C 1 ATOM 897 O O . ARG A 1 118 ? 38.490 7.549 74.412 1.00 59.73 ? 118 ARG A O 1 ATOM 898 C CB . ARG A 1 118 ? 38.875 10.335 72.840 1.00 62.99 ? 118 ARG A CB 1 ATOM 899 C CG . ARG A 1 118 ? 37.988 10.640 74.023 1.00 66.79 ? 118 ARG A CG 1 ATOM 900 C CD . ARG A 1 118 ? 38.662 10.981 75.328 1.00 70.78 ? 118 ARG A CD 1 ATOM 901 N NE . ARG A 1 118 ? 39.823 10.183 75.704 1.00 74.17 ? 118 ARG A NE 1 ATOM 902 C CZ . ARG A 1 118 ? 41.078 10.476 75.348 1.00 75.72 ? 118 ARG A CZ 1 ATOM 903 N NH1 . ARG A 1 118 ? 41.366 11.534 74.603 1.00 75.08 ? 118 ARG A NH1 1 ATOM 904 N NH2 . ARG A 1 118 ? 42.079 9.684 75.721 1.00 78.86 ? 118 ARG A NH2 1 ATOM 905 N N . SER A 1 119 ? 37.888 7.277 72.261 1.00 59.04 ? 119 SER A N 1 ATOM 906 C CA . SER A 1 119 ? 36.907 6.243 72.419 1.00 58.83 ? 119 SER A CA 1 ATOM 907 C C . SER A 1 119 ? 37.433 4.850 72.665 1.00 58.68 ? 119 SER A C 1 ATOM 908 O O . SER A 1 119 ? 36.615 4.019 73.093 1.00 59.68 ? 119 SER A O 1 ATOM 909 C CB . SER A 1 119 ? 36.062 6.240 71.128 1.00 59.11 ? 119 SER A CB 1 ATOM 910 O OG . SER A 1 119 ? 35.335 5.037 71.024 1.00 61.54 ? 119 SER A OG 1 ATOM 911 N N . VAL A 1 120 ? 38.688 4.550 72.331 1.00 57.87 ? 120 VAL A N 1 ATOM 912 C CA . VAL A 1 120 ? 39.235 3.213 72.567 1.00 56.32 ? 120 VAL A CA 1 ATOM 913 C C . VAL A 1 120 ? 40.384 3.326 73.567 1.00 55.74 ? 120 VAL A C 1 ATOM 914 O O . VAL A 1 120 ? 40.956 2.328 73.999 1.00 55.65 ? 120 VAL A O 1 ATOM 915 C CB . VAL A 1 120 ? 39.780 2.459 71.337 1.00 54.34 ? 120 VAL A CB 1 ATOM 916 C CG1 . VAL A 1 120 ? 38.693 2.154 70.328 1.00 53.24 ? 120 VAL A CG1 1 ATOM 917 C CG2 . VAL A 1 120 ? 40.920 3.223 70.670 1.00 50.76 ? 120 VAL A CG2 1 ATOM 918 N N . ALA A 1 121 ? 40.690 4.554 73.945 1.00 55.71 ? 121 ALA A N 1 ATOM 919 C CA . ALA A 1 121 ? 41.788 4.843 74.855 1.00 56.13 ? 121 ALA A CA 1 ATOM 920 C C . ALA A 1 121 ? 41.815 3.962 76.080 1.00 55.99 ? 121 ALA A C 1 ATOM 921 O O . ALA A 1 121 ? 42.849 3.335 76.288 1.00 57.05 ? 121 ALA A O 1 ATOM 922 C CB . ALA A 1 121 ? 41.816 6.305 75.283 1.00 55.84 ? 121 ALA A CB 1 ATOM 923 N N . ASP A 1 122 ? 40.753 3.879 76.849 1.00 56.21 ? 122 ASP A N 1 ATOM 924 C CA . ASP A 1 122 ? 40.759 3.057 78.054 1.00 56.37 ? 122 ASP A CA 1 ATOM 925 C C . ASP A 1 122 ? 40.931 1.579 77.794 1.00 56.44 ? 122 ASP A C 1 ATOM 926 O O . ASP A 1 122 ? 41.800 1.031 78.478 1.00 56.38 ? 122 ASP A O 1 ATOM 927 C CB . ASP A 1 122 ? 39.568 3.347 78.958 1.00 56.93 ? 122 ASP A CB 1 ATOM 928 C CG . ASP A 1 122 ? 39.536 4.799 79.408 1.00 57.76 ? 122 ASP A CG 1 ATOM 929 O OD1 . ASP A 1 122 ? 40.604 5.444 79.541 1.00 60.37 ? 122 ASP A OD1 1 ATOM 930 O OD2 . ASP A 1 122 ? 38.423 5.310 79.635 1.00 57.60 ? 122 ASP A OD2 1 ATOM 931 N N . THR A 1 123 ? 40.237 0.931 76.859 1.00 56.67 ? 123 THR A N 1 ATOM 932 C CA . THR A 1 123 ? 40.583 -0.481 76.636 1.00 57.10 ? 123 THR A CA 1 ATOM 933 C C . THR A 1 123 ? 42.032 -0.591 76.176 1.00 57.17 ? 123 THR A C 1 ATOM 934 O O . THR A 1 123 ? 42.824 -1.216 76.854 1.00 57.28 ? 123 THR A O 1 ATOM 935 C CB . THR A 1 123 ? 39.652 -1.209 75.659 1.00 56.92 ? 123 THR A CB 1 ATOM 936 O OG1 . THR A 1 123 ? 38.370 -1.347 76.310 1.00 59.07 ? 123 THR A OG1 1 ATOM 937 C CG2 . THR A 1 123 ? 40.136 -2.606 75.297 1.00 53.02 ? 123 THR A CG2 1 ATOM 938 N N . LEU A 1 124 ? 42.453 0.105 75.118 1.00 57.36 ? 124 LEU A N 1 ATOM 939 C CA . LEU A 1 124 ? 43.829 -0.036 74.667 1.00 56.89 ? 124 LEU A CA 1 ATOM 940 C C . LEU A 1 124 ? 44.836 0.367 75.725 1.00 56.49 ? 124 LEU A C 1 ATOM 941 O O . LEU A 1 124 ? 45.770 -0.422 75.937 1.00 55.78 ? 124 LEU A O 1 ATOM 942 C CB . LEU A 1 124 ? 44.050 0.491 73.243 1.00 51.57 ? 124 LEU A CB 1 ATOM 943 C CG . LEU A 1 124 ? 43.151 -0.161 72.191 1.00 50.02 ? 124 LEU A CG 1 ATOM 944 C CD1 . LEU A 1 124 ? 43.146 0.625 70.887 1.00 49.00 ? 124 LEU A CD1 1 ATOM 945 C CD2 . LEU A 1 124 ? 43.475 -1.624 71.900 1.00 47.05 ? 124 LEU A CD2 1 ATOM 946 N N . ARG A 1 125 ? 44.659 1.439 76.484 1.00 56.52 ? 125 ARG A N 1 ATOM 947 C CA . ARG A 1 125 ? 45.622 1.855 77.521 1.00 56.98 ? 125 ARG A CA 1 ATOM 948 C C . ARG A 1 125 ? 45.831 0.719 78.527 1.00 56.17 ? 125 ARG A C 1 ATOM 949 O O . ARG A 1 125 ? 46.908 0.227 78.846 1.00 55.09 ? 125 ARG A O 1 ATOM 950 C CB . ARG A 1 125 ? 45.101 3.090 78.232 1.00 61.31 ? 125 ARG A CB 1 ATOM 951 C CG . ARG A 1 125 ? 45.941 3.763 79.297 1.00 69.18 ? 125 ARG A CG 1 ATOM 952 C CD . ARG A 1 125 ? 45.209 4.925 79.945 1.00 75.65 ? 125 ARG A CD 1 ATOM 953 N NE . ARG A 1 125 ? 45.825 5.795 80.918 1.00 83.22 ? 125 ARG A NE 1 ATOM 954 C CZ . ARG A 1 125 ? 46.726 5.579 81.879 1.00 88.08 ? 125 ARG A CZ 1 ATOM 955 N NH1 . ARG A 1 125 ? 47.198 4.323 81.983 1.00 90.48 ? 125 ARG A NH1 1 ATOM 956 N NH2 . ARG A 1 125 ? 47.187 6.483 82.771 1.00 89.34 ? 125 ARG A NH2 1 ATOM 957 N N . GLN A 1 126 ? 44.690 0.116 78.884 1.00 55.82 ? 126 GLN A N 1 ATOM 958 C CA . GLN A 1 126 ? 44.673 -1.041 79.751 1.00 55.41 ? 126 GLN A CA 1 ATOM 959 C C . GLN A 1 126 ? 45.523 -2.171 79.193 1.00 53.79 ? 126 GLN A C 1 ATOM 960 O O . GLN A 1 126 ? 46.394 -2.715 79.890 1.00 53.03 ? 126 GLN A O 1 ATOM 961 C CB . GLN A 1 126 ? 43.263 -1.477 80.120 1.00 59.76 ? 126 GLN A CB 1 ATOM 962 C CG . GLN A 1 126 ? 43.160 -2.904 80.629 1.00 65.48 ? 126 GLN A CG 1 ATOM 963 C CD . GLN A 1 126 ? 42.667 -3.909 79.595 1.00 69.35 ? 126 GLN A CD 1 ATOM 964 O OE1 . GLN A 1 126 ? 42.179 -3.504 78.526 1.00 67.50 ? 126 GLN A OE1 1 ATOM 965 N NE2 . GLN A 1 126 ? 42.763 -5.209 79.946 1.00 69.76 ? 126 GLN A NE2 1 ATOM 966 N N . LYS A 1 127 ? 45.271 -2.539 77.939 1.00 52.44 ? 127 LYS A N 1 ATOM 967 C CA . LYS A 1 127 ? 45.970 -3.669 77.336 1.00 50.64 ? 127 LYS A CA 1 ATOM 968 C C . LYS A 1 127 ? 47.456 -3.471 77.207 1.00 50.55 ? 127 LYS A C 1 ATOM 969 O O . LYS A 1 127 ? 48.242 -4.340 77.594 1.00 50.66 ? 127 LYS A O 1 ATOM 970 C CB . LYS A 1 127 ? 45.243 -4.039 76.052 1.00 49.55 ? 127 LYS A CB 1 ATOM 971 C CG . LYS A 1 127 ? 44.105 -4.964 76.443 1.00 48.52 ? 127 LYS A CG 1 ATOM 972 C CD . LYS A 1 127 ? 42.950 -4.992 75.479 1.00 48.30 ? 127 LYS A CD 1 ATOM 973 C CE . LYS A 1 127 ? 41.928 -6.045 75.917 1.00 48.89 ? 127 LYS A CE 1 ATOM 974 N NZ . LYS A 1 127 ? 42.556 -7.345 76.287 1.00 48.35 ? 127 LYS A NZ 1 ATOM 975 N N . VAL A 1 128 ? 47.881 -2.238 76.941 1.00 49.99 ? 128 VAL A N 1 ATOM 976 C CA . VAL A 1 128 ? 49.259 -1.836 76.904 1.00 49.31 ? 128 VAL A CA 1 ATOM 977 C C . VAL A 1 128 ? 49.853 -1.926 78.296 1.00 50.24 ? 128 VAL A C 1 ATOM 978 O O . VAL A 1 128 ? 51.001 -2.328 78.483 1.00 49.82 ? 128 VAL A O 1 ATOM 979 C CB . VAL A 1 128 ? 49.412 -0.420 76.327 1.00 45.76 ? 128 VAL A CB 1 ATOM 980 C CG1 . VAL A 1 128 ? 50.862 0.084 76.345 1.00 40.99 ? 128 VAL A CG1 1 ATOM 981 C CG2 . VAL A 1 128 ? 48.953 -0.487 74.883 1.00 45.05 ? 128 VAL A CG2 1 ATOM 982 N N . GLU A 1 129 ? 49.055 -1.574 79.303 1.00 51.37 ? 129 GLU A N 1 ATOM 983 C CA . GLU A 1 129 ? 49.553 -1.683 80.669 1.00 52.23 ? 129 GLU A CA 1 ATOM 984 C C . GLU A 1 129 ? 49.841 -3.100 81.090 1.00 52.92 ? 129 GLU A C 1 ATOM 985 O O . GLU A 1 129 ? 50.918 -3.370 81.636 1.00 53.17 ? 129 GLU A O 1 ATOM 986 C CB . GLU A 1 129 ? 48.613 -0.987 81.642 1.00 52.42 ? 129 GLU A CB 1 ATOM 987 C CG . GLU A 1 129 ? 49.209 0.374 81.834 1.00 53.15 ? 129 GLU A CG 1 ATOM 988 C CD . GLU A 1 129 ? 48.358 1.604 82.060 1.00 54.01 ? 129 GLU A CD 1 ATOM 989 O OE1 . GLU A 1 129 ? 47.303 1.306 82.623 1.00 50.06 ? 129 GLU A OE1 1 ATOM 990 O OE2 . GLU A 1 129 ? 49.005 2.619 81.580 1.00 57.16 ? 129 GLU A OE2 1 ATOM 991 N N . ASP A 1 130 ? 48.970 -4.045 80.758 1.00 53.57 ? 130 ASP A N 1 ATOM 992 C CA . ASP A 1 130 ? 49.283 -5.401 81.191 1.00 54.53 ? 130 ASP A CA 1 ATOM 993 C C . ASP A 1 130 ? 50.539 -5.883 80.504 1.00 54.60 ? 130 ASP A C 1 ATOM 994 O O . ASP A 1 130 ? 51.245 -6.616 81.188 1.00 55.66 ? 130 ASP A O 1 ATOM 995 C CB . ASP A 1 130 ? 48.124 -6.345 80.956 1.00 56.66 ? 130 ASP A CB 1 ATOM 996 C CG . ASP A 1 130 ? 46.846 -5.810 81.554 1.00 58.59 ? 130 ASP A CG 1 ATOM 997 O OD1 . ASP A 1 130 ? 46.849 -5.056 82.558 1.00 60.68 ? 130 ASP A OD1 1 ATOM 998 O OD2 . ASP A 1 130 ? 45.813 -6.181 80.955 1.00 62.23 ? 130 ASP A OD2 1 ATOM 999 N N . ALA A 1 131 ? 50.793 -5.553 79.258 1.00 54.11 ? 131 ALA A N 1 ATOM 1000 C CA . ALA A 1 131 ? 51.978 -6.000 78.541 1.00 53.04 ? 131 ALA A CA 1 ATOM 1001 C C . ALA A 1 131 ? 53.231 -5.429 79.192 1.00 51.89 ? 131 ALA A C 1 ATOM 1002 O O . ALA A 1 131 ? 54.220 -6.121 79.441 1.00 51.38 ? 131 ALA A O 1 ATOM 1003 C CB . ALA A 1 131 ? 51.866 -5.607 77.067 1.00 50.32 ? 131 ALA A CB 1 ATOM 1004 N N . VAL A 1 132 ? 53.186 -4.140 79.493 1.00 51.28 ? 132 VAL A N 1 ATOM 1005 C CA . VAL A 1 132 ? 54.299 -3.514 80.212 1.00 52.33 ? 132 VAL A CA 1 ATOM 1006 C C . VAL A 1 132 ? 54.604 -4.301 81.493 1.00 53.44 ? 132 VAL A C 1 ATOM 1007 O O . VAL A 1 132 ? 55.775 -4.600 81.700 1.00 52.62 ? 132 VAL A O 1 ATOM 1008 C CB . VAL A 1 132 ? 53.946 -2.048 80.418 1.00 49.06 ? 132 VAL A CB 1 ATOM 1009 C CG1 . VAL A 1 132 ? 54.927 -1.337 81.322 1.00 49.82 ? 132 VAL A CG1 1 ATOM 1010 C CG2 . VAL A 1 132 ? 53.960 -1.299 79.087 1.00 47.54 ? 132 VAL A CG2 1 ATOM 1011 N N . ARG A 1 133 ? 53.572 -4.658 82.280 1.00 54.59 ? 133 ARG A N 1 ATOM 1012 C CA . ARG A 1 133 ? 53.751 -5.410 83.460 1.00 55.50 ? 133 ARG A CA 1 ATOM 1013 C C . ARG A 1 133 ? 54.511 -6.691 83.214 1.00 56.36 ? 133 ARG A C 1 ATOM 1014 O O . ARG A 1 133 ? 55.505 -7.021 83.843 1.00 56.13 ? 133 ARG A O 1 ATOM 1015 C CB . ARG A 1 133 ? 52.449 -5.731 84.171 1.00 58.22 ? 133 ARG A CB 1 ATOM 1016 C CG . ARG A 1 133 ? 52.719 -6.293 85.575 1.00 56.85 ? 133 ARG A CG 1 ATOM 1017 C CD . ARG A 1 133 ? 51.386 -6.615 86.197 1.00 59.47 ? 133 ARG A CD 1 ATOM 1018 N NE . ARG A 1 133 ? 50.867 -7.941 85.823 1.00 64.13 ? 133 ARG A NE 1 ATOM 1019 C CZ . ARG A 1 133 ? 49.720 -8.018 85.130 1.00 67.18 ? 133 ARG A CZ 1 ATOM 1020 N NH1 . ARG A 1 133 ? 49.066 -6.894 84.812 1.00 66.91 ? 133 ARG A NH1 1 ATOM 1021 N NH2 . ARG A 1 133 ? 49.236 -9.203 84.800 1.00 68.98 ? 133 ARG A NH2 1 ATOM 1022 N N . GLU A 1 134 ? 53.922 -7.559 82.408 1.00 57.87 ? 134 GLU A N 1 ATOM 1023 C CA . GLU A 1 134 ? 54.488 -8.836 82.009 1.00 58.48 ? 134 GLU A CA 1 ATOM 1024 C C . GLU A 1 134 ? 55.898 -8.681 81.470 1.00 58.42 ? 134 GLU A C 1 ATOM 1025 O O . GLU A 1 134 ? 56.517 -9.715 81.161 1.00 59.48 ? 134 GLU A O 1 ATOM 1026 C CB . GLU A 1 134 ? 53.664 -9.487 80.932 1.00 63.45 ? 134 GLU A CB 1 ATOM 1027 C CG . GLU A 1 134 ? 52.658 -10.578 81.167 1.00 69.96 ? 134 GLU A CG 1 ATOM 1028 C CD . GLU A 1 134 ? 51.301 -10.162 81.668 1.00 72.94 ? 134 GLU A CD 1 ATOM 1029 O OE1 . GLU A 1 134 ? 50.845 -9.042 81.368 1.00 75.28 ? 134 GLU A OE1 1 ATOM 1030 O OE2 . GLU A 1 134 ? 50.595 -10.895 82.405 1.00 75.60 ? 134 GLU A OE2 1 ATOM 1031 N N . HIS A 1 135 ? 56.283 -7.621 80.773 1.00 57.83 ? 135 HIS A N 1 ATOM 1032 C CA . HIS A 1 135 ? 57.564 -7.450 80.120 1.00 57.07 ? 135 HIS A CA 1 ATOM 1033 C C . HIS A 1 135 ? 58.140 -6.053 80.305 1.00 57.13 ? 135 HIS A C 1 ATOM 1034 O O . HIS A 1 135 ? 58.369 -5.251 79.408 1.00 57.69 ? 135 HIS A O 1 ATOM 1035 C CB . HIS A 1 135 ? 57.463 -7.710 78.599 1.00 51.72 ? 135 HIS A CB 1 ATOM 1036 C CG . HIS A 1 135 ? 56.741 -8.975 78.264 1.00 51.77 ? 135 HIS A CG 1 ATOM 1037 N ND1 . HIS A 1 135 ? 57.326 -10.226 78.269 1.00 49.65 ? 135 HIS A ND1 1 ATOM 1038 C CD2 . HIS A 1 135 ? 55.409 -9.149 78.005 1.00 50.55 ? 135 HIS A CD2 1 ATOM 1039 C CE1 . HIS A 1 135 ? 56.377 -11.102 77.988 1.00 50.38 ? 135 HIS A CE1 1 ATOM 1040 N NE2 . HIS A 1 135 ? 55.207 -10.497 77.850 1.00 48.68 ? 135 HIS A NE2 1 ATOM 1041 N N . PRO A 1 136 ? 58.591 -5.730 81.503 1.00 56.93 ? 136 PRO A N 1 ATOM 1042 C CA . PRO A 1 136 ? 59.034 -4.416 81.920 1.00 56.33 ? 136 PRO A CA 1 ATOM 1043 C C . PRO A 1 136 ? 60.213 -3.881 81.107 1.00 55.38 ? 136 PRO A C 1 ATOM 1044 O O . PRO A 1 136 ? 60.446 -2.688 80.929 1.00 53.62 ? 136 PRO A O 1 ATOM 1045 C CB . PRO A 1 136 ? 59.408 -4.616 83.407 1.00 56.05 ? 136 PRO A CB 1 ATOM 1046 C CG . PRO A 1 136 ? 59.589 -6.086 83.583 1.00 55.92 ? 136 PRO A CG 1 ATOM 1047 C CD . PRO A 1 136 ? 58.555 -6.693 82.676 1.00 56.71 ? 136 PRO A CD 1 ATOM 1048 N N . ASP A 1 137 ? 61.010 -4.844 80.694 1.00 54.76 ? 137 ASP A N 1 ATOM 1049 C CA . ASP A 1 137 ? 62.225 -4.659 79.933 1.00 55.25 ? 137 ASP A CA 1 ATOM 1050 C C . ASP A 1 137 ? 61.957 -4.351 78.461 1.00 54.03 ? 137 ASP A C 1 ATOM 1051 O O . ASP A 1 137 ? 62.690 -3.573 77.856 1.00 54.22 ? 137 ASP A O 1 ATOM 1052 C CB . ASP A 1 137 ? 63.105 -5.904 80.153 1.00 57.61 ? 137 ASP A CB 1 ATOM 1053 C CG . ASP A 1 137 ? 62.447 -7.206 79.701 1.00 62.20 ? 137 ASP A CG 1 ATOM 1054 O OD1 . ASP A 1 137 ? 61.200 -7.414 79.761 1.00 57.57 ? 137 ASP A OD1 1 ATOM 1055 O OD2 . ASP A 1 137 ? 63.218 -8.118 79.260 1.00 65.75 ? 137 ASP A OD2 1 ATOM 1056 N N . TYR A 1 138 ? 60.772 -4.623 77.937 1.00 52.80 ? 138 TYR A N 1 ATOM 1057 C CA . TYR A 1 138 ? 60.462 -4.512 76.518 1.00 51.55 ? 138 TYR A CA 1 ATOM 1058 C C . TYR A 1 138 ? 60.155 -3.081 76.108 1.00 50.48 ? 138 TYR A C 1 ATOM 1059 O O . TYR A 1 138 ? 59.486 -2.388 76.856 1.00 50.64 ? 138 TYR A O 1 ATOM 1060 C CB . TYR A 1 138 ? 59.283 -5.422 76.151 1.00 49.90 ? 138 TYR A CB 1 ATOM 1061 C CG . TYR A 1 138 ? 59.594 -6.884 75.954 1.00 47.56 ? 138 TYR A CG 1 ATOM 1062 C CD1 . TYR A 1 138 ? 60.732 -7.507 76.441 1.00 46.89 ? 138 TYR A CD1 1 ATOM 1063 C CD2 . TYR A 1 138 ? 58.696 -7.667 75.235 1.00 46.66 ? 138 TYR A CD2 1 ATOM 1064 C CE1 . TYR A 1 138 ? 60.978 -8.860 76.215 1.00 46.05 ? 138 TYR A CE1 1 ATOM 1065 C CE2 . TYR A 1 138 ? 58.901 -9.011 75.004 1.00 45.52 ? 138 TYR A CE2 1 ATOM 1066 C CZ . TYR A 1 138 ? 60.045 -9.598 75.508 1.00 45.48 ? 138 TYR A CZ 1 ATOM 1067 O OH . TYR A 1 138 ? 60.244 -10.929 75.258 1.00 44.12 ? 138 TYR A OH 1 ATOM 1068 N N . ARG A 1 139 ? 60.497 -2.692 74.900 1.00 49.41 ? 139 ARG A N 1 ATOM 1069 C CA . ARG A 1 139 ? 60.195 -1.361 74.379 1.00 48.07 ? 139 ARG A CA 1 ATOM 1070 C C . ARG A 1 139 ? 58.763 -1.257 73.854 1.00 47.50 ? 139 ARG A C 1 ATOM 1071 O O . ARG A 1 139 ? 58.243 -2.174 73.200 1.00 48.49 ? 139 ARG A O 1 ATOM 1072 C CB . ARG A 1 139 ? 61.207 -1.034 73.312 1.00 45.77 ? 139 ARG A CB 1 ATOM 1073 C CG . ARG A 1 139 ? 61.275 0.338 72.710 1.00 46.45 ? 139 ARG A CG 1 ATOM 1074 C CD . ARG A 1 139 ? 61.583 0.232 71.203 1.00 46.21 ? 139 ARG A CD 1 ATOM 1075 N NE . ARG A 1 139 ? 61.910 1.496 70.599 1.00 44.62 ? 139 ARG A NE 1 ATOM 1076 C CZ . ARG A 1 139 ? 62.513 1.693 69.452 1.00 47.60 ? 139 ARG A CZ 1 ATOM 1077 N NH1 . ARG A 1 139 ? 62.883 0.734 68.616 1.00 49.97 ? 139 ARG A NH1 1 ATOM 1078 N NH2 . ARG A 1 139 ? 62.831 2.920 69.060 1.00 49.09 ? 139 ARG A NH2 1 ATOM 1079 N N . VAL A 1 140 ? 58.072 -0.199 74.249 1.00 45.40 ? 140 VAL A N 1 ATOM 1080 C CA . VAL A 1 140 ? 56.723 0.089 73.898 1.00 44.28 ? 140 VAL A CA 1 ATOM 1081 C C . VAL A 1 140 ? 56.706 1.062 72.721 1.00 44.33 ? 140 VAL A C 1 ATOM 1082 O O . VAL A 1 140 ? 57.244 2.168 72.738 1.00 43.90 ? 140 VAL A O 1 ATOM 1083 C CB . VAL A 1 140 ? 55.824 0.664 75.002 1.00 45.08 ? 140 VAL A CB 1 ATOM 1084 C CG1 . VAL A 1 140 ? 54.424 1.025 74.496 1.00 40.19 ? 140 VAL A CG1 1 ATOM 1085 C CG2 . VAL A 1 140 ? 55.714 -0.341 76.151 1.00 43.61 ? 140 VAL A CG2 1 ATOM 1086 N N . VAL A 1 141 ? 56.089 0.530 71.650 1.00 43.50 ? 141 VAL A N 1 ATOM 1087 C CA . VAL A 1 141 ? 56.109 1.195 70.356 1.00 41.66 ? 141 VAL A CA 1 ATOM 1088 C C . VAL A 1 141 ? 54.728 1.232 69.718 1.00 40.98 ? 141 VAL A C 1 ATOM 1089 O O . VAL A 1 141 ? 54.030 0.219 69.593 1.00 40.58 ? 141 VAL A O 1 ATOM 1090 C CB . VAL A 1 141 ? 57.059 0.397 69.446 1.00 40.71 ? 141 VAL A CB 1 ATOM 1091 C CG1 . VAL A 1 141 ? 56.979 0.899 68.015 1.00 43.00 ? 141 VAL A CG1 1 ATOM 1092 C CG2 . VAL A 1 141 ? 58.512 0.521 69.903 1.00 40.28 ? 141 VAL A CG2 1 ATOM 1093 N N . PHE A 1 142 ? 54.287 2.447 69.388 1.00 39.56 ? 142 PHE A N 1 ATOM 1094 C CA . PHE A 1 142 ? 53.048 2.606 68.649 1.00 38.47 ? 142 PHE A CA 1 ATOM 1095 C C . PHE A 1 142 ? 53.412 2.943 67.196 1.00 38.29 ? 142 PHE A C 1 ATOM 1096 O O . PHE A 1 142 ? 54.263 3.781 66.937 1.00 38.11 ? 142 PHE A O 1 ATOM 1097 C CB . PHE A 1 142 ? 52.182 3.692 69.230 1.00 39.45 ? 142 PHE A CB 1 ATOM 1098 C CG . PHE A 1 142 ? 51.615 3.524 70.603 1.00 39.18 ? 142 PHE A CG 1 ATOM 1099 C CD1 . PHE A 1 142 ? 51.825 2.417 71.391 1.00 38.24 ? 142 PHE A CD1 1 ATOM 1100 C CD2 . PHE A 1 142 ? 50.837 4.545 71.134 1.00 39.04 ? 142 PHE A CD2 1 ATOM 1101 C CE1 . PHE A 1 142 ? 51.326 2.324 72.658 1.00 37.18 ? 142 PHE A CE1 1 ATOM 1102 C CE2 . PHE A 1 142 ? 50.313 4.469 72.396 1.00 36.78 ? 142 PHE A CE2 1 ATOM 1103 C CZ . PHE A 1 142 ? 50.543 3.343 73.156 1.00 37.82 ? 142 PHE A CZ 1 ATOM 1104 N N . THR A 1 143 ? 52.630 2.472 66.251 1.00 37.50 ? 143 THR A N 1 ATOM 1105 C CA . THR A 1 143 ? 52.921 2.612 64.845 1.00 36.68 ? 143 THR A CA 1 ATOM 1106 C C . THR A 1 143 ? 51.650 2.486 64.005 1.00 36.37 ? 143 THR A C 1 ATOM 1107 O O . THR A 1 143 ? 50.604 2.018 64.401 1.00 35.36 ? 143 THR A O 1 ATOM 1108 C CB . THR A 1 143 ? 53.852 1.473 64.406 1.00 37.95 ? 143 THR A CB 1 ATOM 1109 O OG1 . THR A 1 143 ? 54.297 1.804 63.066 1.00 40.20 ? 143 THR A OG1 1 ATOM 1110 C CG2 . THR A 1 143 ? 53.127 0.129 64.335 1.00 36.34 ? 143 THR A CG2 1 ATOM 1111 N N . GLY A 1 144 ? 51.687 3.094 62.825 1.00 36.99 ? 144 GLY A N 1 ATOM 1112 C CA . GLY A 1 144 ? 50.595 2.983 61.864 1.00 36.67 ? 144 GLY A CA 1 ATOM 1113 C C . GLY A 1 144 ? 50.973 3.779 60.614 1.00 37.09 ? 144 GLY A C 1 ATOM 1114 O O . GLY A 1 144 ? 51.723 4.757 60.574 1.00 36.10 ? 144 GLY A O 1 ATOM 1115 N N . HIS A 1 145 ? 50.235 3.395 59.580 1.00 37.45 ? 145 HIS A N 1 ATOM 1116 C CA . HIS A 1 145 ? 50.354 4.044 58.266 1.00 36.47 ? 145 HIS A CA 1 ATOM 1117 C C . HIS A 1 145 ? 49.091 4.872 58.047 1.00 36.33 ? 145 HIS A C 1 ATOM 1118 O O . HIS A 1 145 ? 48.025 4.435 58.509 1.00 35.83 ? 145 HIS A O 1 ATOM 1119 C CB . HIS A 1 145 ? 50.384 2.879 57.258 1.00 35.33 ? 145 HIS A CB 1 ATOM 1120 C CG . HIS A 1 145 ? 50.102 3.299 55.855 1.00 32.28 ? 145 HIS A CG 1 ATOM 1121 N ND1 . HIS A 1 145 ? 48.879 3.214 55.256 1.00 31.14 ? 145 HIS A ND1 1 ATOM 1122 C CD2 . HIS A 1 145 ? 51.003 3.897 55.003 1.00 30.65 ? 145 HIS A CD2 1 ATOM 1123 C CE1 . HIS A 1 145 ? 49.034 3.728 53.997 1.00 29.71 ? 145 HIS A CE1 1 ATOM 1124 N NE2 . HIS A 1 145 ? 50.273 4.153 53.862 1.00 32.64 ? 145 HIS A NE2 1 ATOM 1125 N N . SER A 1 146 ? 49.218 6.026 57.415 1.00 35.93 ? 146 SER A N 1 ATOM 1126 C CA . SER A 1 146 ? 48.015 6.774 57.046 1.00 38.21 ? 146 SER A CA 1 ATOM 1127 C C . SER A 1 146 ? 47.176 7.261 58.222 1.00 38.40 ? 146 SER A C 1 ATOM 1128 O O . SER A 1 146 ? 47.709 7.488 59.296 1.00 39.13 ? 146 SER A O 1 ATOM 1129 C CB . SER A 1 146 ? 47.107 5.920 56.105 1.00 36.24 ? 146 SER A CB 1 ATOM 1130 O OG . SER A 1 146 ? 46.406 6.860 55.299 1.00 39.14 ? 146 SER A OG 1 ATOM 1131 N N . LEU A 1 147 ? 45.867 7.105 58.166 1.00 38.33 ? 147 LEU A N 1 ATOM 1132 C CA . LEU A 1 147 ? 44.967 7.320 59.276 1.00 39.15 ? 147 LEU A CA 1 ATOM 1133 C C . LEU A 1 147 ? 45.447 6.639 60.557 1.00 38.95 ? 147 LEU A C 1 ATOM 1134 O O . LEU A 1 147 ? 45.389 7.234 61.646 1.00 39.43 ? 147 LEU A O 1 ATOM 1135 C CB . LEU A 1 147 ? 43.556 6.836 58.908 1.00 38.63 ? 147 LEU A CB 1 ATOM 1136 C CG . LEU A 1 147 ? 42.584 6.727 60.089 1.00 40.86 ? 147 LEU A CG 1 ATOM 1137 C CD1 . LEU A 1 147 ? 42.384 8.080 60.768 1.00 38.22 ? 147 LEU A CD1 1 ATOM 1138 C CD2 . LEU A 1 147 ? 41.309 5.984 59.737 1.00 35.06 ? 147 LEU A CD2 1 ATOM 1139 N N . GLY A 1 148 ? 45.998 5.448 60.470 1.00 38.24 ? 148 GLY A N 1 ATOM 1140 C CA . GLY A 1 148 ? 46.619 4.753 61.585 1.00 38.44 ? 148 GLY A CA 1 ATOM 1141 C C . GLY A 1 148 ? 47.872 5.488 62.092 1.00 38.31 ? 148 GLY A C 1 ATOM 1142 O O . GLY A 1 148 ? 48.368 5.091 63.138 1.00 37.65 ? 148 GLY A O 1 ATOM 1143 N N . GLY A 1 149 ? 48.574 6.258 61.282 1.00 37.67 ? 149 GLY A N 1 ATOM 1144 C CA . GLY A 1 149 ? 49.713 7.038 61.719 1.00 39.00 ? 149 GLY A CA 1 ATOM 1145 C C . GLY A 1 149 ? 49.165 8.142 62.658 1.00 40.13 ? 149 GLY A C 1 ATOM 1146 O O . GLY A 1 149 ? 49.747 8.405 63.727 1.00 40.37 ? 149 GLY A O 1 ATOM 1147 N N . ALA A 1 150 ? 48.064 8.765 62.233 1.00 38.69 ? 150 ALA A N 1 ATOM 1148 C CA . ALA A 1 150 ? 47.358 9.713 63.062 1.00 39.11 ? 150 ALA A CA 1 ATOM 1149 C C . ALA A 1 150 ? 47.008 9.086 64.442 1.00 39.08 ? 150 ALA A C 1 ATOM 1150 O O . ALA A 1 150 ? 47.399 9.632 65.454 1.00 38.49 ? 150 ALA A O 1 ATOM 1151 C CB . ALA A 1 150 ? 46.050 10.147 62.410 1.00 32.88 ? 150 ALA A CB 1 ATOM 1152 N N . LEU A 1 151 ? 46.203 8.024 64.388 1.00 38.87 ? 151 LEU A N 1 ATOM 1153 C CA . LEU A 1 151 ? 45.758 7.434 65.605 1.00 40.11 ? 151 LEU A CA 1 ATOM 1154 C C . LEU A 1 151 ? 46.928 7.038 66.502 1.00 40.82 ? 151 LEU A C 1 ATOM 1155 O O . LEU A 1 151 ? 46.774 7.159 67.737 1.00 42.05 ? 151 LEU A O 1 ATOM 1156 C CB . LEU A 1 151 ? 44.795 6.277 65.519 1.00 39.14 ? 151 LEU A CB 1 ATOM 1157 C CG . LEU A 1 151 ? 43.474 6.394 64.710 1.00 40.41 ? 151 LEU A CG 1 ATOM 1158 C CD1 . LEU A 1 151 ? 43.034 5.016 64.208 1.00 39.76 ? 151 LEU A CD1 1 ATOM 1159 C CD2 . LEU A 1 151 ? 42.342 6.973 65.552 1.00 38.36 ? 151 LEU A CD2 1 ATOM 1160 N N . ALA A 1 152 ? 48.043 6.576 65.999 1.00 39.88 ? 152 ALA A N 1 ATOM 1161 C CA . ALA A 1 152 ? 49.153 6.120 66.770 1.00 39.03 ? 152 ALA A CA 1 ATOM 1162 C C . ALA A 1 152 ? 49.881 7.339 67.322 1.00 39.63 ? 152 ALA A C 1 ATOM 1163 O O . ALA A 1 152 ? 50.454 7.204 68.420 1.00 39.91 ? 152 ALA A O 1 ATOM 1164 C CB . ALA A 1 152 ? 50.141 5.266 66.042 1.00 34.49 ? 152 ALA A CB 1 ATOM 1165 N N . THR A 1 153 ? 49.923 8.391 66.519 1.00 39.40 ? 153 THR A N 1 ATOM 1166 C CA . THR A 1 153 ? 50.445 9.657 67.043 1.00 39.77 ? 153 THR A CA 1 ATOM 1167 C C . THR A 1 153 ? 49.544 10.232 68.138 1.00 40.29 ? 153 THR A C 1 ATOM 1168 O O . THR A 1 153 ? 50.110 10.623 69.165 1.00 40.21 ? 153 THR A O 1 ATOM 1169 C CB . THR A 1 153 ? 50.614 10.720 65.970 1.00 39.19 ? 153 THR A CB 1 ATOM 1170 O OG1 . THR A 1 153 ? 51.330 10.145 64.850 1.00 41.61 ? 153 THR A OG1 1 ATOM 1171 C CG2 . THR A 1 153 ? 51.264 11.971 66.499 1.00 36.48 ? 153 THR A CG2 1 ATOM 1172 N N . VAL A 1 154 ? 48.228 10.251 68.003 1.00 40.36 ? 154 VAL A N 1 ATOM 1173 C CA . VAL A 1 154 ? 47.357 10.763 69.051 1.00 41.85 ? 154 VAL A CA 1 ATOM 1174 C C . VAL A 1 154 ? 47.332 9.931 70.327 1.00 42.91 ? 154 VAL A C 1 ATOM 1175 O O . VAL A 1 154 ? 47.737 10.421 71.397 1.00 42.95 ? 154 VAL A O 1 ATOM 1176 C CB . VAL A 1 154 ? 45.965 11.093 68.514 1.00 41.67 ? 154 VAL A CB 1 ATOM 1177 C CG1 . VAL A 1 154 ? 44.954 11.355 69.605 1.00 40.91 ? 154 VAL A CG1 1 ATOM 1178 C CG2 . VAL A 1 154 ? 46.112 12.311 67.585 1.00 42.30 ? 154 VAL A CG2 1 ATOM 1179 N N . ALA A 1 155 ? 47.308 8.618 70.214 1.00 43.46 ? 155 ALA A N 1 ATOM 1180 C CA . ALA A 1 155 ? 47.491 7.699 71.318 1.00 44.53 ? 155 ALA A CA 1 ATOM 1181 C C . ALA A 1 155 ? 48.867 7.830 71.981 1.00 45.14 ? 155 ALA A C 1 ATOM 1182 O O . ALA A 1 155 ? 48.944 7.914 73.218 1.00 45.02 ? 155 ALA A O 1 ATOM 1183 C CB . ALA A 1 155 ? 47.227 6.278 70.864 1.00 41.74 ? 155 ALA A CB 1 ATOM 1184 N N . GLY A 1 156 ? 49.901 8.169 71.218 1.00 45.05 ? 156 GLY A N 1 ATOM 1185 C CA . GLY A 1 156 ? 51.224 8.300 71.812 1.00 45.72 ? 156 GLY A CA 1 ATOM 1186 C C . GLY A 1 156 ? 51.334 9.558 72.643 1.00 46.31 ? 156 GLY A C 1 ATOM 1187 O O . GLY A 1 156 ? 51.578 9.487 73.851 1.00 46.83 ? 156 GLY A O 1 ATOM 1188 N N . ALA A 1 157 ? 50.759 10.649 72.143 1.00 47.17 ? 157 ALA A N 1 ATOM 1189 C CA . ALA A 1 157 ? 50.773 11.922 72.853 1.00 47.26 ? 157 ALA A CA 1 ATOM 1190 C C . ALA A 1 157 ? 49.959 11.853 74.146 1.00 47.42 ? 157 ALA A C 1 ATOM 1191 O O . ALA A 1 157 ? 50.304 12.493 75.139 1.00 47.49 ? 157 ALA A O 1 ATOM 1192 C CB . ALA A 1 157 ? 50.288 13.058 71.990 1.00 44.90 ? 157 ALA A CB 1 ATOM 1193 N N . ASP A 1 158 ? 48.932 11.058 74.177 1.00 47.07 ? 158 ASP A N 1 ATOM 1194 C CA . ASP A 1 158 ? 48.051 10.908 75.299 1.00 48.02 ? 158 ASP A CA 1 ATOM 1195 C C . ASP A 1 158 ? 48.524 9.903 76.332 1.00 49.20 ? 158 ASP A C 1 ATOM 1196 O O . ASP A 1 158 ? 47.953 9.897 77.426 1.00 50.18 ? 158 ASP A O 1 ATOM 1197 C CB . ASP A 1 158 ? 46.733 10.343 74.708 1.00 48.02 ? 158 ASP A CB 1 ATOM 1198 C CG . ASP A 1 158 ? 45.564 10.433 75.660 1.00 47.23 ? 158 ASP A CG 1 ATOM 1199 O OD1 . ASP A 1 158 ? 45.654 11.365 76.491 1.00 50.25 ? 158 ASP A OD1 1 ATOM 1200 O OD2 . ASP A 1 158 ? 44.625 9.623 75.566 1.00 45.39 ? 158 ASP A OD2 1 ATOM 1201 N N . LEU A 1 159 ? 49.311 8.884 75.995 1.00 49.46 ? 159 LEU A N 1 ATOM 1202 C CA . LEU A 1 159 ? 49.586 7.843 76.969 1.00 49.37 ? 159 LEU A CA 1 ATOM 1203 C C . LEU A 1 159 ? 50.951 7.983 77.582 1.00 50.23 ? 159 LEU A C 1 ATOM 1204 O O . LEU A 1 159 ? 51.331 7.160 78.413 1.00 50.58 ? 159 LEU A O 1 ATOM 1205 C CB . LEU A 1 159 ? 49.342 6.470 76.365 1.00 48.25 ? 159 LEU A CB 1 ATOM 1206 C CG . LEU A 1 159 ? 47.924 6.000 76.107 1.00 48.59 ? 159 LEU A CG 1 ATOM 1207 C CD1 . LEU A 1 159 ? 47.856 4.474 76.059 1.00 49.10 ? 159 LEU A CD1 1 ATOM 1208 C CD2 . LEU A 1 159 ? 46.868 6.502 77.094 1.00 44.40 ? 159 LEU A CD2 1 ATOM 1209 N N . ARG A 1 160 ? 51.799 8.785 76.973 1.00 51.53 ? 160 ARG A N 1 ATOM 1210 C CA . ARG A 1 160 ? 53.150 9.021 77.484 1.00 53.41 ? 160 ARG A CA 1 ATOM 1211 C C . ARG A 1 160 ? 53.089 9.652 78.861 1.00 53.96 ? 160 ARG A C 1 ATOM 1212 O O . ARG A 1 160 ? 52.065 10.273 79.123 1.00 54.15 ? 160 ARG A O 1 ATOM 1213 C CB . ARG A 1 160 ? 53.882 9.923 76.477 1.00 56.68 ? 160 ARG A CB 1 ATOM 1214 C CG . ARG A 1 160 ? 54.322 9.153 75.225 1.00 58.37 ? 160 ARG A CG 1 ATOM 1215 C CD . ARG A 1 160 ? 54.738 10.072 74.113 1.00 56.57 ? 160 ARG A CD 1 ATOM 1216 N NE . ARG A 1 160 ? 55.700 9.525 73.150 1.00 55.17 ? 160 ARG A NE 1 ATOM 1217 C CZ . ARG A 1 160 ? 55.986 10.275 72.079 1.00 52.83 ? 160 ARG A CZ 1 ATOM 1218 N NH1 . ARG A 1 160 ? 55.360 11.433 72.003 1.00 53.75 ? 160 ARG A NH1 1 ATOM 1219 N NH2 . ARG A 1 160 ? 56.826 9.973 71.128 1.00 50.63 ? 160 ARG A NH2 1 ATOM 1220 N N . GLY A 1 161 ? 54.059 9.454 79.748 1.00 54.97 ? 161 GLY A N 1 ATOM 1221 C CA . GLY A 1 161 ? 54.063 10.034 81.056 1.00 54.58 ? 161 GLY A CA 1 ATOM 1222 C C . GLY A 1 161 ? 53.750 9.103 82.199 1.00 55.24 ? 161 GLY A C 1 ATOM 1223 O O . GLY A 1 161 ? 53.883 9.535 83.348 1.00 55.68 ? 161 GLY A O 1 ATOM 1224 N N . ASN A 1 162 ? 53.257 7.900 82.027 1.00 55.55 ? 162 ASN A N 1 ATOM 1225 C CA . ASN A 1 162 ? 52.752 6.997 83.048 1.00 55.90 ? 162 ASN A CA 1 ATOM 1226 C C . ASN A 1 162 ? 53.843 5.970 83.339 1.00 55.24 ? 162 ASN A C 1 ATOM 1227 O O . ASN A 1 162 ? 53.592 4.803 83.670 1.00 55.39 ? 162 ASN A O 1 ATOM 1228 C CB . ASN A 1 162 ? 51.320 6.469 82.800 1.00 60.93 ? 162 ASN A CB 1 ATOM 1229 C CG . ASN A 1 162 ? 50.496 7.362 81.876 1.00 67.28 ? 162 ASN A CG 1 ATOM 1230 O OD1 . ASN A 1 162 ? 49.673 6.971 80.992 1.00 71.53 ? 162 ASN A OD1 1 ATOM 1231 N ND2 . ASN A 1 162 ? 50.590 8.709 81.890 1.00 67.62 ? 162 ASN A ND2 1 ATOM 1232 N N . GLY A 1 163 ? 55.100 6.427 83.241 1.00 53.96 ? 163 GLY A N 1 ATOM 1233 C CA . GLY A 1 163 ? 56.229 5.592 83.553 1.00 53.45 ? 163 GLY A CA 1 ATOM 1234 C C . GLY A 1 163 ? 56.702 4.734 82.391 1.00 53.47 ? 163 GLY A C 1 ATOM 1235 O O . GLY A 1 163 ? 57.627 3.912 82.597 1.00 54.21 ? 163 GLY A O 1 ATOM 1236 N N . TYR A 1 164 ? 56.128 4.768 81.181 1.00 51.80 ? 164 TYR A N 1 ATOM 1237 C CA . TYR A 1 164 ? 56.810 3.920 80.181 1.00 50.55 ? 164 TYR A CA 1 ATOM 1238 C C . TYR A 1 164 ? 56.973 4.703 78.900 1.00 49.18 ? 164 TYR A C 1 ATOM 1239 O O . TYR A 1 164 ? 56.051 5.450 78.590 1.00 49.71 ? 164 TYR A O 1 ATOM 1240 C CB . TYR A 1 164 ? 56.160 2.562 80.077 1.00 50.20 ? 164 TYR A CB 1 ATOM 1241 C CG . TYR A 1 164 ? 54.697 2.668 79.723 1.00 49.60 ? 164 TYR A CG 1 ATOM 1242 C CD1 . TYR A 1 164 ? 53.740 2.666 80.715 1.00 47.90 ? 164 TYR A CD1 1 ATOM 1243 C CD2 . TYR A 1 164 ? 54.306 2.802 78.392 1.00 49.31 ? 164 TYR A CD2 1 ATOM 1244 C CE1 . TYR A 1 164 ? 52.400 2.732 80.428 1.00 47.95 ? 164 TYR A CE1 1 ATOM 1245 C CE2 . TYR A 1 164 ? 52.953 2.899 78.096 1.00 49.36 ? 164 TYR A CE2 1 ATOM 1246 C CZ . TYR A 1 164 ? 52.027 2.871 79.111 1.00 49.42 ? 164 TYR A CZ 1 ATOM 1247 O OH . TYR A 1 164 ? 50.697 2.984 78.777 1.00 51.38 ? 164 TYR A OH 1 ATOM 1248 N N . ASP A 1 165 ? 58.183 4.739 78.384 1.00 47.84 ? 165 ASP A N 1 ATOM 1249 C CA . ASP A 1 165 ? 58.474 5.523 77.182 1.00 46.27 ? 165 ASP A CA 1 ATOM 1250 C C . ASP A 1 165 ? 57.649 4.977 76.031 1.00 45.03 ? 165 ASP A C 1 ATOM 1251 O O . ASP A 1 165 ? 57.409 3.766 76.008 1.00 44.41 ? 165 ASP A O 1 ATOM 1252 C CB . ASP A 1 165 ? 59.951 5.411 76.791 1.00 47.57 ? 165 ASP A CB 1 ATOM 1253 C CG . ASP A 1 165 ? 60.853 6.358 77.537 1.00 51.05 ? 165 ASP A CG 1 ATOM 1254 O OD1 . ASP A 1 165 ? 60.330 7.176 78.331 1.00 52.02 ? 165 ASP A OD1 1 ATOM 1255 O OD2 . ASP A 1 165 ? 62.086 6.308 77.325 1.00 53.59 ? 165 ASP A OD2 1 ATOM 1256 N N . ILE A 1 166 ? 57.048 5.878 75.257 1.00 44.30 ? 166 ILE A N 1 ATOM 1257 C CA . ILE A 1 166 ? 56.350 5.439 74.042 1.00 44.06 ? 166 ILE A CA 1 ATOM 1258 C C . ILE A 1 166 ? 56.968 5.957 72.756 1.00 44.37 ? 166 ILE A C 1 ATOM 1259 O O . ILE A 1 166 ? 57.099 7.164 72.479 1.00 44.92 ? 166 ILE A O 1 ATOM 1260 C CB . ILE A 1 166 ? 54.856 5.790 74.056 1.00 43.24 ? 166 ILE A CB 1 ATOM 1261 C CG1 . ILE A 1 166 ? 54.240 5.334 75.403 1.00 42.19 ? 166 ILE A CG1 1 ATOM 1262 C CG2 . ILE A 1 166 ? 54.139 5.196 72.861 1.00 39.19 ? 166 ILE A CG2 1 ATOM 1263 C CD1 . ILE A 1 166 ? 52.809 5.711 75.640 1.00 40.33 ? 166 ILE A CD1 1 ATOM 1264 N N . ASP A 1 167 ? 57.522 5.017 71.990 1.00 44.35 ? 167 ASP A N 1 ATOM 1265 C CA . ASP A 1 167 ? 58.048 5.383 70.657 1.00 43.38 ? 167 ASP A CA 1 ATOM 1266 C C . ASP A 1 167 ? 56.923 5.309 69.635 1.00 42.54 ? 167 ASP A C 1 ATOM 1267 O O . ASP A 1 167 ? 56.041 4.452 69.782 1.00 43.38 ? 167 ASP A O 1 ATOM 1268 C CB . ASP A 1 167 ? 59.231 4.508 70.276 1.00 43.79 ? 167 ASP A CB 1 ATOM 1269 C CG . ASP A 1 167 ? 60.526 4.969 70.923 1.00 46.90 ? 167 ASP A CG 1 ATOM 1270 O OD1 . ASP A 1 167 ? 60.515 6.127 71.383 1.00 45.82 ? 167 ASP A OD1 1 ATOM 1271 O OD2 . ASP A 1 167 ? 61.534 4.215 70.991 1.00 48.62 ? 167 ASP A OD2 1 ATOM 1272 N N . VAL A 1 168 ? 56.739 6.328 68.822 1.00 41.78 ? 168 VAL A N 1 ATOM 1273 C CA . VAL A 1 168 ? 55.765 6.350 67.743 1.00 40.69 ? 168 VAL A CA 1 ATOM 1274 C C . VAL A 1 168 ? 56.506 6.333 66.399 1.00 39.34 ? 168 VAL A C 1 ATOM 1275 O O . VAL A 1 168 ? 57.340 7.244 66.231 1.00 39.95 ? 168 VAL A O 1 ATOM 1276 C CB . VAL A 1 168 ? 54.864 7.594 67.681 1.00 40.42 ? 168 VAL A CB 1 ATOM 1277 C CG1 . VAL A 1 168 ? 53.869 7.423 66.539 1.00 40.66 ? 168 VAL A CG1 1 ATOM 1278 C CG2 . VAL A 1 168 ? 54.114 7.802 68.989 1.00 42.16 ? 168 VAL A CG2 1 ATOM 1279 N N . PHE A 1 169 ? 56.041 5.504 65.489 1.00 37.64 ? 169 PHE A N 1 ATOM 1280 C CA . PHE A 1 169 ? 56.543 5.450 64.129 1.00 36.37 ? 169 PHE A CA 1 ATOM 1281 C C . PHE A 1 169 ? 55.311 5.526 63.225 1.00 36.73 ? 169 PHE A C 1 ATOM 1282 O O . PHE A 1 169 ? 54.430 4.662 63.363 1.00 37.63 ? 169 PHE A O 1 ATOM 1283 C CB . PHE A 1 169 ? 57.276 4.152 63.821 1.00 33.50 ? 169 PHE A CB 1 ATOM 1284 C CG . PHE A 1 169 ? 58.635 3.971 64.424 1.00 29.46 ? 169 PHE A CG 1 ATOM 1285 C CD1 . PHE A 1 169 ? 58.684 3.645 65.764 1.00 25.88 ? 169 PHE A CD1 1 ATOM 1286 C CD2 . PHE A 1 169 ? 59.821 4.075 63.742 1.00 31.10 ? 169 PHE A CD2 1 ATOM 1287 C CE1 . PHE A 1 169 ? 59.875 3.473 66.421 1.00 26.62 ? 169 PHE A CE1 1 ATOM 1288 C CE2 . PHE A 1 169 ? 61.048 3.874 64.405 1.00 32.46 ? 169 PHE A CE2 1 ATOM 1289 C CZ . PHE A 1 169 ? 61.061 3.556 65.771 1.00 28.13 ? 169 PHE A CZ 1 ATOM 1290 N N . SER A 1 170 ? 55.182 6.638 62.513 1.00 35.49 ? 170 SER A N 1 ATOM 1291 C CA . SER A 1 170 ? 53.980 6.797 61.712 1.00 35.09 ? 170 SER A CA 1 ATOM 1292 C C . SER A 1 170 ? 54.330 6.951 60.235 1.00 34.17 ? 170 SER A C 1 ATOM 1293 O O . SER A 1 170 ? 55.493 7.308 59.972 1.00 34.96 ? 170 SER A O 1 ATOM 1294 C CB . SER A 1 170 ? 53.225 8.035 62.221 1.00 34.17 ? 170 SER A CB 1 ATOM 1295 O OG . SER A 1 170 ? 54.135 9.095 61.849 1.00 38.66 ? 170 SER A OG 1 ATOM 1296 N N . TYR A 1 171 ? 53.601 6.268 59.346 1.00 32.13 ? 171 TYR A N 1 ATOM 1297 C CA . TYR A 1 171 ? 53.983 6.272 57.938 1.00 31.29 ? 171 TYR A CA 1 ATOM 1298 C C . TYR A 1 171 ? 52.903 7.004 57.170 1.00 31.03 ? 171 TYR A C 1 ATOM 1299 O O . TYR A 1 171 ? 51.716 6.682 57.305 1.00 31.23 ? 171 TYR A O 1 ATOM 1300 C CB . TYR A 1 171 ? 54.260 4.838 57.419 1.00 30.85 ? 171 TYR A CB 1 ATOM 1301 C CG . TYR A 1 171 ? 55.396 4.236 58.211 1.00 30.25 ? 171 TYR A CG 1 ATOM 1302 C CD1 . TYR A 1 171 ? 55.155 3.711 59.484 1.00 30.77 ? 171 TYR A CD1 1 ATOM 1303 C CD2 . TYR A 1 171 ? 56.695 4.234 57.704 1.00 30.34 ? 171 TYR A CD2 1 ATOM 1304 C CE1 . TYR A 1 171 ? 56.200 3.222 60.249 1.00 31.08 ? 171 TYR A CE1 1 ATOM 1305 C CE2 . TYR A 1 171 ? 57.748 3.742 58.464 1.00 30.81 ? 171 TYR A CE2 1 ATOM 1306 C CZ . TYR A 1 171 ? 57.474 3.235 59.718 1.00 31.47 ? 171 TYR A CZ 1 ATOM 1307 O OH . TYR A 1 171 ? 58.482 2.692 60.461 1.00 32.91 ? 171 TYR A OH 1 ATOM 1308 N N . GLY A 1 172 ? 53.270 8.000 56.377 1.00 30.95 ? 172 GLY A N 1 ATOM 1309 C CA . GLY A 1 172 ? 52.368 8.880 55.670 1.00 31.40 ? 172 GLY A CA 1 ATOM 1310 C C . GLY A 1 172 ? 51.135 9.324 56.422 1.00 31.95 ? 172 GLY A C 1 ATOM 1311 O O . GLY A 1 172 ? 50.044 9.308 55.839 1.00 31.21 ? 172 GLY A O 1 ATOM 1312 N N . ALA A 1 173 ? 51.337 9.736 57.682 1.00 32.72 ? 173 ALA A N 1 ATOM 1313 C CA . ALA A 1 173 ? 50.193 10.208 58.460 1.00 33.98 ? 173 ALA A CA 1 ATOM 1314 C C . ALA A 1 173 ? 49.885 11.658 58.076 1.00 34.94 ? 173 ALA A C 1 ATOM 1315 O O . ALA A 1 173 ? 50.782 12.408 57.692 1.00 34.55 ? 173 ALA A O 1 ATOM 1316 C CB . ALA A 1 173 ? 50.542 10.110 59.929 1.00 32.86 ? 173 ALA A CB 1 ATOM 1317 N N . PRO A 1 174 ? 48.631 12.036 58.211 1.00 36.20 ? 174 PRO A N 1 ATOM 1318 C CA . PRO A 1 174 ? 48.167 13.397 58.003 1.00 37.42 ? 174 PRO A CA 1 ATOM 1319 C C . PRO A 1 174 ? 48.507 14.246 59.221 1.00 38.62 ? 174 PRO A C 1 ATOM 1320 O O . PRO A 1 174 ? 48.993 13.754 60.248 1.00 39.41 ? 174 PRO A O 1 ATOM 1321 C CB . PRO A 1 174 ? 46.642 13.278 57.908 1.00 36.96 ? 174 PRO A CB 1 ATOM 1322 C CG . PRO A 1 174 ? 46.282 12.002 58.545 1.00 36.95 ? 174 PRO A CG 1 ATOM 1323 C CD . PRO A 1 174 ? 47.536 11.196 58.757 1.00 36.71 ? 174 PRO A CD 1 ATOM 1324 N N . ARG A 1 175 ? 48.413 15.559 59.059 1.00 39.57 ? 175 ARG A N 1 ATOM 1325 C CA . ARG A 1 175 ? 48.594 16.483 60.185 1.00 38.81 ? 175 ARG A CA 1 ATOM 1326 C C . ARG A 1 175 ? 47.544 16.075 61.215 1.00 39.24 ? 175 ARG A C 1 ATOM 1327 O O . ARG A 1 175 ? 46.482 15.523 60.853 1.00 38.46 ? 175 ARG A O 1 ATOM 1328 C CB . ARG A 1 175 ? 48.433 17.953 59.773 1.00 35.13 ? 175 ARG A CB 1 ATOM 1329 C CG . ARG A 1 175 ? 49.610 18.395 58.902 1.00 35.25 ? 175 ARG A CG 1 ATOM 1330 C CD . ARG A 1 175 ? 49.565 19.856 58.496 1.00 35.37 ? 175 ARG A CD 1 ATOM 1331 N NE . ARG A 1 175 ? 50.530 20.120 57.456 1.00 36.70 ? 175 ARG A NE 1 ATOM 1332 C CZ . ARG A 1 175 ? 50.313 20.229 56.135 1.00 34.91 ? 175 ARG A CZ 1 ATOM 1333 N NH1 . ARG A 1 175 ? 51.411 20.371 55.366 1.00 33.53 ? 175 ARG A NH1 1 ATOM 1334 N NH2 . ARG A 1 175 ? 49.057 20.085 55.708 1.00 30.72 ? 175 ARG A NH2 1 ATOM 1335 N N . VAL A 1 176 ? 47.783 16.465 62.466 1.00 39.70 ? 176 VAL A N 1 ATOM 1336 C CA . VAL A 1 176 ? 46.860 15.913 63.492 1.00 40.72 ? 176 VAL A CA 1 ATOM 1337 C C . VAL A 1 176 ? 46.236 17.006 64.341 1.00 42.35 ? 176 VAL A C 1 ATOM 1338 O O . VAL A 1 176 ? 45.273 16.733 65.106 1.00 41.64 ? 176 VAL A O 1 ATOM 1339 C CB . VAL A 1 176 ? 47.700 14.785 64.096 0.50 36.39 ? 176 VAL A CB 1 ATOM 1340 C CG1 . VAL A 1 176 ? 48.215 15.101 65.468 0.50 29.95 ? 176 VAL A CG1 1 ATOM 1341 C CG2 . VAL A 1 176 ? 47.032 13.440 63.864 0.50 32.52 ? 176 VAL A CG2 1 ATOM 1342 N N . GLY A 1 177 ? 46.784 18.233 64.143 1.00 42.36 ? 177 GLY A N 1 ATOM 1343 C CA . GLY A 1 177 ? 46.217 19.333 64.911 1.00 43.88 ? 177 GLY A CA 1 ATOM 1344 C C . GLY A 1 177 ? 47.057 20.596 64.791 1.00 44.59 ? 177 GLY A C 1 ATOM 1345 O O . GLY A 1 177 ? 47.534 20.865 63.684 1.00 44.98 ? 177 GLY A O 1 ATOM 1346 N N . ASN A 1 178 ? 46.970 21.464 65.794 1.00 45.54 ? 178 ASN A N 1 ATOM 1347 C CA . ASN A 1 178 ? 47.481 22.816 65.660 1.00 46.68 ? 178 ASN A CA 1 ATOM 1348 C C . ASN A 1 178 ? 48.938 22.884 66.047 1.00 47.13 ? 178 ASN A C 1 ATOM 1349 O O . ASN A 1 178 ? 49.503 21.847 66.358 1.00 47.36 ? 178 ASN A O 1 ATOM 1350 C CB . ASN A 1 178 ? 46.686 23.892 66.339 1.00 46.92 ? 178 ASN A CB 1 ATOM 1351 C CG . ASN A 1 178 ? 46.530 23.739 67.825 1.00 49.08 ? 178 ASN A CG 1 ATOM 1352 O OD1 . ASN A 1 178 ? 47.281 23.052 68.513 1.00 48.90 ? 178 ASN A OD1 1 ATOM 1353 N ND2 . ASN A 1 178 ? 45.500 24.437 68.269 1.00 51.16 ? 178 ASN A ND2 1 ATOM 1354 N N . ARG A 1 179 ? 49.415 24.107 65.927 1.00 47.66 ? 179 ARG A N 1 ATOM 1355 C CA . ARG A 1 179 ? 50.791 24.506 66.180 1.00 49.07 ? 179 ARG A CA 1 ATOM 1356 C C . ARG A 1 179 ? 51.130 24.074 67.570 1.00 49.79 ? 179 ARG A C 1 ATOM 1357 O O . ARG A 1 179 ? 52.121 23.386 67.757 1.00 51.55 ? 179 ARG A O 1 ATOM 1358 C CB . ARG A 1 179 ? 51.024 26.016 66.096 1.00 53.20 ? 179 ARG A CB 1 ATOM 1359 C CG . ARG A 1 179 ? 52.386 26.530 66.436 1.00 55.29 ? 179 ARG A CG 1 ATOM 1360 C CD . ARG A 1 179 ? 53.371 26.213 65.350 1.00 58.68 ? 179 ARG A CD 1 ATOM 1361 N NE . ARG A 1 179 ? 54.710 26.712 65.721 1.00 62.87 ? 179 ARG A NE 1 ATOM 1362 C CZ . ARG A 1 179 ? 55.532 27.263 64.811 1.00 65.97 ? 179 ARG A CZ 1 ATOM 1363 N NH1 . ARG A 1 179 ? 55.148 27.417 63.535 1.00 64.73 ? 179 ARG A NH1 1 ATOM 1364 N NH2 . ARG A 1 179 ? 56.774 27.652 65.151 1.00 66.71 ? 179 ARG A NH2 1 ATOM 1365 N N . ALA A 1 180 ? 50.253 24.452 68.504 1.00 49.47 ? 180 ALA A N 1 ATOM 1366 C CA . ALA A 1 180 ? 50.543 24.015 69.873 1.00 48.70 ? 180 ALA A CA 1 ATOM 1367 C C . ALA A 1 180 ? 50.625 22.496 69.866 1.00 47.67 ? 180 ALA A C 1 ATOM 1368 O O . ALA A 1 180 ? 51.599 21.971 70.412 1.00 48.07 ? 180 ALA A O 1 ATOM 1369 C CB . ALA A 1 180 ? 49.541 24.580 70.865 1.00 47.71 ? 180 ALA A CB 1 ATOM 1370 N N . PHE A 1 181 ? 49.717 21.758 69.233 1.00 46.32 ? 181 PHE A N 1 ATOM 1371 C CA . PHE A 1 181 ? 49.828 20.307 69.256 1.00 45.71 ? 181 PHE A CA 1 ATOM 1372 C C . PHE A 1 181 ? 51.114 19.800 68.613 1.00 46.24 ? 181 PHE A C 1 ATOM 1373 O O . PHE A 1 181 ? 51.776 18.875 69.112 1.00 46.09 ? 181 PHE A O 1 ATOM 1374 C CB . PHE A 1 181 ? 48.623 19.623 68.644 1.00 45.88 ? 181 PHE A CB 1 ATOM 1375 C CG . PHE A 1 181 ? 48.497 18.179 69.035 1.00 46.62 ? 181 PHE A CG 1 ATOM 1376 C CD1 . PHE A 1 181 ? 49.059 17.685 70.205 1.00 44.03 ? 181 PHE A CD1 1 ATOM 1377 C CD2 . PHE A 1 181 ? 47.740 17.338 68.239 1.00 44.43 ? 181 PHE A CD2 1 ATOM 1378 C CE1 . PHE A 1 181 ? 48.907 16.357 70.538 1.00 45.12 ? 181 PHE A CE1 1 ATOM 1379 C CE2 . PHE A 1 181 ? 47.589 16.011 68.611 1.00 45.43 ? 181 PHE A CE2 1 ATOM 1380 C CZ . PHE A 1 181 ? 48.175 15.491 69.729 1.00 43.63 ? 181 PHE A CZ 1 ATOM 1381 N N . ALA A 1 182 ? 51.539 20.492 67.573 1.00 45.51 ? 182 ALA A N 1 ATOM 1382 C CA . ALA A 1 182 ? 52.787 20.297 66.901 1.00 46.21 ? 182 ALA A CA 1 ATOM 1383 C C . ALA A 1 182 ? 53.966 20.501 67.830 1.00 47.42 ? 182 ALA A C 1 ATOM 1384 O O . ALA A 1 182 ? 54.980 19.789 67.815 1.00 47.64 ? 182 ALA A O 1 ATOM 1385 C CB . ALA A 1 182 ? 52.838 21.293 65.730 1.00 46.60 ? 182 ALA A CB 1 ATOM 1386 N N . GLU A 1 183 ? 53.857 21.549 68.670 1.00 47.65 ? 183 GLU A N 1 ATOM 1387 C CA . GLU A 1 183 ? 54.970 21.866 69.565 1.00 47.58 ? 183 GLU A CA 1 ATOM 1388 C C . GLU A 1 183 ? 55.060 20.823 70.645 1.00 46.53 ? 183 GLU A C 1 ATOM 1389 O O . GLU A 1 183 ? 56.112 20.230 70.906 1.00 46.49 ? 183 GLU A O 1 ATOM 1390 C CB . GLU A 1 183 ? 54.859 23.310 70.031 1.00 53.85 ? 183 GLU A CB 1 ATOM 1391 C CG . GLU A 1 183 ? 55.258 24.215 68.865 1.00 59.62 ? 183 GLU A CG 1 ATOM 1392 C CD . GLU A 1 183 ? 54.815 25.645 69.039 1.00 63.73 ? 183 GLU A CD 1 ATOM 1393 O OE1 . GLU A 1 183 ? 54.155 25.938 70.063 1.00 65.97 ? 183 GLU A OE1 1 ATOM 1394 O OE2 . GLU A 1 183 ? 55.172 26.425 68.120 1.00 66.19 ? 183 GLU A OE2 1 ATOM 1395 N N . PHE A 1 184 ? 53.888 20.398 71.082 1.00 46.09 ? 184 PHE A N 1 ATOM 1396 C CA . PHE A 1 184 ? 53.867 19.366 72.119 1.00 47.67 ? 184 PHE A CA 1 ATOM 1397 C C . PHE A 1 184 ? 54.548 18.128 71.559 1.00 48.67 ? 184 PHE A C 1 ATOM 1398 O O . PHE A 1 184 ? 55.586 17.699 72.043 1.00 49.28 ? 184 PHE A O 1 ATOM 1399 C CB . PHE A 1 184 ? 52.471 19.119 72.648 1.00 43.45 ? 184 PHE A CB 1 ATOM 1400 C CG . PHE A 1 184 ? 52.405 18.082 73.721 1.00 43.08 ? 184 PHE A CG 1 ATOM 1401 C CD1 . PHE A 1 184 ? 52.770 18.417 75.034 1.00 44.27 ? 184 PHE A CD1 1 ATOM 1402 C CD2 . PHE A 1 184 ? 51.828 16.844 73.481 1.00 38.87 ? 184 PHE A CD2 1 ATOM 1403 C CE1 . PHE A 1 184 ? 52.619 17.478 76.057 1.00 41.91 ? 184 PHE A CE1 1 ATOM 1404 C CE2 . PHE A 1 184 ? 51.667 15.926 74.498 1.00 40.09 ? 184 PHE A CE2 1 ATOM 1405 C CZ . PHE A 1 184 ? 52.099 16.214 75.790 1.00 40.60 ? 184 PHE A CZ 1 ATOM 1406 N N . LEU A 1 185 ? 54.067 17.603 70.430 1.00 49.59 ? 185 LEU A N 1 ATOM 1407 C CA . LEU A 1 185 ? 54.656 16.446 69.794 1.00 48.85 ? 185 LEU A CA 1 ATOM 1408 C C . LEU A 1 185 ? 56.103 16.676 69.399 1.00 48.66 ? 185 LEU A C 1 ATOM 1409 O O . LEU A 1 185 ? 56.857 15.697 69.318 1.00 48.36 ? 185 LEU A O 1 ATOM 1410 C CB . LEU A 1 185 ? 53.780 16.048 68.605 1.00 50.28 ? 185 LEU A CB 1 ATOM 1411 C CG . LEU A 1 185 ? 52.467 15.357 69.005 1.00 52.46 ? 185 LEU A CG 1 ATOM 1412 C CD1 . LEU A 1 185 ? 51.626 15.170 67.748 1.00 50.87 ? 185 LEU A CD1 1 ATOM 1413 C CD2 . LEU A 1 185 ? 52.720 14.039 69.722 1.00 51.47 ? 185 LEU A CD2 1 ATOM 1414 N N . THR A 1 186 ? 56.565 17.892 69.125 1.00 48.58 ? 186 THR A N 1 ATOM 1415 C CA . THR A 1 186 ? 57.994 18.020 68.869 1.00 49.28 ? 186 THR A CA 1 ATOM 1416 C C . THR A 1 186 ? 58.786 17.796 70.160 1.00 51.26 ? 186 THR A C 1 ATOM 1417 O O . THR A 1 186 ? 59.868 17.203 70.083 1.00 51.60 ? 186 THR A O 1 ATOM 1418 C CB . THR A 1 186 ? 58.405 19.366 68.275 1.00 43.36 ? 186 THR A CB 1 ATOM 1419 O OG1 . THR A 1 186 ? 57.825 19.602 67.000 1.00 43.78 ? 186 THR A OG1 1 ATOM 1420 C CG2 . THR A 1 186 ? 59.906 19.446 68.125 1.00 38.27 ? 186 THR A CG2 1 ATOM 1421 N N . VAL A 1 187 ? 58.346 18.324 71.308 1.00 52.27 ? 187 VAL A N 1 ATOM 1422 C CA . VAL A 1 187 ? 59.140 18.269 72.534 1.00 53.16 ? 187 VAL A CA 1 ATOM 1423 C C . VAL A 1 187 ? 58.644 17.328 73.607 1.00 53.88 ? 187 VAL A C 1 ATOM 1424 O O . VAL A 1 187 ? 59.102 17.317 74.747 1.00 53.99 ? 187 VAL A O 1 ATOM 1425 C CB . VAL A 1 187 ? 59.283 19.681 73.178 1.00 52.41 ? 187 VAL A CB 1 ATOM 1426 C CG1 . VAL A 1 187 ? 59.828 20.716 72.205 1.00 51.74 ? 187 VAL A CG1 1 ATOM 1427 C CG2 . VAL A 1 187 ? 57.937 20.168 73.709 1.00 50.82 ? 187 VAL A CG2 1 ATOM 1428 N N . GLN A 1 188 ? 57.554 16.616 73.377 1.00 54.85 ? 188 GLN A N 1 ATOM 1429 C CA . GLN A 1 188 ? 57.016 15.787 74.454 1.00 55.80 ? 188 GLN A CA 1 ATOM 1430 C C . GLN A 1 188 ? 57.974 14.665 74.844 1.00 56.22 ? 188 GLN A C 1 ATOM 1431 O O . GLN A 1 188 ? 58.061 13.616 74.186 1.00 56.62 ? 188 GLN A O 1 ATOM 1432 C CB . GLN A 1 188 ? 55.620 15.303 74.084 1.00 53.80 ? 188 GLN A CB 1 ATOM 1433 C CG . GLN A 1 188 ? 55.206 14.164 75.015 1.00 53.71 ? 188 GLN A CG 1 ATOM 1434 C CD . GLN A 1 188 ? 54.042 13.465 74.340 1.00 58.94 ? 188 GLN A CD 1 ATOM 1435 O OE1 . GLN A 1 188 ? 54.130 13.138 73.157 1.00 53.23 ? 188 GLN A OE1 1 ATOM 1436 N NE2 . GLN A 1 188 ? 52.994 13.308 75.163 1.00 60.99 ? 188 GLN A NE2 1 ATOM 1437 N N . THR A 1 189 ? 58.530 14.770 76.044 1.00 56.00 ? 189 THR A N 1 ATOM 1438 C CA . THR A 1 189 ? 59.450 13.712 76.500 1.00 56.18 ? 189 THR A CA 1 ATOM 1439 C C . THR A 1 189 ? 58.809 12.361 76.768 1.00 55.13 ? 189 THR A C 1 ATOM 1440 O O . THR A 1 189 ? 57.609 12.274 76.999 1.00 55.35 ? 189 THR A O 1 ATOM 1441 C CB . THR A 1 189 ? 60.100 14.218 77.818 1.00 57.34 ? 189 THR A CB 1 ATOM 1442 O OG1 . THR A 1 189 ? 59.042 14.836 78.570 1.00 55.94 ? 189 THR A OG1 1 ATOM 1443 C CG2 . THR A 1 189 ? 61.253 15.136 77.448 1.00 55.37 ? 189 THR A CG2 1 ATOM 1444 N N . GLY A 1 190 ? 59.616 11.332 77.022 1.00 54.44 ? 190 GLY A N 1 ATOM 1445 C CA . GLY A 1 190 ? 59.071 10.015 77.334 1.00 53.57 ? 190 GLY A CA 1 ATOM 1446 C C . GLY A 1 190 ? 58.807 9.219 76.055 1.00 53.10 ? 190 GLY A C 1 ATOM 1447 O O . GLY A 1 190 ? 57.961 8.321 76.061 1.00 53.12 ? 190 GLY A O 1 ATOM 1448 N N . GLY A 1 191 ? 59.612 9.475 75.020 1.00 51.72 ? 191 GLY A N 1 ATOM 1449 C CA . GLY A 1 191 ? 59.463 8.740 73.777 1.00 50.45 ? 191 GLY A CA 1 ATOM 1450 C C . GLY A 1 191 ? 59.802 9.612 72.585 1.00 49.42 ? 191 GLY A C 1 ATOM 1451 O O . GLY A 1 191 ? 59.842 10.835 72.696 1.00 50.61 ? 191 GLY A O 1 ATOM 1452 N N . THR A 1 192 ? 60.119 9.000 71.443 1.00 47.57 ? 192 THR A N 1 ATOM 1453 C CA . THR A 1 192 ? 60.456 9.755 70.250 1.00 44.08 ? 192 THR A CA 1 ATOM 1454 C C . THR A 1 192 ? 59.474 9.425 69.135 1.00 42.77 ? 192 THR A C 1 ATOM 1455 O O . THR A 1 192 ? 58.929 8.334 69.118 1.00 41.34 ? 192 THR A O 1 ATOM 1456 C CB . THR A 1 192 ? 61.887 9.479 69.849 1.00 43.19 ? 192 THR A CB 1 ATOM 1457 O OG1 . THR A 1 192 ? 62.822 10.012 70.820 1.00 47.13 ? 192 THR A OG1 1 ATOM 1458 C CG2 . THR A 1 192 ? 62.197 10.035 68.484 1.00 38.84 ? 192 THR A CG2 1 ATOM 1459 N N . LEU A 1 193 ? 58.923 10.477 68.501 1.00 41.51 ? 193 LEU A N 1 ATOM 1460 C CA . LEU A 1 193 ? 58.044 10.275 67.373 1.00 40.36 ? 193 LEU A CA 1 ATOM 1461 C C . LEU A 1 193 ? 58.841 10.347 66.054 1.00 39.97 ? 193 LEU A C 1 ATOM 1462 O O . LEU A 1 193 ? 59.750 11.154 65.846 1.00 39.37 ? 193 LEU A O 1 ATOM 1463 C CB . LEU A 1 193 ? 56.810 11.143 67.469 1.00 39.84 ? 193 LEU A CB 1 ATOM 1464 C CG . LEU A 1 193 ? 56.335 11.822 66.169 1.00 40.66 ? 193 LEU A CG 1 ATOM 1465 C CD1 . LEU A 1 193 ? 55.847 10.756 65.198 1.00 43.51 ? 193 LEU A CD1 1 ATOM 1466 C CD2 . LEU A 1 193 ? 55.295 12.866 66.452 1.00 40.18 ? 193 LEU A CD2 1 ATOM 1467 N N . TYR A 1 194 ? 58.699 9.254 65.280 1.00 38.84 ? 194 TYR A N 1 ATOM 1468 C CA . TYR A 1 194 ? 59.370 9.235 63.994 1.00 38.68 ? 194 TYR A CA 1 ATOM 1469 C C . TYR A 1 194 ? 58.360 9.399 62.859 1.00 38.27 ? 194 TYR A C 1 ATOM 1470 O O . TYR A 1 194 ? 57.601 8.458 62.620 1.00 39.24 ? 194 TYR A O 1 ATOM 1471 C CB . TYR A 1 194 ? 60.209 8.012 63.739 1.00 37.93 ? 194 TYR A CB 1 ATOM 1472 C CG . TYR A 1 194 ? 61.261 7.827 64.786 1.00 36.30 ? 194 TYR A CG 1 ATOM 1473 C CD1 . TYR A 1 194 ? 62.518 8.334 64.567 1.00 35.95 ? 194 TYR A CD1 1 ATOM 1474 C CD2 . TYR A 1 194 ? 61.037 7.131 65.957 1.00 36.09 ? 194 TYR A CD2 1 ATOM 1475 C CE1 . TYR A 1 194 ? 63.551 8.203 65.476 1.00 34.49 ? 194 TYR A CE1 1 ATOM 1476 C CE2 . TYR A 1 194 ? 62.047 6.926 66.870 1.00 35.00 ? 194 TYR A CE2 1 ATOM 1477 C CZ . TYR A 1 194 ? 63.268 7.503 66.619 1.00 35.61 ? 194 TYR A CZ 1 ATOM 1478 O OH . TYR A 1 194 ? 64.299 7.373 67.532 1.00 37.27 ? 194 TYR A OH 1 ATOM 1479 N N . ARG A 1 195 ? 58.183 10.634 62.421 1.00 37.00 ? 195 ARG A N 1 ATOM 1480 C CA . ARG A 1 195 ? 57.176 10.941 61.448 1.00 35.80 ? 195 ARG A CA 1 ATOM 1481 C C . ARG A 1 195 ? 57.833 10.748 60.090 1.00 37.37 ? 195 ARG A C 1 ATOM 1482 O O . ARG A 1 195 ? 58.589 11.619 59.628 1.00 38.51 ? 195 ARG A O 1 ATOM 1483 C CB . ARG A 1 195 ? 56.657 12.353 61.570 1.00 32.56 ? 195 ARG A CB 1 ATOM 1484 C CG . ARG A 1 195 ? 55.228 12.504 61.086 1.00 30.31 ? 195 ARG A CG 1 ATOM 1485 C CD . ARG A 1 195 ? 54.725 13.911 61.205 1.00 29.56 ? 195 ARG A CD 1 ATOM 1486 N NE . ARG A 1 195 ? 55.784 14.900 61.000 1.00 32.83 ? 195 ARG A NE 1 ATOM 1487 C CZ . ARG A 1 195 ? 56.019 15.474 59.816 1.00 33.10 ? 195 ARG A CZ 1 ATOM 1488 N NH1 . ARG A 1 195 ? 57.021 16.344 59.820 1.00 34.97 ? 195 ARG A NH1 1 ATOM 1489 N NH2 . ARG A 1 195 ? 55.310 15.212 58.712 1.00 28.95 ? 195 ARG A NH2 1 ATOM 1490 N N . ILE A 1 196 ? 57.361 9.692 59.419 1.00 37.14 ? 196 ILE A N 1 ATOM 1491 C CA . ILE A 1 196 ? 58.070 9.268 58.213 1.00 35.81 ? 196 ILE A CA 1 ATOM 1492 C C . ILE A 1 196 ? 57.265 9.655 57.009 1.00 35.36 ? 196 ILE A C 1 ATOM 1493 O O . ILE A 1 196 ? 56.070 9.364 56.934 1.00 35.70 ? 196 ILE A O 1 ATOM 1494 C CB . ILE A 1 196 ? 58.325 7.745 58.272 1.00 34.39 ? 196 ILE A CB 1 ATOM 1495 C CG1 . ILE A 1 196 ? 59.500 7.523 59.241 1.00 31.66 ? 196 ILE A CG1 1 ATOM 1496 C CG2 . ILE A 1 196 ? 58.672 7.168 56.901 1.00 31.22 ? 196 ILE A CG2 1 ATOM 1497 C CD1 . ILE A 1 196 ? 59.334 6.378 60.176 1.00 29.09 ? 196 ILE A CD1 1 ATOM 1498 N N . THR A 1 197 ? 57.929 10.303 56.065 1.00 34.58 ? 197 THR A N 1 ATOM 1499 C CA . THR A 1 197 ? 57.139 10.672 54.881 1.00 33.89 ? 197 THR A CA 1 ATOM 1500 C C . THR A 1 197 ? 57.791 10.149 53.600 1.00 33.98 ? 197 THR A C 1 ATOM 1501 O O . THR A 1 197 ? 58.964 9.730 53.675 1.00 34.26 ? 197 THR A O 1 ATOM 1502 C CB . THR A 1 197 ? 56.893 12.166 54.722 1.00 30.93 ? 197 THR A CB 1 ATOM 1503 O OG1 . THR A 1 197 ? 58.033 12.949 54.663 1.00 28.68 ? 197 THR A OG1 1 ATOM 1504 C CG2 . THR A 1 197 ? 55.948 12.686 55.740 1.00 24.80 ? 197 THR A CG2 1 ATOM 1505 N N . HIS A 1 198 ? 57.002 10.126 52.533 1.00 32.99 ? 198 HIS A N 1 ATOM 1506 C CA . HIS A 1 198 ? 57.541 9.627 51.270 1.00 34.51 ? 198 HIS A CA 1 ATOM 1507 C C . HIS A 1 198 ? 57.278 10.567 50.082 1.00 35.68 ? 198 HIS A C 1 ATOM 1508 O O . HIS A 1 198 ? 56.145 10.861 49.667 1.00 35.25 ? 198 HIS A O 1 ATOM 1509 C CB . HIS A 1 198 ? 56.924 8.228 50.985 1.00 32.91 ? 198 HIS A CB 1 ATOM 1510 C CG . HIS A 1 198 ? 57.341 7.690 49.657 1.00 31.37 ? 198 HIS A CG 1 ATOM 1511 N ND1 . HIS A 1 198 ? 56.471 7.275 48.681 1.00 31.95 ? 198 HIS A ND1 1 ATOM 1512 C CD2 . HIS A 1 198 ? 58.601 7.592 49.139 1.00 31.50 ? 198 HIS A CD2 1 ATOM 1513 C CE1 . HIS A 1 198 ? 57.193 6.880 47.638 1.00 31.94 ? 198 HIS A CE1 1 ATOM 1514 N NE2 . HIS A 1 198 ? 58.478 7.092 47.872 1.00 30.42 ? 198 HIS A NE2 1 ATOM 1515 N N . THR A 1 199 ? 58.338 10.889 49.342 1.00 35.24 ? 199 THR A N 1 ATOM 1516 C CA . THR A 1 199 ? 58.298 11.767 48.198 1.00 36.50 ? 199 THR A CA 1 ATOM 1517 C C . THR A 1 199 ? 57.126 12.738 48.228 1.00 37.49 ? 199 THR A C 1 ATOM 1518 O O . THR A 1 199 ? 57.023 13.486 49.189 1.00 38.10 ? 199 THR A O 1 ATOM 1519 C CB . THR A 1 199 ? 58.257 10.968 46.858 1.00 31.90 ? 199 THR A CB 1 ATOM 1520 O OG1 . THR A 1 199 ? 57.313 9.918 47.082 1.00 30.15 ? 199 THR A OG1 1 ATOM 1521 C CG2 . THR A 1 199 ? 59.633 10.395 46.628 1.00 25.36 ? 199 THR A CG2 1 ATOM 1522 N N . ASN A 1 200 ? 56.220 12.676 47.261 1.00 38.28 ? 200 ASN A N 1 ATOM 1523 C CA . ASN A 1 200 ? 55.077 13.562 47.188 1.00 38.96 ? 200 ASN A CA 1 ATOM 1524 C C . ASN A 1 200 ? 53.820 12.930 47.713 1.00 38.46 ? 200 ASN A C 1 ATOM 1525 O O . ASN A 1 200 ? 52.735 13.229 47.213 1.00 39.42 ? 200 ASN A O 1 ATOM 1526 C CB . ASN A 1 200 ? 54.892 14.163 45.786 1.00 45.97 ? 200 ASN A CB 1 ATOM 1527 C CG . ASN A 1 200 ? 54.534 13.211 44.667 1.00 53.54 ? 200 ASN A CG 1 ATOM 1528 O OD1 . ASN A 1 200 ? 54.848 12.000 44.769 1.00 56.55 ? 200 ASN A OD1 1 ATOM 1529 N ND2 . ASN A 1 200 ? 53.904 13.650 43.559 1.00 53.86 ? 200 ASN A ND2 1 ATOM 1530 N N . ASP A 1 201 ? 53.879 12.049 48.697 1.00 38.25 ? 201 ASP A N 1 ATOM 1531 C CA . ASP A 1 201 ? 52.648 11.473 49.262 1.00 37.91 ? 201 ASP A CA 1 ATOM 1532 C C . ASP A 1 201 ? 51.716 12.641 49.593 1.00 39.32 ? 201 ASP A C 1 ATOM 1533 O O . ASP A 1 201 ? 52.143 13.725 50.009 1.00 38.88 ? 201 ASP A O 1 ATOM 1534 C CB . ASP A 1 201 ? 53.006 10.641 50.458 1.00 35.79 ? 201 ASP A CB 1 ATOM 1535 C CG . ASP A 1 201 ? 51.944 9.984 51.300 1.00 34.09 ? 201 ASP A CG 1 ATOM 1536 O OD1 . ASP A 1 201 ? 50.754 10.043 50.917 1.00 36.31 ? 201 ASP A OD1 1 ATOM 1537 O OD2 . ASP A 1 201 ? 52.282 9.366 52.331 1.00 26.13 ? 201 ASP A OD2 1 ATOM 1538 N N . ILE A 1 202 ? 50.432 12.463 49.302 1.00 39.99 ? 202 ILE A N 1 ATOM 1539 C CA . ILE A 1 202 ? 49.386 13.433 49.517 1.00 39.94 ? 202 ILE A CA 1 ATOM 1540 C C . ILE A 1 202 ? 48.892 13.447 50.958 1.00 40.92 ? 202 ILE A C 1 ATOM 1541 O O . ILE A 1 202 ? 48.577 14.543 51.431 1.00 40.88 ? 202 ILE A O 1 ATOM 1542 C CB . ILE A 1 202 ? 48.175 13.193 48.590 1.00 37.80 ? 202 ILE A CB 1 ATOM 1543 C CG1 . ILE A 1 202 ? 47.123 14.306 48.696 1.00 37.82 ? 202 ILE A CG1 1 ATOM 1544 C CG2 . ILE A 1 202 ? 47.486 11.860 48.871 1.00 35.60 ? 202 ILE A CG2 1 ATOM 1545 C CD1 . ILE A 1 202 ? 45.955 14.208 47.713 1.00 33.20 ? 202 ILE A CD1 1 ATOM 1546 N N . VAL A 1 203 ? 48.879 12.315 51.678 1.00 40.94 ? 203 VAL A N 1 ATOM 1547 C CA . VAL A 1 203 ? 48.279 12.301 53.001 1.00 40.57 ? 203 VAL A CA 1 ATOM 1548 C C . VAL A 1 203 ? 48.893 13.280 53.980 1.00 40.78 ? 203 VAL A C 1 ATOM 1549 O O . VAL A 1 203 ? 48.111 14.111 54.434 1.00 39.16 ? 203 VAL A O 1 ATOM 1550 C CB . VAL A 1 203 ? 47.934 10.926 53.583 1.00 41.48 ? 203 VAL A CB 1 ATOM 1551 C CG1 . VAL A 1 203 ? 47.154 11.090 54.920 1.00 40.01 ? 203 VAL A CG1 1 ATOM 1552 C CG2 . VAL A 1 203 ? 47.130 10.112 52.562 1.00 38.68 ? 203 VAL A CG2 1 ATOM 1553 N N . PRO A 1 204 ? 50.210 13.455 54.031 1.00 41.22 ? 204 PRO A N 1 ATOM 1554 C CA . PRO A 1 204 ? 50.887 14.382 54.884 1.00 41.96 ? 204 PRO A CA 1 ATOM 1555 C C . PRO A 1 204 ? 50.613 15.823 54.596 1.00 42.62 ? 204 PRO A C 1 ATOM 1556 O O . PRO A 1 204 ? 51.359 16.655 55.131 1.00 43.65 ? 204 PRO A O 1 ATOM 1557 C CB . PRO A 1 204 ? 52.399 14.166 54.671 1.00 42.28 ? 204 PRO A CB 1 ATOM 1558 C CG . PRO A 1 204 ? 52.356 12.682 54.418 1.00 43.19 ? 204 PRO A CG 1 ATOM 1559 C CD . PRO A 1 204 ? 51.117 12.374 53.636 1.00 41.84 ? 204 PRO A CD 1 ATOM 1560 N N . ARG A 1 205 ? 49.952 16.134 53.517 1.00 43.23 ? 205 ARG A N 1 ATOM 1561 C CA . ARG A 1 205 ? 49.673 17.481 53.007 1.00 42.51 ? 205 ARG A CA 1 ATOM 1562 C C . ARG A 1 205 ? 48.284 17.837 53.495 1.00 42.50 ? 205 ARG A C 1 ATOM 1563 O O . ARG A 1 205 ? 47.649 18.856 53.343 1.00 44.45 ? 205 ARG A O 1 ATOM 1564 C CB . ARG A 1 205 ? 49.779 17.274 51.506 1.00 39.78 ? 205 ARG A CB 1 ATOM 1565 C CG . ARG A 1 205 ? 50.844 17.840 50.665 1.00 40.75 ? 205 ARG A CG 1 ATOM 1566 C CD . ARG A 1 205 ? 52.165 17.243 50.351 1.00 39.38 ? 205 ARG A CD 1 ATOM 1567 N NE . ARG A 1 205 ? 52.641 17.536 49.049 1.00 37.59 ? 205 ARG A NE 1 ATOM 1568 C CZ . ARG A 1 205 ? 53.535 17.546 48.121 1.00 40.44 ? 205 ARG A CZ 1 ATOM 1569 N NH1 . ARG A 1 205 ? 54.778 17.077 48.237 1.00 43.05 ? 205 ARG A NH1 1 ATOM 1570 N NH2 . ARG A 1 205 ? 53.263 18.043 46.909 1.00 37.80 ? 205 ARG A NH2 1 ATOM 1571 N N . LEU A 1 206 ? 47.682 16.905 54.176 1.00 42.35 ? 206 LEU A N 1 ATOM 1572 C CA . LEU A 1 206 ? 46.353 17.023 54.730 1.00 42.77 ? 206 LEU A CA 1 ATOM 1573 C C . LEU A 1 206 ? 46.261 16.734 56.230 1.00 42.47 ? 206 LEU A C 1 ATOM 1574 O O . LEU A 1 206 ? 46.980 15.862 56.732 1.00 42.82 ? 206 LEU A O 1 ATOM 1575 C CB . LEU A 1 206 ? 45.544 15.929 54.012 1.00 43.92 ? 206 LEU A CB 1 ATOM 1576 C CG . LEU A 1 206 ? 45.189 16.091 52.546 1.00 45.35 ? 206 LEU A CG 1 ATOM 1577 C CD1 . LEU A 1 206 ? 44.209 14.975 52.160 1.00 43.58 ? 206 LEU A CD1 1 ATOM 1578 C CD2 . LEU A 1 206 ? 44.659 17.495 52.286 1.00 44.95 ? 206 LEU A CD2 1 ATOM 1579 N N . PRO A 1 207 ? 45.417 17.415 56.963 1.00 41.64 ? 207 PRO A N 1 ATOM 1580 C CA . PRO A 1 207 ? 44.705 18.552 56.442 1.00 41.86 ? 207 PRO A CA 1 ATOM 1581 C C . PRO A 1 207 ? 45.667 19.709 56.228 1.00 42.04 ? 207 PRO A C 1 ATOM 1582 O O . PRO A 1 207 ? 46.876 19.534 56.469 1.00 40.79 ? 207 PRO A O 1 ATOM 1583 C CB . PRO A 1 207 ? 43.689 18.909 57.523 1.00 42.24 ? 207 PRO A CB 1 ATOM 1584 C CG . PRO A 1 207 ? 43.591 17.642 58.323 1.00 42.60 ? 207 PRO A CG 1 ATOM 1585 C CD . PRO A 1 207 ? 45.049 17.193 58.372 1.00 41.79 ? 207 PRO A CD 1 ATOM 1586 N N . PRO A 1 208 ? 45.290 20.591 55.292 1.00 42.54 ? 208 PRO A N 1 ATOM 1587 C CA . PRO A 1 208 ? 46.104 21.734 54.920 1.00 42.34 ? 208 PRO A CA 1 ATOM 1588 C C . PRO A 1 208 ? 46.427 22.612 56.100 1.00 42.80 ? 208 PRO A C 1 ATOM 1589 O O . PRO A 1 208 ? 45.570 22.755 56.988 1.00 43.58 ? 208 PRO A O 1 ATOM 1590 C CB . PRO A 1 208 ? 45.161 22.523 54.014 1.00 42.14 ? 208 PRO A CB 1 ATOM 1591 C CG . PRO A 1 208 ? 44.147 21.583 53.483 1.00 41.24 ? 208 PRO A CG 1 ATOM 1592 C CD . PRO A 1 208 ? 43.994 20.535 54.541 1.00 42.28 ? 208 PRO A CD 1 ATOM 1593 N N . ARG A 1 209 ? 47.563 23.263 56.119 1.00 43.00 ? 209 ARG A N 1 ATOM 1594 C CA . ARG A 1 209 ? 47.873 24.317 57.063 1.00 44.05 ? 209 ARG A CA 1 ATOM 1595 C C . ARG A 1 209 ? 46.847 25.433 57.099 1.00 44.76 ? 209 ARG A C 1 ATOM 1596 O O . ARG A 1 209 ? 46.342 25.890 58.144 1.00 45.31 ? 209 ARG A O 1 ATOM 1597 C CB . ARG A 1 209 ? 49.205 24.949 56.615 1.00 45.20 ? 209 ARG A CB 1 ATOM 1598 C CG . ARG A 1 209 ? 50.318 23.908 56.758 1.00 49.55 ? 209 ARG A CG 1 ATOM 1599 C CD . ARG A 1 209 ? 51.656 24.555 56.570 1.00 53.18 ? 209 ARG A CD 1 ATOM 1600 N NE . ARG A 1 209 ? 52.025 25.602 57.471 1.00 62.28 ? 209 ARG A NE 1 ATOM 1601 C CZ . ARG A 1 209 ? 51.657 26.128 58.627 1.00 65.44 ? 209 ARG A CZ 1 ATOM 1602 N NH1 . ARG A 1 209 ? 50.637 25.697 59.375 1.00 63.93 ? 209 ARG A NH1 1 ATOM 1603 N NH2 . ARG A 1 209 ? 52.366 27.157 59.127 1.00 66.26 ? 209 ARG A NH2 1 ATOM 1604 N N . GLU A 1 210 ? 46.347 25.884 55.960 1.00 44.91 ? 210 GLU A N 1 ATOM 1605 C CA . GLU A 1 210 ? 45.321 26.912 55.862 1.00 45.34 ? 210 GLU A CA 1 ATOM 1606 C C . GLU A 1 210 ? 44.158 26.640 56.801 1.00 45.41 ? 210 GLU A C 1 ATOM 1607 O O . GLU A 1 210 ? 43.662 27.628 57.342 1.00 45.44 ? 210 GLU A O 1 ATOM 1608 C CB . GLU A 1 210 ? 44.861 27.060 54.420 1.00 45.77 ? 210 GLU A CB 1 ATOM 1609 C CG . GLU A 1 210 ? 45.941 27.597 53.500 1.00 48.40 ? 210 GLU A CG 1 ATOM 1610 C CD . GLU A 1 210 ? 46.970 26.596 53.018 1.00 49.14 ? 210 GLU A CD 1 ATOM 1611 O OE1 . GLU A 1 210 ? 48.050 27.002 52.552 1.00 51.59 ? 210 GLU A OE1 1 ATOM 1612 O OE2 . GLU A 1 210 ? 46.750 25.367 53.108 1.00 50.40 ? 210 GLU A OE2 1 ATOM 1613 N N . PHE A 1 211 ? 43.845 25.401 57.181 1.00 44.68 ? 211 PHE A N 1 ATOM 1614 C CA . PHE A 1 211 ? 42.804 25.158 58.149 1.00 44.65 ? 211 PHE A CA 1 ATOM 1615 C C . PHE A 1 211 ? 43.273 25.064 59.594 1.00 45.12 ? 211 PHE A C 1 ATOM 1616 O O . PHE A 1 211 ? 42.543 24.533 60.438 1.00 45.18 ? 211 PHE A O 1 ATOM 1617 C CB . PHE A 1 211 ? 42.008 23.910 57.791 1.00 44.19 ? 211 PHE A CB 1 ATOM 1618 C CG . PHE A 1 211 ? 41.217 24.110 56.535 1.00 46.60 ? 211 PHE A CG 1 ATOM 1619 C CD1 . PHE A 1 211 ? 41.752 23.871 55.281 1.00 47.62 ? 211 PHE A CD1 1 ATOM 1620 C CD2 . PHE A 1 211 ? 39.897 24.524 56.608 1.00 43.56 ? 211 PHE A CD2 1 ATOM 1621 C CE1 . PHE A 1 211 ? 40.983 24.058 54.132 1.00 48.50 ? 211 PHE A CE1 1 ATOM 1622 C CE2 . PHE A 1 211 ? 39.148 24.708 55.463 1.00 45.78 ? 211 PHE A CE2 1 ATOM 1623 C CZ . PHE A 1 211 ? 39.677 24.480 54.215 1.00 46.98 ? 211 PHE A CZ 1 ATOM 1624 N N . GLY A 1 212 ? 44.429 25.615 59.942 1.00 44.75 ? 212 GLY A N 1 ATOM 1625 C CA . GLY A 1 212 ? 44.946 25.687 61.277 1.00 43.92 ? 212 GLY A CA 1 ATOM 1626 C C . GLY A 1 212 ? 45.839 24.522 61.673 1.00 44.59 ? 212 GLY A C 1 ATOM 1627 O O . GLY A 1 212 ? 45.968 24.257 62.882 1.00 43.92 ? 212 GLY A O 1 ATOM 1628 N N . TYR A 1 213 ? 46.337 23.760 60.682 1.00 44.30 ? 213 TYR A N 1 ATOM 1629 C CA . TYR A 1 213 ? 47.126 22.592 61.008 1.00 44.21 ? 213 TYR A CA 1 ATOM 1630 C C . TYR A 1 213 ? 48.626 22.742 60.806 1.00 43.87 ? 213 TYR A C 1 ATOM 1631 O O . TYR A 1 213 ? 49.119 23.369 59.874 1.00 44.51 ? 213 TYR A O 1 ATOM 1632 C CB . TYR A 1 213 ? 46.708 21.329 60.286 1.00 44.05 ? 213 TYR A CB 1 ATOM 1633 C CG . TYR A 1 213 ? 45.359 20.794 60.680 1.00 43.77 ? 213 TYR A CG 1 ATOM 1634 C CD1 . TYR A 1 213 ? 44.230 21.422 60.166 1.00 43.76 ? 213 TYR A CD1 1 ATOM 1635 C CD2 . TYR A 1 213 ? 45.189 19.697 61.510 1.00 42.62 ? 213 TYR A CD2 1 ATOM 1636 C CE1 . TYR A 1 213 ? 42.972 20.928 60.467 1.00 42.61 ? 213 TYR A CE1 1 ATOM 1637 C CE2 . TYR A 1 213 ? 43.938 19.200 61.800 1.00 41.59 ? 213 TYR A CE2 1 ATOM 1638 C CZ . TYR A 1 213 ? 42.838 19.835 61.278 1.00 41.73 ? 213 TYR A CZ 1 ATOM 1639 O OH . TYR A 1 213 ? 41.559 19.411 61.543 1.00 42.33 ? 213 TYR A OH 1 ATOM 1640 N N . SER A 1 214 ? 49.328 22.021 61.668 1.00 42.63 ? 214 SER A N 1 ATOM 1641 C CA . SER A 1 214 ? 50.783 22.068 61.656 1.00 42.04 ? 214 SER A CA 1 ATOM 1642 C C . SER A 1 214 ? 51.326 20.645 61.791 1.00 40.55 ? 214 SER A C 1 ATOM 1643 O O . SER A 1 214 ? 50.620 19.771 62.286 1.00 40.42 ? 214 SER A O 1 ATOM 1644 C CB . SER A 1 214 ? 51.224 22.890 62.884 1.00 43.70 ? 214 SER A CB 1 ATOM 1645 O OG . SER A 1 214 ? 51.782 24.130 62.492 1.00 47.26 ? 214 SER A OG 1 ATOM 1646 N N . HIS A 1 215 ? 52.560 20.446 61.382 1.00 39.23 ? 215 HIS A N 1 ATOM 1647 C CA . HIS A 1 215 ? 53.235 19.187 61.568 1.00 38.45 ? 215 HIS A CA 1 ATOM 1648 C C . HIS A 1 215 ? 54.275 19.284 62.687 1.00 37.84 ? 215 HIS A C 1 ATOM 1649 O O . HIS A 1 215 ? 55.107 20.190 62.697 1.00 37.70 ? 215 HIS A O 1 ATOM 1650 C CB . HIS A 1 215 ? 53.917 18.702 60.289 1.00 38.74 ? 215 HIS A CB 1 ATOM 1651 C CG . HIS A 1 215 ? 53.156 17.731 59.451 1.00 39.43 ? 215 HIS A CG 1 ATOM 1652 N ND1 . HIS A 1 215 ? 52.396 16.705 60.000 1.00 39.41 ? 215 HIS A ND1 1 ATOM 1653 C CD2 . HIS A 1 215 ? 53.115 17.556 58.101 1.00 37.87 ? 215 HIS A CD2 1 ATOM 1654 C CE1 . HIS A 1 215 ? 51.891 15.963 59.039 1.00 37.80 ? 215 HIS A CE1 1 ATOM 1655 N NE2 . HIS A 1 215 ? 52.338 16.450 57.869 1.00 38.20 ? 215 HIS A NE2 1 ATOM 1656 N N . SER A 1 216 ? 54.426 18.176 63.388 1.00 37.89 ? 216 SER A N 1 ATOM 1657 C CA . SER A 1 216 ? 55.486 17.904 64.344 1.00 38.02 ? 216 SER A CA 1 ATOM 1658 C C . SER A 1 216 ? 56.832 18.114 63.663 1.00 37.15 ? 216 SER A C 1 ATOM 1659 O O . SER A 1 216 ? 56.947 17.798 62.487 1.00 37.13 ? 216 SER A O 1 ATOM 1660 C CB . SER A 1 216 ? 55.320 16.404 64.770 1.00 39.61 ? 216 SER A CB 1 ATOM 1661 O OG . SER A 1 216 ? 56.382 15.669 64.022 1.00 50.59 ? 216 SER A OG 1 ATOM 1662 N N . SER A 1 217 ? 57.922 18.138 64.396 1.00 37.76 ? 217 SER A N 1 ATOM 1663 C CA . SER A 1 217 ? 59.292 18.117 63.835 1.00 37.70 ? 217 SER A CA 1 ATOM 1664 C C . SER A 1 217 ? 60.143 17.155 64.668 1.00 36.88 ? 217 SER A C 1 ATOM 1665 O O . SER A 1 217 ? 59.832 17.122 65.821 1.00 37.83 ? 217 SER A O 1 ATOM 1666 C CB . SER A 1 217 ? 59.894 19.511 63.924 1.00 36.53 ? 217 SER A CB 1 ATOM 1667 O OG . SER A 1 217 ? 61.149 19.529 63.305 1.00 35.66 ? 217 SER A OG 1 ATOM 1668 N N . PRO A 1 218 ? 61.070 16.362 64.178 1.00 36.34 ? 218 PRO A N 1 ATOM 1669 C CA . PRO A 1 218 ? 61.372 16.472 62.734 1.00 36.86 ? 218 PRO A CA 1 ATOM 1670 C C . PRO A 1 218 ? 60.616 15.569 61.789 1.00 37.50 ? 218 PRO A C 1 ATOM 1671 O O . PRO A 1 218 ? 59.654 14.914 62.168 1.00 38.65 ? 218 PRO A O 1 ATOM 1672 C CB . PRO A 1 218 ? 62.848 16.084 62.725 1.00 36.93 ? 218 PRO A CB 1 ATOM 1673 C CG . PRO A 1 218 ? 62.952 15.083 63.851 1.00 35.92 ? 218 PRO A CG 1 ATOM 1674 C CD . PRO A 1 218 ? 61.842 15.336 64.834 1.00 34.53 ? 218 PRO A CD 1 ATOM 1675 N N . GLU A 1 219 ? 61.007 15.553 60.512 1.00 38.01 ? 219 GLU A N 1 ATOM 1676 C CA . GLU A 1 219 ? 60.404 14.732 59.479 1.00 37.20 ? 219 GLU A CA 1 ATOM 1677 C C . GLU A 1 219 ? 61.428 13.802 58.837 1.00 36.09 ? 219 GLU A C 1 ATOM 1678 O O . GLU A 1 219 ? 62.566 14.252 58.691 1.00 35.79 ? 219 GLU A O 1 ATOM 1679 C CB . GLU A 1 219 ? 59.723 15.614 58.441 1.00 37.90 ? 219 GLU A CB 1 ATOM 1680 C CG . GLU A 1 219 ? 59.319 14.895 57.149 1.00 37.39 ? 219 GLU A CG 1 ATOM 1681 C CD . GLU A 1 219 ? 58.910 15.819 56.035 1.00 38.56 ? 219 GLU A CD 1 ATOM 1682 O OE1 . GLU A 1 219 ? 58.998 17.050 56.171 1.00 40.30 ? 219 GLU A OE1 1 ATOM 1683 O OE2 . GLU A 1 219 ? 58.395 15.430 54.963 1.00 40.45 ? 219 GLU A OE2 1 ATOM 1684 N N . TYR A 1 220 ? 61.099 12.538 58.624 1.00 35.50 ? 220 TYR A N 1 ATOM 1685 C CA . TYR A 1 220 ? 62.050 11.646 57.942 1.00 36.20 ? 220 TYR A CA 1 ATOM 1686 C C . TYR A 1 220 ? 61.574 11.334 56.530 1.00 36.43 ? 220 TYR A C 1 ATOM 1687 O O . TYR A 1 220 ? 60.539 10.682 56.362 1.00 36.65 ? 220 TYR A O 1 ATOM 1688 C CB . TYR A 1 220 ? 62.278 10.313 58.663 1.00 36.54 ? 220 TYR A CB 1 ATOM 1689 C CG . TYR A 1 220 ? 63.045 10.559 59.944 1.00 37.86 ? 220 TYR A CG 1 ATOM 1690 C CD1 . TYR A 1 220 ? 64.430 10.594 59.972 1.00 37.85 ? 220 TYR A CD1 1 ATOM 1691 C CD2 . TYR A 1 220 ? 62.312 10.824 61.112 1.00 38.05 ? 220 TYR A CD2 1 ATOM 1692 C CE1 . TYR A 1 220 ? 65.080 10.922 61.147 1.00 38.56 ? 220 TYR A CE1 1 ATOM 1693 C CE2 . TYR A 1 220 ? 62.961 11.082 62.301 1.00 37.64 ? 220 TYR A CE2 1 ATOM 1694 C CZ . TYR A 1 220 ? 64.332 11.128 62.295 1.00 39.51 ? 220 TYR A CZ 1 ATOM 1695 O OH . TYR A 1 220 ? 64.987 11.404 63.483 1.00 43.11 ? 220 TYR A OH 1 ATOM 1696 N N . TRP A 1 221 ? 62.090 12.094 55.577 1.00 36.55 ? 221 TRP A N 1 ATOM 1697 C CA . TRP A 1 221 ? 61.650 11.978 54.190 1.00 36.54 ? 221 TRP A CA 1 ATOM 1698 C C . TRP A 1 221 ? 62.312 10.968 53.250 1.00 36.73 ? 221 TRP A C 1 ATOM 1699 O O . TRP A 1 221 ? 63.519 11.073 52.931 1.00 36.53 ? 221 TRP A O 1 ATOM 1700 C CB . TRP A 1 221 ? 61.850 13.354 53.541 1.00 29.96 ? 221 TRP A CB 1 ATOM 1701 C CG . TRP A 1 221 ? 61.167 13.526 52.220 1.00 25.13 ? 221 TRP A CG 1 ATOM 1702 C CD1 . TRP A 1 221 ? 59.854 13.228 51.954 1.00 19.56 ? 221 TRP A CD1 1 ATOM 1703 C CD2 . TRP A 1 221 ? 61.725 14.174 51.072 1.00 20.84 ? 221 TRP A CD2 1 ATOM 1704 N NE1 . TRP A 1 221 ? 59.601 13.612 50.660 1.00 23.57 ? 221 TRP A NE1 1 ATOM 1705 C CE2 . TRP A 1 221 ? 60.722 14.193 50.101 1.00 22.54 ? 221 TRP A CE2 1 ATOM 1706 C CE3 . TRP A 1 221 ? 62.940 14.746 50.770 1.00 25.31 ? 221 TRP A CE3 1 ATOM 1707 C CZ2 . TRP A 1 221 ? 60.912 14.717 48.825 1.00 25.38 ? 221 TRP A CZ2 1 ATOM 1708 C CZ3 . TRP A 1 221 ? 63.170 15.255 49.467 1.00 28.48 ? 221 TRP A CZ3 1 ATOM 1709 C CH2 . TRP A 1 221 ? 62.144 15.247 48.506 1.00 24.82 ? 221 TRP A CH2 1 ATOM 1710 N N . ILE A 1 222 ? 61.525 10.014 52.732 1.00 36.63 ? 222 ILE A N 1 ATOM 1711 C CA . ILE A 1 222 ? 62.110 8.992 51.815 1.00 36.07 ? 222 ILE A CA 1 ATOM 1712 C C . ILE A 1 222 ? 62.137 9.542 50.401 1.00 36.25 ? 222 ILE A C 1 ATOM 1713 O O . ILE A 1 222 ? 61.066 9.974 49.931 1.00 37.56 ? 222 ILE A O 1 ATOM 1714 C CB . ILE A 1 222 ? 61.225 7.725 51.870 1.00 32.96 ? 222 ILE A CB 1 ATOM 1715 C CG1 . ILE A 1 222 ? 61.199 7.167 53.280 1.00 31.11 ? 222 ILE A CG1 1 ATOM 1716 C CG2 . ILE A 1 222 ? 61.639 6.661 50.859 1.00 32.80 ? 222 ILE A CG2 1 ATOM 1717 C CD1 . ILE A 1 222 ? 60.057 6.242 53.594 1.00 28.29 ? 222 ILE A CD1 1 ATOM 1718 N N . LYS A 1 223 ? 63.230 9.623 49.680 1.00 36.17 ? 223 LYS A N 1 ATOM 1719 C CA . LYS A 1 223 ? 63.210 10.242 48.357 1.00 36.60 ? 223 LYS A CA 1 ATOM 1720 C C . LYS A 1 223 ? 63.070 9.209 47.239 1.00 36.22 ? 223 LYS A C 1 ATOM 1721 O O . LYS A 1 223 ? 62.845 9.587 46.076 1.00 38.02 ? 223 LYS A O 1 ATOM 1722 C CB . LYS A 1 223 ? 64.519 10.948 48.042 1.00 41.42 ? 223 LYS A CB 1 ATOM 1723 C CG . LYS A 1 223 ? 65.182 11.804 49.097 1.00 46.84 ? 223 LYS A CG 1 ATOM 1724 C CD . LYS A 1 223 ? 66.497 12.381 48.564 1.00 50.93 ? 223 LYS A CD 1 ATOM 1725 C CE . LYS A 1 223 ? 67.597 11.304 48.569 1.00 53.86 ? 223 LYS A CE 1 ATOM 1726 N NZ . LYS A 1 223 ? 68.924 11.923 48.926 1.00 56.32 ? 223 LYS A NZ 1 ATOM 1727 N N . SER A 1 224 ? 63.403 7.965 47.453 1.00 33.99 ? 224 SER A N 1 ATOM 1728 C CA . SER A 1 224 ? 63.297 6.992 46.384 1.00 33.49 ? 224 SER A CA 1 ATOM 1729 C C . SER A 1 224 ? 61.845 6.985 45.962 1.00 34.17 ? 224 SER A C 1 ATOM 1730 O O . SER A 1 224 ? 60.945 7.353 46.725 1.00 33.66 ? 224 SER A O 1 ATOM 1731 C CB . SER A 1 224 ? 63.895 5.678 46.843 1.00 31.92 ? 224 SER A CB 1 ATOM 1732 O OG . SER A 1 224 ? 63.879 5.593 48.250 1.00 33.65 ? 224 SER A OG 1 ATOM 1733 N N . GLY A 1 225 ? 61.590 6.548 44.742 1.00 35.15 ? 225 GLY A N 1 ATOM 1734 C CA . GLY A 1 225 ? 60.300 6.638 44.123 1.00 35.93 ? 225 GLY A CA 1 ATOM 1735 C C . GLY A 1 225 ? 59.347 5.530 44.483 1.00 37.62 ? 225 GLY A C 1 ATOM 1736 O O . GLY A 1 225 ? 59.767 4.591 45.175 1.00 39.53 ? 225 GLY A O 1 ATOM 1737 N N . THR A 1 226 ? 58.117 5.623 43.965 1.00 37.30 ? 226 THR A N 1 ATOM 1738 C CA . THR A 1 226 ? 57.173 4.539 44.140 1.00 36.58 ? 226 THR A CA 1 ATOM 1739 C C . THR A 1 226 ? 57.727 3.240 43.578 1.00 36.26 ? 226 THR A C 1 ATOM 1740 O O . THR A 1 226 ? 58.347 3.202 42.512 1.00 35.90 ? 226 THR A O 1 ATOM 1741 C CB . THR A 1 226 ? 55.828 4.835 43.440 1.00 34.26 ? 226 THR A CB 1 ATOM 1742 O OG1 . THR A 1 226 ? 55.368 5.990 44.124 1.00 39.82 ? 226 THR A OG1 1 ATOM 1743 C CG2 . THR A 1 226 ? 54.826 3.753 43.762 1.00 35.92 ? 226 THR A CG2 1 ATOM 1744 N N . LEU A 1 227 ? 57.538 2.165 44.335 1.00 35.58 ? 227 LEU A N 1 ATOM 1745 C CA . LEU A 1 227 ? 58.043 0.891 43.854 1.00 36.00 ? 227 LEU A CA 1 ATOM 1746 C C . LEU A 1 227 ? 59.547 0.909 43.750 1.00 36.14 ? 227 LEU A C 1 ATOM 1747 O O . LEU A 1 227 ? 60.064 -0.068 43.172 1.00 36.98 ? 227 LEU A O 1 ATOM 1748 C CB . LEU A 1 227 ? 57.345 0.496 42.544 1.00 34.85 ? 227 LEU A CB 1 ATOM 1749 C CG . LEU A 1 227 ? 55.842 0.192 42.715 1.00 36.78 ? 227 LEU A CG 1 ATOM 1750 C CD1 . LEU A 1 227 ? 55.062 0.592 41.485 1.00 37.96 ? 227 LEU A CD1 1 ATOM 1751 C CD2 . LEU A 1 227 ? 55.639 -1.271 43.093 1.00 36.33 ? 227 LEU A CD2 1 ATOM 1752 N N . VAL A 1 228 ? 60.286 1.784 44.422 1.00 35.86 ? 228 VAL A N 1 ATOM 1753 C CA . VAL A 1 228 ? 61.740 1.651 44.485 1.00 36.10 ? 228 VAL A CA 1 ATOM 1754 C C . VAL A 1 228 ? 62.207 1.215 45.857 1.00 36.85 ? 228 VAL A C 1 ATOM 1755 O O . VAL A 1 228 ? 61.711 1.613 46.892 1.00 37.72 ? 228 VAL A O 1 ATOM 1756 C CB . VAL A 1 228 ? 62.431 2.977 44.147 1.00 36.47 ? 228 VAL A CB 1 ATOM 1757 C CG1 . VAL A 1 228 ? 63.960 2.825 44.136 1.00 30.02 ? 228 VAL A CG1 1 ATOM 1758 C CG2 . VAL A 1 228 ? 61.883 3.413 42.764 1.00 36.58 ? 228 VAL A CG2 1 ATOM 1759 N N . PRO A 1 229 ? 63.082 0.227 45.937 1.00 38.10 ? 229 PRO A N 1 ATOM 1760 C CA . PRO A 1 229 ? 63.607 -0.219 47.232 1.00 37.69 ? 229 PRO A CA 1 ATOM 1761 C C . PRO A 1 229 ? 64.125 0.995 47.998 1.00 37.69 ? 229 PRO A C 1 ATOM 1762 O O . PRO A 1 229 ? 64.622 1.918 47.359 1.00 35.88 ? 229 PRO A O 1 ATOM 1763 C CB . PRO A 1 229 ? 64.792 -1.102 46.880 1.00 36.62 ? 229 PRO A CB 1 ATOM 1764 C CG . PRO A 1 229 ? 64.586 -1.478 45.475 1.00 36.62 ? 229 PRO A CG 1 ATOM 1765 C CD . PRO A 1 229 ? 63.684 -0.498 44.780 1.00 36.80 ? 229 PRO A CD 1 ATOM 1766 N N . VAL A 1 230 ? 64.052 0.950 49.346 1.00 38.11 ? 230 VAL A N 1 ATOM 1767 C CA . VAL A 1 230 ? 64.587 2.098 50.079 1.00 37.78 ? 230 VAL A CA 1 ATOM 1768 C C . VAL A 1 230 ? 65.924 1.721 50.719 1.00 37.85 ? 230 VAL A C 1 ATOM 1769 O O . VAL A 1 230 ? 66.050 0.543 51.024 1.00 36.89 ? 230 VAL A O 1 ATOM 1770 C CB . VAL A 1 230 ? 63.597 2.551 51.155 1.00 37.71 ? 230 VAL A CB 1 ATOM 1771 C CG1 . VAL A 1 230 ? 64.153 3.737 51.927 1.00 35.23 ? 230 VAL A CG1 1 ATOM 1772 C CG2 . VAL A 1 230 ? 62.219 2.786 50.611 1.00 34.85 ? 230 VAL A CG2 1 ATOM 1773 N N . THR A 1 231 ? 66.944 2.572 50.736 1.00 37.98 ? 231 THR A N 1 ATOM 1774 C CA . THR A 1 231 ? 68.129 2.248 51.510 1.00 39.72 ? 231 THR A CA 1 ATOM 1775 C C . THR A 1 231 ? 68.361 3.349 52.562 1.00 41.23 ? 231 THR A C 1 ATOM 1776 O O . THR A 1 231 ? 67.834 4.454 52.445 1.00 41.36 ? 231 THR A O 1 ATOM 1777 C CB . THR A 1 231 ? 69.479 2.185 50.779 1.00 35.61 ? 231 THR A CB 1 ATOM 1778 O OG1 . THR A 1 231 ? 69.698 3.581 50.504 1.00 41.74 ? 231 THR A OG1 1 ATOM 1779 C CG2 . THR A 1 231 ? 69.470 1.396 49.499 1.00 34.29 ? 231 THR A CG2 1 ATOM 1780 N N . ARG A 1 232 ? 69.319 3.113 53.473 1.00 42.09 ? 232 ARG A N 1 ATOM 1781 C CA . ARG A 1 232 ? 69.692 4.195 54.357 1.00 42.75 ? 232 ARG A CA 1 ATOM 1782 C C . ARG A 1 232 ? 70.125 5.478 53.655 1.00 43.00 ? 232 ARG A C 1 ATOM 1783 O O . ARG A 1 232 ? 69.906 6.517 54.284 1.00 42.81 ? 232 ARG A O 1 ATOM 1784 C CB . ARG A 1 232 ? 70.691 3.810 55.404 1.00 43.70 ? 232 ARG A CB 1 ATOM 1785 C CG . ARG A 1 232 ? 71.831 2.897 55.192 1.00 48.19 ? 232 ARG A CG 1 ATOM 1786 C CD . ARG A 1 232 ? 73.108 3.548 54.821 1.00 51.25 ? 232 ARG A CD 1 ATOM 1787 N NE . ARG A 1 232 ? 73.572 4.461 55.845 1.00 59.57 ? 232 ARG A NE 1 ATOM 1788 C CZ . ARG A 1 232 ? 74.864 4.535 56.240 1.00 62.22 ? 232 ARG A CZ 1 ATOM 1789 N NH1 . ARG A 1 232 ? 75.856 3.822 55.722 1.00 58.30 ? 232 ARG A NH1 1 ATOM 1790 N NH2 . ARG A 1 232 ? 75.058 5.431 57.230 1.00 62.16 ? 232 ARG A NH2 1 ATOM 1791 N N . ASN A 1 233 ? 70.575 5.553 52.414 1.00 43.24 ? 233 ASN A N 1 ATOM 1792 C CA . ASN A 1 233 ? 70.949 6.799 51.786 1.00 43.92 ? 233 ASN A CA 1 ATOM 1793 C C . ASN A 1 233 ? 69.773 7.525 51.146 1.00 43.98 ? 233 ASN A C 1 ATOM 1794 O O . ASN A 1 233 ? 69.866 8.726 50.811 1.00 44.17 ? 233 ASN A O 1 ATOM 1795 C CB . ASN A 1 233 ? 72.147 6.616 50.865 1.00 46.32 ? 233 ASN A CB 1 ATOM 1796 C CG . ASN A 1 233 ? 73.314 5.946 51.582 1.00 52.73 ? 233 ASN A CG 1 ATOM 1797 O OD1 . ASN A 1 233 ? 73.800 4.834 51.305 1.00 52.44 ? 233 ASN A OD1 1 ATOM 1798 N ND2 . ASN A 1 233 ? 73.836 6.611 52.626 1.00 54.73 ? 233 ASN A ND2 1 ATOM 1799 N N . ASP A 1 234 ? 68.595 6.897 51.130 1.00 42.81 ? 234 ASP A N 1 ATOM 1800 C CA . ASP A 1 234 ? 67.448 7.566 50.546 1.00 42.41 ? 234 ASP A CA 1 ATOM 1801 C C . ASP A 1 234 ? 66.586 8.313 51.553 1.00 41.63 ? 234 ASP A C 1 ATOM 1802 O O . ASP A 1 234 ? 65.557 8.798 51.050 1.00 42.19 ? 234 ASP A O 1 ATOM 1803 C CB . ASP A 1 234 ? 66.495 6.670 49.726 1.00 40.06 ? 234 ASP A CB 1 ATOM 1804 C CG . ASP A 1 234 ? 67.365 5.888 48.762 1.00 41.61 ? 234 ASP A CG 1 ATOM 1805 O OD1 . ASP A 1 234 ? 67.961 6.638 47.962 1.00 44.12 ? 234 ASP A OD1 1 ATOM 1806 O OD2 . ASP A 1 234 ? 67.496 4.654 48.884 1.00 39.94 ? 234 ASP A OD2 1 ATOM 1807 N N . ILE A 1 235 ? 66.922 8.371 52.819 1.00 40.38 ? 235 ILE A N 1 ATOM 1808 C CA . ILE A 1 235 ? 66.058 9.038 53.790 1.00 40.56 ? 235 ILE A CA 1 ATOM 1809 C C . ILE A 1 235 ? 66.847 10.227 54.331 1.00 41.77 ? 235 ILE A C 1 ATOM 1810 O O . ILE A 1 235 ? 68.045 10.152 54.602 1.00 41.94 ? 235 ILE A O 1 ATOM 1811 C CB . ILE A 1 235 ? 65.690 8.042 54.878 1.00 35.98 ? 235 ILE A CB 1 ATOM 1812 C CG1 . ILE A 1 235 ? 65.144 6.707 54.314 1.00 34.82 ? 235 ILE A CG1 1 ATOM 1813 C CG2 . ILE A 1 235 ? 64.650 8.658 55.816 1.00 34.01 ? 235 ILE A CG2 1 ATOM 1814 C CD1 . ILE A 1 235 ? 65.169 5.546 55.338 1.00 29.05 ? 235 ILE A CD1 1 ATOM 1815 N N . VAL A 1 236 ? 66.197 11.372 54.403 1.00 42.55 ? 236 VAL A N 1 ATOM 1816 C CA . VAL A 1 236 ? 66.931 12.586 54.902 1.00 43.45 ? 236 VAL A CA 1 ATOM 1817 C C . VAL A 1 236 ? 66.140 13.227 56.027 1.00 43.06 ? 236 VAL A C 1 ATOM 1818 O O . VAL A 1 236 ? 64.902 13.221 55.994 1.00 43.15 ? 236 VAL A O 1 ATOM 1819 C CB . VAL A 1 236 ? 66.944 13.493 53.659 1.00 45.49 ? 236 VAL A CB 1 ATOM 1820 C CG1 . VAL A 1 236 ? 66.488 14.882 53.992 1.00 44.54 ? 236 VAL A CG1 1 ATOM 1821 C CG2 . VAL A 1 236 ? 68.179 13.458 52.803 1.00 46.62 ? 236 VAL A CG2 1 ATOM 1822 N N . LYS A 1 237 ? 66.736 13.614 57.129 1.00 43.44 ? 237 LYS A N 1 ATOM 1823 C CA . LYS A 1 237 ? 65.991 14.167 58.251 1.00 42.68 ? 237 LYS A CA 1 ATOM 1824 C C . LYS A 1 237 ? 65.816 15.661 57.992 1.00 42.93 ? 237 LYS A C 1 ATOM 1825 O O . LYS A 1 237 ? 66.633 16.227 57.267 1.00 42.59 ? 237 LYS A O 1 ATOM 1826 C CB . LYS A 1 237 ? 66.774 14.028 59.527 1.00 41.82 ? 237 LYS A CB 1 ATOM 1827 C CG . LYS A 1 237 ? 65.917 14.239 60.777 1.00 44.55 ? 237 LYS A CG 1 ATOM 1828 C CD . LYS A 1 237 ? 66.923 14.202 61.924 1.00 49.03 ? 237 LYS A CD 1 ATOM 1829 C CE . LYS A 1 237 ? 66.305 14.168 63.304 1.00 49.08 ? 237 LYS A CE 1 ATOM 1830 N NZ . LYS A 1 237 ? 67.444 14.506 64.225 1.00 55.86 ? 237 LYS A NZ 1 ATOM 1831 N N . ILE A 1 238 ? 64.626 16.133 58.287 1.00 43.14 ? 238 ILE A N 1 ATOM 1832 C CA . ILE A 1 238 ? 64.237 17.504 58.039 1.00 44.71 ? 238 ILE A CA 1 ATOM 1833 C C . ILE A 1 238 ? 63.672 18.159 59.287 1.00 45.80 ? 238 ILE A C 1 ATOM 1834 O O . ILE A 1 238 ? 62.630 17.824 59.839 1.00 45.91 ? 238 ILE A O 1 ATOM 1835 C CB . ILE A 1 238 ? 63.251 17.538 56.862 1.00 45.76 ? 238 ILE A CB 1 ATOM 1836 C CG1 . ILE A 1 238 ? 64.069 17.393 55.572 1.00 45.65 ? 238 ILE A CG1 1 ATOM 1837 C CG2 . ILE A 1 238 ? 62.435 18.811 56.889 1.00 43.96 ? 238 ILE A CG2 1 ATOM 1838 C CD1 . ILE A 1 238 ? 63.299 17.230 54.309 1.00 45.86 ? 238 ILE A CD1 1 ATOM 1839 N N . GLU A 1 239 ? 64.326 19.260 59.640 1.00 46.25 ? 239 GLU A N 1 ATOM 1840 C CA . GLU A 1 239 ? 64.147 19.866 60.969 1.00 45.68 ? 239 GLU A CA 1 ATOM 1841 C C . GLU A 1 239 ? 63.279 21.092 60.816 1.00 44.68 ? 239 GLU A C 1 ATOM 1842 O O . GLU A 1 239 ? 63.402 21.713 59.761 1.00 43.82 ? 239 GLU A O 1 ATOM 1843 C CB . GLU A 1 239 ? 65.610 20.095 61.374 1.00 50.03 ? 239 GLU A CB 1 ATOM 1844 C CG . GLU A 1 239 ? 65.924 19.897 62.823 1.00 57.98 ? 239 GLU A CG 1 ATOM 1845 C CD . GLU A 1 239 ? 66.118 18.498 63.328 1.00 60.91 ? 239 GLU A CD 1 ATOM 1846 O OE1 . GLU A 1 239 ? 67.091 17.895 62.833 1.00 63.63 ? 239 GLU A OE1 1 ATOM 1847 O OE2 . GLU A 1 239 ? 65.353 17.992 64.202 1.00 65.98 ? 239 GLU A OE2 1 ATOM 1848 N N . GLY A 1 240 ? 62.395 21.408 61.754 1.00 43.87 ? 240 GLY A N 1 ATOM 1849 C CA . GLY A 1 240 ? 61.552 22.567 61.721 1.00 42.63 ? 240 GLY A CA 1 ATOM 1850 C C . GLY A 1 240 ? 60.059 22.316 61.668 1.00 43.09 ? 240 GLY A C 1 ATOM 1851 O O . GLY A 1 240 ? 59.610 21.671 60.698 1.00 43.16 ? 240 GLY A O 1 ATOM 1852 N N . ILE A 1 241 ? 59.252 22.893 62.572 1.00 42.26 ? 241 ILE A N 1 ATOM 1853 C CA . ILE A 1 241 ? 57.807 22.762 62.465 1.00 42.35 ? 241 ILE A CA 1 ATOM 1854 C C . ILE A 1 241 ? 57.390 23.419 61.148 1.00 42.72 ? 241 ILE A C 1 ATOM 1855 O O . ILE A 1 241 ? 58.052 24.380 60.790 1.00 43.41 ? 241 ILE A O 1 ATOM 1856 C CB . ILE A 1 241 ? 56.925 23.493 63.470 1.00 41.38 ? 241 ILE A CB 1 ATOM 1857 C CG1 . ILE A 1 241 ? 56.725 22.605 64.682 1.00 41.70 ? 241 ILE A CG1 1 ATOM 1858 C CG2 . ILE A 1 241 ? 55.551 23.889 62.981 1.00 40.25 ? 241 ILE A CG2 1 ATOM 1859 C CD1 . ILE A 1 241 ? 57.593 22.916 65.850 1.00 38.70 ? 241 ILE A CD1 1 ATOM 1860 N N . ASP A 1 242 ? 56.625 22.677 60.364 1.00 42.98 ? 242 ASP A N 1 ATOM 1861 C CA . ASP A 1 242 ? 56.098 23.204 59.106 1.00 41.84 ? 242 ASP A CA 1 ATOM 1862 C C . ASP A 1 242 ? 57.205 23.392 58.078 1.00 41.78 ? 242 ASP A C 1 ATOM 1863 O O . ASP A 1 242 ? 57.095 24.059 57.045 1.00 40.97 ? 242 ASP A O 1 ATOM 1864 C CB . ASP A 1 242 ? 55.236 24.391 59.457 1.00 40.96 ? 242 ASP A CB 1 ATOM 1865 C CG . ASP A 1 242 ? 53.921 23.995 60.103 1.00 45.29 ? 242 ASP A CG 1 ATOM 1866 O OD1 . ASP A 1 242 ? 53.552 22.805 60.082 1.00 44.89 ? 242 ASP A OD1 1 ATOM 1867 O OD2 . ASP A 1 242 ? 53.231 24.849 60.723 1.00 48.05 ? 242 ASP A OD2 1 ATOM 1868 N N . ALA A 1 243 ? 58.333 22.691 58.282 1.00 40.43 ? 243 ALA A N 1 ATOM 1869 C CA . ALA A 1 243 ? 59.447 22.734 57.385 1.00 40.46 ? 243 ALA A CA 1 ATOM 1870 C C . ALA A 1 243 ? 59.029 22.460 55.931 1.00 40.57 ? 243 ALA A C 1 ATOM 1871 O O . ALA A 1 243 ? 58.179 21.626 55.716 1.00 39.26 ? 243 ALA A O 1 ATOM 1872 C CB . ALA A 1 243 ? 60.491 21.755 57.882 1.00 39.46 ? 243 ALA A CB 1 ATOM 1873 N N . THR A 1 244 ? 59.877 22.906 55.002 1.00 41.50 ? 244 THR A N 1 ATOM 1874 C CA . THR A 1 244 ? 59.555 22.714 53.585 1.00 43.76 ? 244 THR A CA 1 ATOM 1875 C C . THR A 1 244 ? 60.580 21.893 52.813 1.00 43.98 ? 244 THR A C 1 ATOM 1876 O O . THR A 1 244 ? 61.701 21.560 53.240 1.00 43.49 ? 244 THR A O 1 ATOM 1877 C CB . THR A 1 244 ? 59.159 23.987 52.827 1.00 43.94 ? 244 THR A CB 1 ATOM 1878 O OG1 . THR A 1 244 ? 60.161 24.998 52.886 1.00 43.10 ? 244 THR A OG1 1 ATOM 1879 C CG2 . THR A 1 244 ? 57.889 24.617 53.387 1.00 44.10 ? 244 THR A CG2 1 ATOM 1880 N N . GLY A 1 245 ? 60.235 21.338 51.658 1.00 44.75 ? 245 GLY A N 1 ATOM 1881 C CA . GLY A 1 245 ? 61.360 20.549 51.074 1.00 48.38 ? 245 GLY A CA 1 ATOM 1882 C C . GLY A 1 245 ? 61.791 19.306 51.851 1.00 48.83 ? 245 GLY A C 1 ATOM 1883 O O . GLY A 1 245 ? 62.940 18.911 51.937 1.00 48.95 ? 245 GLY A O 1 ATOM 1884 N N . GLY A 1 246 ? 60.850 18.415 52.013 1.00 48.70 ? 246 GLY A N 1 ATOM 1885 C CA . GLY A 1 246 ? 60.573 17.099 52.462 1.00 47.39 ? 246 GLY A CA 1 ATOM 1886 C C . GLY A 1 246 ? 59.199 16.828 51.818 1.00 46.42 ? 246 GLY A C 1 ATOM 1887 O O . GLY A 1 246 ? 59.031 17.339 50.719 1.00 46.98 ? 246 GLY A O 1 ATOM 1888 N N . ASN A 1 247 ? 58.183 16.249 52.392 1.00 45.73 ? 247 ASN A N 1 ATOM 1889 C CA . ASN A 1 247 ? 56.878 16.151 51.746 1.00 45.19 ? 247 ASN A CA 1 ATOM 1890 C C . ASN A 1 247 ? 56.140 17.467 51.490 1.00 45.73 ? 247 ASN A C 1 ATOM 1891 O O . ASN A 1 247 ? 55.334 17.622 50.560 1.00 43.47 ? 247 ASN A O 1 ATOM 1892 C CB . ASN A 1 247 ? 56.056 15.240 52.652 1.00 38.71 ? 247 ASN A CB 1 ATOM 1893 C CG . ASN A 1 247 ? 54.618 15.178 52.186 1.00 40.45 ? 247 ASN A CG 1 ATOM 1894 O OD1 . ASN A 1 247 ? 53.765 15.907 52.728 1.00 40.36 ? 247 ASN A OD1 1 ATOM 1895 N ND2 . ASN A 1 247 ? 54.438 14.327 51.182 1.00 37.26 ? 247 ASN A ND2 1 ATOM 1896 N N . ASN A 1 248 ? 56.313 18.434 52.398 1.00 46.93 ? 248 ASN A N 1 ATOM 1897 C CA . ASN A 1 248 ? 55.669 19.737 52.332 1.00 48.29 ? 248 ASN A CA 1 ATOM 1898 C C . ASN A 1 248 ? 56.314 20.712 51.343 1.00 48.22 ? 248 ASN A C 1 ATOM 1899 O O . ASN A 1 248 ? 56.944 21.705 51.697 1.00 48.13 ? 248 ASN A O 1 ATOM 1900 C CB . ASN A 1 248 ? 55.588 20.344 53.723 1.00 50.44 ? 248 ASN A CB 1 ATOM 1901 C CG . ASN A 1 248 ? 54.780 21.610 53.784 1.00 55.80 ? 248 ASN A CG 1 ATOM 1902 O OD1 . ASN A 1 248 ? 53.690 21.674 53.184 1.00 60.61 ? 248 ASN A OD1 1 ATOM 1903 N ND2 . ASN A 1 248 ? 55.301 22.652 54.443 1.00 55.99 ? 248 ASN A ND2 1 ATOM 1904 N N . GLN A 1 249 ? 56.074 20.486 50.062 1.00 47.96 ? 249 GLN A N 1 ATOM 1905 C CA . GLN A 1 249 ? 56.600 21.250 48.967 1.00 48.38 ? 249 GLN A CA 1 ATOM 1906 C C . GLN A 1 249 ? 55.486 21.545 47.972 1.00 48.42 ? 249 GLN A C 1 ATOM 1907 O O . GLN A 1 249 ? 54.516 20.805 47.910 1.00 48.43 ? 249 GLN A O 1 ATOM 1908 C CB . GLN A 1 249 ? 57.699 20.514 48.229 1.00 52.34 ? 249 GLN A CB 1 ATOM 1909 C CG . GLN A 1 249 ? 59.062 20.717 48.869 1.00 56.53 ? 249 GLN A CG 1 ATOM 1910 C CD . GLN A 1 249 ? 60.055 19.838 48.135 1.00 58.56 ? 249 GLN A CD 1 ATOM 1911 O OE1 . GLN A 1 249 ? 60.348 20.141 46.985 1.00 61.48 ? 249 GLN A OE1 1 ATOM 1912 N NE2 . GLN A 1 249 ? 60.520 18.789 48.796 1.00 60.02 ? 249 GLN A NE2 1 ATOM 1913 N N . PRO A 1 250 ? 55.626 22.660 47.286 1.00 48.45 ? 250 PRO A N 1 ATOM 1914 C CA . PRO A 1 250 ? 54.626 23.144 46.353 1.00 48.55 ? 250 PRO A CA 1 ATOM 1915 C C . PRO A 1 250 ? 54.699 22.463 44.993 1.00 48.22 ? 250 PRO A C 1 ATOM 1916 O O . PRO A 1 250 ? 55.457 22.929 44.142 1.00 48.87 ? 250 PRO A O 1 ATOM 1917 C CB . PRO A 1 250 ? 55.031 24.616 46.185 1.00 48.62 ? 250 PRO A CB 1 ATOM 1918 C CG . PRO A 1 250 ? 56.509 24.613 46.330 1.00 48.47 ? 250 PRO A CG 1 ATOM 1919 C CD . PRO A 1 250 ? 56.874 23.476 47.246 1.00 48.62 ? 250 PRO A CD 1 ATOM 1920 N N . ASN A 1 251 ? 54.175 21.264 44.876 1.00 46.98 ? 251 ASN A N 1 ATOM 1921 C CA . ASN A 1 251 ? 54.095 20.525 43.619 1.00 45.62 ? 251 ASN A CA 1 ATOM 1922 C C . ASN A 1 251 ? 52.859 19.652 43.684 1.00 45.46 ? 251 ASN A C 1 ATOM 1923 O O . ASN A 1 251 ? 52.137 19.788 44.680 1.00 46.20 ? 251 ASN A O 1 ATOM 1924 C CB . ASN A 1 251 ? 55.388 19.798 43.399 1.00 41.45 ? 251 ASN A CB 1 ATOM 1925 C CG . ASN A 1 251 ? 55.707 18.739 44.441 1.00 41.17 ? 251 ASN A CG 1 ATOM 1926 O OD1 . ASN A 1 251 ? 54.794 18.071 44.922 1.00 42.50 ? 251 ASN A OD1 1 ATOM 1927 N ND2 . ASN A 1 251 ? 56.969 18.523 44.805 1.00 35.51 ? 251 ASN A ND2 1 ATOM 1928 N N . ILE A 1 252 ? 52.488 18.846 42.740 1.00 46.56 ? 252 ILE A N 1 ATOM 1929 C CA . ILE A 1 252 ? 51.277 18.032 42.819 1.00 48.47 ? 252 ILE A CA 1 ATOM 1930 C C . ILE A 1 252 ? 51.495 16.700 43.554 1.00 48.82 ? 252 ILE A C 1 ATOM 1931 O O . ILE A 1 252 ? 52.443 15.954 43.357 1.00 47.84 ? 252 ILE A O 1 ATOM 1932 C CB . ILE A 1 252 ? 50.607 17.792 41.464 1.00 51.08 ? 252 ILE A CB 1 ATOM 1933 C CG1 . ILE A 1 252 ? 50.441 19.150 40.746 1.00 51.82 ? 252 ILE A CG1 1 ATOM 1934 C CG2 . ILE A 1 252 ? 49.219 17.162 41.574 1.00 50.03 ? 252 ILE A CG2 1 ATOM 1935 C CD1 . ILE A 1 252 ? 50.301 18.957 39.245 1.00 52.07 ? 252 ILE A CD1 1 ATOM 1936 N N . PRO A 1 253 ? 50.648 16.503 44.575 1.00 49.05 ? 253 PRO A N 1 ATOM 1937 C CA . PRO A 1 253 ? 50.708 15.312 45.406 1.00 48.58 ? 253 PRO A CA 1 ATOM 1938 C C . PRO A 1 253 ? 50.269 14.080 44.629 1.00 47.76 ? 253 PRO A C 1 ATOM 1939 O O . PRO A 1 253 ? 49.547 14.194 43.626 1.00 48.12 ? 253 PRO A O 1 ATOM 1940 C CB . PRO A 1 253 ? 49.747 15.630 46.555 1.00 48.83 ? 253 PRO A CB 1 ATOM 1941 C CG . PRO A 1 253 ? 48.781 16.620 45.993 1.00 49.16 ? 253 PRO A CG 1 ATOM 1942 C CD . PRO A 1 253 ? 49.488 17.372 44.910 1.00 48.46 ? 253 PRO A CD 1 ATOM 1943 N N . ASP A 1 254 ? 50.228 12.941 45.325 1.00 46.98 ? 254 ASP A N 1 ATOM 1944 C CA . ASP A 1 254 ? 49.927 11.698 44.585 1.00 44.90 ? 254 ASP A CA 1 ATOM 1945 C C . ASP A 1 254 ? 49.477 10.592 45.503 1.00 43.12 ? 254 ASP A C 1 ATOM 1946 O O . ASP A 1 254 ? 50.214 10.236 46.403 1.00 42.36 ? 254 ASP A O 1 ATOM 1947 C CB . ASP A 1 254 ? 51.336 11.447 44.007 1.00 49.41 ? 254 ASP A CB 1 ATOM 1948 C CG . ASP A 1 254 ? 51.447 10.121 43.319 1.00 51.25 ? 254 ASP A CG 1 ATOM 1949 O OD1 . ASP A 1 254 ? 50.859 10.168 42.216 1.00 53.52 ? 254 ASP A OD1 1 ATOM 1950 O OD2 . ASP A 1 254 ? 52.026 9.152 43.852 1.00 52.96 ? 254 ASP A OD2 1 ATOM 1951 N N . ILE A 1 255 ? 48.568 9.733 45.107 1.00 42.87 ? 255 ILE A N 1 ATOM 1952 C CA . ILE A 1 255 ? 48.154 8.579 45.883 1.00 42.57 ? 255 ILE A CA 1 ATOM 1953 C C . ILE A 1 255 ? 49.057 7.374 45.913 1.00 42.23 ? 255 ILE A C 1 ATOM 1954 O O . ILE A 1 255 ? 49.372 6.852 46.989 1.00 42.34 ? 255 ILE A O 1 ATOM 1955 C CB . ILE A 1 255 ? 46.683 8.226 45.620 1.00 40.10 ? 255 ILE A CB 1 ATOM 1956 C CG1 . ILE A 1 255 ? 45.843 9.487 45.884 1.00 43.23 ? 255 ILE A CG1 1 ATOM 1957 C CG2 . ILE A 1 255 ? 46.181 7.160 46.566 1.00 38.47 ? 255 ILE A CG2 1 ATOM 1958 C CD1 . ILE A 1 255 ? 44.414 9.304 45.383 1.00 45.18 ? 255 ILE A CD1 1 ATOM 1959 N N . PRO A 1 256 ? 49.602 6.880 44.813 1.00 42.36 ? 256 PRO A N 1 ATOM 1960 C CA . PRO A 1 256 ? 50.482 5.722 44.769 1.00 41.37 ? 256 PRO A CA 1 ATOM 1961 C C . PRO A 1 256 ? 51.728 5.939 45.605 1.00 40.74 ? 256 PRO A C 1 ATOM 1962 O O . PRO A 1 256 ? 52.211 5.021 46.252 1.00 40.18 ? 256 PRO A O 1 ATOM 1963 C CB . PRO A 1 256 ? 50.871 5.555 43.298 1.00 41.33 ? 256 PRO A CB 1 ATOM 1964 C CG . PRO A 1 256 ? 49.815 6.289 42.540 1.00 40.95 ? 256 PRO A CG 1 ATOM 1965 C CD . PRO A 1 256 ? 49.359 7.411 43.430 1.00 41.83 ? 256 PRO A CD 1 ATOM 1966 N N . ALA A 1 257 ? 52.179 7.179 45.729 1.00 40.40 ? 257 ALA A N 1 ATOM 1967 C CA . ALA A 1 257 ? 53.265 7.584 46.601 1.00 39.89 ? 257 ALA A CA 1 ATOM 1968 C C . ALA A 1 257 ? 52.947 7.241 48.061 1.00 40.03 ? 257 ALA A C 1 ATOM 1969 O O . ALA A 1 257 ? 53.873 6.871 48.783 1.00 40.70 ? 257 ALA A O 1 ATOM 1970 C CB . ALA A 1 257 ? 53.580 9.063 46.443 1.00 33.53 ? 257 ALA A CB 1 ATOM 1971 N N . HIS A 1 258 ? 51.710 7.303 48.494 1.00 39.22 ? 258 HIS A N 1 ATOM 1972 C CA . HIS A 1 258 ? 51.242 6.939 49.817 1.00 38.93 ? 258 HIS A CA 1 ATOM 1973 C C . HIS A 1 258 ? 51.253 5.440 50.103 1.00 38.88 ? 258 HIS A C 1 ATOM 1974 O O . HIS A 1 258 ? 51.180 5.046 51.264 1.00 38.32 ? 258 HIS A O 1 ATOM 1975 C CB . HIS A 1 258 ? 49.751 7.344 49.921 1.00 35.92 ? 258 HIS A CB 1 ATOM 1976 C CG . HIS A 1 258 ? 49.121 7.248 51.264 1.00 33.72 ? 258 HIS A CG 1 ATOM 1977 N ND1 . HIS A 1 258 ? 49.708 7.791 52.383 1.00 33.17 ? 258 HIS A ND1 1 ATOM 1978 C CD2 . HIS A 1 258 ? 47.956 6.655 51.671 1.00 32.49 ? 258 HIS A CD2 1 ATOM 1979 C CE1 . HIS A 1 258 ? 48.897 7.504 53.408 1.00 34.27 ? 258 HIS A CE1 1 ATOM 1980 N NE2 . HIS A 1 258 ? 47.867 6.783 53.035 1.00 30.20 ? 258 HIS A NE2 1 ATOM 1981 N N . LEU A 1 259 ? 51.318 4.596 49.079 1.00 38.87 ? 259 LEU A N 1 ATOM 1982 C CA . LEU A 1 259 ? 51.133 3.159 49.310 1.00 38.85 ? 259 LEU A CA 1 ATOM 1983 C C . LEU A 1 259 ? 52.472 2.428 49.253 1.00 39.03 ? 259 LEU A C 1 ATOM 1984 O O . LEU A 1 259 ? 52.451 1.196 49.323 1.00 38.67 ? 259 LEU A O 1 ATOM 1985 C CB . LEU A 1 259 ? 50.207 2.566 48.251 1.00 34.14 ? 259 LEU A CB 1 ATOM 1986 C CG . LEU A 1 259 ? 48.813 3.207 48.173 1.00 33.80 ? 259 LEU A CG 1 ATOM 1987 C CD1 . LEU A 1 259 ? 47.969 2.467 47.156 1.00 26.00 ? 259 LEU A CD1 1 ATOM 1988 C CD2 . LEU A 1 259 ? 48.127 3.242 49.541 1.00 29.76 ? 259 LEU A CD2 1 ATOM 1989 N N . TRP A 1 260 ? 53.526 3.247 49.060 1.00 38.24 ? 260 TRP A N 1 ATOM 1990 C CA . TRP A 1 260 ? 54.845 2.667 48.982 1.00 37.36 ? 260 TRP A CA 1 ATOM 1991 C C . TRP A 1 260 ? 55.695 3.223 50.117 1.00 37.56 ? 260 TRP A C 1 ATOM 1992 O O . TRP A 1 260 ? 56.036 4.395 50.028 1.00 38.45 ? 260 TRP A O 1 ATOM 1993 C CB . TRP A 1 260 ? 55.521 2.934 47.636 1.00 33.71 ? 260 TRP A CB 1 ATOM 1994 C CG . TRP A 1 260 ? 56.799 2.146 47.510 1.00 32.36 ? 260 TRP A CG 1 ATOM 1995 C CD1 . TRP A 1 260 ? 58.070 2.572 47.661 1.00 31.84 ? 260 TRP A CD1 1 ATOM 1996 C CD2 . TRP A 1 260 ? 56.898 0.745 47.222 1.00 33.13 ? 260 TRP A CD2 1 ATOM 1997 N NE1 . TRP A 1 260 ? 58.976 1.541 47.511 1.00 30.20 ? 260 TRP A NE1 1 ATOM 1998 C CE2 . TRP A 1 260 ? 58.274 0.405 47.244 1.00 33.95 ? 260 TRP A CE2 1 ATOM 1999 C CE3 . TRP A 1 260 ? 55.965 -0.251 46.938 1.00 32.07 ? 260 TRP A CE3 1 ATOM 2000 C CZ2 . TRP A 1 260 ? 58.722 -0.889 46.968 1.00 31.37 ? 260 TRP A CZ2 1 ATOM 2001 C CZ3 . TRP A 1 260 ? 56.397 -1.533 46.707 1.00 33.53 ? 260 TRP A CZ3 1 ATOM 2002 C CH2 . TRP A 1 260 ? 57.775 -1.836 46.736 1.00 32.00 ? 260 TRP A CH2 1 ATOM 2003 N N . TYR A 1 261 ? 55.748 2.563 51.269 1.00 36.62 ? 261 TYR A N 1 ATOM 2004 C CA . TYR A 1 261 ? 56.647 2.963 52.346 1.00 35.28 ? 261 TYR A CA 1 ATOM 2005 C C . TYR A 1 261 ? 57.567 1.776 52.596 1.00 34.75 ? 261 TYR A C 1 ATOM 2006 O O . TYR A 1 261 ? 57.240 0.817 53.330 1.00 34.99 ? 261 TYR A O 1 ATOM 2007 C CB . TYR A 1 261 ? 55.896 3.305 53.644 1.00 35.91 ? 261 TYR A CB 1 ATOM 2008 C CG . TYR A 1 261 ? 55.508 4.766 53.663 1.00 36.04 ? 261 TYR A CG 1 ATOM 2009 C CD1 . TYR A 1 261 ? 54.355 5.157 52.967 1.00 34.82 ? 261 TYR A CD1 1 ATOM 2010 C CD2 . TYR A 1 261 ? 56.342 5.704 54.290 1.00 35.36 ? 261 TYR A CD2 1 ATOM 2011 C CE1 . TYR A 1 261 ? 54.026 6.490 52.912 1.00 33.93 ? 261 TYR A CE1 1 ATOM 2012 C CE2 . TYR A 1 261 ? 56.046 7.061 54.190 1.00 33.67 ? 261 TYR A CE2 1 ATOM 2013 C CZ . TYR A 1 261 ? 54.880 7.417 53.560 1.00 33.25 ? 261 TYR A CZ 1 ATOM 2014 O OH . TYR A 1 261 ? 54.450 8.688 53.378 1.00 31.29 ? 261 TYR A OH 1 ATOM 2015 N N . PHE A 1 262 ? 58.775 1.776 52.072 1.00 33.59 ? 262 PHE A N 1 ATOM 2016 C CA . PHE A 1 262 ? 59.707 0.673 52.154 1.00 34.10 ? 262 PHE A CA 1 ATOM 2017 C C . PHE A 1 262 ? 59.297 -0.556 51.352 1.00 33.69 ? 262 PHE A C 1 ATOM 2018 O O . PHE A 1 262 ? 60.150 -1.359 51.038 1.00 33.30 ? 262 PHE A O 1 ATOM 2019 C CB . PHE A 1 262 ? 60.095 0.149 53.545 1.00 33.20 ? 262 PHE A CB 1 ATOM 2020 C CG . PHE A 1 262 ? 60.838 1.235 54.301 1.00 32.71 ? 262 PHE A CG 1 ATOM 2021 C CD1 . PHE A 1 262 ? 62.189 1.320 54.406 1.00 31.00 ? 262 PHE A CD1 1 ATOM 2022 C CD2 . PHE A 1 262 ? 60.071 2.218 54.900 1.00 32.17 ? 262 PHE A CD2 1 ATOM 2023 C CE1 . PHE A 1 262 ? 62.810 2.369 55.036 1.00 30.46 ? 262 PHE A CE1 1 ATOM 2024 C CE2 . PHE A 1 262 ? 60.671 3.251 55.576 1.00 33.50 ? 262 PHE A CE2 1 ATOM 2025 C CZ . PHE A 1 262 ? 62.043 3.329 55.673 1.00 30.68 ? 262 PHE A CZ 1 ATOM 2026 N N . GLY A 1 263 ? 58.042 -0.839 51.200 1.00 34.01 ? 263 GLY A N 1 ATOM 2027 C CA . GLY A 1 263 ? 57.308 -1.804 50.487 1.00 34.62 ? 263 GLY A CA 1 ATOM 2028 C C . GLY A 1 263 ? 55.813 -1.483 50.393 1.00 34.90 ? 263 GLY A C 1 ATOM 2029 O O . GLY A 1 263 ? 55.351 -0.442 50.861 1.00 36.02 ? 263 GLY A O 1 ATOM 2030 N N . LEU A 1 264 ? 55.025 -2.411 49.883 1.00 34.70 ? 264 LEU A N 1 ATOM 2031 C CA . LEU A 1 264 ? 53.609 -2.199 49.639 1.00 35.03 ? 264 LEU A CA 1 ATOM 2032 C C . LEU A 1 264 ? 52.904 -1.947 50.945 1.00 34.69 ? 264 LEU A C 1 ATOM 2033 O O . LEU A 1 264 ? 53.165 -2.766 51.816 1.00 35.21 ? 264 LEU A O 1 ATOM 2034 C CB . LEU A 1 264 ? 52.989 -3.446 48.962 1.00 34.70 ? 264 LEU A CB 1 ATOM 2035 C CG . LEU A 1 264 ? 51.669 -3.151 48.266 1.00 33.92 ? 264 LEU A CG 1 ATOM 2036 C CD1 . LEU A 1 264 ? 51.843 -1.947 47.315 1.00 36.18 ? 264 LEU A CD1 1 ATOM 2037 C CD2 . LEU A 1 264 ? 51.221 -4.326 47.397 1.00 36.62 ? 264 LEU A CD2 1 ATOM 2038 N N . ILE A 1 265 ? 52.046 -0.978 51.084 1.00 35.33 ? 265 ILE A N 1 ATOM 2039 C CA . ILE A 1 265 ? 51.414 -0.655 52.368 1.00 36.38 ? 265 ILE A CA 1 ATOM 2040 C C . ILE A 1 265 ? 50.121 0.107 52.092 1.00 38.09 ? 265 ILE A C 1 ATOM 2041 O O . ILE A 1 265 ? 50.098 0.877 51.127 1.00 36.82 ? 265 ILE A O 1 ATOM 2042 C CB . ILE A 1 265 ? 52.354 0.190 53.234 1.00 34.06 ? 265 ILE A CB 1 ATOM 2043 C CG1 . ILE A 1 265 ? 52.017 0.248 54.729 1.00 33.27 ? 265 ILE A CG1 1 ATOM 2044 C CG2 . ILE A 1 265 ? 52.561 1.610 52.673 1.00 32.58 ? 265 ILE A CG2 1 ATOM 2045 C CD1 . ILE A 1 265 ? 53.203 0.809 55.571 1.00 29.00 ? 265 ILE A CD1 1 ATOM 2046 N N . GLY A 1 266 ? 49.051 -0.310 52.803 1.00 40.23 ? 266 GLY A N 1 ATOM 2047 C CA . GLY A 1 266 ? 47.752 0.357 52.647 1.00 41.71 ? 266 GLY A CA 1 ATOM 2048 C C . GLY A 1 266 ? 46.887 -0.453 51.699 1.00 43.06 ? 266 GLY A C 1 ATOM 2049 O O . GLY A 1 266 ? 45.914 0.028 51.137 1.00 44.37 ? 266 GLY A O 1 ATOM 2050 N N . THR A 1 267 ? 47.399 -1.629 51.345 1.00 42.96 ? 267 THR A N 1 ATOM 2051 C CA . THR A 1 267 ? 46.755 -2.408 50.302 1.00 42.99 ? 267 THR A CA 1 ATOM 2052 C C . THR A 1 267 ? 47.412 -3.767 50.261 1.00 43.17 ? 267 THR A C 1 ATOM 2053 O O . THR A 1 267 ? 48.543 -3.896 50.722 1.00 43.22 ? 267 THR A O 1 ATOM 2054 C CB . THR A 1 267 ? 46.859 -1.684 48.949 1.00 44.52 ? 267 THR A CB 1 ATOM 2055 O OG1 . THR A 1 267 ? 46.203 -2.525 47.990 1.00 44.60 ? 267 THR A OG1 1 ATOM 2056 C CG2 . THR A 1 267 ? 48.301 -1.395 48.511 1.00 40.28 ? 267 THR A CG2 1 ATOM 2057 N N . CYS A 1 268 ? 46.646 -4.805 49.967 1.00 44.03 ? 268 CYS A N 1 ATOM 2058 C CA . CYS A 1 268 ? 47.206 -6.159 50.046 1.00 44.59 ? 268 CYS A CA 1 ATOM 2059 C C . CYS A 1 268 ? 47.180 -6.833 48.701 1.00 45.30 ? 268 CYS A C 1 ATOM 2060 O O . CYS A 1 268 ? 46.130 -6.784 48.052 1.00 46.11 ? 268 CYS A O 1 ATOM 2061 C CB . CYS A 1 268 ? 46.365 -6.921 51.073 1.00 45.02 ? 268 CYS A CB 1 ATOM 2062 S SG . CYS A 1 268 ? 46.360 -6.089 52.704 1.00 45.65 ? 268 CYS A SG 1 ATOM 2063 N N . LEU A 1 269 ? 48.295 -7.372 48.239 1.00 45.56 ? 269 LEU A N 1 ATOM 2064 C CA . LEU A 1 269 ? 48.316 -8.088 46.974 1.00 45.98 ? 269 LEU A CA 1 ATOM 2065 C C . LEU A 1 269 ? 47.402 -9.314 47.108 1.00 47.28 ? 269 LEU A C 1 ATOM 2066 O O . LEU A 1 269 ? 47.477 -9.966 48.183 1.00 47.90 ? 269 LEU A O 1 ATOM 2067 C CB . LEU A 1 269 ? 49.724 -8.577 46.677 1.00 43.67 ? 269 LEU A CB 1 ATOM 2068 C CG . LEU A 1 269 ? 50.763 -7.641 46.098 1.00 41.56 ? 269 LEU A CG 1 ATOM 2069 C CD1 . LEU A 1 269 ? 51.895 -8.486 45.522 1.00 39.08 ? 269 LEU A CD1 1 ATOM 2070 C CD2 . LEU A 1 269 ? 50.216 -6.727 45.004 1.00 40.04 ? 269 LEU A CD2 1 ATOM 2071 O OXT . LEU A 1 269 ? 46.778 -9.724 46.101 1.00 48.55 ? 269 LEU A OXT 1 ATOM 2072 N N . GLU B 1 1 ? 50.878 54.212 47.595 1.00 55.87 ? 1 GLU B N 1 ATOM 2073 C CA . GLU B 1 1 ? 50.559 52.717 47.669 1.00 54.74 ? 1 GLU B CA 1 ATOM 2074 C C . GLU B 1 1 ? 49.767 52.367 46.439 1.00 52.43 ? 1 GLU B C 1 ATOM 2075 O O . GLU B 1 1 ? 50.361 51.756 45.538 1.00 52.80 ? 1 GLU B O 1 ATOM 2076 C CB . GLU B 1 1 ? 49.993 52.464 49.036 1.00 64.23 ? 1 GLU B CB 1 ATOM 2077 C CG . GLU B 1 1 ? 50.761 53.175 50.148 1.00 72.51 ? 1 GLU B CG 1 ATOM 2078 C CD . GLU B 1 1 ? 50.417 54.636 50.425 1.00 77.23 ? 1 GLU B CD 1 ATOM 2079 O OE1 . GLU B 1 1 ? 50.024 55.428 49.522 1.00 78.03 ? 1 GLU B OE1 1 ATOM 2080 O OE2 . GLU B 1 1 ? 50.497 55.040 51.630 1.00 76.25 ? 1 GLU B OE2 1 ATOM 2081 N N . VAL B 1 2 ? 48.557 52.861 46.251 1.00 49.69 ? 2 VAL B N 1 ATOM 2082 C CA . VAL B 1 2 ? 47.906 52.728 44.951 1.00 46.94 ? 2 VAL B CA 1 ATOM 2083 C C . VAL B 1 2 ? 47.323 54.129 44.684 1.00 46.46 ? 2 VAL B C 1 ATOM 2084 O O . VAL B 1 2 ? 47.154 54.884 45.653 1.00 46.55 ? 2 VAL B O 1 ATOM 2085 C CB . VAL B 1 2 ? 46.847 51.686 44.681 1.00 43.43 ? 2 VAL B CB 1 ATOM 2086 C CG1 . VAL B 1 2 ? 47.388 50.275 44.644 1.00 39.71 ? 2 VAL B CG1 1 ATOM 2087 C CG2 . VAL B 1 2 ? 45.629 51.832 45.590 1.00 40.55 ? 2 VAL B CG2 1 ATOM 2088 N N . SER B 1 3 ? 47.050 54.462 43.422 1.00 44.77 ? 3 SER B N 1 ATOM 2089 C CA . SER B 1 3 ? 46.543 55.814 43.148 1.00 42.30 ? 3 SER B CA 1 ATOM 2090 C C . SER B 1 3 ? 45.078 56.021 43.514 1.00 41.93 ? 3 SER B C 1 ATOM 2091 O O . SER B 1 3 ? 44.301 55.056 43.606 1.00 41.96 ? 3 SER B O 1 ATOM 2092 C CB . SER B 1 3 ? 46.698 56.111 41.665 1.00 36.01 ? 3 SER B CB 1 ATOM 2093 O OG . SER B 1 3 ? 45.780 55.362 40.897 1.00 31.69 ? 3 SER B OG 1 ATOM 2094 N N . GLN B 1 4 ? 44.669 57.280 43.665 1.00 40.38 ? 4 GLN B N 1 ATOM 2095 C CA . GLN B 1 4 ? 43.271 57.566 43.903 1.00 40.43 ? 4 GLN B CA 1 ATOM 2096 C C . GLN B 1 4 ? 42.418 56.981 42.768 1.00 39.44 ? 4 GLN B C 1 ATOM 2097 O O . GLN B 1 4 ? 41.406 56.312 42.976 1.00 38.02 ? 4 GLN B O 1 ATOM 2098 C CB . GLN B 1 4 ? 43.018 59.065 44.096 1.00 44.73 ? 4 GLN B CB 1 ATOM 2099 C CG . GLN B 1 4 ? 41.644 59.443 44.611 1.00 49.62 ? 4 GLN B CG 1 ATOM 2100 C CD . GLN B 1 4 ? 41.213 58.766 45.894 1.00 52.37 ? 4 GLN B CD 1 ATOM 2101 O OE1 . GLN B 1 4 ? 40.098 58.266 46.070 1.00 53.29 ? 4 GLN B OE1 1 ATOM 2102 N NE2 . GLN B 1 4 ? 42.073 58.671 46.909 1.00 55.10 ? 4 GLN B NE2 1 ATOM 2103 N N . ASP B 1 5 ? 42.819 57.172 41.508 1.00 38.83 ? 5 ASP B N 1 ATOM 2104 C CA . ASP B 1 5 ? 42.079 56.585 40.414 1.00 38.32 ? 5 ASP B CA 1 ATOM 2105 C C . ASP B 1 5 ? 41.983 55.078 40.623 1.00 37.61 ? 5 ASP B C 1 ATOM 2106 O O . ASP B 1 5 ? 40.863 54.601 40.806 1.00 36.58 ? 5 ASP B O 1 ATOM 2107 C CB . ASP B 1 5 ? 42.382 56.981 38.950 1.00 39.17 ? 5 ASP B CB 1 ATOM 2108 C CG . ASP B 1 5 ? 41.523 56.158 37.979 1.00 41.94 ? 5 ASP B CG 1 ATOM 2109 O OD1 . ASP B 1 5 ? 40.267 56.261 37.941 1.00 40.30 ? 5 ASP B OD1 1 ATOM 2110 O OD2 . ASP B 1 5 ? 42.164 55.330 37.290 1.00 43.82 ? 5 ASP B OD2 1 ATOM 2111 N N . LEU B 1 6 ? 43.060 54.320 40.760 1.00 37.69 ? 6 LEU B N 1 ATOM 2112 C CA . LEU B 1 6 ? 42.930 52.880 40.967 1.00 37.21 ? 6 LEU B CA 1 ATOM 2113 C C . LEU B 1 6 ? 42.143 52.516 42.214 1.00 36.39 ? 6 LEU B C 1 ATOM 2114 O O . LEU B 1 6 ? 41.338 51.577 42.160 1.00 36.58 ? 6 LEU B O 1 ATOM 2115 C CB . LEU B 1 6 ? 44.296 52.224 41.011 1.00 40.97 ? 6 LEU B CB 1 ATOM 2116 C CG . LEU B 1 6 ? 44.369 50.707 40.740 1.00 41.76 ? 6 LEU B CG 1 ATOM 2117 C CD1 . LEU B 1 6 ? 43.607 50.301 39.488 1.00 39.08 ? 6 LEU B CD1 1 ATOM 2118 C CD2 . LEU B 1 6 ? 45.860 50.378 40.567 1.00 36.23 ? 6 LEU B CD2 1 ATOM 2119 N N . PHE B 1 7 ? 42.294 53.259 43.305 1.00 35.03 ? 7 PHE B N 1 ATOM 2120 C CA . PHE B 1 7 ? 41.484 52.961 44.492 1.00 34.39 ? 7 PHE B CA 1 ATOM 2121 C C . PHE B 1 7 ? 40.001 53.125 44.181 1.00 34.01 ? 7 PHE B C 1 ATOM 2122 O O . PHE B 1 7 ? 39.213 52.205 44.440 1.00 34.70 ? 7 PHE B O 1 ATOM 2123 C CB . PHE B 1 7 ? 41.985 53.814 45.655 1.00 33.42 ? 7 PHE B CB 1 ATOM 2124 C CG . PHE B 1 7 ? 41.027 53.834 46.813 1.00 37.14 ? 7 PHE B CG 1 ATOM 2125 C CD1 . PHE B 1 7 ? 41.236 52.950 47.878 1.00 37.25 ? 7 PHE B CD1 1 ATOM 2126 C CD2 . PHE B 1 7 ? 39.926 54.697 46.843 1.00 33.57 ? 7 PHE B CD2 1 ATOM 2127 C CE1 . PHE B 1 7 ? 40.370 52.947 48.954 1.00 36.58 ? 7 PHE B CE1 1 ATOM 2128 C CE2 . PHE B 1 7 ? 39.072 54.658 47.922 1.00 33.06 ? 7 PHE B CE2 1 ATOM 2129 C CZ . PHE B 1 7 ? 39.284 53.796 48.981 1.00 32.93 ? 7 PHE B CZ 1 ATOM 2130 N N . ASN B 1 8 ? 39.568 54.179 43.503 1.00 33.16 ? 8 ASN B N 1 ATOM 2131 C CA . ASN B 1 8 ? 38.198 54.389 43.072 1.00 33.45 ? 8 ASN B CA 1 ATOM 2132 C C . ASN B 1 8 ? 37.672 53.191 42.288 1.00 33.87 ? 8 ASN B C 1 ATOM 2133 O O . ASN B 1 8 ? 36.616 52.618 42.620 1.00 34.92 ? 8 ASN B O 1 ATOM 2134 C CB . ASN B 1 8 ? 38.010 55.708 42.297 1.00 29.03 ? 8 ASN B CB 1 ATOM 2135 C CG . ASN B 1 8 ? 38.184 56.865 43.241 1.00 31.27 ? 8 ASN B CG 1 ATOM 2136 O OD1 . ASN B 1 8 ? 38.030 56.678 44.459 1.00 35.47 ? 8 ASN B OD1 1 ATOM 2137 N ND2 . ASN B 1 8 ? 38.610 58.068 42.885 1.00 31.84 ? 8 ASN B ND2 1 ATOM 2138 N N . GLN B 1 9 ? 38.455 52.663 41.355 1.00 33.02 ? 9 GLN B N 1 ATOM 2139 C CA . GLN B 1 9 ? 38.047 51.529 40.579 1.00 32.87 ? 9 GLN B CA 1 ATOM 2140 C C . GLN B 1 9 ? 38.075 50.194 41.356 1.00 32.16 ? 9 GLN B C 1 ATOM 2141 O O . GLN B 1 9 ? 37.156 49.369 41.245 1.00 29.50 ? 9 GLN B O 1 ATOM 2142 C CB . GLN B 1 9 ? 38.795 51.411 39.293 1.00 32.40 ? 9 GLN B CB 1 ATOM 2143 C CG . GLN B 1 9 ? 39.504 52.442 38.537 1.00 35.42 ? 9 GLN B CG 1 ATOM 2144 C CD . GLN B 1 9 ? 40.110 51.969 37.227 1.00 39.08 ? 9 GLN B CD 1 ATOM 2145 O OE1 . GLN B 1 9 ? 39.796 50.900 36.702 1.00 41.51 ? 9 GLN B OE1 1 ATOM 2146 N NE2 . GLN B 1 9 ? 40.916 52.814 36.587 1.00 41.53 ? 9 GLN B NE2 1 ATOM 2147 N N . PHE B 1 10 ? 39.037 50.021 42.253 1.00 32.23 ? 10 PHE B N 1 ATOM 2148 C CA . PHE B 1 10 ? 39.001 48.833 43.130 1.00 33.07 ? 10 PHE B CA 1 ATOM 2149 C C . PHE B 1 10 ? 37.703 48.814 43.927 1.00 33.52 ? 10 PHE B C 1 ATOM 2150 O O . PHE B 1 10 ? 36.987 47.795 43.992 1.00 31.81 ? 10 PHE B O 1 ATOM 2151 C CB . PHE B 1 10 ? 40.247 48.809 44.049 1.00 34.28 ? 10 PHE B CB 1 ATOM 2152 C CG . PHE B 1 10 ? 41.530 48.353 43.379 1.00 30.90 ? 10 PHE B CG 1 ATOM 2153 C CD1 . PHE B 1 10 ? 41.606 48.003 42.055 1.00 31.11 ? 10 PHE B CD1 1 ATOM 2154 C CD2 . PHE B 1 10 ? 42.706 48.277 44.094 1.00 30.78 ? 10 PHE B CD2 1 ATOM 2155 C CE1 . PHE B 1 10 ? 42.793 47.598 41.448 1.00 31.48 ? 10 PHE B CE1 1 ATOM 2156 C CE2 . PHE B 1 10 ? 43.904 47.863 43.555 1.00 28.49 ? 10 PHE B CE2 1 ATOM 2157 C CZ . PHE B 1 10 ? 43.950 47.531 42.204 1.00 29.76 ? 10 PHE B CZ 1 ATOM 2158 N N . ASN B 1 11 ? 37.341 49.996 44.488 1.00 33.36 ? 11 ASN B N 1 ATOM 2159 C CA . ASN B 1 11 ? 36.118 50.113 45.293 1.00 33.12 ? 11 ASN B CA 1 ATOM 2160 C C . ASN B 1 11 ? 34.797 49.902 44.613 1.00 32.87 ? 11 ASN B C 1 ATOM 2161 O O . ASN B 1 11 ? 33.809 49.320 45.067 1.00 32.41 ? 11 ASN B O 1 ATOM 2162 C CB . ASN B 1 11 ? 36.203 51.492 45.944 1.00 38.24 ? 11 ASN B CB 1 ATOM 2163 C CG . ASN B 1 11 ? 35.134 51.801 46.965 1.00 39.72 ? 11 ASN B CG 1 ATOM 2164 O OD1 . ASN B 1 11 ? 34.872 51.080 47.930 1.00 41.78 ? 11 ASN B OD1 1 ATOM 2165 N ND2 . ASN B 1 11 ? 34.464 52.924 46.720 1.00 38.81 ? 11 ASN B ND2 1 ATOM 2166 N N . LEU B 1 12 ? 34.725 50.341 43.359 1.00 34.00 ? 12 LEU B N 1 ATOM 2167 C CA . LEU B 1 12 ? 33.551 50.203 42.513 1.00 34.05 ? 12 LEU B CA 1 ATOM 2168 C C . LEU B 1 12 ? 33.405 48.772 41.993 1.00 35.31 ? 12 LEU B C 1 ATOM 2169 O O . LEU B 1 12 ? 32.255 48.284 41.969 1.00 35.72 ? 12 LEU B O 1 ATOM 2170 C CB . LEU B 1 12 ? 33.641 51.184 41.352 1.00 31.20 ? 12 LEU B CB 1 ATOM 2171 C CG . LEU B 1 12 ? 32.490 51.048 40.325 1.00 30.84 ? 12 LEU B CG 1 ATOM 2172 C CD1 . LEU B 1 12 ? 31.173 51.433 40.972 1.00 27.33 ? 12 LEU B CD1 1 ATOM 2173 C CD2 . LEU B 1 12 ? 32.823 51.814 39.080 1.00 22.85 ? 12 LEU B CD2 1 ATOM 2174 N N . PHE B 1 13 ? 34.513 48.032 41.843 1.00 35.03 ? 13 PHE B N 1 ATOM 2175 C CA . PHE B 1 13 ? 34.325 46.644 41.393 1.00 35.95 ? 13 PHE B CA 1 ATOM 2176 C C . PHE B 1 13 ? 34.089 45.718 42.587 1.00 36.12 ? 13 PHE B C 1 ATOM 2177 O O . PHE B 1 13 ? 33.354 44.716 42.542 1.00 35.44 ? 13 PHE B O 1 ATOM 2178 C CB . PHE B 1 13 ? 35.371 46.205 40.372 1.00 34.14 ? 13 PHE B CB 1 ATOM 2179 C CG . PHE B 1 13 ? 35.309 47.042 39.105 1.00 32.73 ? 13 PHE B CG 1 ATOM 2180 C CD1 . PHE B 1 13 ? 34.219 46.993 38.266 1.00 32.64 ? 13 PHE B CD1 1 ATOM 2181 C CD2 . PHE B 1 13 ? 36.354 47.896 38.823 1.00 30.83 ? 13 PHE B CD2 1 ATOM 2182 C CE1 . PHE B 1 13 ? 34.125 47.813 37.140 1.00 33.93 ? 13 PHE B CE1 1 ATOM 2183 C CE2 . PHE B 1 13 ? 36.262 48.725 37.734 1.00 35.21 ? 13 PHE B CE2 1 ATOM 2184 C CZ . PHE B 1 13 ? 35.167 48.676 36.852 1.00 34.04 ? 13 PHE B CZ 1 ATOM 2185 N N . ALA B 1 14 ? 34.405 46.247 43.776 1.00 36.25 ? 14 ALA B N 1 ATOM 2186 C CA . ALA B 1 14 ? 34.045 45.518 45.001 1.00 37.29 ? 14 ALA B CA 1 ATOM 2187 C C . ALA B 1 14 ? 32.546 45.624 45.239 1.00 37.77 ? 14 ALA B C 1 ATOM 2188 O O . ALA B 1 14 ? 31.916 44.602 45.516 1.00 36.81 ? 14 ALA B O 1 ATOM 2189 C CB . ALA B 1 14 ? 34.875 45.931 46.182 1.00 36.32 ? 14 ALA B CB 1 ATOM 2190 N N . GLN B 1 15 ? 31.931 46.767 44.853 1.00 38.72 ? 15 GLN B N 1 ATOM 2191 C CA . GLN B 1 15 ? 30.477 46.871 45.042 1.00 37.89 ? 15 GLN B CA 1 ATOM 2192 C C . GLN B 1 15 ? 29.696 46.147 43.974 1.00 37.57 ? 15 GLN B C 1 ATOM 2193 O O . GLN B 1 15 ? 28.636 45.580 44.253 1.00 37.83 ? 15 GLN B O 1 ATOM 2194 C CB . GLN B 1 15 ? 30.030 48.319 45.202 1.00 37.89 ? 15 GLN B CB 1 ATOM 2195 C CG . GLN B 1 15 ? 30.714 48.988 46.372 1.00 38.74 ? 15 GLN B CG 1 ATOM 2196 C CD . GLN B 1 15 ? 30.413 50.437 46.577 1.00 38.80 ? 15 GLN B CD 1 ATOM 2197 O OE1 . GLN B 1 15 ? 29.506 51.041 46.010 1.00 42.12 ? 15 GLN B OE1 1 ATOM 2198 N NE2 . GLN B 1 15 ? 31.222 51.074 47.402 1.00 39.87 ? 15 GLN B NE2 1 ATOM 2199 N N . TYR B 1 16 ? 30.187 46.155 42.741 1.00 37.37 ? 16 TYR B N 1 ATOM 2200 C CA . TYR B 1 16 ? 29.579 45.372 41.646 1.00 36.47 ? 16 TYR B CA 1 ATOM 2201 C C . TYR B 1 16 ? 29.726 43.894 42.038 1.00 36.01 ? 16 TYR B C 1 ATOM 2202 O O . TYR B 1 16 ? 28.741 43.150 41.957 1.00 35.52 ? 16 TYR B O 1 ATOM 2203 C CB . TYR B 1 16 ? 30.133 45.663 40.241 1.00 35.23 ? 16 TYR B CB 1 ATOM 2204 C CG . TYR B 1 16 ? 29.602 46.836 39.421 1.00 33.21 ? 16 TYR B CG 1 ATOM 2205 C CD1 . TYR B 1 16 ? 28.404 46.738 38.699 1.00 33.58 ? 16 TYR B CD1 1 ATOM 2206 C CD2 . TYR B 1 16 ? 30.377 47.956 39.187 1.00 32.07 ? 16 TYR B CD2 1 ATOM 2207 C CE1 . TYR B 1 16 ? 27.951 47.780 37.946 1.00 33.36 ? 16 TYR B CE1 1 ATOM 2208 C CE2 . TYR B 1 16 ? 29.967 49.063 38.469 1.00 32.78 ? 16 TYR B CE2 1 ATOM 2209 C CZ . TYR B 1 16 ? 28.729 48.922 37.798 1.00 33.84 ? 16 TYR B CZ 1 ATOM 2210 O OH . TYR B 1 16 ? 28.286 49.979 37.029 1.00 31.99 ? 16 TYR B OH 1 ATOM 2211 N N . SER B 1 17 ? 30.844 43.490 42.655 1.00 35.31 ? 17 SER B N 1 ATOM 2212 C CA . SER B 1 17 ? 30.955 42.131 43.181 1.00 36.04 ? 17 SER B CA 1 ATOM 2213 C C . SER B 1 17 ? 30.040 41.897 44.400 1.00 36.61 ? 17 SER B C 1 ATOM 2214 O O . SER B 1 17 ? 29.080 41.115 44.270 1.00 36.29 ? 17 SER B O 1 ATOM 2215 C CB . SER B 1 17 ? 32.432 41.879 43.519 1.00 36.24 ? 17 SER B CB 1 ATOM 2216 O OG . SER B 1 17 ? 33.192 41.659 42.347 1.00 32.44 ? 17 SER B OG 1 ATOM 2217 N N . ALA B 1 18 ? 29.829 42.926 45.240 1.00 36.78 ? 18 ALA B N 1 ATOM 2218 C CA . ALA B 1 18 ? 28.875 42.794 46.322 1.00 39.44 ? 18 ALA B CA 1 ATOM 2219 C C . ALA B 1 18 ? 27.439 42.688 45.818 1.00 40.28 ? 18 ALA B C 1 ATOM 2220 O O . ALA B 1 18 ? 26.670 41.789 46.245 1.00 41.32 ? 18 ALA B O 1 ATOM 2221 C CB . ALA B 1 18 ? 28.940 43.802 47.457 1.00 40.26 ? 18 ALA B CB 1 ATOM 2222 N N . ALA B 1 19 ? 27.119 43.463 44.800 1.00 39.58 ? 19 ALA B N 1 ATOM 2223 C CA . ALA B 1 19 ? 25.760 43.483 44.232 1.00 38.68 ? 19 ALA B CA 1 ATOM 2224 C C . ALA B 1 19 ? 25.296 42.134 43.721 1.00 38.60 ? 19 ALA B C 1 ATOM 2225 O O . ALA B 1 19 ? 24.106 41.855 43.633 1.00 36.99 ? 19 ALA B O 1 ATOM 2226 C CB . ALA B 1 19 ? 25.703 44.460 43.058 1.00 34.13 ? 19 ALA B CB 1 ATOM 2227 N N . ALA B 1 20 ? 26.259 41.284 43.333 1.00 39.99 ? 20 ALA B N 1 ATOM 2228 C CA . ALA B 1 20 ? 25.962 39.929 42.880 1.00 40.64 ? 20 ALA B CA 1 ATOM 2229 C C . ALA B 1 20 ? 25.336 39.130 44.023 1.00 41.57 ? 20 ALA B C 1 ATOM 2230 O O . ALA B 1 20 ? 24.708 38.126 43.734 1.00 40.92 ? 20 ALA B O 1 ATOM 2231 C CB . ALA B 1 20 ? 27.184 39.191 42.385 1.00 36.26 ? 20 ALA B CB 1 ATOM 2232 N N . TYR B 1 21 ? 25.689 39.411 45.286 1.00 43.16 ? 21 TYR B N 1 ATOM 2233 C CA . TYR B 1 21 ? 24.945 38.709 46.325 1.00 44.78 ? 21 TYR B CA 1 ATOM 2234 C C . TYR B 1 21 ? 23.727 39.487 46.841 1.00 47.02 ? 21 TYR B C 1 ATOM 2235 O O . TYR B 1 21 ? 22.822 38.820 47.327 1.00 46.18 ? 21 TYR B O 1 ATOM 2236 C CB . TYR B 1 21 ? 25.789 38.339 47.500 1.00 41.15 ? 21 TYR B CB 1 ATOM 2237 C CG . TYR B 1 21 ? 27.122 37.698 47.380 1.00 38.19 ? 21 TYR B CG 1 ATOM 2238 C CD1 . TYR B 1 21 ? 27.274 36.330 47.591 1.00 36.86 ? 21 TYR B CD1 1 ATOM 2239 C CD2 . TYR B 1 21 ? 28.250 38.436 47.056 1.00 37.26 ? 21 TYR B CD2 1 ATOM 2240 C CE1 . TYR B 1 21 ? 28.507 35.725 47.511 1.00 35.89 ? 21 TYR B CE1 1 ATOM 2241 C CE2 . TYR B 1 21 ? 29.491 37.850 46.960 1.00 36.61 ? 21 TYR B CE2 1 ATOM 2242 C CZ . TYR B 1 21 ? 29.609 36.493 47.211 1.00 36.92 ? 21 TYR B CZ 1 ATOM 2243 O OH . TYR B 1 21 ? 30.856 35.893 47.135 1.00 36.57 ? 21 TYR B OH 1 ATOM 2244 N N . CYS B 1 22 ? 23.756 40.809 46.853 1.00 50.68 ? 22 CYS B N 1 ATOM 2245 C CA . CYS B 1 22 ? 22.898 41.588 47.687 1.00 55.86 ? 22 CYS B CA 1 ATOM 2246 C C . CYS B 1 22 ? 21.938 42.559 47.069 1.00 60.63 ? 22 CYS B C 1 ATOM 2247 O O . CYS B 1 22 ? 21.765 43.658 47.629 1.00 61.24 ? 22 CYS B O 1 ATOM 2248 C CB . CYS B 1 22 ? 23.681 42.443 48.730 1.00 48.90 ? 22 CYS B CB 1 ATOM 2249 S SG . CYS B 1 22 ? 24.646 41.479 49.831 1.00 46.21 ? 22 CYS B SG 1 ATOM 2250 N N . GLY B 1 23 ? 21.167 42.154 46.065 1.00 66.24 ? 23 GLY B N 1 ATOM 2251 C CA . GLY B 1 23 ? 20.120 43.152 45.788 1.00 73.37 ? 23 GLY B CA 1 ATOM 2252 C C . GLY B 1 23 ? 19.332 42.921 44.571 1.00 77.69 ? 23 GLY B C 1 ATOM 2253 O O . GLY B 1 23 ? 19.840 43.358 43.531 1.00 78.36 ? 23 GLY B O 1 ATOM 2254 N N . LYS B 1 24 ? 18.279 42.115 44.566 1.00 82.10 ? 24 LYS B N 1 ATOM 2255 C CA . LYS B 1 24 ? 17.387 41.979 43.409 1.00 87.14 ? 24 LYS B CA 1 ATOM 2256 C C . LYS B 1 24 ? 18.009 41.457 42.127 1.00 90.14 ? 24 LYS B C 1 ATOM 2257 O O . LYS B 1 24 ? 17.439 41.016 41.124 1.00 90.60 ? 24 LYS B O 1 ATOM 2258 C CB . LYS B 1 24 ? 16.640 43.302 43.170 1.00 88.22 ? 24 LYS B CB 1 ATOM 2259 C CG . LYS B 1 24 ? 15.867 43.812 44.391 1.00 89.47 ? 24 LYS B CG 1 ATOM 2260 C CD . LYS B 1 24 ? 16.520 45.068 44.950 1.00 89.98 ? 24 LYS B CD 1 ATOM 2261 C CE . LYS B 1 24 ? 16.021 45.424 46.334 1.00 90.54 ? 24 LYS B CE 1 ATOM 2262 N NZ . LYS B 1 24 ? 16.818 46.537 46.932 1.00 90.97 ? 24 LYS B NZ 1 ATOM 2263 N N . ASN B 1 25 ? 19.299 41.357 42.067 1.00 93.21 ? 25 ASN B N 1 ATOM 2264 C CA . ASN B 1 25 ? 20.387 40.945 41.280 1.00 96.50 ? 25 ASN B CA 1 ATOM 2265 C C . ASN B 1 25 ? 20.118 39.699 40.432 1.00 98.12 ? 25 ASN B C 1 ATOM 2266 O O . ASN B 1 25 ? 20.126 39.607 39.221 1.00 97.91 ? 25 ASN B O 1 ATOM 2267 C CB . ASN B 1 25 ? 21.464 40.498 42.341 1.00 100.06 ? 25 ASN B CB 1 ATOM 2268 C CG . ASN B 1 25 ? 22.707 40.073 41.575 1.00 102.38 ? 25 ASN B CG 1 ATOM 2269 O OD1 . ASN B 1 25 ? 23.212 41.027 40.992 1.00 104.81 ? 25 ASN B OD1 1 ATOM 2270 N ND2 . ASN B 1 25 ? 23.096 38.811 41.571 1.00 102.15 ? 25 ASN B ND2 1 ATOM 2271 N N . ASN B 1 26 ? 19.898 38.670 41.245 1.00 99.63 ? 26 ASN B N 1 ATOM 2272 C CA . ASN B 1 26 ? 19.746 37.276 40.872 1.00 100.68 ? 26 ASN B CA 1 ATOM 2273 C C . ASN B 1 26 ? 18.794 37.184 39.695 1.00 100.90 ? 26 ASN B C 1 ATOM 2274 O O . ASN B 1 26 ? 19.286 36.734 38.633 1.00 100.50 ? 26 ASN B O 1 ATOM 2275 C CB . ASN B 1 26 ? 19.522 36.504 42.175 1.00 102.55 ? 26 ASN B CB 1 ATOM 2276 C CG . ASN B 1 26 ? 20.276 37.045 43.387 1.00 103.68 ? 26 ASN B CG 1 ATOM 2277 O OD1 . ASN B 1 26 ? 21.375 36.632 43.783 1.00 103.34 ? 26 ASN B OD1 1 ATOM 2278 N ND2 . ASN B 1 26 ? 19.715 38.037 44.080 1.00 103.84 ? 26 ASN B ND2 1 ATOM 2279 N N . ASP B 1 27 ? 17.547 37.684 39.736 1.00 100.85 ? 27 ASP B N 1 ATOM 2280 C CA . ASP B 1 27 ? 16.688 37.609 38.564 1.00 100.82 ? 27 ASP B CA 1 ATOM 2281 C C . ASP B 1 27 ? 15.599 38.664 38.376 1.00 100.49 ? 27 ASP B C 1 ATOM 2282 O O . ASP B 1 27 ? 14.534 38.427 37.775 1.00 100.21 ? 27 ASP B O 1 ATOM 2283 C CB . ASP B 1 27 ? 16.117 36.200 38.337 1.00 101.36 ? 27 ASP B CB 1 ATOM 2284 C CG . ASP B 1 27 ? 16.784 35.520 37.150 1.00 101.09 ? 27 ASP B CG 1 ATOM 2285 O OD1 . ASP B 1 27 ? 18.019 35.322 37.195 1.00 100.38 ? 27 ASP B OD1 1 ATOM 2286 O OD2 . ASP B 1 27 ? 16.037 35.213 36.203 1.00 101.48 ? 27 ASP B OD2 1 ATOM 2287 N N . ALA B 1 28 ? 15.986 39.915 38.684 1.00 99.67 ? 28 ALA B N 1 ATOM 2288 C CA . ALA B 1 28 ? 15.194 41.096 38.369 1.00 98.46 ? 28 ALA B CA 1 ATOM 2289 C C . ALA B 1 28 ? 15.086 41.265 36.850 1.00 97.26 ? 28 ALA B C 1 ATOM 2290 O O . ALA B 1 28 ? 15.895 40.760 36.066 1.00 97.99 ? 28 ALA B O 1 ATOM 2291 C CB . ALA B 1 28 ? 15.858 42.360 38.917 1.00 98.08 ? 28 ALA B CB 1 ATOM 2292 N N . PRO B 1 29 ? 14.107 42.041 36.405 1.00 95.76 ? 29 PRO B N 1 ATOM 2293 C CA . PRO B 1 29 ? 13.858 42.288 34.996 1.00 94.00 ? 29 PRO B CA 1 ATOM 2294 C C . PRO B 1 29 ? 14.873 43.169 34.290 1.00 91.84 ? 29 PRO B C 1 ATOM 2295 O O . PRO B 1 29 ? 15.223 44.274 34.714 1.00 91.43 ? 29 PRO B O 1 ATOM 2296 C CB . PRO B 1 29 ? 12.466 42.908 34.965 1.00 94.44 ? 29 PRO B CB 1 ATOM 2297 C CG . PRO B 1 29 ? 12.208 43.414 36.332 1.00 95.28 ? 29 PRO B CG 1 ATOM 2298 C CD . PRO B 1 29 ? 13.102 42.679 37.295 1.00 95.68 ? 29 PRO B CD 1 ATOM 2299 N N . ALA B 1 30 ? 15.140 42.874 33.019 1.00 89.20 ? 30 ALA B N 1 ATOM 2300 C CA . ALA B 1 30 ? 16.139 43.552 32.206 1.00 85.90 ? 30 ALA B CA 1 ATOM 2301 C C . ALA B 1 30 ? 15.891 45.009 31.849 1.00 83.32 ? 30 ALA B C 1 ATOM 2302 O O . ALA B 1 30 ? 14.874 45.408 31.283 1.00 83.50 ? 30 ALA B O 1 ATOM 2303 C CB . ALA B 1 30 ? 16.386 42.740 30.939 1.00 84.69 ? 30 ALA B CB 1 ATOM 2304 N N . GLY B 1 31 ? 16.896 45.861 32.062 1.00 80.27 ? 31 GLY B N 1 ATOM 2305 C CA . GLY B 1 31 ? 16.853 47.294 31.862 1.00 75.62 ? 31 GLY B CA 1 ATOM 2306 C C . GLY B 1 31 ? 16.656 48.041 33.180 1.00 72.86 ? 31 GLY B C 1 ATOM 2307 O O . GLY B 1 31 ? 16.546 49.263 33.262 1.00 72.25 ? 31 GLY B O 1 ATOM 2308 N N . THR B 1 32 ? 16.506 47.301 34.261 1.00 69.98 ? 32 THR B N 1 ATOM 2309 C CA . THR B 1 32 ? 16.292 47.830 35.607 1.00 67.16 ? 32 THR B CA 1 ATOM 2310 C C . THR B 1 32 ? 17.551 48.409 36.229 1.00 64.34 ? 32 THR B C 1 ATOM 2311 O O . THR B 1 32 ? 18.661 48.035 35.862 1.00 63.79 ? 32 THR B O 1 ATOM 2312 C CB . THR B 1 32 ? 15.769 46.605 36.398 1.00 68.83 ? 32 THR B CB 1 ATOM 2313 O OG1 . THR B 1 32 ? 14.425 46.338 35.954 1.00 70.44 ? 32 THR B OG1 1 ATOM 2314 C CG2 . THR B 1 32 ? 15.882 46.649 37.892 1.00 66.30 ? 32 THR B CG2 1 ATOM 2315 N N . ASN B 1 33 ? 17.462 49.398 37.085 1.00 61.63 ? 33 ASN B N 1 ATOM 2316 C CA . ASN B 1 33 ? 18.529 49.945 37.891 1.00 59.46 ? 33 ASN B CA 1 ATOM 2317 C C . ASN B 1 33 ? 19.070 48.992 38.951 1.00 56.71 ? 33 ASN B C 1 ATOM 2318 O O . ASN B 1 33 ? 18.209 48.456 39.651 1.00 57.01 ? 33 ASN B O 1 ATOM 2319 C CB . ASN B 1 33 ? 18.151 51.226 38.707 1.00 58.85 ? 33 ASN B CB 1 ATOM 2320 C CG . ASN B 1 33 ? 18.025 52.266 37.604 1.00 62.12 ? 33 ASN B CG 1 ATOM 2321 O OD1 . ASN B 1 33 ? 17.217 51.963 36.712 1.00 64.22 ? 33 ASN B OD1 1 ATOM 2322 N ND2 . ASN B 1 33 ? 18.802 53.316 37.405 1.00 63.02 ? 33 ASN B ND2 1 ATOM 2323 N N . ILE B 1 34 ? 20.353 48.712 38.916 1.00 53.62 ? 34 ILE B N 1 ATOM 2324 C CA . ILE B 1 34 ? 20.965 47.807 39.868 1.00 51.68 ? 34 ILE B CA 1 ATOM 2325 C C . ILE B 1 34 ? 21.025 48.501 41.229 1.00 50.38 ? 34 ILE B C 1 ATOM 2326 O O . ILE B 1 34 ? 21.270 49.710 41.265 1.00 49.29 ? 34 ILE B O 1 ATOM 2327 C CB . ILE B 1 34 ? 22.411 47.395 39.466 1.00 49.21 ? 34 ILE B CB 1 ATOM 2328 C CG1 . ILE B 1 34 ? 22.349 46.847 38.052 1.00 49.78 ? 34 ILE B CG1 1 ATOM 2329 C CG2 . ILE B 1 34 ? 22.995 46.361 40.398 1.00 45.68 ? 34 ILE B CG2 1 ATOM 2330 C CD1 . ILE B 1 34 ? 23.617 46.262 37.475 1.00 49.77 ? 34 ILE B CD1 1 ATOM 2331 N N . THR B 1 35 ? 20.318 47.965 42.229 1.00 49.78 ? 35 THR B N 1 ATOM 2332 C CA . THR B 1 35 ? 20.377 48.521 43.588 1.00 48.84 ? 35 THR B CA 1 ATOM 2333 C C . THR B 1 35 ? 20.571 47.360 44.570 1.00 47.95 ? 35 THR B C 1 ATOM 2334 O O . THR B 1 35 ? 20.418 46.182 44.212 1.00 48.03 ? 35 THR B O 1 ATOM 2335 C CB . THR B 1 35 ? 19.106 49.286 43.973 1.00 48.75 ? 35 THR B CB 1 ATOM 2336 O OG1 . THR B 1 35 ? 18.056 48.303 43.980 1.00 48.54 ? 35 THR B OG1 1 ATOM 2337 C CG2 . THR B 1 35 ? 18.750 50.380 42.982 1.00 46.24 ? 35 THR B CG2 1 ATOM 2338 N N . CYS B 1 36 ? 21.123 47.646 45.747 1.00 46.31 ? 36 CYS B N 1 ATOM 2339 C CA . CYS B 1 36 ? 21.365 46.546 46.688 1.00 44.36 ? 36 CYS B CA 1 ATOM 2340 C C . CYS B 1 36 ? 20.617 46.763 47.992 1.00 43.60 ? 36 CYS B C 1 ATOM 2341 O O . CYS B 1 36 ? 20.225 47.872 48.363 1.00 43.76 ? 36 CYS B O 1 ATOM 2342 C CB . CYS B 1 36 ? 22.885 46.462 46.959 1.00 39.91 ? 36 CYS B CB 1 ATOM 2343 S SG . CYS B 1 36 ? 23.959 46.223 45.549 1.00 38.52 ? 36 CYS B SG 1 ATOM 2344 N N . THR B 1 37 ? 20.603 45.766 48.872 1.00 43.31 ? 37 THR B N 1 ATOM 2345 C CA . THR B 1 37 ? 20.042 46.034 50.213 1.00 42.53 ? 37 THR B CA 1 ATOM 2346 C C . THR B 1 37 ? 21.223 46.406 51.086 1.00 44.05 ? 37 THR B C 1 ATOM 2347 O O . THR B 1 37 ? 22.378 46.319 50.609 1.00 44.43 ? 37 THR B O 1 ATOM 2348 C CB . THR B 1 37 ? 19.347 44.781 50.719 1.00 38.00 ? 37 THR B CB 1 ATOM 2349 O OG1 . THR B 1 37 ? 20.305 43.728 50.503 1.00 36.28 ? 37 THR B OG1 1 ATOM 2350 C CG2 . THR B 1 37 ? 18.026 44.505 50.017 1.00 28.69 ? 37 THR B CG2 1 ATOM 2351 N N . GLY B 1 38 ? 20.970 46.923 52.286 1.00 44.14 ? 38 GLY B N 1 ATOM 2352 C CA . GLY B 1 38 ? 21.988 47.265 53.244 1.00 44.22 ? 38 GLY B CA 1 ATOM 2353 C C . GLY B 1 38 ? 23.205 48.063 52.921 1.00 45.00 ? 38 GLY B C 1 ATOM 2354 O O . GLY B 1 38 ? 24.347 47.807 53.366 1.00 46.60 ? 38 GLY B O 1 ATOM 2355 N N . ASN B 1 39 ? 23.076 49.029 52.016 1.00 45.11 ? 39 ASN B N 1 ATOM 2356 C CA . ASN B 1 39 ? 24.121 49.941 51.587 1.00 43.30 ? 39 ASN B CA 1 ATOM 2357 C C . ASN B 1 39 ? 25.338 49.214 51.033 1.00 42.21 ? 39 ASN B C 1 ATOM 2358 O O . ASN B 1 39 ? 26.478 49.673 51.151 1.00 41.74 ? 39 ASN B O 1 ATOM 2359 C CB . ASN B 1 39 ? 24.491 50.825 52.759 1.00 47.07 ? 39 ASN B CB 1 ATOM 2360 C CG . ASN B 1 39 ? 24.956 52.210 52.418 1.00 50.47 ? 39 ASN B CG 1 ATOM 2361 O OD1 . ASN B 1 39 ? 24.272 52.929 51.690 1.00 56.67 ? 39 ASN B OD1 1 ATOM 2362 N ND2 . ASN B 1 39 ? 26.092 52.720 52.873 1.00 51.61 ? 39 ASN B ND2 1 ATOM 2363 N N . ALA B 1 40 ? 25.117 48.060 50.417 1.00 40.72 ? 40 ALA B N 1 ATOM 2364 C CA . ALA B 1 40 ? 26.153 47.265 49.808 1.00 39.93 ? 40 ALA B CA 1 ATOM 2365 C C . ALA B 1 40 ? 26.685 47.782 48.494 1.00 39.56 ? 40 ALA B C 1 ATOM 2366 O O . ALA B 1 40 ? 27.833 47.514 48.202 1.00 41.39 ? 40 ALA B O 1 ATOM 2367 C CB . ALA B 1 40 ? 25.684 45.842 49.642 1.00 40.37 ? 40 ALA B CB 1 ATOM 2368 N N . CYS B 1 41 ? 26.071 48.610 47.698 1.00 39.63 ? 41 CYS B N 1 ATOM 2369 C CA . CYS B 1 41 ? 26.590 49.127 46.463 1.00 38.93 ? 41 CYS B CA 1 ATOM 2370 C C . CYS B 1 41 ? 26.068 50.516 46.096 1.00 39.08 ? 41 CYS B C 1 ATOM 2371 O O . CYS B 1 41 ? 25.675 50.765 44.953 1.00 38.07 ? 41 CYS B O 1 ATOM 2372 C CB . CYS B 1 41 ? 26.287 48.143 45.337 1.00 37.77 ? 41 CYS B CB 1 ATOM 2373 S SG . CYS B 1 41 ? 24.556 48.087 44.924 1.00 33.88 ? 41 CYS B SG 1 ATOM 2374 N N . PRO B 1 42 ? 26.465 51.498 46.922 1.00 39.44 ? 42 PRO B N 1 ATOM 2375 C CA . PRO B 1 42 ? 26.148 52.893 46.684 1.00 38.90 ? 42 PRO B CA 1 ATOM 2376 C C . PRO B 1 42 ? 26.811 53.423 45.435 1.00 39.63 ? 42 PRO B C 1 ATOM 2377 O O . PRO B 1 42 ? 26.174 54.109 44.632 1.00 39.99 ? 42 PRO B O 1 ATOM 2378 C CB . PRO B 1 42 ? 26.627 53.617 47.932 1.00 38.41 ? 42 PRO B CB 1 ATOM 2379 C CG . PRO B 1 42 ? 27.244 52.637 48.869 1.00 37.87 ? 42 PRO B CG 1 ATOM 2380 C CD . PRO B 1 42 ? 27.090 51.282 48.270 1.00 38.71 ? 42 PRO B CD 1 ATOM 2381 N N . GLU B 1 43 ? 28.080 53.142 45.140 1.00 40.09 ? 43 GLU B N 1 ATOM 2382 C CA . GLU B 1 43 ? 28.695 53.726 43.931 1.00 39.95 ? 43 GLU B CA 1 ATOM 2383 C C . GLU B 1 43 ? 28.004 53.196 42.688 1.00 39.50 ? 43 GLU B C 1 ATOM 2384 O O . GLU B 1 43 ? 27.915 53.889 41.694 1.00 38.37 ? 43 GLU B O 1 ATOM 2385 C CB . GLU B 1 43 ? 30.193 53.476 43.831 1.00 39.25 ? 43 GLU B CB 1 ATOM 2386 C CG . GLU B 1 43 ? 30.982 54.099 44.957 1.00 43.86 ? 43 GLU B CG 1 ATOM 2387 C CD . GLU B 1 43 ? 30.727 55.589 45.049 1.00 48.48 ? 43 GLU B CD 1 ATOM 2388 O OE1 . GLU B 1 43 ? 30.734 56.239 43.969 1.00 48.75 ? 43 GLU B OE1 1 ATOM 2389 O OE2 . GLU B 1 43 ? 30.505 56.061 46.196 1.00 52.44 ? 43 GLU B OE2 1 ATOM 2390 N N . VAL B 1 44 ? 27.545 51.938 42.728 1.00 40.58 ? 44 VAL B N 1 ATOM 2391 C CA . VAL B 1 44 ? 26.771 51.405 41.615 1.00 41.18 ? 44 VAL B CA 1 ATOM 2392 C C . VAL B 1 44 ? 25.403 52.082 41.612 1.00 41.73 ? 44 VAL B C 1 ATOM 2393 O O . VAL B 1 44 ? 24.919 52.450 40.555 1.00 41.50 ? 44 VAL B O 1 ATOM 2394 C CB . VAL B 1 44 ? 26.604 49.904 41.563 1.00 39.79 ? 44 VAL B CB 1 ATOM 2395 C CG1 . VAL B 1 44 ? 25.781 49.495 40.357 1.00 41.12 ? 44 VAL B CG1 1 ATOM 2396 C CG2 . VAL B 1 44 ? 27.953 49.206 41.518 1.00 40.81 ? 44 VAL B CG2 1 ATOM 2397 N N . GLU B 1 45 ? 24.863 52.415 42.774 1.00 42.50 ? 45 GLU B N 1 ATOM 2398 C CA . GLU B 1 45 ? 23.571 53.072 42.814 1.00 43.15 ? 45 GLU B CA 1 ATOM 2399 C C . GLU B 1 45 ? 23.628 54.490 42.323 1.00 43.25 ? 45 GLU B C 1 ATOM 2400 O O . GLU B 1 45 ? 22.639 55.008 41.840 1.00 43.72 ? 45 GLU B O 1 ATOM 2401 C CB . GLU B 1 45 ? 22.934 52.951 44.187 1.00 43.55 ? 45 GLU B CB 1 ATOM 2402 C CG . GLU B 1 45 ? 22.235 51.624 44.350 1.00 48.39 ? 45 GLU B CG 1 ATOM 2403 C CD . GLU B 1 45 ? 21.527 51.498 45.680 1.00 53.28 ? 45 GLU B CD 1 ATOM 2404 O OE1 . GLU B 1 45 ? 21.196 52.572 46.222 1.00 54.75 ? 45 GLU B OE1 1 ATOM 2405 O OE2 . GLU B 1 45 ? 21.284 50.339 46.105 1.00 56.67 ? 45 GLU B OE2 1 ATOM 2406 N N . LYS B 1 46 ? 24.761 55.118 42.331 1.00 43.93 ? 46 LYS B N 1 ATOM 2407 C CA . LYS B 1 46 ? 24.927 56.506 41.933 1.00 45.70 ? 46 LYS B CA 1 ATOM 2408 C C . LYS B 1 46 ? 25.245 56.577 40.455 1.00 47.23 ? 46 LYS B C 1 ATOM 2409 O O . LYS B 1 46 ? 25.137 57.614 39.811 1.00 47.48 ? 46 LYS B O 1 ATOM 2410 C CB . LYS B 1 46 ? 25.944 57.020 42.914 1.00 50.03 ? 46 LYS B CB 1 ATOM 2411 C CG . LYS B 1 46 ? 26.671 58.318 42.761 1.00 57.07 ? 46 LYS B CG 1 ATOM 2412 C CD . LYS B 1 46 ? 27.091 58.972 44.064 1.00 60.16 ? 46 LYS B CD 1 ATOM 2413 C CE . LYS B 1 46 ? 27.614 57.996 45.093 1.00 64.71 ? 46 LYS B CE 1 ATOM 2414 N NZ . LYS B 1 46 ? 27.635 58.533 46.485 1.00 68.02 ? 46 LYS B NZ 1 ATOM 2415 N N . ALA B 1 47 ? 25.510 55.443 39.789 1.00 48.16 ? 47 ALA B N 1 ATOM 2416 C CA . ALA B 1 47 ? 25.807 55.441 38.365 1.00 48.03 ? 47 ALA B CA 1 ATOM 2417 C C . ALA B 1 47 ? 24.546 55.077 37.604 1.00 48.66 ? 47 ALA B C 1 ATOM 2418 O O . ALA B 1 47 ? 23.627 54.404 38.069 1.00 47.56 ? 47 ALA B O 1 ATOM 2419 C CB . ALA B 1 47 ? 27.024 54.570 38.054 1.00 42.79 ? 47 ALA B CB 1 ATOM 2420 N N . ASP B 1 48 ? 24.472 55.557 36.347 1.00 49.62 ? 48 ASP B N 1 ATOM 2421 C CA . ASP B 1 48 ? 23.338 55.135 35.496 1.00 50.86 ? 48 ASP B CA 1 ATOM 2422 C C . ASP B 1 48 ? 23.613 53.663 35.164 1.00 50.37 ? 48 ASP B C 1 ATOM 2423 O O . ASP B 1 48 ? 24.330 53.456 34.155 1.00 51.35 ? 48 ASP B O 1 ATOM 2424 C CB . ASP B 1 48 ? 23.272 56.032 34.261 1.00 53.97 ? 48 ASP B CB 1 ATOM 2425 C CG . ASP B 1 48 ? 22.257 55.609 33.216 1.00 56.86 ? 48 ASP B CG 1 ATOM 2426 O OD1 . ASP B 1 48 ? 21.347 54.814 33.539 1.00 59.16 ? 48 ASP B OD1 1 ATOM 2427 O OD2 . ASP B 1 48 ? 22.312 56.021 32.035 1.00 58.54 ? 48 ASP B OD2 1 ATOM 2428 N N . ALA B 1 49 ? 23.245 52.745 36.047 1.00 48.87 ? 49 ALA B N 1 ATOM 2429 C CA . ALA B 1 49 ? 23.741 51.375 35.919 1.00 48.51 ? 49 ALA B CA 1 ATOM 2430 C C . ALA B 1 49 ? 22.646 50.333 36.038 1.00 48.16 ? 49 ALA B C 1 ATOM 2431 O O . ALA B 1 49 ? 21.996 50.121 37.048 1.00 47.59 ? 49 ALA B O 1 ATOM 2432 C CB . ALA B 1 49 ? 24.870 51.135 36.909 1.00 47.81 ? 49 ALA B CB 1 ATOM 2433 N N . THR B 1 50 ? 22.400 49.639 34.927 1.00 48.32 ? 50 THR B N 1 ATOM 2434 C CA . THR B 1 50 ? 21.241 48.774 34.793 1.00 48.51 ? 50 THR B CA 1 ATOM 2435 C C . THR B 1 50 ? 21.638 47.375 34.357 1.00 48.82 ? 50 THR B C 1 ATOM 2436 O O . THR B 1 50 ? 22.641 47.194 33.664 1.00 48.26 ? 50 THR B O 1 ATOM 2437 C CB . THR B 1 50 ? 20.261 49.373 33.751 1.00 44.01 ? 50 THR B CB 1 ATOM 2438 O OG1 . THR B 1 50 ? 21.097 49.581 32.603 1.00 48.97 ? 50 THR B OG1 1 ATOM 2439 C CG2 . THR B 1 50 ? 19.799 50.767 34.122 1.00 39.75 ? 50 THR B CG2 1 ATOM 2440 N N . PHE B 1 51 ? 20.729 46.455 34.652 1.00 49.36 ? 51 PHE B N 1 ATOM 2441 C CA . PHE B 1 51 ? 20.895 45.066 34.261 1.00 50.46 ? 51 PHE B CA 1 ATOM 2442 C C . PHE B 1 51 ? 20.757 44.908 32.744 1.00 51.26 ? 51 PHE B C 1 ATOM 2443 O O . PHE B 1 51 ? 19.867 45.514 32.156 1.00 50.52 ? 51 PHE B O 1 ATOM 2444 C CB . PHE B 1 51 ? 19.790 44.243 34.935 1.00 51.55 ? 51 PHE B CB 1 ATOM 2445 C CG . PHE B 1 51 ? 19.946 43.982 36.404 1.00 53.21 ? 51 PHE B CG 1 ATOM 2446 C CD1 . PHE B 1 51 ? 21.034 43.265 36.885 1.00 53.41 ? 51 PHE B CD1 1 ATOM 2447 C CD2 . PHE B 1 51 ? 18.990 44.460 37.312 1.00 52.42 ? 51 PHE B CD2 1 ATOM 2448 C CE1 . PHE B 1 51 ? 21.191 43.019 38.238 1.00 52.25 ? 51 PHE B CE1 1 ATOM 2449 C CE2 . PHE B 1 51 ? 19.163 44.203 38.645 1.00 53.40 ? 51 PHE B CE2 1 ATOM 2450 C CZ . PHE B 1 51 ? 20.260 43.491 39.106 1.00 52.16 ? 51 PHE B CZ 1 ATOM 2451 N N . LEU B 1 52 ? 21.614 44.101 32.132 1.00 51.78 ? 52 LEU B N 1 ATOM 2452 C CA . LEU B 1 52 ? 21.532 43.781 30.713 1.00 52.19 ? 52 LEU B CA 1 ATOM 2453 C C . LEU B 1 52 ? 21.091 42.315 30.608 1.00 53.32 ? 52 LEU B C 1 ATOM 2454 O O . LEU B 1 52 ? 20.256 41.923 29.787 1.00 54.26 ? 52 LEU B O 1 ATOM 2455 C CB . LEU B 1 52 ? 22.851 43.961 29.956 1.00 48.10 ? 52 LEU B CB 1 ATOM 2456 C CG . LEU B 1 52 ? 23.317 45.377 29.605 1.00 47.01 ? 52 LEU B CG 1 ATOM 2457 C CD1 . LEU B 1 52 ? 24.748 45.436 29.099 1.00 46.23 ? 52 LEU B CD1 1 ATOM 2458 C CD2 . LEU B 1 52 ? 22.462 46.097 28.574 1.00 40.16 ? 52 LEU B CD2 1 ATOM 2459 N N . TYR B 1 53 ? 21.596 41.497 31.526 1.00 53.46 ? 53 TYR B N 1 ATOM 2460 C CA . TYR B 1 53 ? 21.240 40.080 31.586 1.00 53.46 ? 53 TYR B CA 1 ATOM 2461 C C . TYR B 1 53 ? 21.433 39.599 33.021 1.00 53.39 ? 53 TYR B C 1 ATOM 2462 O O . TYR B 1 53 ? 22.404 40.046 33.643 1.00 53.78 ? 53 TYR B O 1 ATOM 2463 C CB . TYR B 1 53 ? 22.134 39.283 30.630 1.00 53.56 ? 53 TYR B CB 1 ATOM 2464 C CG . TYR B 1 53 ? 21.890 37.795 30.646 1.00 55.14 ? 53 TYR B CG 1 ATOM 2465 C CD1 . TYR B 1 53 ? 20.592 37.312 30.480 1.00 56.10 ? 53 TYR B CD1 1 ATOM 2466 C CD2 . TYR B 1 53 ? 22.896 36.855 30.812 1.00 55.93 ? 53 TYR B CD2 1 ATOM 2467 C CE1 . TYR B 1 53 ? 20.303 35.963 30.490 1.00 57.35 ? 53 TYR B CE1 1 ATOM 2468 C CE2 . TYR B 1 53 ? 22.636 35.492 30.822 1.00 56.75 ? 53 TYR B CE2 1 ATOM 2469 C CZ . TYR B 1 53 ? 21.333 35.058 30.674 1.00 58.45 ? 53 TYR B CZ 1 ATOM 2470 O OH . TYR B 1 53 ? 21.000 33.715 30.705 1.00 59.96 ? 53 TYR B OH 1 ATOM 2471 N N . SER B 1 54 ? 20.600 38.741 33.567 1.00 53.07 ? 54 SER B N 1 ATOM 2472 C CA . SER B 1 54 ? 20.819 38.228 34.911 1.00 53.44 ? 54 SER B CA 1 ATOM 2473 C C . SER B 1 54 ? 20.899 36.708 34.820 1.00 54.36 ? 54 SER B C 1 ATOM 2474 O O . SER B 1 54 ? 19.969 36.148 34.262 1.00 54.57 ? 54 SER B O 1 ATOM 2475 C CB . SER B 1 54 ? 19.717 38.522 35.904 1.00 52.25 ? 54 SER B CB 1 ATOM 2476 O OG . SER B 1 54 ? 19.398 39.853 36.202 1.00 53.35 ? 54 SER B OG 1 ATOM 2477 N N . PHE B 1 55 ? 21.807 36.077 35.538 1.00 55.35 ? 55 PHE B N 1 ATOM 2478 C CA . PHE B 1 55 ? 21.786 34.619 35.649 1.00 56.29 ? 55 PHE B CA 1 ATOM 2479 C C . PHE B 1 55 ? 21.915 34.094 37.087 1.00 58.38 ? 55 PHE B C 1 ATOM 2480 O O . PHE B 1 55 ? 22.214 34.777 38.090 1.00 58.11 ? 55 PHE B O 1 ATOM 2481 C CB . PHE B 1 55 ? 22.850 34.015 34.759 1.00 50.83 ? 55 PHE B CB 1 ATOM 2482 C CG . PHE B 1 55 ? 24.203 34.645 34.915 1.00 49.46 ? 55 PHE B CG 1 ATOM 2483 C CD1 . PHE B 1 55 ? 25.197 33.981 35.607 1.00 46.47 ? 55 PHE B CD1 1 ATOM 2484 C CD2 . PHE B 1 55 ? 24.498 35.895 34.384 1.00 48.48 ? 55 PHE B CD2 1 ATOM 2485 C CE1 . PHE B 1 55 ? 26.459 34.513 35.749 1.00 46.15 ? 55 PHE B CE1 1 ATOM 2486 C CE2 . PHE B 1 55 ? 25.758 36.440 34.516 1.00 46.53 ? 55 PHE B CE2 1 ATOM 2487 C CZ . PHE B 1 55 ? 26.721 35.753 35.215 1.00 47.30 ? 55 PHE B CZ 1 ATOM 2488 N N . GLU B 1 56 ? 21.368 32.884 37.226 1.00 60.15 ? 56 GLU B N 1 ATOM 2489 C CA . GLU B 1 56 ? 21.209 32.251 38.524 1.00 62.42 ? 56 GLU B CA 1 ATOM 2490 C C . GLU B 1 56 ? 21.233 30.738 38.489 1.00 63.31 ? 56 GLU B C 1 ATOM 2491 O O . GLU B 1 56 ? 20.200 30.191 38.170 1.00 62.90 ? 56 GLU B O 1 ATOM 2492 C CB . GLU B 1 56 ? 19.854 32.752 39.078 1.00 63.57 ? 56 GLU B CB 1 ATOM 2493 C CG . GLU B 1 56 ? 19.516 32.029 40.381 1.00 66.50 ? 56 GLU B CG 1 ATOM 2494 C CD . GLU B 1 56 ? 18.555 32.837 41.231 1.00 68.77 ? 56 GLU B CD 1 ATOM 2495 O OE1 . GLU B 1 56 ? 17.462 33.131 40.704 1.00 68.86 ? 56 GLU B OE1 1 ATOM 2496 O OE2 . GLU B 1 56 ? 18.939 33.149 42.384 1.00 70.30 ? 56 GLU B OE2 1 ATOM 2497 N N . ASP B 1 57 ? 22.247 30.066 38.971 1.00 65.12 ? 57 ASP B N 1 ATOM 2498 C CA . ASP B 1 57 ? 22.323 28.624 39.114 1.00 67.31 ? 57 ASP B CA 1 ATOM 2499 C C . ASP B 1 57 ? 22.376 28.043 37.712 1.00 68.71 ? 57 ASP B C 1 ATOM 2500 O O . ASP B 1 57 ? 21.845 26.986 37.397 1.00 69.67 ? 57 ASP B O 1 ATOM 2501 C CB . ASP B 1 57 ? 21.113 28.081 39.846 1.00 67.97 ? 57 ASP B CB 1 ATOM 2502 C CG . ASP B 1 57 ? 21.236 28.110 41.346 1.00 70.76 ? 57 ASP B CG 1 ATOM 2503 O OD1 . ASP B 1 57 ? 22.363 28.006 41.875 1.00 72.75 ? 57 ASP B OD1 1 ATOM 2504 O OD2 . ASP B 1 57 ? 20.169 28.233 41.987 1.00 73.61 ? 57 ASP B OD2 1 ATOM 2505 N N . SER B 1 58 ? 23.121 28.739 36.868 1.00 69.51 ? 58 SER B N 1 ATOM 2506 C CA . SER B 1 58 ? 23.130 28.472 35.435 1.00 69.59 ? 58 SER B CA 1 ATOM 2507 C C . SER B 1 58 ? 24.209 27.450 35.151 1.00 69.78 ? 58 SER B C 1 ATOM 2508 O O . SER B 1 58 ? 25.323 27.524 35.666 1.00 69.54 ? 58 SER B O 1 ATOM 2509 C CB . SER B 1 58 ? 23.266 29.806 34.716 1.00 68.93 ? 58 SER B CB 1 ATOM 2510 O OG . SER B 1 58 ? 23.740 29.744 33.392 1.00 70.62 ? 58 SER B OG 1 ATOM 2511 N N . GLY B 1 59 ? 23.830 26.415 34.412 1.00 70.18 ? 59 GLY B N 1 ATOM 2512 C CA . GLY B 1 59 ? 24.756 25.370 34.031 1.00 70.76 ? 59 GLY B CA 1 ATOM 2513 C C . GLY B 1 59 ? 25.218 24.442 35.143 1.00 70.89 ? 59 GLY B C 1 ATOM 2514 O O . GLY B 1 59 ? 24.708 24.325 36.242 1.00 70.36 ? 59 GLY B O 1 ATOM 2515 N N . VAL B 1 60 ? 26.299 23.742 34.834 1.00 71.13 ? 60 VAL B N 1 ATOM 2516 C CA . VAL B 1 60 ? 26.941 22.745 35.648 1.00 71.31 ? 60 VAL B CA 1 ATOM 2517 C C . VAL B 1 60 ? 27.465 23.181 36.993 1.00 71.27 ? 60 VAL B C 1 ATOM 2518 O O . VAL B 1 60 ? 27.267 22.409 37.946 1.00 72.23 ? 60 VAL B O 1 ATOM 2519 C CB . VAL B 1 60 ? 28.027 22.004 34.832 1.00 71.06 ? 60 VAL B CB 1 ATOM 2520 C CG1 . VAL B 1 60 ? 28.965 21.194 35.716 1.00 70.10 ? 60 VAL B CG1 1 ATOM 2521 C CG2 . VAL B 1 60 ? 27.346 21.076 33.822 1.00 71.94 ? 60 VAL B CG2 1 ATOM 2522 N N . GLY B 1 61 ? 28.087 24.324 37.231 1.00 70.63 ? 61 GLY B N 1 ATOM 2523 C CA . GLY B 1 61 ? 28.669 24.641 38.531 1.00 68.59 ? 61 GLY B CA 1 ATOM 2524 C C . GLY B 1 61 ? 27.771 25.614 39.268 1.00 67.80 ? 61 GLY B C 1 ATOM 2525 O O . GLY B 1 61 ? 28.188 26.226 40.247 1.00 68.16 ? 61 GLY B O 1 ATOM 2526 N N . ASP B 1 62 ? 26.519 25.705 38.839 1.00 66.30 ? 62 ASP B N 1 ATOM 2527 C CA . ASP B 1 62 ? 25.526 26.599 39.379 1.00 64.72 ? 62 ASP B CA 1 ATOM 2528 C C . ASP B 1 62 ? 26.073 28.007 39.574 1.00 62.75 ? 62 ASP B C 1 ATOM 2529 O O . ASP B 1 62 ? 26.378 28.495 40.650 1.00 63.60 ? 62 ASP B O 1 ATOM 2530 C CB . ASP B 1 62 ? 24.904 26.036 40.646 1.00 68.93 ? 62 ASP B CB 1 ATOM 2531 C CG . ASP B 1 62 ? 23.746 25.073 40.417 1.00 72.77 ? 62 ASP B CG 1 ATOM 2532 O OD1 . ASP B 1 62 ? 23.569 24.510 39.310 1.00 71.46 ? 62 ASP B OD1 1 ATOM 2533 O OD2 . ASP B 1 62 ? 23.002 24.884 41.422 1.00 73.30 ? 62 ASP B OD2 1 ATOM 2534 N N . VAL B 1 63 ? 26.278 28.717 38.496 1.00 59.80 ? 63 VAL B N 1 ATOM 2535 C CA . VAL B 1 63 ? 26.808 30.024 38.252 1.00 55.94 ? 63 VAL B CA 1 ATOM 2536 C C . VAL B 1 63 ? 25.743 31.120 38.230 1.00 52.88 ? 63 VAL B C 1 ATOM 2537 O O . VAL B 1 63 ? 24.822 31.078 37.446 1.00 50.68 ? 63 VAL B O 1 ATOM 2538 C CB . VAL B 1 63 ? 27.583 29.981 36.924 1.00 56.43 ? 63 VAL B CB 1 ATOM 2539 C CG1 . VAL B 1 63 ? 27.817 31.356 36.340 1.00 56.83 ? 63 VAL B CG1 1 ATOM 2540 C CG2 . VAL B 1 63 ? 28.874 29.205 37.205 1.00 56.68 ? 63 VAL B CG2 1 ATOM 2541 N N . THR B 1 64 ? 25.985 32.121 39.079 1.00 50.50 ? 64 THR B N 1 ATOM 2542 C CA . THR B 1 64 ? 25.038 33.209 39.321 1.00 49.00 ? 64 THR B CA 1 ATOM 2543 C C . THR B 1 64 ? 25.715 34.568 39.245 1.00 47.53 ? 64 THR B C 1 ATOM 2544 O O . THR B 1 64 ? 26.928 34.532 39.381 1.00 48.02 ? 64 THR B O 1 ATOM 2545 C CB . THR B 1 64 ? 24.434 33.066 40.730 1.00 47.55 ? 64 THR B CB 1 ATOM 2546 O OG1 . THR B 1 64 ? 23.821 31.778 40.926 1.00 44.60 ? 64 THR B OG1 1 ATOM 2547 C CG2 . THR B 1 64 ? 23.416 34.140 41.026 1.00 46.67 ? 64 THR B CG2 1 ATOM 2548 N N . GLY B 1 65 ? 25.048 35.607 38.824 1.00 46.52 ? 65 GLY B N 1 ATOM 2549 C CA . GLY B 1 65 ? 25.466 36.975 38.771 1.00 45.22 ? 65 GLY B CA 1 ATOM 2550 C C . GLY B 1 65 ? 24.733 37.816 37.725 1.00 44.99 ? 65 GLY B C 1 ATOM 2551 O O . GLY B 1 65 ? 23.645 37.464 37.212 1.00 44.57 ? 65 GLY B O 1 ATOM 2552 N N . PHE B 1 66 ? 25.404 38.888 37.285 1.00 44.62 ? 66 PHE B N 1 ATOM 2553 C CA . PHE B 1 66 ? 24.765 39.690 36.225 1.00 44.63 ? 66 PHE B CA 1 ATOM 2554 C C . PHE B 1 66 ? 25.746 40.320 35.260 1.00 44.38 ? 66 PHE B C 1 ATOM 2555 O O . PHE B 1 66 ? 26.971 40.267 35.334 1.00 44.01 ? 66 PHE B O 1 ATOM 2556 C CB . PHE B 1 66 ? 23.834 40.784 36.776 1.00 45.35 ? 66 PHE B CB 1 ATOM 2557 C CG . PHE B 1 66 ? 24.590 41.755 37.660 1.00 44.99 ? 66 PHE B CG 1 ATOM 2558 C CD1 . PHE B 1 66 ? 25.212 42.874 37.098 1.00 41.32 ? 66 PHE B CD1 1 ATOM 2559 C CD2 . PHE B 1 66 ? 24.923 41.393 38.966 1.00 42.35 ? 66 PHE B CD2 1 ATOM 2560 C CE1 . PHE B 1 66 ? 25.963 43.691 37.907 1.00 39.47 ? 66 PHE B CE1 1 ATOM 2561 C CE2 . PHE B 1 66 ? 25.643 42.243 39.783 1.00 40.27 ? 66 PHE B CE2 1 ATOM 2562 C CZ . PHE B 1 66 ? 26.179 43.388 39.239 1.00 41.05 ? 66 PHE B CZ 1 ATOM 2563 N N . LEU B 1 67 ? 25.154 40.860 34.193 1.00 45.26 ? 67 LEU B N 1 ATOM 2564 C CA . LEU B 1 67 ? 25.886 41.625 33.173 1.00 43.56 ? 67 LEU B CA 1 ATOM 2565 C C . LEU B 1 67 ? 25.203 42.989 33.134 1.00 42.41 ? 67 LEU B C 1 ATOM 2566 O O . LEU B 1 67 ? 24.004 43.005 32.928 1.00 41.22 ? 67 LEU B O 1 ATOM 2567 C CB . LEU B 1 67 ? 25.855 41.003 31.795 1.00 44.81 ? 67 LEU B CB 1 ATOM 2568 C CG . LEU B 1 67 ? 26.468 41.878 30.657 1.00 48.35 ? 67 LEU B CG 1 ATOM 2569 C CD1 . LEU B 1 67 ? 27.982 41.925 30.842 1.00 46.67 ? 67 LEU B CD1 1 ATOM 2570 C CD2 . LEU B 1 67 ? 26.092 41.363 29.270 1.00 43.99 ? 67 LEU B CD2 1 ATOM 2571 N N . ALA B 1 68 ? 25.978 44.041 33.391 1.00 42.80 ? 68 ALA B N 1 ATOM 2572 C CA . ALA B 1 68 ? 25.383 45.371 33.459 1.00 42.17 ? 68 ALA B CA 1 ATOM 2573 C C . ALA B 1 68 ? 25.921 46.461 32.552 1.00 42.39 ? 68 ALA B C 1 ATOM 2574 O O . ALA B 1 68 ? 27.086 46.510 32.150 1.00 42.66 ? 68 ALA B O 1 ATOM 2575 C CB . ALA B 1 68 ? 25.626 45.866 34.880 1.00 41.14 ? 68 ALA B CB 1 ATOM 2576 N N . LEU B 1 69 ? 25.096 47.500 32.363 1.00 41.83 ? 69 LEU B N 1 ATOM 2577 C CA . LEU B 1 69 ? 25.506 48.626 31.524 1.00 40.62 ? 69 LEU B CA 1 ATOM 2578 C C . LEU B 1 69 ? 25.625 49.855 32.416 1.00 40.64 ? 69 LEU B C 1 ATOM 2579 O O . LEU B 1 69 ? 24.777 50.123 33.275 1.00 40.68 ? 69 LEU B O 1 ATOM 2580 C CB . LEU B 1 69 ? 24.589 48.817 30.345 1.00 37.50 ? 69 LEU B CB 1 ATOM 2581 C CG . LEU B 1 69 ? 24.946 49.940 29.327 1.00 39.91 ? 69 LEU B CG 1 ATOM 2582 C CD1 . LEU B 1 69 ? 26.123 49.557 28.418 1.00 32.49 ? 69 LEU B CD1 1 ATOM 2583 C CD2 . LEU B 1 69 ? 23.647 50.314 28.633 1.00 34.89 ? 69 LEU B CD2 1 ATOM 2584 N N . ASP B 1 70 ? 26.821 50.433 32.421 1.00 40.17 ? 70 ASP B N 1 ATOM 2585 C CA . ASP B 1 70 ? 27.079 51.570 33.311 1.00 39.62 ? 70 ASP B CA 1 ATOM 2586 C C . ASP B 1 70 ? 27.422 52.749 32.402 1.00 39.92 ? 70 ASP B C 1 ATOM 2587 O O . ASP B 1 70 ? 28.611 52.914 32.110 1.00 39.58 ? 70 ASP B O 1 ATOM 2588 C CB . ASP B 1 70 ? 28.198 51.297 34.286 1.00 36.07 ? 70 ASP B CB 1 ATOM 2589 C CG . ASP B 1 70 ? 28.667 52.429 35.162 1.00 36.94 ? 70 ASP B CG 1 ATOM 2590 O OD1 . ASP B 1 70 ? 28.450 53.606 34.787 1.00 35.49 ? 70 ASP B OD1 1 ATOM 2591 O OD2 . ASP B 1 70 ? 29.310 52.191 36.232 1.00 34.88 ? 70 ASP B OD2 1 ATOM 2592 N N . ASN B 1 71 ? 26.425 53.614 32.195 1.00 39.80 ? 71 ASN B N 1 ATOM 2593 C CA . ASN B 1 71 ? 26.680 54.766 31.361 1.00 39.92 ? 71 ASN B CA 1 ATOM 2594 C C . ASN B 1 71 ? 27.507 55.841 32.056 1.00 39.62 ? 71 ASN B C 1 ATOM 2595 O O . ASN B 1 71 ? 27.834 56.809 31.363 1.00 41.02 ? 71 ASN B O 1 ATOM 2596 C CB . ASN B 1 71 ? 25.451 55.464 30.784 1.00 39.54 ? 71 ASN B CB 1 ATOM 2597 C CG . ASN B 1 71 ? 24.671 54.526 29.899 1.00 40.19 ? 71 ASN B CG 1 ATOM 2598 O OD1 . ASN B 1 71 ? 25.188 53.736 29.117 1.00 42.92 ? 71 ASN B OD1 1 ATOM 2599 N ND2 . ASN B 1 71 ? 23.380 54.639 30.115 1.00 41.25 ? 71 ASN B ND2 1 ATOM 2600 N N . THR B 1 72 ? 27.571 55.853 33.366 1.00 38.39 ? 72 THR B N 1 ATOM 2601 C CA . THR B 1 72 ? 28.288 56.914 34.035 1.00 37.46 ? 72 THR B CA 1 ATOM 2602 C C . THR B 1 72 ? 29.764 56.633 33.842 1.00 37.47 ? 72 THR B C 1 ATOM 2603 O O . THR B 1 72 ? 30.481 57.524 33.401 1.00 37.86 ? 72 THR B O 1 ATOM 2604 C CB . THR B 1 72 ? 27.896 57.025 35.523 1.00 36.99 ? 72 THR B CB 1 ATOM 2605 O OG1 . THR B 1 72 ? 26.484 57.243 35.583 1.00 39.68 ? 72 THR B OG1 1 ATOM 2606 C CG2 . THR B 1 72 ? 28.643 58.167 36.156 1.00 34.59 ? 72 THR B CG2 1 ATOM 2607 N N . ASN B 1 73 ? 30.206 55.423 34.172 1.00 37.41 ? 73 ASN B N 1 ATOM 2608 C CA . ASN B 1 73 ? 31.593 55.036 34.028 1.00 37.32 ? 73 ASN B CA 1 ATOM 2609 C C . ASN B 1 73 ? 31.931 54.450 32.672 1.00 38.52 ? 73 ASN B C 1 ATOM 2610 O O . ASN B 1 73 ? 33.116 54.164 32.451 1.00 38.71 ? 73 ASN B O 1 ATOM 2611 C CB . ASN B 1 73 ? 31.995 54.036 35.126 1.00 36.20 ? 73 ASN B CB 1 ATOM 2612 C CG . ASN B 1 73 ? 31.736 54.668 36.470 1.00 36.25 ? 73 ASN B CG 1 ATOM 2613 O OD1 . ASN B 1 73 ? 32.509 55.561 36.814 1.00 40.60 ? 73 ASN B OD1 1 ATOM 2614 N ND2 . ASN B 1 73 ? 30.637 54.305 37.082 1.00 35.84 ? 73 ASN B ND2 1 ATOM 2615 N N . LYS B 1 74 ? 30.976 54.283 31.753 1.00 38.91 ? 74 LYS B N 1 ATOM 2616 C CA . LYS B 1 74 ? 31.284 53.842 30.390 1.00 40.23 ? 74 LYS B CA 1 ATOM 2617 C C . LYS B 1 74 ? 31.740 52.384 30.403 1.00 41.21 ? 74 LYS B C 1 ATOM 2618 O O . LYS B 1 74 ? 32.692 51.979 29.733 1.00 42.10 ? 74 LYS B O 1 ATOM 2619 C CB . LYS B 1 74 ? 32.336 54.681 29.678 1.00 35.69 ? 74 LYS B CB 1 ATOM 2620 C CG . LYS B 1 74 ? 32.144 56.183 29.665 1.00 38.69 ? 74 LYS B CG 1 ATOM 2621 C CD . LYS B 1 74 ? 31.094 56.562 28.620 1.00 42.76 ? 74 LYS B CD 1 ATOM 2622 C CE . LYS B 1 74 ? 29.867 57.180 29.259 1.00 47.81 ? 74 LYS B CE 1 ATOM 2623 N NZ . LYS B 1 74 ? 29.152 58.081 28.266 1.00 50.70 ? 74 LYS B NZ 1 ATOM 2624 N N . LEU B 1 75 ? 31.048 51.594 31.239 1.00 40.53 ? 75 LEU B N 1 ATOM 2625 C CA . LEU B 1 75 ? 31.358 50.193 31.336 1.00 38.47 ? 75 LEU B CA 1 ATOM 2626 C C . LEU B 1 75 ? 30.278 49.241 30.846 1.00 37.88 ? 75 LEU B C 1 ATOM 2627 O O . LEU B 1 75 ? 29.082 49.493 30.859 1.00 37.06 ? 75 LEU B O 1 ATOM 2628 C CB . LEU B 1 75 ? 31.546 49.850 32.844 1.00 34.45 ? 75 LEU B CB 1 ATOM 2629 C CG . LEU B 1 75 ? 32.520 50.801 33.579 1.00 33.80 ? 75 LEU B CG 1 ATOM 2630 C CD1 . LEU B 1 75 ? 32.412 50.407 35.058 1.00 29.69 ? 75 LEU B CD1 1 ATOM 2631 C CD2 . LEU B 1 75 ? 33.958 50.831 33.047 1.00 23.87 ? 75 LEU B CD2 1 ATOM 2632 N N . ILE B 1 76 ? 30.790 48.048 30.567 1.00 37.46 ? 76 ILE B N 1 ATOM 2633 C CA . ILE B 1 76 ? 30.024 46.832 30.467 1.00 37.68 ? 76 ILE B CA 1 ATOM 2634 C C . ILE B 1 76 ? 30.636 45.872 31.483 1.00 38.86 ? 76 ILE B C 1 ATOM 2635 O O . ILE B 1 76 ? 31.812 45.534 31.365 1.00 40.71 ? 76 ILE B O 1 ATOM 2636 C CB . ILE B 1 76 ? 30.151 46.203 29.113 1.00 37.46 ? 76 ILE B CB 1 ATOM 2637 C CG1 . ILE B 1 76 ? 29.252 46.919 28.076 1.00 35.75 ? 76 ILE B CG1 1 ATOM 2638 C CG2 . ILE B 1 76 ? 29.791 44.739 29.082 1.00 38.32 ? 76 ILE B CG2 1 ATOM 2639 C CD1 . ILE B 1 76 ? 29.918 46.836 26.717 1.00 33.52 ? 76 ILE B CD1 1 ATOM 2640 N N . VAL B 1 77 ? 29.948 45.534 32.555 1.00 39.52 ? 77 VAL B N 1 ATOM 2641 C CA . VAL B 1 77 ? 30.396 44.687 33.634 1.00 38.00 ? 77 VAL B CA 1 ATOM 2642 C C . VAL B 1 77 ? 29.611 43.382 33.759 1.00 38.28 ? 77 VAL B C 1 ATOM 2643 O O . VAL B 1 77 ? 28.383 43.247 33.754 1.00 37.31 ? 77 VAL B O 1 ATOM 2644 C CB . VAL B 1 77 ? 30.208 45.487 34.941 1.00 35.43 ? 77 VAL B CB 1 ATOM 2645 C CG1 . VAL B 1 77 ? 30.598 44.698 36.182 1.00 33.92 ? 77 VAL B CG1 1 ATOM 2646 C CG2 . VAL B 1 77 ? 30.957 46.781 34.882 1.00 34.18 ? 77 VAL B CG2 1 ATOM 2647 N N . LEU B 1 78 ? 30.411 42.342 33.914 1.00 38.51 ? 78 LEU B N 1 ATOM 2648 C CA . LEU B 1 78 ? 29.977 40.965 34.080 1.00 38.97 ? 78 LEU B CA 1 ATOM 2649 C C . LEU B 1 78 ? 30.418 40.545 35.481 1.00 39.28 ? 78 LEU B C 1 ATOM 2650 O O . LEU B 1 78 ? 31.599 40.542 35.803 1.00 38.22 ? 78 LEU B O 1 ATOM 2651 C CB . LEU B 1 78 ? 30.556 40.054 33.025 1.00 40.51 ? 78 LEU B CB 1 ATOM 2652 C CG . LEU B 1 78 ? 30.404 38.547 33.147 1.00 45.33 ? 78 LEU B CG 1 ATOM 2653 C CD1 . LEU B 1 78 ? 29.001 38.066 32.818 1.00 43.98 ? 78 LEU B CD1 1 ATOM 2654 C CD2 . LEU B 1 78 ? 31.440 37.812 32.275 1.00 47.24 ? 78 LEU B CD2 1 ATOM 2655 N N . SER B 1 79 ? 29.396 40.502 36.346 1.00 40.31 ? 79 SER B N 1 ATOM 2656 C CA . SER B 1 79 ? 29.659 40.236 37.755 1.00 40.71 ? 79 SER B CA 1 ATOM 2657 C C . SER B 1 79 ? 29.298 38.829 38.158 1.00 41.50 ? 79 SER B C 1 ATOM 2658 O O . SER B 1 79 ? 28.169 38.373 38.008 1.00 40.77 ? 79 SER B O 1 ATOM 2659 C CB . SER B 1 79 ? 29.045 41.377 38.508 1.00 41.10 ? 79 SER B CB 1 ATOM 2660 O OG . SER B 1 79 ? 29.092 41.240 39.919 1.00 40.48 ? 79 SER B OG 1 ATOM 2661 N N . PHE B 1 80 ? 30.333 38.127 38.649 1.00 42.09 ? 80 PHE B N 1 ATOM 2662 C CA . PHE B 1 80 ? 30.113 36.720 39.080 1.00 43.54 ? 80 PHE B CA 1 ATOM 2663 C C . PHE B 1 80 ? 29.869 36.585 40.574 1.00 43.53 ? 80 PHE B C 1 ATOM 2664 O O . PHE B 1 80 ? 30.711 36.991 41.392 1.00 43.20 ? 80 PHE B O 1 ATOM 2665 C CB . PHE B 1 80 ? 31.276 35.748 38.787 1.00 45.75 ? 80 PHE B CB 1 ATOM 2666 C CG . PHE B 1 80 ? 31.312 35.406 37.316 1.00 48.04 ? 80 PHE B CG 1 ATOM 2667 C CD1 . PHE B 1 80 ? 30.474 34.402 36.855 1.00 48.37 ? 80 PHE B CD1 1 ATOM 2668 C CD2 . PHE B 1 80 ? 32.138 36.066 36.424 1.00 48.74 ? 80 PHE B CD2 1 ATOM 2669 C CE1 . PHE B 1 80 ? 30.486 34.031 35.537 1.00 50.36 ? 80 PHE B CE1 1 ATOM 2670 C CE2 . PHE B 1 80 ? 32.091 35.707 35.078 1.00 50.88 ? 80 PHE B CE2 1 ATOM 2671 C CZ . PHE B 1 80 ? 31.270 34.699 34.626 1.00 49.17 ? 80 PHE B CZ 1 ATOM 2672 N N . ARG B 1 81 ? 28.755 35.974 40.948 1.00 43.85 ? 81 ARG B N 1 ATOM 2673 C CA . ARG B 1 81 ? 28.513 35.791 42.394 1.00 44.46 ? 81 ARG B CA 1 ATOM 2674 C C . ARG B 1 81 ? 29.319 34.647 43.002 1.00 44.45 ? 81 ARG B C 1 ATOM 2675 O O . ARG B 1 81 ? 29.335 33.556 42.459 1.00 44.89 ? 81 ARG B O 1 ATOM 2676 C CB . ARG B 1 81 ? 27.042 35.548 42.693 1.00 40.91 ? 81 ARG B CB 1 ATOM 2677 C CG . ARG B 1 81 ? 26.683 35.777 44.155 1.00 39.65 ? 81 ARG B CG 1 ATOM 2678 C CD . ARG B 1 81 ? 26.107 34.539 44.772 1.00 41.29 ? 81 ARG B CD 1 ATOM 2679 N NE . ARG B 1 81 ? 24.745 34.160 44.634 1.00 45.12 ? 81 ARG B NE 1 ATOM 2680 C CZ . ARG B 1 81 ? 24.191 32.944 44.482 1.00 48.10 ? 81 ARG B CZ 1 ATOM 2681 N NH1 . ARG B 1 81 ? 24.845 31.785 44.391 1.00 42.98 ? 81 ARG B NH1 1 ATOM 2682 N NH2 . ARG B 1 81 ? 22.843 32.862 44.370 1.00 46.74 ? 81 ARG B NH2 1 ATOM 2683 N N . GLY B 1 82 ? 29.818 34.764 44.206 1.00 45.31 ? 82 GLY B N 1 ATOM 2684 C CA . GLY B 1 82 ? 30.476 33.650 44.879 1.00 47.44 ? 82 GLY B CA 1 ATOM 2685 C C . GLY B 1 82 ? 29.439 32.697 45.485 1.00 48.47 ? 82 GLY B C 1 ATOM 2686 O O . GLY B 1 82 ? 28.240 32.834 45.251 1.00 47.17 ? 82 GLY B O 1 ATOM 2687 N N . SER B 1 83 ? 29.899 31.850 46.426 1.00 49.33 ? 83 SER B N 1 ATOM 2688 C CA . SER B 1 83 ? 28.921 30.891 46.946 1.00 51.48 ? 83 SER B CA 1 ATOM 2689 C C . SER B 1 83 ? 27.903 31.504 47.890 1.00 51.98 ? 83 SER B C 1 ATOM 2690 O O . SER B 1 83 ? 28.109 32.381 48.725 1.00 51.68 ? 83 SER B O 1 ATOM 2691 C CB . SER B 1 83 ? 29.688 29.660 47.419 1.00 51.50 ? 83 SER B CB 1 ATOM 2692 O OG . SER B 1 83 ? 28.949 28.986 48.436 1.00 54.92 ? 83 SER B OG 1 ATOM 2693 N N . ARG B 1 84 ? 26.668 30.996 47.849 1.00 52.89 ? 84 ARG B N 1 ATOM 2694 C CA . ARG B 1 84 ? 25.610 31.365 48.801 1.00 53.71 ? 84 ARG B CA 1 ATOM 2695 C C . ARG B 1 84 ? 25.920 30.975 50.238 1.00 52.82 ? 84 ARG B C 1 ATOM 2696 O O . ARG B 1 84 ? 25.248 31.465 51.125 1.00 53.01 ? 84 ARG B O 1 ATOM 2697 C CB . ARG B 1 84 ? 24.316 30.677 48.375 1.00 59.49 ? 84 ARG B CB 1 ATOM 2698 C CG . ARG B 1 84 ? 23.025 31.405 48.695 1.00 66.09 ? 84 ARG B CG 1 ATOM 2699 C CD . ARG B 1 84 ? 21.894 30.863 47.816 1.00 72.10 ? 84 ARG B CD 1 ATOM 2700 N NE . ARG B 1 84 ? 21.836 29.397 47.929 1.00 79.32 ? 84 ARG B NE 1 ATOM 2701 C CZ . ARG B 1 84 ? 20.906 28.793 48.676 1.00 82.90 ? 84 ARG B CZ 1 ATOM 2702 N NH1 . ARG B 1 84 ? 19.982 29.508 49.321 1.00 83.02 ? 84 ARG B NH1 1 ATOM 2703 N NH2 . ARG B 1 84 ? 20.909 27.465 48.751 1.00 84.65 ? 84 ARG B NH2 1 ATOM 2704 N N . SER B 1 85 ? 26.747 30.003 50.530 1.00 52.56 ? 85 SER B N 1 ATOM 2705 C CA . SER B 1 85 ? 27.197 29.631 51.834 1.00 53.33 ? 85 SER B CA 1 ATOM 2706 C C . SER B 1 85 ? 28.722 29.480 51.701 1.00 53.71 ? 85 SER B C 1 ATOM 2707 O O . SER B 1 85 ? 29.247 28.390 51.463 1.00 53.68 ? 85 SER B O 1 ATOM 2708 C CB . SER B 1 85 ? 26.613 28.380 52.463 1.00 53.64 ? 85 SER B CB 1 ATOM 2709 O OG . SER B 1 85 ? 25.216 28.314 52.378 1.00 57.56 ? 85 SER B OG 1 ATOM 2710 N N . ILE B 1 86 ? 29.441 30.530 52.058 1.00 53.54 ? 86 ILE B N 1 ATOM 2711 C CA . ILE B 1 86 ? 30.899 30.464 51.980 1.00 54.09 ? 86 ILE B CA 1 ATOM 2712 C C . ILE B 1 86 ? 31.572 29.512 52.938 1.00 54.66 ? 86 ILE B C 1 ATOM 2713 O O . ILE B 1 86 ? 32.584 28.851 52.631 1.00 53.26 ? 86 ILE B O 1 ATOM 2714 C CB . ILE B 1 86 ? 31.424 31.917 51.944 1.00 51.58 ? 86 ILE B CB 1 ATOM 2715 C CG1 . ILE B 1 86 ? 30.870 32.581 50.670 1.00 48.74 ? 86 ILE B CG1 1 ATOM 2716 C CG2 . ILE B 1 86 ? 32.936 31.979 52.055 1.00 49.90 ? 86 ILE B CG2 1 ATOM 2717 C CD1 . ILE B 1 86 ? 31.258 33.988 50.337 1.00 43.98 ? 86 ILE B CD1 1 ATOM 2718 N N . GLU B 1 87 ? 31.129 29.367 54.188 1.00 56.38 ? 87 GLU B N 1 ATOM 2719 C CA . GLU B 1 87 ? 31.716 28.483 55.194 1.00 57.75 ? 87 GLU B CA 1 ATOM 2720 C C . GLU B 1 87 ? 31.810 27.066 54.604 1.00 58.22 ? 87 GLU B C 1 ATOM 2721 O O . GLU B 1 87 ? 32.841 26.399 54.597 1.00 57.53 ? 87 GLU B O 1 ATOM 2722 C CB . GLU B 1 87 ? 30.874 28.297 56.443 1.00 63.12 ? 87 GLU B CB 1 ATOM 2723 C CG . GLU B 1 87 ? 29.393 27.979 56.485 1.00 69.05 ? 87 GLU B CG 1 ATOM 2724 C CD . GLU B 1 87 ? 28.452 28.227 55.353 1.00 70.16 ? 87 GLU B CD 1 ATOM 2725 O OE1 . GLU B 1 87 ? 28.812 27.846 54.230 1.00 71.57 ? 87 GLU B OE1 1 ATOM 2726 O OE2 . GLU B 1 87 ? 27.340 28.764 55.467 1.00 73.78 ? 87 GLU B OE2 1 ATOM 2727 N N . ASN B 1 88 ? 30.688 26.569 54.084 1.00 57.87 ? 88 ASN B N 1 ATOM 2728 C CA . ASN B 1 88 ? 30.690 25.170 53.681 1.00 58.80 ? 88 ASN B CA 1 ATOM 2729 C C . ASN B 1 88 ? 31.300 24.957 52.325 1.00 58.26 ? 88 ASN B C 1 ATOM 2730 O O . ASN B 1 88 ? 32.013 23.980 52.066 1.00 58.27 ? 88 ASN B O 1 ATOM 2731 C CB . ASN B 1 88 ? 29.313 24.662 54.094 1.00 62.41 ? 88 ASN B CB 1 ATOM 2732 C CG . ASN B 1 88 ? 29.251 24.395 55.613 1.00 65.26 ? 88 ASN B CG 1 ATOM 2733 O OD1 . ASN B 1 88 ? 30.110 24.580 56.510 1.00 63.19 ? 88 ASN B OD1 1 ATOM 2734 N ND2 . ASN B 1 88 ? 28.139 23.757 56.005 1.00 67.40 ? 88 ASN B ND2 1 ATOM 2735 N N . TRP B 1 89 ? 31.360 26.000 51.510 1.00 57.25 ? 89 TRP B N 1 ATOM 2736 C CA . TRP B 1 89 ? 32.092 25.971 50.265 1.00 56.69 ? 89 TRP B CA 1 ATOM 2737 C C . TRP B 1 89 ? 33.585 25.848 50.505 1.00 57.36 ? 89 TRP B C 1 ATOM 2738 O O . TRP B 1 89 ? 34.241 25.101 49.771 1.00 57.27 ? 89 TRP B O 1 ATOM 2739 C CB . TRP B 1 89 ? 31.693 27.198 49.449 1.00 53.79 ? 89 TRP B CB 1 ATOM 2740 C CG . TRP B 1 89 ? 32.506 27.375 48.202 1.00 49.87 ? 89 TRP B CG 1 ATOM 2741 C CD1 . TRP B 1 89 ? 32.192 26.898 46.967 1.00 50.07 ? 89 TRP B CD1 1 ATOM 2742 C CD2 . TRP B 1 89 ? 33.729 28.090 48.063 1.00 46.65 ? 89 TRP B CD2 1 ATOM 2743 N NE1 . TRP B 1 89 ? 33.189 27.223 46.071 1.00 51.66 ? 89 TRP B NE1 1 ATOM 2744 C CE2 . TRP B 1 89 ? 34.150 27.944 46.737 1.00 50.20 ? 89 TRP B CE2 1 ATOM 2745 C CE3 . TRP B 1 89 ? 34.521 28.842 48.918 1.00 47.19 ? 89 TRP B CE3 1 ATOM 2746 C CZ2 . TRP B 1 89 ? 35.307 28.552 46.237 1.00 49.74 ? 89 TRP B CZ2 1 ATOM 2747 C CZ3 . TRP B 1 89 ? 35.702 29.377 48.451 1.00 46.43 ? 89 TRP B CZ3 1 ATOM 2748 C CH2 . TRP B 1 89 ? 36.087 29.232 47.130 1.00 46.39 ? 89 TRP B CH2 1 ATOM 2749 N N . ILE B 1 90 ? 34.178 26.498 51.498 1.00 58.37 ? 90 ILE B N 1 ATOM 2750 C CA . ILE B 1 90 ? 35.612 26.432 51.750 1.00 59.84 ? 90 ILE B CA 1 ATOM 2751 C C . ILE B 1 90 ? 36.108 25.037 52.094 1.00 61.73 ? 90 ILE B C 1 ATOM 2752 O O . ILE B 1 90 ? 37.094 24.516 51.565 1.00 61.57 ? 90 ILE B O 1 ATOM 2753 C CB . ILE B 1 90 ? 36.037 27.449 52.813 1.00 56.75 ? 90 ILE B CB 1 ATOM 2754 C CG1 . ILE B 1 90 ? 36.278 28.792 52.096 1.00 58.19 ? 90 ILE B CG1 1 ATOM 2755 C CG2 . ILE B 1 90 ? 37.256 27.124 53.650 1.00 56.32 ? 90 ILE B CG2 1 ATOM 2756 C CD1 . ILE B 1 90 ? 36.038 30.032 52.936 1.00 53.59 ? 90 ILE B CD1 1 ATOM 2757 N N . GLY B 1 91 ? 35.397 24.398 53.009 1.00 63.13 ? 91 GLY B N 1 ATOM 2758 C CA . GLY B 1 91 ? 35.736 23.121 53.598 1.00 64.75 ? 91 GLY B CA 1 ATOM 2759 C C . GLY B 1 91 ? 35.327 21.923 52.759 1.00 65.62 ? 91 GLY B C 1 ATOM 2760 O O . GLY B 1 91 ? 35.864 20.828 52.984 1.00 66.59 ? 91 GLY B O 1 ATOM 2761 N N . ASN B 1 92 ? 34.494 22.168 51.752 1.00 65.51 ? 92 ASN B N 1 ATOM 2762 C CA . ASN B 1 92 ? 34.085 21.106 50.857 1.00 66.08 ? 92 ASN B CA 1 ATOM 2763 C C . ASN B 1 92 ? 34.739 21.210 49.493 1.00 66.14 ? 92 ASN B C 1 ATOM 2764 O O . ASN B 1 92 ? 34.327 20.554 48.529 1.00 66.82 ? 92 ASN B O 1 ATOM 2765 C CB . ASN B 1 92 ? 32.558 21.091 50.705 1.00 69.12 ? 92 ASN B CB 1 ATOM 2766 C CG . ASN B 1 92 ? 31.987 20.443 51.960 1.00 73.35 ? 92 ASN B CG 1 ATOM 2767 O OD1 . ASN B 1 92 ? 31.640 19.268 51.907 1.00 74.84 ? 92 ASN B OD1 1 ATOM 2768 N ND2 . ASN B 1 92 ? 32.035 21.171 53.076 1.00 76.73 ? 92 ASN B ND2 1 ATOM 2769 N N . LEU B 1 93 ? 35.802 21.977 49.392 1.00 65.56 ? 93 LEU B N 1 ATOM 2770 C CA . LEU B 1 93 ? 36.454 22.281 48.134 1.00 65.19 ? 93 LEU B CA 1 ATOM 2771 C C . LEU B 1 93 ? 37.463 21.234 47.708 1.00 66.30 ? 93 LEU B C 1 ATOM 2772 O O . LEU B 1 93 ? 38.486 21.043 48.369 1.00 67.15 ? 93 LEU B O 1 ATOM 2773 C CB . LEU B 1 93 ? 37.221 23.591 48.333 1.00 61.23 ? 93 LEU B CB 1 ATOM 2774 C CG . LEU B 1 93 ? 37.847 24.237 47.116 1.00 57.58 ? 93 LEU B CG 1 ATOM 2775 C CD1 . LEU B 1 93 ? 36.760 24.945 46.339 1.00 56.38 ? 93 LEU B CD1 1 ATOM 2776 C CD2 . LEU B 1 93 ? 38.938 25.191 47.574 1.00 59.22 ? 93 LEU B CD2 1 ATOM 2777 N N . ASN B 1 94 ? 37.271 20.659 46.543 1.00 67.07 ? 94 ASN B N 1 ATOM 2778 C CA . ASN B 1 94 ? 38.109 19.660 45.917 1.00 67.46 ? 94 ASN B CA 1 ATOM 2779 C C . ASN B 1 94 ? 39.258 20.235 45.100 1.00 66.93 ? 94 ASN B C 1 ATOM 2780 O O . ASN B 1 94 ? 39.226 20.136 43.845 1.00 68.41 ? 94 ASN B O 1 ATOM 2781 C CB . ASN B 1 94 ? 37.137 18.887 45.007 1.00 72.18 ? 94 ASN B CB 1 ATOM 2782 C CG . ASN B 1 94 ? 37.762 17.802 44.174 1.00 77.89 ? 94 ASN B CG 1 ATOM 2783 O OD1 . ASN B 1 94 ? 38.927 17.433 44.369 1.00 81.90 ? 94 ASN B OD1 1 ATOM 2784 N ND2 . ASN B 1 94 ? 36.996 17.286 43.217 1.00 81.89 ? 94 ASN B ND2 1 ATOM 2785 N N . PHE B 1 95 ? 40.474 20.191 45.609 1.00 65.61 ? 95 PHE B N 1 ATOM 2786 C CA . PHE B 1 95 ? 41.703 20.605 44.966 1.00 64.41 ? 95 PHE B CA 1 ATOM 2787 C C . PHE B 1 95 ? 42.084 20.038 43.613 1.00 63.40 ? 95 PHE B C 1 ATOM 2788 O O . PHE B 1 95 ? 43.055 20.526 43.023 1.00 63.01 ? 95 PHE B O 1 ATOM 2789 C CB . PHE B 1 95 ? 42.872 20.422 45.968 1.00 61.25 ? 95 PHE B CB 1 ATOM 2790 C CG . PHE B 1 95 ? 42.546 20.924 47.343 1.00 59.81 ? 95 PHE B CG 1 ATOM 2791 C CD1 . PHE B 1 95 ? 41.748 22.034 47.569 1.00 60.18 ? 95 PHE B CD1 1 ATOM 2792 C CD2 . PHE B 1 95 ? 43.061 20.265 48.448 1.00 61.04 ? 95 PHE B CD2 1 ATOM 2793 C CE1 . PHE B 1 95 ? 41.453 22.468 48.844 1.00 61.37 ? 95 PHE B CE1 1 ATOM 2794 C CE2 . PHE B 1 95 ? 42.788 20.693 49.734 1.00 61.38 ? 95 PHE B CE2 1 ATOM 2795 C CZ . PHE B 1 95 ? 41.974 21.792 49.935 1.00 61.79 ? 95 PHE B CZ 1 ATOM 2796 N N . ASP B 1 96 ? 41.365 19.114 43.005 1.00 63.30 ? 96 ASP B N 1 ATOM 2797 C CA . ASP B 1 96 ? 41.718 18.532 41.726 1.00 63.35 ? 96 ASP B CA 1 ATOM 2798 C C . ASP B 1 96 ? 41.929 19.559 40.624 1.00 63.19 ? 96 ASP B C 1 ATOM 2799 O O . ASP B 1 96 ? 41.197 20.537 40.490 1.00 64.20 ? 96 ASP B O 1 ATOM 2800 C CB . ASP B 1 96 ? 40.717 17.476 41.271 1.00 62.04 ? 96 ASP B CB 1 ATOM 2801 C CG . ASP B 1 96 ? 40.670 16.321 42.251 1.00 61.52 ? 96 ASP B CG 1 ATOM 2802 O OD1 . ASP B 1 96 ? 41.717 15.992 42.831 1.00 63.73 ? 96 ASP B OD1 1 ATOM 2803 O OD2 . ASP B 1 96 ? 39.572 15.779 42.444 1.00 60.26 ? 96 ASP B OD2 1 ATOM 2804 N N . LEU B 1 97 ? 43.033 19.378 39.941 1.00 62.27 ? 97 LEU B N 1 ATOM 2805 C CA . LEU B 1 97 ? 43.542 20.113 38.822 1.00 62.03 ? 97 LEU B CA 1 ATOM 2806 C C . LEU B 1 97 ? 43.173 19.400 37.510 1.00 63.06 ? 97 LEU B C 1 ATOM 2807 O O . LEU B 1 97 ? 42.843 18.200 37.501 1.00 62.76 ? 97 LEU B O 1 ATOM 2808 C CB . LEU B 1 97 ? 45.055 20.086 38.969 1.00 57.24 ? 97 LEU B CB 1 ATOM 2809 C CG . LEU B 1 97 ? 45.729 21.199 39.739 1.00 57.90 ? 97 LEU B CG 1 ATOM 2810 C CD1 . LEU B 1 97 ? 47.233 21.064 39.813 1.00 54.99 ? 97 LEU B CD1 1 ATOM 2811 C CD2 . LEU B 1 97 ? 45.319 22.587 39.244 1.00 56.57 ? 97 LEU B CD2 1 ATOM 2812 N N . LYS B 1 98 ? 43.374 20.064 36.374 1.00 63.87 ? 98 LYS B N 1 ATOM 2813 C CA . LYS B 1 98 ? 42.932 19.535 35.085 1.00 64.24 ? 98 LYS B CA 1 ATOM 2814 C C . LYS B 1 98 ? 43.413 20.367 33.904 1.00 64.65 ? 98 LYS B C 1 ATOM 2815 O O . LYS B 1 98 ? 43.440 21.589 33.952 1.00 65.25 ? 98 LYS B O 1 ATOM 2816 C CB . LYS B 1 98 ? 41.429 19.427 35.038 1.00 63.22 ? 98 LYS B CB 1 ATOM 2817 C CG . LYS B 1 98 ? 40.680 19.813 33.789 1.00 63.57 ? 98 LYS B CG 1 ATOM 2818 C CD . LYS B 1 98 ? 39.227 19.376 34.009 1.00 65.29 ? 98 LYS B CD 1 ATOM 2819 C CE . LYS B 1 98 ? 38.288 20.490 33.587 1.00 66.30 ? 98 LYS B CE 1 ATOM 2820 N NZ . LYS B 1 98 ? 38.496 20.765 32.125 1.00 69.93 ? 98 LYS B NZ 1 ATOM 2821 N N . GLU B 1 99 ? 43.561 19.683 32.777 1.00 64.82 ? 99 GLU B N 1 ATOM 2822 C CA . GLU B 1 99 ? 44.050 20.267 31.548 1.00 64.57 ? 99 GLU B CA 1 ATOM 2823 C C . GLU B 1 99 ? 43.258 21.466 31.055 1.00 64.14 ? 99 GLU B C 1 ATOM 2824 O O . GLU B 1 99 ? 42.043 21.387 30.845 1.00 63.62 ? 99 GLU B O 1 ATOM 2825 C CB . GLU B 1 99 ? 44.205 19.194 30.471 1.00 63.90 ? 99 GLU B CB 1 ATOM 2826 C CG . GLU B 1 99 ? 43.156 18.949 29.419 1.00 61.38 ? 99 GLU B CG 1 ATOM 2827 C CD . GLU B 1 99 ? 43.036 19.963 28.304 1.00 59.62 ? 99 GLU B CD 1 ATOM 2828 O OE1 . GLU B 1 99 ? 43.878 20.851 28.080 1.00 59.32 ? 99 GLU B OE1 1 ATOM 2829 O OE2 . GLU B 1 99 ? 41.989 19.885 27.643 1.00 60.25 ? 99 GLU B OE2 1 ATOM 2830 N N . ILE B 1 100 ? 43.956 22.588 30.904 1.00 64.20 ? 100 ILE B N 1 ATOM 2831 C CA . ILE B 1 100 ? 43.347 23.756 30.277 1.00 65.50 ? 100 ILE B CA 1 ATOM 2832 C C . ILE B 1 100 ? 44.268 24.238 29.154 1.00 67.03 ? 100 ILE B C 1 ATOM 2833 O O . ILE B 1 100 ? 44.398 25.419 28.795 1.00 66.98 ? 100 ILE B O 1 ATOM 2834 C CB . ILE B 1 100 ? 42.895 24.900 31.189 1.00 62.13 ? 100 ILE B CB 1 ATOM 2835 C CG1 . ILE B 1 100 ? 43.957 25.319 32.192 1.00 61.11 ? 100 ILE B CG1 1 ATOM 2836 C CG2 . ILE B 1 100 ? 41.607 24.586 31.924 1.00 57.17 ? 100 ILE B CG2 1 ATOM 2837 C CD1 . ILE B 1 100 ? 43.844 26.716 32.750 1.00 60.25 ? 100 ILE B CD1 1 ATOM 2838 N N . ASN B 1 101 ? 44.602 23.259 28.283 1.00 68.55 ? 101 ASN B N 1 ATOM 2839 C CA . ASN B 1 101 ? 45.397 23.516 27.087 1.00 69.82 ? 101 ASN B CA 1 ATOM 2840 C C . ASN B 1 101 ? 44.601 24.502 26.226 1.00 70.44 ? 101 ASN B C 1 ATOM 2841 O O . ASN B 1 101 ? 45.041 25.600 25.912 1.00 69.40 ? 101 ASN B O 1 ATOM 2842 C CB . ASN B 1 101 ? 45.736 22.300 26.265 1.00 72.23 ? 101 ASN B CB 1 ATOM 2843 C CG . ASN B 1 101 ? 46.607 21.271 26.958 1.00 74.90 ? 101 ASN B CG 1 ATOM 2844 O OD1 . ASN B 1 101 ? 47.714 21.588 27.443 1.00 75.86 ? 101 ASN B OD1 1 ATOM 2845 N ND2 . ASN B 1 101 ? 46.065 20.041 26.988 1.00 73.19 ? 101 ASN B ND2 1 ATOM 2846 N N . ASP B 1 102 ? 43.297 24.267 26.212 1.00 71.55 ? 102 ASP B N 1 ATOM 2847 C CA . ASP B 1 102 ? 42.322 25.139 25.602 1.00 73.19 ? 102 ASP B CA 1 ATOM 2848 C C . ASP B 1 102 ? 42.553 26.631 25.790 1.00 73.38 ? 102 ASP B C 1 ATOM 2849 O O . ASP B 1 102 ? 42.068 27.386 24.931 1.00 73.45 ? 102 ASP B O 1 ATOM 2850 C CB . ASP B 1 102 ? 40.942 24.713 26.071 1.00 77.83 ? 102 ASP B CB 1 ATOM 2851 C CG . ASP B 1 102 ? 40.823 23.781 27.266 1.00 81.87 ? 102 ASP B CG 1 ATOM 2852 O OD1 . ASP B 1 102 ? 41.032 22.537 27.083 1.00 83.25 ? 102 ASP B OD1 1 ATOM 2853 O OD2 . ASP B 1 102 ? 40.390 24.240 28.375 1.00 80.85 ? 102 ASP B OD2 1 ATOM 2854 N N . ILE B 1 103 ? 43.064 27.107 26.912 1.00 72.80 ? 103 ILE B N 1 ATOM 2855 C CA . ILE B 1 103 ? 43.223 28.505 27.238 1.00 72.25 ? 103 ILE B CA 1 ATOM 2856 C C . ILE B 1 103 ? 44.684 28.877 27.349 1.00 72.11 ? 103 ILE B C 1 ATOM 2857 O O . ILE B 1 103 ? 45.010 30.037 27.604 1.00 72.99 ? 103 ILE B O 1 ATOM 2858 C CB . ILE B 1 103 ? 42.542 28.803 28.585 1.00 72.21 ? 103 ILE B CB 1 ATOM 2859 C CG1 . ILE B 1 103 ? 41.038 28.526 28.385 1.00 71.60 ? 103 ILE B CG1 1 ATOM 2860 C CG2 . ILE B 1 103 ? 42.720 30.124 29.260 1.00 70.54 ? 103 ILE B CG2 1 ATOM 2861 C CD1 . ILE B 1 103 ? 40.809 27.153 28.981 1.00 74.83 ? 103 ILE B CD1 1 ATOM 2862 N N . CYS B 1 104 ? 45.611 27.951 27.447 1.00 71.50 ? 104 CYS B N 1 ATOM 2863 C CA . CYS B 1 104 ? 47.036 28.187 27.386 1.00 70.57 ? 104 CYS B CA 1 ATOM 2864 C C . CYS B 1 104 ? 47.688 26.799 27.402 1.00 70.65 ? 104 CYS B C 1 ATOM 2865 O O . CYS B 1 104 ? 47.072 25.872 27.920 1.00 70.78 ? 104 CYS B O 1 ATOM 2866 C CB . CYS B 1 104 ? 47.825 28.988 28.384 1.00 67.13 ? 104 CYS B CB 1 ATOM 2867 S SG . CYS B 1 104 ? 47.351 28.926 30.116 1.00 66.14 ? 104 CYS B SG 1 ATOM 2868 N N . SER B 1 105 ? 48.971 26.767 27.086 1.00 70.77 ? 105 SER B N 1 ATOM 2869 C CA . SER B 1 105 ? 49.517 25.438 26.858 1.00 70.37 ? 105 SER B CA 1 ATOM 2870 C C . SER B 1 105 ? 50.363 24.879 27.955 1.00 69.81 ? 105 SER B C 1 ATOM 2871 O O . SER B 1 105 ? 51.200 25.522 28.550 1.00 69.79 ? 105 SER B O 1 ATOM 2872 C CB . SER B 1 105 ? 50.141 25.319 25.468 1.00 71.72 ? 105 SER B CB 1 ATOM 2873 O OG . SER B 1 105 ? 49.180 24.667 24.635 1.00 72.56 ? 105 SER B OG 1 ATOM 2874 N N . GLY B 1 106 ? 49.975 23.650 28.289 1.00 69.45 ? 106 GLY B N 1 ATOM 2875 C CA . GLY B 1 106 ? 50.494 22.914 29.440 1.00 68.87 ? 106 GLY B CA 1 ATOM 2876 C C . GLY B 1 106 ? 49.921 23.453 30.758 1.00 68.32 ? 106 GLY B C 1 ATOM 2877 O O . GLY B 1 106 ? 50.387 23.152 31.857 1.00 68.36 ? 106 GLY B O 1 ATOM 2878 N N . CYS B 1 107 ? 48.903 24.298 30.696 1.00 67.18 ? 107 CYS B N 1 ATOM 2879 C CA . CYS B 1 107 ? 48.285 24.937 31.825 1.00 65.76 ? 107 CYS B CA 1 ATOM 2880 C C . CYS B 1 107 ? 47.257 23.972 32.427 1.00 64.66 ? 107 CYS B C 1 ATOM 2881 O O . CYS B 1 107 ? 46.562 23.328 31.637 1.00 63.65 ? 107 CYS B O 1 ATOM 2882 C CB . CYS B 1 107 ? 47.583 26.223 31.389 1.00 65.49 ? 107 CYS B CB 1 ATOM 2883 S SG . CYS B 1 107 ? 48.638 27.639 31.046 1.00 63.58 ? 107 CYS B SG 1 ATOM 2884 N N . ARG B 1 108 ? 47.148 24.003 33.762 1.00 62.80 ? 108 ARG B N 1 ATOM 2885 C CA . ARG B 1 108 ? 46.145 23.161 34.398 1.00 61.65 ? 108 ARG B CA 1 ATOM 2886 C C . ARG B 1 108 ? 45.371 24.053 35.375 1.00 60.71 ? 108 ARG B C 1 ATOM 2887 O O . ARG B 1 108 ? 45.938 24.862 36.119 1.00 60.81 ? 108 ARG B O 1 ATOM 2888 C CB . ARG B 1 108 ? 46.688 21.917 35.065 1.00 62.12 ? 108 ARG B CB 1 ATOM 2889 C CG . ARG B 1 108 ? 47.806 21.097 34.475 1.00 62.00 ? 108 ARG B CG 1 ATOM 2890 C CD . ARG B 1 108 ? 48.114 19.822 35.277 1.00 62.24 ? 108 ARG B CD 1 ATOM 2891 N NE . ARG B 1 108 ? 47.168 18.782 34.897 1.00 63.63 ? 108 ARG B NE 1 ATOM 2892 C CZ . ARG B 1 108 ? 46.487 18.005 35.723 1.00 65.02 ? 108 ARG B CZ 1 ATOM 2893 N NH1 . ARG B 1 108 ? 46.695 18.064 37.037 1.00 68.79 ? 108 ARG B NH1 1 ATOM 2894 N NH2 . ARG B 1 108 ? 45.573 17.170 35.247 1.00 64.50 ? 108 ARG B NH2 1 ATOM 2895 N N . GLY B 1 109 ? 44.050 23.907 35.367 1.00 59.27 ? 109 GLY B N 1 ATOM 2896 C CA . GLY B 1 109 ? 43.231 24.739 36.229 1.00 57.74 ? 109 GLY B CA 1 ATOM 2897 C C . GLY B 1 109 ? 42.404 23.889 37.185 1.00 57.10 ? 109 GLY B C 1 ATOM 2898 O O . GLY B 1 109 ? 42.048 22.761 36.848 1.00 56.66 ? 109 GLY B O 1 ATOM 2899 N N . HIS B 1 110 ? 41.963 24.546 38.266 1.00 56.01 ? 110 HIS B N 1 ATOM 2900 C CA . HIS B 1 110 ? 41.045 23.908 39.209 1.00 55.47 ? 110 HIS B CA 1 ATOM 2901 C C . HIS B 1 110 ? 39.946 23.259 38.397 1.00 55.35 ? 110 HIS B C 1 ATOM 2902 O O . HIS B 1 110 ? 39.424 23.940 37.531 1.00 55.35 ? 110 HIS B O 1 ATOM 2903 C CB . HIS B 1 110 ? 40.508 24.945 40.209 1.00 50.91 ? 110 HIS B CB 1 ATOM 2904 C CG . HIS B 1 110 ? 39.566 24.358 41.222 1.00 47.57 ? 110 HIS B CG 1 ATOM 2905 N ND1 . HIS B 1 110 ? 38.194 24.308 40.990 1.00 45.19 ? 110 HIS B ND1 1 ATOM 2906 C CD2 . HIS B 1 110 ? 39.795 23.779 42.423 1.00 46.00 ? 110 HIS B CD2 1 ATOM 2907 C CE1 . HIS B 1 110 ? 37.614 23.703 42.005 1.00 47.94 ? 110 HIS B CE1 1 ATOM 2908 N NE2 . HIS B 1 110 ? 38.567 23.366 42.890 1.00 49.05 ? 110 HIS B NE2 1 ATOM 2909 N N . ASP B 1 111 ? 39.355 22.136 38.720 1.00 56.07 ? 111 ASP B N 1 ATOM 2910 C CA . ASP B 1 111 ? 38.511 21.472 37.725 1.00 56.33 ? 111 ASP B CA 1 ATOM 2911 C C . ASP B 1 111 ? 37.076 21.874 37.893 1.00 55.11 ? 111 ASP B C 1 ATOM 2912 O O . ASP B 1 111 ? 36.404 22.075 36.872 1.00 55.50 ? 111 ASP B O 1 ATOM 2913 C CB . ASP B 1 111 ? 38.899 19.999 37.548 1.00 59.29 ? 111 ASP B CB 1 ATOM 2914 C CG . ASP B 1 111 ? 37.669 19.179 37.227 1.00 61.79 ? 111 ASP B CG 1 ATOM 2915 O OD1 . ASP B 1 111 ? 37.147 19.066 36.089 1.00 64.25 ? 111 ASP B OD1 1 ATOM 2916 O OD2 . ASP B 1 111 ? 36.958 18.713 38.130 1.00 64.06 ? 111 ASP B OD2 1 ATOM 2917 N N . GLY B 1 112 ? 36.617 22.218 39.061 1.00 54.80 ? 112 GLY B N 1 ATOM 2918 C CA . GLY B 1 112 ? 35.214 22.693 39.107 1.00 54.32 ? 112 GLY B CA 1 ATOM 2919 C C . GLY B 1 112 ? 35.171 24.080 38.482 1.00 53.97 ? 112 GLY B C 1 ATOM 2920 O O . GLY B 1 112 ? 34.183 24.409 37.827 1.00 54.22 ? 112 GLY B O 1 ATOM 2921 N N . PHE B 1 113 ? 36.087 24.992 38.808 1.00 53.20 ? 113 PHE B N 1 ATOM 2922 C CA . PHE B 1 113 ? 36.045 26.363 38.332 1.00 52.07 ? 113 PHE B CA 1 ATOM 2923 C C . PHE B 1 113 ? 36.043 26.360 36.819 1.00 53.17 ? 113 PHE B C 1 ATOM 2924 O O . PHE B 1 113 ? 35.103 26.817 36.176 1.00 54.34 ? 113 PHE B O 1 ATOM 2925 C CB . PHE B 1 113 ? 37.199 27.224 38.814 1.00 42.47 ? 113 PHE B CB 1 ATOM 2926 C CG . PHE B 1 113 ? 37.392 27.294 40.307 1.00 34.29 ? 113 PHE B CG 1 ATOM 2927 C CD1 . PHE B 1 113 ? 36.336 27.050 41.181 1.00 30.20 ? 113 PHE B CD1 1 ATOM 2928 C CD2 . PHE B 1 113 ? 38.635 27.639 40.809 1.00 28.90 ? 113 PHE B CD2 1 ATOM 2929 C CE1 . PHE B 1 113 ? 36.554 27.117 42.537 1.00 28.80 ? 113 PHE B CE1 1 ATOM 2930 C CE2 . PHE B 1 113 ? 38.846 27.733 42.168 1.00 27.03 ? 113 PHE B CE2 1 ATOM 2931 C CZ . PHE B 1 113 ? 37.802 27.426 43.028 1.00 28.49 ? 113 PHE B CZ 1 ATOM 2932 N N . THR B 1 114 ? 37.108 25.792 36.282 1.00 53.65 ? 114 THR B N 1 ATOM 2933 C CA . THR B 1 114 ? 37.244 25.650 34.830 1.00 53.82 ? 114 THR B CA 1 ATOM 2934 C C . THR B 1 114 ? 35.982 25.085 34.198 1.00 53.82 ? 114 THR B C 1 ATOM 2935 O O . THR B 1 114 ? 35.477 25.600 33.214 1.00 53.54 ? 114 THR B O 1 ATOM 2936 C CB . THR B 1 114 ? 38.437 24.687 34.609 1.00 53.64 ? 114 THR B CB 1 ATOM 2937 O OG1 . THR B 1 114 ? 39.642 25.386 34.948 1.00 52.15 ? 114 THR B OG1 1 ATOM 2938 C CG2 . THR B 1 114 ? 38.512 24.224 33.163 1.00 56.02 ? 114 THR B CG2 1 ATOM 2939 N N . SER B 1 115 ? 35.467 23.965 34.692 1.00 54.16 ? 115 SER B N 1 ATOM 2940 C CA . SER B 1 115 ? 34.292 23.323 34.175 1.00 54.40 ? 115 SER B CA 1 ATOM 2941 C C . SER B 1 115 ? 33.065 24.196 34.329 1.00 54.29 ? 115 SER B C 1 ATOM 2942 O O . SER B 1 115 ? 32.174 24.030 33.517 1.00 55.13 ? 115 SER B O 1 ATOM 2943 C CB . SER B 1 115 ? 33.912 22.023 34.920 1.00 54.61 ? 115 SER B CB 1 ATOM 2944 O OG . SER B 1 115 ? 34.993 21.123 34.968 1.00 52.52 ? 115 SER B OG 1 ATOM 2945 N N . SER B 1 116 ? 32.972 24.913 35.433 1.00 54.86 ? 116 SER B N 1 ATOM 2946 C CA . SER B 1 116 ? 31.778 25.713 35.665 1.00 55.04 ? 116 SER B CA 1 ATOM 2947 C C . SER B 1 116 ? 31.734 26.788 34.579 1.00 55.12 ? 116 SER B C 1 ATOM 2948 O O . SER B 1 116 ? 30.691 26.976 33.952 1.00 54.44 ? 116 SER B O 1 ATOM 2949 C CB . SER B 1 116 ? 31.729 26.358 37.037 1.00 55.06 ? 116 SER B CB 1 ATOM 2950 O OG . SER B 1 116 ? 31.845 25.447 38.088 1.00 53.55 ? 116 SER B OG 1 ATOM 2951 N N . TRP B 1 117 ? 32.861 27.486 34.447 1.00 55.42 ? 117 TRP B N 1 ATOM 2952 C CA . TRP B 1 117 ? 32.912 28.535 33.433 1.00 57.00 ? 117 TRP B CA 1 ATOM 2953 C C . TRP B 1 117 ? 32.530 27.969 32.062 1.00 57.93 ? 117 TRP B C 1 ATOM 2954 O O . TRP B 1 117 ? 31.618 28.474 31.410 1.00 57.94 ? 117 TRP B O 1 ATOM 2955 C CB . TRP B 1 117 ? 34.264 29.208 33.299 1.00 54.08 ? 117 TRP B CB 1 ATOM 2956 C CG . TRP B 1 117 ? 34.327 30.111 32.093 1.00 54.72 ? 117 TRP B CG 1 ATOM 2957 C CD1 . TRP B 1 117 ? 35.255 30.040 31.086 1.00 52.98 ? 117 TRP B CD1 1 ATOM 2958 C CD2 . TRP B 1 117 ? 33.455 31.192 31.770 1.00 53.65 ? 117 TRP B CD2 1 ATOM 2959 N NE1 . TRP B 1 117 ? 35.008 31.022 30.170 1.00 54.23 ? 117 TRP B NE1 1 ATOM 2960 C CE2 . TRP B 1 117 ? 33.908 31.748 30.565 1.00 55.70 ? 117 TRP B CE2 1 ATOM 2961 C CE3 . TRP B 1 117 ? 32.342 31.764 32.374 1.00 55.55 ? 117 TRP B CE3 1 ATOM 2962 C CZ2 . TRP B 1 117 ? 33.283 32.853 29.962 1.00 55.69 ? 117 TRP B CZ2 1 ATOM 2963 C CZ3 . TRP B 1 117 ? 31.724 32.851 31.788 1.00 54.39 ? 117 TRP B CZ3 1 ATOM 2964 C CH2 . TRP B 1 117 ? 32.197 33.381 30.584 1.00 54.10 ? 117 TRP B CH2 1 ATOM 2965 N N . ARG B 1 118 ? 33.263 26.928 31.686 1.00 58.65 ? 118 ARG B N 1 ATOM 2966 C CA . ARG B 1 118 ? 33.087 26.225 30.423 1.00 60.49 ? 118 ARG B CA 1 ATOM 2967 C C . ARG B 1 118 ? 31.640 25.853 30.152 1.00 60.66 ? 118 ARG B C 1 ATOM 2968 O O . ARG B 1 118 ? 31.128 26.219 29.083 1.00 61.15 ? 118 ARG B O 1 ATOM 2969 C CB . ARG B 1 118 ? 34.063 25.068 30.336 1.00 64.34 ? 118 ARG B CB 1 ATOM 2970 C CG . ARG B 1 118 ? 33.939 23.945 29.369 1.00 68.93 ? 118 ARG B CG 1 ATOM 2971 C CD . ARG B 1 118 ? 34.203 24.272 27.906 1.00 76.70 ? 118 ARG B CD 1 ATOM 2972 N NE . ARG B 1 118 ? 34.453 25.664 27.584 1.00 81.72 ? 118 ARG B NE 1 ATOM 2973 C CZ . ARG B 1 118 ? 35.576 26.373 27.541 1.00 83.12 ? 118 ARG B CZ 1 ATOM 2974 N NH1 . ARG B 1 118 ? 36.799 25.915 27.761 1.00 83.36 ? 118 ARG B NH1 1 ATOM 2975 N NH2 . ARG B 1 118 ? 35.428 27.673 27.251 1.00 85.49 ? 118 ARG B NH2 1 ATOM 2976 N N . SER B 1 119 ? 30.844 25.460 31.136 1.00 60.18 ? 119 SER B N 1 ATOM 2977 C CA . SER B 1 119 ? 29.442 25.175 30.905 1.00 59.90 ? 119 SER B CA 1 ATOM 2978 C C . SER B 1 119 ? 28.623 26.410 30.570 1.00 59.62 ? 119 SER B C 1 ATOM 2979 O O . SER B 1 119 ? 27.574 26.306 29.929 1.00 59.39 ? 119 SER B O 1 ATOM 2980 C CB . SER B 1 119 ? 28.843 24.469 32.125 1.00 61.58 ? 119 SER B CB 1 ATOM 2981 O OG . SER B 1 119 ? 27.423 24.614 32.094 1.00 64.38 ? 119 SER B OG 1 ATOM 2982 N N . VAL B 1 120 ? 29.020 27.581 31.041 1.00 59.47 ? 120 VAL B N 1 ATOM 2983 C CA . VAL B 1 120 ? 28.225 28.786 30.862 1.00 59.45 ? 120 VAL B CA 1 ATOM 2984 C C . VAL B 1 120 ? 28.945 29.735 29.913 1.00 59.50 ? 120 VAL B C 1 ATOM 2985 O O . VAL B 1 120 ? 28.377 30.741 29.513 1.00 59.46 ? 120 VAL B O 1 ATOM 2986 C CB . VAL B 1 120 ? 27.925 29.515 32.179 1.00 60.06 ? 120 VAL B CB 1 ATOM 2987 C CG1 . VAL B 1 120 ? 27.075 28.694 33.132 1.00 57.79 ? 120 VAL B CG1 1 ATOM 2988 C CG2 . VAL B 1 120 ? 29.219 29.937 32.868 1.00 61.00 ? 120 VAL B CG2 1 ATOM 2989 N N . ALA B 1 121 ? 30.097 29.312 29.436 1.00 59.73 ? 121 ALA B N 1 ATOM 2990 C CA . ALA B 1 121 ? 30.961 30.056 28.548 1.00 60.44 ? 121 ALA B CA 1 ATOM 2991 C C . ALA B 1 121 ? 30.307 30.617 27.321 1.00 61.25 ? 121 ALA B C 1 ATOM 2992 O O . ALA B 1 121 ? 30.083 31.845 27.326 1.00 61.61 ? 121 ALA B O 1 ATOM 2993 C CB . ALA B 1 121 ? 32.283 29.317 28.357 1.00 56.76 ? 121 ALA B CB 1 ATOM 2994 N N . ASP B 1 122 ? 30.083 29.941 26.211 1.00 62.26 ? 122 ASP B N 1 ATOM 2995 C CA . ASP B 1 122 ? 29.386 30.398 25.024 1.00 62.28 ? 122 ASP B CA 1 ATOM 2996 C C . ASP B 1 122 ? 28.239 31.365 25.268 1.00 62.08 ? 122 ASP B C 1 ATOM 2997 O O . ASP B 1 122 ? 28.227 32.396 24.600 1.00 62.19 ? 122 ASP B O 1 ATOM 2998 C CB . ASP B 1 122 ? 28.790 29.220 24.244 1.00 65.87 ? 122 ASP B CB 1 ATOM 2999 C CG . ASP B 1 122 ? 29.793 28.241 23.678 1.00 70.25 ? 122 ASP B CG 1 ATOM 3000 O OD1 . ASP B 1 122 ? 30.969 28.597 23.415 1.00 72.20 ? 122 ASP B OD1 1 ATOM 3001 O OD2 . ASP B 1 122 ? 29.417 27.060 23.471 1.00 72.59 ? 122 ASP B OD2 1 ATOM 3002 N N . THR B 1 123 ? 27.240 31.069 26.102 1.00 61.72 ? 123 THR B N 1 ATOM 3003 C CA . THR B 1 123 ? 26.191 32.060 26.356 1.00 61.63 ? 123 THR B CA 1 ATOM 3004 C C . THR B 1 123 ? 26.791 33.368 26.871 1.00 61.45 ? 123 THR B C 1 ATOM 3005 O O . THR B 1 123 ? 26.377 34.418 26.395 1.00 60.42 ? 123 THR B O 1 ATOM 3006 C CB . THR B 1 123 ? 25.131 31.520 27.333 1.00 60.67 ? 123 THR B CB 1 ATOM 3007 O OG1 . THR B 1 123 ? 24.757 30.263 26.784 1.00 59.39 ? 123 THR B OG1 1 ATOM 3008 C CG2 . THR B 1 123 ? 23.921 32.402 27.589 1.00 60.22 ? 123 THR B CG2 1 ATOM 3009 N N . LEU B 1 124 ? 27.618 33.329 27.921 1.00 61.44 ? 124 LEU B N 1 ATOM 3010 C CA . LEU B 1 124 ? 28.062 34.607 28.486 1.00 61.71 ? 124 LEU B CA 1 ATOM 3011 C C . LEU B 1 124 ? 28.849 35.511 27.566 1.00 61.57 ? 124 LEU B C 1 ATOM 3012 O O . LEU B 1 124 ? 28.352 36.584 27.193 1.00 61.48 ? 124 LEU B O 1 ATOM 3013 C CB . LEU B 1 124 ? 28.627 34.344 29.881 1.00 59.17 ? 124 LEU B CB 1 ATOM 3014 C CG . LEU B 1 124 ? 27.545 33.940 30.901 1.00 57.38 ? 124 LEU B CG 1 ATOM 3015 C CD1 . LEU B 1 124 ? 28.117 33.985 32.313 1.00 55.99 ? 124 LEU B CD1 1 ATOM 3016 C CD2 . LEU B 1 124 ? 26.282 34.781 30.795 1.00 55.02 ? 124 LEU B CD2 1 ATOM 3017 N N . ARG B 1 125 ? 29.810 34.999 26.839 1.00 61.82 ? 125 ARG B N 1 ATOM 3018 C CA . ARG B 1 125 ? 30.552 35.630 25.787 1.00 62.24 ? 125 ARG B CA 1 ATOM 3019 C C . ARG B 1 125 ? 29.608 36.138 24.706 1.00 61.26 ? 125 ARG B C 1 ATOM 3020 O O . ARG B 1 125 ? 29.807 37.277 24.277 1.00 60.73 ? 125 ARG B O 1 ATOM 3021 C CB . ARG B 1 125 ? 31.600 34.631 25.326 1.00 67.33 ? 125 ARG B CB 1 ATOM 3022 C CG . ARG B 1 125 ? 31.474 34.012 23.957 1.00 72.47 ? 125 ARG B CG 1 ATOM 3023 C CD . ARG B 1 125 ? 32.539 34.513 23.027 1.00 76.05 ? 125 ARG B CD 1 ATOM 3024 N NE . ARG B 1 125 ? 33.633 33.600 22.713 1.00 82.42 ? 125 ARG B NE 1 ATOM 3025 C CZ . ARG B 1 125 ? 34.591 33.951 21.836 1.00 85.99 ? 125 ARG B CZ 1 ATOM 3026 N NH1 . ARG B 1 125 ? 34.527 35.159 21.258 1.00 89.40 ? 125 ARG B NH1 1 ATOM 3027 N NH2 . ARG B 1 125 ? 35.621 33.197 21.481 1.00 85.42 ? 125 ARG B NH2 1 ATOM 3028 N N . GLN B 1 126 ? 28.469 35.487 24.507 1.00 60.32 ? 126 GLN B N 1 ATOM 3029 C CA . GLN B 1 126 ? 27.428 35.906 23.595 1.00 59.55 ? 126 GLN B CA 1 ATOM 3030 C C . GLN B 1 126 ? 26.738 37.166 24.082 1.00 57.74 ? 126 GLN B C 1 ATOM 3031 O O . GLN B 1 126 ? 26.697 38.183 23.407 1.00 56.87 ? 126 GLN B O 1 ATOM 3032 C CB . GLN B 1 126 ? 26.381 34.812 23.372 1.00 66.85 ? 126 GLN B CB 1 ATOM 3033 C CG . GLN B 1 126 ? 25.256 35.023 22.386 1.00 71.35 ? 126 GLN B CG 1 ATOM 3034 C CD . GLN B 1 126 ? 23.866 35.252 22.951 1.00 74.38 ? 126 GLN B CD 1 ATOM 3035 O OE1 . GLN B 1 126 ? 23.421 34.580 23.896 1.00 75.61 ? 126 GLN B OE1 1 ATOM 3036 N NE2 . GLN B 1 126 ? 23.150 36.212 22.354 1.00 72.74 ? 126 GLN B NE2 1 ATOM 3037 N N . LYS B 1 127 ? 26.491 37.220 25.387 1.00 57.35 ? 127 LYS B N 1 ATOM 3038 C CA . LYS B 1 127 ? 25.786 38.366 25.947 1.00 55.25 ? 127 LYS B CA 1 ATOM 3039 C C . LYS B 1 127 ? 26.727 39.548 25.943 1.00 54.30 ? 127 LYS B C 1 ATOM 3040 O O . LYS B 1 127 ? 26.447 40.662 25.474 1.00 53.91 ? 127 LYS B O 1 ATOM 3041 C CB . LYS B 1 127 ? 25.169 37.941 27.247 1.00 56.37 ? 127 LYS B CB 1 ATOM 3042 C CG . LYS B 1 127 ? 23.687 37.649 27.160 1.00 55.83 ? 127 LYS B CG 1 ATOM 3043 C CD . LYS B 1 127 ? 23.478 36.143 27.263 1.00 57.53 ? 127 LYS B CD 1 ATOM 3044 C CE . LYS B 1 127 ? 21.950 35.964 27.207 1.00 58.96 ? 127 LYS B CE 1 ATOM 3045 N NZ . LYS B 1 127 ? 21.342 36.766 26.107 1.00 57.88 ? 127 LYS B NZ 1 ATOM 3046 N N . VAL B 1 128 ? 28.001 39.251 26.192 1.00 53.36 ? 128 VAL B N 1 ATOM 3047 C CA . VAL B 1 128 ? 29.050 40.267 26.265 1.00 52.40 ? 128 VAL B CA 1 ATOM 3048 C C . VAL B 1 128 ? 29.289 40.895 24.898 1.00 52.33 ? 128 VAL B C 1 ATOM 3049 O O . VAL B 1 128 ? 29.570 42.084 24.790 1.00 51.13 ? 128 VAL B O 1 ATOM 3050 C CB . VAL B 1 128 ? 30.363 39.766 26.856 1.00 49.75 ? 128 VAL B CB 1 ATOM 3051 C CG1 . VAL B 1 128 ? 31.539 40.737 26.720 1.00 47.15 ? 128 VAL B CG1 1 ATOM 3052 C CG2 . VAL B 1 128 ? 30.143 39.404 28.320 1.00 48.15 ? 128 VAL B CG2 1 ATOM 3053 N N . GLU B 1 129 ? 29.452 40.010 23.921 1.00 52.86 ? 129 GLU B N 1 ATOM 3054 C CA . GLU B 1 129 ? 29.534 40.408 22.521 1.00 53.87 ? 129 GLU B CA 1 ATOM 3055 C C . GLU B 1 129 ? 28.394 41.339 22.104 1.00 54.34 ? 129 GLU B C 1 ATOM 3056 O O . GLU B 1 129 ? 28.676 42.426 21.570 1.00 54.29 ? 129 GLU B O 1 ATOM 3057 C CB . GLU B 1 129 ? 29.611 39.184 21.607 1.00 52.15 ? 129 GLU B CB 1 ATOM 3058 C CG . GLU B 1 129 ? 31.014 38.901 21.106 1.00 53.13 ? 129 GLU B CG 1 ATOM 3059 C CD . GLU B 1 129 ? 31.236 37.425 20.812 1.00 55.36 ? 129 GLU B CD 1 ATOM 3060 O OE1 . GLU B 1 129 ? 30.274 36.858 20.255 1.00 54.98 ? 129 GLU B OE1 1 ATOM 3061 O OE2 . GLU B 1 129 ? 32.325 36.901 21.155 1.00 56.72 ? 129 GLU B OE2 1 ATOM 3062 N N . ASP B 1 130 ? 27.147 41.045 22.469 1.00 54.39 ? 130 ASP B N 1 ATOM 3063 C CA . ASP B 1 130 ? 26.030 41.914 22.163 1.00 54.80 ? 130 ASP B CA 1 ATOM 3064 C C . ASP B 1 130 ? 26.144 43.241 22.901 1.00 55.73 ? 130 ASP B C 1 ATOM 3065 O O . ASP B 1 130 ? 25.929 44.298 22.294 1.00 56.98 ? 130 ASP B O 1 ATOM 3066 C CB . ASP B 1 130 ? 24.678 41.272 22.389 1.00 52.38 ? 130 ASP B CB 1 ATOM 3067 C CG . ASP B 1 130 ? 24.410 40.005 21.599 1.00 53.82 ? 130 ASP B CG 1 ATOM 3068 O OD1 . ASP B 1 130 ? 24.585 39.937 20.359 1.00 51.97 ? 130 ASP B OD1 1 ATOM 3069 O OD2 . ASP B 1 130 ? 24.007 38.993 22.224 1.00 52.42 ? 130 ASP B OD2 1 ATOM 3070 N N . ALA B 1 131 ? 26.768 43.271 24.077 1.00 55.55 ? 131 ALA B N 1 ATOM 3071 C CA . ALA B 1 131 ? 26.968 44.557 24.746 1.00 54.74 ? 131 ALA B CA 1 ATOM 3072 C C . ALA B 1 131 ? 28.102 45.312 24.083 1.00 54.80 ? 131 ALA B C 1 ATOM 3073 O O . ALA B 1 131 ? 28.080 46.539 23.960 1.00 54.33 ? 131 ALA B O 1 ATOM 3074 C CB . ALA B 1 131 ? 27.151 44.277 26.226 1.00 52.63 ? 131 ALA B CB 1 ATOM 3075 N N . VAL B 1 132 ? 29.164 44.604 23.689 1.00 55.34 ? 132 VAL B N 1 ATOM 3076 C CA . VAL B 1 132 ? 30.330 45.172 23.028 1.00 55.09 ? 132 VAL B CA 1 ATOM 3077 C C . VAL B 1 132 ? 30.002 45.806 21.687 1.00 55.66 ? 132 VAL B C 1 ATOM 3078 O O . VAL B 1 132 ? 30.512 46.897 21.397 1.00 55.23 ? 132 VAL B O 1 ATOM 3079 C CB . VAL B 1 132 ? 31.525 44.221 22.928 1.00 54.43 ? 132 VAL B CB 1 ATOM 3080 C CG1 . VAL B 1 132 ? 32.682 44.793 22.105 1.00 51.56 ? 132 VAL B CG1 1 ATOM 3081 C CG2 . VAL B 1 132 ? 32.073 43.786 24.291 1.00 51.47 ? 132 VAL B CG2 1 ATOM 3082 N N . ARG B 1 133 ? 29.057 45.280 20.920 1.00 56.85 ? 133 ARG B N 1 ATOM 3083 C CA . ARG B 1 133 ? 28.610 45.870 19.655 1.00 57.28 ? 133 ARG B CA 1 ATOM 3084 C C . ARG B 1 133 ? 27.802 47.124 19.904 1.00 57.24 ? 133 ARG B C 1 ATOM 3085 O O . ARG B 1 133 ? 28.163 48.160 19.379 1.00 57.44 ? 133 ARG B O 1 ATOM 3086 C CB . ARG B 1 133 ? 27.730 44.898 18.901 1.00 59.90 ? 133 ARG B CB 1 ATOM 3087 C CG . ARG B 1 133 ? 27.361 45.226 17.464 1.00 59.87 ? 133 ARG B CG 1 ATOM 3088 C CD . ARG B 1 133 ? 26.216 44.293 17.121 1.00 62.24 ? 133 ARG B CD 1 ATOM 3089 N NE . ARG B 1 133 ? 24.895 44.914 17.118 1.00 63.31 ? 133 ARG B NE 1 ATOM 3090 C CZ . ARG B 1 133 ? 23.868 44.332 17.734 1.00 65.49 ? 133 ARG B CZ 1 ATOM 3091 N NH1 . ARG B 1 133 ? 24.059 43.183 18.373 1.00 66.65 ? 133 ARG B NH1 1 ATOM 3092 N NH2 . ARG B 1 133 ? 22.712 44.967 17.646 1.00 67.46 ? 133 ARG B NH2 1 ATOM 3093 N N . GLU B 1 134 ? 26.716 47.071 20.644 1.00 58.11 ? 134 GLU B N 1 ATOM 3094 C CA . GLU B 1 134 ? 26.002 48.271 21.053 1.00 59.26 ? 134 GLU B CA 1 ATOM 3095 C C . GLU B 1 134 ? 26.899 49.376 21.572 1.00 58.59 ? 134 GLU B C 1 ATOM 3096 O O . GLU B 1 134 ? 26.670 50.546 21.325 1.00 59.06 ? 134 GLU B O 1 ATOM 3097 C CB . GLU B 1 134 ? 25.033 47.975 22.207 1.00 63.23 ? 134 GLU B CB 1 ATOM 3098 C CG . GLU B 1 134 ? 23.563 48.009 21.809 1.00 68.49 ? 134 GLU B CG 1 ATOM 3099 C CD . GLU B 1 134 ? 23.285 46.727 21.013 1.00 72.31 ? 134 GLU B CD 1 ATOM 3100 O OE1 . GLU B 1 134 ? 23.295 45.680 21.702 1.00 71.87 ? 134 GLU B OE1 1 ATOM 3101 O OE2 . GLU B 1 134 ? 23.125 46.861 19.773 1.00 74.38 ? 134 GLU B OE2 1 ATOM 3102 N N . HIS B 1 135 ? 27.818 49.125 22.492 1.00 58.68 ? 135 HIS B N 1 ATOM 3103 C CA . HIS B 1 135 ? 28.672 50.109 23.132 1.00 58.45 ? 135 HIS B CA 1 ATOM 3104 C C . HIS B 1 135 ? 30.136 49.802 22.906 1.00 58.48 ? 135 HIS B C 1 ATOM 3105 O O . HIS B 1 135 ? 30.882 49.394 23.800 1.00 59.55 ? 135 HIS B O 1 ATOM 3106 C CB . HIS B 1 135 ? 28.410 50.164 24.646 1.00 56.92 ? 135 HIS B CB 1 ATOM 3107 C CG . HIS B 1 135 ? 26.951 50.324 24.952 1.00 57.11 ? 135 HIS B CG 1 ATOM 3108 N ND1 . HIS B 1 135 ? 26.338 51.558 25.063 1.00 57.42 ? 135 HIS B ND1 1 ATOM 3109 C CD2 . HIS B 1 135 ? 25.998 49.371 25.108 1.00 56.85 ? 135 HIS B CD2 1 ATOM 3110 C CE1 . HIS B 1 135 ? 25.052 51.343 25.299 1.00 59.13 ? 135 HIS B CE1 1 ATOM 3111 N NE2 . HIS B 1 135 ? 24.811 50.027 25.340 1.00 58.09 ? 135 HIS B NE2 1 ATOM 3112 N N . PRO B 1 136 ? 30.599 49.995 21.677 1.00 57.80 ? 136 PRO B N 1 ATOM 3113 C CA . PRO B 1 136 ? 31.954 49.701 21.279 1.00 56.58 ? 136 PRO B CA 1 ATOM 3114 C C . PRO B 1 136 ? 32.980 50.452 22.094 1.00 55.12 ? 136 PRO B C 1 ATOM 3115 O O . PRO B 1 136 ? 34.105 50.003 22.219 1.00 54.73 ? 136 PRO B O 1 ATOM 3116 C CB . PRO B 1 136 ? 32.042 50.169 19.824 1.00 57.21 ? 136 PRO B CB 1 ATOM 3117 C CG . PRO B 1 136 ? 30.868 51.045 19.590 1.00 56.83 ? 136 PRO B CG 1 ATOM 3118 C CD . PRO B 1 136 ? 29.827 50.583 20.542 1.00 57.66 ? 136 PRO B CD 1 ATOM 3119 N N . ASP B 1 137 ? 32.656 51.683 22.426 1.00 54.21 ? 137 ASP B N 1 ATOM 3120 C CA . ASP B 1 137 ? 33.545 52.544 23.182 1.00 53.13 ? 137 ASP B CA 1 ATOM 3121 C C . ASP B 1 137 ? 33.834 51.976 24.569 1.00 50.68 ? 137 ASP B C 1 ATOM 3122 O O . ASP B 1 137 ? 34.902 52.292 25.024 1.00 51.13 ? 137 ASP B O 1 ATOM 3123 C CB . ASP B 1 137 ? 33.010 53.964 23.289 1.00 58.86 ? 137 ASP B CB 1 ATOM 3124 C CG . ASP B 1 137 ? 31.502 54.210 23.340 1.00 62.40 ? 137 ASP B CG 1 ATOM 3125 O OD1 . ASP B 1 137 ? 30.759 53.425 22.675 1.00 57.33 ? 137 ASP B OD1 1 ATOM 3126 O OD2 . ASP B 1 137 ? 31.075 55.216 24.028 1.00 63.24 ? 137 ASP B OD2 1 ATOM 3127 N N . TYR B 1 138 ? 32.846 51.566 25.309 1.00 48.28 ? 138 TYR B N 1 ATOM 3128 C CA . TYR B 1 138 ? 32.757 51.159 26.678 1.00 46.40 ? 138 TYR B CA 1 ATOM 3129 C C . TYR B 1 138 ? 33.642 49.952 26.960 1.00 46.59 ? 138 TYR B C 1 ATOM 3130 O O . TYR B 1 138 ? 33.781 49.083 26.112 1.00 47.49 ? 138 TYR B O 1 ATOM 3131 C CB . TYR B 1 138 ? 31.290 50.758 26.913 1.00 44.08 ? 138 TYR B CB 1 ATOM 3132 C CG . TYR B 1 138 ? 30.273 51.868 27.079 1.00 40.84 ? 138 TYR B CG 1 ATOM 3133 C CD1 . TYR B 1 138 ? 30.297 53.139 26.460 1.00 38.28 ? 138 TYR B CD1 1 ATOM 3134 C CD2 . TYR B 1 138 ? 29.244 51.574 27.952 1.00 39.08 ? 138 TYR B CD2 1 ATOM 3135 C CE1 . TYR B 1 138 ? 29.322 54.056 26.770 1.00 36.61 ? 138 TYR B CE1 1 ATOM 3136 C CE2 . TYR B 1 138 ? 28.236 52.473 28.189 1.00 37.88 ? 138 TYR B CE2 1 ATOM 3137 C CZ . TYR B 1 138 ? 28.293 53.714 27.604 1.00 36.95 ? 138 TYR B CZ 1 ATOM 3138 O OH . TYR B 1 138 ? 27.239 54.518 27.915 1.00 36.86 ? 138 TYR B OH 1 ATOM 3139 N N . ARG B 1 139 ? 34.380 49.883 28.037 1.00 45.78 ? 139 ARG B N 1 ATOM 3140 C CA . ARG B 1 139 ? 35.296 48.980 28.628 1.00 44.59 ? 139 ARG B CA 1 ATOM 3141 C C . ARG B 1 139 ? 34.557 47.802 29.304 1.00 44.36 ? 139 ARG B C 1 ATOM 3142 O O . ARG B 1 139 ? 33.670 47.991 30.139 1.00 44.51 ? 139 ARG B O 1 ATOM 3143 C CB . ARG B 1 139 ? 36.007 49.733 29.737 1.00 42.72 ? 139 ARG B CB 1 ATOM 3144 C CG . ARG B 1 139 ? 37.240 49.141 30.367 1.00 47.14 ? 139 ARG B CG 1 ATOM 3145 C CD . ARG B 1 139 ? 37.419 49.864 31.705 1.00 53.64 ? 139 ARG B CD 1 ATOM 3146 N NE . ARG B 1 139 ? 38.344 49.305 32.690 1.00 52.52 ? 139 ARG B NE 1 ATOM 3147 C CZ . ARG B 1 139 ? 38.651 50.004 33.785 1.00 55.09 ? 139 ARG B CZ 1 ATOM 3148 N NH1 . ARG B 1 139 ? 38.107 51.206 34.007 1.00 55.70 ? 139 ARG B NH1 1 ATOM 3149 N NH2 . ARG B 1 139 ? 39.527 49.471 34.634 1.00 55.79 ? 139 ARG B NH2 1 ATOM 3150 N N . VAL B 1 140 ? 34.924 46.603 28.883 1.00 42.40 ? 140 VAL B N 1 ATOM 3151 C CA . VAL B 1 140 ? 34.521 45.387 29.487 1.00 41.46 ? 140 VAL B CA 1 ATOM 3152 C C . VAL B 1 140 ? 35.333 45.075 30.741 1.00 41.90 ? 140 VAL B C 1 ATOM 3153 O O . VAL B 1 140 ? 36.559 44.972 30.645 1.00 41.10 ? 140 VAL B O 1 ATOM 3154 C CB . VAL B 1 140 ? 34.662 44.131 28.592 1.00 41.58 ? 140 VAL B CB 1 ATOM 3155 C CG1 . VAL B 1 140 ? 33.995 42.995 29.385 1.00 39.95 ? 140 VAL B CG1 1 ATOM 3156 C CG2 . VAL B 1 140 ? 34.067 44.430 27.219 1.00 35.85 ? 140 VAL B CG2 1 ATOM 3157 N N . VAL B 1 141 ? 34.561 44.855 31.813 1.00 40.83 ? 141 VAL B N 1 ATOM 3158 C CA . VAL B 1 141 ? 35.169 44.535 33.100 1.00 39.67 ? 141 VAL B CA 1 ATOM 3159 C C . VAL B 1 141 ? 34.508 43.269 33.640 1.00 38.95 ? 141 VAL B C 1 ATOM 3160 O O . VAL B 1 141 ? 33.281 43.164 33.660 1.00 38.63 ? 141 VAL B O 1 ATOM 3161 C CB . VAL B 1 141 ? 34.981 45.631 34.193 1.00 38.58 ? 141 VAL B CB 1 ATOM 3162 C CG1 . VAL B 1 141 ? 35.750 45.202 35.447 1.00 36.12 ? 141 VAL B CG1 1 ATOM 3163 C CG2 . VAL B 1 141 ? 35.572 46.970 33.755 1.00 37.46 ? 141 VAL B CG2 1 ATOM 3164 N N . PHE B 1 142 ? 35.309 42.258 33.932 1.00 38.96 ? 142 PHE B N 1 ATOM 3165 C CA . PHE B 1 142 ? 34.798 41.089 34.654 1.00 38.22 ? 142 PHE B CA 1 ATOM 3166 C C . PHE B 1 142 ? 35.228 41.228 36.113 1.00 37.37 ? 142 PHE B C 1 ATOM 3167 O O . PHE B 1 142 ? 36.368 41.585 36.445 1.00 36.84 ? 142 PHE B O 1 ATOM 3168 C CB . PHE B 1 142 ? 35.192 39.725 34.120 1.00 39.89 ? 142 PHE B CB 1 ATOM 3169 C CG . PHE B 1 142 ? 34.777 39.394 32.718 1.00 43.07 ? 142 PHE B CG 1 ATOM 3170 C CD1 . PHE B 1 142 ? 33.872 40.158 31.995 1.00 43.22 ? 142 PHE B CD1 1 ATOM 3171 C CD2 . PHE B 1 142 ? 35.325 38.275 32.089 1.00 43.82 ? 142 PHE B CD2 1 ATOM 3172 C CE1 . PHE B 1 142 ? 33.524 39.843 30.696 1.00 42.91 ? 142 PHE B CE1 1 ATOM 3173 C CE2 . PHE B 1 142 ? 34.979 37.935 30.798 1.00 42.57 ? 142 PHE B CE2 1 ATOM 3174 C CZ . PHE B 1 142 ? 34.072 38.715 30.113 1.00 43.56 ? 142 PHE B CZ 1 ATOM 3175 N N . THR B 1 143 ? 34.279 40.939 37.004 1.00 36.98 ? 143 THR B N 1 ATOM 3176 C CA . THR B 1 143 ? 34.600 41.031 38.437 1.00 35.55 ? 143 THR B CA 1 ATOM 3177 C C . THR B 1 143 ? 33.903 39.954 39.209 1.00 35.91 ? 143 THR B C 1 ATOM 3178 O O . THR B 1 143 ? 32.956 39.290 38.754 1.00 36.45 ? 143 THR B O 1 ATOM 3179 C CB . THR B 1 143 ? 34.155 42.390 38.985 1.00 32.09 ? 143 THR B CB 1 ATOM 3180 O OG1 . THR B 1 143 ? 34.801 42.577 40.268 1.00 36.62 ? 143 THR B OG1 1 ATOM 3181 C CG2 . THR B 1 143 ? 32.688 42.555 39.245 1.00 28.07 ? 143 THR B CG2 1 ATOM 3182 N N . GLY B 1 144 ? 34.361 39.766 40.452 1.00 36.50 ? 144 GLY B N 1 ATOM 3183 C CA . GLY B 1 144 ? 33.718 38.850 41.403 1.00 35.65 ? 144 GLY B CA 1 ATOM 3184 C C . GLY B 1 144 ? 34.492 38.688 42.700 1.00 36.56 ? 144 GLY B C 1 ATOM 3185 O O . GLY B 1 144 ? 35.707 38.960 42.789 1.00 35.19 ? 144 GLY B O 1 ATOM 3186 N N . HIS B 1 145 ? 33.747 38.213 43.729 1.00 36.90 ? 145 HIS B N 1 ATOM 3187 C CA . HIS B 1 145 ? 34.447 37.945 45.002 1.00 37.21 ? 145 HIS B CA 1 ATOM 3188 C C . HIS B 1 145 ? 34.386 36.455 45.274 1.00 37.81 ? 145 HIS B C 1 ATOM 3189 O O . HIS B 1 145 ? 33.499 35.792 44.746 1.00 37.73 ? 145 HIS B O 1 ATOM 3190 C CB . HIS B 1 145 ? 33.784 38.723 46.116 1.00 37.39 ? 145 HIS B CB 1 ATOM 3191 C CG . HIS B 1 145 ? 33.931 38.177 47.510 1.00 34.61 ? 145 HIS B CG 1 ATOM 3192 N ND1 . HIS B 1 145 ? 33.013 37.291 48.014 1.00 31.56 ? 145 HIS B ND1 1 ATOM 3193 C CD2 . HIS B 1 145 ? 34.832 38.439 48.491 1.00 32.68 ? 145 HIS B CD2 1 ATOM 3194 C CE1 . HIS B 1 145 ? 33.368 37.005 49.278 1.00 35.23 ? 145 HIS B CE1 1 ATOM 3195 N NE2 . HIS B 1 145 ? 34.471 37.667 49.567 1.00 35.00 ? 145 HIS B NE2 1 ATOM 3196 N N . SER B 1 146 ? 35.418 35.893 45.882 1.00 38.53 ? 146 SER B N 1 ATOM 3197 C CA . SER B 1 146 ? 35.398 34.476 46.243 1.00 39.31 ? 146 SER B CA 1 ATOM 3198 C C . SER B 1 146 ? 35.345 33.572 45.042 1.00 39.92 ? 146 SER B C 1 ATOM 3199 O O . SER B 1 146 ? 36.211 33.653 44.154 1.00 40.98 ? 146 SER B O 1 ATOM 3200 C CB . SER B 1 146 ? 34.192 34.195 47.165 1.00 40.90 ? 146 SER B CB 1 ATOM 3201 O OG . SER B 1 146 ? 34.598 33.297 48.184 1.00 42.94 ? 146 SER B OG 1 ATOM 3202 N N . LEU B 1 147 ? 34.563 32.497 45.055 1.00 40.06 ? 147 LEU B N 1 ATOM 3203 C CA . LEU B 1 147 ? 34.370 31.694 43.831 1.00 39.85 ? 147 LEU B CA 1 ATOM 3204 C C . LEU B 1 147 ? 34.081 32.541 42.605 1.00 39.15 ? 147 LEU B C 1 ATOM 3205 O O . LEU B 1 147 ? 34.671 32.369 41.533 1.00 39.41 ? 147 LEU B O 1 ATOM 3206 C CB . LEU B 1 147 ? 33.257 30.663 44.117 1.00 40.74 ? 147 LEU B CB 1 ATOM 3207 C CG . LEU B 1 147 ? 32.536 30.014 42.948 1.00 39.06 ? 147 LEU B CG 1 ATOM 3208 C CD1 . LEU B 1 147 ? 33.461 29.179 42.071 1.00 34.31 ? 147 LEU B CD1 1 ATOM 3209 C CD2 . LEU B 1 147 ? 31.307 29.240 43.377 1.00 34.65 ? 147 LEU B CD2 1 ATOM 3210 N N . GLY B 1 148 ? 33.253 33.575 42.684 1.00 38.27 ? 148 GLY B N 1 ATOM 3211 C CA . GLY B 1 148 ? 32.889 34.479 41.627 1.00 37.80 ? 148 GLY B CA 1 ATOM 3212 C C . GLY B 1 148 ? 34.129 35.161 41.069 1.00 38.27 ? 148 GLY B C 1 ATOM 3213 O O . GLY B 1 148 ? 34.294 35.337 39.879 1.00 37.12 ? 148 GLY B O 1 ATOM 3214 N N . GLY B 1 149 ? 35.083 35.482 41.954 1.00 38.21 ? 149 GLY B N 1 ATOM 3215 C CA . GLY B 1 149 ? 36.374 36.006 41.572 1.00 38.51 ? 149 GLY B CA 1 ATOM 3216 C C . GLY B 1 149 ? 37.128 34.967 40.745 1.00 40.23 ? 149 GLY B C 1 ATOM 3217 O O . GLY B 1 149 ? 37.898 35.340 39.841 1.00 40.21 ? 149 GLY B O 1 ATOM 3218 N N . ALA B 1 150 ? 36.915 33.672 41.082 1.00 39.49 ? 150 ALA B N 1 ATOM 3219 C CA . ALA B 1 150 ? 37.551 32.591 40.372 1.00 38.62 ? 150 ALA B CA 1 ATOM 3220 C C . ALA B 1 150 ? 36.853 32.523 39.008 1.00 38.73 ? 150 ALA B C 1 ATOM 3221 O O . ALA B 1 150 ? 37.611 32.422 38.052 1.00 38.40 ? 150 ALA B O 1 ATOM 3222 C CB . ALA B 1 150 ? 37.569 31.248 41.067 1.00 34.22 ? 150 ALA B CB 1 ATOM 3223 N N . LEU B 1 151 ? 35.559 32.766 38.947 1.00 39.00 ? 151 LEU B N 1 ATOM 3224 C CA . LEU B 1 151 ? 34.962 32.751 37.636 1.00 39.74 ? 151 LEU B CA 1 ATOM 3225 C C . LEU B 1 151 ? 35.363 33.971 36.846 1.00 41.19 ? 151 LEU B C 1 ATOM 3226 O O . LEU B 1 151 ? 35.921 33.695 35.754 1.00 43.47 ? 151 LEU B O 1 ATOM 3227 C CB . LEU B 1 151 ? 33.446 32.662 37.720 1.00 38.84 ? 151 LEU B CB 1 ATOM 3228 C CG . LEU B 1 151 ? 33.103 31.350 38.474 1.00 39.58 ? 151 LEU B CG 1 ATOM 3229 C CD1 . LEU B 1 151 ? 31.619 31.265 38.800 1.00 39.03 ? 151 LEU B CD1 1 ATOM 3230 C CD2 . LEU B 1 151 ? 33.512 30.170 37.576 1.00 36.68 ? 151 LEU B CD2 1 ATOM 3231 N N . ALA B 1 152 ? 35.408 35.176 37.420 1.00 40.66 ? 152 ALA B N 1 ATOM 3232 C CA . ALA B 1 152 ? 35.854 36.277 36.582 1.00 40.92 ? 152 ALA B CA 1 ATOM 3233 C C . ALA B 1 152 ? 37.230 35.949 35.973 1.00 41.02 ? 152 ALA B C 1 ATOM 3234 O O . ALA B 1 152 ? 37.448 36.263 34.798 1.00 40.32 ? 152 ALA B O 1 ATOM 3235 C CB . ALA B 1 152 ? 35.932 37.645 37.232 1.00 36.23 ? 152 ALA B CB 1 ATOM 3236 N N . THR B 1 153 ? 38.138 35.448 36.811 1.00 40.98 ? 153 THR B N 1 ATOM 3237 C CA . THR B 1 153 ? 39.497 35.232 36.375 1.00 41.73 ? 153 THR B CA 1 ATOM 3238 C C . THR B 1 153 ? 39.577 34.203 35.271 1.00 42.72 ? 153 THR B C 1 ATOM 3239 O O . THR B 1 153 ? 40.204 34.531 34.257 1.00 43.65 ? 153 THR B O 1 ATOM 3240 C CB . THR B 1 153 ? 40.401 34.806 37.520 1.00 43.51 ? 153 THR B CB 1 ATOM 3241 O OG1 . THR B 1 153 ? 40.383 35.842 38.528 1.00 40.50 ? 153 THR B OG1 1 ATOM 3242 C CG2 . THR B 1 153 ? 41.822 34.518 37.064 1.00 39.93 ? 153 THR B CG2 1 ATOM 3243 N N . VAL B 1 154 ? 38.935 33.067 35.418 1.00 42.82 ? 154 VAL B N 1 ATOM 3244 C CA . VAL B 1 154 ? 39.024 32.051 34.356 1.00 43.69 ? 154 VAL B CA 1 ATOM 3245 C C . VAL B 1 154 ? 38.422 32.580 33.061 1.00 44.76 ? 154 VAL B C 1 ATOM 3246 O O . VAL B 1 154 ? 39.025 32.542 31.994 1.00 44.57 ? 154 VAL B O 1 ATOM 3247 C CB . VAL B 1 154 ? 38.328 30.737 34.756 1.00 41.52 ? 154 VAL B CB 1 ATOM 3248 C CG1 . VAL B 1 154 ? 38.395 29.715 33.631 1.00 39.50 ? 154 VAL B CG1 1 ATOM 3249 C CG2 . VAL B 1 154 ? 38.951 30.164 36.020 1.00 37.05 ? 154 VAL B CG2 1 ATOM 3250 N N . ALA B 1 155 ? 37.182 33.060 33.178 1.00 45.53 ? 155 ALA B N 1 ATOM 3251 C CA . ALA B 1 155 ? 36.459 33.628 32.045 1.00 46.57 ? 155 ALA B CA 1 ATOM 3252 C C . ALA B 1 155 ? 37.201 34.765 31.344 1.00 46.73 ? 155 ALA B C 1 ATOM 3253 O O . ALA B 1 155 ? 37.191 34.869 30.115 1.00 46.58 ? 155 ALA B O 1 ATOM 3254 C CB . ALA B 1 155 ? 35.086 34.123 32.493 1.00 44.59 ? 155 ALA B CB 1 ATOM 3255 N N . GLY B 1 156 ? 37.948 35.564 32.094 1.00 46.85 ? 156 GLY B N 1 ATOM 3256 C CA . GLY B 1 156 ? 38.676 36.659 31.454 1.00 47.75 ? 156 GLY B CA 1 ATOM 3257 C C . GLY B 1 156 ? 39.903 36.067 30.768 1.00 48.23 ? 156 GLY B C 1 ATOM 3258 O O . GLY B 1 156 ? 40.258 36.479 29.678 1.00 48.13 ? 156 GLY B O 1 ATOM 3259 N N . ALA B 1 157 ? 40.479 35.000 31.319 1.00 48.56 ? 157 ALA B N 1 ATOM 3260 C CA . ALA B 1 157 ? 41.612 34.346 30.691 1.00 48.28 ? 157 ALA B CA 1 ATOM 3261 C C . ALA B 1 157 ? 41.084 33.803 29.383 1.00 48.59 ? 157 ALA B C 1 ATOM 3262 O O . ALA B 1 157 ? 41.831 33.794 28.400 1.00 49.30 ? 157 ALA B O 1 ATOM 3263 C CB . ALA B 1 157 ? 42.258 33.263 31.519 1.00 48.29 ? 157 ALA B CB 1 ATOM 3264 N N . ASP B 1 158 ? 39.915 33.230 29.339 1.00 48.78 ? 158 ASP B N 1 ATOM 3265 C CA . ASP B 1 158 ? 39.304 32.696 28.157 1.00 49.30 ? 158 ASP B CA 1 ATOM 3266 C C . ASP B 1 158 ? 38.774 33.591 27.040 1.00 50.02 ? 158 ASP B C 1 ATOM 3267 O O . ASP B 1 158 ? 38.475 33.039 25.973 1.00 50.50 ? 158 ASP B O 1 ATOM 3268 C CB . ASP B 1 158 ? 37.998 32.003 28.641 1.00 50.14 ? 158 ASP B CB 1 ATOM 3269 C CG . ASP B 1 158 ? 37.868 30.809 27.737 1.00 51.68 ? 158 ASP B CG 1 ATOM 3270 O OD1 . ASP B 1 158 ? 38.853 30.596 26.987 1.00 56.93 ? 158 ASP B OD1 1 ATOM 3271 O OD2 . ASP B 1 158 ? 36.828 30.164 27.821 1.00 50.17 ? 158 ASP B OD2 1 ATOM 3272 N N . LEU B 1 159 ? 38.285 34.805 27.298 1.00 49.40 ? 159 LEU B N 1 ATOM 3273 C CA . LEU B 1 159 ? 37.532 35.540 26.283 1.00 48.95 ? 159 LEU B CA 1 ATOM 3274 C C . LEU B 1 159 ? 38.386 36.604 25.636 1.00 48.42 ? 159 LEU B C 1 ATOM 3275 O O . LEU B 1 159 ? 38.071 37.259 24.674 1.00 48.49 ? 159 LEU B O 1 ATOM 3276 C CB . LEU B 1 159 ? 36.197 36.042 26.864 1.00 45.51 ? 159 LEU B CB 1 ATOM 3277 C CG . LEU B 1 159 ? 35.309 34.891 27.299 1.00 45.72 ? 159 LEU B CG 1 ATOM 3278 C CD1 . LEU B 1 159 ? 33.873 35.364 27.545 1.00 46.92 ? 159 LEU B CD1 1 ATOM 3279 C CD2 . LEU B 1 159 ? 35.256 33.737 26.294 1.00 43.08 ? 159 LEU B CD2 1 ATOM 3280 N N . ARG B 1 160 ? 39.417 36.987 26.334 1.00 49.05 ? 160 ARG B N 1 ATOM 3281 C CA . ARG B 1 160 ? 40.428 37.942 25.950 1.00 50.28 ? 160 ARG B CA 1 ATOM 3282 C C . ARG B 1 160 ? 40.884 37.538 24.556 1.00 50.70 ? 160 ARG B C 1 ATOM 3283 O O . ARG B 1 160 ? 40.760 36.382 24.206 1.00 50.62 ? 160 ARG B O 1 ATOM 3284 C CB . ARG B 1 160 ? 41.585 37.846 26.958 1.00 50.23 ? 160 ARG B CB 1 ATOM 3285 C CG . ARG B 1 160 ? 41.525 38.936 28.011 1.00 49.62 ? 160 ARG B CG 1 ATOM 3286 C CD . ARG B 1 160 ? 42.243 38.523 29.292 1.00 48.85 ? 160 ARG B CD 1 ATOM 3287 N NE . ARG B 1 160 ? 42.164 39.589 30.275 1.00 46.38 ? 160 ARG B NE 1 ATOM 3288 C CZ . ARG B 1 160 ? 42.963 39.643 31.328 1.00 44.07 ? 160 ARG B CZ 1 ATOM 3289 N NH1 . ARG B 1 160 ? 43.841 38.672 31.467 1.00 43.72 ? 160 ARG B NH1 1 ATOM 3290 N NH2 . ARG B 1 160 ? 42.871 40.629 32.190 1.00 43.00 ? 160 ARG B NH2 1 ATOM 3291 N N . GLY B 1 161 ? 41.482 38.433 23.790 1.00 52.09 ? 161 GLY B N 1 ATOM 3292 C CA . GLY B 1 161 ? 41.903 38.208 22.432 1.00 51.76 ? 161 GLY B CA 1 ATOM 3293 C C . GLY B 1 161 ? 40.839 38.234 21.354 1.00 51.99 ? 161 GLY B C 1 ATOM 3294 O O . GLY B 1 161 ? 41.247 37.843 20.253 1.00 52.74 ? 161 GLY B O 1 ATOM 3295 N N . ASN B 1 162 ? 39.554 38.489 21.507 1.00 51.53 ? 162 ASN B N 1 ATOM 3296 C CA . ASN B 1 162 ? 38.618 38.542 20.394 1.00 51.90 ? 162 ASN B CA 1 ATOM 3297 C C . ASN B 1 162 ? 38.331 39.994 19.988 1.00 49.89 ? 162 ASN B C 1 ATOM 3298 O O . ASN B 1 162 ? 37.231 40.325 19.553 1.00 48.88 ? 162 ASN B O 1 ATOM 3299 C CB . ASN B 1 162 ? 37.284 37.796 20.547 1.00 60.60 ? 162 ASN B CB 1 ATOM 3300 C CG . ASN B 1 162 ? 37.425 36.495 21.314 1.00 71.74 ? 162 ASN B CG 1 ATOM 3301 O OD1 . ASN B 1 162 ? 36.659 36.138 22.244 1.00 76.22 ? 162 ASN B OD1 1 ATOM 3302 N ND2 . ASN B 1 162 ? 38.445 35.682 20.993 1.00 76.70 ? 162 ASN B ND2 1 ATOM 3303 N N . GLY B 1 163 ? 39.233 40.936 20.270 1.00 48.91 ? 163 GLY B N 1 ATOM 3304 C CA . GLY B 1 163 ? 39.036 42.297 19.825 1.00 48.52 ? 163 GLY B CA 1 ATOM 3305 C C . GLY B 1 163 ? 38.677 43.409 20.778 1.00 47.50 ? 163 GLY B C 1 ATOM 3306 O O . GLY B 1 163 ? 38.929 44.588 20.498 1.00 47.37 ? 163 GLY B O 1 ATOM 3307 N N . TYR B 1 164 ? 38.248 43.124 21.976 1.00 46.63 ? 164 TYR B N 1 ATOM 3308 C CA . TYR B 1 164 ? 38.012 44.085 23.047 1.00 46.16 ? 164 TYR B CA 1 ATOM 3309 C C . TYR B 1 164 ? 38.811 43.661 24.272 1.00 45.75 ? 164 TYR B C 1 ATOM 3310 O O . TYR B 1 164 ? 38.920 42.464 24.556 1.00 46.63 ? 164 TYR B O 1 ATOM 3311 C CB . TYR B 1 164 ? 36.500 44.099 23.314 1.00 44.52 ? 164 TYR B CB 1 ATOM 3312 C CG . TYR B 1 164 ? 35.912 42.728 23.598 1.00 43.52 ? 164 TYR B CG 1 ATOM 3313 C CD1 . TYR B 1 164 ? 35.480 41.878 22.583 1.00 43.72 ? 164 TYR B CD1 1 ATOM 3314 C CD2 . TYR B 1 164 ? 35.810 42.264 24.893 1.00 41.97 ? 164 TYR B CD2 1 ATOM 3315 C CE1 . TYR B 1 164 ? 34.895 40.662 22.860 1.00 44.09 ? 164 TYR B CE1 1 ATOM 3316 C CE2 . TYR B 1 164 ? 35.181 41.092 25.209 1.00 42.67 ? 164 TYR B CE2 1 ATOM 3317 C CZ . TYR B 1 164 ? 34.766 40.271 24.184 1.00 44.72 ? 164 TYR B CZ 1 ATOM 3318 O OH . TYR B 1 164 ? 34.247 39.037 24.507 1.00 45.01 ? 164 TYR B OH 1 ATOM 3319 N N . ASP B 1 165 ? 39.510 44.551 24.924 1.00 45.78 ? 165 ASP B N 1 ATOM 3320 C CA . ASP B 1 165 ? 40.230 44.320 26.166 1.00 46.15 ? 165 ASP B CA 1 ATOM 3321 C C . ASP B 1 165 ? 39.279 43.888 27.272 1.00 46.49 ? 165 ASP B C 1 ATOM 3322 O O . ASP B 1 165 ? 38.126 44.348 27.169 1.00 45.89 ? 165 ASP B O 1 ATOM 3323 C CB . ASP B 1 165 ? 40.804 45.694 26.605 1.00 49.00 ? 165 ASP B CB 1 ATOM 3324 C CG . ASP B 1 165 ? 42.169 45.909 25.989 1.00 51.39 ? 165 ASP B CG 1 ATOM 3325 O OD1 . ASP B 1 165 ? 42.652 44.950 25.352 1.00 51.43 ? 165 ASP B OD1 1 ATOM 3326 O OD2 . ASP B 1 165 ? 42.806 46.975 26.135 1.00 53.43 ? 165 ASP B OD2 1 ATOM 3327 N N . ILE B 1 166 ? 39.648 42.977 28.199 1.00 46.24 ? 166 ILE B N 1 ATOM 3328 C CA . ILE B 1 166 ? 38.810 42.570 29.336 1.00 45.23 ? 166 ILE B CA 1 ATOM 3329 C C . ILE B 1 166 ? 39.637 42.695 30.601 1.00 44.96 ? 166 ILE B C 1 ATOM 3330 O O . ILE B 1 166 ? 40.687 42.063 30.694 1.00 45.21 ? 166 ILE B O 1 ATOM 3331 C CB . ILE B 1 166 ? 38.406 41.091 29.294 1.00 44.79 ? 166 ILE B CB 1 ATOM 3332 C CG1 . ILE B 1 166 ? 37.712 40.883 27.913 1.00 43.32 ? 166 ILE B CG1 1 ATOM 3333 C CG2 . ILE B 1 166 ? 37.487 40.779 30.453 1.00 43.90 ? 166 ILE B CG2 1 ATOM 3334 C CD1 . ILE B 1 166 ? 37.255 39.534 27.507 1.00 42.28 ? 166 ILE B CD1 1 ATOM 3335 N N . ASP B 1 167 ? 39.179 43.600 31.468 1.00 44.49 ? 167 ASP B N 1 ATOM 3336 C CA . ASP B 1 167 ? 39.910 43.761 32.725 1.00 42.63 ? 167 ASP B CA 1 ATOM 3337 C C . ASP B 1 167 ? 39.205 42.854 33.735 1.00 41.48 ? 167 ASP B C 1 ATOM 3338 O O . ASP B 1 167 ? 38.038 42.453 33.593 1.00 40.41 ? 167 ASP B O 1 ATOM 3339 C CB . ASP B 1 167 ? 39.965 45.193 33.185 1.00 45.83 ? 167 ASP B CB 1 ATOM 3340 C CG . ASP B 1 167 ? 40.938 46.093 32.437 1.00 50.16 ? 167 ASP B CG 1 ATOM 3341 O OD1 . ASP B 1 167 ? 41.892 45.646 31.751 1.00 47.19 ? 167 ASP B OD1 1 ATOM 3342 O OD2 . ASP B 1 167 ? 40.720 47.331 32.608 1.00 51.09 ? 167 ASP B OD2 1 ATOM 3343 N N . VAL B 1 168 ? 40.038 42.347 34.646 1.00 39.78 ? 168 VAL B N 1 ATOM 3344 C CA . VAL B 1 168 ? 39.521 41.484 35.692 1.00 38.26 ? 168 VAL B CA 1 ATOM 3345 C C . VAL B 1 168 ? 39.888 42.151 37.026 1.00 38.39 ? 168 VAL B C 1 ATOM 3346 O O . VAL B 1 168 ? 41.020 42.647 37.195 1.00 38.77 ? 168 VAL B O 1 ATOM 3347 C CB . VAL B 1 168 ? 40.117 40.078 35.683 1.00 37.99 ? 168 VAL B CB 1 ATOM 3348 C CG1 . VAL B 1 168 ? 39.501 39.183 36.755 1.00 35.50 ? 168 VAL B CG1 1 ATOM 3349 C CG2 . VAL B 1 168 ? 39.999 39.434 34.305 1.00 38.67 ? 168 VAL B CG2 1 ATOM 3350 N N . PHE B 1 169 ? 38.825 42.264 37.830 1.00 36.45 ? 169 PHE B N 1 ATOM 3351 C CA . PHE B 1 169 ? 38.985 42.709 39.205 1.00 34.49 ? 169 PHE B CA 1 ATOM 3352 C C . PHE B 1 169 ? 38.341 41.650 40.099 1.00 33.46 ? 169 PHE B C 1 ATOM 3353 O O . PHE B 1 169 ? 37.210 41.157 39.862 1.00 32.64 ? 169 PHE B O 1 ATOM 3354 C CB . PHE B 1 169 ? 38.251 44.025 39.368 1.00 33.15 ? 169 PHE B CB 1 ATOM 3355 C CG . PHE B 1 169 ? 38.837 45.227 38.697 1.00 30.93 ? 169 PHE B CG 1 ATOM 3356 C CD1 . PHE B 1 169 ? 38.532 45.490 37.376 1.00 30.07 ? 169 PHE B CD1 1 ATOM 3357 C CD2 . PHE B 1 169 ? 39.471 46.207 39.453 1.00 29.77 ? 169 PHE B CD2 1 ATOM 3358 C CE1 . PHE B 1 169 ? 38.910 46.669 36.777 1.00 26.55 ? 169 PHE B CE1 1 ATOM 3359 C CE2 . PHE B 1 169 ? 39.950 47.357 38.832 1.00 31.58 ? 169 PHE B CE2 1 ATOM 3360 C CZ . PHE B 1 169 ? 39.675 47.554 37.458 1.00 28.45 ? 169 PHE B CZ 1 ATOM 3361 N N . SER B 1 170 ? 39.249 40.961 40.796 1.00 33.24 ? 170 SER B N 1 ATOM 3362 C CA . SER B 1 170 ? 38.821 39.767 41.591 1.00 32.67 ? 170 SER B CA 1 ATOM 3363 C C . SER B 1 170 ? 39.009 40.013 43.059 1.00 30.81 ? 170 SER B C 1 ATOM 3364 O O . SER B 1 170 ? 39.881 40.811 43.425 1.00 31.43 ? 170 SER B O 1 ATOM 3365 C CB . SER B 1 170 ? 39.582 38.498 41.140 1.00 31.64 ? 170 SER B CB 1 ATOM 3366 O OG . SER B 1 170 ? 40.892 38.440 41.767 1.00 32.24 ? 170 SER B OG 1 ATOM 3367 N N . TYR B 1 171 ? 38.075 39.656 43.913 1.00 31.52 ? 171 TYR B N 1 ATOM 3368 C CA . TYR B 1 171 ? 38.147 39.973 45.362 1.00 31.24 ? 171 TYR B CA 1 ATOM 3369 C C . TYR B 1 171 ? 38.136 38.728 46.233 1.00 31.85 ? 171 TYR B C 1 ATOM 3370 O O . TYR B 1 171 ? 37.198 37.903 46.227 1.00 32.16 ? 171 TYR B O 1 ATOM 3371 C CB . TYR B 1 171 ? 37.008 40.893 45.846 1.00 30.29 ? 171 TYR B CB 1 ATOM 3372 C CG . TYR B 1 171 ? 37.105 42.207 45.065 1.00 30.97 ? 171 TYR B CG 1 ATOM 3373 C CD1 . TYR B 1 171 ? 36.542 42.279 43.807 1.00 29.92 ? 171 TYR B CD1 1 ATOM 3374 C CD2 . TYR B 1 171 ? 37.730 43.339 45.592 1.00 31.94 ? 171 TYR B CD2 1 ATOM 3375 C CE1 . TYR B 1 171 ? 36.694 43.424 43.071 1.00 31.88 ? 171 TYR B CE1 1 ATOM 3376 C CE2 . TYR B 1 171 ? 37.830 44.508 44.881 1.00 31.87 ? 171 TYR B CE2 1 ATOM 3377 C CZ . TYR B 1 171 ? 37.326 44.520 43.597 1.00 33.23 ? 171 TYR B CZ 1 ATOM 3378 O OH . TYR B 1 171 ? 37.407 45.657 42.809 1.00 35.39 ? 171 TYR B OH 1 ATOM 3379 N N . GLY B 1 172 ? 39.249 38.598 46.954 1.00 31.69 ? 172 GLY B N 1 ATOM 3380 C CA . GLY B 1 172 ? 39.557 37.374 47.635 1.00 32.93 ? 172 GLY B CA 1 ATOM 3381 C C . GLY B 1 172 ? 39.354 36.114 46.814 1.00 33.78 ? 172 GLY B C 1 ATOM 3382 O O . GLY B 1 172 ? 38.803 35.140 47.354 1.00 33.50 ? 172 GLY B O 1 ATOM 3383 N N . ALA B 1 173 ? 39.796 36.061 45.559 1.00 35.23 ? 173 ALA B N 1 ATOM 3384 C CA . ALA B 1 173 ? 39.738 34.795 44.800 1.00 36.67 ? 173 ALA B CA 1 ATOM 3385 C C . ALA B 1 173 ? 40.766 33.769 45.286 1.00 37.20 ? 173 ALA B C 1 ATOM 3386 O O . ALA B 1 173 ? 41.890 34.106 45.656 1.00 38.28 ? 173 ALA B O 1 ATOM 3387 C CB . ALA B 1 173 ? 40.057 35.044 43.332 1.00 33.01 ? 173 ALA B CB 1 ATOM 3388 N N . PRO B 1 174 ? 40.407 32.509 45.216 1.00 37.74 ? 174 PRO B N 1 ATOM 3389 C CA . PRO B 1 174 ? 41.354 31.416 45.413 1.00 39.39 ? 174 PRO B CA 1 ATOM 3390 C C . PRO B 1 174 ? 42.249 31.223 44.173 1.00 40.86 ? 174 PRO B C 1 ATOM 3391 O O . PRO B 1 174 ? 41.983 31.681 43.064 1.00 41.45 ? 174 PRO B O 1 ATOM 3392 C CB . PRO B 1 174 ? 40.460 30.167 45.474 1.00 37.83 ? 174 PRO B CB 1 ATOM 3393 C CG . PRO B 1 174 ? 39.241 30.541 44.713 1.00 37.71 ? 174 PRO B CG 1 ATOM 3394 C CD . PRO B 1 174 ? 39.085 32.036 44.734 1.00 37.25 ? 174 PRO B CD 1 ATOM 3395 N N . ARG B 1 175 ? 43.229 30.330 44.289 1.00 42.39 ? 175 ARG B N 1 ATOM 3396 C CA . ARG B 1 175 ? 44.103 29.930 43.172 1.00 41.56 ? 175 ARG B CA 1 ATOM 3397 C C . ARG B 1 175 ? 43.248 29.147 42.196 1.00 40.97 ? 175 ARG B C 1 ATOM 3398 O O . ARG B 1 175 ? 42.208 28.626 42.584 1.00 40.41 ? 175 ARG B O 1 ATOM 3399 C CB . ARG B 1 175 ? 45.329 29.172 43.709 1.00 39.51 ? 175 ARG B CB 1 ATOM 3400 C CG . ARG B 1 175 ? 46.350 30.120 44.312 1.00 38.22 ? 175 ARG B CG 1 ATOM 3401 C CD . ARG B 1 175 ? 47.555 29.543 45.010 1.00 41.52 ? 175 ARG B CD 1 ATOM 3402 N NE . ARG B 1 175 ? 47.342 29.101 46.368 1.00 44.25 ? 175 ARG B NE 1 ATOM 3403 C CZ . ARG B 1 175 ? 48.080 29.429 47.425 1.00 42.09 ? 175 ARG B CZ 1 ATOM 3404 N NH1 . ARG B 1 175 ? 49.126 30.240 47.313 1.00 41.17 ? 175 ARG B NH1 1 ATOM 3405 N NH2 . ARG B 1 175 ? 47.753 28.891 48.592 1.00 39.68 ? 175 ARG B NH2 1 ATOM 3406 N N . VAL B 1 176 ? 43.445 29.380 40.904 1.00 42.32 ? 176 VAL B N 1 ATOM 3407 C CA . VAL B 1 176 ? 42.556 28.843 39.845 1.00 42.95 ? 176 VAL B CA 1 ATOM 3408 C C . VAL B 1 176 ? 43.301 27.789 39.042 1.00 44.04 ? 176 VAL B C 1 ATOM 3409 O O . VAL B 1 176 ? 42.771 26.986 38.233 1.00 43.45 ? 176 VAL B O 1 ATOM 3410 C CB . VAL B 1 176 ? 42.132 30.075 39.047 0.50 41.32 ? 176 VAL B CB 1 ATOM 3411 C CG1 . VAL B 1 176 ? 41.724 29.770 37.639 0.50 42.53 ? 176 VAL B CG1 1 ATOM 3412 C CG2 . VAL B 1 176 ? 40.916 30.652 39.778 0.50 40.55 ? 176 VAL B CG2 1 ATOM 3413 N N . GLY B 1 177 ? 44.611 27.704 39.364 1.00 44.42 ? 177 GLY B N 1 ATOM 3414 C CA . GLY B 1 177 ? 45.450 26.790 38.670 1.00 45.97 ? 177 GLY B CA 1 ATOM 3415 C C . GLY B 1 177 ? 46.924 26.691 38.891 1.00 47.16 ? 177 GLY B C 1 ATOM 3416 O O . GLY B 1 177 ? 47.569 27.065 39.863 1.00 46.29 ? 177 GLY B O 1 ATOM 3417 N N . ASN B 1 178 ? 47.539 26.061 37.862 1.00 49.40 ? 178 ASN B N 1 ATOM 3418 C CA . ASN B 1 178 ? 48.966 25.754 37.896 1.00 51.35 ? 178 ASN B CA 1 ATOM 3419 C C . ASN B 1 178 ? 49.978 26.826 37.658 1.00 51.82 ? 178 ASN B C 1 ATOM 3420 O O . ASN B 1 178 ? 49.621 28.005 37.821 1.00 52.74 ? 178 ASN B O 1 ATOM 3421 C CB . ASN B 1 178 ? 49.192 24.474 37.107 1.00 55.44 ? 178 ASN B CB 1 ATOM 3422 C CG . ASN B 1 178 ? 49.486 24.679 35.641 1.00 59.13 ? 178 ASN B CG 1 ATOM 3423 O OD1 . ASN B 1 178 ? 49.450 25.813 35.129 1.00 60.29 ? 178 ASN B OD1 1 ATOM 3424 N ND2 . ASN B 1 178 ? 49.739 23.487 35.089 1.00 57.24 ? 178 ASN B ND2 1 ATOM 3425 N N . ARG B 1 179 ? 51.266 26.516 37.519 1.00 52.95 ? 179 ARG B N 1 ATOM 3426 C CA . ARG B 1 179 ? 52.226 27.630 37.455 1.00 53.71 ? 179 ARG B CA 1 ATOM 3427 C C . ARG B 1 179 ? 52.199 28.242 36.069 1.00 54.44 ? 179 ARG B C 1 ATOM 3428 O O . ARG B 1 179 ? 52.613 29.371 35.905 1.00 55.17 ? 179 ARG B O 1 ATOM 3429 C CB . ARG B 1 179 ? 53.695 27.416 37.761 1.00 54.57 ? 179 ARG B CB 1 ATOM 3430 C CG . ARG B 1 179 ? 54.307 28.665 38.407 1.00 56.24 ? 179 ARG B CG 1 ATOM 3431 C CD . ARG B 1 179 ? 55.777 28.517 38.687 1.00 59.03 ? 179 ARG B CD 1 ATOM 3432 N NE . ARG B 1 179 ? 56.498 29.545 37.910 1.00 63.69 ? 179 ARG B NE 1 ATOM 3433 C CZ . ARG B 1 179 ? 57.178 30.561 38.436 1.00 64.79 ? 179 ARG B CZ 1 ATOM 3434 N NH1 . ARG B 1 179 ? 57.289 30.649 39.770 1.00 65.77 ? 179 ARG B NH1 1 ATOM 3435 N NH2 . ARG B 1 179 ? 57.703 31.501 37.660 1.00 63.79 ? 179 ARG B NH2 1 ATOM 3436 N N . ALA B 1 180 ? 51.986 27.349 35.113 1.00 55.03 ? 180 ALA B N 1 ATOM 3437 C CA . ALA B 1 180 ? 51.920 27.788 33.725 1.00 54.93 ? 180 ALA B CA 1 ATOM 3438 C C . ALA B 1 180 ? 50.785 28.812 33.627 1.00 53.80 ? 180 ALA B C 1 ATOM 3439 O O . ALA B 1 180 ? 51.014 29.904 33.127 1.00 53.26 ? 180 ALA B O 1 ATOM 3440 C CB . ALA B 1 180 ? 51.743 26.533 32.871 1.00 56.06 ? 180 ALA B CB 1 ATOM 3441 N N . PHE B 1 181 ? 49.665 28.499 34.252 1.00 53.06 ? 181 PHE B N 1 ATOM 3442 C CA . PHE B 1 181 ? 48.480 29.347 34.264 1.00 52.65 ? 181 PHE B CA 1 ATOM 3443 C C . PHE B 1 181 ? 48.669 30.637 35.043 1.00 51.78 ? 181 PHE B C 1 ATOM 3444 O O . PHE B 1 181 ? 48.430 31.721 34.531 1.00 51.01 ? 181 PHE B O 1 ATOM 3445 C CB . PHE B 1 181 ? 47.262 28.591 34.804 1.00 52.41 ? 181 PHE B CB 1 ATOM 3446 C CG . PHE B 1 181 ? 45.932 29.173 34.446 1.00 54.66 ? 181 PHE B CG 1 ATOM 3447 C CD1 . PHE B 1 181 ? 45.764 30.006 33.350 1.00 54.48 ? 181 PHE B CD1 1 ATOM 3448 C CD2 . PHE B 1 181 ? 44.811 28.882 35.222 1.00 53.20 ? 181 PHE B CD2 1 ATOM 3449 C CE1 . PHE B 1 181 ? 44.529 30.536 33.019 1.00 53.41 ? 181 PHE B CE1 1 ATOM 3450 C CE2 . PHE B 1 181 ? 43.586 29.406 34.880 1.00 52.59 ? 181 PHE B CE2 1 ATOM 3451 C CZ . PHE B 1 181 ? 43.437 30.239 33.798 1.00 52.85 ? 181 PHE B CZ 1 ATOM 3452 N N . ALA B 1 182 ? 49.364 30.550 36.162 1.00 51.65 ? 182 ALA B N 1 ATOM 3453 C CA . ALA B 1 182 ? 49.789 31.684 36.956 1.00 52.17 ? 182 ALA B CA 1 ATOM 3454 C C . ALA B 1 182 ? 50.619 32.641 36.099 1.00 52.99 ? 182 ALA B C 1 ATOM 3455 O O . ALA B 1 182 ? 50.578 33.875 36.131 1.00 51.50 ? 182 ALA B O 1 ATOM 3456 C CB . ALA B 1 182 ? 50.581 31.159 38.157 1.00 48.64 ? 182 ALA B CB 1 ATOM 3457 N N . GLU B 1 183 ? 51.463 32.023 35.274 1.00 54.50 ? 183 GLU B N 1 ATOM 3458 C CA . GLU B 1 183 ? 52.378 32.668 34.350 1.00 55.36 ? 183 GLU B CA 1 ATOM 3459 C C . GLU B 1 183 ? 51.642 33.304 33.172 1.00 54.70 ? 183 GLU B C 1 ATOM 3460 O O . GLU B 1 183 ? 51.901 34.476 32.904 1.00 53.64 ? 183 GLU B O 1 ATOM 3461 C CB . GLU B 1 183 ? 53.389 31.608 33.874 1.00 58.98 ? 183 GLU B CB 1 ATOM 3462 C CG . GLU B 1 183 ? 54.821 32.066 34.143 1.00 63.58 ? 183 GLU B CG 1 ATOM 3463 C CD . GLU B 1 183 ? 55.724 30.906 34.509 1.00 67.60 ? 183 GLU B CD 1 ATOM 3464 O OE1 . GLU B 1 183 ? 55.697 29.886 33.768 1.00 69.74 ? 183 GLU B OE1 1 ATOM 3465 O OE2 . GLU B 1 183 ? 56.458 31.028 35.518 1.00 68.48 ? 183 GLU B OE2 1 ATOM 3466 N N . PHE B 1 184 ? 50.641 32.597 32.664 1.00 54.29 ? 184 PHE B N 1 ATOM 3467 C CA . PHE B 1 184 ? 49.805 33.078 31.590 1.00 55.75 ? 184 PHE B CA 1 ATOM 3468 C C . PHE B 1 184 ? 49.036 34.309 32.058 1.00 57.13 ? 184 PHE B C 1 ATOM 3469 O O . PHE B 1 184 ? 49.309 35.410 31.554 1.00 58.10 ? 184 PHE B O 1 ATOM 3470 C CB . PHE B 1 184 ? 48.796 32.037 31.114 1.00 57.00 ? 184 PHE B CB 1 ATOM 3471 C CG . PHE B 1 184 ? 47.885 32.389 29.981 1.00 59.73 ? 184 PHE B CG 1 ATOM 3472 C CD1 . PHE B 1 184 ? 48.385 32.575 28.677 1.00 60.57 ? 184 PHE B CD1 1 ATOM 3473 C CD2 . PHE B 1 184 ? 46.518 32.512 30.142 1.00 59.29 ? 184 PHE B CD2 1 ATOM 3474 C CE1 . PHE B 1 184 ? 47.528 32.896 27.635 1.00 60.63 ? 184 PHE B CE1 1 ATOM 3475 C CE2 . PHE B 1 184 ? 45.685 32.814 29.075 1.00 59.60 ? 184 PHE B CE2 1 ATOM 3476 C CZ . PHE B 1 184 ? 46.166 33.014 27.809 1.00 57.69 ? 184 PHE B CZ 1 ATOM 3477 N N . LEU B 1 185 ? 48.359 34.193 33.215 1.00 56.79 ? 185 LEU B N 1 ATOM 3478 C CA . LEU B 1 185 ? 47.618 35.312 33.749 1.00 55.88 ? 185 LEU B CA 1 ATOM 3479 C C . LEU B 1 185 ? 48.472 36.531 34.009 1.00 56.19 ? 185 LEU B C 1 ATOM 3480 O O . LEU B 1 185 ? 47.904 37.629 33.958 1.00 57.02 ? 185 LEU B O 1 ATOM 3481 C CB . LEU B 1 185 ? 46.889 34.875 35.028 1.00 52.22 ? 185 LEU B CB 1 ATOM 3482 C CG . LEU B 1 185 ? 45.854 33.777 34.689 1.00 50.85 ? 185 LEU B CG 1 ATOM 3483 C CD1 . LEU B 1 185 ? 45.479 33.050 35.953 1.00 44.76 ? 185 LEU B CD1 1 ATOM 3484 C CD2 . LEU B 1 185 ? 44.690 34.376 33.912 1.00 50.67 ? 185 LEU B CD2 1 ATOM 3485 N N . THR B 1 186 ? 49.747 36.384 34.323 1.00 55.73 ? 186 THR B N 1 ATOM 3486 C CA . THR B 1 186 ? 50.635 37.484 34.623 1.00 55.79 ? 186 THR B CA 1 ATOM 3487 C C . THR B 1 186 ? 51.083 38.293 33.407 1.00 56.70 ? 186 THR B C 1 ATOM 3488 O O . THR B 1 186 ? 51.440 39.469 33.579 1.00 56.61 ? 186 THR B O 1 ATOM 3489 C CB . THR B 1 186 ? 51.900 36.939 35.317 1.00 52.93 ? 186 THR B CB 1 ATOM 3490 O OG1 . THR B 1 186 ? 51.487 36.057 36.371 1.00 53.80 ? 186 THR B OG1 1 ATOM 3491 C CG2 . THR B 1 186 ? 52.823 38.004 35.860 1.00 47.71 ? 186 THR B CG2 1 ATOM 3492 N N . VAL B 1 187 ? 51.263 37.620 32.271 1.00 56.57 ? 187 VAL B N 1 ATOM 3493 C CA . VAL B 1 187 ? 51.810 38.270 31.091 1.00 56.78 ? 187 VAL B CA 1 ATOM 3494 C C . VAL B 1 187 ? 50.875 38.383 29.885 1.00 57.09 ? 187 VAL B C 1 ATOM 3495 O O . VAL B 1 187 ? 51.267 38.899 28.845 1.00 56.49 ? 187 VAL B O 1 ATOM 3496 C CB . VAL B 1 187 ? 53.110 37.564 30.629 1.00 55.82 ? 187 VAL B CB 1 ATOM 3497 C CG1 . VAL B 1 187 ? 54.169 37.602 31.725 1.00 54.45 ? 187 VAL B CG1 1 ATOM 3498 C CG2 . VAL B 1 187 ? 52.853 36.159 30.131 1.00 50.43 ? 187 VAL B CG2 1 ATOM 3499 N N . GLN B 1 188 ? 49.652 37.833 30.017 1.00 57.01 ? 188 GLN B N 1 ATOM 3500 C CA . GLN B 1 188 ? 48.634 37.886 28.967 1.00 55.46 ? 188 GLN B CA 1 ATOM 3501 C C . GLN B 1 188 ? 48.390 39.392 28.749 1.00 55.31 ? 188 GLN B C 1 ATOM 3502 O O . GLN B 1 188 ? 48.492 40.209 29.703 1.00 55.00 ? 188 GLN B O 1 ATOM 3503 C CB . GLN B 1 188 ? 47.315 37.190 29.337 1.00 51.28 ? 188 GLN B CB 1 ATOM 3504 C CG . GLN B 1 188 ? 46.331 36.885 28.231 1.00 48.62 ? 188 GLN B CG 1 ATOM 3505 C CD . GLN B 1 188 ? 44.990 36.366 28.705 1.00 51.97 ? 188 GLN B CD 1 ATOM 3506 O OE1 . GLN B 1 188 ? 44.605 36.695 29.865 1.00 50.47 ? 188 GLN B OE1 1 ATOM 3507 N NE2 . GLN B 1 188 ? 44.229 35.662 27.867 1.00 49.61 ? 188 GLN B NE2 1 ATOM 3508 N N . THR B 1 189 ? 48.047 39.658 27.499 1.00 54.17 ? 189 THR B N 1 ATOM 3509 C CA . THR B 1 189 ? 47.772 41.038 27.104 1.00 52.95 ? 189 THR B CA 1 ATOM 3510 C C . THR B 1 189 ? 46.269 41.032 26.793 1.00 52.51 ? 189 THR B C 1 ATOM 3511 O O . THR B 1 189 ? 45.614 39.988 26.740 1.00 51.76 ? 189 THR B O 1 ATOM 3512 C CB . THR B 1 189 ? 48.549 41.266 25.775 1.00 54.24 ? 189 THR B CB 1 ATOM 3513 O OG1 . THR B 1 189 ? 48.136 40.211 24.860 1.00 49.16 ? 189 THR B OG1 1 ATOM 3514 C CG2 . THR B 1 189 ? 50.053 41.226 26.034 1.00 52.39 ? 189 THR B CG2 1 ATOM 3515 N N . GLY B 1 190 ? 45.840 42.239 26.430 1.00 51.72 ? 190 GLY B N 1 ATOM 3516 C CA . GLY B 1 190 ? 44.440 42.429 26.059 1.00 50.96 ? 190 GLY B CA 1 ATOM 3517 C C . GLY B 1 190 ? 43.591 42.625 27.318 1.00 51.02 ? 190 GLY B C 1 ATOM 3518 O O . GLY B 1 190 ? 42.453 42.140 27.293 1.00 50.99 ? 190 GLY B O 1 ATOM 3519 N N . GLY B 1 191 ? 44.094 43.358 28.317 1.00 50.06 ? 191 GLY B N 1 ATOM 3520 C CA . GLY B 1 191 ? 43.312 43.453 29.536 1.00 50.04 ? 191 GLY B CA 1 ATOM 3521 C C . GLY B 1 191 ? 44.256 43.175 30.713 1.00 50.20 ? 191 GLY B C 1 ATOM 3522 O O . GLY B 1 191 ? 45.200 42.398 30.577 1.00 50.28 ? 191 GLY B O 1 ATOM 3523 N N . THR B 1 192 ? 44.003 43.812 31.852 1.00 49.36 ? 192 THR B N 1 ATOM 3524 C CA . THR B 1 192 ? 44.808 43.666 33.036 1.00 48.44 ? 192 THR B CA 1 ATOM 3525 C C . THR B 1 192 ? 43.982 43.000 34.134 1.00 48.91 ? 192 THR B C 1 ATOM 3526 O O . THR B 1 192 ? 42.798 43.301 34.307 1.00 49.87 ? 192 THR B O 1 ATOM 3527 C CB . THR B 1 192 ? 45.213 45.048 33.570 1.00 47.88 ? 192 THR B CB 1 ATOM 3528 O OG1 . THR B 1 192 ? 46.015 45.707 32.584 1.00 51.45 ? 192 THR B OG1 1 ATOM 3529 C CG2 . THR B 1 192 ? 46.020 45.006 34.845 1.00 42.96 ? 192 THR B CG2 1 ATOM 3530 N N . LEU B 1 193 ? 44.637 42.160 34.924 1.00 47.70 ? 193 LEU B N 1 ATOM 3531 C CA . LEU B 1 193 ? 43.951 41.497 36.006 1.00 45.97 ? 193 LEU B CA 1 ATOM 3532 C C . LEU B 1 193 ? 44.336 42.066 37.358 1.00 45.57 ? 193 LEU B C 1 ATOM 3533 O O . LEU B 1 193 ? 45.474 41.961 37.803 1.00 45.64 ? 193 LEU B O 1 ATOM 3534 C CB . LEU B 1 193 ? 44.302 40.027 35.953 1.00 43.94 ? 193 LEU B CB 1 ATOM 3535 C CG . LEU B 1 193 ? 44.185 39.336 37.317 1.00 42.58 ? 193 LEU B CG 1 ATOM 3536 C CD1 . LEU B 1 193 ? 42.711 39.242 37.670 1.00 41.70 ? 193 LEU B CD1 1 ATOM 3537 C CD2 . LEU B 1 193 ? 44.924 38.031 37.139 1.00 42.11 ? 193 LEU B CD2 1 ATOM 3538 N N . TYR B 1 194 ? 43.288 42.405 38.134 1.00 44.39 ? 194 TYR B N 1 ATOM 3539 C CA . TYR B 1 194 ? 43.597 43.023 39.438 1.00 43.32 ? 194 TYR B CA 1 ATOM 3540 C C . TYR B 1 194 ? 43.145 42.128 40.584 1.00 42.90 ? 194 TYR B C 1 ATOM 3541 O O . TYR B 1 194 ? 41.950 41.853 40.759 1.00 43.35 ? 194 TYR B O 1 ATOM 3542 C CB . TYR B 1 194 ? 43.061 44.428 39.469 1.00 42.67 ? 194 TYR B CB 1 ATOM 3543 C CG . TYR B 1 194 ? 43.544 45.400 38.448 1.00 40.67 ? 194 TYR B CG 1 ATOM 3544 C CD1 . TYR B 1 194 ? 44.651 46.177 38.608 1.00 39.68 ? 194 TYR B CD1 1 ATOM 3545 C CD2 . TYR B 1 194 ? 42.721 45.651 37.347 1.00 41.13 ? 194 TYR B CD2 1 ATOM 3546 C CE1 . TYR B 1 194 ? 44.960 47.160 37.687 1.00 38.88 ? 194 TYR B CE1 1 ATOM 3547 C CE2 . TYR B 1 194 ? 43.010 46.632 36.419 1.00 40.21 ? 194 TYR B CE2 1 ATOM 3548 C CZ . TYR B 1 194 ? 44.162 47.346 36.600 1.00 40.14 ? 194 TYR B CZ 1 ATOM 3549 O OH . TYR B 1 194 ? 44.520 48.261 35.653 1.00 43.26 ? 194 TYR B OH 1 ATOM 3550 N N . ARG B 1 195 ? 44.118 41.419 41.169 1.00 41.76 ? 195 ARG B N 1 ATOM 3551 C CA . ARG B 1 195 ? 43.865 40.375 42.146 1.00 40.63 ? 195 ARG B CA 1 ATOM 3552 C C . ARG B 1 195 ? 44.036 40.989 43.531 1.00 40.23 ? 195 ARG B C 1 ATOM 3553 O O . ARG B 1 195 ? 45.186 41.123 43.959 1.00 41.70 ? 195 ARG B O 1 ATOM 3554 C CB . ARG B 1 195 ? 44.828 39.200 42.015 1.00 37.28 ? 195 ARG B CB 1 ATOM 3555 C CG . ARG B 1 195 ? 44.196 37.836 42.123 1.00 38.78 ? 195 ARG B CG 1 ATOM 3556 C CD . ARG B 1 195 ? 45.135 36.635 42.113 1.00 36.62 ? 195 ARG B CD 1 ATOM 3557 N NE . ARG B 1 195 ? 46.154 36.689 43.056 1.00 35.71 ? 195 ARG B NE 1 ATOM 3558 C CZ . ARG B 1 195 ? 47.145 36.789 43.845 1.00 39.50 ? 195 ARG B CZ 1 ATOM 3559 N NH1 . ARG B 1 195 ? 48.294 37.312 43.432 1.00 41.21 ? 195 ARG B NH1 1 ATOM 3560 N NH2 . ARG B 1 195 ? 47.074 36.466 45.152 1.00 41.91 ? 195 ARG B NH2 1 ATOM 3561 N N . ILE B 1 196 ? 42.945 41.422 44.124 1.00 38.43 ? 196 ILE B N 1 ATOM 3562 C CA . ILE B 1 196 ? 42.954 42.063 45.428 1.00 37.12 ? 196 ILE B CA 1 ATOM 3563 C C . ILE B 1 196 ? 42.683 41.041 46.519 1.00 36.60 ? 196 ILE B C 1 ATOM 3564 O O . ILE B 1 196 ? 41.848 40.139 46.426 1.00 36.71 ? 196 ILE B O 1 ATOM 3565 C CB . ILE B 1 196 ? 41.786 43.097 45.423 1.00 38.21 ? 196 ILE B CB 1 ATOM 3566 C CG1 . ILE B 1 196 ? 42.046 44.198 44.387 1.00 37.99 ? 196 ILE B CG1 1 ATOM 3567 C CG2 . ILE B 1 196 ? 41.529 43.744 46.765 1.00 32.76 ? 196 ILE B CG2 1 ATOM 3568 C CD1 . ILE B 1 196 ? 41.096 44.048 43.228 1.00 41.75 ? 196 ILE B CD1 1 ATOM 3569 N N . THR B 1 197 ? 43.543 40.972 47.498 1.00 36.54 ? 197 THR B N 1 ATOM 3570 C CA . THR B 1 197 ? 43.493 40.120 48.658 1.00 35.92 ? 197 THR B CA 1 ATOM 3571 C C . THR B 1 197 ? 43.404 40.939 49.950 1.00 36.27 ? 197 THR B C 1 ATOM 3572 O O . THR B 1 197 ? 43.628 42.169 49.988 1.00 35.19 ? 197 THR B O 1 ATOM 3573 C CB . THR B 1 197 ? 44.762 39.245 48.700 1.00 35.35 ? 197 THR B CB 1 ATOM 3574 O OG1 . THR B 1 197 ? 45.929 40.046 48.796 1.00 34.71 ? 197 THR B OG1 1 ATOM 3575 C CG2 . THR B 1 197 ? 44.867 38.333 47.511 1.00 31.33 ? 197 THR B CG2 1 ATOM 3576 N N . HIS B 1 198 ? 42.668 40.334 50.902 1.00 36.74 ? 198 HIS B N 1 ATOM 3577 C CA . HIS B 1 198 ? 42.516 40.982 52.222 1.00 37.62 ? 198 HIS B CA 1 ATOM 3578 C C . HIS B 1 198 ? 43.246 40.212 53.345 1.00 38.44 ? 198 HIS B C 1 ATOM 3579 O O . HIS B 1 198 ? 43.061 39.054 53.769 1.00 37.51 ? 198 HIS B O 1 ATOM 3580 C CB . HIS B 1 198 ? 41.123 41.442 52.595 1.00 31.60 ? 198 HIS B CB 1 ATOM 3581 C CG . HIS B 1 198 ? 40.950 42.223 53.838 1.00 32.71 ? 198 HIS B CG 1 ATOM 3582 N ND1 . HIS B 1 198 ? 40.101 41.844 54.880 1.00 32.25 ? 198 HIS B ND1 1 ATOM 3583 C CD2 . HIS B 1 198 ? 41.593 43.355 54.284 1.00 34.97 ? 198 HIS B CD2 1 ATOM 3584 C CE1 . HIS B 1 198 ? 40.300 42.685 55.902 1.00 31.12 ? 198 HIS B CE1 1 ATOM 3585 N NE2 . HIS B 1 198 ? 41.198 43.597 55.606 1.00 31.01 ? 198 HIS B NE2 1 ATOM 3586 N N . THR B 1 199 ? 44.007 41.097 53.999 1.00 38.44 ? 199 THR B N 1 ATOM 3587 C CA . THR B 1 199 ? 44.819 40.796 55.144 1.00 40.75 ? 199 THR B CA 1 ATOM 3588 C C . THR B 1 199 ? 45.262 39.343 55.081 1.00 42.37 ? 199 THR B C 1 ATOM 3589 O O . THR B 1 199 ? 46.108 39.036 54.214 1.00 43.99 ? 199 THR B O 1 ATOM 3590 C CB . THR B 1 199 ? 44.114 41.043 56.489 1.00 38.37 ? 199 THR B CB 1 ATOM 3591 O OG1 . THR B 1 199 ? 42.703 40.734 56.338 1.00 38.77 ? 199 THR B OG1 1 ATOM 3592 C CG2 . THR B 1 199 ? 44.438 42.469 56.876 1.00 33.94 ? 199 THR B CG2 1 ATOM 3593 N N . ASN B 1 200 ? 44.741 38.472 55.893 1.00 42.50 ? 200 ASN B N 1 ATOM 3594 C CA . ASN B 1 200 ? 45.083 37.092 55.982 1.00 43.45 ? 200 ASN B CA 1 ATOM 3595 C C . ASN B 1 200 ? 43.836 36.240 55.644 1.00 43.37 ? 200 ASN B C 1 ATOM 3596 O O . ASN B 1 200 ? 43.588 35.184 56.299 1.00 43.02 ? 200 ASN B O 1 ATOM 3597 C CB . ASN B 1 200 ? 45.556 36.726 57.409 1.00 48.12 ? 200 ASN B CB 1 ATOM 3598 C CG . ASN B 1 200 ? 44.461 36.854 58.444 1.00 55.72 ? 200 ASN B CG 1 ATOM 3599 O OD1 . ASN B 1 200 ? 43.430 37.503 58.155 1.00 56.89 ? 200 ASN B OD1 1 ATOM 3600 N ND2 . ASN B 1 200 ? 44.614 36.276 59.648 1.00 57.84 ? 200 ASN B ND2 1 ATOM 3601 N N . ASP B 1 201 ? 42.983 36.784 54.766 1.00 41.99 ? 201 ASP B N 1 ATOM 3602 C CA . ASP B 1 201 ? 41.866 35.982 54.293 1.00 40.88 ? 201 ASP B CA 1 ATOM 3603 C C . ASP B 1 201 ? 42.360 34.610 53.889 1.00 41.58 ? 201 ASP B C 1 ATOM 3604 O O . ASP B 1 201 ? 43.330 34.558 53.164 1.00 42.17 ? 201 ASP B O 1 ATOM 3605 C CB . ASP B 1 201 ? 41.217 36.736 53.156 1.00 36.90 ? 201 ASP B CB 1 ATOM 3606 C CG . ASP B 1 201 ? 40.200 36.063 52.276 1.00 32.63 ? 201 ASP B CG 1 ATOM 3607 O OD1 . ASP B 1 201 ? 39.723 34.968 52.618 1.00 29.11 ? 201 ASP B OD1 1 ATOM 3608 O OD2 . ASP B 1 201 ? 39.811 36.644 51.218 1.00 29.36 ? 201 ASP B OD2 1 ATOM 3609 N N . ILE B 1 202 ? 41.439 33.637 53.947 1.00 42.53 ? 202 ILE B N 1 ATOM 3610 C CA . ILE B 1 202 ? 41.762 32.259 53.703 1.00 42.51 ? 202 ILE B CA 1 ATOM 3611 C C . ILE B 1 202 ? 41.604 31.808 52.270 1.00 43.60 ? 202 ILE B C 1 ATOM 3612 O O . ILE B 1 202 ? 42.337 30.909 51.829 1.00 43.86 ? 202 ILE B O 1 ATOM 3613 C CB . ILE B 1 202 ? 40.877 31.307 54.562 1.00 41.80 ? 202 ILE B CB 1 ATOM 3614 C CG1 . ILE B 1 202 ? 41.319 29.851 54.360 1.00 39.16 ? 202 ILE B CG1 1 ATOM 3615 C CG2 . ILE B 1 202 ? 39.388 31.493 54.256 1.00 38.54 ? 202 ILE B CG2 1 ATOM 3616 C CD1 . ILE B 1 202 ? 40.756 28.762 55.216 1.00 39.81 ? 202 ILE B CD1 1 ATOM 3617 N N . VAL B 1 203 ? 40.680 32.421 51.536 1.00 43.74 ? 203 VAL B N 1 ATOM 3618 C CA . VAL B 1 203 ? 40.352 31.944 50.207 1.00 43.88 ? 203 VAL B CA 1 ATOM 3619 C C . VAL B 1 203 ? 41.477 31.985 49.199 1.00 44.40 ? 203 VAL B C 1 ATOM 3620 O O . VAL B 1 203 ? 41.871 30.913 48.706 1.00 43.62 ? 203 VAL B O 1 ATOM 3621 C CB . VAL B 1 203 ? 38.985 32.491 49.763 1.00 43.12 ? 203 VAL B CB 1 ATOM 3622 C CG1 . VAL B 1 203 ? 38.457 31.890 48.452 1.00 39.72 ? 203 VAL B CG1 1 ATOM 3623 C CG2 . VAL B 1 203 ? 37.977 32.188 50.882 1.00 37.77 ? 203 VAL B CG2 1 ATOM 3624 N N . PRO B 1 204 ? 42.335 33.008 49.216 1.00 44.84 ? 204 PRO B N 1 ATOM 3625 C CA . PRO B 1 204 ? 43.414 33.158 48.257 1.00 45.10 ? 204 PRO B CA 1 ATOM 3626 C C . PRO B 1 204 ? 44.643 32.331 48.566 1.00 45.65 ? 204 PRO B C 1 ATOM 3627 O O . PRO B 1 204 ? 45.708 32.333 47.948 1.00 45.54 ? 204 PRO B O 1 ATOM 3628 C CB . PRO B 1 204 ? 43.785 34.635 48.319 1.00 44.94 ? 204 PRO B CB 1 ATOM 3629 C CG . PRO B 1 204 ? 42.537 35.307 48.784 1.00 45.45 ? 204 PRO B CG 1 ATOM 3630 C CD . PRO B 1 204 ? 41.945 34.331 49.788 1.00 45.20 ? 204 PRO B CD 1 ATOM 3631 N N . ARG B 1 205 ? 44.499 31.559 49.602 1.00 46.10 ? 205 ARG B N 1 ATOM 3632 C CA . ARG B 1 205 ? 45.375 30.652 50.272 1.00 46.51 ? 205 ARG B CA 1 ATOM 3633 C C . ARG B 1 205 ? 44.919 29.228 49.945 1.00 47.60 ? 205 ARG B C 1 ATOM 3634 O O . ARG B 1 205 ? 45.656 28.293 50.267 1.00 48.05 ? 205 ARG B O 1 ATOM 3635 C CB . ARG B 1 205 ? 45.171 30.923 51.753 1.00 47.20 ? 205 ARG B CB 1 ATOM 3636 C CG . ARG B 1 205 ? 46.268 31.098 52.736 1.00 44.95 ? 205 ARG B CG 1 ATOM 3637 C CD . ARG B 1 205 ? 46.489 32.536 53.190 1.00 43.01 ? 205 ARG B CD 1 ATOM 3638 N NE . ARG B 1 205 ? 46.883 32.415 54.564 1.00 46.56 ? 205 ARG B NE 1 ATOM 3639 C CZ . ARG B 1 205 ? 47.283 33.234 55.478 1.00 50.08 ? 205 ARG B CZ 1 ATOM 3640 N NH1 . ARG B 1 205 ? 47.415 34.543 55.288 1.00 52.11 ? 205 ARG B NH1 1 ATOM 3641 N NH2 . ARG B 1 205 ? 47.657 32.754 56.646 1.00 50.94 ? 205 ARG B NH2 1 ATOM 3642 N N . LEU B 1 206 ? 43.835 29.087 49.204 1.00 47.74 ? 206 LEU B N 1 ATOM 3643 C CA . LEU B 1 206 ? 43.331 27.830 48.709 1.00 47.81 ? 206 LEU B CA 1 ATOM 3644 C C . LEU B 1 206 ? 43.006 27.906 47.229 1.00 49.12 ? 206 LEU B C 1 ATOM 3645 O O . LEU B 1 206 ? 42.738 28.966 46.667 1.00 50.60 ? 206 LEU B O 1 ATOM 3646 C CB . LEU B 1 206 ? 42.011 27.448 49.376 1.00 44.71 ? 206 LEU B CB 1 ATOM 3647 C CG . LEU B 1 206 ? 41.980 27.330 50.899 1.00 43.61 ? 206 LEU B CG 1 ATOM 3648 C CD1 . LEU B 1 206 ? 40.572 27.043 51.399 1.00 40.25 ? 206 LEU B CD1 1 ATOM 3649 C CD2 . LEU B 1 206 ? 42.988 26.309 51.425 1.00 44.38 ? 206 LEU B CD2 1 ATOM 3650 N N . PRO B 1 207 ? 43.104 26.791 46.525 1.00 49.50 ? 207 PRO B N 1 ATOM 3651 C CA . PRO B 1 207 ? 43.658 25.574 47.108 1.00 49.45 ? 207 PRO B CA 1 ATOM 3652 C C . PRO B 1 207 ? 45.165 25.821 47.293 1.00 48.92 ? 207 PRO B C 1 ATOM 3653 O O . PRO B 1 207 ? 45.728 26.876 46.958 1.00 48.09 ? 207 PRO B O 1 ATOM 3654 C CB . PRO B 1 207 ? 43.331 24.525 46.069 1.00 50.01 ? 207 PRO B CB 1 ATOM 3655 C CG . PRO B 1 207 ? 42.238 25.132 45.222 1.00 49.79 ? 207 PRO B CG 1 ATOM 3656 C CD . PRO B 1 207 ? 42.688 26.577 45.114 1.00 49.24 ? 207 PRO B CD 1 ATOM 3657 N N . PRO B 1 208 ? 45.763 24.980 48.134 1.00 47.65 ? 208 PRO B N 1 ATOM 3658 C CA . PRO B 1 208 ? 47.145 25.095 48.495 1.00 47.14 ? 208 PRO B CA 1 ATOM 3659 C C . PRO B 1 208 ? 48.155 24.913 47.373 1.00 46.77 ? 208 PRO B C 1 ATOM 3660 O O . PRO B 1 208 ? 48.062 24.067 46.497 1.00 45.09 ? 208 PRO B O 1 ATOM 3661 C CB . PRO B 1 208 ? 47.344 24.023 49.559 1.00 47.22 ? 208 PRO B CB 1 ATOM 3662 C CG . PRO B 1 208 ? 45.958 23.690 50.004 1.00 47.81 ? 208 PRO B CG 1 ATOM 3663 C CD . PRO B 1 208 ? 45.153 23.759 48.718 1.00 47.67 ? 208 PRO B CD 1 ATOM 3664 N N . ARG B 1 209 ? 49.308 25.526 47.625 1.00 47.01 ? 209 ARG B N 1 ATOM 3665 C CA . ARG B 1 209 ? 50.535 25.420 46.883 1.00 48.22 ? 209 ARG B CA 1 ATOM 3666 C C . ARG B 1 209 ? 51.083 24.002 46.812 1.00 48.24 ? 209 ARG B C 1 ATOM 3667 O O . ARG B 1 209 ? 51.439 23.541 45.722 1.00 49.45 ? 209 ARG B O 1 ATOM 3668 C CB . ARG B 1 209 ? 51.638 26.309 47.493 1.00 47.99 ? 209 ARG B CB 1 ATOM 3669 C CG . ARG B 1 209 ? 51.248 27.775 47.343 1.00 46.77 ? 209 ARG B CG 1 ATOM 3670 C CD . ARG B 1 209 ? 51.885 28.353 46.095 1.00 50.01 ? 209 ARG B CD 1 ATOM 3671 N NE . ARG B 1 209 ? 53.329 28.509 46.235 1.00 51.27 ? 209 ARG B NE 1 ATOM 3672 C CZ . ARG B 1 209 ? 54.176 28.012 45.324 1.00 52.27 ? 209 ARG B CZ 1 ATOM 3673 N NH1 . ARG B 1 209 ? 53.667 27.369 44.268 1.00 50.98 ? 209 ARG B NH1 1 ATOM 3674 N NH2 . ARG B 1 209 ? 55.475 28.197 45.521 1.00 49.63 ? 209 ARG B NH2 1 ATOM 3675 N N . GLU B 1 210 ? 50.873 23.229 47.845 1.00 48.04 ? 210 GLU B N 1 ATOM 3676 C CA . GLU B 1 210 ? 51.279 21.838 47.922 1.00 48.37 ? 210 GLU B CA 1 ATOM 3677 C C . GLU B 1 210 ? 50.269 20.886 47.309 1.00 47.42 ? 210 GLU B C 1 ATOM 3678 O O . GLU B 1 210 ? 50.260 19.681 47.561 1.00 48.21 ? 210 GLU B O 1 ATOM 3679 C CB . GLU B 1 210 ? 51.706 21.449 49.327 1.00 48.95 ? 210 GLU B CB 1 ATOM 3680 C CG . GLU B 1 210 ? 51.368 22.479 50.376 1.00 55.40 ? 210 GLU B CG 1 ATOM 3681 C CD . GLU B 1 210 ? 52.319 23.635 50.541 1.00 58.00 ? 210 GLU B CD 1 ATOM 3682 O OE1 . GLU B 1 210 ? 53.482 23.590 50.074 1.00 61.68 ? 210 GLU B OE1 1 ATOM 3683 O OE2 . GLU B 1 210 ? 51.882 24.614 51.189 1.00 58.40 ? 210 GLU B OE2 1 ATOM 3684 N N . PHE B 1 211 ? 49.260 21.413 46.623 1.00 45.89 ? 211 PHE B N 1 ATOM 3685 C CA . PHE B 1 211 ? 48.457 20.622 45.714 1.00 44.28 ? 211 PHE B CA 1 ATOM 3686 C C . PHE B 1 211 ? 48.844 21.107 44.318 1.00 44.15 ? 211 PHE B C 1 ATOM 3687 O O . PHE B 1 211 ? 48.093 20.864 43.411 1.00 44.51 ? 211 PHE B O 1 ATOM 3688 C CB . PHE B 1 211 ? 46.943 20.606 45.851 1.00 40.22 ? 211 PHE B CB 1 ATOM 3689 C CG . PHE B 1 211 ? 46.558 19.745 47.023 1.00 40.14 ? 211 PHE B CG 1 ATOM 3690 C CD1 . PHE B 1 211 ? 46.840 20.173 48.323 1.00 39.10 ? 211 PHE B CD1 1 ATOM 3691 C CD2 . PHE B 1 211 ? 45.984 18.506 46.816 1.00 37.84 ? 211 PHE B CD2 1 ATOM 3692 C CE1 . PHE B 1 211 ? 46.555 19.342 49.393 1.00 39.91 ? 211 PHE B CE1 1 ATOM 3693 C CE2 . PHE B 1 211 ? 45.683 17.696 47.890 1.00 38.25 ? 211 PHE B CE2 1 ATOM 3694 C CZ . PHE B 1 211 ? 45.973 18.104 49.177 1.00 40.08 ? 211 PHE B CZ 1 ATOM 3695 N N . GLY B 1 212 ? 49.880 21.924 44.231 1.00 44.41 ? 212 GLY B N 1 ATOM 3696 C CA . GLY B 1 212 ? 50.455 22.328 42.979 1.00 45.09 ? 212 GLY B CA 1 ATOM 3697 C C . GLY B 1 212 ? 49.737 23.504 42.343 1.00 45.83 ? 212 GLY B C 1 ATOM 3698 O O . GLY B 1 212 ? 49.548 23.555 41.120 1.00 46.11 ? 212 GLY B O 1 ATOM 3699 N N . TYR B 1 213 ? 49.476 24.518 43.185 1.00 45.23 ? 213 TYR B N 1 ATOM 3700 C CA . TYR B 1 213 ? 48.748 25.669 42.649 1.00 43.77 ? 213 TYR B CA 1 ATOM 3701 C C . TYR B 1 213 ? 49.646 26.874 42.819 1.00 43.33 ? 213 TYR B C 1 ATOM 3702 O O . TYR B 1 213 ? 50.490 26.883 43.707 1.00 44.54 ? 213 TYR B O 1 ATOM 3703 C CB . TYR B 1 213 ? 47.430 25.871 43.342 1.00 42.66 ? 213 TYR B CB 1 ATOM 3704 C CG . TYR B 1 213 ? 46.270 25.020 42.911 1.00 40.48 ? 213 TYR B CG 1 ATOM 3705 C CD1 . TYR B 1 213 ? 46.206 23.679 43.268 1.00 40.52 ? 213 TYR B CD1 1 ATOM 3706 C CD2 . TYR B 1 213 ? 45.207 25.573 42.215 1.00 39.30 ? 213 TYR B CD2 1 ATOM 3707 C CE1 . TYR B 1 213 ? 45.104 22.904 42.877 1.00 39.94 ? 213 TYR B CE1 1 ATOM 3708 C CE2 . TYR B 1 213 ? 44.102 24.828 41.859 1.00 39.08 ? 213 TYR B CE2 1 ATOM 3709 C CZ . TYR B 1 213 ? 44.064 23.487 42.195 1.00 39.07 ? 213 TYR B CZ 1 ATOM 3710 O OH . TYR B 1 213 ? 43.015 22.703 41.798 1.00 38.44 ? 213 TYR B OH 1 ATOM 3711 N N . SER B 1 214 ? 49.400 27.880 42.017 1.00 42.58 ? 214 SER B N 1 ATOM 3712 C CA . SER B 1 214 ? 50.154 29.116 42.207 1.00 41.93 ? 214 SER B CA 1 ATOM 3713 C C . SER B 1 214 ? 49.237 30.317 41.964 1.00 40.74 ? 214 SER B C 1 ATOM 3714 O O . SER B 1 214 ? 48.216 30.140 41.319 1.00 39.51 ? 214 SER B O 1 ATOM 3715 C CB . SER B 1 214 ? 51.178 29.090 41.042 1.00 44.64 ? 214 SER B CB 1 ATOM 3716 O OG . SER B 1 214 ? 52.401 28.668 41.570 1.00 46.95 ? 214 SER B OG 1 ATOM 3717 N N . HIS B 1 215 ? 49.732 31.489 42.304 1.00 40.57 ? 215 HIS B N 1 ATOM 3718 C CA . HIS B 1 215 ? 49.068 32.736 42.040 1.00 40.39 ? 215 HIS B CA 1 ATOM 3719 C C . HIS B 1 215 ? 49.812 33.566 40.978 1.00 41.10 ? 215 HIS B C 1 ATOM 3720 O O . HIS B 1 215 ? 51.025 33.810 40.992 1.00 41.11 ? 215 HIS B O 1 ATOM 3721 C CB . HIS B 1 215 ? 49.003 33.639 43.290 1.00 39.68 ? 215 HIS B CB 1 ATOM 3722 C CG . HIS B 1 215 ? 47.715 33.514 44.031 1.00 39.22 ? 215 HIS B CG 1 ATOM 3723 N ND1 . HIS B 1 215 ? 46.498 33.391 43.373 1.00 38.66 ? 215 HIS B ND1 1 ATOM 3724 C CD2 . HIS B 1 215 ? 47.436 33.483 45.350 1.00 39.49 ? 215 HIS B CD2 1 ATOM 3725 C CE1 . HIS B 1 215 ? 45.522 33.284 44.258 1.00 36.69 ? 215 HIS B CE1 1 ATOM 3726 N NE2 . HIS B 1 215 ? 46.066 33.344 45.457 1.00 37.90 ? 215 HIS B NE2 1 ATOM 3727 N N . SER B 1 216 ? 48.943 34.299 40.273 1.00 41.31 ? 216 SER B N 1 ATOM 3728 C CA . SER B 1 216 ? 49.347 35.211 39.232 1.00 40.36 ? 216 SER B CA 1 ATOM 3729 C C . SER B 1 216 ? 49.998 36.405 39.943 1.00 40.43 ? 216 SER B C 1 ATOM 3730 O O . SER B 1 216 ? 49.744 36.489 41.156 1.00 38.50 ? 216 SER B O 1 ATOM 3731 C CB . SER B 1 216 ? 48.237 35.717 38.360 1.00 39.56 ? 216 SER B CB 1 ATOM 3732 O OG . SER B 1 216 ? 47.111 36.069 39.139 1.00 46.54 ? 216 SER B OG 1 ATOM 3733 N N . SER B 1 217 ? 50.655 37.244 39.118 1.00 39.97 ? 217 SER B N 1 ATOM 3734 C CA . SER B 1 217 ? 51.243 38.406 39.870 1.00 40.42 ? 217 SER B CA 1 ATOM 3735 C C . SER B 1 217 ? 50.787 39.625 39.087 1.00 39.77 ? 217 SER B C 1 ATOM 3736 O O . SER B 1 217 ? 50.667 39.377 37.885 1.00 41.53 ? 217 SER B O 1 ATOM 3737 C CB . SER B 1 217 ? 52.756 38.225 39.748 1.00 42.62 ? 217 SER B CB 1 ATOM 3738 O OG . SER B 1 217 ? 53.546 39.347 40.065 1.00 41.65 ? 217 SER B OG 1 ATOM 3739 N N . PRO B 1 218 ? 50.635 40.784 39.608 1.00 38.52 ? 218 PRO B N 1 ATOM 3740 C CA . PRO B 1 218 ? 50.845 41.007 41.018 1.00 39.13 ? 218 PRO B CA 1 ATOM 3741 C C . PRO B 1 218 ? 49.612 40.872 41.904 1.00 39.54 ? 218 PRO B C 1 ATOM 3742 O O . PRO B 1 218 ? 48.709 40.061 41.668 1.00 39.20 ? 218 PRO B O 1 ATOM 3743 C CB . PRO B 1 218 ? 51.370 42.439 40.992 1.00 38.71 ? 218 PRO B CB 1 ATOM 3744 C CG . PRO B 1 218 ? 50.489 43.096 39.957 1.00 38.87 ? 218 PRO B CG 1 ATOM 3745 C CD . PRO B 1 218 ? 50.273 42.016 38.913 1.00 38.27 ? 218 PRO B CD 1 ATOM 3746 N N . GLU B 1 219 ? 49.793 41.230 43.178 1.00 40.39 ? 219 GLU B N 1 ATOM 3747 C CA . GLU B 1 219 ? 48.779 41.136 44.225 1.00 40.94 ? 219 GLU B CA 1 ATOM 3748 C C . GLU B 1 219 ? 48.553 42.530 44.842 1.00 40.56 ? 219 GLU B C 1 ATOM 3749 O O . GLU B 1 219 ? 49.487 43.256 45.216 1.00 38.09 ? 219 GLU B O 1 ATOM 3750 C CB . GLU B 1 219 ? 49.126 40.130 45.307 1.00 44.36 ? 219 GLU B CB 1 ATOM 3751 C CG . GLU B 1 219 ? 48.305 40.034 46.562 1.00 48.44 ? 219 GLU B CG 1 ATOM 3752 C CD . GLU B 1 219 ? 48.892 39.247 47.713 1.00 51.19 ? 219 GLU B CD 1 ATOM 3753 O OE1 . GLU B 1 219 ? 49.823 38.428 47.529 1.00 55.41 ? 219 GLU B OE1 1 ATOM 3754 O OE2 . GLU B 1 219 ? 48.456 39.390 48.878 1.00 49.78 ? 219 GLU B OE2 1 ATOM 3755 N N . TYR B 1 220 ? 47.265 42.929 44.763 1.00 40.03 ? 220 TYR B N 1 ATOM 3756 C CA . TYR B 1 220 ? 46.977 44.226 45.440 1.00 40.04 ? 220 TYR B CA 1 ATOM 3757 C C . TYR B 1 220 ? 46.479 43.804 46.808 1.00 39.84 ? 220 TYR B C 1 ATOM 3758 O O . TYR B 1 220 ? 45.470 43.124 46.781 1.00 39.98 ? 220 TYR B O 1 ATOM 3759 C CB . TYR B 1 220 ? 45.942 45.060 44.700 1.00 39.06 ? 220 TYR B CB 1 ATOM 3760 C CG . TYR B 1 220 ? 46.553 45.596 43.421 1.00 37.09 ? 220 TYR B CG 1 ATOM 3761 C CD1 . TYR B 1 220 ? 47.265 46.784 43.498 1.00 36.76 ? 220 TYR B CD1 1 ATOM 3762 C CD2 . TYR B 1 220 ? 46.506 44.906 42.217 1.00 35.40 ? 220 TYR B CD2 1 ATOM 3763 C CE1 . TYR B 1 220 ? 47.913 47.279 42.378 1.00 35.78 ? 220 TYR B CE1 1 ATOM 3764 C CE2 . TYR B 1 220 ? 47.119 45.409 41.097 1.00 34.22 ? 220 TYR B CE2 1 ATOM 3765 C CZ . TYR B 1 220 ? 47.839 46.576 41.193 1.00 35.46 ? 220 TYR B CZ 1 ATOM 3766 O OH . TYR B 1 220 ? 48.491 47.129 40.110 1.00 37.05 ? 220 TYR B OH 1 ATOM 3767 N N . TRP B 1 221 ? 47.263 44.014 47.852 1.00 40.51 ? 221 TRP B N 1 ATOM 3768 C CA . TRP B 1 221 ? 46.980 43.497 49.189 1.00 39.87 ? 221 TRP B CA 1 ATOM 3769 C C . TRP B 1 221 ? 46.522 44.598 50.132 1.00 39.63 ? 221 TRP B C 1 ATOM 3770 O O . TRP B 1 221 ? 47.189 45.622 50.207 1.00 40.00 ? 221 TRP B O 1 ATOM 3771 C CB . TRP B 1 221 ? 48.179 42.756 49.783 1.00 36.93 ? 221 TRP B CB 1 ATOM 3772 C CG . TRP B 1 221 ? 48.026 42.140 51.135 1.00 35.07 ? 221 TRP B CG 1 ATOM 3773 C CD1 . TRP B 1 221 ? 47.083 41.250 51.551 1.00 35.34 ? 221 TRP B CD1 1 ATOM 3774 C CD2 . TRP B 1 221 ? 48.912 42.305 52.255 1.00 34.47 ? 221 TRP B CD2 1 ATOM 3775 N NE1 . TRP B 1 221 ? 47.283 40.891 52.882 1.00 34.54 ? 221 TRP B NE1 1 ATOM 3776 C CE2 . TRP B 1 221 ? 48.388 41.547 53.322 1.00 34.34 ? 221 TRP B CE2 1 ATOM 3777 C CE3 . TRP B 1 221 ? 50.096 43.028 52.449 1.00 33.18 ? 221 TRP B CE3 1 ATOM 3778 C CZ2 . TRP B 1 221 ? 49.006 41.486 54.574 1.00 36.08 ? 221 TRP B CZ2 1 ATOM 3779 C CZ3 . TRP B 1 221 ? 50.670 42.985 53.739 1.00 36.14 ? 221 TRP B CZ3 1 ATOM 3780 C CH2 . TRP B 1 221 ? 50.149 42.226 54.793 1.00 34.75 ? 221 TRP B CH2 1 ATOM 3781 N N . ILE B 1 222 ? 45.448 44.304 50.890 1.00 39.28 ? 222 ILE B N 1 ATOM 3782 C CA . ILE B 1 222 ? 44.792 45.288 51.732 1.00 37.57 ? 222 ILE B CA 1 ATOM 3783 C C . ILE B 1 222 ? 45.258 44.968 53.154 1.00 38.81 ? 222 ILE B C 1 ATOM 3784 O O . ILE B 1 222 ? 44.905 43.962 53.782 1.00 38.45 ? 222 ILE B O 1 ATOM 3785 C CB . ILE B 1 222 ? 43.256 45.305 51.625 1.00 31.32 ? 222 ILE B CB 1 ATOM 3786 C CG1 . ILE B 1 222 ? 42.689 45.655 50.247 1.00 26.67 ? 222 ILE B CG1 1 ATOM 3787 C CG2 . ILE B 1 222 ? 42.596 46.243 52.657 1.00 28.79 ? 222 ILE B CG2 1 ATOM 3788 C CD1 . ILE B 1 222 ? 41.270 45.124 49.976 1.00 18.53 ? 222 ILE B CD1 1 ATOM 3789 N N . LYS B 1 223 ? 45.925 45.947 53.772 1.00 38.92 ? 223 LYS B N 1 ATOM 3790 C CA . LYS B 1 223 ? 46.445 45.682 55.096 1.00 39.56 ? 223 LYS B CA 1 ATOM 3791 C C . LYS B 1 223 ? 45.476 46.084 56.209 1.00 39.26 ? 223 LYS B C 1 ATOM 3792 O O . LYS B 1 223 ? 45.728 45.773 57.369 1.00 39.67 ? 223 LYS B O 1 ATOM 3793 C CB . LYS B 1 223 ? 47.646 46.570 55.343 1.00 43.95 ? 223 LYS B CB 1 ATOM 3794 C CG . LYS B 1 223 ? 48.882 46.428 54.509 1.00 49.41 ? 223 LYS B CG 1 ATOM 3795 C CD . LYS B 1 223 ? 50.060 47.175 55.150 1.00 52.68 ? 223 LYS B CD 1 ATOM 3796 C CE . LYS B 1 223 ? 49.746 48.532 55.793 1.00 54.32 ? 223 LYS B CE 1 ATOM 3797 N NZ . LYS B 1 223 ? 50.751 49.583 55.443 1.00 54.95 ? 223 LYS B NZ 1 ATOM 3798 N N . SER B 1 224 ? 44.441 46.842 55.913 1.00 38.53 ? 224 SER B N 1 ATOM 3799 C CA . SER B 1 224 ? 43.584 47.320 57.007 1.00 37.64 ? 224 SER B CA 1 ATOM 3800 C C . SER B 1 224 ? 42.748 46.142 57.481 1.00 36.80 ? 224 SER B C 1 ATOM 3801 O O . SER B 1 224 ? 42.470 45.207 56.716 1.00 37.28 ? 224 SER B O 1 ATOM 3802 C CB . SER B 1 224 ? 42.878 48.617 56.563 1.00 33.74 ? 224 SER B CB 1 ATOM 3803 O OG . SER B 1 224 ? 42.511 48.448 55.184 1.00 35.65 ? 224 SER B OG 1 ATOM 3804 N N . GLY B 1 225 ? 42.294 46.164 58.717 1.00 35.61 ? 225 GLY B N 1 ATOM 3805 C CA . GLY B 1 225 ? 41.625 45.054 59.312 1.00 35.37 ? 225 GLY B CA 1 ATOM 3806 C C . GLY B 1 225 ? 40.193 44.844 58.921 1.00 36.44 ? 225 GLY B C 1 ATOM 3807 O O . GLY B 1 225 ? 39.580 45.636 58.206 1.00 37.27 ? 225 GLY B O 1 ATOM 3808 N N . THR B 1 226 ? 39.594 43.791 59.459 1.00 36.69 ? 226 THR B N 1 ATOM 3809 C CA . THR B 1 226 ? 38.200 43.478 59.176 1.00 36.64 ? 226 THR B CA 1 ATOM 3810 C C . THR B 1 226 ? 37.303 44.553 59.729 1.00 37.60 ? 226 THR B C 1 ATOM 3811 O O . THR B 1 226 ? 37.611 45.133 60.773 1.00 37.72 ? 226 THR B O 1 ATOM 3812 C CB . THR B 1 226 ? 37.975 42.100 59.825 1.00 34.82 ? 226 THR B CB 1 ATOM 3813 O OG1 . THR B 1 226 ? 39.025 41.321 59.219 1.00 32.28 ? 226 THR B OG1 1 ATOM 3814 C CG2 . THR B 1 226 ? 36.578 41.584 59.511 1.00 36.09 ? 226 THR B CG2 1 ATOM 3815 N N . LEU B 1 227 ? 36.275 44.966 58.994 1.00 38.31 ? 227 LEU B N 1 ATOM 3816 C CA . LEU B 1 227 ? 35.436 46.088 59.369 1.00 38.73 ? 227 LEU B CA 1 ATOM 3817 C C . LEU B 1 227 ? 36.169 47.424 59.458 1.00 38.24 ? 227 LEU B C 1 ATOM 3818 O O . LEU B 1 227 ? 35.571 48.312 60.045 1.00 38.57 ? 227 LEU B O 1 ATOM 3819 C CB . LEU B 1 227 ? 34.771 45.812 60.725 1.00 41.03 ? 227 LEU B CB 1 ATOM 3820 C CG . LEU B 1 227 ? 33.792 44.627 60.618 1.00 44.86 ? 227 LEU B CG 1 ATOM 3821 C CD1 . LEU B 1 227 ? 33.704 43.853 61.916 1.00 43.80 ? 227 LEU B CD1 1 ATOM 3822 C CD2 . LEU B 1 227 ? 32.459 45.179 60.147 1.00 46.17 ? 227 LEU B CD2 1 ATOM 3823 N N . VAL B 1 228 ? 37.276 47.713 58.824 1.00 37.32 ? 228 VAL B N 1 ATOM 3824 C CA . VAL B 1 228 ? 37.963 48.994 58.917 1.00 38.09 ? 228 VAL B CA 1 ATOM 3825 C C . VAL B 1 228 ? 37.991 49.614 57.533 1.00 39.42 ? 228 VAL B C 1 ATOM 3826 O O . VAL B 1 228 ? 38.258 48.930 56.536 1.00 41.01 ? 228 VAL B O 1 ATOM 3827 C CB . VAL B 1 228 ? 39.429 48.755 59.370 1.00 36.62 ? 228 VAL B CB 1 ATOM 3828 C CG1 . VAL B 1 228 ? 40.253 50.014 59.553 1.00 31.23 ? 228 VAL B CG1 1 ATOM 3829 C CG2 . VAL B 1 228 ? 39.454 47.931 60.670 1.00 33.83 ? 228 VAL B CG2 1 ATOM 3830 N N . PRO B 1 229 ? 37.601 50.854 57.366 1.00 39.68 ? 229 PRO B N 1 ATOM 3831 C CA . PRO B 1 229 ? 37.649 51.438 56.018 1.00 39.83 ? 229 PRO B CA 1 ATOM 3832 C C . PRO B 1 229 ? 39.007 51.178 55.380 1.00 39.45 ? 229 PRO B C 1 ATOM 3833 O O . PRO B 1 229 ? 40.017 51.593 55.895 1.00 38.39 ? 229 PRO B O 1 ATOM 3834 C CB . PRO B 1 229 ? 37.629 52.969 56.338 1.00 39.59 ? 229 PRO B CB 1 ATOM 3835 C CG . PRO B 1 229 ? 36.879 53.029 57.652 1.00 38.93 ? 229 PRO B CG 1 ATOM 3836 C CD . PRO B 1 229 ? 37.174 51.782 58.428 1.00 38.54 ? 229 PRO B CD 1 ATOM 3837 N N . VAL B 1 230 ? 39.178 51.034 54.099 1.00 40.71 ? 230 VAL B N 1 ATOM 3838 C CA . VAL B 1 230 ? 40.464 51.047 53.455 1.00 42.57 ? 230 VAL B CA 1 ATOM 3839 C C . VAL B 1 230 ? 40.690 52.491 52.996 1.00 44.81 ? 230 VAL B C 1 ATOM 3840 O O . VAL B 1 230 ? 39.752 53.211 52.683 1.00 45.80 ? 230 VAL B O 1 ATOM 3841 C CB . VAL B 1 230 ? 40.402 50.119 52.226 1.00 40.08 ? 230 VAL B CB 1 ATOM 3842 C CG1 . VAL B 1 230 ? 41.807 49.859 51.707 1.00 42.70 ? 230 VAL B CG1 1 ATOM 3843 C CG2 . VAL B 1 230 ? 39.668 48.828 52.550 1.00 38.97 ? 230 VAL B CG2 1 ATOM 3844 N N . THR B 1 231 ? 41.916 52.954 52.955 1.00 45.79 ? 231 THR B N 1 ATOM 3845 C CA . THR B 1 231 ? 42.337 54.161 52.295 1.00 46.93 ? 231 THR B CA 1 ATOM 3846 C C . THR B 1 231 ? 43.361 53.692 51.260 1.00 47.92 ? 231 THR B C 1 ATOM 3847 O O . THR B 1 231 ? 43.947 52.644 51.547 1.00 47.59 ? 231 THR B O 1 ATOM 3848 C CB . THR B 1 231 ? 43.125 55.135 53.184 1.00 48.93 ? 231 THR B CB 1 ATOM 3849 O OG1 . THR B 1 231 ? 44.313 54.471 53.637 1.00 48.63 ? 231 THR B OG1 1 ATOM 3850 C CG2 . THR B 1 231 ? 42.233 55.587 54.307 1.00 46.41 ? 231 THR B CG2 1 ATOM 3851 N N . ARG B 1 232 ? 43.806 54.547 50.342 1.00 49.13 ? 232 ARG B N 1 ATOM 3852 C CA . ARG B 1 232 ? 44.682 54.005 49.296 1.00 50.18 ? 232 ARG B CA 1 ATOM 3853 C C . ARG B 1 232 ? 46.077 53.736 49.828 1.00 51.04 ? 232 ARG B C 1 ATOM 3854 O O . ARG B 1 232 ? 46.836 52.981 49.244 1.00 50.92 ? 232 ARG B O 1 ATOM 3855 C CB . ARG B 1 232 ? 44.694 54.864 48.057 1.00 50.30 ? 232 ARG B CB 1 ATOM 3856 C CG . ARG B 1 232 ? 44.935 56.339 48.347 1.00 50.48 ? 232 ARG B CG 1 ATOM 3857 C CD . ARG B 1 232 ? 45.041 57.019 46.993 1.00 49.90 ? 232 ARG B CD 1 ATOM 3858 N NE . ARG B 1 232 ? 46.441 57.243 46.612 1.00 48.02 ? 232 ARG B NE 1 ATOM 3859 C CZ . ARG B 1 232 ? 46.859 58.518 46.598 1.00 46.33 ? 232 ARG B CZ 1 ATOM 3860 N NH1 . ARG B 1 232 ? 45.958 59.445 46.943 1.00 44.95 ? 232 ARG B NH1 1 ATOM 3861 N NH2 . ARG B 1 232 ? 48.104 58.793 46.262 1.00 42.89 ? 232 ARG B NH2 1 ATOM 3862 N N . ASN B 1 233 ? 46.393 54.275 50.994 1.00 51.53 ? 233 ASN B N 1 ATOM 3863 C CA . ASN B 1 233 ? 47.638 53.963 51.647 1.00 52.10 ? 233 ASN B CA 1 ATOM 3864 C C . ASN B 1 233 ? 47.659 52.542 52.161 1.00 52.29 ? 233 ASN B C 1 ATOM 3865 O O . ASN B 1 233 ? 48.760 51.973 52.286 1.00 52.89 ? 233 ASN B O 1 ATOM 3866 C CB . ASN B 1 233 ? 47.875 55.014 52.738 1.00 56.05 ? 233 ASN B CB 1 ATOM 3867 C CG . ASN B 1 233 ? 47.656 56.422 52.180 1.00 59.78 ? 233 ASN B CG 1 ATOM 3868 O OD1 . ASN B 1 233 ? 46.605 57.017 52.473 1.00 58.98 ? 233 ASN B OD1 1 ATOM 3869 N ND2 . ASN B 1 233 ? 48.601 56.925 51.385 1.00 59.48 ? 233 ASN B ND2 1 ATOM 3870 N N . ASP B 1 234 ? 46.542 51.912 52.516 1.00 51.41 ? 234 ASP B N 1 ATOM 3871 C CA . ASP B 1 234 ? 46.516 50.557 53.034 1.00 50.42 ? 234 ASP B CA 1 ATOM 3872 C C . ASP B 1 234 ? 46.698 49.459 51.986 1.00 50.22 ? 234 ASP B C 1 ATOM 3873 O O . ASP B 1 234 ? 46.438 48.286 52.311 1.00 50.33 ? 234 ASP B O 1 ATOM 3874 C CB . ASP B 1 234 ? 45.164 50.319 53.734 1.00 49.97 ? 234 ASP B CB 1 ATOM 3875 C CG . ASP B 1 234 ? 44.924 51.306 54.860 1.00 52.38 ? 234 ASP B CG 1 ATOM 3876 O OD1 . ASP B 1 234 ? 45.800 51.320 55.779 1.00 51.17 ? 234 ASP B OD1 1 ATOM 3877 O OD2 . ASP B 1 234 ? 43.896 52.050 54.814 1.00 52.28 ? 234 ASP B OD2 1 ATOM 3878 N N . ILE B 1 235 ? 46.743 49.801 50.699 1.00 49.18 ? 235 ILE B N 1 ATOM 3879 C CA . ILE B 1 235 ? 46.893 48.830 49.641 1.00 49.71 ? 235 ILE B CA 1 ATOM 3880 C C . ILE B 1 235 ? 48.334 48.723 49.125 1.00 50.61 ? 235 ILE B C 1 ATOM 3881 O O . ILE B 1 235 ? 49.019 49.682 48.764 1.00 50.28 ? 235 ILE B O 1 ATOM 3882 C CB . ILE B 1 235 ? 45.882 49.031 48.491 1.00 44.83 ? 235 ILE B CB 1 ATOM 3883 C CG1 . ILE B 1 235 ? 44.462 49.152 49.044 1.00 40.87 ? 235 ILE B CG1 1 ATOM 3884 C CG2 . ILE B 1 235 ? 45.994 47.908 47.479 1.00 41.25 ? 235 ILE B CG2 1 ATOM 3885 C CD1 . ILE B 1 235 ? 43.379 49.507 48.060 1.00 32.36 ? 235 ILE B CD1 1 ATOM 3886 N N . VAL B 1 236 ? 48.860 47.484 49.145 1.00 50.72 ? 236 VAL B N 1 ATOM 3887 C CA . VAL B 1 236 ? 50.257 47.276 48.783 1.00 51.38 ? 236 VAL B CA 1 ATOM 3888 C C . VAL B 1 236 ? 50.365 46.453 47.519 1.00 51.14 ? 236 VAL B C 1 ATOM 3889 O O . VAL B 1 236 ? 49.630 45.480 47.434 1.00 51.22 ? 236 VAL B O 1 ATOM 3890 C CB . VAL B 1 236 ? 51.030 46.607 49.935 1.00 53.25 ? 236 VAL B CB 1 ATOM 3891 C CG1 . VAL B 1 236 ? 52.515 46.539 49.623 1.00 53.86 ? 236 VAL B CG1 1 ATOM 3892 C CG2 . VAL B 1 236 ? 50.837 47.281 51.283 1.00 51.81 ? 236 VAL B CG2 1 ATOM 3893 N N . LYS B 1 237 ? 51.194 46.853 46.556 1.00 51.53 ? 237 LYS B N 1 ATOM 3894 C CA . LYS B 1 237 ? 51.268 46.105 45.290 1.00 51.37 ? 237 LYS B CA 1 ATOM 3895 C C . LYS B 1 237 ? 52.442 45.133 45.438 1.00 51.20 ? 237 LYS B C 1 ATOM 3896 O O . LYS B 1 237 ? 53.441 45.532 46.048 1.00 51.26 ? 237 LYS B O 1 ATOM 3897 C CB . LYS B 1 237 ? 51.346 47.050 44.098 1.00 52.34 ? 237 LYS B CB 1 ATOM 3898 C CG . LYS B 1 237 ? 51.287 46.418 42.721 1.00 53.38 ? 237 LYS B CG 1 ATOM 3899 C CD . LYS B 1 237 ? 51.804 47.242 41.527 1.00 51.34 ? 237 LYS B CD 1 ATOM 3900 C CE . LYS B 1 237 ? 51.424 46.405 40.302 1.00 56.14 ? 237 LYS B CE 1 ATOM 3901 N NZ . LYS B 1 237 ? 51.464 47.081 38.977 1.00 57.99 ? 237 LYS B NZ 1 ATOM 3902 N N . ILE B 1 238 ? 52.191 43.834 45.338 1.00 50.45 ? 238 ILE B N 1 ATOM 3903 C CA . ILE B 1 238 ? 53.167 42.807 45.608 1.00 49.88 ? 238 ILE B CA 1 ATOM 3904 C C . ILE B 1 238 ? 53.497 42.092 44.288 1.00 50.11 ? 238 ILE B C 1 ATOM 3905 O O . ILE B 1 238 ? 52.688 41.250 43.872 1.00 49.40 ? 238 ILE B O 1 ATOM 3906 C CB . ILE B 1 238 ? 52.727 41.726 46.617 1.00 47.54 ? 238 ILE B CB 1 ATOM 3907 C CG1 . ILE B 1 238 ? 52.242 42.369 47.914 1.00 46.56 ? 238 ILE B CG1 1 ATOM 3908 C CG2 . ILE B 1 238 ? 53.879 40.765 46.897 1.00 41.46 ? 238 ILE B CG2 1 ATOM 3909 C CD1 . ILE B 1 238 ? 53.239 43.283 48.571 1.00 48.20 ? 238 ILE B CD1 1 ATOM 3910 N N . GLU B 1 239 ? 54.796 42.170 43.971 1.00 50.03 ? 239 GLU B N 1 ATOM 3911 C CA . GLU B 1 239 ? 55.217 41.709 42.653 1.00 50.95 ? 239 GLU B CA 1 ATOM 3912 C C . GLU B 1 239 ? 55.873 40.345 42.693 1.00 50.64 ? 239 GLU B C 1 ATOM 3913 O O . GLU B 1 239 ? 56.379 39.972 43.764 1.00 50.86 ? 239 GLU B O 1 ATOM 3914 C CB . GLU B 1 239 ? 56.084 42.822 42.058 1.00 57.59 ? 239 GLU B CB 1 ATOM 3915 C CG . GLU B 1 239 ? 55.974 43.009 40.542 1.00 61.95 ? 239 GLU B CG 1 ATOM 3916 C CD . GLU B 1 239 ? 54.955 44.070 40.142 1.00 65.22 ? 239 GLU B CD 1 ATOM 3917 O OE1 . GLU B 1 239 ? 54.668 44.875 41.070 1.00 65.07 ? 239 GLU B OE1 1 ATOM 3918 O OE2 . GLU B 1 239 ? 54.496 44.049 38.947 1.00 67.79 ? 239 GLU B OE2 1 ATOM 3919 N N . GLY B 1 240 ? 55.571 39.457 41.730 1.00 50.00 ? 240 GLY B N 1 ATOM 3920 C CA . GLY B 1 240 ? 56.162 38.132 41.708 1.00 49.16 ? 240 GLY B CA 1 ATOM 3921 C C . GLY B 1 240 ? 55.248 36.949 41.916 1.00 49.34 ? 240 GLY B C 1 ATOM 3922 O O . GLY B 1 240 ? 54.335 36.996 42.749 1.00 49.80 ? 240 GLY B O 1 ATOM 3923 N N . ILE B 1 241 ? 55.384 35.888 41.117 1.00 49.11 ? 241 ILE B N 1 ATOM 3924 C CA . ILE B 1 241 ? 54.559 34.708 41.253 1.00 49.38 ? 241 ILE B CA 1 ATOM 3925 C C . ILE B 1 241 ? 54.881 33.978 42.558 1.00 50.05 ? 241 ILE B C 1 ATOM 3926 O O . ILE B 1 241 ? 55.957 34.185 43.146 1.00 50.02 ? 241 ILE B O 1 ATOM 3927 C CB . ILE B 1 241 ? 54.688 33.759 40.073 1.00 49.31 ? 241 ILE B CB 1 ATOM 3928 C CG1 . ILE B 1 241 ? 54.018 34.458 38.885 1.00 48.21 ? 241 ILE B CG1 1 ATOM 3929 C CG2 . ILE B 1 241 ? 54.062 32.410 40.400 1.00 48.06 ? 241 ILE B CG2 1 ATOM 3930 C CD1 . ILE B 1 241 ? 54.074 33.823 37.550 1.00 43.96 ? 241 ILE B CD1 1 ATOM 3931 N N . ASP B 1 242 ? 53.798 33.630 43.249 1.00 49.69 ? 242 ASP B N 1 ATOM 3932 C CA . ASP B 1 242 ? 53.759 33.056 44.575 1.00 48.22 ? 242 ASP B CA 1 ATOM 3933 C C . ASP B 1 242 ? 54.516 33.916 45.572 1.00 47.95 ? 242 ASP B C 1 ATOM 3934 O O . ASP B 1 242 ? 54.935 33.398 46.613 1.00 47.30 ? 242 ASP B O 1 ATOM 3935 C CB . ASP B 1 242 ? 54.138 31.577 44.621 1.00 45.58 ? 242 ASP B CB 1 ATOM 3936 C CG . ASP B 1 242 ? 53.272 30.778 43.660 1.00 50.96 ? 242 ASP B CG 1 ATOM 3937 O OD1 . ASP B 1 242 ? 52.025 30.932 43.759 1.00 52.56 ? 242 ASP B OD1 1 ATOM 3938 O OD2 . ASP B 1 242 ? 53.796 30.052 42.772 1.00 49.99 ? 242 ASP B OD2 1 ATOM 3939 N N . ALA B 1 243 ? 54.468 35.242 45.435 1.00 47.52 ? 243 ALA B N 1 ATOM 3940 C CA . ALA B 1 243 ? 55.101 36.098 46.431 1.00 47.87 ? 243 ALA B CA 1 ATOM 3941 C C . ALA B 1 243 ? 54.506 35.918 47.807 1.00 48.03 ? 243 ALA B C 1 ATOM 3942 O O . ALA B 1 243 ? 53.369 35.513 47.998 1.00 48.89 ? 243 ALA B O 1 ATOM 3943 C CB . ALA B 1 243 ? 55.031 37.577 46.095 1.00 47.33 ? 243 ALA B CB 1 ATOM 3944 N N . THR B 1 244 ? 55.352 36.056 48.804 1.00 49.03 ? 244 THR B N 1 ATOM 3945 C CA . THR B 1 244 ? 54.924 36.038 50.224 1.00 50.61 ? 244 THR B CA 1 ATOM 3946 C C . THR B 1 244 ? 55.061 37.470 50.699 1.00 52.01 ? 244 THR B C 1 ATOM 3947 O O . THR B 1 244 ? 55.526 38.280 49.845 1.00 53.84 ? 244 THR B O 1 ATOM 3948 C CB . THR B 1 244 ? 55.809 35.014 50.947 1.00 50.40 ? 244 THR B CB 1 ATOM 3949 O OG1 . THR B 1 244 ? 57.174 35.480 50.992 1.00 48.46 ? 244 THR B OG1 1 ATOM 3950 C CG2 . THR B 1 244 ? 55.831 33.666 50.209 1.00 44.28 ? 244 THR B CG2 1 ATOM 3951 N N . GLY B 1 245 ? 54.483 38.015 51.756 1.00 52.95 ? 245 GLY B N 1 ATOM 3952 C CA . GLY B 1 245 ? 54.657 39.484 51.947 1.00 53.37 ? 245 GLY B CA 1 ATOM 3953 C C . GLY B 1 245 ? 53.327 40.219 51.845 1.00 53.79 ? 245 GLY B C 1 ATOM 3954 O O . GLY B 1 245 ? 53.226 41.429 52.051 1.00 54.80 ? 245 GLY B O 1 ATOM 3955 N N . GLY B 1 246 ? 52.353 39.535 51.267 1.00 53.33 ? 246 GLY B N 1 ATOM 3956 C CA . GLY B 1 246 ? 50.960 39.948 51.163 1.00 51.87 ? 246 GLY B CA 1 ATOM 3957 C C . GLY B 1 246 ? 50.077 38.894 51.847 1.00 50.13 ? 246 GLY B C 1 ATOM 3958 O O . GLY B 1 246 ? 50.246 38.621 53.031 1.00 50.21 ? 246 GLY B O 1 ATOM 3959 N N . ASN B 1 247 ? 49.077 38.352 51.180 1.00 48.46 ? 247 ASN B N 1 ATOM 3960 C CA . ASN B 1 247 ? 48.214 37.346 51.776 1.00 47.32 ? 247 ASN B CA 1 ATOM 3961 C C . ASN B 1 247 ? 48.923 36.010 51.988 1.00 48.07 ? 247 ASN B C 1 ATOM 3962 O O . ASN B 1 247 ? 48.638 35.213 52.899 1.00 45.95 ? 247 ASN B O 1 ATOM 3963 C CB . ASN B 1 247 ? 47.029 37.161 50.842 1.00 42.56 ? 247 ASN B CB 1 ATOM 3964 C CG . ASN B 1 247 ? 46.095 36.065 51.286 1.00 42.37 ? 247 ASN B CG 1 ATOM 3965 O OD1 . ASN B 1 247 ? 46.031 34.997 50.683 1.00 42.29 ? 247 ASN B OD1 1 ATOM 3966 N ND2 . ASN B 1 247 ? 45.340 36.309 52.347 1.00 39.83 ? 247 ASN B ND2 1 ATOM 3967 N N . ASN B 1 248 ? 49.847 35.678 51.070 1.00 48.99 ? 248 ASN B N 1 ATOM 3968 C CA . ASN B 1 248 ? 50.570 34.423 51.098 1.00 50.51 ? 248 ASN B CA 1 ATOM 3969 C C . ASN B 1 248 ? 51.675 34.382 52.158 1.00 51.79 ? 248 ASN B C 1 ATOM 3970 O O . ASN B 1 248 ? 52.882 34.386 51.900 1.00 52.94 ? 248 ASN B O 1 ATOM 3971 C CB . ASN B 1 248 ? 51.081 34.061 49.721 1.00 48.19 ? 248 ASN B CB 1 ATOM 3972 C CG . ASN B 1 248 ? 51.836 32.743 49.735 1.00 48.41 ? 248 ASN B CG 1 ATOM 3973 O OD1 . ASN B 1 248 ? 51.426 31.807 50.414 1.00 47.34 ? 248 ASN B OD1 1 ATOM 3974 N ND2 . ASN B 1 248 ? 52.932 32.702 48.982 1.00 48.99 ? 248 ASN B ND2 1 ATOM 3975 N N . GLN B 1 249 ? 51.263 34.357 53.413 1.00 51.88 ? 249 GLN B N 1 ATOM 3976 C CA . GLN B 1 249 ? 52.074 34.357 54.586 1.00 52.58 ? 249 GLN B CA 1 ATOM 3977 C C . GLN B 1 249 ? 51.781 33.065 55.342 1.00 54.19 ? 249 GLN B C 1 ATOM 3978 O O . GLN B 1 249 ? 50.631 32.590 55.386 1.00 54.52 ? 249 GLN B O 1 ATOM 3979 C CB . GLN B 1 249 ? 51.811 35.544 55.478 1.00 49.71 ? 249 GLN B CB 1 ATOM 3980 C CG . GLN B 1 249 ? 52.455 36.763 54.795 1.00 50.93 ? 249 GLN B CG 1 ATOM 3981 C CD . GLN B 1 249 ? 52.552 37.934 55.739 1.00 50.77 ? 249 GLN B CD 1 ATOM 3982 O OE1 . GLN B 1 249 ? 53.452 37.879 56.569 1.00 55.51 ? 249 GLN B OE1 1 ATOM 3983 N NE2 . GLN B 1 249 ? 51.741 38.966 55.748 1.00 49.82 ? 249 GLN B NE2 1 ATOM 3984 N N . PRO B 1 250 ? 52.757 32.716 56.174 1.00 55.00 ? 250 PRO B N 1 ATOM 3985 C CA . PRO B 1 250 ? 52.664 31.455 56.891 1.00 55.37 ? 250 PRO B CA 1 ATOM 3986 C C . PRO B 1 250 ? 51.873 31.509 58.172 1.00 55.52 ? 250 PRO B C 1 ATOM 3987 O O . PRO B 1 250 ? 52.009 30.571 58.976 1.00 57.06 ? 250 PRO B O 1 ATOM 3988 C CB . PRO B 1 250 ? 54.121 31.102 57.184 1.00 55.42 ? 250 PRO B CB 1 ATOM 3989 C CG . PRO B 1 250 ? 54.857 32.410 57.169 1.00 55.53 ? 250 PRO B CG 1 ATOM 3990 C CD . PRO B 1 250 ? 54.171 33.212 56.093 1.00 55.31 ? 250 PRO B CD 1 ATOM 3991 N N . ASN B 1 251 ? 51.156 32.570 58.474 1.00 54.61 ? 251 ASN B N 1 ATOM 3992 C CA . ASN B 1 251 ? 50.434 32.740 59.726 1.00 52.95 ? 251 ASN B CA 1 ATOM 3993 C C . ASN B 1 251 ? 49.072 32.077 59.640 1.00 52.13 ? 251 ASN B C 1 ATOM 3994 O O . ASN B 1 251 ? 48.859 31.436 58.638 1.00 51.76 ? 251 ASN B O 1 ATOM 3995 C CB . ASN B 1 251 ? 50.288 34.234 59.997 1.00 49.63 ? 251 ASN B CB 1 ATOM 3996 C CG . ASN B 1 251 ? 49.863 35.000 58.763 1.00 47.58 ? 251 ASN B CG 1 ATOM 3997 O OD1 . ASN B 1 251 ? 49.257 34.536 57.795 1.00 46.71 ? 251 ASN B OD1 1 ATOM 3998 N ND2 . ASN B 1 251 ? 50.180 36.289 58.783 1.00 50.06 ? 251 ASN B ND2 1 ATOM 3999 N N . ILE B 1 252 ? 48.304 32.039 60.709 1.00 52.22 ? 252 ILE B N 1 ATOM 4000 C CA . ILE B 1 252 ? 46.987 31.418 60.677 1.00 52.33 ? 252 ILE B CA 1 ATOM 4001 C C . ILE B 1 252 ? 45.998 32.350 60.001 1.00 51.64 ? 252 ILE B C 1 ATOM 4002 O O . ILE B 1 252 ? 45.985 33.533 60.341 1.00 51.77 ? 252 ILE B O 1 ATOM 4003 C CB . ILE B 1 252 ? 46.472 31.161 62.115 1.00 55.11 ? 252 ILE B CB 1 ATOM 4004 C CG1 . ILE B 1 252 ? 47.690 30.791 62.957 1.00 52.90 ? 252 ILE B CG1 1 ATOM 4005 C CG2 . ILE B 1 252 ? 45.364 30.108 62.032 1.00 54.70 ? 252 ILE B CG2 1 ATOM 4006 C CD1 . ILE B 1 252 ? 47.663 29.460 63.633 1.00 53.62 ? 252 ILE B CD1 1 ATOM 4007 N N . PRO B 1 253 ? 45.120 31.788 59.201 1.00 50.57 ? 253 PRO B N 1 ATOM 4008 C CA . PRO B 1 253 ? 44.287 32.610 58.333 1.00 49.67 ? 253 PRO B CA 1 ATOM 4009 C C . PRO B 1 253 ? 42.972 32.861 59.009 1.00 47.89 ? 253 PRO B C 1 ATOM 4010 O O . PRO B 1 253 ? 42.890 32.604 60.189 1.00 47.73 ? 253 PRO B O 1 ATOM 4011 C CB . PRO B 1 253 ? 44.256 31.836 57.019 1.00 50.41 ? 253 PRO B CB 1 ATOM 4012 C CG . PRO B 1 253 ? 44.290 30.420 57.471 1.00 51.05 ? 253 PRO B CG 1 ATOM 4013 C CD . PRO B 1 253 ? 45.132 30.388 58.732 1.00 51.07 ? 253 PRO B CD 1 ATOM 4014 N N . ASP B 1 254 ? 42.013 33.438 58.327 1.00 46.79 ? 254 ASP B N 1 ATOM 4015 C CA . ASP B 1 254 ? 40.738 33.866 58.850 1.00 44.98 ? 254 ASP B CA 1 ATOM 4016 C C . ASP B 1 254 ? 39.669 33.851 57.757 1.00 44.66 ? 254 ASP B C 1 ATOM 4017 O O . ASP B 1 254 ? 39.995 34.149 56.600 1.00 43.42 ? 254 ASP B O 1 ATOM 4018 C CB . ASP B 1 254 ? 40.958 35.361 59.205 1.00 45.38 ? 254 ASP B CB 1 ATOM 4019 C CG . ASP B 1 254 ? 39.767 35.974 59.891 1.00 45.92 ? 254 ASP B CG 1 ATOM 4020 O OD1 . ASP B 1 254 ? 39.327 35.363 60.882 1.00 52.40 ? 254 ASP B OD1 1 ATOM 4021 O OD2 . ASP B 1 254 ? 39.219 37.019 59.530 1.00 45.18 ? 254 ASP B OD2 1 ATOM 4022 N N . ILE B 1 255 ? 38.446 33.552 58.160 1.00 43.65 ? 255 ILE B N 1 ATOM 4023 C CA . ILE B 1 255 ? 37.275 33.638 57.314 1.00 43.50 ? 255 ILE B CA 1 ATOM 4024 C C . ILE B 1 255 ? 36.603 34.997 57.400 1.00 43.53 ? 255 ILE B C 1 ATOM 4025 O O . ILE B 1 255 ? 36.494 35.709 56.419 1.00 44.07 ? 255 ILE B O 1 ATOM 4026 C CB . ILE B 1 255 ? 36.221 32.552 57.622 1.00 42.86 ? 255 ILE B CB 1 ATOM 4027 C CG1 . ILE B 1 255 ? 36.850 31.175 57.538 1.00 44.13 ? 255 ILE B CG1 1 ATOM 4028 C CG2 . ILE B 1 255 ? 34.972 32.744 56.791 1.00 39.65 ? 255 ILE B CG2 1 ATOM 4029 C CD1 . ILE B 1 255 ? 35.934 29.993 57.276 1.00 43.28 ? 255 ILE B CD1 1 ATOM 4030 N N . PRO B 1 256 ? 36.441 35.629 58.553 1.00 43.34 ? 256 PRO B N 1 ATOM 4031 C CA . PRO B 1 256 ? 35.864 36.981 58.602 1.00 42.71 ? 256 PRO B CA 1 ATOM 4032 C C . PRO B 1 256 ? 36.607 37.967 57.740 1.00 41.17 ? 256 PRO B C 1 ATOM 4033 O O . PRO B 1 256 ? 35.966 38.774 57.060 1.00 41.42 ? 256 PRO B O 1 ATOM 4034 C CB . PRO B 1 256 ? 35.884 37.314 60.085 1.00 43.46 ? 256 PRO B CB 1 ATOM 4035 C CG . PRO B 1 256 ? 35.796 35.978 60.765 1.00 43.24 ? 256 PRO B CG 1 ATOM 4036 C CD . PRO B 1 256 ? 36.522 34.989 59.885 1.00 42.70 ? 256 PRO B CD 1 ATOM 4037 N N . ALA B 1 257 ? 37.900 37.857 57.500 1.00 39.76 ? 257 ALA B N 1 ATOM 4038 C CA . ALA B 1 257 ? 38.630 38.767 56.632 1.00 39.32 ? 257 ALA B CA 1 ATOM 4039 C C . ALA B 1 257 ? 38.167 38.703 55.161 1.00 39.07 ? 257 ALA B C 1 ATOM 4040 O O . ALA B 1 257 ? 38.416 39.593 54.341 1.00 39.16 ? 257 ALA B O 1 ATOM 4041 C CB . ALA B 1 257 ? 40.125 38.550 56.741 1.00 36.58 ? 257 ALA B CB 1 ATOM 4042 N N . HIS B 1 258 ? 37.712 37.542 54.763 1.00 37.72 ? 258 HIS B N 1 ATOM 4043 C CA . HIS B 1 258 ? 37.190 37.186 53.495 1.00 37.64 ? 258 HIS B CA 1 ATOM 4044 C C . HIS B 1 258 ? 35.946 38.005 53.181 1.00 38.39 ? 258 HIS B C 1 ATOM 4045 O O . HIS B 1 258 ? 35.774 38.413 52.022 1.00 38.66 ? 258 HIS B O 1 ATOM 4046 C CB . HIS B 1 258 ? 36.928 35.691 53.348 1.00 33.21 ? 258 HIS B CB 1 ATOM 4047 C CG . HIS B 1 258 ? 36.482 35.316 51.974 1.00 28.88 ? 258 HIS B CG 1 ATOM 4048 N ND1 . HIS B 1 258 ? 37.315 35.494 50.900 1.00 27.06 ? 258 HIS B ND1 1 ATOM 4049 C CD2 . HIS B 1 258 ? 35.334 34.789 51.510 1.00 28.89 ? 258 HIS B CD2 1 ATOM 4050 C CE1 . HIS B 1 258 ? 36.639 35.118 49.822 1.00 29.37 ? 258 HIS B CE1 1 ATOM 4051 N NE2 . HIS B 1 258 ? 35.437 34.716 50.141 1.00 28.60 ? 258 HIS B NE2 1 ATOM 4052 N N . LEU B 1 259 ? 35.129 38.316 54.202 1.00 38.55 ? 259 LEU B N 1 ATOM 4053 C CA . LEU B 1 259 ? 33.964 39.203 53.909 1.00 37.95 ? 259 LEU B CA 1 ATOM 4054 C C . LEU B 1 259 ? 34.241 40.707 54.010 1.00 35.96 ? 259 LEU B C 1 ATOM 4055 O O . LEU B 1 259 ? 33.212 41.407 53.944 1.00 34.71 ? 259 LEU B O 1 ATOM 4056 C CB . LEU B 1 259 ? 32.770 38.836 54.852 1.00 33.51 ? 259 LEU B CB 1 ATOM 4057 C CG . LEU B 1 259 ? 32.713 37.308 54.990 1.00 32.78 ? 259 LEU B CG 1 ATOM 4058 C CD1 . LEU B 1 259 ? 31.612 36.827 55.945 1.00 31.55 ? 259 LEU B CD1 1 ATOM 4059 C CD2 . LEU B 1 259 ? 32.503 36.641 53.654 1.00 29.68 ? 259 LEU B CD2 1 ATOM 4060 N N . TRP B 1 260 ? 35.436 41.225 54.089 1.00 34.63 ? 260 TRP B N 1 ATOM 4061 C CA . TRP B 1 260 ? 35.486 42.687 54.161 1.00 34.97 ? 260 TRP B CA 1 ATOM 4062 C C . TRP B 1 260 ? 36.493 43.167 53.139 1.00 35.27 ? 260 TRP B C 1 ATOM 4063 O O . TRP B 1 260 ? 37.693 42.952 53.334 1.00 36.20 ? 260 TRP B O 1 ATOM 4064 C CB . TRP B 1 260 ? 35.895 43.074 55.609 1.00 32.41 ? 260 TRP B CB 1 ATOM 4065 C CG . TRP B 1 260 ? 35.894 44.586 55.789 1.00 31.07 ? 260 TRP B CG 1 ATOM 4066 C CD1 . TRP B 1 260 ? 36.943 45.461 55.744 1.00 25.83 ? 260 TRP B CD1 1 ATOM 4067 C CD2 . TRP B 1 260 ? 34.693 45.347 56.035 1.00 28.63 ? 260 TRP B CD2 1 ATOM 4068 N NE1 . TRP B 1 260 ? 36.460 46.703 55.954 1.00 28.06 ? 260 TRP B NE1 1 ATOM 4069 C CE2 . TRP B 1 260 ? 35.086 46.700 56.084 1.00 29.88 ? 260 TRP B CE2 1 ATOM 4070 C CE3 . TRP B 1 260 ? 33.344 45.002 56.119 1.00 29.89 ? 260 TRP B CE3 1 ATOM 4071 C CZ2 . TRP B 1 260 ? 34.180 47.727 56.323 1.00 25.28 ? 260 TRP B CZ2 1 ATOM 4072 C CZ3 . TRP B 1 260 ? 32.444 46.054 56.328 1.00 30.14 ? 260 TRP B CZ3 1 ATOM 4073 C CH2 . TRP B 1 260 ? 32.866 47.389 56.436 1.00 24.92 ? 260 TRP B CH2 1 ATOM 4074 N N . TYR B 1 261 ? 36.082 43.511 51.946 1.00 35.65 ? 261 TYR B N 1 ATOM 4075 C CA . TYR B 1 261 ? 36.828 44.059 50.835 1.00 34.77 ? 261 TYR B CA 1 ATOM 4076 C C . TYR B 1 261 ? 36.260 45.440 50.532 1.00 34.65 ? 261 TYR B C 1 ATOM 4077 O O . TYR B 1 261 ? 35.170 45.607 49.975 1.00 33.47 ? 261 TYR B O 1 ATOM 4078 C CB . TYR B 1 261 ? 36.646 43.159 49.606 1.00 34.65 ? 261 TYR B CB 1 ATOM 4079 C CG . TYR B 1 261 ? 37.671 42.046 49.714 1.00 36.16 ? 261 TYR B CG 1 ATOM 4080 C CD1 . TYR B 1 261 ? 37.392 40.824 50.346 1.00 36.72 ? 261 TYR B CD1 1 ATOM 4081 C CD2 . TYR B 1 261 ? 38.941 42.265 49.206 1.00 35.40 ? 261 TYR B CD2 1 ATOM 4082 C CE1 . TYR B 1 261 ? 38.386 39.864 50.447 1.00 36.55 ? 261 TYR B CE1 1 ATOM 4083 C CE2 . TYR B 1 261 ? 39.925 41.305 49.309 1.00 34.55 ? 261 TYR B CE2 1 ATOM 4084 C CZ . TYR B 1 261 ? 39.637 40.114 49.918 1.00 35.46 ? 261 TYR B CZ 1 ATOM 4085 O OH . TYR B 1 261 ? 40.628 39.170 50.014 1.00 36.35 ? 261 TYR B OH 1 ATOM 4086 N N . PHE B 1 262 ? 36.784 46.462 51.194 1.00 34.82 ? 262 PHE B N 1 ATOM 4087 C CA . PHE B 1 262 ? 36.368 47.858 51.115 1.00 35.50 ? 262 PHE B CA 1 ATOM 4088 C C . PHE B 1 262 ? 35.051 48.178 51.822 1.00 35.63 ? 262 PHE B C 1 ATOM 4089 O O . PHE B 1 262 ? 34.888 49.152 52.556 1.00 36.19 ? 262 PHE B O 1 ATOM 4090 C CB . PHE B 1 262 ? 36.293 48.440 49.716 1.00 34.26 ? 262 PHE B CB 1 ATOM 4091 C CG . PHE B 1 262 ? 37.601 48.490 48.977 1.00 38.49 ? 262 PHE B CG 1 ATOM 4092 C CD1 . PHE B 1 262 ? 38.444 49.590 49.083 1.00 37.54 ? 262 PHE B CD1 1 ATOM 4093 C CD2 . PHE B 1 262 ? 38.035 47.404 48.213 1.00 35.33 ? 262 PHE B CD2 1 ATOM 4094 C CE1 . PHE B 1 262 ? 39.654 49.630 48.426 1.00 36.38 ? 262 PHE B CE1 1 ATOM 4095 C CE2 . PHE B 1 262 ? 39.206 47.441 47.517 1.00 32.22 ? 262 PHE B CE2 1 ATOM 4096 C CZ . PHE B 1 262 ? 40.012 48.550 47.641 1.00 37.23 ? 262 PHE B CZ 1 ATOM 4097 N N . GLY B 1 263 ? 34.163 47.236 51.891 1.00 35.86 ? 263 GLY B N 1 ATOM 4098 C CA . GLY B 1 263 ? 32.852 47.282 52.458 1.00 36.96 ? 263 GLY B CA 1 ATOM 4099 C C . GLY B 1 263 ? 32.503 45.797 52.662 1.00 38.24 ? 263 GLY B C 1 ATOM 4100 O O . GLY B 1 263 ? 33.327 44.962 52.344 1.00 37.55 ? 263 GLY B O 1 ATOM 4101 N N . LEU B 1 264 ? 31.288 45.595 53.152 1.00 39.66 ? 264 LEU B N 1 ATOM 4102 C CA . LEU B 1 264 ? 30.889 44.250 53.534 1.00 40.28 ? 264 LEU B CA 1 ATOM 4103 C C . LEU B 1 264 ? 30.625 43.509 52.230 1.00 40.98 ? 264 LEU B C 1 ATOM 4104 O O . LEU B 1 264 ? 29.893 44.049 51.389 1.00 42.02 ? 264 LEU B O 1 ATOM 4105 C CB . LEU B 1 264 ? 29.616 44.396 54.373 1.00 39.65 ? 264 LEU B CB 1 ATOM 4106 C CG . LEU B 1 264 ? 29.179 43.040 54.895 1.00 39.71 ? 264 LEU B CG 1 ATOM 4107 C CD1 . LEU B 1 264 ? 30.067 42.565 56.029 1.00 40.02 ? 264 LEU B CD1 1 ATOM 4108 C CD2 . LEU B 1 264 ? 27.776 43.137 55.432 1.00 41.57 ? 264 LEU B CD2 1 ATOM 4109 N N . ILE B 1 265 ? 31.087 42.275 52.103 1.00 40.60 ? 265 ILE B N 1 ATOM 4110 C CA . ILE B 1 265 ? 30.897 41.586 50.810 1.00 40.15 ? 265 ILE B CA 1 ATOM 4111 C C . ILE B 1 265 ? 30.781 40.090 51.050 1.00 40.71 ? 265 ILE B C 1 ATOM 4112 O O . ILE B 1 265 ? 31.403 39.602 51.995 1.00 41.37 ? 265 ILE B O 1 ATOM 4113 C CB . ILE B 1 265 ? 32.054 41.897 49.852 1.00 36.75 ? 265 ILE B CB 1 ATOM 4114 C CG1 . ILE B 1 265 ? 31.771 41.556 48.397 1.00 32.73 ? 265 ILE B CG1 1 ATOM 4115 C CG2 . ILE B 1 265 ? 33.376 41.265 50.303 1.00 35.30 ? 265 ILE B CG2 1 ATOM 4116 C CD1 . ILE B 1 265 ? 32.945 41.929 47.495 1.00 29.63 ? 265 ILE B CD1 1 ATOM 4117 N N . GLY B 1 266 ? 29.957 39.413 50.275 1.00 40.74 ? 266 GLY B N 1 ATOM 4118 C CA . GLY B 1 266 ? 29.780 37.985 50.378 1.00 41.50 ? 266 GLY B CA 1 ATOM 4119 C C . GLY B 1 266 ? 28.746 37.617 51.415 1.00 42.55 ? 266 GLY B C 1 ATOM 4120 O O . GLY B 1 266 ? 28.659 36.473 51.839 1.00 43.23 ? 266 GLY B O 1 ATOM 4121 N N . THR B 1 267 ? 27.964 38.550 51.911 1.00 43.22 ? 267 THR B N 1 ATOM 4122 C CA . THR B 1 267 ? 27.007 38.346 52.998 1.00 43.59 ? 267 THR B CA 1 ATOM 4123 C C . THR B 1 267 ? 26.121 39.575 53.007 1.00 44.21 ? 267 THR B C 1 ATOM 4124 O O . THR B 1 267 ? 26.706 40.575 52.584 1.00 44.83 ? 267 THR B O 1 ATOM 4125 C CB . THR B 1 267 ? 27.705 38.183 54.364 1.00 43.60 ? 267 THR B CB 1 ATOM 4126 O OG1 . THR B 1 267 ? 26.726 38.033 55.403 1.00 41.73 ? 267 THR B OG1 1 ATOM 4127 C CG2 . THR B 1 267 ? 28.726 39.237 54.696 1.00 34.57 ? 267 THR B CG2 1 ATOM 4128 N N . CYS B 1 268 ? 24.816 39.524 53.185 1.00 44.46 ? 268 CYS B N 1 ATOM 4129 C CA . CYS B 1 268 ? 24.072 40.792 53.123 1.00 44.49 ? 268 CYS B CA 1 ATOM 4130 C C . CYS B 1 268 ? 23.519 41.222 54.486 1.00 44.70 ? 268 CYS B C 1 ATOM 4131 O O . CYS B 1 268 ? 23.131 40.363 55.274 1.00 43.30 ? 268 CYS B O 1 ATOM 4132 C CB . CYS B 1 268 ? 22.926 40.542 52.113 1.00 46.96 ? 268 CYS B CB 1 ATOM 4133 S SG . CYS B 1 268 ? 23.578 39.969 50.509 1.00 44.87 ? 268 CYS B SG 1 ATOM 4134 N N . LEU B 1 269 ? 23.884 42.417 54.991 1.00 45.00 ? 269 LEU B N 1 ATOM 4135 C CA . LEU B 1 269 ? 23.100 42.960 56.100 1.00 45.94 ? 269 LEU B CA 1 ATOM 4136 C C . LEU B 1 269 ? 21.577 42.812 56.007 1.00 45.84 ? 269 LEU B C 1 ATOM 4137 O O . LEU B 1 269 ? 20.956 42.801 54.933 1.00 46.50 ? 269 LEU B O 1 ATOM 4138 C CB . LEU B 1 269 ? 23.396 44.424 56.376 1.00 43.81 ? 269 LEU B CB 1 ATOM 4139 C CG . LEU B 1 269 ? 24.664 44.705 57.166 1.00 44.22 ? 269 LEU B CG 1 ATOM 4140 C CD1 . LEU B 1 269 ? 24.681 46.153 57.605 1.00 42.87 ? 269 LEU B CD1 1 ATOM 4141 C CD2 . LEU B 1 269 ? 24.801 43.732 58.332 1.00 43.52 ? 269 LEU B CD2 1 ATOM 4142 O OXT . LEU B 1 269 ? 20.884 42.400 57.001 1.00 47.01 ? 269 LEU B OXT 1 HETATM 4143 O O . HOH C 2 . ? 56.839 -2.055 54.103 1.00 33.06 ? 270 HOH A O 1 HETATM 4144 O O . HOH C 2 . ? 64.019 7.062 42.381 1.00 35.79 ? 271 HOH A O 1 HETATM 4145 O O . HOH C 2 . ? 74.651 1.650 53.795 1.00 31.57 ? 272 HOH A O 1 HETATM 4146 O O . HOH C 2 . ? 50.245 17.349 63.209 1.00 34.21 ? 273 HOH A O 1 HETATM 4147 O O . HOH C 2 . ? 62.959 -1.152 50.970 1.00 37.10 ? 274 HOH A O 1 HETATM 4148 O O . HOH C 2 . ? 64.227 24.171 52.790 1.00 75.01 ? 275 HOH A O 1 HETATM 4149 O O . HOH C 2 . ? 58.468 26.653 49.691 1.00 78.79 ? 276 HOH A O 1 HETATM 4150 O O . HOH C 2 . ? 49.478 -3.408 53.929 1.00 42.84 ? 277 HOH A O 1 HETATM 4151 O O . HOH C 2 . ? 55.660 -9.078 86.296 1.00 54.04 ? 278 HOH A O 1 HETATM 4152 O O . HOH C 2 . ? 70.345 0.772 54.130 1.00 35.74 ? 279 HOH A O 1 HETATM 4153 O O . HOH C 2 . ? 62.554 24.320 50.700 1.00 60.45 ? 280 HOH A O 1 HETATM 4154 O O . HOH C 2 . ? 57.313 -6.191 51.869 1.00 31.59 ? 281 HOH A O 1 HETATM 4155 O O . HOH C 2 . ? 50.881 8.987 39.479 1.00 48.50 ? 282 HOH A O 1 HETATM 4156 O O . HOH C 2 . ? 41.649 -5.029 57.031 1.00 61.40 ? 283 HOH A O 1 HETATM 4157 O O . HOH C 2 . ? 60.525 27.756 54.375 1.00 71.54 ? 284 HOH A O 1 HETATM 4158 O O . HOH C 2 . ? 44.329 -16.131 62.112 1.00 81.18 ? 285 HOH A O 1 HETATM 4159 O O . HOH C 2 . ? 62.679 -8.742 62.693 1.00 47.99 ? 286 HOH A O 1 HETATM 4160 O O . HOH C 2 . ? 50.000 -16.395 54.999 1.00 67.07 ? 287 HOH A O 1 HETATM 4161 O O . HOH C 2 . ? 61.409 -13.918 56.421 1.00 61.00 ? 288 HOH A O 1 HETATM 4162 O O . HOH C 2 . ? 40.484 -8.575 55.311 1.00 83.49 ? 289 HOH A O 1 HETATM 4163 O O . HOH C 2 . ? 68.974 17.312 59.021 1.00 80.89 ? 290 HOH A O 1 HETATM 4164 O O . HOH C 2 . ? 54.142 30.251 66.831 1.00 100.13 ? 291 HOH A O 1 HETATM 4165 O O . HOH C 2 . ? 74.269 9.718 50.474 1.00 80.08 ? 292 HOH A O 1 HETATM 4166 O O . HOH C 2 . ? 70.503 8.957 61.498 1.00 41.26 ? 293 HOH A O 1 HETATM 4167 O O . HOH C 2 . ? 37.367 1.868 56.121 1.00 62.75 ? 294 HOH A O 1 HETATM 4168 O O . HOH C 2 . ? 50.950 13.612 62.090 1.00 58.76 ? 295 HOH A O 1 HETATM 4169 O O . HOH C 2 . ? 50.794 -20.805 67.767 1.00 86.43 ? 296 HOH A O 1 HETATM 4170 O O . HOH C 2 . ? 45.227 -11.052 49.524 1.00 40.20 ? 297 HOH A O 1 HETATM 4171 O O . HOH C 2 . ? 54.976 -3.818 53.367 1.00 51.53 ? 298 HOH A O 1 HETATM 4172 O O . HOH C 2 . ? 31.639 8.158 56.623 1.00 95.84 ? 299 HOH A O 1 HETATM 4173 O O . HOH C 2 . ? 60.319 18.996 60.441 1.00 29.56 ? 300 HOH A O 1 HETATM 4174 O O . HOH C 2 . ? 33.020 11.086 46.908 1.00 95.35 ? 301 HOH A O 1 HETATM 4175 O O . HOH C 2 . ? 32.367 5.584 51.242 1.00 86.71 ? 302 HOH A O 1 HETATM 4176 O O . HOH C 2 . ? 71.697 14.080 55.159 1.00 52.67 ? 303 HOH A O 1 HETATM 4177 O O . HOH C 2 . ? 45.041 -11.883 45.898 1.00 57.75 ? 304 HOH A O 1 HETATM 4178 O O . HOH C 2 . ? 33.435 12.303 65.040 1.00 71.01 ? 305 HOH A O 1 HETATM 4179 O O . HOH C 2 . ? 61.890 22.596 65.809 1.00 64.85 ? 306 HOH A O 1 HETATM 4180 O O . HOH C 2 . ? 66.221 -12.729 54.925 1.00 80.06 ? 307 HOH A O 1 HETATM 4181 O O . HOH C 2 . ? 44.479 12.264 44.729 1.00 68.03 ? 308 HOH A O 1 HETATM 4182 O O . HOH C 2 . ? 50.536 27.412 62.796 1.00 72.49 ? 309 HOH A O 1 HETATM 4183 O O . HOH C 2 . ? 40.176 15.942 52.056 1.00 74.41 ? 310 HOH A O 1 HETATM 4184 O O . HOH C 2 . ? 54.375 25.758 55.253 1.00 64.61 ? 311 HOH A O 1 HETATM 4185 O O . HOH C 2 . ? 64.909 24.147 61.801 1.00 75.51 ? 312 HOH A O 1 HETATM 4186 O O . HOH C 2 . ? 64.220 -6.511 61.252 1.00 76.80 ? 313 HOH A O 1 HETATM 4187 O O . HOH C 2 . ? 71.674 4.041 47.263 1.00 64.12 ? 314 HOH A O 1 HETATM 4188 O O . HOH C 2 . ? 35.349 23.491 64.944 1.00 68.44 ? 315 HOH A O 1 HETATM 4189 O O . HOH C 2 . ? 63.667 -4.433 48.301 1.00 65.62 ? 316 HOH A O 1 HETATM 4190 O O . HOH C 2 . ? 67.325 4.730 67.954 1.00 46.18 ? 317 HOH A O 1 HETATM 4191 O O . HOH C 2 . ? 41.941 29.276 67.829 1.00 109.73 ? 318 HOH A O 1 HETATM 4192 O O . HOH C 2 . ? 53.680 17.841 54.615 1.00 26.94 ? 319 HOH A O 1 HETATM 4193 O O . HOH C 2 . ? 59.532 11.884 43.154 1.00 53.59 ? 320 HOH A O 1 HETATM 4194 O O . HOH C 2 . ? 64.690 22.604 57.694 1.00 66.88 ? 321 HOH A O 1 HETATM 4195 O O . HOH C 2 . ? 38.717 10.171 59.635 1.00 66.42 ? 322 HOH A O 1 HETATM 4196 O O . HOH C 2 . ? 63.268 13.423 45.223 1.00 49.81 ? 323 HOH A O 1 HETATM 4197 O O . HOH C 2 . ? 59.646 -4.132 49.611 1.00 80.94 ? 324 HOH A O 1 HETATM 4198 O O . HOH C 2 . ? 65.214 22.364 64.365 1.00 58.51 ? 325 HOH A O 1 HETATM 4199 O O . HOH C 2 . ? 40.514 -15.392 64.951 1.00 78.46 ? 326 HOH A O 1 HETATM 4200 O O . HOH C 2 . ? 50.912 -4.532 51.665 1.00 57.43 ? 327 HOH A O 1 HETATM 4201 O O . HOH C 2 . ? 53.280 -15.475 55.294 1.00 43.02 ? 328 HOH A O 1 HETATM 4202 O O . HOH C 2 . ? 38.488 -6.025 55.668 1.00 72.98 ? 329 HOH A O 1 HETATM 4203 O O . HOH C 2 . ? 37.272 12.481 58.764 1.00 73.72 ? 330 HOH A O 1 HETATM 4204 O O . HOH C 2 . ? 28.344 2.692 59.723 1.00 73.13 ? 331 HOH A O 1 HETATM 4205 O O . HOH C 2 . ? 71.276 -5.557 62.216 1.00 63.99 ? 332 HOH A O 1 HETATM 4206 O O . HOH C 2 . ? 59.371 27.813 64.970 1.00 69.77 ? 333 HOH A O 1 HETATM 4207 O O . HOH C 2 . ? 64.064 13.884 67.939 1.00 66.57 ? 334 HOH A O 1 HETATM 4208 O O . HOH C 2 . ? 66.873 -0.436 68.550 1.00 76.57 ? 335 HOH A O 1 HETATM 4209 O O . HOH C 2 . ? 59.667 -7.153 51.248 1.00 50.03 ? 336 HOH A O 1 HETATM 4210 O O . HOH C 2 . ? 30.345 8.410 52.216 1.00 84.37 ? 337 HOH A O 1 HETATM 4211 O O . HOH C 2 . ? 67.074 4.483 44.486 1.00 43.53 ? 338 HOH A O 1 HETATM 4212 O O . HOH C 2 . ? 52.635 -17.941 57.545 1.00 73.12 ? 339 HOH A O 1 HETATM 4213 O O . HOH C 2 . ? 60.330 24.937 59.654 1.00 52.63 ? 340 HOH A O 1 HETATM 4214 O O . HOH C 2 . ? 67.342 3.013 46.668 1.00 37.18 ? 341 HOH A O 1 HETATM 4215 O O . HOH C 2 . ? 70.759 -2.063 63.343 1.00 73.73 ? 342 HOH A O 1 HETATM 4216 O O . HOH C 2 . ? 39.144 8.670 62.647 1.00 49.90 ? 343 HOH A O 1 HETATM 4217 O O . HOH C 2 . ? 37.315 27.521 68.027 1.00 78.46 ? 344 HOH A O 1 HETATM 4218 O O . HOH C 2 . ? 72.875 2.460 49.507 1.00 57.05 ? 345 HOH A O 1 HETATM 4219 O O . HOH C 2 . ? 57.800 30.335 50.658 1.00 38.20 ? 346 HOH A O 1 HETATM 4220 O O . HOH C 2 . ? 36.028 -4.615 50.672 1.00 95.23 ? 347 HOH A O 1 HETATM 4221 O O . HOH C 2 . ? 36.443 23.627 70.788 1.00 117.19 ? 348 HOH A O 1 HETATM 4222 O O . HOH C 2 . ? 70.179 -3.028 54.458 1.00 52.53 ? 349 HOH A O 1 HETATM 4223 O O . HOH C 2 . ? 65.927 6.740 44.010 1.00 44.78 ? 350 HOH A O 1 HETATM 4224 O O . HOH C 2 . ? 37.713 23.886 59.707 1.00 67.57 ? 351 HOH A O 1 HETATM 4225 O O . HOH C 2 . ? 33.747 6.635 61.342 1.00 75.17 ? 352 HOH A O 1 HETATM 4226 O O . HOH C 2 . ? 63.141 7.343 72.129 1.00 46.17 ? 353 HOH A O 1 HETATM 4227 O O . HOH C 2 . ? 65.161 17.796 51.180 1.00 65.60 ? 354 HOH A O 1 HETATM 4228 O O . HOH C 2 . ? 56.418 20.604 40.396 1.00 83.48 ? 355 HOH A O 1 HETATM 4229 O O . HOH C 2 . ? 33.528 -1.759 70.031 1.00 51.33 ? 356 HOH A O 1 HETATM 4230 O O . HOH C 2 . ? 60.469 20.306 43.938 1.00 103.37 ? 357 HOH A O 1 HETATM 4231 O O . HOH C 2 . ? 33.692 12.296 57.541 1.00 68.97 ? 358 HOH A O 1 HETATM 4232 O O . HOH C 2 . ? 41.029 -11.885 60.820 1.00 67.60 ? 359 HOH A O 1 HETATM 4233 O O . HOH C 2 . ? 64.152 -2.696 69.181 1.00 67.35 ? 360 HOH A O 1 HETATM 4234 O O . HOH C 2 . ? 34.597 15.984 52.812 1.00 87.50 ? 361 HOH A O 1 HETATM 4235 O O . HOH C 2 . ? 74.342 12.231 46.658 1.00 105.54 ? 362 HOH A O 1 HETATM 4236 O O . HOH C 2 . ? 56.689 -4.642 49.746 1.00 62.28 ? 363 HOH A O 1 HETATM 4237 O O . HOH C 2 . ? 66.072 15.640 48.207 1.00 97.39 ? 364 HOH A O 1 HETATM 4238 O O . HOH C 2 . ? 57.833 16.951 48.334 1.00 52.01 ? 365 HOH A O 1 HETATM 4239 O O . HOH C 2 . ? 68.240 15.796 46.004 1.00 96.74 ? 366 HOH A O 1 HETATM 4240 O O . HOH C 2 . ? 62.429 10.970 76.684 1.00 62.92 ? 367 HOH A O 1 HETATM 4241 O O . HOH C 2 . ? 61.364 0.098 40.191 1.00 58.47 ? 368 HOH A O 1 HETATM 4242 O O . HOH D 2 . ? 34.489 54.163 43.611 1.00 38.36 ? 270 HOH B O 1 HETATM 4243 O O . HOH D 2 . ? 13.120 40.037 40.470 1.00 62.70 ? 271 HOH B O 1 HETATM 4244 O O . HOH D 2 . ? 43.972 47.986 61.392 1.00 42.63 ? 272 HOH B O 1 HETATM 4245 O O . HOH D 2 . ? 49.716 33.171 63.517 1.00 58.50 ? 273 HOH B O 1 HETATM 4246 O O . HOH D 2 . ? 23.850 35.860 54.432 1.00 51.23 ? 274 HOH B O 1 HETATM 4247 O O . HOH D 2 . ? 55.079 29.948 49.452 1.00 63.31 ? 275 HOH B O 1 HETATM 4248 O O . HOH D 2 . ? 48.758 53.077 40.801 1.00 48.52 ? 276 HOH B O 1 HETATM 4249 O O . HOH D 2 . ? 20.544 26.397 32.917 1.00 72.38 ? 277 HOH B O 1 HETATM 4250 O O . HOH D 2 . ? 56.689 26.028 35.408 1.00 70.09 ? 278 HOH B O 1 HETATM 4251 O O . HOH D 2 . ? 26.686 26.957 47.788 1.00 65.15 ? 279 HOH B O 1 HETATM 4252 O O . HOH D 2 . ? 30.748 47.766 17.496 1.00 49.28 ? 280 HOH B O 1 HETATM 4253 O O . HOH D 2 . ? 16.760 55.071 37.988 1.00 62.58 ? 281 HOH B O 1 HETATM 4254 O O . HOH D 2 . ? 24.085 30.343 22.968 1.00 96.24 ? 282 HOH B O 1 HETATM 4255 O O . HOH D 2 . ? 22.324 55.058 55.148 1.00 50.46 ? 283 HOH B O 1 HETATM 4256 O O . HOH D 2 . ? 14.592 51.270 36.853 1.00 57.15 ? 284 HOH B O 1 HETATM 4257 O O . HOH D 2 . ? 32.969 27.191 58.958 1.00 61.92 ? 285 HOH B O 1 HETATM 4258 O O . HOH D 2 . ? 44.569 58.918 50.584 1.00 71.02 ? 286 HOH B O 1 HETATM 4259 O O . HOH D 2 . ? 39.447 47.199 23.835 1.00 54.88 ? 287 HOH B O 1 HETATM 4260 O O . HOH D 2 . ? 51.883 20.318 32.782 1.00 69.78 ? 288 HOH B O 1 HETATM 4261 O O . HOH D 2 . ? 38.414 39.957 16.417 1.00 65.35 ? 289 HOH B O 1 HETATM 4262 O O . HOH D 2 . ? 38.204 31.935 61.175 1.00 53.23 ? 290 HOH B O 1 HETATM 4263 O O . HOH D 2 . ? 26.845 56.470 25.839 1.00 90.24 ? 291 HOH B O 1 HETATM 4264 O O . HOH D 2 . ? 19.830 38.971 27.283 1.00 69.08 ? 292 HOH B O 1 HETATM 4265 O O . HOH D 2 . ? 33.175 53.982 49.311 1.00 68.10 ? 293 HOH B O 1 HETATM 4266 O O . HOH D 2 . ? 54.190 35.884 58.507 1.00 59.57 ? 294 HOH B O 1 HETATM 4267 O O . HOH D 2 . ? 25.076 57.723 47.097 1.00 64.25 ? 295 HOH B O 1 HETATM 4268 O O . HOH D 2 . ? 34.763 30.510 20.859 1.00 51.48 ? 296 HOH B O 1 HETATM 4269 O O . HOH D 2 . ? 57.867 40.949 39.349 1.00 79.85 ? 297 HOH B O 1 HETATM 4270 O O . HOH D 2 . ? 32.878 51.376 56.742 1.00 50.85 ? 298 HOH B O 1 HETATM 4271 O O . HOH D 2 . ? 37.071 56.362 58.557 1.00 50.83 ? 299 HOH B O 1 HETATM 4272 O O . HOH D 2 . ? 28.115 18.080 34.902 1.00 84.84 ? 300 HOH B O 1 HETATM 4273 O O . HOH D 2 . ? 46.190 56.873 55.315 1.00 59.57 ? 301 HOH B O 1 HETATM 4274 O O . HOH D 2 . ? 41.734 41.722 59.066 1.00 45.51 ? 302 HOH B O 1 HETATM 4275 O O . HOH D 2 . ? 36.303 33.415 63.322 1.00 58.33 ? 303 HOH B O 1 HETATM 4276 O O . HOH D 2 . ? 58.550 36.664 47.913 1.00 75.38 ? 304 HOH B O 1 HETATM 4277 O O . HOH D 2 . ? 12.064 38.397 38.491 1.00 113.67 ? 305 HOH B O 1 HETATM 4278 O O . HOH D 2 . ? 20.244 26.889 52.430 1.00 125.34 ? 306 HOH B O 1 HETATM 4279 O O . HOH D 2 . ? 32.187 50.253 53.785 1.00 47.76 ? 307 HOH B O 1 HETATM 4280 O O . HOH D 2 . ? 52.759 28.459 25.134 1.00 79.80 ? 308 HOH B O 1 HETATM 4281 O O . HOH D 2 . ? 38.587 39.297 61.056 1.00 37.82 ? 309 HOH B O 1 HETATM 4282 O O . HOH D 2 . ? 25.636 58.832 33.710 1.00 62.77 ? 310 HOH B O 1 HETATM 4283 O O . HOH D 2 . ? 51.378 21.677 36.947 1.00 43.47 ? 311 HOH B O 1 HETATM 4284 O O . HOH D 2 . ? 27.691 35.013 55.847 1.00 75.63 ? 312 HOH B O 1 HETATM 4285 O O . HOH D 2 . ? 27.126 32.247 59.617 1.00 84.13 ? 313 HOH B O 1 HETATM 4286 O O . HOH D 2 . ? 50.495 31.899 45.904 1.00 47.86 ? 314 HOH B O 1 HETATM 4287 O O . HOH D 2 . ? 52.610 23.129 22.945 1.00 82.04 ? 315 HOH B O 1 HETATM 4288 O O . HOH D 2 . ? 53.063 49.675 46.319 1.00 50.45 ? 316 HOH B O 1 HETATM 4289 O O . HOH D 2 . ? 58.663 33.322 39.526 1.00 102.46 ? 317 HOH B O 1 HETATM 4290 O O . HOH D 2 . ? 38.488 55.770 52.782 1.00 70.69 ? 318 HOH B O 1 HETATM 4291 O O . HOH D 2 . ? 24.907 47.466 17.122 1.00 53.94 ? 319 HOH B O 1 HETATM 4292 O O . HOH D 2 . ? 30.966 38.601 43.787 1.00 39.88 ? 320 HOH B O 1 HETATM 4293 O O . HOH D 2 . ? 32.099 18.869 35.263 1.00 103.47 ? 321 HOH B O 1 HETATM 4294 O O . HOH D 2 . ? 44.960 52.781 36.311 1.00 40.71 ? 322 HOH B O 1 HETATM 4295 O O . HOH D 2 . ? 27.382 27.986 27.205 1.00 37.95 ? 323 HOH B O 1 HETATM 4296 O O . HOH D 2 . ? 19.696 43.436 26.964 1.00 47.98 ? 324 HOH B O 1 HETATM 4297 O O . HOH D 2 . ? 27.844 41.059 49.404 1.00 35.65 ? 325 HOH B O 1 HETATM 4298 O O . HOH D 2 . ? 42.332 34.841 19.885 1.00 55.35 ? 326 HOH B O 1 HETATM 4299 O O . HOH D 2 . ? 32.249 16.983 50.592 1.00 88.37 ? 327 HOH B O 1 HETATM 4300 O O . HOH D 2 . ? 31.788 26.913 40.367 1.00 63.60 ? 328 HOH B O 1 HETATM 4301 O O . HOH D 2 . ? 52.433 30.269 30.577 1.00 59.95 ? 329 HOH B O 1 HETATM 4302 O O . HOH D 2 . ? 51.990 24.853 53.822 1.00 58.17 ? 330 HOH B O 1 HETATM 4303 O O . HOH D 2 . ? 41.975 18.780 25.149 1.00 72.98 ? 331 HOH B O 1 HETATM 4304 O O . HOH D 2 . ? 57.989 35.837 43.742 1.00 62.46 ? 332 HOH B O 1 HETATM 4305 O O . HOH D 2 . ? 20.709 37.291 23.427 1.00 56.67 ? 333 HOH B O 1 HETATM 4306 O O . HOH D 2 . ? 32.530 46.796 49.344 1.00 45.36 ? 334 HOH B O 1 HETATM 4307 O O . HOH D 2 . ? 38.953 58.051 48.413 1.00 92.45 ? 335 HOH B O 1 HETATM 4308 O O . HOH D 2 . ? 50.574 43.463 21.747 1.00 89.15 ? 336 HOH B O 1 HETATM 4309 O O . HOH D 2 . ? 29.821 51.061 51.323 1.00 42.75 ? 337 HOH B O 1 HETATM 4310 O O . HOH D 2 . ? 38.887 45.380 53.117 1.00 28.55 ? 338 HOH B O 1 HETATM 4311 O O . HOH D 2 . ? 29.624 31.827 55.583 1.00 58.79 ? 339 HOH B O 1 HETATM 4312 O O . HOH D 2 . ? 32.047 21.557 31.716 1.00 57.38 ? 340 HOH B O 1 HETATM 4313 O O . HOH D 2 . ? 42.297 52.467 56.968 1.00 66.38 ? 341 HOH B O 1 HETATM 4314 O O . HOH D 2 . ? 26.097 39.792 58.067 1.00 40.03 ? 342 HOH B O 1 HETATM 4315 O O . HOH D 2 . ? 47.537 41.200 58.249 1.00 54.76 ? 343 HOH B O 1 HETATM 4316 O O . HOH D 2 . ? 46.418 53.912 57.347 1.00 73.87 ? 344 HOH B O 1 HETATM 4317 O O . HOH D 2 . ? 27.512 37.704 58.718 1.00 76.98 ? 345 HOH B O 1 HETATM 4318 O O . HOH D 2 . ? 17.993 39.377 32.610 1.00 59.08 ? 346 HOH B O 1 HETATM 4319 O O . HOH D 2 . ? 42.879 17.189 45.021 1.00 55.77 ? 347 HOH B O 1 HETATM 4320 O O . HOH D 2 . ? 37.958 35.866 63.569 1.00 54.53 ? 348 HOH B O 1 HETATM 4321 O O . HOH D 2 . ? 14.783 44.955 49.759 1.00 74.28 ? 349 HOH B O 1 HETATM 4322 O O . HOH D 2 . ? 42.395 57.083 50.352 1.00 52.86 ? 350 HOH B O 1 HETATM 4323 O O . HOH D 2 . ? 19.701 41.486 49.577 1.00 63.56 ? 351 HOH B O 1 HETATM 4324 O O . HOH D 2 . ? 29.827 22.890 50.139 1.00 77.99 ? 352 HOH B O 1 HETATM 4325 O O . HOH D 2 . ? 57.397 35.779 38.693 1.00 76.04 ? 353 HOH B O 1 HETATM 4326 O O . HOH D 2 . ? 37.721 23.255 30.274 1.00 75.14 ? 354 HOH B O 1 HETATM 4327 O O . HOH D 2 . ? 17.214 54.805 27.477 1.00 101.23 ? 355 HOH B O 1 HETATM 4328 O O . HOH D 2 . ? 28.470 61.393 29.709 1.00 62.45 ? 356 HOH B O 1 HETATM 4329 O O . HOH D 2 . ? 27.336 41.212 18.042 1.00 60.52 ? 357 HOH B O 1 HETATM 4330 O O . HOH D 2 . ? 17.859 41.561 57.183 1.00 56.81 ? 358 HOH B O 1 HETATM 4331 O O . HOH D 2 . ? 37.778 16.677 32.797 1.00 99.06 ? 359 HOH B O 1 HETATM 4332 O O . HOH D 2 . ? 49.951 60.704 45.026 1.00 39.59 ? 360 HOH B O 1 HETATM 4333 O O . HOH D 2 . ? 47.457 41.895 34.322 1.00 46.08 ? 361 HOH B O 1 HETATM 4334 O O . HOH D 2 . ? 47.889 51.388 37.036 1.00 81.96 ? 362 HOH B O 1 HETATM 4335 O O . HOH D 2 . ? 31.770 57.951 38.248 1.00 42.61 ? 363 HOH B O 1 HETATM 4336 O O . HOH D 2 . ? 11.990 45.750 38.509 1.00 88.09 ? 364 HOH B O 1 HETATM 4337 O O . HOH D 2 . ? 14.059 42.603 41.725 1.00 89.87 ? 365 HOH B O 1 HETATM 4338 O O . HOH D 2 . ? 20.357 43.238 17.758 1.00 66.06 ? 366 HOH B O 1 HETATM 4339 O O . HOH D 2 . ? 18.196 35.282 27.074 1.00 83.75 ? 367 HOH B O 1 HETATM 4340 O O . HOH D 2 . ? 15.828 39.236 43.491 1.00 104.48 ? 368 HOH B O 1 HETATM 4341 O O . HOH D 2 . ? 52.097 37.674 26.428 1.00 63.97 ? 369 HOH B O 1 HETATM 4342 O O . HOH D 2 . ? 46.930 48.864 57.446 1.00 81.17 ? 370 HOH B O 1 HETATM 4343 O O . HOH D 2 . ? 21.072 56.451 44.569 1.00 69.71 ? 371 HOH B O 1 HETATM 4344 O O . HOH D 2 . ? 24.213 53.525 22.084 1.00 65.16 ? 372 HOH B O 1 HETATM 4345 O O . HOH D 2 . ? 56.879 43.544 46.192 1.00 64.41 ? 373 HOH B O 1 HETATM 4346 O O . HOH D 2 . ? 30.686 30.158 18.756 1.00 102.21 ? 374 HOH B O 1 HETATM 4347 O O . HOH D 2 . ? 18.727 32.583 34.394 1.00 61.39 ? 375 HOH B O 1 HETATM 4348 O O . HOH D 2 . ? 51.962 34.204 62.564 1.00 92.31 ? 376 HOH B O 1 HETATM 4349 O O . HOH D 2 . ? 21.628 25.087 47.689 1.00 77.43 ? 377 HOH B O 1 HETATM 4350 O O . HOH D 2 . ? 47.838 33.857 48.814 1.00 38.34 ? 378 HOH B O 1 HETATM 4351 O O . HOH D 2 . ? 36.209 53.092 36.374 1.00 76.38 ? 379 HOH B O 1 HETATM 4352 O O . HOH D 2 . ? 41.043 31.087 25.304 1.00 74.51 ? 380 HOH B O 1 HETATM 4353 O O . HOH D 2 . ? 29.861 47.856 51.868 1.00 103.93 ? 381 HOH B O 1 HETATM 4354 O O . HOH D 2 . ? 54.383 53.356 53.617 1.00 99.57 ? 382 HOH B O 1 HETATM 4355 O O . HOH D 2 . ? 25.029 44.490 52.652 1.00 45.38 ? 383 HOH B O 1 HETATM 4356 O O . HOH D 2 . ? 28.612 33.599 53.497 1.00 59.64 ? 384 HOH B O 1 HETATM 4357 O O . HOH D 2 . ? 43.077 58.977 52.780 1.00 60.58 ? 385 HOH B O 1 HETATM 4358 O O . HOH D 2 . ? 13.809 50.690 28.972 1.00 77.40 ? 386 HOH B O 1 HETATM 4359 O O . HOH D 2 . ? 57.351 33.710 54.520 1.00 61.23 ? 387 HOH B O 1 HETATM 4360 O O . HOH D 2 . ? 31.165 32.125 21.695 1.00 65.63 ? 388 HOH B O 1 HETATM 4361 O O . HOH D 2 . ? 17.000 54.674 32.738 1.00 62.18 ? 389 HOH B O 1 HETATM 4362 O O . HOH D 2 . ? 41.123 16.061 46.671 1.00 108.40 ? 390 HOH B O 1 HETATM 4363 O O . HOH D 2 . ? 20.047 33.505 26.995 1.00 68.82 ? 391 HOH B O 1 HETATM 4364 O O . HOH D 2 . ? 13.279 34.414 37.284 1.00 71.34 ? 392 HOH B O 1 HETATM 4365 O O . HOH D 2 . ? 33.329 58.980 41.643 1.00 86.78 ? 393 HOH B O 1 HETATM 4366 O O . HOH D 2 . ? 32.663 31.358 47.280 1.00 37.54 ? 394 HOH B O 1 HETATM 4367 O O . HOH D 2 . ? 22.580 50.215 20.060 1.00 80.18 ? 395 HOH B O 1 HETATM 4368 O O . HOH D 2 . ? 21.795 51.787 39.168 1.00 64.13 ? 396 HOH B O 1 HETATM 4369 O O . HOH D 2 . ? 32.783 56.092 40.656 1.00 127.94 ? 397 HOH B O 1 HETATM 4370 O O . HOH D 2 . ? 23.042 47.423 25.176 1.00 59.67 ? 398 HOH B O 1 HETATM 4371 O O . HOH D 2 . ? 26.013 31.318 55.042 1.00 81.06 ? 399 HOH B O 1 HETATM 4372 O O . HOH D 2 . ? 43.875 15.951 32.742 1.00 51.10 ? 400 HOH B O 1 HETATM 4373 O O . HOH D 2 . ? 33.907 16.041 45.770 1.00 83.11 ? 401 HOH B O 1 HETATM 4374 O O . HOH D 2 . ? 15.575 50.916 45.301 1.00 100.10 ? 402 HOH B O 1 HETATM 4375 O O . HOH D 2 . ? 43.023 36.362 62.673 1.00 74.26 ? 403 HOH B O 1 HETATM 4376 O O . HOH D 2 . ? 46.960 49.547 35.363 1.00 66.56 ? 404 HOH B O 1 HETATM 4377 O O . HOH D 2 . ? 35.514 56.176 39.579 1.00 48.25 ? 405 HOH B O 1 HETATM 4378 O O . HOH D 2 . ? 25.422 24.846 29.737 1.00 90.24 ? 406 HOH B O 1 HETATM 4379 O O . HOH D 2 . ? 16.444 46.987 28.223 1.00 59.38 ? 407 HOH B O 1 HETATM 4380 O O . HOH D 2 . ? 45.744 17.378 40.427 1.00 63.71 ? 408 HOH B O 1 HETATM 4381 O O . HOH D 2 . ? 20.074 33.895 23.507 1.00 74.10 ? 409 HOH B O 1 HETATM 4382 O O . HOH D 2 . ? 52.012 41.295 29.017 1.00 51.53 ? 410 HOH B O 1 HETATM 4383 O O . HOH D 2 . ? 13.760 53.960 39.186 1.00 85.65 ? 411 HOH B O 1 HETATM 4384 O O . HOH D 2 . ? 30.332 20.095 55.890 1.00 64.41 ? 412 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 GLU 1 1 1 GLU GLU A . n A 1 2 VAL 2 2 2 VAL VAL A . n A 1 3 SER 3 3 3 SER SER A . n A 1 4 GLN 4 4 4 GLN GLN A . n A 1 5 ASP 5 5 5 ASP ASP A . n A 1 6 LEU 6 6 6 LEU LEU A . n A 1 7 PHE 7 7 7 PHE PHE A . n A 1 8 ASN 8 8 8 ASN ASN A . n A 1 9 GLN 9 9 9 GLN GLN A . n A 1 10 PHE 10 10 10 PHE PHE A . n A 1 11 ASN 11 11 11 ASN ASN A . n A 1 12 LEU 12 12 12 LEU LEU A . n A 1 13 PHE 13 13 13 PHE PHE A . n A 1 14 ALA 14 14 14 ALA ALA A . n A 1 15 GLN 15 15 15 GLN GLN A . n A 1 16 TYR 16 16 16 TYR TYR A . n A 1 17 SER 17 17 17 SER SER A . n A 1 18 ALA 18 18 18 ALA ALA A . n A 1 19 ALA 19 19 19 ALA ALA A . n A 1 20 ALA 20 20 20 ALA ALA A . n A 1 21 TYR 21 21 21 TYR TYR A . n A 1 22 CYS 22 22 22 CYS CYS A . n A 1 23 GLY 23 23 23 GLY GLY A . n A 1 24 LYS 24 24 24 LYS LYS A . n A 1 25 ASN 25 25 25 ASN ASN A . n A 1 26 ASN 26 26 26 ASN ASN A . n A 1 27 ASP 27 27 27 ASP ASP A . n A 1 28 ALA 28 28 28 ALA ALA A . n A 1 29 PRO 29 29 29 PRO PRO A . n A 1 30 ALA 30 30 30 ALA ALA A . n A 1 31 GLY 31 31 31 GLY GLY A . n A 1 32 THR 32 32 32 THR THR A . n A 1 33 ASN 33 33 33 ASN ASN A . n A 1 34 ILE 34 34 34 ILE ILE A . n A 1 35 THR 35 35 35 THR THR A . n A 1 36 CYS 36 36 36 CYS CYS A . n A 1 37 THR 37 37 37 THR THR A . n A 1 38 GLY 38 38 38 GLY GLY A . n A 1 39 ASN 39 39 39 ASN ASN A . n A 1 40 ALA 40 40 40 ALA ALA A . n A 1 41 CYS 41 41 41 CYS CYS A . n A 1 42 PRO 42 42 42 PRO PRO A . n A 1 43 GLU 43 43 43 GLU GLU A . n A 1 44 VAL 44 44 44 VAL VAL A . n A 1 45 GLU 45 45 45 GLU GLU A . n A 1 46 LYS 46 46 46 LYS LYS A . n A 1 47 ALA 47 47 47 ALA ALA A . n A 1 48 ASP 48 48 48 ASP ASP A . n A 1 49 ALA 49 49 49 ALA ALA A . n A 1 50 THR 50 50 50 THR THR A . n A 1 51 PHE 51 51 51 PHE PHE A . n A 1 52 LEU 52 52 52 LEU LEU A . n A 1 53 TYR 53 53 53 TYR TYR A . n A 1 54 SER 54 54 54 SER SER A . n A 1 55 PHE 55 55 55 PHE PHE A . n A 1 56 GLU 56 56 56 GLU GLU A . n A 1 57 ASP 57 57 57 ASP ASP A . n A 1 58 SER 58 58 58 SER SER A . n A 1 59 GLY 59 59 59 GLY GLY A . n A 1 60 VAL 60 60 60 VAL VAL A . n A 1 61 GLY 61 61 61 GLY GLY A . n A 1 62 ASP 62 62 62 ASP ASP A . n A 1 63 VAL 63 63 63 VAL VAL A . n A 1 64 THR 64 64 64 THR THR A . n A 1 65 GLY 65 65 65 GLY GLY A . n A 1 66 PHE 66 66 66 PHE PHE A . n A 1 67 LEU 67 67 67 LEU LEU A . n A 1 68 ALA 68 68 68 ALA ALA A . n A 1 69 LEU 69 69 69 LEU LEU A . n A 1 70 ASP 70 70 70 ASP ASP A . n A 1 71 ASN 71 71 71 ASN ASN A . n A 1 72 THR 72 72 72 THR THR A . n A 1 73 ASN 73 73 73 ASN ASN A . n A 1 74 LYS 74 74 74 LYS LYS A . n A 1 75 LEU 75 75 75 LEU LEU A . n A 1 76 ILE 76 76 76 ILE ILE A . n A 1 77 VAL 77 77 77 VAL VAL A . n A 1 78 LEU 78 78 78 LEU LEU A . n A 1 79 SER 79 79 79 SER SER A . n A 1 80 PHE 80 80 80 PHE PHE A . n A 1 81 ARG 81 81 81 ARG ARG A . n A 1 82 GLY 82 82 82 GLY GLY A . n A 1 83 SER 83 83 83 SER SER A . n A 1 84 ARG 84 84 84 ARG ARG A . n A 1 85 SER 85 85 85 SER SER A . n A 1 86 ILE 86 86 86 ILE ILE A . n A 1 87 GLU 87 87 87 GLU GLU A . n A 1 88 ASN 88 88 88 ASN ASN A . n A 1 89 TRP 89 89 89 TRP TRP A . n A 1 90 ILE 90 90 90 ILE ILE A . n A 1 91 GLY 91 91 91 GLY GLY A . n A 1 92 ASN 92 92 92 ASN ASN A . n A 1 93 LEU 93 93 93 LEU LEU A . n A 1 94 ASN 94 94 94 ASN ASN A . n A 1 95 PHE 95 95 95 PHE PHE A . n A 1 96 ASP 96 96 96 ASP ASP A . n A 1 97 LEU 97 97 97 LEU LEU A . n A 1 98 LYS 98 98 98 LYS LYS A . n A 1 99 GLU 99 99 99 GLU GLU A . n A 1 100 ILE 100 100 100 ILE ILE A . n A 1 101 ASN 101 101 101 ASN ASN A . n A 1 102 ASP 102 102 102 ASP ASP A . n A 1 103 ILE 103 103 103 ILE ILE A . n A 1 104 CYS 104 104 104 CYS CYS A . n A 1 105 SER 105 105 105 SER SER A . n A 1 106 GLY 106 106 106 GLY GLY A . n A 1 107 CYS 107 107 107 CYS CYS A . n A 1 108 ARG 108 108 108 ARG ARG A . n A 1 109 GLY 109 109 109 GLY GLY A . n A 1 110 HIS 110 110 110 HIS HIS A . n A 1 111 ASP 111 111 111 ASP ASP A . n A 1 112 GLY 112 112 112 GLY GLY A . n A 1 113 PHE 113 113 113 PHE PHE A . n A 1 114 THR 114 114 114 THR THR A . n A 1 115 SER 115 115 115 SER SER A . n A 1 116 SER 116 116 116 SER SER A . n A 1 117 TRP 117 117 117 TRP TRP A . n A 1 118 ARG 118 118 118 ARG ARG A . n A 1 119 SER 119 119 119 SER SER A . n A 1 120 VAL 120 120 120 VAL VAL A . n A 1 121 ALA 121 121 121 ALA ALA A . n A 1 122 ASP 122 122 122 ASP ASP A . n A 1 123 THR 123 123 123 THR THR A . n A 1 124 LEU 124 124 124 LEU LEU A . n A 1 125 ARG 125 125 125 ARG ARG A . n A 1 126 GLN 126 126 126 GLN GLN A . n A 1 127 LYS 127 127 127 LYS LYS A . n A 1 128 VAL 128 128 128 VAL VAL A . n A 1 129 GLU 129 129 129 GLU GLU A . n A 1 130 ASP 130 130 130 ASP ASP A . n A 1 131 ALA 131 131 131 ALA ALA A . n A 1 132 VAL 132 132 132 VAL VAL A . n A 1 133 ARG 133 133 133 ARG ARG A . n A 1 134 GLU 134 134 134 GLU GLU A . n A 1 135 HIS 135 135 135 HIS HIS A . n A 1 136 PRO 136 136 136 PRO PRO A . n A 1 137 ASP 137 137 137 ASP ASP A . n A 1 138 TYR 138 138 138 TYR TYR A . n A 1 139 ARG 139 139 139 ARG ARG A . n A 1 140 VAL 140 140 140 VAL VAL A . n A 1 141 VAL 141 141 141 VAL VAL A . n A 1 142 PHE 142 142 142 PHE PHE A . n A 1 143 THR 143 143 143 THR THR A . n A 1 144 GLY 144 144 144 GLY GLY A . n A 1 145 HIS 145 145 145 HIS HIS A . n A 1 146 SER 146 146 146 SER SER A . n A 1 147 LEU 147 147 147 LEU LEU A . n A 1 148 GLY 148 148 148 GLY GLY A . n A 1 149 GLY 149 149 149 GLY GLY A . n A 1 150 ALA 150 150 150 ALA ALA A . n A 1 151 LEU 151 151 151 LEU LEU A . n A 1 152 ALA 152 152 152 ALA ALA A . n A 1 153 THR 153 153 153 THR THR A . n A 1 154 VAL 154 154 154 VAL VAL A . n A 1 155 ALA 155 155 155 ALA ALA A . n A 1 156 GLY 156 156 156 GLY GLY A . n A 1 157 ALA 157 157 157 ALA ALA A . n A 1 158 ASP 158 158 158 ASP ASP A . n A 1 159 LEU 159 159 159 LEU LEU A . n A 1 160 ARG 160 160 160 ARG ARG A . n A 1 161 GLY 161 161 161 GLY GLY A . n A 1 162 ASN 162 162 162 ASN ASN A . n A 1 163 GLY 163 163 163 GLY GLY A . n A 1 164 TYR 164 164 164 TYR TYR A . n A 1 165 ASP 165 165 165 ASP ASP A . n A 1 166 ILE 166 166 166 ILE ILE A . n A 1 167 ASP 167 167 167 ASP ASP A . n A 1 168 VAL 168 168 168 VAL VAL A . n A 1 169 PHE 169 169 169 PHE PHE A . n A 1 170 SER 170 170 170 SER SER A . n A 1 171 TYR 171 171 171 TYR TYR A . n A 1 172 GLY 172 172 172 GLY GLY A . n A 1 173 ALA 173 173 173 ALA ALA A . n A 1 174 PRO 174 174 174 PRO PRO A . n A 1 175 ARG 175 175 175 ARG ARG A . n A 1 176 VAL 176 176 176 VAL VAL A . n A 1 177 GLY 177 177 177 GLY GLY A . n A 1 178 ASN 178 178 178 ASN ASN A . n A 1 179 ARG 179 179 179 ARG ARG A . n A 1 180 ALA 180 180 180 ALA ALA A . n A 1 181 PHE 181 181 181 PHE PHE A . n A 1 182 ALA 182 182 182 ALA ALA A . n A 1 183 GLU 183 183 183 GLU GLU A . n A 1 184 PHE 184 184 184 PHE PHE A . n A 1 185 LEU 185 185 185 LEU LEU A . n A 1 186 THR 186 186 186 THR THR A . n A 1 187 VAL 187 187 187 VAL VAL A . n A 1 188 GLN 188 188 188 GLN GLN A . n A 1 189 THR 189 189 189 THR THR A . n A 1 190 GLY 190 190 190 GLY GLY A . n A 1 191 GLY 191 191 191 GLY GLY A . n A 1 192 THR 192 192 192 THR THR A . n A 1 193 LEU 193 193 193 LEU LEU A . n A 1 194 TYR 194 194 194 TYR TYR A . n A 1 195 ARG 195 195 195 ARG ARG A . n A 1 196 ILE 196 196 196 ILE ILE A . n A 1 197 THR 197 197 197 THR THR A . n A 1 198 HIS 198 198 198 HIS HIS A . n A 1 199 THR 199 199 199 THR THR A . n A 1 200 ASN 200 200 200 ASN ASN A . n A 1 201 ASP 201 201 201 ASP ASP A . n A 1 202 ILE 202 202 202 ILE ILE A . n A 1 203 VAL 203 203 203 VAL VAL A . n A 1 204 PRO 204 204 204 PRO PRO A . n A 1 205 ARG 205 205 205 ARG ARG A . n A 1 206 LEU 206 206 206 LEU LEU A . n A 1 207 PRO 207 207 207 PRO PRO A . n A 1 208 PRO 208 208 208 PRO PRO A . n A 1 209 ARG 209 209 209 ARG ARG A . n A 1 210 GLU 210 210 210 GLU GLU A . n A 1 211 PHE 211 211 211 PHE PHE A . n A 1 212 GLY 212 212 212 GLY GLY A . n A 1 213 TYR 213 213 213 TYR TYR A . n A 1 214 SER 214 214 214 SER SER A . n A 1 215 HIS 215 215 215 HIS HIS A . n A 1 216 SER 216 216 216 SER SER A . n A 1 217 SER 217 217 217 SER SER A . n A 1 218 PRO 218 218 218 PRO PRO A . n A 1 219 GLU 219 219 219 GLU GLU A . n A 1 220 TYR 220 220 220 TYR TYR A . n A 1 221 TRP 221 221 221 TRP TRP A . n A 1 222 ILE 222 222 222 ILE ILE A . n A 1 223 LYS 223 223 223 LYS LYS A . n A 1 224 SER 224 224 224 SER SER A . n A 1 225 GLY 225 225 225 GLY GLY A . n A 1 226 THR 226 226 226 THR THR A . n A 1 227 LEU 227 227 227 LEU LEU A . n A 1 228 VAL 228 228 228 VAL VAL A . n A 1 229 PRO 229 229 229 PRO PRO A . n A 1 230 VAL 230 230 230 VAL VAL A . n A 1 231 THR 231 231 231 THR THR A . n A 1 232 ARG 232 232 232 ARG ARG A . n A 1 233 ASN 233 233 233 ASN ASN A . n A 1 234 ASP 234 234 234 ASP ASP A . n A 1 235 ILE 235 235 235 ILE ILE A . n A 1 236 VAL 236 236 236 VAL VAL A . n A 1 237 LYS 237 237 237 LYS LYS A . n A 1 238 ILE 238 238 238 ILE ILE A . n A 1 239 GLU 239 239 239 GLU GLU A . n A 1 240 GLY 240 240 240 GLY GLY A . n A 1 241 ILE 241 241 241 ILE ILE A . n A 1 242 ASP 242 242 242 ASP ASP A . n A 1 243 ALA 243 243 243 ALA ALA A . n A 1 244 THR 244 244 244 THR THR A . n A 1 245 GLY 245 245 245 GLY GLY A . n A 1 246 GLY 246 246 246 GLY GLY A . n A 1 247 ASN 247 247 247 ASN ASN A . n A 1 248 ASN 248 248 248 ASN ASN A . n A 1 249 GLN 249 249 249 GLN GLN A . n A 1 250 PRO 250 250 250 PRO PRO A . n A 1 251 ASN 251 251 251 ASN ASN A . n A 1 252 ILE 252 252 252 ILE ILE A . n A 1 253 PRO 253 253 253 PRO PRO A . n A 1 254 ASP 254 254 254 ASP ASP A . n A 1 255 ILE 255 255 255 ILE ILE A . n A 1 256 PRO 256 256 256 PRO PRO A . n A 1 257 ALA 257 257 257 ALA ALA A . n A 1 258 HIS 258 258 258 HIS HIS A . n A 1 259 LEU 259 259 259 LEU LEU A . n A 1 260 TRP 260 260 260 TRP TRP A . n A 1 261 TYR 261 261 261 TYR TYR A . n A 1 262 PHE 262 262 262 PHE PHE A . n A 1 263 GLY 263 263 263 GLY GLY A . n A 1 264 LEU 264 264 264 LEU LEU A . n A 1 265 ILE 265 265 265 ILE ILE A . n A 1 266 GLY 266 266 266 GLY GLY A . n A 1 267 THR 267 267 267 THR THR A . n A 1 268 CYS 268 268 268 CYS CYS A . n A 1 269 LEU 269 269 269 LEU LEU A . n B 1 1 GLU 1 1 1 GLU GLU B . n B 1 2 VAL 2 2 2 VAL VAL B . n B 1 3 SER 3 3 3 SER SER B . n B 1 4 GLN 4 4 4 GLN GLN B . n B 1 5 ASP 5 5 5 ASP ASP B . n B 1 6 LEU 6 6 6 LEU LEU B . n B 1 7 PHE 7 7 7 PHE PHE B . n B 1 8 ASN 8 8 8 ASN ASN B . n B 1 9 GLN 9 9 9 GLN GLN B . n B 1 10 PHE 10 10 10 PHE PHE B . n B 1 11 ASN 11 11 11 ASN ASN B . n B 1 12 LEU 12 12 12 LEU LEU B . n B 1 13 PHE 13 13 13 PHE PHE B . n B 1 14 ALA 14 14 14 ALA ALA B . n B 1 15 GLN 15 15 15 GLN GLN B . n B 1 16 TYR 16 16 16 TYR TYR B . n B 1 17 SER 17 17 17 SER SER B . n B 1 18 ALA 18 18 18 ALA ALA B . n B 1 19 ALA 19 19 19 ALA ALA B . n B 1 20 ALA 20 20 20 ALA ALA B . n B 1 21 TYR 21 21 21 TYR TYR B . n B 1 22 CYS 22 22 22 CYS CYS B . n B 1 23 GLY 23 23 23 GLY GLY B . n B 1 24 LYS 24 24 24 LYS LYS B . n B 1 25 ASN 25 25 25 ASN ASN B . n B 1 26 ASN 26 26 26 ASN ASN B . n B 1 27 ASP 27 27 27 ASP ASP B . n B 1 28 ALA 28 28 28 ALA ALA B . n B 1 29 PRO 29 29 29 PRO PRO B . n B 1 30 ALA 30 30 30 ALA ALA B . n B 1 31 GLY 31 31 31 GLY GLY B . n B 1 32 THR 32 32 32 THR THR B . n B 1 33 ASN 33 33 33 ASN ASN B . n B 1 34 ILE 34 34 34 ILE ILE B . n B 1 35 THR 35 35 35 THR THR B . n B 1 36 CYS 36 36 36 CYS CYS B . n B 1 37 THR 37 37 37 THR THR B . n B 1 38 GLY 38 38 38 GLY GLY B . n B 1 39 ASN 39 39 39 ASN ASN B . n B 1 40 ALA 40 40 40 ALA ALA B . n B 1 41 CYS 41 41 41 CYS CYS B . n B 1 42 PRO 42 42 42 PRO PRO B . n B 1 43 GLU 43 43 43 GLU GLU B . n B 1 44 VAL 44 44 44 VAL VAL B . n B 1 45 GLU 45 45 45 GLU GLU B . n B 1 46 LYS 46 46 46 LYS LYS B . n B 1 47 ALA 47 47 47 ALA ALA B . n B 1 48 ASP 48 48 48 ASP ASP B . n B 1 49 ALA 49 49 49 ALA ALA B . n B 1 50 THR 50 50 50 THR THR B . n B 1 51 PHE 51 51 51 PHE PHE B . n B 1 52 LEU 52 52 52 LEU LEU B . n B 1 53 TYR 53 53 53 TYR TYR B . n B 1 54 SER 54 54 54 SER SER B . n B 1 55 PHE 55 55 55 PHE PHE B . n B 1 56 GLU 56 56 56 GLU GLU B . n B 1 57 ASP 57 57 57 ASP ASP B . n B 1 58 SER 58 58 58 SER SER B . n B 1 59 GLY 59 59 59 GLY GLY B . n B 1 60 VAL 60 60 60 VAL VAL B . n B 1 61 GLY 61 61 61 GLY GLY B . n B 1 62 ASP 62 62 62 ASP ASP B . n B 1 63 VAL 63 63 63 VAL VAL B . n B 1 64 THR 64 64 64 THR THR B . n B 1 65 GLY 65 65 65 GLY GLY B . n B 1 66 PHE 66 66 66 PHE PHE B . n B 1 67 LEU 67 67 67 LEU LEU B . n B 1 68 ALA 68 68 68 ALA ALA B . n B 1 69 LEU 69 69 69 LEU LEU B . n B 1 70 ASP 70 70 70 ASP ASP B . n B 1 71 ASN 71 71 71 ASN ASN B . n B 1 72 THR 72 72 72 THR THR B . n B 1 73 ASN 73 73 73 ASN ASN B . n B 1 74 LYS 74 74 74 LYS LYS B . n B 1 75 LEU 75 75 75 LEU LEU B . n B 1 76 ILE 76 76 76 ILE ILE B . n B 1 77 VAL 77 77 77 VAL VAL B . n B 1 78 LEU 78 78 78 LEU LEU B . n B 1 79 SER 79 79 79 SER SER B . n B 1 80 PHE 80 80 80 PHE PHE B . n B 1 81 ARG 81 81 81 ARG ARG B . n B 1 82 GLY 82 82 82 GLY GLY B . n B 1 83 SER 83 83 83 SER SER B . n B 1 84 ARG 84 84 84 ARG ARG B . n B 1 85 SER 85 85 85 SER SER B . n B 1 86 ILE 86 86 86 ILE ILE B . n B 1 87 GLU 87 87 87 GLU GLU B . n B 1 88 ASN 88 88 88 ASN ASN B . n B 1 89 TRP 89 89 89 TRP TRP B . n B 1 90 ILE 90 90 90 ILE ILE B . n B 1 91 GLY 91 91 91 GLY GLY B . n B 1 92 ASN 92 92 92 ASN ASN B . n B 1 93 LEU 93 93 93 LEU LEU B . n B 1 94 ASN 94 94 94 ASN ASN B . n B 1 95 PHE 95 95 95 PHE PHE B . n B 1 96 ASP 96 96 96 ASP ASP B . n B 1 97 LEU 97 97 97 LEU LEU B . n B 1 98 LYS 98 98 98 LYS LYS B . n B 1 99 GLU 99 99 99 GLU GLU B . n B 1 100 ILE 100 100 100 ILE ILE B . n B 1 101 ASN 101 101 101 ASN ASN B . n B 1 102 ASP 102 102 102 ASP ASP B . n B 1 103 ILE 103 103 103 ILE ILE B . n B 1 104 CYS 104 104 104 CYS CYS B . n B 1 105 SER 105 105 105 SER SER B . n B 1 106 GLY 106 106 106 GLY GLY B . n B 1 107 CYS 107 107 107 CYS CYS B . n B 1 108 ARG 108 108 108 ARG ARG B . n B 1 109 GLY 109 109 109 GLY GLY B . n B 1 110 HIS 110 110 110 HIS HIS B . n B 1 111 ASP 111 111 111 ASP ASP B . n B 1 112 GLY 112 112 112 GLY GLY B . n B 1 113 PHE 113 113 113 PHE PHE B . n B 1 114 THR 114 114 114 THR THR B . n B 1 115 SER 115 115 115 SER SER B . n B 1 116 SER 116 116 116 SER SER B . n B 1 117 TRP 117 117 117 TRP TRP B . n B 1 118 ARG 118 118 118 ARG ARG B . n B 1 119 SER 119 119 119 SER SER B . n B 1 120 VAL 120 120 120 VAL VAL B . n B 1 121 ALA 121 121 121 ALA ALA B . n B 1 122 ASP 122 122 122 ASP ASP B . n B 1 123 THR 123 123 123 THR THR B . n B 1 124 LEU 124 124 124 LEU LEU B . n B 1 125 ARG 125 125 125 ARG ARG B . n B 1 126 GLN 126 126 126 GLN GLN B . n B 1 127 LYS 127 127 127 LYS LYS B . n B 1 128 VAL 128 128 128 VAL VAL B . n B 1 129 GLU 129 129 129 GLU GLU B . n B 1 130 ASP 130 130 130 ASP ASP B . n B 1 131 ALA 131 131 131 ALA ALA B . n B 1 132 VAL 132 132 132 VAL VAL B . n B 1 133 ARG 133 133 133 ARG ARG B . n B 1 134 GLU 134 134 134 GLU GLU B . n B 1 135 HIS 135 135 135 HIS HIS B . n B 1 136 PRO 136 136 136 PRO PRO B . n B 1 137 ASP 137 137 137 ASP ASP B . n B 1 138 TYR 138 138 138 TYR TYR B . n B 1 139 ARG 139 139 139 ARG ARG B . n B 1 140 VAL 140 140 140 VAL VAL B . n B 1 141 VAL 141 141 141 VAL VAL B . n B 1 142 PHE 142 142 142 PHE PHE B . n B 1 143 THR 143 143 143 THR THR B . n B 1 144 GLY 144 144 144 GLY GLY B . n B 1 145 HIS 145 145 145 HIS HIS B . n B 1 146 SER 146 146 146 SER SER B . n B 1 147 LEU 147 147 147 LEU LEU B . n B 1 148 GLY 148 148 148 GLY GLY B . n B 1 149 GLY 149 149 149 GLY GLY B . n B 1 150 ALA 150 150 150 ALA ALA B . n B 1 151 LEU 151 151 151 LEU LEU B . n B 1 152 ALA 152 152 152 ALA ALA B . n B 1 153 THR 153 153 153 THR THR B . n B 1 154 VAL 154 154 154 VAL VAL B . n B 1 155 ALA 155 155 155 ALA ALA B . n B 1 156 GLY 156 156 156 GLY GLY B . n B 1 157 ALA 157 157 157 ALA ALA B . n B 1 158 ASP 158 158 158 ASP ASP B . n B 1 159 LEU 159 159 159 LEU LEU B . n B 1 160 ARG 160 160 160 ARG ARG B . n B 1 161 GLY 161 161 161 GLY GLY B . n B 1 162 ASN 162 162 162 ASN ASN B . n B 1 163 GLY 163 163 163 GLY GLY B . n B 1 164 TYR 164 164 164 TYR TYR B . n B 1 165 ASP 165 165 165 ASP ASP B . n B 1 166 ILE 166 166 166 ILE ILE B . n B 1 167 ASP 167 167 167 ASP ASP B . n B 1 168 VAL 168 168 168 VAL VAL B . n B 1 169 PHE 169 169 169 PHE PHE B . n B 1 170 SER 170 170 170 SER SER B . n B 1 171 TYR 171 171 171 TYR TYR B . n B 1 172 GLY 172 172 172 GLY GLY B . n B 1 173 ALA 173 173 173 ALA ALA B . n B 1 174 PRO 174 174 174 PRO PRO B . n B 1 175 ARG 175 175 175 ARG ARG B . n B 1 176 VAL 176 176 176 VAL VAL B . n B 1 177 GLY 177 177 177 GLY GLY B . n B 1 178 ASN 178 178 178 ASN ASN B . n B 1 179 ARG 179 179 179 ARG ARG B . n B 1 180 ALA 180 180 180 ALA ALA B . n B 1 181 PHE 181 181 181 PHE PHE B . n B 1 182 ALA 182 182 182 ALA ALA B . n B 1 183 GLU 183 183 183 GLU GLU B . n B 1 184 PHE 184 184 184 PHE PHE B . n B 1 185 LEU 185 185 185 LEU LEU B . n B 1 186 THR 186 186 186 THR THR B . n B 1 187 VAL 187 187 187 VAL VAL B . n B 1 188 GLN 188 188 188 GLN GLN B . n B 1 189 THR 189 189 189 THR THR B . n B 1 190 GLY 190 190 190 GLY GLY B . n B 1 191 GLY 191 191 191 GLY GLY B . n B 1 192 THR 192 192 192 THR THR B . n B 1 193 LEU 193 193 193 LEU LEU B . n B 1 194 TYR 194 194 194 TYR TYR B . n B 1 195 ARG 195 195 195 ARG ARG B . n B 1 196 ILE 196 196 196 ILE ILE B . n B 1 197 THR 197 197 197 THR THR B . n B 1 198 HIS 198 198 198 HIS HIS B . n B 1 199 THR 199 199 199 THR THR B . n B 1 200 ASN 200 200 200 ASN ASN B . n B 1 201 ASP 201 201 201 ASP ASP B . n B 1 202 ILE 202 202 202 ILE ILE B . n B 1 203 VAL 203 203 203 VAL VAL B . n B 1 204 PRO 204 204 204 PRO PRO B . n B 1 205 ARG 205 205 205 ARG ARG B . n B 1 206 LEU 206 206 206 LEU LEU B . n B 1 207 PRO 207 207 207 PRO PRO B . n B 1 208 PRO 208 208 208 PRO PRO B . n B 1 209 ARG 209 209 209 ARG ARG B . n B 1 210 GLU 210 210 210 GLU GLU B . n B 1 211 PHE 211 211 211 PHE PHE B . n B 1 212 GLY 212 212 212 GLY GLY B . n B 1 213 TYR 213 213 213 TYR TYR B . n B 1 214 SER 214 214 214 SER SER B . n B 1 215 HIS 215 215 215 HIS HIS B . n B 1 216 SER 216 216 216 SER SER B . n B 1 217 SER 217 217 217 SER SER B . n B 1 218 PRO 218 218 218 PRO PRO B . n B 1 219 GLU 219 219 219 GLU GLU B . n B 1 220 TYR 220 220 220 TYR TYR B . n B 1 221 TRP 221 221 221 TRP TRP B . n B 1 222 ILE 222 222 222 ILE ILE B . n B 1 223 LYS 223 223 223 LYS LYS B . n B 1 224 SER 224 224 224 SER SER B . n B 1 225 GLY 225 225 225 GLY GLY B . n B 1 226 THR 226 226 226 THR THR B . n B 1 227 LEU 227 227 227 LEU LEU B . n B 1 228 VAL 228 228 228 VAL VAL B . n B 1 229 PRO 229 229 229 PRO PRO B . n B 1 230 VAL 230 230 230 VAL VAL B . n B 1 231 THR 231 231 231 THR THR B . n B 1 232 ARG 232 232 232 ARG ARG B . n B 1 233 ASN 233 233 233 ASN ASN B . n B 1 234 ASP 234 234 234 ASP ASP B . n B 1 235 ILE 235 235 235 ILE ILE B . n B 1 236 VAL 236 236 236 VAL VAL B . n B 1 237 LYS 237 237 237 LYS LYS B . n B 1 238 ILE 238 238 238 ILE ILE B . n B 1 239 GLU 239 239 239 GLU GLU B . n B 1 240 GLY 240 240 240 GLY GLY B . n B 1 241 ILE 241 241 241 ILE ILE B . n B 1 242 ASP 242 242 242 ASP ASP B . n B 1 243 ALA 243 243 243 ALA ALA B . n B 1 244 THR 244 244 244 THR THR B . n B 1 245 GLY 245 245 245 GLY GLY B . n B 1 246 GLY 246 246 246 GLY GLY B . n B 1 247 ASN 247 247 247 ASN ASN B . n B 1 248 ASN 248 248 248 ASN ASN B . n B 1 249 GLN 249 249 249 GLN GLN B . n B 1 250 PRO 250 250 250 PRO PRO B . n B 1 251 ASN 251 251 251 ASN ASN B . n B 1 252 ILE 252 252 252 ILE ILE B . n B 1 253 PRO 253 253 253 PRO PRO B . n B 1 254 ASP 254 254 254 ASP ASP B . n B 1 255 ILE 255 255 255 ILE ILE B . n B 1 256 PRO 256 256 256 PRO PRO B . n B 1 257 ALA 257 257 257 ALA ALA B . n B 1 258 HIS 258 258 258 HIS HIS B . n B 1 259 LEU 259 259 259 LEU LEU B . n B 1 260 TRP 260 260 260 TRP TRP B . n B 1 261 TYR 261 261 261 TYR TYR B . n B 1 262 PHE 262 262 262 PHE PHE B . n B 1 263 GLY 263 263 263 GLY GLY B . n B 1 264 LEU 264 264 264 LEU LEU B . n B 1 265 ILE 265 265 265 ILE ILE B . n B 1 266 GLY 266 266 266 GLY GLY B . n B 1 267 THR 267 267 267 THR THR B . n B 1 268 CYS 268 268 268 CYS CYS B . n B 1 269 LEU 269 269 269 LEU LEU 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 HOH 1 270 1 HOH HOH A . C 2 HOH 2 271 3 HOH HOH A . C 2 HOH 3 272 4 HOH HOH A . C 2 HOH 4 273 7 HOH HOH A . C 2 HOH 5 274 8 HOH HOH A . C 2 HOH 6 275 9 HOH HOH A . C 2 HOH 7 276 15 HOH HOH A . C 2 HOH 8 277 16 HOH HOH A . C 2 HOH 9 278 17 HOH HOH A . C 2 HOH 10 279 18 HOH HOH A . C 2 HOH 11 280 23 HOH HOH A . C 2 HOH 12 281 27 HOH HOH A . C 2 HOH 13 282 28 HOH HOH A . C 2 HOH 14 283 29 HOH HOH A . C 2 HOH 15 284 34 HOH HOH A . C 2 HOH 16 285 37 HOH HOH A . C 2 HOH 17 286 39 HOH HOH A . C 2 HOH 18 287 44 HOH HOH A . C 2 HOH 19 288 45 HOH HOH A . C 2 HOH 20 289 46 HOH HOH A . C 2 HOH 21 290 49 HOH HOH A . C 2 HOH 22 291 52 HOH HOH A . C 2 HOH 23 292 54 HOH HOH A . C 2 HOH 24 293 55 HOH HOH A . C 2 HOH 25 294 56 HOH HOH A . C 2 HOH 26 295 59 HOH HOH A . C 2 HOH 27 296 61 HOH HOH A . C 2 HOH 28 297 62 HOH HOH A . C 2 HOH 29 298 63 HOH HOH A . C 2 HOH 30 299 64 HOH HOH A . C 2 HOH 31 300 68 HOH HOH A . C 2 HOH 32 301 71 HOH HOH A . C 2 HOH 33 302 72 HOH HOH A . C 2 HOH 34 303 76 HOH HOH A . C 2 HOH 35 304 78 HOH HOH A . C 2 HOH 36 305 81 HOH HOH A . C 2 HOH 37 306 83 HOH HOH A . C 2 HOH 38 307 84 HOH HOH A . C 2 HOH 39 308 86 HOH HOH A . C 2 HOH 40 309 90 HOH HOH A . C 2 HOH 41 310 93 HOH HOH A . C 2 HOH 42 311 97 HOH HOH A . C 2 HOH 43 312 99 HOH HOH A . C 2 HOH 44 313 100 HOH HOH A . C 2 HOH 45 314 101 HOH HOH A . C 2 HOH 46 315 104 HOH HOH A . C 2 HOH 47 316 105 HOH HOH A . C 2 HOH 48 317 107 HOH HOH A . C 2 HOH 49 318 108 HOH HOH A . C 2 HOH 50 319 116 HOH HOH A . C 2 HOH 51 320 119 HOH HOH A . C 2 HOH 52 321 120 HOH HOH A . C 2 HOH 53 322 123 HOH HOH A . C 2 HOH 54 323 125 HOH HOH A . C 2 HOH 55 324 126 HOH HOH A . C 2 HOH 56 325 127 HOH HOH A . C 2 HOH 57 326 131 HOH HOH A . C 2 HOH 58 327 132 HOH HOH A . C 2 HOH 59 328 138 HOH HOH A . C 2 HOH 60 329 139 HOH HOH A . C 2 HOH 61 330 144 HOH HOH A . C 2 HOH 62 331 148 HOH HOH A . C 2 HOH 63 332 149 HOH HOH A . C 2 HOH 64 333 151 HOH HOH A . C 2 HOH 65 334 152 HOH HOH A . C 2 HOH 66 335 153 HOH HOH A . C 2 HOH 67 336 157 HOH HOH A . C 2 HOH 68 337 158 HOH HOH A . C 2 HOH 69 338 165 HOH HOH A . C 2 HOH 70 339 166 HOH HOH A . C 2 HOH 71 340 169 HOH HOH A . C 2 HOH 72 341 171 HOH HOH A . C 2 HOH 73 342 172 HOH HOH A . C 2 HOH 74 343 173 HOH HOH A . C 2 HOH 75 344 175 HOH HOH A . C 2 HOH 76 345 179 HOH HOH A . C 2 HOH 77 346 180 HOH HOH A . C 2 HOH 78 347 181 HOH HOH A . C 2 HOH 79 348 182 HOH HOH A . C 2 HOH 80 349 185 HOH HOH A . C 2 HOH 81 350 189 HOH HOH A . C 2 HOH 82 351 192 HOH HOH A . C 2 HOH 83 352 196 HOH HOH A . C 2 HOH 84 353 197 HOH HOH A . C 2 HOH 85 354 203 HOH HOH A . C 2 HOH 86 355 208 HOH HOH A . C 2 HOH 87 356 212 HOH HOH A . C 2 HOH 88 357 215 HOH HOH A . C 2 HOH 89 358 216 HOH HOH A . C 2 HOH 90 359 218 HOH HOH A . C 2 HOH 91 360 221 HOH HOH A . C 2 HOH 92 361 229 HOH HOH A . C 2 HOH 93 362 230 HOH HOH A . C 2 HOH 94 363 232 HOH HOH A . C 2 HOH 95 364 237 HOH HOH A . C 2 HOH 96 365 238 HOH HOH A . C 2 HOH 97 366 240 HOH HOH A . C 2 HOH 98 367 243 HOH HOH A . C 2 HOH 99 368 245 HOH HOH A . D 2 HOH 1 270 2 HOH HOH B . D 2 HOH 2 271 5 HOH HOH B . D 2 HOH 3 272 6 HOH HOH B . D 2 HOH 4 273 10 HOH HOH B . D 2 HOH 5 274 11 HOH HOH B . D 2 HOH 6 275 12 HOH HOH B . D 2 HOH 7 276 13 HOH HOH B . D 2 HOH 8 277 14 HOH HOH B . D 2 HOH 9 278 19 HOH HOH B . D 2 HOH 10 279 20 HOH HOH B . D 2 HOH 11 280 21 HOH HOH B . D 2 HOH 12 281 22 HOH HOH B . D 2 HOH 13 282 24 HOH HOH B . D 2 HOH 14 283 25 HOH HOH B . D 2 HOH 15 284 26 HOH HOH B . D 2 HOH 16 285 30 HOH HOH B . D 2 HOH 17 286 31 HOH HOH B . D 2 HOH 18 287 32 HOH HOH B . D 2 HOH 19 288 35 HOH HOH B . D 2 HOH 20 289 36 HOH HOH B . D 2 HOH 21 290 38 HOH HOH B . D 2 HOH 22 291 40 HOH HOH B . D 2 HOH 23 292 41 HOH HOH B . D 2 HOH 24 293 42 HOH HOH B . D 2 HOH 25 294 48 HOH HOH B . D 2 HOH 26 295 50 HOH HOH B . D 2 HOH 27 296 51 HOH HOH B . D 2 HOH 28 297 53 HOH HOH B . D 2 HOH 29 298 57 HOH HOH B . D 2 HOH 30 299 58 HOH HOH B . D 2 HOH 31 300 60 HOH HOH B . D 2 HOH 32 301 66 HOH HOH B . D 2 HOH 33 302 67 HOH HOH B . D 2 HOH 34 303 69 HOH HOH B . D 2 HOH 35 304 70 HOH HOH B . D 2 HOH 36 305 73 HOH HOH B . D 2 HOH 37 306 74 HOH HOH B . D 2 HOH 38 307 75 HOH HOH B . D 2 HOH 39 308 77 HOH HOH B . D 2 HOH 40 309 79 HOH HOH B . D 2 HOH 41 310 80 HOH HOH B . D 2 HOH 42 311 82 HOH HOH B . D 2 HOH 43 312 85 HOH HOH B . D 2 HOH 44 313 87 HOH HOH B . D 2 HOH 45 314 88 HOH HOH B . D 2 HOH 46 315 89 HOH HOH B . D 2 HOH 47 316 91 HOH HOH B . D 2 HOH 48 317 94 HOH HOH B . D 2 HOH 49 318 95 HOH HOH B . D 2 HOH 50 319 96 HOH HOH B . D 2 HOH 51 320 98 HOH HOH B . D 2 HOH 52 321 102 HOH HOH B . D 2 HOH 53 322 103 HOH HOH B . D 2 HOH 54 323 106 HOH HOH B . D 2 HOH 55 324 109 HOH HOH B . D 2 HOH 56 325 110 HOH HOH B . D 2 HOH 57 326 111 HOH HOH B . D 2 HOH 58 327 112 HOH HOH B . D 2 HOH 59 328 113 HOH HOH B . D 2 HOH 60 329 114 HOH HOH B . D 2 HOH 61 330 117 HOH HOH B . D 2 HOH 62 331 121 HOH HOH B . D 2 HOH 63 332 122 HOH HOH B . D 2 HOH 64 333 124 HOH HOH B . D 2 HOH 65 334 128 HOH HOH B . D 2 HOH 66 335 129 HOH HOH B . D 2 HOH 67 336 130 HOH HOH B . D 2 HOH 68 337 133 HOH HOH B . D 2 HOH 69 338 135 HOH HOH B . D 2 HOH 70 339 136 HOH HOH B . D 2 HOH 71 340 137 HOH HOH B . D 2 HOH 72 341 140 HOH HOH B . D 2 HOH 73 342 141 HOH HOH B . D 2 HOH 74 343 142 HOH HOH B . D 2 HOH 75 344 143 HOH HOH B . D 2 HOH 76 345 145 HOH HOH B . D 2 HOH 77 346 146 HOH HOH B . D 2 HOH 78 347 147 HOH HOH B . D 2 HOH 79 348 150 HOH HOH B . D 2 HOH 80 349 154 HOH HOH B . D 2 HOH 81 350 155 HOH HOH B . D 2 HOH 82 351 156 HOH HOH B . D 2 HOH 83 352 159 HOH HOH B . D 2 HOH 84 353 160 HOH HOH B . D 2 HOH 85 354 161 HOH HOH B . D 2 HOH 86 355 162 HOH HOH B . D 2 HOH 87 356 163 HOH HOH B . D 2 HOH 88 357 164 HOH HOH B . D 2 HOH 89 358 167 HOH HOH B . D 2 HOH 90 359 168 HOH HOH B . D 2 HOH 91 360 170 HOH HOH B . D 2 HOH 92 361 174 HOH HOH B . D 2 HOH 93 362 176 HOH HOH B . D 2 HOH 94 363 177 HOH HOH B . D 2 HOH 95 364 178 HOH HOH B . D 2 HOH 96 365 183 HOH HOH B . D 2 HOH 97 366 184 HOH HOH B . D 2 HOH 98 367 186 HOH HOH B . D 2 HOH 99 368 187 HOH HOH B . D 2 HOH 100 369 188 HOH HOH B . D 2 HOH 101 370 190 HOH HOH B . D 2 HOH 102 371 191 HOH HOH B . D 2 HOH 103 372 193 HOH HOH B . D 2 HOH 104 373 194 HOH HOH B . D 2 HOH 105 374 195 HOH HOH B . D 2 HOH 106 375 198 HOH HOH B . D 2 HOH 107 376 199 HOH HOH B . D 2 HOH 108 377 200 HOH HOH B . D 2 HOH 109 378 201 HOH HOH B . D 2 HOH 110 379 202 HOH HOH B . D 2 HOH 111 380 204 HOH HOH B . D 2 HOH 112 381 205 HOH HOH B . D 2 HOH 113 382 206 HOH HOH B . D 2 HOH 114 383 207 HOH HOH B . D 2 HOH 115 384 209 HOH HOH B . D 2 HOH 116 385 210 HOH HOH B . D 2 HOH 117 386 211 HOH HOH B . D 2 HOH 118 387 213 HOH HOH B . D 2 HOH 119 388 214 HOH HOH B . D 2 HOH 120 389 217 HOH HOH B . D 2 HOH 121 390 219 HOH HOH B . D 2 HOH 122 391 220 HOH HOH B . D 2 HOH 123 392 222 HOH HOH B . D 2 HOH 124 393 223 HOH HOH B . D 2 HOH 125 394 224 HOH HOH B . D 2 HOH 126 395 225 HOH HOH B . D 2 HOH 127 396 226 HOH HOH B . D 2 HOH 128 397 227 HOH HOH B . D 2 HOH 129 398 228 HOH HOH B . D 2 HOH 130 399 231 HOH HOH B . D 2 HOH 131 400 233 HOH HOH B . D 2 HOH 132 401 234 HOH HOH B . D 2 HOH 133 402 235 HOH HOH B . D 2 HOH 134 403 236 HOH HOH B . D 2 HOH 135 404 239 HOH HOH B . D 2 HOH 136 405 241 HOH HOH B . D 2 HOH 137 406 242 HOH HOH B . D 2 HOH 138 407 244 HOH HOH B . D 2 HOH 139 408 246 HOH HOH B . D 2 HOH 140 409 247 HOH HOH B . D 2 HOH 141 410 248 HOH HOH B . D 2 HOH 142 411 249 HOH HOH B . D 2 HOH 143 412 250 HOH HOH B . # loop_ _pdbx_struct_assembly.id _pdbx_struct_assembly.details _pdbx_struct_assembly.method_details _pdbx_struct_assembly.oligomeric_details _pdbx_struct_assembly.oligomeric_count 1 author_defined_assembly ? monomeric 1 2 author_defined_assembly ? monomeric 1 # loop_ _pdbx_struct_assembly_gen.assembly_id _pdbx_struct_assembly_gen.oper_expression _pdbx_struct_assembly_gen.asym_id_list 1 1 A,C 2 1 B,D # _pdbx_struct_oper_list.id 1 _pdbx_struct_oper_list.type 'identity operation' _pdbx_struct_oper_list.name 1_555 _pdbx_struct_oper_list.symmetry_operation x,y,z _pdbx_struct_oper_list.matrix[1][1] 1.0000000000 _pdbx_struct_oper_list.matrix[1][2] 0.0000000000 _pdbx_struct_oper_list.matrix[1][3] 0.0000000000 _pdbx_struct_oper_list.vector[1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][1] 0.0000000000 _pdbx_struct_oper_list.matrix[2][2] 1.0000000000 _pdbx_struct_oper_list.matrix[2][3] 0.0000000000 _pdbx_struct_oper_list.vector[2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][1] 0.0000000000 _pdbx_struct_oper_list.matrix[3][2] 0.0000000000 _pdbx_struct_oper_list.matrix[3][3] 1.0000000000 _pdbx_struct_oper_list.vector[3] 0.0000000000 # loop_ _pdbx_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 2000-12-20 2 'Structure model' 1 1 2008-04-27 3 'Structure model' 1 2 2011-07-13 4 'Structure model' 1 3 2018-01-31 # _pdbx_audit_revision_details.ordinal 1 _pdbx_audit_revision_details.revision_ordinal 1 _pdbx_audit_revision_details.data_content_type 'Structure model' _pdbx_audit_revision_details.provider repository _pdbx_audit_revision_details.type 'Initial release' _pdbx_audit_revision_details.description ? # loop_ _pdbx_audit_revision_group.ordinal _pdbx_audit_revision_group.revision_ordinal _pdbx_audit_revision_group.data_content_type _pdbx_audit_revision_group.group 1 2 'Structure model' 'Version format compliance' 2 3 'Structure model' 'Version format compliance' 3 4 'Structure model' 'Experimental preparation' # _pdbx_audit_revision_category.ordinal 1 _pdbx_audit_revision_category.revision_ordinal 4 _pdbx_audit_revision_category.data_content_type 'Structure model' _pdbx_audit_revision_category.category exptl_crystal_grow # _pdbx_audit_revision_item.ordinal 1 _pdbx_audit_revision_item.revision_ordinal 4 _pdbx_audit_revision_item.data_content_type 'Structure model' _pdbx_audit_revision_item.item '_exptl_crystal_grow.temp' # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal DENZO 'data reduction' . ? 1 SCALEPACK 'data scaling' . ? 2 AMoRE phasing . ? 3 REFMAC refinement . ? 4 # loop_ _pdbx_validate_rmsd_angle.id _pdbx_validate_rmsd_angle.PDB_model_num _pdbx_validate_rmsd_angle.auth_atom_id_1 _pdbx_validate_rmsd_angle.auth_asym_id_1 _pdbx_validate_rmsd_angle.auth_comp_id_1 _pdbx_validate_rmsd_angle.auth_seq_id_1 _pdbx_validate_rmsd_angle.PDB_ins_code_1 _pdbx_validate_rmsd_angle.label_alt_id_1 _pdbx_validate_rmsd_angle.auth_atom_id_2 _pdbx_validate_rmsd_angle.auth_asym_id_2 _pdbx_validate_rmsd_angle.auth_comp_id_2 _pdbx_validate_rmsd_angle.auth_seq_id_2 _pdbx_validate_rmsd_angle.PDB_ins_code_2 _pdbx_validate_rmsd_angle.label_alt_id_2 _pdbx_validate_rmsd_angle.auth_atom_id_3 _pdbx_validate_rmsd_angle.auth_asym_id_3 _pdbx_validate_rmsd_angle.auth_comp_id_3 _pdbx_validate_rmsd_angle.auth_seq_id_3 _pdbx_validate_rmsd_angle.PDB_ins_code_3 _pdbx_validate_rmsd_angle.label_alt_id_3 _pdbx_validate_rmsd_angle.angle_value _pdbx_validate_rmsd_angle.angle_target_value _pdbx_validate_rmsd_angle.angle_deviation _pdbx_validate_rmsd_angle.angle_standard_deviation _pdbx_validate_rmsd_angle.linker_flag 1 1 CB A ASP 5 ? ? CG A ASP 5 ? ? OD2 A ASP 5 ? ? 111.35 118.30 -6.95 0.90 N 2 1 CB A TYR 16 ? ? CG A TYR 16 ? ? CD2 A TYR 16 ? ? 115.78 121.00 -5.22 0.60 N 3 1 CB A TYR 21 ? ? CG A TYR 21 ? ? CD2 A TYR 21 ? ? 111.74 121.00 -9.26 0.60 N 4 1 CB A TYR 21 ? ? CG A TYR 21 ? ? CD1 A TYR 21 ? ? 128.73 121.00 7.73 0.60 N 5 1 CA A CYS 22 ? ? C A CYS 22 ? ? N A GLY 23 ? ? 102.47 116.20 -13.73 2.00 Y 6 1 NE A ARG 81 ? ? CZ A ARG 81 ? ? NH1 A ARG 81 ? ? 127.82 120.30 7.52 0.50 N 7 1 NE A ARG 84 ? ? CZ A ARG 84 ? ? NH1 A ARG 84 ? ? 125.51 120.30 5.21 0.50 N 8 1 NE A ARG 84 ? ? CZ A ARG 84 ? ? NH2 A ARG 84 ? ? 115.86 120.30 -4.44 0.50 N 9 1 NE A ARG 108 ? ? CZ A ARG 108 ? ? NH2 A ARG 108 ? ? 115.63 120.30 -4.67 0.50 N 10 1 CD A ARG 125 ? ? NE A ARG 125 ? ? CZ A ARG 125 ? ? 132.52 123.60 8.92 1.40 N 11 1 NE A ARG 125 ? ? CZ A ARG 125 ? ? NH1 A ARG 125 ? ? 116.32 120.30 -3.98 0.50 N 12 1 NE A ARG 125 ? ? CZ A ARG 125 ? ? NH2 A ARG 125 ? ? 126.68 120.30 6.38 0.50 N 13 1 OE1 A GLU 129 ? ? CD A GLU 129 ? ? OE2 A GLU 129 ? ? 141.82 123.30 18.52 1.20 N 14 1 O A GLU 134 ? ? C A GLU 134 ? ? N A HIS 135 ? ? 112.92 122.70 -9.78 1.60 Y 15 1 NE A ARG 139 ? ? CZ A ARG 139 ? ? NH1 A ARG 139 ? ? 124.88 120.30 4.58 0.50 N 16 1 NE A ARG 160 ? ? CZ A ARG 160 ? ? NH1 A ARG 160 ? ? 115.90 120.30 -4.40 0.50 N 17 1 NE A ARG 160 ? ? CZ A ARG 160 ? ? NH2 A ARG 160 ? ? 126.25 120.30 5.95 0.50 N 18 1 CB A PHE 169 ? ? CG A PHE 169 ? ? CD2 A PHE 169 ? ? 125.10 120.80 4.30 0.70 N 19 1 NH1 A ARG 175 ? ? CZ A ARG 175 ? ? NH2 A ARG 175 ? ? 126.55 119.40 7.15 1.10 N 20 1 NE A ARG 175 ? ? CZ A ARG 175 ? ? NH1 A ARG 175 ? ? 115.98 120.30 -4.32 0.50 N 21 1 NE A ARG 175 ? ? CZ A ARG 175 ? ? NH2 A ARG 175 ? ? 117.26 120.30 -3.04 0.50 N 22 1 NE A ARG 195 ? ? CZ A ARG 195 ? ? NH1 A ARG 195 ? ? 114.31 120.30 -5.99 0.50 N 23 1 NE A ARG 195 ? ? CZ A ARG 195 ? ? NH2 A ARG 195 ? ? 123.62 120.30 3.32 0.50 N 24 1 CB A ARG 205 ? ? CG A ARG 205 ? ? CD A ARG 205 ? ? 127.68 111.60 16.08 2.60 N 25 1 CD A ARG 205 ? ? NE A ARG 205 ? ? CZ A ARG 205 ? ? 153.69 123.60 30.09 1.40 N 26 1 NE A ARG 205 ? ? CZ A ARG 205 ? ? NH1 A ARG 205 ? ? 125.54 120.30 5.24 0.50 N 27 1 CD A ARG 209 ? ? NE A ARG 209 ? ? CZ A ARG 209 ? ? 140.39 123.60 16.79 1.40 N 28 1 NE A ARG 209 ? ? CZ A ARG 209 ? ? NH1 A ARG 209 ? ? 124.99 120.30 4.69 0.50 N 29 1 OE1 A GLU 219 ? ? CD A GLU 219 ? ? OE2 A GLU 219 ? ? 115.55 123.30 -7.75 1.20 N 30 1 NE A ARG 232 ? ? CZ A ARG 232 ? ? NH1 A ARG 232 ? ? 124.79 120.30 4.49 0.50 N 31 1 NE A ARG 232 ? ? CZ A ARG 232 ? ? NH2 A ARG 232 ? ? 112.82 120.30 -7.48 0.50 N 32 1 CB A ASP 234 ? ? CG A ASP 234 ? ? OD1 A ASP 234 ? ? 111.82 118.30 -6.48 0.90 N 33 1 C A GLY 245 ? ? N A GLY 246 ? ? CA A GLY 246 ? ? 144.42 122.30 22.12 2.10 Y 34 1 N A ASP 254 ? ? CA A ASP 254 ? ? CB A ASP 254 ? ? 97.95 110.60 -12.65 1.80 N 35 1 CB A ASP 254 ? ? CG A ASP 254 ? ? OD1 A ASP 254 ? ? 109.69 118.30 -8.61 0.90 N 36 1 C A PHE 262 ? ? N A GLY 263 ? ? CA A GLY 263 ? ? 135.64 122.30 13.34 2.10 Y 37 1 CA B GLN 9 ? ? CB B GLN 9 ? ? CG B GLN 9 ? ? 129.27 113.40 15.87 2.20 N 38 1 C B LYS 24 ? ? N B ASN 25 ? ? CA B ASN 25 ? ? 145.09 121.70 23.39 2.50 Y 39 1 CB B ASN 26 ? ? CA B ASN 26 ? ? C B ASN 26 ? ? 122.55 110.40 12.15 2.00 N 40 1 NE B ARG 81 ? ? CZ B ARG 81 ? ? NH1 B ARG 81 ? ? 126.25 120.30 5.95 0.50 N 41 1 CB B ASN 88 ? ? CA B ASN 88 ? ? C B ASN 88 ? ? 124.34 110.40 13.94 2.00 N 42 1 N B CYS 104 ? ? CA B CYS 104 ? ? CB B CYS 104 ? ? 125.19 110.80 14.39 1.50 N 43 1 CB B ASP 111 ? ? CG B ASP 111 ? ? OD1 B ASP 111 ? ? 125.34 118.30 7.04 0.90 N 44 1 NE B ARG 118 ? ? CZ B ARG 118 ? ? NH1 B ARG 118 ? ? 126.20 120.30 5.90 0.50 N 45 1 NE B ARG 118 ? ? CZ B ARG 118 ? ? NH2 B ARG 118 ? ? 115.55 120.30 -4.75 0.50 N 46 1 NE B ARG 125 ? ? CZ B ARG 125 ? ? NH2 B ARG 125 ? ? 125.43 120.30 5.13 0.50 N 47 1 NE B ARG 133 ? ? CZ B ARG 133 ? ? NH2 B ARG 133 ? ? 115.71 120.30 -4.59 0.50 N 48 1 CB B TYR 138 ? ? CG B TYR 138 ? ? CD2 B TYR 138 ? ? 114.43 121.00 -6.57 0.60 N 49 1 CB B TYR 138 ? ? CG B TYR 138 ? ? CD1 B TYR 138 ? ? 126.83 121.00 5.83 0.60 N 50 1 C B TYR 138 ? ? N B ARG 139 ? ? CA B ARG 139 ? ? 137.98 121.70 16.28 2.50 Y 51 1 NE B ARG 160 ? ? CZ B ARG 160 ? ? NH1 B ARG 160 ? ? 117.18 120.30 -3.12 0.50 N 52 1 CD B ARG 195 ? ? NE B ARG 195 ? ? CZ B ARG 195 ? ? 175.18 123.60 51.58 1.40 N 53 1 CD B ARG 205 ? ? NE B ARG 205 ? ? CZ B ARG 205 ? ? 135.22 123.60 11.62 1.40 N 54 1 NE B ARG 205 ? ? CZ B ARG 205 ? ? NH1 B ARG 205 ? ? 123.67 120.30 3.37 0.50 N 55 1 O B PRO 229 ? ? C B PRO 229 ? ? N B VAL 230 ? ? 110.38 122.70 -12.32 1.60 Y 56 1 NE B ARG 232 ? ? CZ B ARG 232 ? ? NH1 B ARG 232 ? ? 116.48 120.30 -3.82 0.50 N 57 1 CB B ASP 254 ? ? CG B ASP 254 ? ? OD2 B ASP 254 ? ? 124.27 118.30 5.97 0.90 N # loop_ _pdbx_validate_torsion.id _pdbx_validate_torsion.PDB_model_num _pdbx_validate_torsion.auth_comp_id _pdbx_validate_torsion.auth_asym_id _pdbx_validate_torsion.auth_seq_id _pdbx_validate_torsion.PDB_ins_code _pdbx_validate_torsion.label_alt_id _pdbx_validate_torsion.phi _pdbx_validate_torsion.psi 1 1 CYS A 22 ? ? -106.57 65.18 2 1 LYS A 24 ? ? 79.83 -31.87 3 1 ASP A 27 ? ? -167.56 96.56 4 1 ASP A 62 ? ? 50.23 92.08 5 1 SER A 146 ? ? 63.92 -135.12 6 1 THR A 199 ? ? 24.08 -118.05 7 1 ASN A 200 ? ? -99.35 32.22 8 1 PRO A 253 ? ? -69.43 -176.93 9 1 PHE A 262 ? ? 68.76 -32.02 10 1 THR A 267 ? ? -171.33 145.37 11 1 LYS B 24 ? ? 61.65 -10.17 12 1 ASP B 27 ? ? -152.50 41.25 13 1 CYS B 41 ? ? -150.75 66.60 14 1 ASP B 62 ? ? 45.77 72.44 15 1 PHE B 95 ? ? -54.29 -3.41 16 1 ASP B 102 ? ? -39.88 -35.25 17 1 ALA B 121 ? ? -51.39 -82.50 18 1 SER B 146 ? ? 64.75 -138.79 19 1 ARG B 160 ? ? -49.04 159.24 20 1 THR B 199 ? ? 28.88 -107.55 21 1 ASP B 201 ? ? -47.20 154.68 22 1 PHE B 262 ? ? 74.04 -29.83 # loop_ _pdbx_validate_main_chain_plane.id _pdbx_validate_main_chain_plane.PDB_model_num _pdbx_validate_main_chain_plane.auth_comp_id _pdbx_validate_main_chain_plane.auth_asym_id _pdbx_validate_main_chain_plane.auth_seq_id _pdbx_validate_main_chain_plane.PDB_ins_code _pdbx_validate_main_chain_plane.label_alt_id _pdbx_validate_main_chain_plane.improper_torsion_angle 1 1 ALA A 20 ? ? 13.81 2 1 CYS A 22 ? ? -15.45 3 1 LYS A 24 ? ? -13.51 4 1 ASN A 26 ? ? -13.28 5 1 ASN A 33 ? ? 11.31 6 1 VAL A 44 ? ? -14.36 7 1 ALA A 47 ? ? -11.27 8 1 PHE A 51 ? ? -16.73 9 1 TYR A 53 ? ? 13.91 10 1 PHE A 66 ? ? 15.02 11 1 ALA A 68 ? ? -11.90 12 1 ILE A 76 ? ? 11.00 13 1 LEU A 93 ? ? -13.34 14 1 GLU A 134 ? ? 17.58 15 1 VAL A 154 ? ? -11.99 16 1 GLY A 156 ? ? -11.02 17 1 SER A 170 ? ? 13.21 18 1 THR A 192 ? ? 11.64 19 1 VAL A 203 ? ? -10.53 20 1 PRO A 204 ? ? 12.64 21 1 PRO A 207 ? ? 15.03 22 1 SER A 216 ? ? -13.86 23 1 ILE A 241 ? ? 10.03 24 1 GLY A 245 ? ? -12.23 25 1 PRO A 253 ? ? -13.62 26 1 ASP A 254 ? ? -12.70 27 1 SER B 17 ? ? -18.62 28 1 ILE B 34 ? ? 14.38 29 1 CYS B 41 ? ? -10.81 30 1 ASN B 94 ? ? -18.76 31 1 ILE B 100 ? ? -10.40 32 1 ASN B 101 ? ? -10.40 33 1 LEU B 124 ? ? -12.16 34 1 ASP B 137 ? ? 11.50 35 1 ASP B 158 ? ? 10.93 36 1 PHE B 169 ? ? 12.34 37 1 ARG B 175 ? ? 10.40 38 1 THR B 197 ? ? 10.35 39 1 ASP B 201 ? ? -12.73 40 1 VAL B 203 ? ? -13.74 41 1 PRO B 218 ? ? 13.80 42 1 PRO B 229 ? ? -16.22 43 1 ASP B 234 ? ? 10.67 44 1 LYS B 237 ? ? 12.57 45 1 ILE B 238 ? ? -10.43 46 1 GLU B 239 ? ? 10.14 47 1 ILE B 241 ? ? 14.42 48 1 THR B 244 ? ? 10.07 49 1 ILE B 255 ? ? -10.38 50 1 CYS B 268 ? ? 12.68 # _pdbx_entity_nonpoly.entity_id 2 _pdbx_entity_nonpoly.name water _pdbx_entity_nonpoly.comp_id HOH # If you find results from this site helpful for your research, please cite one of our papers:
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