data_5FN6 # _entry.id 5FN6 # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.279 _audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic # loop_ _database_2.database_id _database_2.database_code PDB 5FN6 PDBE EBI-65477 WWPDB D_1290065477 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.content_type _pdbx_database_related.details PDB 5FMV unspecified 'CRYSTAL STRUCTURE OF HUMAN CD45 EXTRACELLULAR REGION, DOMAINS D1-D4' PDB 5FN7 unspecified 'CRYSTAL STRUCTURE OF HUMAN CD45 EXTRACELLULAR REGION, DOMAINS D1-D2' PDB 5FN8 unspecified 'CRYSTAL STRUCTURE OF RAT CD45 EXTRACELLULAR REGION, DOMAINS D3-D4' # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 5FN6 _pdbx_database_status.deposit_site PDBE _pdbx_database_status.process_site PDBE _pdbx_database_status.SG_entry . _pdbx_database_status.recvd_initial_deposition_date 2015-11-10 _pdbx_database_status.pdb_format_compatible Y _pdbx_database_status.status_code_sf ? _pdbx_database_status.status_code_mr ? _pdbx_database_status.status_code_cs ? _pdbx_database_status.methods_development_category ? # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Chang, V.T.' 1 'Fernandes, R.A.' 2 'Ganzinger, K.A.' 3 'Lee, S.F.' 4 'Siebold, C.' 5 'McColl, J.' 6 'Jonsson, P.' 7 'Palayret, M.' 8 'Harlos, K.' 9 'Coles, C.H.' 10 'Jones, E.Y.' 11 'Lui, Y.' 12 'Huang, E.' 13 'Gilbert, R.J.C.' 14 'Klenerman, D.' 15 'Aricescu, A.R.' 16 'Davis, S.J.' 17 # _citation.id primary _citation.title ;Initiation of T Cell Signaling by Cd45 Segregation at 'Close Contacts'. ; _citation.journal_abbrev Nat.Immunol. _citation.journal_volume 17 _citation.page_first 574 _citation.page_last ? _citation.year 2016 _citation.journal_id_ASTM ? _citation.country UK _citation.journal_id_ISSN 1529-2908 _citation.journal_id_CSD ? _citation.book_publisher ? _citation.pdbx_database_id_PubMed 26998761 _citation.pdbx_database_id_DOI 10.1038/NI.3392 # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Chang, V.T.' 1 primary 'Fernandes, R.A.' 2 primary 'Ganzinger, K.A.' 3 primary 'Lee, S.F.' 4 primary 'Siebold, C.' 5 primary 'Mccoll, J.' 6 primary 'Jonsson, P.' 7 primary 'Palayret, M.' 8 primary 'Harlos, K.' 9 primary 'Coles, C.H.' 10 primary 'Jones, E.Y.' 11 primary 'Lui, Y.' 12 primary 'Huang, E.' 13 primary 'Gilbert, R.J.' 14 primary 'Klenerman, D.' 15 primary 'Aricescu, A.R.' 16 primary 'Davis, S.J.' 17 # _cell.entry_id 5FN6 _cell.length_a 132.384 _cell.length_b 132.384 _cell.length_c 58.099 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 120.00 _cell.Z_PDB 9 _cell.pdbx_unique_axis ? # _symmetry.entry_id 5FN6 _symmetry.space_group_name_H-M 'H 3' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 146 # loop_ _entity.id _entity.type _entity.src_method _entity.pdbx_description _entity.formula_weight _entity.pdbx_number_of_molecules _entity.pdbx_ec _entity.pdbx_mutation _entity.pdbx_fragment _entity.details 1 polymer man 'RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE C' 30969.953 1 3.1.3.48 ? 'DOMAINS D1-D3, RESIDUES 223-479' ? 2 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 5 ? ? ? ? # _entity_name_com.entity_id 1 _entity_name_com.name 'LEUKOCYTE COMMON ANTIGEN, L-CA, T200, CD45' # _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 ;ETGKPTCDEKYANITVDYLYNKETKLFTAKLNVNENVECGNNTCTNNEVHNLTECKNASVSISHNSCTAPDKTLILDVPP GVEKFQLHDCTQVEKADTTICLKWKNIETFTCDTQNITYRFQCGNMIFDNKEIKLENLEPEHEYKCDSEILYNNHKFTNA SKIIKTDFGSPGEPQIIFCRSEAAHQGVITWNPPQRSFHNFTLCYIKETEKDCLNLDKNLIKYDLQNLKPYTKYVLSLHA YIIAKVQRNGSAAMCHFTTKGTKHHHHHH ; _entity_poly.pdbx_seq_one_letter_code_can ;ETGKPTCDEKYANITVDYLYNKETKLFTAKLNVNENVECGNNTCTNNEVHNLTECKNASVSISHNSCTAPDKTLILDVPP GVEKFQLHDCTQVEKADTTICLKWKNIETFTCDTQNITYRFQCGNMIFDNKEIKLENLEPEHEYKCDSEILYNNHKFTNA SKIIKTDFGSPGEPQIIFCRSEAAHQGVITWNPPQRSFHNFTLCYIKETEKDCLNLDKNLIKYDLQNLKPYTKYVLSLHA YIIAKVQRNGSAAMCHFTTKGTKHHHHHH ; _entity_poly.pdbx_strand_id A _entity_poly.pdbx_target_identifier ? # loop_ _entity_poly_seq.entity_id _entity_poly_seq.num _entity_poly_seq.mon_id _entity_poly_seq.hetero 1 1 GLU n 1 2 THR n 1 3 GLY n 1 4 LYS n 1 5 PRO n 1 6 THR n 1 7 CYS n 1 8 ASP n 1 9 GLU n 1 10 LYS n 1 11 TYR n 1 12 ALA n 1 13 ASN n 1 14 ILE n 1 15 THR n 1 16 VAL n 1 17 ASP n 1 18 TYR n 1 19 LEU n 1 20 TYR n 1 21 ASN n 1 22 LYS n 1 23 GLU n 1 24 THR n 1 25 LYS n 1 26 LEU n 1 27 PHE n 1 28 THR n 1 29 ALA n 1 30 LYS n 1 31 LEU n 1 32 ASN n 1 33 VAL n 1 34 ASN n 1 35 GLU n 1 36 ASN n 1 37 VAL n 1 38 GLU n 1 39 CYS n 1 40 GLY n 1 41 ASN n 1 42 ASN n 1 43 THR n 1 44 CYS n 1 45 THR n 1 46 ASN n 1 47 ASN n 1 48 GLU n 1 49 VAL n 1 50 HIS n 1 51 ASN n 1 52 LEU n 1 53 THR n 1 54 GLU n 1 55 CYS n 1 56 LYS n 1 57 ASN n 1 58 ALA n 1 59 SER n 1 60 VAL n 1 61 SER n 1 62 ILE n 1 63 SER n 1 64 HIS n 1 65 ASN n 1 66 SER n 1 67 CYS n 1 68 THR n 1 69 ALA n 1 70 PRO n 1 71 ASP n 1 72 LYS n 1 73 THR n 1 74 LEU n 1 75 ILE n 1 76 LEU n 1 77 ASP n 1 78 VAL n 1 79 PRO n 1 80 PRO n 1 81 GLY n 1 82 VAL n 1 83 GLU n 1 84 LYS n 1 85 PHE n 1 86 GLN n 1 87 LEU n 1 88 HIS n 1 89 ASP n 1 90 CYS n 1 91 THR n 1 92 GLN n 1 93 VAL n 1 94 GLU n 1 95 LYS n 1 96 ALA n 1 97 ASP n 1 98 THR n 1 99 THR n 1 100 ILE n 1 101 CYS n 1 102 LEU n 1 103 LYS n 1 104 TRP n 1 105 LYS n 1 106 ASN n 1 107 ILE n 1 108 GLU n 1 109 THR n 1 110 PHE n 1 111 THR n 1 112 CYS n 1 113 ASP n 1 114 THR n 1 115 GLN n 1 116 ASN n 1 117 ILE n 1 118 THR n 1 119 TYR n 1 120 ARG n 1 121 PHE n 1 122 GLN n 1 123 CYS n 1 124 GLY n 1 125 ASN n 1 126 MET n 1 127 ILE n 1 128 PHE n 1 129 ASP n 1 130 ASN n 1 131 LYS n 1 132 GLU n 1 133 ILE n 1 134 LYS n 1 135 LEU n 1 136 GLU n 1 137 ASN n 1 138 LEU n 1 139 GLU n 1 140 PRO n 1 141 GLU n 1 142 HIS n 1 143 GLU n 1 144 TYR n 1 145 LYS n 1 146 CYS n 1 147 ASP n 1 148 SER n 1 149 GLU n 1 150 ILE n 1 151 LEU n 1 152 TYR n 1 153 ASN n 1 154 ASN n 1 155 HIS n 1 156 LYS n 1 157 PHE n 1 158 THR n 1 159 ASN n 1 160 ALA n 1 161 SER n 1 162 LYS n 1 163 ILE n 1 164 ILE n 1 165 LYS n 1 166 THR n 1 167 ASP n 1 168 PHE n 1 169 GLY n 1 170 SER n 1 171 PRO n 1 172 GLY n 1 173 GLU n 1 174 PRO n 1 175 GLN n 1 176 ILE n 1 177 ILE n 1 178 PHE n 1 179 CYS n 1 180 ARG n 1 181 SER n 1 182 GLU n 1 183 ALA n 1 184 ALA n 1 185 HIS n 1 186 GLN n 1 187 GLY n 1 188 VAL n 1 189 ILE n 1 190 THR n 1 191 TRP n 1 192 ASN n 1 193 PRO n 1 194 PRO n 1 195 GLN n 1 196 ARG n 1 197 SER n 1 198 PHE n 1 199 HIS n 1 200 ASN n 1 201 PHE n 1 202 THR n 1 203 LEU n 1 204 CYS n 1 205 TYR n 1 206 ILE n 1 207 LYS n 1 208 GLU n 1 209 THR n 1 210 GLU n 1 211 LYS n 1 212 ASP n 1 213 CYS n 1 214 LEU n 1 215 ASN n 1 216 LEU n 1 217 ASP n 1 218 LYS n 1 219 ASN n 1 220 LEU n 1 221 ILE n 1 222 LYS n 1 223 TYR n 1 224 ASP n 1 225 LEU n 1 226 GLN n 1 227 ASN n 1 228 LEU n 1 229 LYS n 1 230 PRO n 1 231 TYR n 1 232 THR n 1 233 LYS n 1 234 TYR n 1 235 VAL n 1 236 LEU n 1 237 SER n 1 238 LEU n 1 239 HIS n 1 240 ALA n 1 241 TYR n 1 242 ILE n 1 243 ILE n 1 244 ALA n 1 245 LYS n 1 246 VAL n 1 247 GLN n 1 248 ARG n 1 249 ASN n 1 250 GLY n 1 251 SER n 1 252 ALA n 1 253 ALA n 1 254 MET n 1 255 CYS n 1 256 HIS n 1 257 PHE n 1 258 THR n 1 259 THR n 1 260 LYS n 1 261 GLY n 1 262 THR n 1 263 LYS n 1 264 HIS n 1 265 HIS n 1 266 HIS n 1 267 HIS n 1 268 HIS n 1 269 HIS n # _entity_src_gen.entity_id 1 _entity_src_gen.pdbx_src_id 1 _entity_src_gen.pdbx_alt_source_flag sample _entity_src_gen.pdbx_seq_type ? _entity_src_gen.pdbx_beg_seq_num ? _entity_src_gen.pdbx_end_seq_num ? _entity_src_gen.gene_src_common_name HUMAN _entity_src_gen.gene_src_genus ? _entity_src_gen.pdbx_gene_src_gene ? _entity_src_gen.gene_src_species ? _entity_src_gen.gene_src_strain ? _entity_src_gen.gene_src_tissue ? _entity_src_gen.gene_src_tissue_fraction ? _entity_src_gen.gene_src_details ? _entity_src_gen.pdbx_gene_src_fragment ? _entity_src_gen.pdbx_gene_src_scientific_name 'HOMO SAPIENS' _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 9606 _entity_src_gen.pdbx_gene_src_variant ? _entity_src_gen.pdbx_gene_src_cell_line ? _entity_src_gen.pdbx_gene_src_atcc ? _entity_src_gen.pdbx_gene_src_organ ? _entity_src_gen.pdbx_gene_src_organelle ? _entity_src_gen.pdbx_gene_src_cell ? _entity_src_gen.pdbx_gene_src_cellular_location ? _entity_src_gen.host_org_common_name HUMAN _entity_src_gen.pdbx_host_org_scientific_name 'HOMO SAPIENS' _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 9606 _entity_src_gen.host_org_genus ? _entity_src_gen.pdbx_host_org_gene ? _entity_src_gen.pdbx_host_org_organ ? _entity_src_gen.host_org_species ? _entity_src_gen.pdbx_host_org_tissue ? _entity_src_gen.pdbx_host_org_tissue_fraction ? _entity_src_gen.pdbx_host_org_strain ? _entity_src_gen.pdbx_host_org_variant ? _entity_src_gen.pdbx_host_org_cell_line 'HEK 293T' _entity_src_gen.pdbx_host_org_atcc ? _entity_src_gen.pdbx_host_org_culture_collection ? _entity_src_gen.pdbx_host_org_cell ? _entity_src_gen.pdbx_host_org_organelle ? _entity_src_gen.pdbx_host_org_cellular_location ? _entity_src_gen.pdbx_host_org_vector_type PLASMID _entity_src_gen.pdbx_host_org_vector ? _entity_src_gen.host_org_details ? _entity_src_gen.expression_system_id ? _entity_src_gen.plasmid_name PHLSEC _entity_src_gen.plasmid_details ? _entity_src_gen.pdbx_description ? # _struct_ref.id 1 _struct_ref.db_name UNP _struct_ref.db_code PTPRC_HUMAN _struct_ref.entity_id 1 _struct_ref.pdbx_seq_one_letter_code ? _struct_ref.pdbx_align_begin ? _struct_ref.pdbx_db_accession P08575 _struct_ref.pdbx_db_isoform ? # _struct_ref_seq.align_id 1 _struct_ref_seq.ref_id 1 _struct_ref_seq.pdbx_PDB_id_code 5FN6 _struct_ref_seq.pdbx_strand_id A _struct_ref_seq.seq_align_beg 4 _struct_ref_seq.pdbx_seq_align_beg_ins_code ? _struct_ref_seq.seq_align_end 260 _struct_ref_seq.pdbx_seq_align_end_ins_code ? _struct_ref_seq.pdbx_db_accession P08575 _struct_ref_seq.db_align_beg 223 _struct_ref_seq.pdbx_db_align_beg_ins_code ? _struct_ref_seq.db_align_end 479 _struct_ref_seq.pdbx_db_align_end_ins_code ? _struct_ref_seq.pdbx_auth_seq_align_beg 8 _struct_ref_seq.pdbx_auth_seq_align_end 264 # loop_ _struct_ref_seq_dif.align_id _struct_ref_seq_dif.pdbx_pdb_id_code _struct_ref_seq_dif.mon_id _struct_ref_seq_dif.pdbx_pdb_strand_id _struct_ref_seq_dif.seq_num _struct_ref_seq_dif.pdbx_pdb_ins_code _struct_ref_seq_dif.pdbx_seq_db_name _struct_ref_seq_dif.pdbx_seq_db_accession_code _struct_ref_seq_dif.db_mon_id _struct_ref_seq_dif.pdbx_seq_db_seq_num _struct_ref_seq_dif.details _struct_ref_seq_dif.pdbx_auth_seq_num _struct_ref_seq_dif.pdbx_ordinal 1 5FN6 GLU A 1 ? UNP P08575 ? ? 'expression tag' 5 1 1 5FN6 THR A 2 ? UNP P08575 ? ? 'expression tag' 6 2 1 5FN6 GLY A 3 ? UNP P08575 ? ? 'expression tag' 7 3 1 5FN6 GLY A 261 ? UNP P08575 ? ? 'expression tag' 265 4 1 5FN6 THR A 262 ? UNP P08575 ? ? 'expression tag' 266 5 1 5FN6 LYS A 263 ? UNP P08575 ? ? 'expression tag' 267 6 1 5FN6 HIS A 264 ? UNP P08575 ? ? 'expression tag' 268 7 1 5FN6 HIS A 265 ? UNP P08575 ? ? 'expression tag' 269 8 1 5FN6 HIS A 266 ? UNP P08575 ? ? 'expression tag' 270 9 1 5FN6 HIS A 267 ? UNP P08575 ? ? 'expression tag' 271 10 1 5FN6 HIS A 268 ? UNP P08575 ? ? 'expression tag' 272 11 1 5FN6 HIS A 269 ? UNP P08575 ? ? 'expression tag' 273 12 # 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 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 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 NAG D-saccharide . N-ACETYL-D-GLUCOSAMINE ? 'C8 H15 N O6' 221.208 PHE 'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2' 165.189 PRO 'L-peptide linking' y PROLINE ? 'C5 H9 N O2' 115.130 SER 'L-peptide linking' y SERINE ? 'C3 H7 N O3' 105.093 THR 'L-peptide linking' y THREONINE ? 'C4 H9 N O3' 119.119 TRP 'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2' 204.225 TYR 'L-peptide linking' y TYROSINE ? 'C9 H11 N O3' 181.189 VAL 'L-peptide linking' y VALINE ? 'C5 H11 N O2' 117.146 # _exptl.entry_id 5FN6 _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 3.39 _exptl_crystal.density_percent_sol 64 _exptl_crystal.description NONE # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method ? _exptl_crystal_grow.temp ? _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH 6.5 _exptl_crystal_grow.pdbx_pH_range ? _exptl_crystal_grow.pdbx_details '30% PEG8K, 0.2M (NH4)2SO4, 0.1M NA CACODYLATE, PH=6.5' # _diffrn.id 1 _diffrn.ambient_temp 100 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector CCD _diffrn_detector.type 'ADSC CCD' _diffrn_detector.pdbx_collection_date 2008-04-26 _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 0.8726 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'ESRF BEAMLINE ID23-2' _diffrn_source.pdbx_synchrotron_site ESRF _diffrn_source.pdbx_synchrotron_beamline ID23-2 _diffrn_source.pdbx_wavelength 0.8726 _diffrn_source.pdbx_wavelength_list ? # _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 _reflns.entry_id 5FN6 _reflns.observed_criterion_sigma_I 2.0 _reflns.observed_criterion_sigma_F ? _reflns.d_resolution_low 50.00 _reflns.d_resolution_high 3.30 _reflns.number_obs 5693 _reflns.number_all ? _reflns.percent_possible_obs 100.0 _reflns.pdbx_Rmerge_I_obs 0.26 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI 6.80 _reflns.B_iso_Wilson_estimate 56.65 _reflns.pdbx_redundancy 4.5 # _reflns_shell.pdbx_diffrn_id 1 _reflns_shell.pdbx_ordinal 1 _reflns_shell.d_res_high 3.30 _reflns_shell.d_res_low 3.42 _reflns_shell.percent_possible_all 100.0 _reflns_shell.Rmerge_I_obs 0.90 _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs 2.00 _reflns_shell.pdbx_redundancy 4.5 # _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.entry_id 5FN6 _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.ls_number_reflns_obs 5687 _refine.ls_number_reflns_all ? _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F 0.0 _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 40.81 _refine.ls_d_res_high 3.30 _refine.ls_percent_reflns_obs 99.77 _refine.ls_R_factor_obs 0.2114 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.2089 _refine.ls_R_factor_R_free 0.2414 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 7.60 _refine.ls_number_reflns_R_free 432 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc 0.8779 _refine.correlation_coeff_Fo_to_Fc_free 0.8608 _refine.B_iso_mean 62.99 _refine.aniso_B[1][1] -3.6174 _refine.aniso_B[2][2] -3.6174 _refine.aniso_B[3][3] 7.2347 _refine.aniso_B[1][2] 0.0000 _refine.aniso_B[1][3] 0.0000 _refine.aniso_B[2][3] 0.0000 _refine.solvent_model_details ? _refine.solvent_model_param_ksol ? _refine.solvent_model_param_bsol ? _refine.pdbx_solvent_vdw_probe_radii ? _refine.pdbx_solvent_ion_probe_radii ? _refine.pdbx_solvent_shrinkage_radii ? _refine.pdbx_ls_cross_valid_method THROUGHOUT _refine.details 'IDEAL-DIST CONTACT TERM CONTACT SETUP. ALL ATOMS HAVE CCP4 ATOM TYPE FROM LIBRARY' _refine.pdbx_starting_model 'CD45 EXTRACELLULAR REGION D1-D2' _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_stereochemistry_target_values ? _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details RANDOM _refine.pdbx_overall_ESU_R ? _refine.pdbx_overall_ESU_R_Free ? _refine.overall_SU_ML ? _refine.pdbx_overall_phase_error ? _refine.overall_SU_B ? _refine.overall_SU_R_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI 0.459 # _refine_analyze.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_analyze.entry_id 5FN6 _refine_analyze.Luzzati_coordinate_error_obs 0.645 _refine_analyze.Luzzati_sigma_a_obs ? _refine_analyze.Luzzati_d_res_low_obs ? _refine_analyze.Luzzati_coordinate_error_free ? _refine_analyze.Luzzati_sigma_a_free ? _refine_analyze.Luzzati_d_res_low_free ? _refine_analyze.number_disordered_residues ? _refine_analyze.occupancy_sum_hydrogen ? _refine_analyze.occupancy_sum_non_hydrogen ? # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 2030 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 70 _refine_hist.number_atoms_solvent 0 _refine_hist.number_atoms_total 2100 _refine_hist.d_res_high 3.30 _refine_hist.d_res_low 40.81 # 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 t_bond_d 0.009 ? 2.00 2156 'X-RAY DIFFRACTION' HARMONIC t_angle_deg 1.31 ? 2.00 2934 'X-RAY DIFFRACTION' HARMONIC t_dihedral_angle_d ? ? 2.00 774 'X-RAY DIFFRACTION' SINUSOIDAL t_incorr_chiral_ct ? ? ? ? 'X-RAY DIFFRACTION' ? t_pseud_angle ? ? ? ? 'X-RAY DIFFRACTION' ? t_trig_c_planes ? ? 2.00 65 'X-RAY DIFFRACTION' HARMONIC t_gen_planes ? ? 5.00 302 'X-RAY DIFFRACTION' HARMONIC t_it ? ? 20.00 2156 'X-RAY DIFFRACTION' HARMONIC t_nbd ? ? ? ? 'X-RAY DIFFRACTION' ? t_omega_torsion 3.06 ? ? ? 'X-RAY DIFFRACTION' ? t_other_torsion 20.12 ? ? ? 'X-RAY DIFFRACTION' ? t_improper_torsion ? ? ? ? 'X-RAY DIFFRACTION' ? t_chiral_improper_torsion ? ? 5.00 311 'X-RAY DIFFRACTION' SEMIHARMONIC t_sum_occupancies ? ? ? ? 'X-RAY DIFFRACTION' ? t_utility_distance ? ? ? ? 'X-RAY DIFFRACTION' ? t_utility_angle ? ? ? ? 'X-RAY DIFFRACTION' ? t_utility_torsion ? ? ? ? 'X-RAY DIFFRACTION' ? t_ideal_dist_contact ? ? 4.00 2253 'X-RAY DIFFRACTION' SEMIHARMONIC # _refine_ls_shell.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_ls_shell.pdbx_total_number_of_bins_used 5 _refine_ls_shell.d_res_high 3.30 _refine_ls_shell.d_res_low 3.69 _refine_ls_shell.number_reflns_R_work 1466 _refine_ls_shell.R_factor_R_work 0.2308 _refine_ls_shell.percent_reflns_obs 99.77 _refine_ls_shell.R_factor_R_free 0.2900 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free 8.20 _refine_ls_shell.number_reflns_R_free 131 _refine_ls_shell.number_reflns_all 1597 _refine_ls_shell.R_factor_all 0.2353 # _struct.entry_id 5FN6 _struct.title 'Crystal structure of human CD45 extracellular region, domains d1-d3' _struct.pdbx_descriptor 'RECEPTOR-TYPE TYROSINE-PROTEIN PHOSPHATASE C (E.C.3.1.3.48)' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 5FN6 _struct_keywords.pdbx_keywords HYDROLASE _struct_keywords.text 'HYDROLASE, RECEPTOR PROTEIN TYROSINE PHOSPHATASE, CD45, PTPRC' # loop_ _struct_asym.id _struct_asym.pdbx_blank_PDB_chainid_flag _struct_asym.pdbx_modified _struct_asym.entity_id _struct_asym.details A N N 1 ? B N N 2 ? C N N 2 ? D N N 2 ? E N N 2 ? F N N 2 ? # _struct_biol.id 1 # loop_ _struct_conf.conf_type_id _struct_conf.id _struct_conf.pdbx_PDB_helix_id _struct_conf.beg_label_comp_id _struct_conf.beg_label_asym_id _struct_conf.beg_label_seq_id _struct_conf.pdbx_beg_PDB_ins_code _struct_conf.end_label_comp_id _struct_conf.end_label_asym_id _struct_conf.end_label_seq_id _struct_conf.pdbx_end_PDB_ins_code _struct_conf.beg_auth_comp_id _struct_conf.beg_auth_asym_id _struct_conf.beg_auth_seq_id _struct_conf.end_auth_comp_id _struct_conf.end_auth_asym_id _struct_conf.end_auth_seq_id _struct_conf.pdbx_PDB_helix_class _struct_conf.details _struct_conf.pdbx_PDB_helix_length HELX_P HELX_P1 1 THR A 6 ? TYR A 11 ? THR A 10 TYR A 15 1 ? 6 HELX_P HELX_P2 2 CYS A 44 ? ASN A 46 ? CYS A 48 ASN A 50 5 ? 3 HELX_P HELX_P3 3 GLY A 81 ? GLU A 83 ? GLY A 85 GLU A 87 5 ? 3 HELX_P HELX_P4 4 GLN A 92 ? ALA A 96 ? GLN A 96 ALA A 100 5 ? 5 HELX_P HELX_P5 5 ASP A 113 ? GLN A 115 ? ASP A 117 GLN A 119 5 ? 3 # _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 7 SG ? ? ? 1_555 A CYS 67 SG ? ? A CYS 11 A CYS 71 1_555 ? ? ? ? ? ? ? 2.047 ? disulf2 disulf ? ? A CYS 39 SG ? ? ? 1_555 A CYS 44 SG ? ? A CYS 43 A CYS 48 1_555 ? ? ? ? ? ? ? 2.026 ? disulf3 disulf ? ? A CYS 55 SG ? ? ? 1_555 A CYS 112 SG ? ? A CYS 59 A CYS 116 1_555 ? ? ? ? ? ? ? 2.036 ? disulf4 disulf ? ? A CYS 90 SG ? ? ? 1_555 A CYS 101 SG ? ? A CYS 94 A CYS 105 1_555 ? ? ? ? ? ? ? 2.050 ? disulf5 disulf ? ? A CYS 123 SG ? ? ? 1_555 A CYS 146 SG ? ? A CYS 127 A CYS 150 1_555 ? ? ? ? ? ? ? 2.040 ? disulf6 disulf ? ? A CYS 179 SG ? ? ? 1_555 A CYS 255 SG ? ? A CYS 183 A CYS 259 1_555 ? ? ? ? ? ? ? 2.023 ? disulf7 disulf ? ? A CYS 204 SG ? ? ? 1_555 A CYS 213 SG ? ? A CYS 208 A CYS 217 1_555 ? ? ? ? ? ? ? 2.058 ? covale1 covale ? ? A ASN 51 ND2 ? ? ? 1_555 D NAG . C1 ? ? A ASN 55 A NAG 1267 1_555 ? ? ? ? ? ? ? 1.434 ? covale2 covale ? ? A ASN 57 ND2 ? ? ? 1_555 E NAG . C1 ? ? A ASN 61 A NAG 1268 1_555 ? ? ? ? ? ? ? 1.440 ? covale3 covale ? ? A ASN 159 ND2 ? ? ? 1_555 C NAG . C1 ? ? A ASN 163 A NAG 1266 1_555 ? ? ? ? ? ? ? 1.444 ? covale4 covale ? ? A ASN 200 ND2 ? ? ? 1_555 B NAG . C1 ? ? A ASN 204 A NAG 1265 1_555 ? ? ? ? ? ? ? 1.429 ? covale5 covale ? ? A ASN 249 ND2 ? ? ? 1_555 F NAG . C1 ? ? A ASN 253 A NAG 1269 1_555 ? ? ? ? ? ? ? 1.431 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? # loop_ _struct_mon_prot_cis.pdbx_id _struct_mon_prot_cis.label_comp_id _struct_mon_prot_cis.label_seq_id _struct_mon_prot_cis.label_asym_id _struct_mon_prot_cis.label_alt_id _struct_mon_prot_cis.pdbx_PDB_ins_code _struct_mon_prot_cis.auth_comp_id _struct_mon_prot_cis.auth_seq_id _struct_mon_prot_cis.auth_asym_id _struct_mon_prot_cis.pdbx_label_comp_id_2 _struct_mon_prot_cis.pdbx_label_seq_id_2 _struct_mon_prot_cis.pdbx_label_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_ins_code_2 _struct_mon_prot_cis.pdbx_auth_comp_id_2 _struct_mon_prot_cis.pdbx_auth_seq_id_2 _struct_mon_prot_cis.pdbx_auth_asym_id_2 _struct_mon_prot_cis.pdbx_PDB_model_num _struct_mon_prot_cis.pdbx_omega_angle 1 ALA 69 A . ? ALA 73 A PRO 70 A ? PRO 74 A 1 1.67 2 GLY 172 A . ? GLY 176 A GLU 173 A ? GLU 177 A 1 2.03 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details AA ? 3 ? AB ? 3 ? AC ? 3 ? AD ? 4 ? AE ? 3 ? AF ? 2 ? AG ? 2 ? AH ? 2 ? AI ? 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 AA 1 2 ? anti-parallel AA 2 3 ? anti-parallel AB 1 2 ? anti-parallel AB 2 3 ? anti-parallel AC 1 2 ? anti-parallel AC 2 3 ? anti-parallel AD 1 2 ? anti-parallel AD 2 3 ? anti-parallel AD 3 4 ? anti-parallel AE 1 2 ? anti-parallel AE 2 3 ? anti-parallel AF 1 2 ? anti-parallel AG 1 2 ? anti-parallel AH 1 2 ? anti-parallel AI 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 AA 1 THR A 15 ? ASN A 21 ? THR A 19 ASN A 25 AA 2 LEU A 26 ? ASN A 32 ? LEU A 30 ASN A 36 AA 3 GLU A 48 ? LEU A 52 ? GLU A 52 LEU A 56 AB 1 GLU A 38 ? CYS A 39 ? GLU A 42 CYS A 43 AB 2 ASN A 57 ? SER A 63 ? ASN A 61 SER A 67 AB 3 LYS A 72 ? ASP A 77 ? LYS A 76 ASP A 81 AC 1 PHE A 85 ? ASP A 89 ? PHE A 89 ASP A 93 AC 2 ILE A 100 ? ASN A 106 ? ILE A 104 ASN A 110 AC 3 GLU A 132 ? LEU A 135 ? GLU A 136 LEU A 139 AD 1 ILE A 127 ? ASP A 129 ? ILE A 131 ASP A 133 AD 2 ILE A 117 ? GLN A 122 ? ILE A 121 GLN A 126 AD 3 GLU A 143 ? TYR A 152 ? GLU A 147 TYR A 156 AD 4 HIS A 155 ? LYS A 165 ? HIS A 159 LYS A 169 AE 1 GLN A 175 ? ALA A 183 ? GLN A 179 ALA A 187 AE 2 GLN A 186 ? ASN A 192 ? GLN A 190 ASN A 196 AE 3 LYS A 222 ? LEU A 225 ? LYS A 226 LEU A 229 AF 1 GLU A 210 ? CYS A 213 ? GLU A 214 CYS A 217 AF 2 ASN A 200 ? LYS A 207 ? ASN A 204 LYS A 211 AG 1 LEU A 216 ? ASP A 217 ? LEU A 220 ASP A 221 AG 2 ASN A 200 ? LYS A 207 ? ASN A 204 LYS A 211 AH 1 GLN A 247 ? ASN A 249 ? GLN A 251 ASN A 253 AH 2 LYS A 233 ? ILE A 243 ? LYS A 237 ILE A 247 AI 1 ALA A 253 ? THR A 258 ? ALA A 257 THR A 262 AI 2 LYS A 233 ? ILE A 243 ? LYS A 237 ILE A 247 # 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 AA 1 2 N ASN A 21 ? N ASN A 25 O LEU A 26 ? O LEU A 30 AA 2 3 N ALA A 29 ? N ALA A 33 O VAL A 49 ? O VAL A 53 AB 1 2 N GLU A 38 ? N GLU A 42 O SER A 63 ? O SER A 67 AB 2 3 N ILE A 62 ? N ILE A 66 O LYS A 72 ? O LYS A 76 AC 1 2 N HIS A 88 ? N HIS A 92 O LYS A 103 ? O LYS A 107 AC 2 3 N LEU A 102 ? N LEU A 106 O ILE A 133 ? O ILE A 137 AD 1 2 N PHE A 128 ? N PHE A 132 O PHE A 121 ? O PHE A 125 AD 2 3 N GLN A 122 ? N GLN A 126 O ASP A 147 ? O ASP A 151 AD 3 4 N TYR A 152 ? N TYR A 156 O HIS A 155 ? O HIS A 159 AE 1 2 N ALA A 183 ? N ALA A 187 O GLN A 186 ? O GLN A 190 AE 2 3 N ILE A 189 ? N ILE A 193 O TYR A 223 ? O TYR A 227 AF 1 2 N ASP A 212 ? N ASP A 216 O TYR A 205 ? O TYR A 209 AG 1 2 N LEU A 216 ? N LEU A 220 O PHE A 201 ? O PHE A 205 AH 1 2 N ARG A 248 ? N ARG A 252 O ILE A 242 ? O ILE A 246 AI 1 2 N PHE A 257 ? N PHE A 261 O TYR A 234 ? O TYR A 238 # loop_ _struct_site.id _struct_site.pdbx_evidence_code _struct_site.pdbx_auth_asym_id _struct_site.pdbx_auth_comp_id _struct_site.pdbx_auth_seq_id _struct_site.pdbx_auth_ins_code _struct_site.pdbx_num_residues _struct_site.details AC1 Software ? ? ? ? 3 'Binding site for Mono-Saccharide NAG A1267 bound to ASN A 55' AC2 Software ? ? ? ? 4 'Binding site for Mono-Saccharide NAG A1268 bound to ASN A 61' AC3 Software ? ? ? ? 2 'Binding site for Mono-Saccharide NAG A1266 bound to ASN A 163' AC4 Software ? ? ? ? 5 'Binding site for Mono-Saccharide NAG A1265 bound to ASN A 204' AC5 Software ? ? ? ? 6 'Binding site for Mono-Saccharide NAG A1269 bound to ASN A 253' # loop_ _struct_site_gen.id _struct_site_gen.site_id _struct_site_gen.pdbx_num_res _struct_site_gen.label_comp_id _struct_site_gen.label_asym_id _struct_site_gen.label_seq_id _struct_site_gen.pdbx_auth_ins_code _struct_site_gen.auth_comp_id _struct_site_gen.auth_asym_id _struct_site_gen.auth_seq_id _struct_site_gen.label_atom_id _struct_site_gen.label_alt_id _struct_site_gen.symmetry _struct_site_gen.details 1 AC1 3 LEU A 26 ? LEU A 30 . ? 1_555 ? 2 AC1 3 HIS A 50 ? HIS A 54 . ? 1_555 ? 3 AC1 3 ASN A 51 ? ASN A 55 . ? 1_555 ? 4 AC2 4 ASN A 57 ? ASN A 61 . ? 1_555 ? 5 AC2 4 ASP A 77 ? ASP A 81 . ? 1_555 ? 6 AC2 4 PHE A 168 ? PHE A 172 . ? 6_574 ? 7 AC2 4 HIS A 199 ? HIS A 203 . ? 6_574 ? 8 AC3 2 LYS A 156 ? LYS A 160 . ? 1_555 ? 9 AC3 2 ASN A 159 ? ASN A 163 . ? 1_555 ? 10 AC4 5 HIS A 199 ? HIS A 203 . ? 1_555 ? 11 AC4 5 ASN A 200 ? ASN A 204 . ? 1_555 ? 12 AC4 5 ASN A 215 ? ASN A 219 . ? 1_555 ? 13 AC4 5 ILE A 243 ? ILE A 247 . ? 1_555 ? 14 AC4 5 MET A 254 ? MET A 258 . ? 5_765 ? 15 AC5 6 THR A 202 ? THR A 206 . ? 1_555 ? 16 AC5 6 GLN A 226 ? GLN A 230 . ? 9_674 ? 17 AC5 6 ASN A 227 ? ASN A 231 . ? 9_674 ? 18 AC5 6 HIS A 239 ? HIS A 243 . ? 1_555 ? 19 AC5 6 GLN A 247 ? GLN A 251 . ? 1_555 ? 20 AC5 6 ASN A 249 ? ASN A 253 . ? 1_555 ? # _database_PDB_matrix.entry_id 5FN6 _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 5FN6 _atom_sites.fract_transf_matrix[1][1] 0.007554 _atom_sites.fract_transf_matrix[1][2] 0.004361 _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] 0.008722 _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] 0.017212 _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 . THR A 1 6 ? 15.222 143.410 -35.235 1.00 100.51 ? 10 THR A N 1 ATOM 2 C CA . THR A 1 6 ? 15.188 142.282 -34.311 1.00 99.44 ? 10 THR A CA 1 ATOM 3 C C . THR A 1 6 ? 16.093 142.656 -33.139 1.00 101.57 ? 10 THR A C 1 ATOM 4 O O . THR A 1 6 ? 16.989 143.483 -33.318 1.00 100.10 ? 10 THR A O 1 ATOM 5 C CB . THR A 1 6 ? 15.625 140.963 -35.001 1.00 105.61 ? 10 THR A CB 1 ATOM 6 O OG1 . THR A 1 6 ? 17.047 140.891 -35.091 1.00 103.88 ? 10 THR A OG1 1 ATOM 7 C CG2 . THR A 1 6 ? 14.996 140.764 -36.375 1.00 105.76 ? 10 THR A CG2 1 ATOM 8 N N . CYS A 1 7 ? 15.857 142.088 -31.942 1.00 97.68 ? 11 CYS A N 1 ATOM 9 C CA . CYS A 1 7 ? 16.706 142.393 -30.788 1.00 95.05 ? 11 CYS A CA 1 ATOM 10 C C . CYS A 1 7 ? 18.118 141.868 -31.009 1.00 95.41 ? 11 CYS A C 1 ATOM 11 O O . CYS A 1 7 ? 19.087 142.535 -30.630 1.00 93.42 ? 11 CYS A O 1 ATOM 12 C CB . CYS A 1 7 ? 16.092 141.899 -29.483 1.00 95.73 ? 11 CYS A CB 1 ATOM 13 S SG . CYS A 1 7 ? 14.514 142.697 -29.063 1.00 103.10 ? 11 CYS A SG 1 ATOM 14 N N . ASP A 1 8 ? 18.231 140.745 -31.746 1.00 91.27 ? 12 ASP A N 1 ATOM 15 C CA . ASP A 1 8 ? 19.511 140.171 -32.151 1.00 88.94 ? 12 ASP A CA 1 ATOM 16 C C . ASP A 1 8 ? 20.245 141.169 -33.052 1.00 92.12 ? 12 ASP A C 1 ATOM 17 O O . ASP A 1 8 ? 21.467 141.237 -33.006 1.00 90.64 ? 12 ASP A O 1 ATOM 18 C CB . ASP A 1 8 ? 19.301 138.840 -32.894 1.00 91.54 ? 12 ASP A CB 1 ATOM 19 C CG . ASP A 1 8 ? 20.584 138.115 -33.265 1.00 101.90 ? 12 ASP A CG 1 ATOM 20 O OD1 . ASP A 1 8 ? 21.604 138.294 -32.549 1.00 101.20 ? 12 ASP A OD1 1 ATOM 21 O OD2 . ASP A 1 8 ? 20.567 137.351 -34.254 1.00 108.35 ? 12 ASP A OD2 1 ATOM 22 N N . GLU A 1 9 ? 19.494 141.953 -33.847 1.00 88.93 ? 13 GLU A N 1 ATOM 23 C CA . GLU A 1 9 ? 20.034 142.979 -34.736 1.00 87.96 ? 13 GLU A CA 1 ATOM 24 C C . GLU A 1 9 ? 20.433 144.214 -33.912 1.00 88.10 ? 13 GLU A C 1 ATOM 25 O O . GLU A 1 9 ? 21.581 144.649 -34.009 1.00 85.77 ? 13 GLU A O 1 ATOM 26 C CB . GLU A 1 9 ? 18.992 143.322 -35.823 1.00 92.34 ? 13 GLU A CB 1 ATOM 27 C CG . GLU A 1 9 ? 19.442 144.206 -36.975 1.00 105.41 ? 13 GLU A CG 1 ATOM 28 C CD . GLU A 1 9 ? 18.416 144.330 -38.091 1.00 132.20 ? 13 GLU A CD 1 ATOM 29 O OE1 . GLU A 1 9 ? 17.872 143.286 -38.522 1.00 127.62 ? 13 GLU A OE1 1 ATOM 30 O OE2 . GLU A 1 9 ? 18.141 145.474 -38.522 1.00 127.92 ? 13 GLU A OE2 1 ATOM 31 N N . LYS A 1 10 ? 19.500 144.760 -33.095 1.00 84.12 ? 14 LYS A N 1 ATOM 32 C CA . LYS A 1 10 ? 19.731 145.947 -32.264 1.00 82.74 ? 14 LYS A CA 1 ATOM 33 C C . LYS A 1 10 ? 20.878 145.786 -31.250 1.00 85.13 ? 14 LYS A C 1 ATOM 34 O O . LYS A 1 10 ? 21.613 146.754 -31.021 1.00 84.34 ? 14 LYS A O 1 ATOM 35 C CB . LYS A 1 10 ? 18.436 146.407 -31.562 1.00 86.02 ? 14 LYS A CB 1 ATOM 36 C CG . LYS A 1 10 ? 18.534 147.819 -30.980 1.00 91.11 ? 14 LYS A CG 1 ATOM 37 C CD . LYS A 1 10 ? 17.287 148.271 -30.260 1.00 98.06 ? 14 LYS A CD 1 ATOM 38 C CE . LYS A 1 10 ? 17.427 149.707 -29.824 1.00 104.25 ? 14 LYS A CE 1 ATOM 39 N NZ . LYS A 1 10 ? 16.221 150.186 -29.107 1.00 113.42 ? 14 LYS A NZ 1 ATOM 40 N N . TYR A 1 11 ? 21.039 144.577 -30.653 1.00 80.61 ? 15 TYR A N 1 ATOM 41 C CA . TYR A 1 11 ? 22.074 144.320 -29.638 1.00 78.14 ? 15 TYR A CA 1 ATOM 42 C C . TYR A 1 11 ? 23.190 143.348 -30.046 1.00 79.61 ? 15 TYR A C 1 ATOM 43 O O . TYR A 1 11 ? 23.874 142.843 -29.161 1.00 78.12 ? 15 TYR A O 1 ATOM 44 C CB . TYR A 1 11 ? 21.442 143.882 -28.293 1.00 79.21 ? 15 TYR A CB 1 ATOM 45 C CG . TYR A 1 11 ? 20.375 144.822 -27.786 1.00 82.78 ? 15 TYR A CG 1 ATOM 46 C CD1 . TYR A 1 11 ? 20.700 146.101 -27.338 1.00 84.68 ? 15 TYR A CD1 1 ATOM 47 C CD2 . TYR A 1 11 ? 19.041 144.433 -27.741 1.00 85.60 ? 15 TYR A CD2 1 ATOM 48 C CE1 . TYR A 1 11 ? 19.721 146.976 -26.874 1.00 87.23 ? 15 TYR A CE1 1 ATOM 49 C CE2 . TYR A 1 11 ? 18.052 145.298 -27.275 1.00 88.43 ? 15 TYR A CE2 1 ATOM 50 C CZ . TYR A 1 11 ? 18.398 146.570 -26.844 1.00 95.31 ? 15 TYR A CZ 1 ATOM 51 O OH . TYR A 1 11 ? 17.433 147.436 -26.397 1.00 98.15 ? 15 TYR A OH 1 ATOM 52 N N . ALA A 1 12 ? 23.411 143.115 -31.350 1.00 75.38 ? 16 ALA A N 1 ATOM 53 C CA . ALA A 1 12 ? 24.456 142.211 -31.842 1.00 73.79 ? 16 ALA A CA 1 ATOM 54 C C . ALA A 1 12 ? 25.875 142.560 -31.346 1.00 75.03 ? 16 ALA A C 1 ATOM 55 O O . ALA A 1 12 ? 26.656 141.641 -31.088 1.00 73.61 ? 16 ALA A O 1 ATOM 56 C CB . ALA A 1 12 ? 24.427 142.149 -33.360 1.00 75.97 ? 16 ALA A CB 1 ATOM 57 N N . ASN A 1 13 ? 26.193 143.868 -31.185 1.00 70.69 ? 17 ASN A N 1 ATOM 58 C CA . ASN A 1 13 ? 27.521 144.302 -30.728 1.00 68.89 ? 17 ASN A CA 1 ATOM 59 C C . ASN A 1 13 ? 27.581 144.911 -29.292 1.00 72.52 ? 17 ASN A C 1 ATOM 60 O O . ASN A 1 13 ? 28.574 145.563 -28.936 1.00 71.53 ? 17 ASN A O 1 ATOM 61 C CB . ASN A 1 13 ? 28.242 145.191 -31.761 1.00 67.46 ? 17 ASN A CB 1 ATOM 62 C CG . ASN A 1 13 ? 28.056 144.861 -33.219 1.00 83.88 ? 17 ASN A CG 1 ATOM 63 O OD1 . ASN A 1 13 ? 26.971 145.037 -33.746 1.00 76.92 ? 17 ASN A OD1 1 ATOM 64 N ND2 . ASN A 1 13 ? 29.139 144.575 -33.953 1.00 75.68 ? 17 ASN A ND2 1 ATOM 65 N N . ILE A 1 14 ? 26.545 144.655 -28.458 1.00 69.58 ? 18 ILE A N 1 ATOM 66 C CA . ILE A 1 14 ? 26.446 145.110 -27.051 1.00 69.12 ? 18 ILE A CA 1 ATOM 67 C C . ILE A 1 14 ? 27.748 144.815 -26.248 1.00 71.53 ? 18 ILE A C 1 ATOM 68 O O . ILE A 1 14 ? 28.351 143.751 -26.434 1.00 70.81 ? 18 ILE A O 1 ATOM 69 C CB . ILE A 1 14 ? 25.177 144.486 -26.379 1.00 72.71 ? 18 ILE A CB 1 ATOM 70 C CG1 . ILE A 1 14 ? 24.827 145.134 -25.016 1.00 73.18 ? 18 ILE A CG1 1 ATOM 71 C CG2 . ILE A 1 14 ? 25.266 142.952 -26.284 1.00 72.78 ? 18 ILE A CG2 1 ATOM 72 C CD1 . ILE A 1 14 ? 23.484 144.611 -24.367 1.00 81.82 ? 18 ILE A CD1 1 ATOM 73 N N . THR A 1 15 ? 28.191 145.765 -25.400 1.00 66.75 ? 19 THR A N 1 ATOM 74 C CA . THR A 1 15 ? 29.383 145.574 -24.562 1.00 64.97 ? 19 THR A CA 1 ATOM 75 C C . THR A 1 15 ? 29.009 145.417 -23.082 1.00 65.78 ? 19 THR A C 1 ATOM 76 O O . THR A 1 15 ? 27.927 145.834 -22.672 1.00 65.11 ? 19 THR A O 1 ATOM 77 C CB . THR A 1 15 ? 30.436 146.660 -24.781 1.00 75.01 ? 19 THR A CB 1 ATOM 78 O OG1 . THR A 1 15 ? 29.946 147.907 -24.296 1.00 76.07 ? 19 THR A OG1 1 ATOM 79 C CG2 . THR A 1 15 ? 30.892 146.768 -26.237 1.00 73.69 ? 19 THR A CG2 1 ATOM 80 N N . VAL A 1 16 ? 29.930 144.846 -22.283 1.00 60.81 ? 20 VAL A N 1 ATOM 81 C CA . VAL A 1 16 ? 29.737 144.538 -20.864 1.00 60.07 ? 20 VAL A CA 1 ATOM 82 C C . VAL A 1 16 ? 30.917 145.022 -20.005 1.00 64.39 ? 20 VAL A C 1 ATOM 83 O O . VAL A 1 16 ? 32.054 144.959 -20.457 1.00 64.00 ? 20 VAL A O 1 ATOM 84 C CB . VAL A 1 16 ? 29.536 142.994 -20.751 1.00 62.76 ? 20 VAL A CB 1 ATOM 85 C CG1 . VAL A 1 16 ? 29.767 142.466 -19.341 1.00 61.71 ? 20 VAL A CG1 1 ATOM 86 C CG2 . VAL A 1 16 ? 28.169 142.561 -21.282 1.00 63.09 ? 20 VAL A CG2 1 ATOM 87 N N . ASP A 1 17 ? 30.647 145.468 -18.759 1.00 61.52 ? 21 ASP A N 1 ATOM 88 C CA . ASP A 1 17 ? 31.680 145.797 -17.766 1.00 61.80 ? 21 ASP A CA 1 ATOM 89 C C . ASP A 1 17 ? 31.547 144.848 -16.578 1.00 63.67 ? 21 ASP A C 1 ATOM 90 O O . ASP A 1 17 ? 30.431 144.583 -16.141 1.00 62.70 ? 21 ASP A O 1 ATOM 91 C CB . ASP A 1 17 ? 31.625 147.262 -17.317 1.00 65.60 ? 21 ASP A CB 1 ATOM 92 C CG . ASP A 1 17 ? 32.081 148.245 -18.391 1.00 82.70 ? 21 ASP A CG 1 ATOM 93 O OD1 . ASP A 1 17 ? 33.053 147.929 -19.118 1.00 83.54 ? 21 ASP A OD1 1 ATOM 94 O OD2 . ASP A 1 17 ? 31.471 149.333 -18.499 1.00 92.31 ? 21 ASP A OD2 1 ATOM 95 N N . TYR A 1 18 ? 32.671 144.291 -16.097 1.00 59.69 ? 22 TYR A N 1 ATOM 96 C CA . TYR A 1 18 ? 32.685 143.325 -14.989 1.00 58.79 ? 22 TYR A CA 1 ATOM 97 C C . TYR A 1 18 ? 33.049 143.947 -13.658 1.00 62.34 ? 22 TYR A C 1 ATOM 98 O O . TYR A 1 18 ? 34.091 144.581 -13.554 1.00 62.37 ? 22 TYR A O 1 ATOM 99 C CB . TYR A 1 18 ? 33.596 142.133 -15.310 1.00 59.24 ? 22 TYR A CB 1 ATOM 100 C CG . TYR A 1 18 ? 33.005 141.243 -16.377 1.00 60.03 ? 22 TYR A CG 1 ATOM 101 C CD1 . TYR A 1 18 ? 31.929 140.407 -16.095 1.00 61.47 ? 22 TYR A CD1 1 ATOM 102 C CD2 . TYR A 1 18 ? 33.477 141.282 -17.685 1.00 60.71 ? 22 TYR A CD2 1 ATOM 103 C CE1 . TYR A 1 18 ? 31.349 139.618 -17.085 1.00 62.39 ? 22 TYR A CE1 1 ATOM 104 C CE2 . TYR A 1 18 ? 32.920 140.480 -18.679 1.00 60.90 ? 22 TYR A CE2 1 ATOM 105 C CZ . TYR A 1 18 ? 31.849 139.656 -18.377 1.00 66.99 ? 22 TYR A CZ 1 ATOM 106 O OH . TYR A 1 18 ? 31.282 138.870 -19.353 1.00 65.36 ? 22 TYR A OH 1 ATOM 107 N N . LEU A 1 19 ? 32.175 143.785 -12.651 1.00 58.21 ? 23 LEU A N 1 ATOM 108 C CA . LEU A 1 19 ? 32.359 144.332 -11.304 1.00 58.38 ? 23 LEU A CA 1 ATOM 109 C C . LEU A 1 19 ? 32.395 143.180 -10.286 1.00 60.20 ? 23 LEU A C 1 ATOM 110 O O . LEU A 1 19 ? 31.406 142.461 -10.133 1.00 59.67 ? 23 LEU A O 1 ATOM 111 C CB . LEU A 1 19 ? 31.234 145.340 -10.975 1.00 59.56 ? 23 LEU A CB 1 ATOM 112 C CG . LEU A 1 19 ? 31.073 146.566 -11.922 1.00 65.56 ? 23 LEU A CG 1 ATOM 113 C CD1 . LEU A 1 19 ? 29.987 146.326 -13.008 1.00 65.53 ? 23 LEU A CD1 1 ATOM 114 C CD2 . LEU A 1 19 ? 30.754 147.834 -11.119 1.00 69.36 ? 23 LEU A CD2 1 ATOM 115 N N . TYR A 1 20 ? 33.545 142.974 -9.632 1.00 55.99 ? 24 TYR A N 1 ATOM 116 C CA . TYR A 1 20 ? 33.737 141.889 -8.661 1.00 55.66 ? 24 TYR A CA 1 ATOM 117 C C . TYR A 1 20 ? 33.248 142.218 -7.267 1.00 61.64 ? 24 TYR A C 1 ATOM 118 O O . TYR A 1 20 ? 33.490 143.321 -6.772 1.00 62.64 ? 24 TYR A O 1 ATOM 119 C CB . TYR A 1 20 ? 35.220 141.510 -8.558 1.00 57.00 ? 24 TYR A CB 1 ATOM 120 C CG . TYR A 1 20 ? 35.502 140.142 -7.960 1.00 57.75 ? 24 TYR A CG 1 ATOM 121 C CD1 . TYR A 1 20 ? 35.139 138.979 -8.628 1.00 58.05 ? 24 TYR A CD1 1 ATOM 122 C CD2 . TYR A 1 20 ? 36.213 140.011 -6.771 1.00 59.43 ? 24 TYR A CD2 1 ATOM 123 C CE1 . TYR A 1 20 ? 35.479 137.722 -8.135 1.00 58.07 ? 24 TYR A CE1 1 ATOM 124 C CE2 . TYR A 1 20 ? 36.550 138.755 -6.263 1.00 59.85 ? 24 TYR A CE2 1 ATOM 125 C CZ . TYR A 1 20 ? 36.171 137.614 -6.946 1.00 65.80 ? 24 TYR A CZ 1 ATOM 126 O OH . TYR A 1 20 ? 36.486 136.372 -6.466 1.00 67.18 ? 24 TYR A OH 1 ATOM 127 N N . ASN A 1 21 ? 32.609 141.237 -6.612 1.00 57.96 ? 25 ASN A N 1 ATOM 128 C CA . ASN A 1 21 ? 32.200 141.339 -5.217 1.00 58.10 ? 25 ASN A CA 1 ATOM 129 C C . ASN A 1 21 ? 33.154 140.420 -4.446 1.00 60.97 ? 25 ASN A C 1 ATOM 130 O O . ASN A 1 21 ? 33.116 139.198 -4.617 1.00 58.73 ? 25 ASN A O 1 ATOM 131 C CB . ASN A 1 21 ? 30.738 140.931 -5.009 1.00 57.20 ? 25 ASN A CB 1 ATOM 132 C CG . ASN A 1 21 ? 30.242 141.085 -3.574 1.00 74.80 ? 25 ASN A CG 1 ATOM 133 O OD1 . ASN A 1 21 ? 30.976 140.937 -2.588 1.00 59.89 ? 25 ASN A OD1 1 ATOM 134 N ND2 . ASN A 1 21 ? 28.966 141.384 -3.424 1.00 70.11 ? 25 ASN A ND2 1 ATOM 135 N N . LYS A 1 22 ? 34.030 141.016 -3.629 1.00 59.02 ? 26 LYS A N 1 ATOM 136 C CA . LYS A 1 22 ? 35.045 140.307 -2.840 1.00 59.37 ? 26 LYS A CA 1 ATOM 137 C C . LYS A 1 22 ? 34.436 139.355 -1.794 1.00 63.78 ? 26 LYS A C 1 ATOM 138 O O . LYS A 1 22 ? 35.027 138.305 -1.516 1.00 63.36 ? 26 LYS A O 1 ATOM 139 C CB . LYS A 1 22 ? 36.015 141.320 -2.187 1.00 63.27 ? 26 LYS A CB 1 ATOM 140 C CG . LYS A 1 22 ? 36.733 142.286 -3.161 1.00 72.93 ? 26 LYS A CG 1 ATOM 141 C CD . LYS A 1 22 ? 35.994 143.574 -3.646 1.00 77.94 ? 26 LYS A CD 1 ATOM 142 C CE . LYS A 1 22 ? 35.736 144.646 -2.613 1.00 80.84 ? 26 LYS A CE 1 ATOM 143 N NZ . LYS A 1 22 ? 34.349 144.556 -2.103 1.00 83.45 ? 26 LYS A NZ 1 ATOM 144 N N . GLU A 1 23 ? 33.252 139.720 -1.242 1.00 60.52 ? 27 GLU A N 1 ATOM 145 C CA . GLU A 1 23 ? 32.522 138.945 -0.233 1.00 60.08 ? 27 GLU A CA 1 ATOM 146 C C . GLU A 1 23 ? 31.922 137.679 -0.811 1.00 61.10 ? 27 GLU A C 1 ATOM 147 O O . GLU A 1 23 ? 32.003 136.630 -0.173 1.00 60.30 ? 27 GLU A O 1 ATOM 148 C CB . GLU A 1 23 ? 31.402 139.779 0.417 1.00 62.60 ? 27 GLU A CB 1 ATOM 149 C CG . GLU A 1 23 ? 31.881 140.945 1.260 1.00 77.57 ? 27 GLU A CG 1 ATOM 150 C CD . GLU A 1 23 ? 30.801 141.783 1.926 1.00 105.05 ? 27 GLU A CD 1 ATOM 151 O OE1 . GLU A 1 23 ? 29.618 141.370 1.916 1.00 103.91 ? 27 GLU A OE1 1 ATOM 152 O OE2 . GLU A 1 23 ? 31.141 142.869 2.450 1.00 100.68 ? 27 GLU A OE2 1 ATOM 153 N N . THR A 1 24 ? 31.284 137.780 -1.987 1.00 56.13 ? 28 THR A N 1 ATOM 154 C CA . THR A 1 24 ? 30.630 136.635 -2.617 1.00 54.64 ? 28 THR A CA 1 ATOM 155 C C . THR A 1 24 ? 31.570 135.848 -3.530 1.00 57.48 ? 28 THR A C 1 ATOM 156 O O . THR A 1 24 ? 31.276 134.687 -3.834 1.00 56.17 ? 28 THR A O 1 ATOM 157 C CB . THR A 1 24 ? 29.352 137.058 -3.378 1.00 62.46 ? 28 THR A CB 1 ATOM 158 O OG1 . THR A 1 24 ? 29.689 137.974 -4.415 1.00 66.28 ? 28 THR A OG1 1 ATOM 159 C CG2 . THR A 1 24 ? 28.292 137.649 -2.476 1.00 59.09 ? 28 THR A CG2 1 ATOM 160 N N . LYS A 1 25 ? 32.677 136.475 -3.989 1.00 53.77 ? 29 LYS A N 1 ATOM 161 C CA . LYS A 1 25 ? 33.635 135.895 -4.943 1.00 52.67 ? 29 LYS A CA 1 ATOM 162 C C . LYS A 1 25 ? 32.950 135.739 -6.318 1.00 55.93 ? 29 LYS A C 1 ATOM 163 O O . LYS A 1 25 ? 33.360 134.904 -7.123 1.00 55.50 ? 29 LYS A O 1 ATOM 164 C CB . LYS A 1 25 ? 34.271 134.561 -4.443 1.00 53.67 ? 29 LYS A CB 1 ATOM 165 C CG . LYS A 1 25 ? 35.373 134.697 -3.377 1.00 57.82 ? 29 LYS A CG 1 ATOM 166 C CD . LYS A 1 25 ? 36.129 133.356 -3.142 1.00 63.42 ? 29 LYS A CD 1 ATOM 167 C CE . LYS A 1 25 ? 37.377 133.444 -2.277 1.00 69.90 ? 29 LYS A CE 1 ATOM 168 N NZ . LYS A 1 25 ? 38.284 132.267 -2.481 1.00 70.72 ? 29 LYS A NZ 1 ATOM 169 N N . LEU A 1 26 ? 31.903 136.556 -6.573 1.00 51.85 ? 30 LEU A N 1 ATOM 170 C CA . LEU A 1 26 ? 31.123 136.555 -7.808 1.00 50.96 ? 30 LEU A CA 1 ATOM 171 C C . LEU A 1 26 ? 31.189 137.904 -8.531 1.00 54.98 ? 30 LEU A C 1 ATOM 172 O O . LEU A 1 26 ? 31.403 138.949 -7.906 1.00 55.60 ? 30 LEU A O 1 ATOM 173 C CB . LEU A 1 26 ? 29.656 136.153 -7.546 1.00 50.95 ? 30 LEU A CB 1 ATOM 174 C CG . LEU A 1 26 ? 29.412 134.759 -6.948 1.00 55.61 ? 30 LEU A CG 1 ATOM 175 C CD1 . LEU A 1 26 ? 28.030 134.673 -6.321 1.00 56.35 ? 30 LEU A CD1 1 ATOM 176 C CD2 . LEU A 1 26 ? 29.650 133.630 -7.977 1.00 58.37 ? 30 LEU A CD2 1 ATOM 177 N N . PHE A 1 27 ? 31.022 137.863 -9.862 1.00 49.69 ? 31 PHE A N 1 ATOM 178 C CA . PHE A 1 27 ? 31.040 139.039 -10.720 1.00 49.06 ? 31 PHE A CA 1 ATOM 179 C C . PHE A 1 27 ? 29.646 139.479 -11.070 1.00 53.96 ? 31 PHE A C 1 ATOM 180 O O . PHE A 1 27 ? 28.722 138.661 -11.121 1.00 53.87 ? 31 PHE A O 1 ATOM 181 C CB . PHE A 1 27 ? 31.775 138.733 -12.036 1.00 49.73 ? 31 PHE A CB 1 ATOM 182 C CG . PHE A 1 27 ? 33.275 138.852 -11.994 1.00 50.83 ? 31 PHE A CG 1 ATOM 183 C CD1 . PHE A 1 27 ? 33.895 140.090 -12.136 1.00 54.26 ? 31 PHE A CD1 1 ATOM 184 C CD2 . PHE A 1 27 ? 34.073 137.722 -11.854 1.00 51.56 ? 31 PHE A CD2 1 ATOM 185 C CE1 . PHE A 1 27 ? 35.284 140.199 -12.095 1.00 55.57 ? 31 PHE A CE1 1 ATOM 186 C CE2 . PHE A 1 27 ? 35.463 137.828 -11.838 1.00 54.66 ? 31 PHE A CE2 1 ATOM 187 C CZ . PHE A 1 27 ? 36.059 139.067 -11.947 1.00 54.03 ? 31 PHE A CZ 1 ATOM 188 N N . THR A 1 28 ? 29.508 140.783 -11.335 1.00 51.55 ? 32 THR A N 1 ATOM 189 C CA . THR A 1 28 ? 28.310 141.415 -11.865 1.00 52.56 ? 32 THR A CA 1 ATOM 190 C C . THR A 1 28 ? 28.702 141.908 -13.264 1.00 59.11 ? 32 THR A C 1 ATOM 191 O O . THR A 1 28 ? 29.748 142.538 -13.419 1.00 59.14 ? 32 THR A O 1 ATOM 192 C CB . THR A 1 28 ? 27.813 142.572 -10.976 1.00 57.44 ? 32 THR A CB 1 ATOM 193 O OG1 . THR A 1 28 ? 27.269 142.035 -9.768 1.00 51.51 ? 32 THR A OG1 1 ATOM 194 C CG2 . THR A 1 28 ? 26.741 143.437 -11.674 1.00 57.71 ? 32 THR A CG2 1 ATOM 195 N N . ALA A 1 29 ? 27.880 141.607 -14.274 1.00 56.98 ? 33 ALA A N 1 ATOM 196 C CA . ALA A 1 29 ? 28.109 142.076 -15.635 1.00 57.13 ? 33 ALA A CA 1 ATOM 197 C C . ALA A 1 29 ? 27.171 143.250 -15.860 1.00 63.00 ? 33 ALA A C 1 ATOM 198 O O . ALA A 1 29 ? 25.955 143.087 -15.764 1.00 62.19 ? 33 ALA A O 1 ATOM 199 C CB . ALA A 1 29 ? 27.803 140.971 -16.636 1.00 57.29 ? 33 ALA A CB 1 ATOM 200 N N . LYS A 1 30 ? 27.725 144.439 -16.103 1.00 61.94 ? 34 LYS A N 1 ATOM 201 C CA . LYS A 1 30 ? 26.912 145.617 -16.396 1.00 63.43 ? 34 LYS A CA 1 ATOM 202 C C . LYS A 1 30 ? 26.799 145.756 -17.922 1.00 68.37 ? 34 LYS A C 1 ATOM 203 O O . LYS A 1 30 ? 27.818 145.871 -18.605 1.00 67.28 ? 34 LYS A O 1 ATOM 204 C CB . LYS A 1 30 ? 27.487 146.901 -15.750 1.00 66.31 ? 34 LYS A CB 1 ATOM 205 C CG . LYS A 1 30 ? 26.703 148.164 -16.109 1.00 83.30 ? 34 LYS A CG 1 ATOM 206 C CD . LYS A 1 30 ? 26.099 148.843 -14.900 1.00 98.73 ? 34 LYS A CD 1 ATOM 207 C CE . LYS A 1 30 ? 24.980 149.785 -15.282 1.00 114.81 ? 34 LYS A CE 1 ATOM 208 N NZ . LYS A 1 30 ? 24.134 150.116 -14.107 1.00 125.12 ? 34 LYS A NZ 1 ATOM 209 N N . LEU A 1 31 ? 25.561 145.708 -18.446 1.00 66.69 ? 35 LEU A N 1 ATOM 210 C CA . LEU A 1 31 ? 25.256 145.832 -19.871 1.00 67.55 ? 35 LEU A CA 1 ATOM 211 C C . LEU A 1 31 ? 25.334 147.300 -20.273 1.00 75.03 ? 35 LEU A C 1 ATOM 212 O O . LEU A 1 31 ? 24.671 148.140 -19.665 1.00 75.86 ? 35 LEU A O 1 ATOM 213 C CB . LEU A 1 31 ? 23.864 145.241 -20.192 1.00 68.45 ? 35 LEU A CB 1 ATOM 214 C CG . LEU A 1 31 ? 23.547 143.865 -19.592 1.00 72.54 ? 35 LEU A CG 1 ATOM 215 C CD1 . LEU A 1 31 ? 22.086 143.515 -19.753 1.00 74.15 ? 35 LEU A CD1 1 ATOM 216 C CD2 . LEU A 1 31 ? 24.424 142.781 -20.192 1.00 73.84 ? 35 LEU A CD2 1 ATOM 217 N N . ASN A 1 32 ? 26.186 147.613 -21.263 1.00 73.69 ? 36 ASN A N 1 ATOM 218 C CA . ASN A 1 32 ? 26.374 148.985 -21.735 1.00 75.74 ? 36 ASN A CA 1 ATOM 219 C C . ASN A 1 32 ? 25.309 149.358 -22.766 1.00 83.80 ? 36 ASN A C 1 ATOM 220 O O . ASN A 1 32 ? 25.538 149.312 -23.981 1.00 83.69 ? 36 ASN A O 1 ATOM 221 C CB . ASN A 1 32 ? 27.808 149.236 -22.238 1.00 76.74 ? 36 ASN A CB 1 ATOM 222 C CG . ASN A 1 32 ? 28.904 148.866 -21.258 1.00 100.28 ? 36 ASN A CG 1 ATOM 223 O OD1 . ASN A 1 32 ? 29.885 148.204 -21.619 1.00 97.83 ? 36 ASN A OD1 1 ATOM 224 N ND2 . ASN A 1 32 ? 28.771 149.285 -19.995 1.00 88.74 ? 36 ASN A ND2 1 ATOM 225 N N . VAL A 1 33 ? 24.115 149.670 -22.248 1.00 83.16 ? 37 VAL A N 1 ATOM 226 C CA . VAL A 1 33 ? 22.925 150.087 -22.989 1.00 85.36 ? 37 VAL A CA 1 ATOM 227 C C . VAL A 1 33 ? 22.216 151.194 -22.208 1.00 92.11 ? 37 VAL A C 1 ATOM 228 O O . VAL A 1 33 ? 22.265 151.210 -20.972 1.00 91.73 ? 37 VAL A O 1 ATOM 229 C CB . VAL A 1 33 ? 21.950 148.920 -23.337 1.00 90.03 ? 37 VAL A CB 1 ATOM 230 C CG1 . VAL A 1 33 ? 22.454 148.102 -24.519 1.00 89.01 ? 37 VAL A CG1 1 ATOM 231 C CG2 . VAL A 1 33 ? 21.652 148.031 -22.125 1.00 89.46 ? 37 VAL A CG2 1 ATOM 232 N N . ASN A 1 34 ? 21.550 152.109 -22.924 1.00 91.00 ? 38 ASN A N 1 ATOM 233 C CA . ASN A 1 34 ? 20.811 153.210 -22.309 1.00 92.72 ? 38 ASN A CA 1 ATOM 234 C C . ASN A 1 34 ? 19.494 152.707 -21.693 1.00 98.18 ? 38 ASN A C 1 ATOM 235 O O . ASN A 1 34 ? 19.325 152.788 -20.473 1.00 97.79 ? 38 ASN A O 1 ATOM 236 C CB . ASN A 1 34 ? 20.573 154.341 -23.320 1.00 94.98 ? 38 ASN A CB 1 ATOM 237 C CG . ASN A 1 34 ? 21.830 154.819 -24.010 1.00 115.89 ? 38 ASN A CG 1 ATOM 238 O OD1 . ASN A 1 34 ? 22.047 154.560 -25.198 1.00 110.96 ? 38 ASN A OD1 1 ATOM 239 N ND2 . ASN A 1 34 ? 22.699 155.506 -23.276 1.00 105.58 ? 38 ASN A ND2 1 ATOM 240 N N . GLU A 1 35 ? 18.601 152.141 -22.535 1.00 96.14 ? 39 GLU A N 1 ATOM 241 C CA . GLU A 1 35 ? 17.288 151.610 -22.166 1.00 98.25 ? 39 GLU A CA 1 ATOM 242 C C . GLU A 1 35 ? 17.315 150.450 -21.161 1.00 102.07 ? 39 GLU A C 1 ATOM 243 O O . GLU A 1 35 ? 18.277 149.674 -21.135 1.00 99.34 ? 39 GLU A O 1 ATOM 244 C CB . GLU A 1 35 ? 16.477 151.229 -23.421 1.00 101.22 ? 39 GLU A CB 1 ATOM 245 C CG . GLU A 1 35 ? 17.106 150.149 -24.296 1.00 108.58 ? 39 GLU A CG 1 ATOM 246 C CD . GLU A 1 35 ? 18.011 150.623 -25.420 1.00 118.67 ? 39 GLU A CD 1 ATOM 247 O OE1 . GLU A 1 35 ? 18.947 151.412 -25.155 1.00 105.45 ? 39 GLU A OE1 1 ATOM 248 O OE2 . GLU A 1 35 ? 17.810 150.159 -26.566 1.00 107.56 ? 39 GLU A OE2 1 ATOM 249 N N . ASN A 1 36 ? 16.238 150.331 -20.349 1.00 101.21 ? 40 ASN A N 1 ATOM 250 C CA . ASN A 1 36 ? 16.096 149.248 -19.379 1.00 100.44 ? 40 ASN A CA 1 ATOM 251 C C . ASN A 1 36 ? 15.644 147.986 -20.100 1.00 104.41 ? 40 ASN A C 1 ATOM 252 O O . ASN A 1 36 ? 14.477 147.827 -20.460 1.00 106.40 ? 40 ASN A O 1 ATOM 253 C CB . ASN A 1 36 ? 15.264 149.638 -18.137 1.00 103.21 ? 40 ASN A CB 1 ATOM 254 C CG . ASN A 1 36 ? 16.122 149.771 -16.864 1.00 121.96 ? 40 ASN A CG 1 ATOM 255 O OD1 . ASN A 1 36 ? 15.921 149.061 -15.864 1.00 117.49 ? 40 ASN A OD1 1 ATOM 256 N ND2 . ASN A 1 36 ? 17.120 150.659 -16.856 1.00 108.96 ? 40 ASN A ND2 1 ATOM 257 N N . VAL A 1 37 ? 16.638 147.143 -20.386 1.00 98.53 ? 41 VAL A N 1 ATOM 258 C CA . VAL A 1 37 ? 16.530 145.897 -21.120 1.00 98.13 ? 41 VAL A CA 1 ATOM 259 C C . VAL A 1 37 ? 15.926 144.742 -20.294 1.00 103.16 ? 41 VAL A C 1 ATOM 260 O O . VAL A 1 37 ? 15.971 144.787 -19.069 1.00 102.82 ? 41 VAL A O 1 ATOM 261 C CB . VAL A 1 37 ? 17.926 145.617 -21.739 1.00 99.31 ? 41 VAL A CB 1 ATOM 262 C CG1 . VAL A 1 37 ? 18.592 144.361 -21.201 1.00 97.01 ? 41 VAL A CG1 1 ATOM 263 C CG2 . VAL A 1 37 ? 17.863 145.626 -23.252 1.00 99.72 ? 41 VAL A CG2 1 ATOM 264 N N . GLU A 1 38 ? 15.326 143.745 -20.962 1.00 100.47 ? 42 GLU A N 1 ATOM 265 C CA . GLU A 1 38 ? 14.725 142.592 -20.306 1.00 100.50 ? 42 GLU A CA 1 ATOM 266 C C . GLU A 1 38 ? 15.547 141.356 -20.620 1.00 102.16 ? 42 GLU A C 1 ATOM 267 O O . GLU A 1 38 ? 15.971 141.157 -21.763 1.00 100.58 ? 42 GLU A O 1 ATOM 268 C CB . GLU A 1 38 ? 13.280 142.378 -20.776 1.00 105.07 ? 42 GLU A CB 1 ATOM 269 C CG . GLU A 1 38 ? 12.297 143.383 -20.203 1.00 118.40 ? 42 GLU A CG 1 ATOM 270 C CD . GLU A 1 38 ? 11.043 143.722 -20.990 1.00 140.50 ? 42 GLU A CD 1 ATOM 271 O OE1 . GLU A 1 38 ? 10.704 142.981 -21.941 1.00 135.41 ? 42 GLU A OE1 1 ATOM 272 O OE2 . GLU A 1 38 ? 10.449 144.792 -20.711 1.00 134.22 ? 42 GLU A OE2 1 ATOM 273 N N . CYS A 1 39 ? 15.766 140.511 -19.610 1.00 98.42 ? 43 CYS A N 1 ATOM 274 C CA . CYS A 1 39 ? 16.500 139.259 -19.792 1.00 96.68 ? 43 CYS A CA 1 ATOM 275 C C . CYS A 1 39 ? 15.637 138.077 -19.450 1.00 100.79 ? 43 CYS A C 1 ATOM 276 O O . CYS A 1 39 ? 15.048 138.051 -18.371 1.00 100.92 ? 43 CYS A O 1 ATOM 277 C CB . CYS A 1 39 ? 17.787 139.240 -18.993 1.00 94.85 ? 43 CYS A CB 1 ATOM 278 S SG . CYS A 1 39 ? 18.897 140.629 -19.309 1.00 98.12 ? 43 CYS A SG 1 ATOM 279 N N . GLY A 1 40 ? 15.580 137.120 -20.367 1.00 97.14 ? 44 GLY A N 1 ATOM 280 C CA . GLY A 1 40 ? 14.779 135.908 -20.247 1.00 120.03 ? 44 GLY A CA 1 ATOM 281 C C . GLY A 1 40 ? 13.308 136.151 -19.942 1.00 122.22 ? 44 GLY A C 1 ATOM 282 O O . GLY A 1 40 ? 12.944 136.419 -18.790 1.00 71.63 ? 44 GLY A O 1 ATOM 283 N N . CYS A 1 44 ? 18.006 140.741 -15.085 1.00 93.83 ? 48 CYS A N 1 ATOM 284 C CA . CYS A 1 44 ? 19.027 141.765 -15.263 1.00 92.76 ? 48 CYS A CA 1 ATOM 285 C C . CYS A 1 44 ? 18.529 143.124 -14.777 1.00 96.83 ? 48 CYS A C 1 ATOM 286 O O . CYS A 1 44 ? 18.451 144.090 -15.558 1.00 97.49 ? 48 CYS A O 1 ATOM 287 C CB . CYS A 1 44 ? 19.555 141.865 -16.695 1.00 92.97 ? 48 CYS A CB 1 ATOM 288 S SG . CYS A 1 44 ? 19.841 140.318 -17.543 1.00 96.00 ? 48 CYS A SG 1 ATOM 289 N N . THR A 1 45 ? 18.204 143.189 -13.473 1.00 92.12 ? 49 THR A N 1 ATOM 290 C CA . THR A 1 45 ? 17.733 144.401 -12.809 1.00 92.61 ? 49 THR A CA 1 ATOM 291 C C . THR A 1 45 ? 18.789 145.498 -12.890 1.00 92.22 ? 49 THR A C 1 ATOM 292 O O . THR A 1 45 ? 19.961 145.252 -12.592 1.00 89.44 ? 49 THR A O 1 ATOM 293 C CB . THR A 1 45 ? 17.298 144.102 -11.361 1.00 103.31 ? 49 THR A CB 1 ATOM 294 O OG1 . THR A 1 45 ? 18.375 143.491 -10.659 1.00 101.83 ? 49 THR A OG1 1 ATOM 295 C CG2 . THR A 1 45 ? 16.062 143.228 -11.309 1.00 104.00 ? 49 THR A CG2 1 ATOM 296 N N . ASN A 1 46 ? 18.374 146.690 -13.378 1.00 88.33 ? 50 ASN A N 1 ATOM 297 C CA . ASN A 1 46 ? 19.199 147.889 -13.583 1.00 86.84 ? 50 ASN A CA 1 ATOM 298 C C . ASN A 1 46 ? 20.342 147.633 -14.594 1.00 85.75 ? 50 ASN A C 1 ATOM 299 O O . ASN A 1 46 ? 21.420 148.231 -14.483 1.00 84.54 ? 50 ASN A O 1 ATOM 300 C CB . ASN A 1 46 ? 19.695 148.463 -12.231 1.00 88.57 ? 50 ASN A CB 1 ATOM 301 C CG . ASN A 1 46 ? 20.067 149.929 -12.200 1.00 120.24 ? 50 ASN A CG 1 ATOM 302 O OD1 . ASN A 1 46 ? 20.134 150.632 -13.223 1.00 117.21 ? 50 ASN A OD1 1 ATOM 303 N ND2 . ASN A 1 46 ? 20.343 150.421 -11.003 1.00 115.04 ? 50 ASN A ND2 1 ATOM 304 N N . ASN A 1 47 ? 20.077 146.760 -15.603 1.00 79.29 ? 51 ASN A N 1 ATOM 305 C CA . ASN A 1 47 ? 21.004 146.349 -16.677 1.00 76.34 ? 51 ASN A CA 1 ATOM 306 C C . ASN A 1 47 ? 22.262 145.642 -16.153 1.00 76.83 ? 51 ASN A C 1 ATOM 307 O O . ASN A 1 47 ? 23.352 145.781 -16.720 1.00 75.91 ? 51 ASN A O 1 ATOM 308 C CB . ASN A 1 47 ? 21.356 147.528 -17.613 1.00 75.69 ? 51 ASN A CB 1 ATOM 309 C CG . ASN A 1 47 ? 20.236 148.030 -18.482 1.00 91.81 ? 51 ASN A CG 1 ATOM 310 O OD1 . ASN A 1 47 ? 19.181 147.405 -18.607 1.00 87.86 ? 51 ASN A OD1 1 ATOM 311 N ND2 . ASN A 1 47 ? 20.465 149.158 -19.140 1.00 81.35 ? 51 ASN A ND2 1 ATOM 312 N N . GLU A 1 48 ? 22.103 144.876 -15.065 1.00 71.51 ? 52 GLU A N 1 ATOM 313 C CA . GLU A 1 48 ? 23.196 144.150 -14.428 1.00 69.11 ? 52 GLU A CA 1 ATOM 314 C C . GLU A 1 48 ? 22.853 142.676 -14.285 1.00 70.08 ? 52 GLU A C 1 ATOM 315 O O . GLU A 1 48 ? 21.773 142.352 -13.790 1.00 69.76 ? 52 GLU A O 1 ATOM 316 C CB . GLU A 1 48 ? 23.491 144.733 -13.033 1.00 70.86 ? 52 GLU A CB 1 ATOM 317 C CG . GLU A 1 48 ? 23.999 146.162 -13.029 1.00 82.84 ? 52 GLU A CG 1 ATOM 318 C CD . GLU A 1 48 ? 24.236 146.764 -11.655 1.00 106.53 ? 52 GLU A CD 1 ATOM 319 O OE1 . GLU A 1 48 ? 23.552 146.362 -10.684 1.00 93.30 ? 52 GLU A OE1 1 ATOM 320 O OE2 . GLU A 1 48 ? 25.081 147.683 -11.563 1.00 106.48 ? 52 GLU A OE2 1 ATOM 321 N N . VAL A 1 49 ? 23.773 141.784 -14.702 1.00 64.12 ? 53 VAL A N 1 ATOM 322 C CA . VAL A 1 49 ? 23.625 140.337 -14.525 1.00 62.24 ? 53 VAL A CA 1 ATOM 323 C C . VAL A 1 49 ? 24.525 139.982 -13.325 1.00 64.72 ? 53 VAL A C 1 ATOM 324 O O . VAL A 1 49 ? 25.740 140.147 -13.396 1.00 62.35 ? 53 VAL A O 1 ATOM 325 C CB . VAL A 1 49 ? 23.955 139.504 -15.789 1.00 64.54 ? 53 VAL A CB 1 ATOM 326 C CG1 . VAL A 1 49 ? 23.718 138.015 -15.538 1.00 63.54 ? 53 VAL A CG1 1 ATOM 327 C CG2 . VAL A 1 49 ? 23.150 139.980 -16.984 1.00 65.26 ? 53 VAL A CG2 1 ATOM 328 N N . HIS A 1 50 ? 23.916 139.567 -12.208 1.00 63.12 ? 54 HIS A N 1 ATOM 329 C CA . HIS A 1 50 ? 24.613 139.265 -10.953 1.00 63.01 ? 54 HIS A CA 1 ATOM 330 C C . HIS A 1 50 ? 25.002 137.803 -10.791 1.00 65.17 ? 54 HIS A C 1 ATOM 331 O O . HIS A 1 50 ? 24.483 136.932 -11.490 1.00 64.37 ? 54 HIS A O 1 ATOM 332 C CB . HIS A 1 50 ? 23.744 139.682 -9.742 1.00 65.67 ? 54 HIS A CB 1 ATOM 333 C CG . HIS A 1 50 ? 23.465 141.154 -9.651 1.00 71.03 ? 54 HIS A CG 1 ATOM 334 N ND1 . HIS A 1 50 ? 24.457 142.053 -9.299 1.00 73.26 ? 54 HIS A ND1 1 ATOM 335 C CD2 . HIS A 1 50 ? 22.310 141.835 -9.853 1.00 74.58 ? 54 HIS A CD2 1 ATOM 336 C CE1 . HIS A 1 50 ? 23.884 143.249 -9.320 1.00 74.17 ? 54 HIS A CE1 1 ATOM 337 N NE2 . HIS A 1 50 ? 22.591 143.168 -9.643 1.00 75.38 ? 54 HIS A NE2 1 ATOM 338 N N . ASN A 1 51 ? 25.875 137.536 -9.806 1.00 61.14 ? 55 ASN A N 1 ATOM 339 C CA . ASN A 1 51 ? 26.304 136.197 -9.372 1.00 59.58 ? 55 ASN A CA 1 ATOM 340 C C . ASN A 1 51 ? 26.900 135.315 -10.461 1.00 61.68 ? 55 ASN A C 1 ATOM 341 O O . ASN A 1 51 ? 26.519 134.155 -10.613 1.00 61.45 ? 55 ASN A O 1 ATOM 342 C CB . ASN A 1 51 ? 25.180 135.453 -8.610 1.00 59.42 ? 55 ASN A CB 1 ATOM 343 C CG . ASN A 1 51 ? 24.557 136.164 -7.440 1.00 85.97 ? 55 ASN A CG 1 ATOM 344 O OD1 . ASN A 1 51 ? 25.160 137.090 -6.844 1.00 79.44 ? 55 ASN A OD1 1 ATOM 345 N ND2 . ASN A 1 51 ? 23.292 135.680 -7.177 1.00 81.19 ? 55 ASN A ND2 1 ATOM 346 N N . LEU A 1 52 ? 27.857 135.854 -11.200 1.00 57.10 ? 56 LEU A N 1 ATOM 347 C CA . LEU A 1 52 ? 28.536 135.098 -12.251 1.00 55.81 ? 56 LEU A CA 1 ATOM 348 C C . LEU A 1 52 ? 29.840 134.522 -11.698 1.00 58.68 ? 56 LEU A C 1 ATOM 349 O O . LEU A 1 52 ? 30.641 135.258 -11.116 1.00 58.40 ? 56 LEU A O 1 ATOM 350 C CB . LEU A 1 52 ? 28.834 135.990 -13.472 1.00 55.95 ? 56 LEU A CB 1 ATOM 351 C CG . LEU A 1 52 ? 27.657 136.689 -14.144 1.00 61.04 ? 56 LEU A CG 1 ATOM 352 C CD1 . LEU A 1 52 ? 28.150 137.756 -15.071 1.00 61.35 ? 56 LEU A CD1 1 ATOM 353 C CD2 . LEU A 1 52 ? 26.778 135.697 -14.910 1.00 63.68 ? 56 LEU A CD2 1 ATOM 354 N N . THR A 1 53 ? 30.049 133.209 -11.885 1.00 53.75 ? 57 THR A N 1 ATOM 355 C CA . THR A 1 53 ? 31.272 132.523 -11.471 1.00 52.82 ? 57 THR A CA 1 ATOM 356 C C . THR A 1 53 ? 32.384 132.921 -12.430 1.00 55.99 ? 57 THR A C 1 ATOM 357 O O . THR A 1 53 ? 32.169 133.015 -13.645 1.00 55.44 ? 57 THR A O 1 ATOM 358 C CB . THR A 1 53 ? 31.072 131.002 -11.476 1.00 60.37 ? 57 THR A CB 1 ATOM 359 O OG1 . THR A 1 53 ? 29.961 130.701 -10.653 1.00 61.06 ? 57 THR A OG1 1 ATOM 360 C CG2 . THR A 1 53 ? 32.308 130.214 -10.986 1.00 57.63 ? 57 THR A CG2 1 ATOM 361 N N . GLU A 1 54 ? 33.576 133.138 -11.868 1.00 51.83 ? 58 GLU A N 1 ATOM 362 C CA . GLU A 1 54 ? 34.788 133.481 -12.597 1.00 51.41 ? 58 GLU A CA 1 ATOM 363 C C . GLU A 1 54 ? 35.136 132.389 -13.603 1.00 54.00 ? 58 GLU A C 1 ATOM 364 O O . GLU A 1 54 ? 34.866 131.212 -13.348 1.00 53.09 ? 58 GLU A O 1 ATOM 365 C CB . GLU A 1 54 ? 35.955 133.679 -11.615 1.00 53.55 ? 58 GLU A CB 1 ATOM 366 C CG . GLU A 1 54 ? 36.407 132.397 -10.931 1.00 63.55 ? 58 GLU A CG 1 ATOM 367 C CD . GLU A 1 54 ? 37.745 132.452 -10.232 1.00 82.93 ? 58 GLU A CD 1 ATOM 368 O OE1 . GLU A 1 54 ? 37.768 132.877 -9.053 1.00 78.55 ? 58 GLU A OE1 1 ATOM 369 O OE2 . GLU A 1 54 ? 38.755 132.023 -10.835 1.00 70.18 ? 58 GLU A OE2 1 ATOM 370 N N . CYS A 1 55 ? 35.691 132.781 -14.756 1.00 51.15 ? 59 CYS A N 1 ATOM 371 C CA . CYS A 1 55 ? 36.186 131.859 -15.783 1.00 50.94 ? 59 CYS A CA 1 ATOM 372 C C . CYS A 1 55 ? 35.201 130.856 -16.339 1.00 51.00 ? 59 CYS A C 1 ATOM 373 O O . CYS A 1 55 ? 35.596 129.758 -16.735 1.00 49.64 ? 59 CYS A O 1 ATOM 374 C CB . CYS A 1 55 ? 37.472 131.190 -15.307 1.00 52.79 ? 59 CYS A CB 1 ATOM 375 S SG . CYS A 1 55 ? 38.847 132.341 -15.096 1.00 58.86 ? 59 CYS A SG 1 ATOM 376 N N . LYS A 1 56 ? 33.928 131.233 -16.382 1.00 47.00 ? 60 LYS A N 1 ATOM 377 C CA . LYS A 1 56 ? 32.846 130.404 -16.905 1.00 46.23 ? 60 LYS A CA 1 ATOM 378 C C . LYS A 1 56 ? 32.064 131.238 -17.895 1.00 50.75 ? 60 LYS A C 1 ATOM 379 O O . LYS A 1 56 ? 31.787 132.408 -17.609 1.00 51.12 ? 60 LYS A O 1 ATOM 380 C CB . LYS A 1 56 ? 31.904 129.924 -15.769 1.00 46.83 ? 60 LYS A CB 1 ATOM 381 C CG . LYS A 1 56 ? 32.529 128.901 -14.826 1.00 51.45 ? 60 LYS A CG 1 ATOM 382 C CD . LYS A 1 56 ? 31.543 127.941 -14.119 1.00 64.80 ? 60 LYS A CD 1 ATOM 383 C CE . LYS A 1 56 ? 30.159 128.386 -13.645 1.00 78.22 ? 60 LYS A CE 1 ATOM 384 N NZ . LYS A 1 56 ? 29.226 127.234 -13.449 1.00 78.60 ? 60 LYS A NZ 1 ATOM 385 N N . ASN A 1 57 ? 31.714 130.663 -19.057 1.00 46.62 ? 61 ASN A N 1 ATOM 386 C CA . ASN A 1 57 ? 30.867 131.362 -20.021 1.00 46.86 ? 61 ASN A CA 1 ATOM 387 C C . ASN A 1 57 ? 29.414 131.203 -19.582 1.00 51.67 ? 61 ASN A C 1 ATOM 388 O O . ASN A 1 57 ? 28.998 130.098 -19.225 1.00 51.01 ? 61 ASN A O 1 ATOM 389 C CB . ASN A 1 57 ? 31.071 130.841 -21.444 1.00 46.10 ? 61 ASN A CB 1 ATOM 390 C CG . ASN A 1 57 ? 32.319 131.358 -22.145 1.00 64.44 ? 61 ASN A CG 1 ATOM 391 O OD1 . ASN A 1 57 ? 33.120 132.097 -21.567 1.00 69.95 ? 61 ASN A OD1 1 ATOM 392 N ND2 . ASN A 1 57 ? 32.547 130.982 -23.410 1.00 48.94 ? 61 ASN A ND2 1 ATOM 393 N N . ALA A 1 58 ? 28.676 132.321 -19.534 1.00 49.40 ? 62 ALA A N 1 ATOM 394 C CA . ALA A 1 58 ? 27.272 132.390 -19.129 1.00 50.32 ? 62 ALA A CA 1 ATOM 395 C C . ALA A 1 58 ? 26.498 133.014 -20.248 1.00 56.78 ? 62 ALA A C 1 ATOM 396 O O . ALA A 1 58 ? 27.057 133.819 -20.989 1.00 56.35 ? 62 ALA A O 1 ATOM 397 C CB . ALA A 1 58 ? 27.121 133.221 -17.864 1.00 51.05 ? 62 ALA A CB 1 ATOM 398 N N . SER A 1 59 ? 25.234 132.615 -20.416 1.00 55.85 ? 63 SER A N 1 ATOM 399 C CA . SER A 1 59 ? 24.438 133.140 -21.509 1.00 57.65 ? 63 SER A CA 1 ATOM 400 C C . SER A 1 59 ? 23.256 133.938 -21.008 1.00 63.90 ? 63 SER A C 1 ATOM 401 O O . SER A 1 59 ? 22.632 133.572 -20.013 1.00 63.33 ? 63 SER A O 1 ATOM 402 C CB . SER A 1 59 ? 23.992 132.010 -22.426 1.00 62.30 ? 63 SER A CB 1 ATOM 403 O OG . SER A 1 59 ? 23.528 132.514 -23.667 1.00 74.63 ? 63 SER A OG 1 ATOM 404 N N . VAL A 1 60 ? 22.987 135.062 -21.672 1.00 62.84 ? 64 VAL A N 1 ATOM 405 C CA . VAL A 1 60 ? 21.864 135.932 -21.351 1.00 64.76 ? 64 VAL A CA 1 ATOM 406 C C . VAL A 1 60 ? 21.073 136.289 -22.617 1.00 71.26 ? 64 VAL A C 1 ATOM 407 O O . VAL A 1 60 ? 21.688 136.646 -23.622 1.00 70.72 ? 64 VAL A O 1 ATOM 408 C CB . VAL A 1 60 ? 22.263 137.142 -20.456 1.00 68.61 ? 64 VAL A CB 1 ATOM 409 C CG1 . VAL A 1 60 ? 23.069 138.213 -21.202 1.00 68.33 ? 64 VAL A CG1 1 ATOM 410 C CG2 . VAL A 1 60 ? 21.042 137.737 -19.764 1.00 70.06 ? 64 VAL A CG2 1 ATOM 411 N N . SER A 1 61 ? 19.733 136.098 -22.602 1.00 70.50 ? 65 SER A N 1 ATOM 412 C CA . SER A 1 61 ? 18.892 136.408 -23.768 1.00 73.18 ? 65 SER A CA 1 ATOM 413 C C . SER A 1 61 ? 18.266 137.784 -23.563 1.00 79.04 ? 65 SER A C 1 ATOM 414 O O . SER A 1 61 ? 17.507 137.975 -22.619 1.00 79.97 ? 65 SER A O 1 ATOM 415 C CB . SER A 1 61 ? 17.850 135.325 -24.008 1.00 79.52 ? 65 SER A CB 1 ATOM 416 O OG . SER A 1 61 ? 17.956 134.819 -25.330 1.00 91.83 ? 65 SER A OG 1 ATOM 417 N N . ILE A 1 62 ? 18.670 138.762 -24.388 1.00 75.64 ? 66 ILE A N 1 ATOM 418 C CA . ILE A 1 62 ? 18.284 140.169 -24.269 1.00 76.67 ? 66 ILE A CA 1 ATOM 419 C C . ILE A 1 62 ? 17.213 140.585 -25.276 1.00 86.03 ? 66 ILE A C 1 ATOM 420 O O . ILE A 1 62 ? 17.330 140.290 -26.466 1.00 86.56 ? 66 ILE A O 1 ATOM 421 C CB . ILE A 1 62 ? 19.564 141.059 -24.370 1.00 77.42 ? 66 ILE A CB 1 ATOM 422 C CG1 . ILE A 1 62 ? 20.548 140.768 -23.222 1.00 75.27 ? 66 ILE A CG1 1 ATOM 423 C CG2 . ILE A 1 62 ? 19.250 142.554 -24.463 1.00 78.99 ? 66 ILE A CG2 1 ATOM 424 C CD1 . ILE A 1 62 ? 21.956 141.142 -23.553 1.00 78.63 ? 66 ILE A CD1 1 ATOM 425 N N . SER A 1 63 ? 16.192 141.309 -24.787 1.00 86.12 ? 67 SER A N 1 ATOM 426 C CA . SER A 1 63 ? 15.100 141.874 -25.576 1.00 89.69 ? 67 SER A CA 1 ATOM 427 C C . SER A 1 63 ? 14.643 143.217 -24.974 1.00 96.31 ? 67 SER A C 1 ATOM 428 O O . SER A 1 63 ? 15.042 143.566 -23.860 1.00 94.23 ? 67 SER A O 1 ATOM 429 C CB . SER A 1 63 ? 13.932 140.894 -25.675 1.00 96.04 ? 67 SER A CB 1 ATOM 430 O OG . SER A 1 63 ? 13.338 140.656 -24.409 1.00 106.29 ? 67 SER A OG 1 ATOM 431 N N . HIS A 1 64 ? 13.826 143.972 -25.732 1.00 97.18 ? 68 HIS A N 1 ATOM 432 C CA . HIS A 1 64 ? 13.250 145.276 -25.368 1.00 99.31 ? 68 HIS A CA 1 ATOM 433 C C . HIS A 1 64 ? 12.016 145.514 -26.253 1.00 106.85 ? 68 HIS A C 1 ATOM 434 O O . HIS A 1 64 ? 11.935 144.940 -27.342 1.00 106.75 ? 68 HIS A O 1 ATOM 435 C CB . HIS A 1 64 ? 14.297 146.393 -25.552 1.00 98.59 ? 68 HIS A CB 1 ATOM 436 C CG . HIS A 1 64 ? 13.915 147.703 -24.935 1.00 103.50 ? 68 HIS A CG 1 ATOM 437 N ND1 . HIS A 1 64 ? 13.493 148.765 -25.709 1.00 107.40 ? 68 HIS A ND1 1 ATOM 438 C CD2 . HIS A 1 64 ? 13.919 148.085 -23.637 1.00 105.07 ? 68 HIS A CD2 1 ATOM 439 C CE1 . HIS A 1 64 ? 13.248 149.753 -24.864 1.00 107.79 ? 68 HIS A CE1 1 ATOM 440 N NE2 . HIS A 1 64 ? 13.486 149.390 -23.606 1.00 106.80 ? 68 HIS A NE2 1 ATOM 441 N N . ASN A 1 65 ? 11.053 146.335 -25.790 1.00 106.51 ? 69 ASN A N 1 ATOM 442 C CA . ASN A 1 65 ? 9.818 146.631 -26.536 1.00 110.63 ? 69 ASN A CA 1 ATOM 443 C C . ASN A 1 65 ? 10.069 147.295 -27.897 1.00 115.03 ? 69 ASN A C 1 ATOM 444 O O . ASN A 1 65 ? 9.257 147.141 -28.810 1.00 117.43 ? 69 ASN A O 1 ATOM 445 C CB . ASN A 1 65 ? 8.831 147.460 -25.703 1.00 115.51 ? 69 ASN A CB 1 ATOM 446 C CG . ASN A 1 65 ? 9.403 148.709 -25.062 1.00 141.17 ? 69 ASN A CG 1 ATOM 447 O OD1 . ASN A 1 65 ? 10.034 149.574 -25.690 1.00 134.17 ? 69 ASN A OD1 1 ATOM 448 N ND2 . ASN A 1 65 ? 9.160 148.846 -23.775 1.00 134.76 ? 69 ASN A ND2 1 ATOM 449 N N . SER A 1 66 ? 11.211 147.996 -28.032 1.00 108.83 ? 70 SER A N 1 ATOM 450 C CA . SER A 1 66 ? 11.648 148.694 -29.243 1.00 108.65 ? 70 SER A CA 1 ATOM 451 C C . SER A 1 66 ? 12.207 147.757 -30.336 1.00 110.47 ? 70 SER A C 1 ATOM 452 O O . SER A 1 66 ? 12.569 148.225 -31.419 1.00 109.81 ? 70 SER A O 1 ATOM 453 C CB . SER A 1 66 ? 12.682 149.754 -28.883 1.00 110.36 ? 70 SER A CB 1 ATOM 454 O OG . SER A 1 66 ? 13.836 149.142 -28.331 1.00 116.20 ? 70 SER A OG 1 ATOM 455 N N . CYS A 1 67 ? 12.290 146.451 -30.054 1.00 105.88 ? 71 CYS A N 1 ATOM 456 C CA . CYS A 1 67 ? 12.799 145.478 -31.012 1.00 105.01 ? 71 CYS A CA 1 ATOM 457 C C . CYS A 1 67 ? 11.993 144.188 -30.991 1.00 109.47 ? 71 CYS A C 1 ATOM 458 O O . CYS A 1 67 ? 11.340 143.882 -29.995 1.00 109.69 ? 71 CYS A O 1 ATOM 459 C CB . CYS A 1 67 ? 14.298 145.234 -30.828 1.00 101.93 ? 71 CYS A CB 1 ATOM 460 S SG . CYS A 1 67 ? 14.798 144.722 -29.154 1.00 103.48 ? 71 CYS A SG 1 ATOM 461 N N . THR A 1 68 ? 12.018 143.442 -32.094 1.00 106.20 ? 72 THR A N 1 ATOM 462 C CA . THR A 1 68 ? 11.247 142.205 -32.215 1.00 107.57 ? 72 THR A CA 1 ATOM 463 C C . THR A 1 68 ? 12.112 140.970 -32.007 1.00 108.21 ? 72 THR A C 1 ATOM 464 O O . THR A 1 68 ? 13.338 141.076 -31.958 1.00 104.84 ? 72 THR A O 1 ATOM 465 C CB . THR A 1 68 ? 10.527 142.158 -33.581 1.00 118.32 ? 72 THR A CB 1 ATOM 466 O OG1 . THR A 1 68 ? 11.460 141.803 -34.606 1.00 115.73 ? 72 THR A OG1 1 ATOM 467 C CG2 . THR A 1 68 ? 9.830 143.467 -33.928 1.00 119.56 ? 72 THR A CG2 1 ATOM 468 N N . ALA A 1 69 ? 11.472 139.786 -31.932 1.00 105.52 ? 73 ALA A N 1 ATOM 469 C CA . ALA A 1 69 ? 12.159 138.499 -31.827 1.00 102.91 ? 73 ALA A CA 1 ATOM 470 C C . ALA A 1 69 ? 12.955 138.254 -33.143 1.00 105.59 ? 73 ALA A C 1 ATOM 471 O O . ALA A 1 69 ? 12.583 138.831 -34.167 1.00 107.22 ? 73 ALA A O 1 ATOM 472 C CB . ALA A 1 69 ? 11.143 137.388 -31.606 1.00 105.78 ? 73 ALA A CB 1 ATOM 473 N N . PRO A 1 70 ? 14.070 137.485 -33.164 1.00 99.05 ? 74 PRO A N 1 ATOM 474 C CA . PRO A 1 70 ? 14.705 136.745 -32.060 1.00 95.99 ? 74 PRO A CA 1 ATOM 475 C C . PRO A 1 70 ? 15.416 137.645 -31.062 1.00 96.55 ? 74 PRO A C 1 ATOM 476 O O . PRO A 1 70 ? 15.919 138.717 -31.423 1.00 95.85 ? 74 PRO A O 1 ATOM 477 C CB . PRO A 1 70 ? 15.731 135.863 -32.786 1.00 96.26 ? 74 PRO A CB 1 ATOM 478 C CG . PRO A 1 70 ? 16.116 136.670 -33.983 1.00 101.51 ? 74 PRO A CG 1 ATOM 479 C CD . PRO A 1 70 ? 14.817 137.297 -34.425 1.00 100.34 ? 74 PRO A CD 1 ATOM 480 N N . ASP A 1 71 ? 15.495 137.169 -29.810 1.00 90.67 ? 75 ASP A N 1 ATOM 481 C CA . ASP A 1 71 ? 16.217 137.813 -28.712 1.00 87.67 ? 75 ASP A CA 1 ATOM 482 C C . ASP A 1 71 ? 17.705 137.791 -29.018 1.00 85.90 ? 75 ASP A C 1 ATOM 483 O O . ASP A 1 71 ? 18.172 136.902 -29.742 1.00 84.88 ? 75 ASP A O 1 ATOM 484 C CB . ASP A 1 71 ? 16.023 137.005 -27.416 1.00 88.96 ? 75 ASP A CB 1 ATOM 485 C CG . ASP A 1 71 ? 14.783 137.319 -26.611 1.00 102.85 ? 75 ASP A CG 1 ATOM 486 O OD1 . ASP A 1 71 ? 13.802 137.834 -27.198 1.00 106.14 ? 75 ASP A OD1 1 ATOM 487 O OD2 . ASP A 1 71 ? 14.774 137.012 -25.406 1.00 108.08 ? 75 ASP A OD2 1 ATOM 488 N N . LYS A 1 72 ? 18.458 138.734 -28.436 1.00 78.37 ? 76 LYS A N 1 ATOM 489 C CA . LYS A 1 72 ? 19.902 138.726 -28.582 1.00 74.77 ? 76 LYS A CA 1 ATOM 490 C C . LYS A 1 72 ? 20.472 137.785 -27.528 1.00 75.12 ? 76 LYS A C 1 ATOM 491 O O . LYS A 1 72 ? 20.337 138.054 -26.332 1.00 73.84 ? 76 LYS A O 1 ATOM 492 C CB . LYS A 1 72 ? 20.521 140.123 -28.430 1.00 75.79 ? 76 LYS A CB 1 ATOM 493 C CG . LYS A 1 72 ? 21.873 140.128 -29.100 1.00 75.95 ? 76 LYS A CG 1 ATOM 494 C CD . LYS A 1 72 ? 23.102 139.939 -28.257 1.00 71.34 ? 76 LYS A CD 1 ATOM 495 C CE . LYS A 1 72 ? 24.255 139.454 -29.106 1.00 66.47 ? 76 LYS A CE 1 ATOM 496 N NZ . LYS A 1 72 ? 25.547 139.436 -28.411 1.00 72.63 ? 76 LYS A NZ 1 ATOM 497 N N . THR A 1 73 ? 21.109 136.684 -27.964 1.00 69.51 ? 77 THR A N 1 ATOM 498 C CA . THR A 1 73 ? 21.763 135.748 -27.047 1.00 66.63 ? 77 THR A CA 1 ATOM 499 C C . THR A 1 73 ? 23.189 136.257 -26.855 1.00 68.42 ? 77 THR A C 1 ATOM 500 O O . THR A 1 73 ? 23.977 136.301 -27.810 1.00 68.17 ? 77 THR A O 1 ATOM 501 C CB . THR A 1 73 ? 21.643 134.287 -27.519 1.00 69.85 ? 77 THR A CB 1 ATOM 502 O OG1 . THR A 1 73 ? 20.299 133.843 -27.320 1.00 71.20 ? 77 THR A OG1 1 ATOM 503 C CG2 . THR A 1 73 ? 22.606 133.349 -26.786 1.00 63.16 ? 77 THR A CG2 1 ATOM 504 N N . LEU A 1 74 ? 23.476 136.735 -25.638 1.00 63.08 ? 78 LEU A N 1 ATOM 505 C CA . LEU A 1 74 ? 24.766 137.302 -25.274 1.00 60.98 ? 78 LEU A CA 1 ATOM 506 C C . LEU A 1 74 ? 25.560 136.351 -24.404 1.00 63.00 ? 78 LEU A C 1 ATOM 507 O O . LEU A 1 74 ? 25.081 135.929 -23.349 1.00 61.67 ? 78 LEU A O 1 ATOM 508 C CB . LEU A 1 74 ? 24.576 138.657 -24.568 1.00 61.03 ? 78 LEU A CB 1 ATOM 509 C CG . LEU A 1 74 ? 25.837 139.346 -24.038 1.00 64.29 ? 78 LEU A CG 1 ATOM 510 C CD1 . LEU A 1 74 ? 26.768 139.746 -25.164 1.00 64.19 ? 78 LEU A CD1 1 ATOM 511 C CD2 . LEU A 1 74 ? 25.491 140.547 -23.206 1.00 67.45 ? 78 LEU A CD2 1 ATOM 512 N N . ILE A 1 75 ? 26.785 136.028 -24.851 1.00 59.32 ? 79 ILE A N 1 ATOM 513 C CA . ILE A 1 75 ? 27.715 135.165 -24.122 1.00 57.98 ? 79 ILE A CA 1 ATOM 514 C C . ILE A 1 75 ? 28.631 136.035 -23.263 1.00 60.29 ? 79 ILE A C 1 ATOM 515 O O . ILE A 1 75 ? 29.348 136.890 -23.784 1.00 60.77 ? 79 ILE A O 1 ATOM 516 C CB . ILE A 1 75 ? 28.510 134.194 -25.048 1.00 61.25 ? 79 ILE A CB 1 ATOM 517 C CG1 . ILE A 1 75 ? 27.583 133.261 -25.891 1.00 62.82 ? 79 ILE A CG1 1 ATOM 518 C CG2 . ILE A 1 75 ? 29.622 133.430 -24.305 1.00 60.70 ? 79 ILE A CG2 1 ATOM 519 C CD1 . ILE A 1 75 ? 26.583 132.347 -25.160 1.00 69.93 ? 79 ILE A CD1 1 ATOM 520 N N . LEU A 1 76 ? 28.582 135.822 -21.949 1.00 54.79 ? 80 LEU A N 1 ATOM 521 C CA . LEU A 1 76 ? 29.408 136.546 -20.994 1.00 53.77 ? 80 LEU A CA 1 ATOM 522 C C . LEU A 1 76 ? 30.642 135.720 -20.699 1.00 55.23 ? 80 LEU A C 1 ATOM 523 O O . LEU A 1 76 ? 30.526 134.645 -20.110 1.00 54.86 ? 80 LEU A O 1 ATOM 524 C CB . LEU A 1 76 ? 28.620 136.851 -19.707 1.00 54.12 ? 80 LEU A CB 1 ATOM 525 C CG . LEU A 1 76 ? 27.271 137.574 -19.888 1.00 60.55 ? 80 LEU A CG 1 ATOM 526 C CD1 . LEU A 1 76 ? 26.517 137.660 -18.599 1.00 61.36 ? 80 LEU A CD1 1 ATOM 527 C CD2 . LEU A 1 76 ? 27.447 138.961 -20.468 1.00 63.86 ? 80 LEU A CD2 1 ATOM 528 N N . ASP A 1 77 ? 31.809 136.176 -21.174 1.00 50.02 ? 81 ASP A N 1 ATOM 529 C CA . ASP A 1 77 ? 33.084 135.497 -20.935 1.00 48.80 ? 81 ASP A CA 1 ATOM 530 C C . ASP A 1 77 ? 33.661 136.120 -19.658 1.00 51.49 ? 81 ASP A C 1 ATOM 531 O O . ASP A 1 77 ? 34.338 137.152 -19.703 1.00 51.69 ? 81 ASP A O 1 ATOM 532 C CB . ASP A 1 77 ? 34.014 135.657 -22.149 1.00 51.29 ? 81 ASP A CB 1 ATOM 533 C CG . ASP A 1 77 ? 35.253 134.765 -22.177 1.00 62.01 ? 81 ASP A CG 1 ATOM 534 O OD1 . ASP A 1 77 ? 35.581 134.158 -21.129 1.00 61.83 ? 81 ASP A OD1 1 ATOM 535 O OD2 . ASP A 1 77 ? 35.915 134.701 -23.240 1.00 69.40 ? 81 ASP A OD2 1 ATOM 536 N N . VAL A 1 78 ? 33.317 135.519 -18.511 1.00 46.50 ? 82 VAL A N 1 ATOM 537 C CA . VAL A 1 78 ? 33.646 136.026 -17.180 1.00 45.36 ? 82 VAL A CA 1 ATOM 538 C C . VAL A 1 78 ? 35.147 135.931 -16.839 1.00 47.50 ? 82 VAL A C 1 ATOM 539 O O . VAL A 1 78 ? 35.751 134.882 -17.066 1.00 47.54 ? 82 VAL A O 1 ATOM 540 C CB . VAL A 1 78 ? 32.691 135.432 -16.118 1.00 48.58 ? 82 VAL A CB 1 ATOM 541 C CG1 . VAL A 1 78 ? 32.928 136.037 -14.743 1.00 48.58 ? 82 VAL A CG1 1 ATOM 542 C CG2 . VAL A 1 78 ? 31.234 135.627 -16.534 1.00 48.52 ? 82 VAL A CG2 1 ATOM 543 N N . PRO A 1 79 ? 35.767 137.041 -16.340 1.00 42.37 ? 83 PRO A N 1 ATOM 544 C CA . PRO A 1 79 ? 37.209 137.019 -16.026 1.00 42.27 ? 83 PRO A CA 1 ATOM 545 C C . PRO A 1 79 ? 37.606 136.224 -14.775 1.00 44.83 ? 83 PRO A C 1 ATOM 546 O O . PRO A 1 79 ? 36.718 135.776 -14.051 1.00 43.38 ? 83 PRO A O 1 ATOM 547 C CB . PRO A 1 79 ? 37.572 138.512 -15.875 1.00 44.43 ? 83 PRO A CB 1 ATOM 548 C CG . PRO A 1 79 ? 36.359 139.282 -16.180 1.00 47.93 ? 83 PRO A CG 1 ATOM 549 C CD . PRO A 1 79 ? 35.194 138.373 -16.061 1.00 43.07 ? 83 PRO A CD 1 ATOM 550 N N . PRO A 1 80 ? 38.923 136.066 -14.467 1.00 42.05 ? 84 PRO A N 1 ATOM 551 C CA . PRO A 1 80 ? 39.310 135.316 -13.258 1.00 42.10 ? 84 PRO A CA 1 ATOM 552 C C . PRO A 1 80 ? 39.060 136.058 -11.954 1.00 46.35 ? 84 PRO A C 1 ATOM 553 O O . PRO A 1 80 ? 38.837 137.269 -11.950 1.00 46.44 ? 84 PRO A O 1 ATOM 554 C CB . PRO A 1 80 ? 40.811 135.069 -13.455 1.00 45.50 ? 84 PRO A CB 1 ATOM 555 C CG . PRO A 1 80 ? 41.112 135.484 -14.851 1.00 50.18 ? 84 PRO A CG 1 ATOM 556 C CD . PRO A 1 80 ? 40.120 136.515 -15.203 1.00 44.77 ? 84 PRO A CD 1 ATOM 557 N N . GLY A 1 81 ? 39.125 135.314 -10.858 1.00 59.10 ? 85 GLY A N 1 ATOM 558 C CA . GLY A 1 81 ? 38.929 135.832 -9.511 1.00 61.29 ? 85 GLY A CA 1 ATOM 559 C C . GLY A 1 81 ? 39.906 136.915 -9.108 1.00 65.32 ? 85 GLY A C 1 ATOM 560 O O . GLY A 1 81 ? 41.127 136.715 -9.142 1.00 63.87 ? 85 GLY A O 1 ATOM 561 N N . VAL A 1 82 ? 39.356 138.084 -8.735 1.00 62.81 ? 86 VAL A N 1 ATOM 562 C CA . VAL A 1 82 ? 40.124 139.253 -8.298 1.00 61.27 ? 86 VAL A CA 1 ATOM 563 C C . VAL A 1 82 ? 41.092 138.882 -7.158 1.00 64.62 ? 86 VAL A C 1 ATOM 564 O O . VAL A 1 82 ? 42.253 139.264 -7.222 1.00 62.21 ? 86 VAL A O 1 ATOM 565 C CB . VAL A 1 82 ? 39.155 140.410 -7.964 1.00 66.66 ? 86 VAL A CB 1 ATOM 566 C CG1 . VAL A 1 82 ? 39.805 141.505 -7.132 1.00 66.47 ? 86 VAL A CG1 1 ATOM 567 C CG2 . VAL A 1 82 ? 38.537 140.986 -9.234 1.00 65.67 ? 86 VAL A CG2 1 ATOM 568 N N . GLU A 1 83 ? 40.657 138.045 -6.204 1.00 63.24 ? 87 GLU A N 1 ATOM 569 C CA . GLU A 1 83 ? 41.470 137.558 -5.078 1.00 64.00 ? 87 GLU A CA 1 ATOM 570 C C . GLU A 1 83 ? 42.610 136.584 -5.487 1.00 66.61 ? 87 GLU A C 1 ATOM 571 O O . GLU A 1 83 ? 43.454 136.236 -4.655 1.00 67.51 ? 87 GLU A O 1 ATOM 572 C CB . GLU A 1 83 ? 40.566 136.932 -3.985 1.00 69.59 ? 87 GLU A CB 1 ATOM 573 C CG . GLU A 1 83 ? 39.263 136.285 -4.469 1.00 79.57 ? 87 GLU A CG 1 ATOM 574 C CD . GLU A 1 83 ? 39.331 134.954 -5.206 1.00 94.66 ? 87 GLU A CD 1 ATOM 575 O OE1 . GLU A 1 83 ? 40.018 134.025 -4.720 1.00 85.32 ? 87 GLU A OE1 1 ATOM 576 O OE2 . GLU A 1 83 ? 38.607 134.810 -6.218 1.00 84.89 ? 87 GLU A OE2 1 ATOM 577 N N . LYS A 1 84 ? 42.638 136.156 -6.764 1.00 61.07 ? 88 LYS A N 1 ATOM 578 C CA . LYS A 1 84 ? 43.650 135.218 -7.261 1.00 60.28 ? 88 LYS A CA 1 ATOM 579 C C . LYS A 1 84 ? 44.936 135.915 -7.716 1.00 63.16 ? 88 LYS A C 1 ATOM 580 O O . LYS A 1 84 ? 45.915 135.254 -8.058 1.00 62.86 ? 88 LYS A O 1 ATOM 581 C CB . LYS A 1 84 ? 43.056 134.302 -8.338 1.00 61.31 ? 88 LYS A CB 1 ATOM 582 C CG . LYS A 1 84 ? 42.039 133.321 -7.759 1.00 63.34 ? 88 LYS A CG 1 ATOM 583 C CD . LYS A 1 84 ? 41.494 132.406 -8.795 1.00 68.16 ? 88 LYS A CD 1 ATOM 584 C CE . LYS A 1 84 ? 40.720 131.283 -8.168 1.00 80.16 ? 88 LYS A CE 1 ATOM 585 N NZ . LYS A 1 84 ? 40.515 130.188 -9.145 1.00 88.18 ? 88 LYS A NZ 1 ATOM 586 N N . PHE A 1 85 ? 44.935 137.258 -7.684 1.00 59.09 ? 89 PHE A N 1 ATOM 587 C CA . PHE A 1 85 ? 46.064 138.101 -8.077 1.00 57.11 ? 89 PHE A CA 1 ATOM 588 C C . PHE A 1 85 ? 46.497 138.973 -6.927 1.00 61.97 ? 89 PHE A C 1 ATOM 589 O O . PHE A 1 85 ? 45.664 139.573 -6.242 1.00 62.42 ? 89 PHE A O 1 ATOM 590 C CB . PHE A 1 85 ? 45.730 138.991 -9.292 1.00 56.91 ? 89 PHE A CB 1 ATOM 591 C CG . PHE A 1 85 ? 45.227 138.234 -10.487 1.00 58.37 ? 89 PHE A CG 1 ATOM 592 C CD1 . PHE A 1 85 ? 46.097 137.490 -11.275 1.00 61.13 ? 89 PHE A CD1 1 ATOM 593 C CD2 . PHE A 1 85 ? 43.885 138.268 -10.833 1.00 61.15 ? 89 PHE A CD2 1 ATOM 594 C CE1 . PHE A 1 85 ? 45.620 136.753 -12.356 1.00 62.56 ? 89 PHE A CE1 1 ATOM 595 C CE2 . PHE A 1 85 ? 43.413 137.538 -11.922 1.00 64.11 ? 89 PHE A CE2 1 ATOM 596 C CZ . PHE A 1 85 ? 44.276 136.764 -12.652 1.00 62.03 ? 89 PHE A CZ 1 ATOM 597 N N . GLN A 1 86 ? 47.804 139.068 -6.731 1.00 58.45 ? 90 GLN A N 1 ATOM 598 C CA . GLN A 1 86 ? 48.366 139.878 -5.672 1.00 58.27 ? 90 GLN A CA 1 ATOM 599 C C . GLN A 1 86 ? 49.457 140.749 -6.224 1.00 57.55 ? 90 GLN A C 1 ATOM 600 O O . GLN A 1 86 ? 50.393 140.254 -6.857 1.00 55.93 ? 90 GLN A O 1 ATOM 601 C CB . GLN A 1 86 ? 48.887 138.981 -4.537 1.00 62.44 ? 90 GLN A CB 1 ATOM 602 C CG . GLN A 1 86 ? 49.774 139.668 -3.504 1.00 84.79 ? 90 GLN A CG 1 ATOM 603 C CD . GLN A 1 86 ? 50.786 138.719 -2.910 1.00 111.09 ? 90 GLN A CD 1 ATOM 604 O OE1 . GLN A 1 86 ? 52.002 138.918 -3.034 1.00 105.85 ? 90 GLN A OE1 1 ATOM 605 N NE2 . GLN A 1 86 ? 50.310 137.659 -2.260 1.00 108.24 ? 90 GLN A NE2 1 ATOM 606 N N . LEU A 1 87 ? 49.358 142.049 -5.948 1.00 52.12 ? 91 LEU A N 1 ATOM 607 C CA . LEU A 1 87 ? 50.395 142.978 -6.350 1.00 49.84 ? 91 LEU A CA 1 ATOM 608 C C . LEU A 1 87 ? 51.496 142.896 -5.285 1.00 54.84 ? 91 LEU A C 1 ATOM 609 O O . LEU A 1 87 ? 51.273 143.237 -4.119 1.00 55.85 ? 91 LEU A O 1 ATOM 610 C CB . LEU A 1 87 ? 49.839 144.392 -6.540 1.00 48.95 ? 91 LEU A CB 1 ATOM 611 C CG . LEU A 1 87 ? 50.805 145.420 -7.075 1.00 51.34 ? 91 LEU A CG 1 ATOM 612 C CD1 . LEU A 1 87 ? 51.464 144.939 -8.379 1.00 50.55 ? 91 LEU A CD1 1 ATOM 613 C CD2 . LEU A 1 87 ? 50.095 146.786 -7.238 1.00 52.90 ? 91 LEU A CD2 1 ATOM 614 N N . HIS A 1 88 ? 52.649 142.336 -5.688 1.00 51.12 ? 92 HIS A N 1 ATOM 615 C CA . HIS A 1 88 ? 53.807 142.031 -4.849 1.00 51.94 ? 92 HIS A CA 1 ATOM 616 C C . HIS A 1 88 ? 54.944 142.989 -5.111 1.00 52.80 ? 92 HIS A C 1 ATOM 617 O O . HIS A 1 88 ? 55.194 143.339 -6.257 1.00 50.21 ? 92 HIS A O 1 ATOM 618 C CB . HIS A 1 88 ? 54.241 140.564 -5.113 1.00 54.78 ? 92 HIS A CB 1 ATOM 619 C CG . HIS A 1 88 ? 55.520 140.122 -4.461 1.00 60.05 ? 92 HIS A CG 1 ATOM 620 N ND1 . HIS A 1 88 ? 55.570 139.757 -3.120 1.00 63.80 ? 92 HIS A ND1 1 ATOM 621 C CD2 . HIS A 1 88 ? 56.745 139.933 -5.011 1.00 62.13 ? 92 HIS A CD2 1 ATOM 622 C CE1 . HIS A 1 88 ? 56.826 139.402 -2.893 1.00 64.32 ? 92 HIS A CE1 1 ATOM 623 N NE2 . HIS A 1 88 ? 57.570 139.489 -4.002 1.00 63.70 ? 92 HIS A NE2 1 ATOM 624 N N . ASP A 1 89 ? 55.646 143.398 -4.045 1.00 50.56 ? 93 ASP A N 1 ATOM 625 C CA . ASP A 1 89 ? 56.813 144.269 -4.125 1.00 50.05 ? 93 ASP A CA 1 ATOM 626 C C . ASP A 1 89 ? 58.036 143.328 -4.181 1.00 55.34 ? 93 ASP A C 1 ATOM 627 O O . ASP A 1 89 ? 58.372 142.688 -3.182 1.00 56.25 ? 93 ASP A O 1 ATOM 628 C CB . ASP A 1 89 ? 56.874 145.222 -2.906 1.00 52.34 ? 93 ASP A CB 1 ATOM 629 C CG . ASP A 1 89 ? 57.985 146.263 -2.954 1.00 63.61 ? 93 ASP A CG 1 ATOM 630 O OD1 . ASP A 1 89 ? 58.997 146.022 -3.635 1.00 63.53 ? 93 ASP A OD1 1 ATOM 631 O OD2 . ASP A 1 89 ? 57.856 147.300 -2.270 1.00 71.64 ? 93 ASP A OD2 1 ATOM 632 N N . CYS A 1 90 ? 58.654 143.203 -5.366 1.00 52.70 ? 94 CYS A N 1 ATOM 633 C CA . CYS A 1 90 ? 59.799 142.310 -5.602 1.00 54.98 ? 94 CYS A CA 1 ATOM 634 C C . CYS A 1 90 ? 61.140 142.972 -5.418 1.00 57.54 ? 94 CYS A C 1 ATOM 635 O O . CYS A 1 90 ? 62.155 142.392 -5.821 1.00 58.41 ? 94 CYS A O 1 ATOM 636 C CB . CYS A 1 90 ? 59.713 141.641 -6.971 1.00 56.81 ? 94 CYS A CB 1 ATOM 637 S SG . CYS A 1 90 ? 59.105 142.723 -8.304 1.00 59.57 ? 94 CYS A SG 1 ATOM 638 N N . THR A 1 91 ? 61.164 144.184 -4.854 1.00 52.25 ? 95 THR A N 1 ATOM 639 C CA . THR A 1 91 ? 62.407 144.930 -4.681 1.00 51.76 ? 95 THR A CA 1 ATOM 640 C C . THR A 1 91 ? 63.472 144.153 -3.918 1.00 58.85 ? 95 THR A C 1 ATOM 641 O O . THR A 1 91 ? 63.197 143.631 -2.828 1.00 58.93 ? 95 THR A O 1 ATOM 642 C CB . THR A 1 91 ? 62.125 146.304 -4.114 1.00 48.77 ? 95 THR A CB 1 ATOM 643 O OG1 . THR A 1 91 ? 61.132 146.921 -4.914 1.00 47.80 ? 95 THR A OG1 1 ATOM 644 C CG2 . THR A 1 91 ? 63.322 147.170 -4.121 1.00 41.83 ? 95 THR A CG2 1 ATOM 645 N N . GLN A 1 92 ? 64.675 144.035 -4.551 1.00 57.61 ? 96 GLN A N 1 ATOM 646 C CA . GLN A 1 92 ? 65.867 143.391 -3.987 1.00 60.42 ? 96 GLN A CA 1 ATOM 647 C C . GLN A 1 92 ? 66.354 144.280 -2.863 1.00 62.64 ? 96 GLN A C 1 ATOM 648 O O . GLN A 1 92 ? 66.566 145.480 -3.082 1.00 60.71 ? 96 GLN A O 1 ATOM 649 C CB . GLN A 1 92 ? 66.972 143.202 -5.048 1.00 64.26 ? 96 GLN A CB 1 ATOM 650 C CG . GLN A 1 92 ? 66.664 142.082 -6.062 1.00 89.33 ? 96 GLN A CG 1 ATOM 651 C CD . GLN A 1 92 ? 67.150 140.670 -5.729 1.00 116.84 ? 96 GLN A CD 1 ATOM 652 O OE1 . GLN A 1 92 ? 68.341 140.375 -5.768 1.00 118.09 ? 96 GLN A OE1 1 ATOM 653 N NE2 . GLN A 1 92 ? 66.222 139.755 -5.465 1.00 107.75 ? 96 GLN A NE2 1 ATOM 654 N N . VAL A 1 93 ? 66.465 143.703 -1.648 1.00 59.55 ? 97 VAL A N 1 ATOM 655 C CA . VAL A 1 93 ? 66.856 144.406 -0.411 1.00 58.52 ? 97 VAL A CA 1 ATOM 656 C C . VAL A 1 93 ? 68.108 145.277 -0.504 1.00 62.77 ? 97 VAL A C 1 ATOM 657 O O . VAL A 1 93 ? 68.160 146.332 0.127 1.00 61.15 ? 97 VAL A O 1 ATOM 658 C CB . VAL A 1 93 ? 66.848 143.526 0.866 1.00 64.20 ? 97 VAL A CB 1 ATOM 659 C CG1 . VAL A 1 93 ? 65.468 142.935 1.120 1.00 64.08 ? 97 VAL A CG1 1 ATOM 660 C CG2 . VAL A 1 93 ? 67.909 142.432 0.805 1.00 67.52 ? 97 VAL A CG2 1 ATOM 661 N N . GLU A 1 94 ? 69.104 144.834 -1.283 1.00 61.64 ? 98 GLU A N 1 ATOM 662 C CA . GLU A 1 94 ? 70.381 145.528 -1.467 1.00 62.42 ? 98 GLU A CA 1 ATOM 663 C C . GLU A 1 94 ? 70.253 146.797 -2.313 1.00 63.04 ? 98 GLU A C 1 ATOM 664 O O . GLU A 1 94 ? 71.119 147.679 -2.244 1.00 62.72 ? 98 GLU A O 1 ATOM 665 C CB . GLU A 1 94 ? 71.470 144.571 -2.012 1.00 67.82 ? 98 GLU A CB 1 ATOM 666 C CG . GLU A 1 94 ? 71.211 144.026 -3.413 1.00 85.70 ? 98 GLU A CG 1 ATOM 667 C CD . GLU A 1 94 ? 70.348 142.784 -3.571 1.00 123.24 ? 98 GLU A CD 1 ATOM 668 O OE1 . GLU A 1 94 ? 69.602 142.429 -2.629 1.00 131.85 ? 98 GLU A OE1 1 ATOM 669 O OE2 . GLU A 1 94 ? 70.400 142.176 -4.666 1.00 118.70 ? 98 GLU A OE2 1 ATOM 670 N N . LYS A 1 95 ? 69.166 146.894 -3.088 1.00 57.49 ? 99 LYS A N 1 ATOM 671 C CA . LYS A 1 95 ? 68.911 148.025 -3.971 1.00 56.04 ? 99 LYS A CA 1 ATOM 672 C C . LYS A 1 95 ? 67.583 148.751 -3.646 1.00 56.88 ? 99 LYS A C 1 ATOM 673 O O . LYS A 1 95 ? 67.110 149.528 -4.475 1.00 55.73 ? 99 LYS A O 1 ATOM 674 C CB . LYS A 1 95 ? 68.921 147.533 -5.439 1.00 59.88 ? 99 LYS A CB 1 ATOM 675 C CG . LYS A 1 95 ? 70.304 147.180 -5.996 1.00 80.52 ? 99 LYS A CG 1 ATOM 676 C CD . LYS A 1 95 ? 70.328 147.060 -7.527 1.00 94.73 ? 99 LYS A CD 1 ATOM 677 C CE . LYS A 1 95 ? 69.680 145.802 -8.091 1.00 108.61 ? 99 LYS A CE 1 ATOM 678 N NZ . LYS A 1 95 ? 70.511 144.593 -7.879 1.00 120.31 ? 99 LYS A NZ 1 ATOM 679 N N . ALA A 1 96 ? 66.994 148.499 -2.449 1.00 51.91 ? 100 ALA A N 1 ATOM 680 C CA . ALA A 1 96 ? 65.691 149.028 -1.994 1.00 49.75 ? 100 ALA A CA 1 ATOM 681 C C . ALA A 1 96 ? 65.568 150.548 -1.887 1.00 52.20 ? 100 ALA A C 1 ATOM 682 O O . ALA A 1 96 ? 64.459 151.101 -1.967 1.00 51.19 ? 100 ALA A O 1 ATOM 683 C CB . ALA A 1 96 ? 65.308 148.386 -0.668 1.00 50.85 ? 100 ALA A CB 1 ATOM 684 N N . ASP A 1 97 ? 66.698 151.206 -1.663 1.00 48.38 ? 101 ASP A N 1 ATOM 685 C CA . ASP A 1 97 ? 66.780 152.635 -1.501 1.00 48.22 ? 101 ASP A CA 1 ATOM 686 C C . ASP A 1 97 ? 66.718 153.402 -2.818 1.00 53.21 ? 101 ASP A C 1 ATOM 687 O O . ASP A 1 97 ? 66.509 154.608 -2.796 1.00 52.59 ? 101 ASP A O 1 ATOM 688 C CB . ASP A 1 97 ? 68.078 152.968 -0.742 1.00 51.07 ? 101 ASP A CB 1 ATOM 689 C CG . ASP A 1 97 ? 69.393 152.643 -1.472 1.00 64.33 ? 101 ASP A CG 1 ATOM 690 O OD1 . ASP A 1 97 ? 69.447 151.610 -2.191 1.00 64.81 ? 101 ASP A OD1 1 ATOM 691 O OD2 . ASP A 1 97 ? 70.370 153.403 -1.301 1.00 72.61 ? 101 ASP A OD2 1 ATOM 692 N N . THR A 1 98 ? 66.951 152.733 -3.963 1.00 51.82 ? 102 THR A N 1 ATOM 693 C CA . THR A 1 98 ? 66.985 153.406 -5.274 1.00 53.47 ? 102 THR A CA 1 ATOM 694 C C . THR A 1 98 ? 66.153 152.715 -6.354 1.00 59.07 ? 102 THR A C 1 ATOM 695 O O . THR A 1 98 ? 66.178 153.142 -7.512 1.00 60.96 ? 102 THR A O 1 ATOM 696 C CB . THR A 1 98 ? 68.437 153.545 -5.765 1.00 62.53 ? 102 THR A CB 1 ATOM 697 O OG1 . THR A 1 98 ? 68.955 152.243 -6.064 1.00 64.00 ? 102 THR A OG1 1 ATOM 698 C CG2 . THR A 1 98 ? 69.340 154.273 -4.775 1.00 60.73 ? 102 THR A CG2 1 ATOM 699 N N . THR A 1 99 ? 65.480 151.617 -6.007 1.00 54.90 ? 103 THR A N 1 ATOM 700 C CA . THR A 1 99 ? 64.707 150.858 -6.980 1.00 55.18 ? 103 THR A CA 1 ATOM 701 C C . THR A 1 99 ? 63.358 150.438 -6.442 1.00 57.24 ? 103 THR A C 1 ATOM 702 O O . THR A 1 99 ? 63.173 150.303 -5.230 1.00 56.63 ? 103 THR A O 1 ATOM 703 C CB . THR A 1 99 ? 65.463 149.587 -7.462 1.00 69.67 ? 103 THR A CB 1 ATOM 704 O OG1 . THR A 1 99 ? 65.449 148.592 -6.428 1.00 74.37 ? 103 THR A OG1 1 ATOM 705 C CG2 . THR A 1 99 ? 66.878 149.866 -7.981 1.00 70.04 ? 103 THR A CG2 1 ATOM 706 N N . ILE A 1 100 ? 62.434 150.171 -7.361 1.00 52.69 ? 104 ILE A N 1 ATOM 707 C CA . ILE A 1 100 ? 61.116 149.629 -7.088 1.00 50.72 ? 104 ILE A CA 1 ATOM 708 C C . ILE A 1 100 ? 60.930 148.513 -8.124 1.00 54.17 ? 104 ILE A C 1 ATOM 709 O O . ILE A 1 100 ? 61.179 148.701 -9.309 1.00 54.06 ? 104 ILE A O 1 ATOM 710 C CB . ILE A 1 100 ? 59.969 150.693 -7.150 1.00 53.75 ? 104 ILE A CB 1 ATOM 711 C CG1 . ILE A 1 100 ? 59.969 151.638 -5.936 1.00 54.16 ? 104 ILE A CG1 1 ATOM 712 C CG2 . ILE A 1 100 ? 58.590 150.047 -7.274 1.00 53.38 ? 104 ILE A CG2 1 ATOM 713 C CD1 . ILE A 1 100 ? 58.986 152.910 -6.119 1.00 67.07 ? 104 ILE A CD1 1 ATOM 714 N N . CYS A 1 101 ? 60.516 147.358 -7.663 1.00 51.68 ? 105 CYS A N 1 ATOM 715 C CA . CYS A 1 101 ? 60.152 146.228 -8.496 1.00 52.66 ? 105 CYS A CA 1 ATOM 716 C C . CYS A 1 101 ? 58.755 145.849 -8.039 1.00 54.57 ? 105 CYS A C 1 ATOM 717 O O . CYS A 1 101 ? 58.557 145.603 -6.849 1.00 54.11 ? 105 CYS A O 1 ATOM 718 C CB . CYS A 1 101 ? 61.136 145.074 -8.341 1.00 55.01 ? 105 CYS A CB 1 ATOM 719 S SG . CYS A 1 101 ? 60.700 143.578 -9.266 1.00 60.74 ? 105 CYS A SG 1 ATOM 720 N N . LEU A 1 102 ? 57.781 145.865 -8.959 1.00 49.75 ? 106 LEU A N 1 ATOM 721 C CA . LEU A 1 102 ? 56.399 145.481 -8.678 1.00 48.97 ? 106 LEU A CA 1 ATOM 722 C C . LEU A 1 102 ? 56.016 144.421 -9.653 1.00 54.53 ? 106 LEU A C 1 ATOM 723 O O . LEU A 1 102 ? 56.363 144.500 -10.832 1.00 56.11 ? 106 LEU A O 1 ATOM 724 C CB . LEU A 1 102 ? 55.414 146.638 -8.773 1.00 48.71 ? 106 LEU A CB 1 ATOM 725 C CG . LEU A 1 102 ? 55.620 147.809 -7.853 1.00 54.19 ? 106 LEU A CG 1 ATOM 726 C CD1 . LEU A 1 102 ? 54.720 148.941 -8.276 1.00 55.40 ? 106 LEU A CD1 1 ATOM 727 C CD2 . LEU A 1 102 ? 55.477 147.432 -6.328 1.00 57.42 ? 106 LEU A CD2 1 ATOM 728 N N . LYS A 1 103 ? 55.312 143.416 -9.164 1.00 50.82 ? 107 LYS A N 1 ATOM 729 C CA . LYS A 1 103 ? 54.954 142.252 -9.948 1.00 51.01 ? 107 LYS A CA 1 ATOM 730 C C . LYS A 1 103 ? 53.615 141.739 -9.491 1.00 55.66 ? 107 LYS A C 1 ATOM 731 O O . LYS A 1 103 ? 53.381 141.612 -8.284 1.00 56.09 ? 107 LYS A O 1 ATOM 732 C CB . LYS A 1 103 ? 56.042 141.183 -9.697 1.00 54.45 ? 107 LYS A CB 1 ATOM 733 C CG . LYS A 1 103 ? 55.915 139.848 -10.414 1.00 68.15 ? 107 LYS A CG 1 ATOM 734 C CD . LYS A 1 103 ? 56.462 138.717 -9.553 1.00 78.79 ? 107 LYS A CD 1 ATOM 735 C CE . LYS A 1 103 ? 57.970 138.624 -9.481 1.00 86.05 ? 107 LYS A CE 1 ATOM 736 N NZ . LYS A 1 103 ? 58.523 137.726 -10.531 1.00 89.42 ? 107 LYS A NZ 1 ATOM 737 N N . TRP A 1 104 ? 52.745 141.396 -10.437 1.00 52.21 ? 108 TRP A N 1 ATOM 738 C CA . TRP A 1 104 ? 51.489 140.772 -10.048 1.00 52.38 ? 108 TRP A CA 1 ATOM 739 C C . TRP A 1 104 ? 51.765 139.281 -9.910 1.00 57.69 ? 108 TRP A C 1 ATOM 740 O O . TRP A 1 104 ? 52.412 138.688 -10.776 1.00 57.16 ? 108 TRP A O 1 ATOM 741 C CB . TRP A 1 104 ? 50.385 141.001 -11.073 1.00 50.52 ? 108 TRP A CB 1 ATOM 742 C CG . TRP A 1 104 ? 49.684 142.330 -10.992 1.00 50.50 ? 108 TRP A CG 1 ATOM 743 C CD1 . TRP A 1 104 ? 49.930 143.423 -11.764 1.00 53.09 ? 108 TRP A CD1 1 ATOM 744 C CD2 . TRP A 1 104 ? 48.564 142.672 -10.154 1.00 50.60 ? 108 TRP A CD2 1 ATOM 745 N NE1 . TRP A 1 104 ? 49.022 144.419 -11.483 1.00 52.56 ? 108 TRP A NE1 1 ATOM 746 C CE2 . TRP A 1 104 ? 48.173 143.990 -10.495 1.00 54.36 ? 108 TRP A CE2 1 ATOM 747 C CE3 . TRP A 1 104 ? 47.856 141.996 -9.141 1.00 52.75 ? 108 TRP A CE3 1 ATOM 748 C CZ2 . TRP A 1 104 ? 47.089 144.646 -9.873 1.00 54.69 ? 108 TRP A CZ2 1 ATOM 749 C CZ3 . TRP A 1 104 ? 46.783 142.639 -8.526 1.00 55.12 ? 108 TRP A CZ3 1 ATOM 750 C CH2 . TRP A 1 104 ? 46.402 143.948 -8.896 1.00 55.73 ? 108 TRP A CH2 1 ATOM 751 N N . LYS A 1 105 ? 51.332 138.695 -8.800 1.00 56.63 ? 109 LYS A N 1 ATOM 752 C CA . LYS A 1 105 ? 51.496 137.270 -8.546 1.00 59.50 ? 109 LYS A CA 1 ATOM 753 C C . LYS A 1 105 ? 50.167 136.554 -8.710 1.00 65.75 ? 109 LYS A C 1 ATOM 754 O O . LYS A 1 105 ? 49.124 137.064 -8.287 1.00 65.91 ? 109 LYS A O 1 ATOM 755 C CB . LYS A 1 105 ? 52.071 137.008 -7.146 1.00 63.95 ? 109 LYS A CB 1 ATOM 756 C CG . LYS A 1 105 ? 53.573 137.272 -7.026 1.00 80.37 ? 109 LYS A CG 1 ATOM 757 C CD . LYS A 1 105 ? 54.439 136.106 -7.616 1.00 93.84 ? 109 LYS A CD 1 ATOM 758 C CE . LYS A 1 105 ? 55.883 135.921 -7.202 1.00 106.14 ? 109 LYS A CE 1 ATOM 759 N NZ . LYS A 1 105 ? 56.043 135.368 -5.822 1.00 116.85 ? 109 LYS A NZ 1 ATOM 760 N N . ASN A 1 106 ? 50.215 135.379 -9.343 1.00 63.44 ? 110 ASN A N 1 ATOM 761 C CA . ASN A 1 106 ? 49.083 134.494 -9.539 1.00 64.43 ? 110 ASN A CA 1 ATOM 762 C C . ASN A 1 106 ? 49.090 133.572 -8.296 1.00 71.34 ? 110 ASN A C 1 ATOM 763 O O . ASN A 1 106 ? 49.833 132.588 -8.281 1.00 73.04 ? 110 ASN A O 1 ATOM 764 C CB . ASN A 1 106 ? 49.306 133.718 -10.858 1.00 66.20 ? 110 ASN A CB 1 ATOM 765 C CG . ASN A 1 106 ? 48.444 132.495 -11.127 1.00 91.92 ? 110 ASN A CG 1 ATOM 766 O OD1 . ASN A 1 106 ? 48.920 131.473 -11.647 1.00 94.97 ? 110 ASN A OD1 1 ATOM 767 N ND2 . ASN A 1 106 ? 47.153 132.580 -10.839 1.00 77.62 ? 110 ASN A ND2 1 ATOM 768 N N . ILE A 1 107 ? 48.336 133.943 -7.224 1.00 68.81 ? 111 ILE A N 1 ATOM 769 C CA . ILE A 1 107 ? 48.316 133.204 -5.943 1.00 72.41 ? 111 ILE A CA 1 ATOM 770 C C . ILE A 1 107 ? 47.491 131.909 -5.897 1.00 79.83 ? 111 ILE A C 1 ATOM 771 O O . ILE A 1 107 ? 47.697 131.083 -5.000 1.00 83.15 ? 111 ILE A O 1 ATOM 772 C CB . ILE A 1 107 ? 48.139 134.101 -4.688 1.00 75.63 ? 111 ILE A CB 1 ATOM 773 C CG1 . ILE A 1 107 ? 46.745 134.776 -4.636 1.00 75.56 ? 111 ILE A CG1 1 ATOM 774 C CG2 . ILE A 1 107 ? 49.288 135.113 -4.579 1.00 73.64 ? 111 ILE A CG2 1 ATOM 775 C CD1 . ILE A 1 107 ? 46.187 134.964 -3.217 1.00 87.69 ? 111 ILE A CD1 1 ATOM 776 N N . GLU A 1 108 ? 46.574 131.732 -6.864 1.00 74.91 ? 112 GLU A N 1 ATOM 777 C CA . GLU A 1 108 ? 45.741 130.543 -6.994 1.00 77.64 ? 112 GLU A CA 1 ATOM 778 C C . GLU A 1 108 ? 45.480 130.307 -8.468 1.00 78.88 ? 112 GLU A C 1 ATOM 779 O O . GLU A 1 108 ? 45.393 131.264 -9.235 1.00 75.33 ? 112 GLU A O 1 ATOM 780 C CB . GLU A 1 108 ? 44.415 130.707 -6.242 1.00 80.65 ? 112 GLU A CB 1 ATOM 781 C CG . GLU A 1 108 ? 43.844 129.386 -5.751 1.00 100.54 ? 112 GLU A CG 1 ATOM 782 C CD . GLU A 1 108 ? 42.380 129.384 -5.348 1.00 132.78 ? 112 GLU A CD 1 ATOM 783 O OE1 . GLU A 1 108 ? 41.886 130.426 -4.859 1.00 131.18 ? 112 GLU A OE1 1 ATOM 784 O OE2 . GLU A 1 108 ? 41.721 128.335 -5.534 1.00 131.67 ? 112 GLU A OE2 1 ATOM 785 N N . THR A 1 109 ? 45.362 129.046 -8.868 1.00 77.48 ? 113 THR A N 1 ATOM 786 C CA . THR A 1 109 ? 45.095 128.690 -10.260 1.00 75.82 ? 113 THR A CA 1 ATOM 787 C C . THR A 1 109 ? 43.683 129.099 -10.706 1.00 76.88 ? 113 THR A C 1 ATOM 788 O O . THR A 1 109 ? 42.769 129.156 -9.885 1.00 77.32 ? 113 THR A O 1 ATOM 789 C CB . THR A 1 109 ? 45.433 127.203 -10.515 1.00 86.68 ? 113 THR A CB 1 ATOM 790 O OG1 . THR A 1 109 ? 45.138 126.859 -11.867 1.00 87.23 ? 113 THR A OG1 1 ATOM 791 C CG2 . THR A 1 109 ? 44.743 126.241 -9.534 1.00 87.65 ? 113 THR A CG2 1 ATOM 792 N N . PHE A 1 110 ? 43.531 129.398 -12.003 1.00 70.17 ? 114 PHE A N 1 ATOM 793 C CA . PHE A 1 110 ? 42.258 129.720 -12.636 1.00 67.99 ? 114 PHE A CA 1 ATOM 794 C C . PHE A 1 110 ? 42.263 129.092 -14.019 1.00 73.35 ? 114 PHE A C 1 ATOM 795 O O . PHE A 1 110 ? 43.337 128.846 -14.572 1.00 73.85 ? 114 PHE A O 1 ATOM 796 C CB . PHE A 1 110 ? 41.997 131.233 -12.693 1.00 65.65 ? 114 PHE A CB 1 ATOM 797 C CG . PHE A 1 110 ? 43.115 132.050 -13.285 1.00 64.02 ? 114 PHE A CG 1 ATOM 798 C CD1 . PHE A 1 110 ? 43.254 132.184 -14.661 1.00 64.77 ? 114 PHE A CD1 1 ATOM 799 C CD2 . PHE A 1 110 ? 44.022 132.692 -12.474 1.00 65.44 ? 114 PHE A CD2 1 ATOM 800 C CE1 . PHE A 1 110 ? 44.297 132.930 -15.209 1.00 63.84 ? 114 PHE A CE1 1 ATOM 801 C CE2 . PHE A 1 110 ? 45.042 133.459 -13.027 1.00 66.36 ? 114 PHE A CE2 1 ATOM 802 C CZ . PHE A 1 110 ? 45.174 133.577 -14.389 1.00 62.94 ? 114 PHE A CZ 1 ATOM 803 N N . THR A 1 111 ? 41.076 128.834 -14.574 1.00 70.20 ? 115 THR A N 1 ATOM 804 C CA . THR A 1 111 ? 40.934 128.177 -15.868 1.00 70.89 ? 115 THR A CA 1 ATOM 805 C C . THR A 1 111 ? 41.002 129.092 -17.087 1.00 74.49 ? 115 THR A C 1 ATOM 806 O O . THR A 1 111 ? 41.270 128.595 -18.180 1.00 74.72 ? 115 THR A O 1 ATOM 807 C CB . THR A 1 111 ? 39.740 127.237 -15.859 1.00 78.57 ? 115 THR A CB 1 ATOM 808 O OG1 . THR A 1 111 ? 38.555 127.997 -15.638 1.00 75.20 ? 115 THR A OG1 1 ATOM 809 C CG2 . THR A 1 111 ? 39.868 126.145 -14.808 1.00 81.13 ? 115 THR A CG2 1 ATOM 810 N N . CYS A 1 112 ? 40.786 130.418 -16.914 1.00 71.07 ? 116 CYS A N 1 ATOM 811 C CA . CYS A 1 112 ? 40.869 131.402 -18.005 1.00 70.35 ? 116 CYS A CA 1 ATOM 812 C C . CYS A 1 112 ? 42.234 131.263 -18.687 1.00 75.46 ? 116 CYS A C 1 ATOM 813 O O . CYS A 1 112 ? 43.223 130.939 -18.024 1.00 75.24 ? 116 CYS A O 1 ATOM 814 C CB . CYS A 1 112 ? 40.669 132.833 -17.493 1.00 69.48 ? 116 CYS A CB 1 ATOM 815 S SG . CYS A 1 112 ? 38.992 133.230 -16.922 1.00 73.87 ? 116 CYS A SG 1 ATOM 816 N N . ASP A 1 113 ? 42.285 131.493 -20.006 1.00 73.68 ? 117 ASP A N 1 ATOM 817 C CA . ASP A 1 113 ? 43.539 131.458 -20.755 1.00 75.03 ? 117 ASP A CA 1 ATOM 818 C C . ASP A 1 113 ? 44.316 132.742 -20.404 1.00 76.71 ? 117 ASP A C 1 ATOM 819 O O . ASP A 1 113 ? 43.744 133.837 -20.426 1.00 74.87 ? 117 ASP A O 1 ATOM 820 C CB . ASP A 1 113 ? 43.267 131.365 -22.271 1.00 78.38 ? 117 ASP A CB 1 ATOM 821 C CG . ASP A 1 113 ? 44.452 130.944 -23.137 1.00 96.07 ? 117 ASP A CG 1 ATOM 822 O OD1 . ASP A 1 113 ? 45.599 131.369 -22.837 1.00 97.29 ? 117 ASP A OD1 1 ATOM 823 O OD2 . ASP A 1 113 ? 44.231 130.216 -24.131 1.00 105.06 ? 117 ASP A OD2 1 ATOM 824 N N . THR A 1 114 ? 45.594 132.593 -20.031 1.00 73.31 ? 118 THR A N 1 ATOM 825 C CA . THR A 1 114 ? 46.447 133.719 -19.641 1.00 71.66 ? 118 THR A CA 1 ATOM 826 C C . THR A 1 114 ? 46.818 134.650 -20.801 1.00 75.63 ? 118 THR A C 1 ATOM 827 O O . THR A 1 114 ? 47.134 135.822 -20.556 1.00 74.13 ? 118 THR A O 1 ATOM 828 C CB . THR A 1 114 ? 47.649 133.248 -18.823 1.00 79.94 ? 118 THR A CB 1 ATOM 829 O OG1 . THR A 1 114 ? 48.267 132.137 -19.473 1.00 80.97 ? 118 THR A OG1 1 ATOM 830 C CG2 . THR A 1 114 ? 47.271 132.873 -17.407 1.00 79.08 ? 118 THR A CG2 1 ATOM 831 N N . GLN A 1 115 ? 46.733 134.153 -22.062 1.00 73.17 ? 119 GLN A N 1 ATOM 832 C CA . GLN A 1 115 ? 47.041 134.949 -23.251 1.00 73.61 ? 119 GLN A CA 1 ATOM 833 C C . GLN A 1 115 ? 46.100 136.146 -23.407 1.00 74.39 ? 119 GLN A C 1 ATOM 834 O O . GLN A 1 115 ? 46.435 137.095 -24.120 1.00 75.25 ? 119 GLN A O 1 ATOM 835 C CB . GLN A 1 115 ? 47.111 134.085 -24.532 1.00 78.18 ? 119 GLN A CB 1 ATOM 836 C CG . GLN A 1 115 ? 45.766 133.775 -25.200 1.00 97.02 ? 119 GLN A CG 1 ATOM 837 C CD . GLN A 1 115 ? 45.912 133.226 -26.599 1.00 119.98 ? 119 GLN A CD 1 ATOM 838 O OE1 . GLN A 1 115 ? 46.360 132.094 -26.807 1.00 119.04 ? 119 GLN A OE1 1 ATOM 839 N NE2 . GLN A 1 115 ? 45.491 134.003 -27.588 1.00 111.50 ? 119 GLN A NE2 1 ATOM 840 N N . ASN A 1 116 ? 44.937 136.105 -22.733 1.00 67.79 ? 120 ASN A N 1 ATOM 841 C CA . ASN A 1 116 ? 43.959 137.186 -22.783 1.00 66.51 ? 120 ASN A CA 1 ATOM 842 C C . ASN A 1 116 ? 44.038 138.093 -21.539 1.00 67.74 ? 120 ASN A C 1 ATOM 843 O O . ASN A 1 116 ? 43.250 139.036 -21.403 1.00 66.96 ? 120 ASN A O 1 ATOM 844 C CB . ASN A 1 116 ? 42.547 136.647 -23.029 1.00 69.18 ? 120 ASN A CB 1 ATOM 845 C CG . ASN A 1 116 ? 42.463 135.381 -23.865 1.00 102.04 ? 120 ASN A CG 1 ATOM 846 O OD1 . ASN A 1 116 ? 42.345 134.299 -23.306 1.00 99.93 ? 120 ASN A OD1 1 ATOM 847 N ND2 . ASN A 1 116 ? 42.522 135.450 -25.207 1.00 96.20 ? 120 ASN A ND2 1 ATOM 848 N N . ILE A 1 117 ? 45.033 137.833 -20.670 1.00 62.89 ? 121 ILE A N 1 ATOM 849 C CA . ILE A 1 117 ? 45.282 138.604 -19.456 1.00 60.73 ? 121 ILE A CA 1 ATOM 850 C C . ILE A 1 117 ? 46.422 139.608 -19.673 1.00 65.33 ? 121 ILE A C 1 ATOM 851 O O . ILE A 1 117 ? 47.538 139.212 -20.024 1.00 66.50 ? 121 ILE A O 1 ATOM 852 C CB . ILE A 1 117 ? 45.486 137.681 -18.232 1.00 63.00 ? 121 ILE A CB 1 ATOM 853 C CG1 . ILE A 1 117 ? 44.203 136.855 -17.982 1.00 63.37 ? 121 ILE A CG1 1 ATOM 854 C CG2 . ILE A 1 117 ? 45.906 138.484 -17.005 1.00 63.36 ? 121 ILE A CG2 1 ATOM 855 C CD1 . ILE A 1 117 ? 44.073 136.174 -16.685 1.00 70.08 ? 121 ILE A CD1 1 ATOM 856 N N . THR A 1 118 ? 46.120 140.910 -19.501 1.00 60.71 ? 122 THR A N 1 ATOM 857 C CA . THR A 1 118 ? 47.098 141.995 -19.642 1.00 60.49 ? 122 THR A CA 1 ATOM 858 C C . THR A 1 118 ? 47.210 142.869 -18.364 1.00 62.45 ? 122 THR A C 1 ATOM 859 O O . THR A 1 118 ? 46.207 143.170 -17.712 1.00 61.43 ? 122 THR A O 1 ATOM 860 C CB . THR A 1 118 ? 46.952 142.739 -20.979 1.00 68.26 ? 122 THR A CB 1 ATOM 861 O OG1 . THR A 1 118 ? 45.648 143.297 -21.075 1.00 64.74 ? 122 THR A OG1 1 ATOM 862 C CG2 . THR A 1 118 ? 47.213 141.838 -22.193 1.00 68.27 ? 122 THR A CG2 1 ATOM 863 N N . TYR A 1 119 ? 48.436 143.228 -17.987 1.00 58.53 ? 123 TYR A N 1 ATOM 864 C CA . TYR A 1 119 ? 48.716 143.995 -16.774 1.00 57.41 ? 123 TYR A CA 1 ATOM 865 C C . TYR A 1 119 ? 49.230 145.376 -17.160 1.00 64.38 ? 123 TYR A C 1 ATOM 866 O O . TYR A 1 119 ? 50.098 145.477 -18.023 1.00 65.58 ? 123 TYR A O 1 ATOM 867 C CB . TYR A 1 119 ? 49.766 143.256 -15.934 1.00 57.31 ? 123 TYR A CB 1 ATOM 868 C CG . TYR A 1 119 ? 49.422 141.810 -15.637 1.00 58.41 ? 123 TYR A CG 1 ATOM 869 C CD1 . TYR A 1 119 ? 49.756 140.791 -16.529 1.00 61.36 ? 123 TYR A CD1 1 ATOM 870 C CD2 . TYR A 1 119 ? 48.787 141.455 -14.454 1.00 58.48 ? 123 TYR A CD2 1 ATOM 871 C CE1 . TYR A 1 119 ? 49.466 139.454 -16.245 1.00 62.11 ? 123 TYR A CE1 1 ATOM 872 C CE2 . TYR A 1 119 ? 48.489 140.123 -14.161 1.00 59.77 ? 123 TYR A CE2 1 ATOM 873 C CZ . TYR A 1 119 ? 48.843 139.123 -15.052 1.00 67.25 ? 123 TYR A CZ 1 ATOM 874 O OH . TYR A 1 119 ? 48.553 137.809 -14.761 1.00 68.17 ? 123 TYR A OH 1 ATOM 875 N N . ARG A 1 120 ? 48.688 146.435 -16.546 1.00 62.12 ? 124 ARG A N 1 ATOM 876 C CA . ARG A 1 120 ? 49.118 147.808 -16.827 1.00 64.07 ? 124 ARG A CA 1 ATOM 877 C C . ARG A 1 120 ? 49.510 148.529 -15.540 1.00 67.85 ? 124 ARG A C 1 ATOM 878 O O . ARG A 1 120 ? 48.877 148.312 -14.509 1.00 66.82 ? 124 ARG A O 1 ATOM 879 C CB . ARG A 1 120 ? 48.036 148.602 -17.567 1.00 67.51 ? 124 ARG A CB 1 ATOM 880 C CG . ARG A 1 120 ? 47.555 147.970 -18.882 1.00 86.14 ? 124 ARG A CG 1 ATOM 881 C CD . ARG A 1 120 ? 46.447 148.800 -19.527 1.00 108.84 ? 124 ARG A CD 1 ATOM 882 N NE . ARG A 1 120 ? 46.942 150.081 -20.052 1.00 129.91 ? 124 ARG A NE 1 ATOM 883 C CZ . ARG A 1 120 ? 46.629 151.277 -19.558 1.00 152.54 ? 124 ARG A CZ 1 ATOM 884 N NH1 . ARG A 1 120 ? 45.801 151.381 -18.524 1.00 140.94 ? 124 ARG A NH1 1 ATOM 885 N NH2 . ARG A 1 120 ? 47.131 152.379 -20.101 1.00 146.09 ? 124 ARG A NH2 1 ATOM 886 N N . PHE A 1 121 ? 50.550 149.377 -15.594 1.00 64.96 ? 125 PHE A N 1 ATOM 887 C CA . PHE A 1 121 ? 51.023 150.138 -14.431 1.00 63.97 ? 125 PHE A CA 1 ATOM 888 C C . PHE A 1 121 ? 51.222 151.578 -14.800 1.00 70.35 ? 125 PHE A C 1 ATOM 889 O O . PHE A 1 121 ? 51.593 151.870 -15.933 1.00 71.61 ? 125 PHE A O 1 ATOM 890 C CB . PHE A 1 121 ? 52.375 149.612 -13.938 1.00 64.25 ? 125 PHE A CB 1 ATOM 891 C CG . PHE A 1 121 ? 52.382 148.252 -13.290 1.00 63.70 ? 125 PHE A CG 1 ATOM 892 C CD1 . PHE A 1 121 ? 52.451 147.099 -14.064 1.00 67.56 ? 125 PHE A CD1 1 ATOM 893 C CD2 . PHE A 1 121 ? 52.370 148.122 -11.903 1.00 64.34 ? 125 PHE A CD2 1 ATOM 894 C CE1 . PHE A 1 121 ? 52.492 145.837 -13.463 1.00 67.48 ? 125 PHE A CE1 1 ATOM 895 C CE2 . PHE A 1 121 ? 52.405 146.861 -11.300 1.00 66.47 ? 125 PHE A CE2 1 ATOM 896 C CZ . PHE A 1 121 ? 52.487 145.727 -12.084 1.00 65.16 ? 125 PHE A CZ 1 ATOM 897 N N . GLN A 1 122 ? 51.038 152.475 -13.822 1.00 68.43 ? 126 GLN A N 1 ATOM 898 C CA . GLN A 1 122 ? 51.271 153.916 -13.951 1.00 71.97 ? 126 GLN A CA 1 ATOM 899 C C . GLN A 1 122 ? 51.991 154.368 -12.682 1.00 76.52 ? 126 GLN A C 1 ATOM 900 O O . GLN A 1 122 ? 51.438 154.313 -11.581 1.00 75.25 ? 126 GLN A O 1 ATOM 901 C CB . GLN A 1 122 ? 49.974 154.709 -14.209 1.00 76.42 ? 126 GLN A CB 1 ATOM 902 C CG . GLN A 1 122 ? 49.033 154.090 -15.257 1.00 98.71 ? 126 GLN A CG 1 ATOM 903 C CD . GLN A 1 122 ? 47.778 154.883 -15.523 1.00 126.30 ? 126 GLN A CD 1 ATOM 904 O OE1 . GLN A 1 122 ? 47.151 155.425 -14.612 1.00 124.63 ? 126 GLN A OE1 1 ATOM 905 N NE2 . GLN A 1 122 ? 47.354 154.917 -16.783 1.00 120.30 ? 126 GLN A NE2 1 ATOM 906 N N . CYS A 1 123 ? 53.265 154.719 -12.829 1.00 74.99 ? 127 CYS A N 1 ATOM 907 C CA . CYS A 1 123 ? 53.997 155.128 -11.662 1.00 75.21 ? 127 CYS A CA 1 ATOM 908 C C . CYS A 1 123 ? 54.000 156.612 -11.344 1.00 84.84 ? 127 CYS A C 1 ATOM 909 O O . CYS A 1 123 ? 53.148 157.017 -10.554 1.00 85.60 ? 127 CYS A O 1 ATOM 910 C CB . CYS A 1 123 ? 55.312 154.377 -11.457 1.00 73.55 ? 127 CYS A CB 1 ATOM 911 S SG . CYS A 1 123 ? 55.056 152.681 -10.845 1.00 73.83 ? 127 CYS A SG 1 ATOM 912 N N . GLY A 1 124 ? 54.784 157.420 -12.027 1.00 85.11 ? 128 GLY A N 1 ATOM 913 C CA . GLY A 1 124 ? 54.629 158.862 -11.916 1.00 89.14 ? 128 GLY A CA 1 ATOM 914 C C . GLY A 1 124 ? 53.582 159.106 -12.980 1.00 96.95 ? 128 GLY A C 1 ATOM 915 O O . GLY A 1 124 ? 52.392 158.834 -12.782 1.00 96.25 ? 128 GLY A O 1 ATOM 916 N N . ASN A 1 125 ? 54.069 159.434 -14.185 1.00 97.32 ? 129 ASN A N 1 ATOM 917 C CA . ASN A 1 125 ? 53.271 159.579 -15.406 1.00 100.94 ? 129 ASN A CA 1 ATOM 918 C C . ASN A 1 125 ? 53.663 158.510 -16.446 1.00 104.99 ? 129 ASN A C 1 ATOM 919 O O . ASN A 1 125 ? 53.129 158.522 -17.555 1.00 107.53 ? 129 ASN A O 1 ATOM 920 C CB . ASN A 1 125 ? 53.416 160.988 -15.991 1.00 106.32 ? 129 ASN A CB 1 ATOM 921 C CG . ASN A 1 125 ? 52.760 162.065 -15.168 1.00 128.82 ? 129 ASN A CG 1 ATOM 922 O OD1 . ASN A 1 125 ? 51.728 161.860 -14.516 1.00 122.64 ? 129 ASN A OD1 1 ATOM 923 N ND2 . ASN A 1 125 ? 53.328 163.257 -15.213 1.00 123.30 ? 129 ASN A ND2 1 ATOM 924 N N . MET A 1 126 ? 54.590 157.586 -16.074 1.00 98.51 ? 130 MET A N 1 ATOM 925 C CA . MET A 1 126 ? 55.087 156.514 -16.936 1.00 97.33 ? 130 MET A CA 1 ATOM 926 C C . MET A 1 126 ? 54.085 155.374 -16.938 1.00 95.25 ? 130 MET A C 1 ATOM 927 O O . MET A 1 126 ? 53.669 154.923 -15.873 1.00 91.78 ? 130 MET A O 1 ATOM 928 C CB . MET A 1 126 ? 56.462 156.008 -16.460 1.00 98.01 ? 130 MET A CB 1 ATOM 929 C CG . MET A 1 126 ? 57.594 156.966 -16.726 1.00 106.15 ? 130 MET A CG 1 ATOM 930 S SD . MET A 1 126 ? 58.821 156.154 -17.764 1.00 112.79 ? 130 MET A SD 1 ATOM 931 C CE . MET A 1 126 ? 58.230 156.605 -19.378 1.00 115.13 ? 130 MET A CE 1 ATOM 932 N N . ILE A 1 127 ? 53.702 154.910 -18.130 1.00 91.10 ? 131 ILE A N 1 ATOM 933 C CA . ILE A 1 127 ? 52.766 153.805 -18.305 1.00 87.78 ? 131 ILE A CA 1 ATOM 934 C C . ILE A 1 127 ? 53.489 152.579 -18.833 1.00 88.11 ? 131 ILE A C 1 ATOM 935 O O . ILE A 1 127 ? 54.211 152.657 -19.823 1.00 90.55 ? 131 ILE A O 1 ATOM 936 C CB . ILE A 1 127 ? 51.503 154.208 -19.123 1.00 93.92 ? 131 ILE A CB 1 ATOM 937 C CG1 . ILE A 1 127 ? 50.763 155.349 -18.384 1.00 96.08 ? 131 ILE A CG1 1 ATOM 938 C CG2 . ILE A 1 127 ? 50.550 152.994 -19.370 1.00 91.71 ? 131 ILE A CG2 1 ATOM 939 C CD1 . ILE A 1 127 ? 49.900 156.195 -19.219 1.00 109.77 ? 131 ILE A CD1 1 ATOM 940 N N . PHE A 1 128 ? 53.311 151.459 -18.136 1.00 79.04 ? 132 PHE A N 1 ATOM 941 C CA . PHE A 1 128 ? 53.926 150.185 -18.470 1.00 76.78 ? 132 PHE A CA 1 ATOM 942 C C . PHE A 1 128 ? 52.872 149.140 -18.797 1.00 77.74 ? 132 PHE A C 1 ATOM 943 O O . PHE A 1 128 ? 51.787 149.161 -18.224 1.00 76.04 ? 132 PHE A O 1 ATOM 944 C CB . PHE A 1 128 ? 54.769 149.691 -17.290 1.00 75.68 ? 132 PHE A CB 1 ATOM 945 C CG . PHE A 1 128 ? 55.850 150.639 -16.826 1.00 78.01 ? 132 PHE A CG 1 ATOM 946 C CD1 . PHE A 1 128 ? 57.040 150.769 -17.537 1.00 83.71 ? 132 PHE A CD1 1 ATOM 947 C CD2 . PHE A 1 128 ? 55.679 151.406 -15.683 1.00 78.79 ? 132 PHE A CD2 1 ATOM 948 C CE1 . PHE A 1 128 ? 58.036 151.654 -17.110 1.00 85.81 ? 132 PHE A CE1 1 ATOM 949 C CE2 . PHE A 1 128 ? 56.680 152.279 -15.249 1.00 82.66 ? 132 PHE A CE2 1 ATOM 950 C CZ . PHE A 1 128 ? 57.854 152.392 -15.962 1.00 83.24 ? 132 PHE A CZ 1 ATOM 951 N N . ASP A 1 129 ? 53.206 148.209 -19.699 1.00 74.13 ? 133 ASP A N 1 ATOM 952 C CA . ASP A 1 129 ? 52.346 147.079 -20.058 1.00 72.65 ? 133 ASP A CA 1 ATOM 953 C C . ASP A 1 129 ? 53.184 145.814 -19.926 1.00 74.48 ? 133 ASP A C 1 ATOM 954 O O . ASP A 1 129 ? 53.964 145.500 -20.825 1.00 76.96 ? 133 ASP A O 1 ATOM 955 C CB . ASP A 1 129 ? 51.765 147.187 -21.484 1.00 77.68 ? 133 ASP A CB 1 ATOM 956 C CG . ASP A 1 129 ? 51.424 148.574 -21.969 1.00 92.21 ? 133 ASP A CG 1 ATOM 957 O OD1 . ASP A 1 129 ? 50.339 149.074 -21.608 1.00 92.26 ? 133 ASP A OD1 1 ATOM 958 O OD2 . ASP A 1 129 ? 52.207 149.128 -22.770 1.00 102.09 ? 133 ASP A OD2 1 ATOM 959 N N . ASN A 1 130 ? 53.076 145.136 -18.765 1.00 66.58 ? 134 ASN A N 1 ATOM 960 C CA . ASN A 1 130 ? 53.785 143.906 -18.402 1.00 65.30 ? 134 ASN A CA 1 ATOM 961 C C . ASN A 1 130 ? 53.352 143.463 -17.015 1.00 65.71 ? 134 ASN A C 1 ATOM 962 O O . ASN A 1 130 ? 52.986 144.308 -16.199 1.00 63.84 ? 134 ASN A O 1 ATOM 963 C CB . ASN A 1 130 ? 55.307 144.118 -18.400 1.00 68.63 ? 134 ASN A CB 1 ATOM 964 C CG . ASN A 1 130 ? 56.101 142.840 -18.518 1.00 97.77 ? 134 ASN A CG 1 ATOM 965 O OD1 . ASN A 1 130 ? 55.917 142.030 -19.429 1.00 97.95 ? 134 ASN A OD1 1 ATOM 966 N ND2 . ASN A 1 130 ? 57.021 142.641 -17.610 1.00 89.13 ? 134 ASN A ND2 1 ATOM 967 N N . LYS A 1 131 ? 53.463 142.141 -16.730 1.00 61.75 ? 135 LYS A N 1 ATOM 968 C CA . LYS A 1 131 ? 53.152 141.493 -15.446 1.00 59.61 ? 135 LYS A CA 1 ATOM 969 C C . LYS A 1 131 ? 54.030 142.073 -14.338 1.00 63.50 ? 135 LYS A C 1 ATOM 970 O O . LYS A 1 131 ? 53.580 142.184 -13.193 1.00 62.34 ? 135 LYS A O 1 ATOM 971 C CB . LYS A 1 131 ? 53.356 139.966 -15.555 1.00 62.36 ? 135 LYS A CB 1 ATOM 972 C CG . LYS A 1 131 ? 52.736 139.154 -14.420 1.00 67.09 ? 135 LYS A CG 1 ATOM 973 C CD . LYS A 1 131 ? 52.687 137.649 -14.706 1.00 76.13 ? 135 LYS A CD 1 ATOM 974 C CE . LYS A 1 131 ? 51.898 136.897 -13.639 1.00 91.21 ? 135 LYS A CE 1 ATOM 975 N NZ . LYS A 1 131 ? 52.119 135.424 -13.667 1.00 106.19 ? 135 LYS A NZ 1 ATOM 976 N N . GLU A 1 132 ? 55.288 142.418 -14.680 1.00 61.20 ? 136 GLU A N 1 ATOM 977 C CA . GLU A 1 132 ? 56.241 143.020 -13.762 1.00 60.65 ? 136 GLU A CA 1 ATOM 978 C C . GLU A 1 132 ? 56.970 144.226 -14.319 1.00 65.49 ? 136 GLU A C 1 ATOM 979 O O . GLU A 1 132 ? 57.250 144.282 -15.515 1.00 67.38 ? 136 GLU A O 1 ATOM 980 C CB . GLU A 1 132 ? 57.191 141.990 -13.146 1.00 63.11 ? 136 GLU A CB 1 ATOM 981 C CG . GLU A 1 132 ? 58.304 141.427 -14.013 1.00 77.13 ? 136 GLU A CG 1 ATOM 982 C CD . GLU A 1 132 ? 59.360 140.695 -13.202 1.00 99.59 ? 136 GLU A CD 1 ATOM 983 O OE1 . GLU A 1 132 ? 60.045 141.350 -12.384 1.00 76.95 ? 136 GLU A OE1 1 ATOM 984 O OE2 . GLU A 1 132 ? 59.478 139.459 -13.361 1.00 101.62 ? 136 GLU A OE2 1 ATOM 985 N N . ILE A 1 133 ? 57.260 145.201 -13.444 1.00 60.97 ? 137 ILE A N 1 ATOM 986 C CA . ILE A 1 133 ? 57.959 146.449 -13.778 1.00 61.75 ? 137 ILE A CA 1 ATOM 987 C C . ILE A 1 133 ? 59.087 146.772 -12.797 1.00 65.99 ? 137 ILE A C 1 ATOM 988 O O . ILE A 1 133 ? 59.021 146.354 -11.646 1.00 63.83 ? 137 ILE A O 1 ATOM 989 C CB . ILE A 1 133 ? 56.980 147.627 -13.934 1.00 64.34 ? 137 ILE A CB 1 ATOM 990 C CG1 . ILE A 1 133 ? 56.319 148.048 -12.587 1.00 62.56 ? 137 ILE A CG1 1 ATOM 991 C CG2 . ILE A 1 133 ? 55.962 147.351 -15.061 1.00 65.74 ? 137 ILE A CG2 1 ATOM 992 C CD1 . ILE A 1 133 ? 55.914 149.545 -12.525 1.00 69.73 ? 137 ILE A CD1 1 ATOM 993 N N . LYS A 1 134 ? 60.122 147.515 -13.244 1.00 65.24 ? 138 LYS A N 1 ATOM 994 C CA . LYS A 1 134 ? 61.278 147.863 -12.409 1.00 65.35 ? 138 LYS A CA 1 ATOM 995 C C . LYS A 1 134 ? 61.667 149.314 -12.645 1.00 69.15 ? 138 LYS A C 1 ATOM 996 O O . LYS A 1 134 ? 61.799 149.720 -13.785 1.00 70.87 ? 138 LYS A O 1 ATOM 997 C CB . LYS A 1 134 ? 62.478 146.916 -12.680 1.00 70.86 ? 138 LYS A CB 1 ATOM 998 C CG . LYS A 1 134 ? 62.231 145.443 -12.289 1.00 99.78 ? 138 LYS A CG 1 ATOM 999 C CD . LYS A 1 134 ? 63.367 144.496 -12.636 1.00 118.02 ? 138 LYS A CD 1 ATOM 1000 C CE . LYS A 1 134 ? 63.037 143.055 -12.282 1.00 134.14 ? 138 LYS A CE 1 ATOM 1001 N NZ . LYS A 1 134 ? 64.175 142.155 -12.580 1.00 149.03 ? 138 LYS A NZ 1 ATOM 1002 N N . LEU A 1 135 ? 61.788 150.104 -11.577 1.00 64.60 ? 139 LEU A N 1 ATOM 1003 C CA . LEU A 1 135 ? 62.216 151.511 -11.621 1.00 66.12 ? 139 LEU A CA 1 ATOM 1004 C C . LEU A 1 135 ? 63.564 151.599 -10.945 1.00 69.70 ? 139 LEU A C 1 ATOM 1005 O O . LEU A 1 135 ? 63.772 150.933 -9.939 1.00 67.12 ? 139 LEU A O 1 ATOM 1006 C CB . LEU A 1 135 ? 61.212 152.451 -10.938 1.00 65.25 ? 139 LEU A CB 1 ATOM 1007 C CG . LEU A 1 135 ? 59.956 152.724 -11.738 1.00 70.89 ? 139 LEU A CG 1 ATOM 1008 C CD1 . LEU A 1 135 ? 58.815 151.872 -11.254 1.00 68.70 ? 139 LEU A CD1 1 ATOM 1009 C CD2 . LEU A 1 135 ? 59.547 154.145 -11.597 1.00 75.63 ? 139 LEU A CD2 1 ATOM 1010 N N . GLU A 1 136 ? 64.489 152.374 -11.521 1.00 68.79 ? 140 GLU A N 1 ATOM 1011 C CA . GLU A 1 136 ? 65.856 152.507 -11.028 1.00 69.39 ? 140 GLU A CA 1 ATOM 1012 C C . GLU A 1 136 ? 66.229 153.974 -10.883 1.00 74.42 ? 140 GLU A C 1 ATOM 1013 O O . GLU A 1 136 ? 65.557 154.825 -11.463 1.00 74.74 ? 140 GLU A O 1 ATOM 1014 C CB . GLU A 1 136 ? 66.826 151.801 -12.003 1.00 73.62 ? 140 GLU A CB 1 ATOM 1015 C CG . GLU A 1 136 ? 66.728 150.283 -11.992 1.00 84.06 ? 140 GLU A CG 1 ATOM 1016 C CD . GLU A 1 136 ? 67.298 149.540 -13.188 1.00 107.27 ? 140 GLU A CD 1 ATOM 1017 O OE1 . GLU A 1 136 ? 68.371 149.936 -13.702 1.00 94.24 ? 140 GLU A OE1 1 ATOM 1018 O OE2 . GLU A 1 136 ? 66.691 148.514 -13.572 1.00 105.49 ? 140 GLU A OE2 1 ATOM 1019 N N . ASN A 1 137 ? 67.320 154.265 -10.129 1.00 71.90 ? 141 ASN A N 1 ATOM 1020 C CA . ASN A 1 137 ? 67.874 155.613 -9.888 1.00 73.33 ? 141 ASN A CA 1 ATOM 1021 C C . ASN A 1 137 ? 66.940 156.510 -9.083 1.00 74.41 ? 141 ASN A C 1 ATOM 1022 O O . ASN A 1 137 ? 67.000 157.741 -9.199 1.00 76.01 ? 141 ASN A O 1 ATOM 1023 C CB . ASN A 1 137 ? 68.265 156.334 -11.202 1.00 77.16 ? 141 ASN A CB 1 ATOM 1024 C CG . ASN A 1 137 ? 69.275 155.676 -12.110 1.00 99.99 ? 141 ASN A CG 1 ATOM 1025 O OD1 . ASN A 1 137 ? 70.084 154.807 -11.739 1.00 93.79 ? 141 ASN A OD1 1 ATOM 1026 N ND2 . ASN A 1 137 ? 69.277 156.136 -13.345 1.00 95.35 ? 141 ASN A ND2 1 ATOM 1027 N N . LEU A 1 138 ? 66.078 155.898 -8.277 1.00 66.37 ? 142 LEU A N 1 ATOM 1028 C CA . LEU A 1 138 ? 65.166 156.645 -7.435 1.00 64.71 ? 142 LEU A CA 1 ATOM 1029 C C . LEU A 1 138 ? 65.954 157.275 -6.301 1.00 67.78 ? 142 LEU A C 1 ATOM 1030 O O . LEU A 1 138 ? 66.966 156.722 -5.868 1.00 66.70 ? 142 LEU A O 1 ATOM 1031 C CB . LEU A 1 138 ? 64.064 155.721 -6.897 1.00 62.40 ? 142 LEU A CB 1 ATOM 1032 C CG . LEU A 1 138 ? 63.061 155.163 -7.944 1.00 67.36 ? 142 LEU A CG 1 ATOM 1033 C CD1 . LEU A 1 138 ? 62.164 154.163 -7.327 1.00 64.81 ? 142 LEU A CD1 1 ATOM 1034 C CD2 . LEU A 1 138 ? 62.204 156.263 -8.551 1.00 72.45 ? 142 LEU A CD2 1 ATOM 1035 N N . GLU A 1 139 ? 65.523 158.442 -5.835 1.00 65.30 ? 143 GLU A N 1 ATOM 1036 C CA . GLU A 1 139 ? 66.241 159.095 -4.744 1.00 65.12 ? 143 GLU A CA 1 ATOM 1037 C C . GLU A 1 139 ? 65.795 158.416 -3.449 1.00 64.86 ? 143 GLU A C 1 ATOM 1038 O O . GLU A 1 139 ? 64.593 158.221 -3.312 1.00 63.13 ? 143 GLU A O 1 ATOM 1039 C CB . GLU A 1 139 ? 65.924 160.597 -4.717 1.00 69.33 ? 143 GLU A CB 1 ATOM 1040 C CG . GLU A 1 139 ? 66.566 161.348 -3.567 1.00 83.41 ? 143 GLU A CG 1 ATOM 1041 C CD . GLU A 1 139 ? 66.595 162.841 -3.797 1.00 114.35 ? 143 GLU A CD 1 ATOM 1042 O OE1 . GLU A 1 139 ? 67.528 163.317 -4.483 1.00 112.19 ? 143 GLU A OE1 1 ATOM 1043 O OE2 . GLU A 1 139 ? 65.661 163.532 -3.331 1.00 115.96 ? 143 GLU A OE2 1 ATOM 1044 N N . PRO A 1 140 ? 66.696 158.044 -2.492 1.00 59.33 ? 144 PRO A N 1 ATOM 1045 C CA . PRO A 1 140 ? 66.227 157.411 -1.231 1.00 56.65 ? 144 PRO A CA 1 ATOM 1046 C C . PRO A 1 140 ? 65.356 158.300 -0.354 1.00 59.85 ? 144 PRO A C 1 ATOM 1047 O O . PRO A 1 140 ? 65.439 159.527 -0.473 1.00 61.36 ? 144 PRO A O 1 ATOM 1048 C CB . PRO A 1 140 ? 67.524 157.122 -0.474 1.00 58.20 ? 144 PRO A CB 1 ATOM 1049 C CG . PRO A 1 140 ? 68.611 157.172 -1.515 1.00 63.96 ? 144 PRO A CG 1 ATOM 1050 C CD . PRO A 1 140 ? 68.165 158.197 -2.498 1.00 61.21 ? 144 PRO A CD 1 ATOM 1051 N N . GLU A 1 141 ? 64.546 157.675 0.536 1.00 54.97 ? 145 GLU A N 1 ATOM 1052 C CA . GLU A 1 141 ? 63.672 158.300 1.544 1.00 56.40 ? 145 GLU A CA 1 ATOM 1053 C C . GLU A 1 141 ? 62.439 159.049 1.005 1.00 64.31 ? 145 GLU A C 1 ATOM 1054 O O . GLU A 1 141 ? 62.025 160.057 1.583 1.00 65.95 ? 145 GLU A O 1 ATOM 1055 C CB . GLU A 1 141 ? 64.487 159.157 2.520 1.00 58.82 ? 145 GLU A CB 1 ATOM 1056 C CG . GLU A 1 141 ? 65.538 158.389 3.287 1.00 68.16 ? 145 GLU A CG 1 ATOM 1057 C CD . GLU A 1 141 ? 66.174 159.177 4.416 1.00 85.97 ? 145 GLU A CD 1 ATOM 1058 O OE1 . GLU A 1 141 ? 65.469 159.499 5.400 1.00 85.16 ? 145 GLU A OE1 1 ATOM 1059 O OE2 . GLU A 1 141 ? 67.400 159.416 4.344 1.00 69.09 ? 145 GLU A OE2 1 ATOM 1060 N N . HIS A 1 142 ? 61.841 158.533 -0.078 1.00 62.21 ? 146 HIS A N 1 ATOM 1061 C CA . HIS A 1 142 ? 60.655 159.091 -0.730 1.00 64.79 ? 146 HIS A CA 1 ATOM 1062 C C . HIS A 1 142 ? 59.619 158.045 -0.868 1.00 68.30 ? 146 HIS A C 1 ATOM 1063 O O . HIS A 1 142 ? 59.936 156.857 -0.803 1.00 66.22 ? 146 HIS A O 1 ATOM 1064 C CB . HIS A 1 142 ? 60.971 159.617 -2.132 1.00 67.29 ? 146 HIS A CB 1 ATOM 1065 C CG . HIS A 1 142 ? 61.854 160.810 -2.124 1.00 73.66 ? 146 HIS A CG 1 ATOM 1066 N ND1 . HIS A 1 142 ? 61.357 162.085 -1.996 1.00 79.14 ? 146 HIS A ND1 1 ATOM 1067 C CD2 . HIS A 1 142 ? 63.203 160.870 -2.230 1.00 75.69 ? 146 HIS A CD2 1 ATOM 1068 C CE1 . HIS A 1 142 ? 62.421 162.878 -2.022 1.00 80.16 ? 146 HIS A CE1 1 ATOM 1069 N NE2 . HIS A 1 142 ? 63.552 162.185 -2.174 1.00 78.28 ? 146 HIS A NE2 1 ATOM 1070 N N . GLU A 1 143 ? 58.368 158.481 -1.107 1.00 66.50 ? 147 GLU A N 1 ATOM 1071 C CA . GLU A 1 143 ? 57.247 157.590 -1.328 1.00 65.37 ? 147 GLU A CA 1 ATOM 1072 C C . GLU A 1 143 ? 56.519 157.819 -2.631 1.00 70.35 ? 147 GLU A C 1 ATOM 1073 O O . GLU A 1 143 ? 56.235 158.953 -3.000 1.00 71.96 ? 147 GLU A O 1 ATOM 1074 C CB . GLU A 1 143 ? 56.319 157.398 -0.129 1.00 67.73 ? 147 GLU A CB 1 ATOM 1075 C CG . GLU A 1 143 ? 55.755 158.597 0.593 1.00 80.35 ? 147 GLU A CG 1 ATOM 1076 C CD . GLU A 1 143 ? 54.896 158.086 1.732 1.00 99.77 ? 147 GLU A CD 1 ATOM 1077 O OE1 . GLU A 1 143 ? 55.455 157.500 2.693 1.00 88.55 ? 147 GLU A OE1 1 ATOM 1078 O OE2 . GLU A 1 143 ? 53.654 158.176 1.606 1.00 93.90 ? 147 GLU A OE2 1 ATOM 1079 N N . TYR A 1 144 ? 56.302 156.730 -3.383 1.00 66.10 ? 148 TYR A N 1 ATOM 1080 C CA . TYR A 1 144 ? 55.672 156.775 -4.703 1.00 67.02 ? 148 TYR A CA 1 ATOM 1081 C C . TYR A 1 144 ? 54.449 155.943 -4.827 1.00 70.51 ? 148 TYR A C 1 ATOM 1082 O O . TYR A 1 144 ? 54.405 154.850 -4.267 1.00 68.46 ? 148 TYR A O 1 ATOM 1083 C CB . TYR A 1 144 ? 56.673 156.411 -5.784 1.00 67.45 ? 148 TYR A CB 1 ATOM 1084 C CG . TYR A 1 144 ? 57.882 157.320 -5.765 1.00 70.66 ? 148 TYR A CG 1 ATOM 1085 C CD1 . TYR A 1 144 ? 57.812 158.622 -6.262 1.00 76.27 ? 148 TYR A CD1 1 ATOM 1086 C CD2 . TYR A 1 144 ? 59.083 156.897 -5.219 1.00 69.82 ? 148 TYR A CD2 1 ATOM 1087 C CE1 . TYR A 1 144 ? 58.912 159.477 -6.213 1.00 79.61 ? 148 TYR A CE1 1 ATOM 1088 C CE2 . TYR A 1 144 ? 60.201 157.730 -5.202 1.00 71.89 ? 148 TYR A CE2 1 ATOM 1089 C CZ . TYR A 1 144 ? 60.105 159.028 -5.679 1.00 82.44 ? 148 TYR A CZ 1 ATOM 1090 O OH . TYR A 1 144 ? 61.182 159.876 -5.635 1.00 84.09 ? 148 TYR A OH 1 ATOM 1091 N N . LYS A 1 145 ? 53.423 156.500 -5.502 1.00 69.10 ? 149 LYS A N 1 ATOM 1092 C CA . LYS A 1 145 ? 52.141 155.840 -5.699 1.00 69.25 ? 149 LYS A CA 1 ATOM 1093 C C . LYS A 1 145 ? 52.090 155.234 -7.093 1.00 72.77 ? 149 LYS A C 1 ATOM 1094 O O . LYS A 1 145 ? 51.986 155.942 -8.097 1.00 73.92 ? 149 LYS A O 1 ATOM 1095 C CB . LYS A 1 145 ? 50.945 156.797 -5.462 1.00 75.62 ? 149 LYS A CB 1 ATOM 1096 C CG . LYS A 1 145 ? 49.571 156.121 -5.570 1.00 93.90 ? 149 LYS A CG 1 ATOM 1097 C CD . LYS A 1 145 ? 48.474 156.962 -4.917 1.00 108.92 ? 149 LYS A CD 1 ATOM 1098 C CE . LYS A 1 145 ? 47.191 156.193 -4.709 1.00 120.03 ? 149 LYS A CE 1 ATOM 1099 N NZ . LYS A 1 145 ? 46.403 156.048 -5.959 1.00 127.90 ? 149 LYS A NZ 1 ATOM 1100 N N . CYS A 1 146 ? 52.192 153.917 -7.148 1.00 68.30 ? 150 CYS A N 1 ATOM 1101 C CA . CYS A 1 146 ? 52.098 153.184 -8.399 1.00 67.91 ? 150 CYS A CA 1 ATOM 1102 C C . CYS A 1 146 ? 50.697 152.570 -8.520 1.00 68.97 ? 150 CYS A C 1 ATOM 1103 O O . CYS A 1 146 ? 50.280 151.788 -7.666 1.00 67.49 ? 150 CYS A O 1 ATOM 1104 C CB . CYS A 1 146 ? 53.194 152.134 -8.479 1.00 67.08 ? 150 CYS A CB 1 ATOM 1105 S SG . CYS A 1 146 ? 54.837 152.822 -8.822 1.00 72.12 ? 150 CYS A SG 1 ATOM 1106 N N . ASP A 1 147 ? 49.947 152.996 -9.542 1.00 65.41 ? 151 ASP A N 1 ATOM 1107 C CA . ASP A 1 147 ? 48.601 152.495 -9.830 1.00 65.19 ? 151 ASP A CA 1 ATOM 1108 C C . ASP A 1 147 ? 48.682 151.377 -10.889 1.00 65.26 ? 151 ASP A C 1 ATOM 1109 O O . ASP A 1 147 ? 49.479 151.468 -11.819 1.00 64.30 ? 151 ASP A O 1 ATOM 1110 C CB . ASP A 1 147 ? 47.679 153.634 -10.306 1.00 71.01 ? 151 ASP A CB 1 ATOM 1111 C CG . ASP A 1 147 ? 47.486 154.759 -9.290 1.00 90.77 ? 151 ASP A CG 1 ATOM 1112 O OD1 . ASP A 1 147 ? 47.126 154.460 -8.147 1.00 93.16 ? 151 ASP A OD1 1 ATOM 1113 O OD2 . ASP A 1 147 ? 47.658 155.949 -9.663 1.00 100.26 ? 151 ASP A OD2 1 ATOM 1114 N N . SER A 1 148 ? 47.882 150.320 -10.739 1.00 59.90 ? 152 SER A N 1 ATOM 1115 C CA . SER A 1 148 ? 47.906 149.184 -11.666 1.00 57.86 ? 152 SER A CA 1 ATOM 1116 C C . SER A 1 148 ? 46.526 148.606 -11.891 1.00 60.84 ? 152 SER A C 1 ATOM 1117 O O . SER A 1 148 ? 45.679 148.693 -11.012 1.00 60.55 ? 152 SER A O 1 ATOM 1118 C CB . SER A 1 148 ? 48.828 148.083 -11.141 1.00 59.57 ? 152 SER A CB 1 ATOM 1119 O OG . SER A 1 148 ? 49.038 147.081 -12.126 1.00 66.67 ? 152 SER A OG 1 ATOM 1120 N N . GLU A 1 149 ? 46.311 147.986 -13.059 1.00 57.08 ? 153 GLU A N 1 ATOM 1121 C CA . GLU A 1 149 ? 45.051 147.318 -13.388 1.00 57.08 ? 153 GLU A CA 1 ATOM 1122 C C . GLU A 1 149 ? 45.305 146.055 -14.190 1.00 59.00 ? 153 GLU A C 1 ATOM 1123 O O . GLU A 1 149 ? 46.347 145.929 -14.836 1.00 57.80 ? 153 GLU A O 1 ATOM 1124 C CB . GLU A 1 149 ? 44.067 148.252 -14.118 1.00 61.01 ? 153 GLU A CB 1 ATOM 1125 C CG . GLU A 1 149 ? 44.448 148.619 -15.542 1.00 75.85 ? 153 GLU A CG 1 ATOM 1126 C CD . GLU A 1 149 ? 43.950 149.992 -15.945 1.00 107.21 ? 153 GLU A CD 1 ATOM 1127 O OE1 . GLU A 1 149 ? 44.004 150.924 -15.107 1.00 101.37 ? 153 GLU A OE1 1 ATOM 1128 O OE2 . GLU A 1 149 ? 43.610 150.159 -17.137 1.00 109.82 ? 153 GLU A OE2 1 ATOM 1129 N N . ILE A 1 150 ? 44.355 145.113 -14.126 1.00 54.87 ? 154 ILE A N 1 ATOM 1130 C CA . ILE A 1 150 ? 44.403 143.865 -14.885 1.00 53.32 ? 154 ILE A CA 1 ATOM 1131 C C . ILE A 1 150 ? 43.214 143.816 -15.810 1.00 56.88 ? 154 ILE A C 1 ATOM 1132 O O . ILE A 1 150 ? 42.093 144.107 -15.399 1.00 56.71 ? 154 ILE A O 1 ATOM 1133 C CB . ILE A 1 150 ? 44.548 142.578 -14.034 1.00 55.36 ? 154 ILE A CB 1 ATOM 1134 C CG1 . ILE A 1 150 ? 45.549 142.768 -12.869 1.00 54.84 ? 154 ILE A CG1 1 ATOM 1135 C CG2 . ILE A 1 150 ? 44.939 141.376 -14.922 1.00 56.11 ? 154 ILE A CG2 1 ATOM 1136 C CD1 . ILE A 1 150 ? 45.664 141.598 -11.945 1.00 61.53 ? 154 ILE A CD1 1 ATOM 1137 N N . LEU A 1 151 ? 43.490 143.522 -17.077 1.00 54.46 ? 155 LEU A N 1 ATOM 1138 C CA . LEU A 1 151 ? 42.504 143.393 -18.133 1.00 56.67 ? 155 LEU A CA 1 ATOM 1139 C C . LEU A 1 151 ? 42.395 141.926 -18.553 1.00 60.58 ? 155 LEU A C 1 ATOM 1140 O O . LEU A 1 151 ? 43.396 141.198 -18.554 1.00 60.21 ? 155 LEU A O 1 ATOM 1141 C CB . LEU A 1 151 ? 42.874 144.231 -19.386 1.00 59.11 ? 155 LEU A CB 1 ATOM 1142 C CG . LEU A 1 151 ? 43.437 145.677 -19.268 1.00 65.86 ? 155 LEU A CG 1 ATOM 1143 C CD1 . LEU A 1 151 ? 43.652 146.287 -20.655 1.00 69.48 ? 155 LEU A CD1 1 ATOM 1144 C CD2 . LEU A 1 151 ? 42.493 146.592 -18.539 1.00 69.98 ? 155 LEU A CD2 1 ATOM 1145 N N . TYR A 1 152 ? 41.172 141.518 -18.931 1.00 57.02 ? 156 TYR A N 1 ATOM 1146 C CA . TYR A 1 152 ? 40.824 140.214 -19.490 1.00 56.60 ? 156 TYR A CA 1 ATOM 1147 C C . TYR A 1 152 ? 40.065 140.536 -20.762 1.00 64.48 ? 156 TYR A C 1 ATOM 1148 O O . TYR A 1 152 ? 39.051 141.231 -20.695 1.00 65.94 ? 156 TYR A O 1 ATOM 1149 C CB . TYR A 1 152 ? 39.967 139.387 -18.527 1.00 56.52 ? 156 TYR A CB 1 ATOM 1150 C CG . TYR A 1 152 ? 39.578 138.033 -19.081 1.00 57.26 ? 156 TYR A CG 1 ATOM 1151 C CD1 . TYR A 1 152 ? 40.544 137.078 -19.387 1.00 59.00 ? 156 TYR A CD1 1 ATOM 1152 C CD2 . TYR A 1 152 ? 38.245 137.706 -19.300 1.00 58.22 ? 156 TYR A CD2 1 ATOM 1153 C CE1 . TYR A 1 152 ? 40.192 135.836 -19.908 1.00 59.99 ? 156 TYR A CE1 1 ATOM 1154 C CE2 . TYR A 1 152 ? 37.879 136.455 -19.781 1.00 59.42 ? 156 TYR A CE2 1 ATOM 1155 C CZ . TYR A 1 152 ? 38.858 135.529 -20.103 1.00 67.19 ? 156 TYR A CZ 1 ATOM 1156 O OH . TYR A 1 152 ? 38.503 134.303 -20.604 1.00 70.17 ? 156 TYR A OH 1 ATOM 1157 N N . ASN A 1 153 ? 40.595 140.123 -21.930 1.00 62.55 ? 157 ASN A N 1 ATOM 1158 C CA . ASN A 1 153 ? 40.016 140.480 -23.245 1.00 64.66 ? 157 ASN A CA 1 ATOM 1159 C C . ASN A 1 153 ? 39.870 142.023 -23.372 1.00 72.73 ? 157 ASN A C 1 ATOM 1160 O O . ASN A 1 153 ? 38.843 142.501 -23.856 1.00 73.83 ? 157 ASN A O 1 ATOM 1161 C CB . ASN A 1 153 ? 38.652 139.775 -23.487 1.00 62.04 ? 157 ASN A CB 1 ATOM 1162 C CG . ASN A 1 153 ? 38.666 138.272 -23.401 1.00 73.53 ? 157 ASN A CG 1 ATOM 1163 O OD1 . ASN A 1 153 ? 39.624 137.604 -23.791 1.00 68.28 ? 157 ASN A OD1 1 ATOM 1164 N ND2 . ASN A 1 153 ? 37.571 137.701 -22.929 1.00 60.62 ? 157 ASN A ND2 1 ATOM 1165 N N . ASN A 1 154 ? 40.872 142.792 -22.866 1.00 71.45 ? 158 ASN A N 1 ATOM 1166 C CA . ASN A 1 154 ? 40.915 144.267 -22.824 1.00 74.37 ? 158 ASN A CA 1 ATOM 1167 C C . ASN A 1 154 ? 39.858 144.897 -21.879 1.00 81.64 ? 158 ASN A C 1 ATOM 1168 O O . ASN A 1 154 ? 39.668 146.114 -21.894 1.00 84.38 ? 158 ASN A O 1 ATOM 1169 C CB . ASN A 1 154 ? 40.926 144.920 -24.217 1.00 78.45 ? 158 ASN A CB 1 ATOM 1170 C CG . ASN A 1 154 ? 41.871 144.289 -25.206 1.00 103.92 ? 158 ASN A CG 1 ATOM 1171 O OD1 . ASN A 1 154 ? 41.503 143.348 -25.894 1.00 101.87 ? 158 ASN A OD1 1 ATOM 1172 N ND2 . ASN A 1 154 ? 43.085 144.831 -25.356 1.00 94.85 ? 158 ASN A ND2 1 ATOM 1173 N N . HIS A 1 155 ? 39.209 144.064 -21.038 1.00 77.71 ? 159 HIS A N 1 ATOM 1174 C CA . HIS A 1 155 ? 38.214 144.458 -20.034 1.00 78.80 ? 159 HIS A CA 1 ATOM 1175 C C . HIS A 1 155 ? 38.897 144.583 -18.695 1.00 77.90 ? 159 HIS A C 1 ATOM 1176 O O . HIS A 1 155 ? 39.412 143.577 -18.215 1.00 75.71 ? 159 HIS A O 1 ATOM 1177 C CB . HIS A 1 155 ? 37.161 143.349 -19.856 1.00 80.20 ? 159 HIS A CB 1 ATOM 1178 C CG . HIS A 1 155 ? 35.985 143.424 -20.780 1.00 86.85 ? 159 HIS A CG 1 ATOM 1179 N ND1 . HIS A 1 155 ? 35.057 142.417 -20.805 1.00 88.84 ? 159 HIS A ND1 1 ATOM 1180 C CD2 . HIS A 1 155 ? 35.644 144.359 -21.709 1.00 92.06 ? 159 HIS A CD2 1 ATOM 1181 C CE1 . HIS A 1 155 ? 34.176 142.755 -21.734 1.00 90.78 ? 159 HIS A CE1 1 ATOM 1182 N NE2 . HIS A 1 155 ? 34.475 143.924 -22.298 1.00 93.29 ? 159 HIS A NE2 1 ATOM 1183 N N . LYS A 1 156 ? 38.836 145.756 -18.044 1.00 72.83 ? 160 LYS A N 1 ATOM 1184 C CA . LYS A 1 156 ? 39.415 145.893 -16.709 1.00 70.22 ? 160 LYS A CA 1 ATOM 1185 C C . LYS A 1 156 ? 38.493 145.183 -15.732 1.00 71.85 ? 160 LYS A C 1 ATOM 1186 O O . LYS A 1 156 ? 37.304 145.500 -15.692 1.00 73.62 ? 160 LYS A O 1 ATOM 1187 C CB . LYS A 1 156 ? 39.578 147.374 -16.303 1.00 74.62 ? 160 LYS A CB 1 ATOM 1188 C CG . LYS A 1 156 ? 40.130 147.559 -14.879 1.00 86.84 ? 160 LYS A CG 1 ATOM 1189 C CD . LYS A 1 156 ? 39.856 148.938 -14.288 1.00 97.10 ? 160 LYS A CD 1 ATOM 1190 C CE . LYS A 1 156 ? 38.508 149.062 -13.617 1.00 108.73 ? 160 LYS A CE 1 ATOM 1191 N NZ . LYS A 1 156 ? 38.411 150.315 -12.839 1.00 120.34 ? 160 LYS A NZ 1 ATOM 1192 N N . PHE A 1 157 ? 39.027 144.230 -14.953 1.00 64.83 ? 161 PHE A N 1 ATOM 1193 C CA . PHE A 1 157 ? 38.241 143.507 -13.951 1.00 64.53 ? 161 PHE A CA 1 ATOM 1194 C C . PHE A 1 157 ? 38.757 143.719 -12.529 1.00 70.59 ? 161 PHE A C 1 ATOM 1195 O O . PHE A 1 157 ? 38.060 143.392 -11.558 1.00 71.80 ? 161 PHE A O 1 ATOM 1196 C CB . PHE A 1 157 ? 38.136 142.014 -14.290 1.00 64.54 ? 161 PHE A CB 1 ATOM 1197 C CG . PHE A 1 157 ? 39.414 141.213 -14.212 1.00 63.31 ? 161 PHE A CG 1 ATOM 1198 C CD1 . PHE A 1 157 ? 40.299 141.184 -15.278 1.00 64.87 ? 161 PHE A CD1 1 ATOM 1199 C CD2 . PHE A 1 157 ? 39.703 140.440 -13.093 1.00 64.79 ? 161 PHE A CD2 1 ATOM 1200 C CE1 . PHE A 1 157 ? 41.464 140.420 -15.216 1.00 64.59 ? 161 PHE A CE1 1 ATOM 1201 C CE2 . PHE A 1 157 ? 40.880 139.689 -13.028 1.00 66.37 ? 161 PHE A CE2 1 ATOM 1202 C CZ . PHE A 1 157 ? 41.754 139.689 -14.086 1.00 63.46 ? 161 PHE A CZ 1 ATOM 1203 N N . THR A 1 158 ? 40.005 144.204 -12.408 1.00 67.47 ? 162 THR A N 1 ATOM 1204 C CA . THR A 1 158 ? 40.658 144.476 -11.128 1.00 67.89 ? 162 THR A CA 1 ATOM 1205 C C . THR A 1 158 ? 41.722 145.528 -11.258 1.00 71.49 ? 162 THR A C 1 ATOM 1206 O O . THR A 1 158 ? 42.215 145.810 -12.349 1.00 69.64 ? 162 THR A O 1 ATOM 1207 C CB . THR A 1 158 ? 41.116 143.198 -10.358 1.00 79.60 ? 162 THR A CB 1 ATOM 1208 O OG1 . THR A 1 158 ? 41.427 143.545 -9.009 1.00 80.70 ? 162 THR A OG1 1 ATOM 1209 C CG2 . THR A 1 158 ? 42.314 142.500 -10.984 1.00 78.45 ? 162 THR A CG2 1 ATOM 1210 N N . ASN A 1 159 ? 42.055 146.124 -10.125 1.00 70.08 ? 163 ASN A N 1 ATOM 1211 C CA . ASN A 1 159 ? 43.051 147.166 -10.022 1.00 69.94 ? 163 ASN A CA 1 ATOM 1212 C C . ASN A 1 159 ? 43.515 147.300 -8.575 1.00 74.15 ? 163 ASN A C 1 ATOM 1213 O O . ASN A 1 159 ? 42.860 146.793 -7.660 1.00 75.09 ? 163 ASN A O 1 ATOM 1214 C CB . ASN A 1 159 ? 42.523 148.497 -10.625 1.00 74.36 ? 163 ASN A CB 1 ATOM 1215 C CG . ASN A 1 159 ? 41.478 149.247 -9.841 1.00 109.04 ? 163 ASN A CG 1 ATOM 1216 O OD1 . ASN A 1 159 ? 41.189 148.945 -8.685 1.00 105.13 ? 163 ASN A OD1 1 ATOM 1217 N ND2 . ASN A 1 159 ? 40.935 150.275 -10.506 1.00 109.82 ? 163 ASN A ND2 1 ATOM 1218 N N . ALA A 1 160 ? 44.664 147.938 -8.377 1.00 70.05 ? 164 ALA A N 1 ATOM 1219 C CA . ALA A 1 160 ? 45.252 148.166 -7.064 1.00 70.25 ? 164 ALA A CA 1 ATOM 1220 C C . ALA A 1 160 ? 46.220 149.330 -7.156 1.00 73.91 ? 164 ALA A C 1 ATOM 1221 O O . ALA A 1 160 ? 46.671 149.713 -8.247 1.00 73.37 ? 164 ALA A O 1 ATOM 1222 C CB . ALA A 1 160 ? 45.988 146.907 -6.574 1.00 69.50 ? 164 ALA A CB 1 ATOM 1223 N N . SER A 1 161 ? 46.526 149.891 -5.991 1.00 70.49 ? 165 SER A N 1 ATOM 1224 C CA . SER A 1 161 ? 47.503 150.944 -5.843 1.00 69.81 ? 165 SER A CA 1 ATOM 1225 C C . SER A 1 161 ? 48.509 150.507 -4.839 1.00 70.68 ? 165 SER A C 1 ATOM 1226 O O . SER A 1 161 ? 48.164 149.899 -3.815 1.00 70.39 ? 165 SER A O 1 ATOM 1227 C CB . SER A 1 161 ? 46.856 152.219 -5.350 1.00 76.77 ? 165 SER A CB 1 ATOM 1228 O OG . SER A 1 161 ? 46.539 153.034 -6.458 1.00 88.75 ? 165 SER A OG 1 ATOM 1229 N N . LYS A 1 162 ? 49.766 150.788 -5.141 1.00 65.12 ? 166 LYS A N 1 ATOM 1230 C CA . LYS A 1 162 ? 50.815 150.446 -4.222 1.00 63.50 ? 166 LYS A CA 1 ATOM 1231 C C . LYS A 1 162 ? 51.672 151.648 -3.964 1.00 65.90 ? 166 LYS A C 1 ATOM 1232 O O . LYS A 1 162 ? 52.213 152.250 -4.899 1.00 64.90 ? 166 LYS A O 1 ATOM 1233 C CB . LYS A 1 162 ? 51.620 149.191 -4.641 1.00 64.05 ? 166 LYS A CB 1 ATOM 1234 C CG . LYS A 1 162 ? 52.624 148.693 -3.568 1.00 75.65 ? 166 LYS A CG 1 ATOM 1235 C CD . LYS A 1 162 ? 51.988 148.085 -2.294 1.00 83.01 ? 166 LYS A CD 1 ATOM 1236 C CE . LYS A 1 162 ? 52.744 148.411 -1.023 1.00 96.64 ? 166 LYS A CE 1 ATOM 1237 N NZ . LYS A 1 162 ? 53.718 147.345 -0.657 1.00 108.72 ? 166 LYS A NZ 1 ATOM 1238 N N . ILE A 1 163 ? 51.703 152.052 -2.679 1.00 62.64 ? 167 ILE A N 1 ATOM 1239 C CA . ILE A 1 163 ? 52.527 153.144 -2.195 1.00 62.57 ? 167 ILE A CA 1 ATOM 1240 C C . ILE A 1 163 ? 53.808 152.481 -1.669 1.00 64.04 ? 167 ILE A C 1 ATOM 1241 O O . ILE A 1 163 ? 53.734 151.612 -0.798 1.00 64.14 ? 167 ILE A O 1 ATOM 1242 C CB . ILE A 1 163 ? 51.817 154.030 -1.144 1.00 68.51 ? 167 ILE A CB 1 ATOM 1243 C CG1 . ILE A 1 163 ? 50.594 154.750 -1.760 1.00 71.30 ? 167 ILE A CG1 1 ATOM 1244 C CG2 . ILE A 1 163 ? 52.797 155.038 -0.541 1.00 69.39 ? 167 ILE A CG2 1 ATOM 1245 C CD1 . ILE A 1 163 ? 49.466 155.080 -0.763 1.00 82.41 ? 167 ILE A CD1 1 ATOM 1246 N N . ILE A 1 164 ? 54.966 152.847 -2.240 1.00 58.41 ? 168 ILE A N 1 ATOM 1247 C CA . ILE A 1 164 ? 56.281 152.286 -1.871 1.00 56.66 ? 168 ILE A CA 1 ATOM 1248 C C . ILE A 1 164 ? 57.206 153.381 -1.408 1.00 59.62 ? 168 ILE A C 1 ATOM 1249 O O . ILE A 1 164 ? 57.268 154.417 -2.076 1.00 60.76 ? 168 ILE A O 1 ATOM 1250 C CB . ILE A 1 164 ? 56.967 151.561 -3.064 1.00 58.42 ? 168 ILE A CB 1 ATOM 1251 C CG1 . ILE A 1 164 ? 56.008 150.686 -3.881 1.00 58.41 ? 168 ILE A CG1 1 ATOM 1252 C CG2 . ILE A 1 164 ? 58.260 150.775 -2.669 1.00 57.92 ? 168 ILE A CG2 1 ATOM 1253 C CD1 . ILE A 1 164 ? 55.724 151.188 -5.266 1.00 66.12 ? 168 ILE A CD1 1 ATOM 1254 N N . LYS A 1 165 ? 58.012 153.093 -0.348 1.00 54.28 ? 169 LYS A N 1 ATOM 1255 C CA . LYS A 1 165 ? 59.058 153.953 0.231 1.00 54.22 ? 169 LYS A CA 1 ATOM 1256 C C . LYS A 1 165 ? 60.492 153.467 -0.194 1.00 56.57 ? 169 LYS A C 1 ATOM 1257 O O . LYS A 1 165 ? 60.758 152.272 -0.146 1.00 57.32 ? 169 LYS A O 1 ATOM 1258 C CB . LYS A 1 165 ? 58.943 153.986 1.765 1.00 57.89 ? 169 LYS A CB 1 ATOM 1259 C CG . LYS A 1 165 ? 58.417 155.307 2.417 1.00 68.00 ? 169 LYS A CG 1 ATOM 1260 C CD . LYS A 1 165 ? 59.341 155.657 3.633 1.00 69.18 ? 169 LYS A CD 1 ATOM 1261 C CE . LYS A 1 165 ? 59.363 157.087 4.112 1.00 69.46 ? 169 LYS A CE 1 ATOM 1262 N NZ . LYS A 1 165 ? 60.288 157.950 3.329 1.00 73.47 ? 169 LYS A NZ 1 ATOM 1263 N N . THR A 1 166 ? 61.383 154.383 -0.628 1.00 50.81 ? 170 THR A N 1 ATOM 1264 C CA . THR A 1 166 ? 62.746 154.061 -1.074 1.00 49.78 ? 170 THR A CA 1 ATOM 1265 C C . THR A 1 166 ? 63.745 154.072 0.077 1.00 53.31 ? 170 THR A C 1 ATOM 1266 O O . THR A 1 166 ? 64.508 155.028 0.211 1.00 56.05 ? 170 THR A O 1 ATOM 1267 C CB . THR A 1 166 ? 63.166 154.936 -2.255 1.00 63.16 ? 170 THR A CB 1 ATOM 1268 O OG1 . THR A 1 166 ? 62.919 156.319 -1.946 1.00 68.39 ? 170 THR A OG1 1 ATOM 1269 C CG2 . THR A 1 166 ? 62.482 154.511 -3.525 1.00 62.23 ? 170 THR A CG2 1 ATOM 1270 N N . ASP A 1 167 ? 63.735 153.023 0.911 1.00 45.61 ? 171 ASP A N 1 ATOM 1271 C CA . ASP A 1 167 ? 64.634 152.749 2.059 1.00 44.47 ? 171 ASP A CA 1 ATOM 1272 C C . ASP A 1 167 ? 65.825 153.716 2.342 1.00 47.78 ? 171 ASP A C 1 ATOM 1273 O O . ASP A 1 167 ? 66.403 154.255 1.410 1.00 46.79 ? 171 ASP A O 1 ATOM 1274 C CB . ASP A 1 167 ? 65.163 151.305 1.914 1.00 45.95 ? 171 ASP A CB 1 ATOM 1275 C CG . ASP A 1 167 ? 65.950 150.646 3.048 1.00 54.93 ? 171 ASP A CG 1 ATOM 1276 O OD1 . ASP A 1 167 ? 66.013 151.229 4.155 1.00 55.53 ? 171 ASP A OD1 1 ATOM 1277 O OD2 . ASP A 1 167 ? 66.536 149.561 2.813 1.00 59.98 ? 171 ASP A OD2 1 ATOM 1278 N N . PHE A 1 168 ? 66.248 153.858 3.606 1.00 45.56 ? 172 PHE A N 1 ATOM 1279 C CA . PHE A 1 168 ? 67.404 154.691 3.971 1.00 45.69 ? 172 PHE A CA 1 ATOM 1280 C C . PHE A 1 168 ? 68.658 154.425 3.054 1.00 50.16 ? 172 PHE A C 1 ATOM 1281 O O . PHE A 1 168 ? 69.139 153.288 3.001 1.00 50.85 ? 172 PHE A O 1 ATOM 1282 C CB . PHE A 1 168 ? 67.784 154.450 5.438 1.00 48.37 ? 172 PHE A CB 1 ATOM 1283 C CG . PHE A 1 168 ? 66.890 155.106 6.457 1.00 50.68 ? 172 PHE A CG 1 ATOM 1284 C CD1 . PHE A 1 168 ? 65.678 154.540 6.802 1.00 54.72 ? 172 PHE A CD1 1 ATOM 1285 C CD2 . PHE A 1 168 ? 67.281 156.275 7.105 1.00 53.68 ? 172 PHE A CD2 1 ATOM 1286 C CE1 . PHE A 1 168 ? 64.849 155.146 7.750 1.00 57.44 ? 172 PHE A CE1 1 ATOM 1287 C CE2 . PHE A 1 168 ? 66.452 156.882 8.048 1.00 58.21 ? 172 PHE A CE2 1 ATOM 1288 C CZ . PHE A 1 168 ? 65.239 156.315 8.360 1.00 57.31 ? 172 PHE A CZ 1 ATOM 1289 N N . GLY A 1 169 ? 69.087 155.438 2.288 1.00 45.98 ? 173 GLY A N 1 ATOM 1290 C CA . GLY A 1 169 ? 70.240 155.342 1.393 1.00 46.22 ? 173 GLY A CA 1 ATOM 1291 C C . GLY A 1 169 ? 71.592 155.387 2.087 1.00 51.31 ? 173 GLY A C 1 ATOM 1292 O O . GLY A 1 169 ? 71.662 155.565 3.309 1.00 51.31 ? 173 GLY A O 1 ATOM 1293 N N . SER A 1 170 ? 72.678 155.222 1.305 1.00 50.15 ? 174 SER A N 1 ATOM 1294 C CA . SER A 1 170 ? 74.057 155.258 1.801 1.00 46.82 ? 174 SER A CA 1 ATOM 1295 C C . SER A 1 170 ? 74.375 156.663 2.342 1.00 48.62 ? 174 SER A C 1 ATOM 1296 O O . SER A 1 170 ? 73.998 157.652 1.699 1.00 50.10 ? 174 SER A O 1 ATOM 1297 C CB . SER A 1 170 ? 75.041 154.890 0.692 1.00 49.95 ? 174 SER A CB 1 ATOM 1298 O OG . SER A 1 170 ? 74.721 153.647 0.085 1.00 59.90 ? 174 SER A OG 1 ATOM 1299 N N . PRO A 1 171 ? 75.030 156.783 3.525 1.00 41.36 ? 175 PRO A N 1 ATOM 1300 C CA . PRO A 1 171 ? 75.335 158.124 4.065 1.00 41.23 ? 175 PRO A CA 1 ATOM 1301 C C . PRO A 1 171 ? 76.653 158.745 3.546 1.00 45.31 ? 175 PRO A C 1 ATOM 1302 O O . PRO A 1 171 ? 77.216 158.277 2.549 1.00 44.47 ? 175 PRO A O 1 ATOM 1303 C CB . PRO A 1 171 ? 75.354 157.883 5.584 1.00 41.52 ? 175 PRO A CB 1 ATOM 1304 C CG . PRO A 1 171 ? 75.528 156.395 5.758 1.00 43.87 ? 175 PRO A CG 1 ATOM 1305 C CD . PRO A 1 171 ? 75.521 155.724 4.426 1.00 39.80 ? 175 PRO A CD 1 ATOM 1306 N N . GLY A 1 172 ? 77.098 159.816 4.201 1.00 42.78 ? 176 GLY A N 1 ATOM 1307 C CA . GLY A 1 172 ? 78.372 160.491 3.967 1.00 42.70 ? 176 GLY A CA 1 ATOM 1308 C C . GLY A 1 172 ? 78.778 160.947 2.578 1.00 50.36 ? 176 GLY A C 1 ATOM 1309 O O . GLY A 1 172 ? 77.913 161.268 1.756 1.00 53.65 ? 176 GLY A O 1 ATOM 1310 N N . GLU A 1 173 ? 80.111 161.026 2.289 1.00 44.90 ? 177 GLU A N 1 ATOM 1311 C CA . GLU A 1 173 ? 81.261 160.681 3.154 1.00 41.84 ? 177 GLU A CA 1 ATOM 1312 C C . GLU A 1 173 ? 81.551 161.762 4.196 1.00 43.17 ? 177 GLU A C 1 ATOM 1313 O O . GLU A 1 173 ? 81.077 162.882 4.007 1.00 44.14 ? 177 GLU A O 1 ATOM 1314 C CB . GLU A 1 173 ? 82.534 160.416 2.301 1.00 42.72 ? 177 GLU A CB 1 ATOM 1315 C CG . GLU A 1 173 ? 83.052 161.565 1.439 1.00 56.82 ? 177 GLU A CG 1 ATOM 1316 C CD . GLU A 1 173 ? 84.391 161.342 0.750 1.00 75.02 ? 177 GLU A CD 1 ATOM 1317 O OE1 . GLU A 1 173 ? 84.542 160.317 0.045 1.00 64.49 ? 177 GLU A OE1 1 ATOM 1318 O OE2 . GLU A 1 173 ? 85.273 162.224 0.874 1.00 65.22 ? 177 GLU A OE2 1 ATOM 1319 N N . PRO A 1 174 ? 82.339 161.500 5.276 1.00 36.94 ? 178 PRO A N 1 ATOM 1320 C CA . PRO A 1 174 ? 82.648 162.584 6.214 1.00 36.34 ? 178 PRO A CA 1 ATOM 1321 C C . PRO A 1 174 ? 83.755 163.491 5.663 1.00 39.04 ? 178 PRO A C 1 ATOM 1322 O O . PRO A 1 174 ? 84.467 163.119 4.727 1.00 37.81 ? 178 PRO A O 1 ATOM 1323 C CB . PRO A 1 174 ? 83.072 161.846 7.495 1.00 36.86 ? 178 PRO A CB 1 ATOM 1324 C CG . PRO A 1 174 ? 82.968 160.374 7.188 1.00 40.51 ? 178 PRO A CG 1 ATOM 1325 C CD . PRO A 1 174 ? 82.996 160.252 5.706 1.00 36.74 ? 178 PRO A CD 1 ATOM 1326 N N . GLN A 1 175 ? 83.870 164.699 6.226 1.00 36.13 ? 179 GLN A N 1 ATOM 1327 C CA . GLN A 1 175 ? 84.864 165.701 5.850 1.00 36.14 ? 179 GLN A CA 1 ATOM 1328 C C . GLN A 1 175 ? 85.996 165.649 6.884 1.00 37.92 ? 179 GLN A C 1 ATOM 1329 O O . GLN A 1 175 ? 85.755 165.965 8.053 1.00 39.11 ? 179 GLN A O 1 ATOM 1330 C CB . GLN A 1 175 ? 84.189 167.089 5.817 1.00 39.58 ? 179 GLN A CB 1 ATOM 1331 C CG . GLN A 1 175 ? 85.111 168.269 5.509 1.00 60.96 ? 179 GLN A CG 1 ATOM 1332 C CD . GLN A 1 175 ? 84.306 169.512 5.218 1.00 87.25 ? 179 GLN A CD 1 ATOM 1333 O OE1 . GLN A 1 175 ? 84.023 169.842 4.058 1.00 84.01 ? 179 GLN A OE1 1 ATOM 1334 N NE2 . GLN A 1 175 ? 83.894 170.219 6.264 1.00 80.59 ? 179 GLN A NE2 1 ATOM 1335 N N . ILE A 1 176 ? 87.207 165.216 6.478 1.00 30.46 ? 180 ILE A N 1 ATOM 1336 C CA . ILE A 1 176 ? 88.336 165.148 7.416 1.00 28.63 ? 180 ILE A CA 1 ATOM 1337 C C . ILE A 1 176 ? 88.957 166.532 7.624 1.00 32.00 ? 180 ILE A C 1 ATOM 1338 O O . ILE A 1 176 ? 89.477 167.113 6.671 1.00 33.24 ? 180 ILE A O 1 ATOM 1339 C CB . ILE A 1 176 ? 89.394 164.074 7.015 1.00 30.34 ? 180 ILE A CB 1 ATOM 1340 C CG1 . ILE A 1 176 ? 88.834 162.647 7.231 1.00 29.65 ? 180 ILE A CG1 1 ATOM 1341 C CG2 . ILE A 1 176 ? 90.713 164.278 7.787 1.00 30.12 ? 180 ILE A CG2 1 ATOM 1342 C CD1 . ILE A 1 176 ? 89.572 161.521 6.516 1.00 35.10 ? 180 ILE A CD1 1 ATOM 1343 N N . ILE A 1 177 ? 88.907 167.060 8.864 1.00 27.22 ? 181 ILE A N 1 ATOM 1344 C CA . ILE A 1 177 ? 89.533 168.353 9.193 1.00 27.45 ? 181 ILE A CA 1 ATOM 1345 C C . ILE A 1 177 ? 91.043 168.151 8.998 1.00 31.36 ? 181 ILE A C 1 ATOM 1346 O O . ILE A 1 177 ? 91.648 168.838 8.172 1.00 31.68 ? 181 ILE A O 1 ATOM 1347 C CB . ILE A 1 177 ? 89.214 168.879 10.630 1.00 30.40 ? 181 ILE A CB 1 ATOM 1348 C CG1 . ILE A 1 177 ? 87.741 168.724 11.041 1.00 29.71 ? 181 ILE A CG1 1 ATOM 1349 C CG2 . ILE A 1 177 ? 89.737 170.301 10.829 1.00 32.72 ? 181 ILE A CG2 1 ATOM 1350 C CD1 . ILE A 1 177 ? 86.846 169.668 10.473 1.00 34.99 ? 181 ILE A CD1 1 ATOM 1351 N N . PHE A 1 178 ? 91.619 167.152 9.710 1.00 27.11 ? 182 PHE A N 1 ATOM 1352 C CA . PHE A 1 178 ? 93.021 166.787 9.601 1.00 26.97 ? 182 PHE A CA 1 ATOM 1353 C C . PHE A 1 178 ? 93.379 165.393 10.127 1.00 33.25 ? 182 PHE A C 1 ATOM 1354 O O . PHE A 1 178 ? 92.577 164.750 10.809 1.00 32.35 ? 182 PHE A O 1 ATOM 1355 C CB . PHE A 1 178 ? 93.918 167.859 10.251 1.00 29.33 ? 182 PHE A CB 1 ATOM 1356 C CG . PHE A 1 178 ? 93.961 167.949 11.752 1.00 30.69 ? 182 PHE A CG 1 ATOM 1357 C CD1 . PHE A 1 178 ? 94.580 166.958 12.507 1.00 32.79 ? 182 PHE A CD1 1 ATOM 1358 C CD2 . PHE A 1 178 ? 93.499 169.081 12.406 1.00 33.63 ? 182 PHE A CD2 1 ATOM 1359 C CE1 . PHE A 1 178 ? 94.634 167.048 13.894 1.00 34.53 ? 182 PHE A CE1 1 ATOM 1360 C CE2 . PHE A 1 178 ? 93.574 169.184 13.791 1.00 37.22 ? 182 PHE A CE2 1 ATOM 1361 C CZ . PHE A 1 178 ? 94.133 168.161 14.526 1.00 35.29 ? 182 PHE A CZ 1 ATOM 1362 N N . CYS A 1 179 ? 94.612 164.953 9.804 1.00 32.27 ? 183 CYS A N 1 ATOM 1363 C CA . CYS A 1 179 ? 95.308 163.783 10.325 1.00 33.15 ? 183 CYS A CA 1 ATOM 1364 C C . CYS A 1 179 ? 96.817 163.933 10.287 1.00 35.83 ? 183 CYS A C 1 ATOM 1365 O O . CYS A 1 179 ? 97.414 164.110 9.223 1.00 35.33 ? 183 CYS A O 1 ATOM 1366 C CB . CYS A 1 179 ? 94.801 162.428 9.828 1.00 33.64 ? 183 CYS A CB 1 ATOM 1367 S SG . CYS A 1 179 ? 95.179 162.039 8.104 1.00 38.10 ? 183 CYS A SG 1 ATOM 1368 N N . ARG A 1 180 ? 97.407 164.003 11.486 1.00 32.48 ? 184 ARG A N 1 ATOM 1369 C CA . ARG A 1 180 ? 98.829 164.261 11.700 1.00 33.83 ? 184 ARG A CA 1 ATOM 1370 C C . ARG A 1 180 ? 99.426 163.444 12.830 1.00 38.12 ? 184 ARG A C 1 ATOM 1371 O O . ARG A 1 180 ? 98.734 163.114 13.792 1.00 37.88 ? 184 ARG A O 1 ATOM 1372 C CB . ARG A 1 180 ? 99.048 165.759 11.998 1.00 35.82 ? 184 ARG A CB 1 ATOM 1373 C CG . ARG A 1 180 ? 98.462 166.232 13.341 1.00 45.73 ? 184 ARG A CG 1 ATOM 1374 C CD . ARG A 1 180 ? 98.570 167.724 13.526 1.00 50.91 ? 184 ARG A CD 1 ATOM 1375 N NE . ARG A 1 180 ? 97.786 168.175 14.674 1.00 49.93 ? 184 ARG A NE 1 ATOM 1376 C CZ . ARG A 1 180 ? 97.430 169.438 14.880 1.00 60.92 ? 184 ARG A CZ 1 ATOM 1377 N NH1 . ARG A 1 180 ? 97.775 170.383 14.010 1.00 47.46 ? 184 ARG A NH1 1 ATOM 1378 N NH2 . ARG A 1 180 ? 96.722 169.767 15.953 1.00 42.92 ? 184 ARG A NH2 1 ATOM 1379 N N . SER A 1 181 ? 100.728 163.173 12.736 1.00 35.64 ? 185 SER A N 1 ATOM 1380 C CA . SER A 1 181 ? 101.449 162.474 13.782 1.00 37.23 ? 185 SER A CA 1 ATOM 1381 C C . SER A 1 181 ? 101.798 163.505 14.842 1.00 45.24 ? 185 SER A C 1 ATOM 1382 O O . SER A 1 181 ? 102.117 164.645 14.509 1.00 45.54 ? 185 SER A O 1 ATOM 1383 C CB . SER A 1 181 ? 102.721 161.853 13.223 1.00 41.42 ? 185 SER A CB 1 ATOM 1384 O OG . SER A 1 181 ? 103.434 161.152 14.226 1.00 51.26 ? 185 SER A OG 1 ATOM 1385 N N . GLU A 1 182 ? 101.701 163.130 16.114 1.00 45.17 ? 186 GLU A N 1 ATOM 1386 C CA . GLU A 1 182 ? 102.026 164.043 17.209 1.00 48.26 ? 186 GLU A CA 1 ATOM 1387 C C . GLU A 1 182 ? 103.044 163.454 18.196 1.00 56.55 ? 186 GLU A C 1 ATOM 1388 O O . GLU A 1 182 ? 103.495 164.151 19.106 1.00 58.37 ? 186 GLU A O 1 ATOM 1389 C CB . GLU A 1 182 ? 100.762 164.600 17.882 1.00 49.15 ? 186 GLU A CB 1 ATOM 1390 C CG . GLU A 1 182 ? 100.088 165.694 17.067 1.00 60.00 ? 186 GLU A CG 1 ATOM 1391 C CD . GLU A 1 182 ? 98.839 166.296 17.678 1.00 84.55 ? 186 GLU A CD 1 ATOM 1392 O OE1 . GLU A 1 182 ? 97.858 165.547 17.896 1.00 77.29 ? 186 GLU A OE1 1 ATOM 1393 O OE2 . GLU A 1 182 ? 98.840 167.524 17.927 1.00 81.56 ? 186 GLU A OE2 1 ATOM 1394 N N . ALA A 1 183 ? 103.428 162.176 17.973 1.00 54.42 ? 187 ALA A N 1 ATOM 1395 C CA . ALA A 1 183 ? 104.433 161.404 18.712 1.00 57.34 ? 187 ALA A CA 1 ATOM 1396 C C . ALA A 1 183 ? 105.104 160.420 17.746 1.00 62.11 ? 187 ALA A C 1 ATOM 1397 O O . ALA A 1 183 ? 104.722 160.355 16.573 1.00 59.38 ? 187 ALA A O 1 ATOM 1398 C CB . ALA A 1 183 ? 103.789 160.653 19.870 1.00 58.53 ? 187 ALA A CB 1 ATOM 1399 N N . ALA A 1 184 ? 106.113 159.673 18.224 1.00 62.32 ? 188 ALA A N 1 ATOM 1400 C CA . ALA A 1 184 ? 106.834 158.697 17.402 1.00 63.14 ? 188 ALA A CA 1 ATOM 1401 C C . ALA A 1 184 ? 105.976 157.463 17.080 1.00 64.28 ? 188 ALA A C 1 ATOM 1402 O O . ALA A 1 184 ? 106.214 156.800 16.069 1.00 62.54 ? 188 ALA A O 1 ATOM 1403 C CB . ALA A 1 184 ? 108.122 158.281 18.094 1.00 68.04 ? 188 ALA A CB 1 ATOM 1404 N N . HIS A 1 185 ? 104.976 157.170 17.937 1.00 59.95 ? 189 HIS A N 1 ATOM 1405 C CA . HIS A 1 185 ? 104.072 156.028 17.778 1.00 57.63 ? 189 HIS A CA 1 ATOM 1406 C C . HIS A 1 185 ? 102.615 156.471 17.725 1.00 56.31 ? 189 HIS A C 1 ATOM 1407 O O . HIS A 1 185 ? 101.725 155.653 17.968 1.00 55.21 ? 189 HIS A O 1 ATOM 1408 C CB . HIS A 1 185 ? 104.290 155.011 18.916 1.00 60.74 ? 189 HIS A CB 1 ATOM 1409 C CG . HIS A 1 185 ? 105.731 154.715 19.173 1.00 67.60 ? 189 HIS A CG 1 ATOM 1410 N ND1 . HIS A 1 185 ? 106.453 153.876 18.344 1.00 70.41 ? 189 HIS A ND1 1 ATOM 1411 C CD2 . HIS A 1 185 ? 106.552 155.198 20.132 1.00 71.96 ? 189 HIS A CD2 1 ATOM 1412 C CE1 . HIS A 1 185 ? 107.679 153.856 18.839 1.00 73.31 ? 189 HIS A CE1 1 ATOM 1413 N NE2 . HIS A 1 185 ? 107.785 154.635 19.915 1.00 74.76 ? 189 HIS A NE2 1 ATOM 1414 N N . GLN A 1 186 ? 102.363 157.755 17.401 1.00 49.95 ? 190 GLN A N 1 ATOM 1415 C CA . GLN A 1 186 ? 100.998 158.265 17.362 1.00 47.02 ? 190 GLN A CA 1 ATOM 1416 C C . GLN A 1 186 ? 100.592 159.108 16.164 1.00 47.43 ? 190 GLN A C 1 ATOM 1417 O O . GLN A 1 186 ? 101.426 159.714 15.504 1.00 47.71 ? 190 GLN A O 1 ATOM 1418 C CB . GLN A 1 186 ? 100.573 158.860 18.726 1.00 49.60 ? 190 GLN A CB 1 ATOM 1419 C CG . GLN A 1 186 ? 100.383 160.387 18.815 1.00 63.48 ? 190 GLN A CG 1 ATOM 1420 C CD . GLN A 1 186 ? 98.967 160.879 18.597 1.00 71.28 ? 190 GLN A CD 1 ATOM 1421 O OE1 . GLN A 1 186 ? 98.754 161.985 18.098 1.00 62.44 ? 190 GLN A OE1 1 ATOM 1422 N NE2 . GLN A 1 186 ? 97.965 160.088 18.969 1.00 61.54 ? 190 GLN A NE2 1 ATOM 1423 N N . GLY A 1 187 ? 99.294 159.124 15.910 1.00 41.06 ? 191 GLY A N 1 ATOM 1424 C CA . GLY A 1 187 ? 98.662 159.887 14.849 1.00 38.82 ? 191 GLY A CA 1 ATOM 1425 C C . GLY A 1 187 ? 97.219 160.179 15.196 1.00 40.90 ? 191 GLY A C 1 ATOM 1426 O O . GLY A 1 187 ? 96.520 159.319 15.743 1.00 41.03 ? 191 GLY A O 1 ATOM 1427 N N . VAL A 1 188 ? 96.767 161.397 14.895 1.00 35.23 ? 192 VAL A N 1 ATOM 1428 C CA . VAL A 1 188 ? 95.399 161.794 15.194 1.00 33.25 ? 192 VAL A CA 1 ATOM 1429 C C . VAL A 1 188 ? 94.611 162.128 13.952 1.00 32.08 ? 192 VAL A C 1 ATOM 1430 O O . VAL A 1 188 ? 95.132 162.774 13.058 1.00 31.18 ? 192 VAL A O 1 ATOM 1431 C CB . VAL A 1 188 ? 95.356 162.890 16.290 1.00 39.25 ? 192 VAL A CB 1 ATOM 1432 C CG1 . VAL A 1 188 ? 94.157 163.826 16.144 1.00 38.63 ? 192 VAL A CG1 1 ATOM 1433 C CG2 . VAL A 1 188 ? 95.364 162.250 17.668 1.00 40.75 ? 192 VAL A CG2 1 ATOM 1434 N N . ILE A 1 189 ? 93.363 161.665 13.898 1.00 26.07 ? 193 ILE A N 1 ATOM 1435 C CA . ILE A 1 189 ? 92.426 161.974 12.835 1.00 24.69 ? 193 ILE A CA 1 ATOM 1436 C C . ILE A 1 189 ? 91.232 162.715 13.439 1.00 29.76 ? 193 ILE A C 1 ATOM 1437 O O . ILE A 1 189 ? 90.643 162.256 14.423 1.00 29.42 ? 193 ILE A O 1 ATOM 1438 C CB . ILE A 1 189 ? 92.025 160.752 11.961 1.00 26.63 ? 193 ILE A CB 1 ATOM 1439 C CG1 . ILE A 1 189 ? 91.088 161.187 10.798 1.00 26.38 ? 193 ILE A CG1 1 ATOM 1440 C CG2 . ILE A 1 189 ? 91.436 159.597 12.798 1.00 27.31 ? 193 ILE A CG2 1 ATOM 1441 C CD1 . ILE A 1 189 ? 90.814 160.182 9.744 1.00 34.80 ? 193 ILE A CD1 1 ATOM 1442 N N . THR A 1 190 ? 90.916 163.884 12.874 1.00 27.20 ? 194 THR A N 1 ATOM 1443 C CA . THR A 1 190 ? 89.781 164.694 13.292 1.00 27.88 ? 194 THR A CA 1 ATOM 1444 C C . THR A 1 190 ? 88.936 165.041 12.081 1.00 31.08 ? 194 THR A C 1 ATOM 1445 O O . THR A 1 190 ? 89.485 165.362 11.030 1.00 29.23 ? 194 THR A O 1 ATOM 1446 C CB . THR A 1 190 ? 90.203 165.851 14.192 1.00 39.23 ? 194 THR A CB 1 ATOM 1447 O OG1 . THR A 1 190 ? 89.044 166.412 14.813 1.00 42.69 ? 194 THR A OG1 1 ATOM 1448 C CG2 . THR A 1 190 ? 90.953 166.911 13.457 1.00 37.91 ? 194 THR A CG2 1 ATOM 1449 N N . TRP A 1 191 ? 87.603 164.930 12.220 1.00 29.22 ? 195 TRP A N 1 ATOM 1450 C CA . TRP A 1 191 ? 86.646 165.134 11.131 1.00 29.27 ? 195 TRP A CA 1 ATOM 1451 C C . TRP A 1 191 ? 85.339 165.814 11.556 1.00 32.69 ? 195 TRP A C 1 ATOM 1452 O O . TRP A 1 191 ? 85.103 166.057 12.741 1.00 31.90 ? 195 TRP A O 1 ATOM 1453 C CB . TRP A 1 191 ? 86.306 163.767 10.503 1.00 27.11 ? 195 TRP A CB 1 ATOM 1454 C CG . TRP A 1 191 ? 85.601 162.842 11.458 1.00 28.15 ? 195 TRP A CG 1 ATOM 1455 C CD1 . TRP A 1 191 ? 84.252 162.696 11.617 1.00 31.61 ? 195 TRP A CD1 1 ATOM 1456 C CD2 . TRP A 1 191 ? 86.215 162.004 12.446 1.00 27.72 ? 195 TRP A CD2 1 ATOM 1457 N NE1 . TRP A 1 191 ? 83.988 161.789 12.618 1.00 30.90 ? 195 TRP A NE1 1 ATOM 1458 C CE2 . TRP A 1 191 ? 85.175 161.337 13.135 1.00 31.97 ? 195 TRP A CE2 1 ATOM 1459 C CE3 . TRP A 1 191 ? 87.548 161.714 12.787 1.00 28.68 ? 195 TRP A CE3 1 ATOM 1460 C CZ2 . TRP A 1 191 ? 85.426 160.413 14.156 1.00 31.37 ? 195 TRP A CZ2 1 ATOM 1461 C CZ3 . TRP A 1 191 ? 87.795 160.791 13.790 1.00 30.59 ? 195 TRP A CZ3 1 ATOM 1462 C CH2 . TRP A 1 191 ? 86.742 160.165 14.475 1.00 31.55 ? 195 TRP A CH2 1 ATOM 1463 N N . ASN A 1 192 ? 84.475 166.062 10.560 1.00 29.71 ? 196 ASN A N 1 ATOM 1464 C CA . ASN A 1 192 ? 83.121 166.580 10.701 1.00 31.23 ? 196 ASN A CA 1 ATOM 1465 C C . ASN A 1 192 ? 82.193 165.448 10.248 1.00 35.60 ? 196 ASN A C 1 ATOM 1466 O O . ASN A 1 192 ? 82.516 164.773 9.261 1.00 34.09 ? 196 ASN A O 1 ATOM 1467 C CB . ASN A 1 192 ? 82.888 167.802 9.810 1.00 30.64 ? 196 ASN A CB 1 ATOM 1468 C CG . ASN A 1 192 ? 83.518 169.083 10.281 1.00 36.09 ? 196 ASN A CG 1 ATOM 1469 O OD1 . ASN A 1 192 ? 83.619 169.378 11.475 1.00 24.32 ? 196 ASN A OD1 1 ATOM 1470 N ND2 . ASN A 1 192 ? 83.915 169.906 9.334 1.00 27.92 ? 196 ASN A ND2 1 ATOM 1471 N N . PRO A 1 193 ? 81.053 165.217 10.941 1.00 33.33 ? 197 PRO A N 1 ATOM 1472 C CA . PRO A 1 193 ? 80.153 164.119 10.550 1.00 32.93 ? 197 PRO A CA 1 ATOM 1473 C C . PRO A 1 193 ? 79.518 164.245 9.163 1.00 38.94 ? 197 PRO A C 1 ATOM 1474 O O . PRO A 1 193 ? 79.336 165.362 8.692 1.00 41.18 ? 197 PRO A O 1 ATOM 1475 C CB . PRO A 1 193 ? 79.077 164.156 11.635 1.00 36.08 ? 197 PRO A CB 1 ATOM 1476 C CG . PRO A 1 193 ? 79.089 165.554 12.125 1.00 42.56 ? 197 PRO A CG 1 ATOM 1477 C CD . PRO A 1 193 ? 80.538 165.915 12.132 1.00 36.87 ? 197 PRO A CD 1 ATOM 1478 N N . PRO A 1 194 ? 79.131 163.120 8.515 1.00 34.67 ? 198 PRO A N 1 ATOM 1479 C CA . PRO A 1 194 ? 78.464 163.216 7.205 1.00 35.48 ? 198 PRO A CA 1 ATOM 1480 C C . PRO A 1 194 ? 77.025 163.773 7.288 1.00 42.37 ? 198 PRO A C 1 ATOM 1481 O O . PRO A 1 194 ? 76.443 163.804 8.378 1.00 42.71 ? 198 PRO A O 1 ATOM 1482 C CB . PRO A 1 194 ? 78.492 161.774 6.715 1.00 35.75 ? 198 PRO A CB 1 ATOM 1483 C CG . PRO A 1 194 ? 78.459 160.958 7.929 1.00 38.99 ? 198 PRO A CG 1 ATOM 1484 C CD . PRO A 1 194 ? 79.272 161.710 8.936 1.00 34.44 ? 198 PRO A CD 1 ATOM 1485 N N . GLN A 1 195 ? 76.449 164.190 6.136 1.00 40.61 ? 199 GLN A N 1 ATOM 1486 C CA . GLN A 1 195 ? 75.126 164.822 6.049 1.00 43.65 ? 199 GLN A CA 1 ATOM 1487 C C . GLN A 1 195 ? 73.861 163.976 6.240 1.00 50.94 ? 199 GLN A C 1 ATOM 1488 O O . GLN A 1 195 ? 72.849 164.515 6.720 1.00 53.71 ? 199 GLN A O 1 ATOM 1489 C CB . GLN A 1 195 ? 75.010 165.712 4.813 1.00 46.58 ? 199 GLN A CB 1 ATOM 1490 C CG . GLN A 1 195 ? 74.951 167.191 5.157 1.00 62.06 ? 199 GLN A CG 1 ATOM 1491 C CD . GLN A 1 195 ? 74.485 168.021 3.989 1.00 90.01 ? 199 GLN A CD 1 ATOM 1492 O OE1 . GLN A 1 195 ? 75.109 168.048 2.918 1.00 84.43 ? 199 GLN A OE1 1 ATOM 1493 N NE2 . GLN A 1 195 ? 73.378 168.732 4.179 1.00 90.07 ? 199 GLN A NE2 1 ATOM 1494 N N . ARG A 1 196 ? 73.888 162.684 5.845 1.00 45.73 ? 200 ARG A N 1 ATOM 1495 C CA . ARG A 1 196 ? 72.713 161.803 5.968 1.00 45.97 ? 200 ARG A CA 1 ATOM 1496 C C . ARG A 1 196 ? 72.656 161.070 7.317 1.00 46.79 ? 200 ARG A C 1 ATOM 1497 O O . ARG A 1 196 ? 73.503 161.315 8.187 1.00 45.32 ? 200 ARG A O 1 ATOM 1498 C CB . ARG A 1 196 ? 72.655 160.813 4.793 1.00 46.29 ? 200 ARG A CB 1 ATOM 1499 C CG . ARG A 1 196 ? 71.420 160.967 3.913 1.00 57.77 ? 200 ARG A CG 1 ATOM 1500 C CD . ARG A 1 196 ? 71.669 160.501 2.486 1.00 64.13 ? 200 ARG A CD 1 ATOM 1501 N NE . ARG A 1 196 ? 72.324 161.535 1.678 1.00 72.81 ? 200 ARG A NE 1 ATOM 1502 C CZ . ARG A 1 196 ? 73.598 161.506 1.299 1.00 82.07 ? 200 ARG A CZ 1 ATOM 1503 N NH1 . ARG A 1 196 ? 74.376 160.484 1.638 1.00 63.28 ? 200 ARG A NH1 1 ATOM 1504 N NH2 . ARG A 1 196 ? 74.102 162.492 0.568 1.00 67.83 ? 200 ARG A NH2 1 ATOM 1505 N N . SER A 1 197 ? 71.635 160.199 7.499 1.00 42.27 ? 201 SER A N 1 ATOM 1506 C CA . SER A 1 197 ? 71.452 159.389 8.708 1.00 40.36 ? 201 SER A CA 1 ATOM 1507 C C . SER A 1 197 ? 72.339 158.154 8.639 1.00 39.15 ? 201 SER A C 1 ATOM 1508 O O . SER A 1 197 ? 72.423 157.517 7.592 1.00 38.34 ? 201 SER A O 1 ATOM 1509 C CB . SER A 1 197 ? 69.997 158.961 8.859 1.00 46.10 ? 201 SER A CB 1 ATOM 1510 O OG . SER A 1 197 ? 69.146 160.092 8.899 1.00 59.46 ? 201 SER A OG 1 ATOM 1511 N N . PHE A 1 198 ? 73.009 157.827 9.748 1.00 32.60 ? 202 PHE A N 1 ATOM 1512 C CA . PHE A 1 198 ? 73.898 156.672 9.864 1.00 29.18 ? 202 PHE A CA 1 ATOM 1513 C C . PHE A 1 198 ? 73.921 156.113 11.306 1.00 32.00 ? 202 PHE A C 1 ATOM 1514 O O . PHE A 1 198 ? 73.347 156.717 12.222 1.00 31.91 ? 202 PHE A O 1 ATOM 1515 C CB . PHE A 1 198 ? 75.304 157.031 9.369 1.00 28.78 ? 202 PHE A CB 1 ATOM 1516 C CG . PHE A 1 198 ? 76.041 158.024 10.233 1.00 29.84 ? 202 PHE A CG 1 ATOM 1517 C CD1 . PHE A 1 198 ? 75.803 159.388 10.111 1.00 34.15 ? 202 PHE A CD1 1 ATOM 1518 C CD2 . PHE A 1 198 ? 76.992 157.599 11.152 1.00 30.66 ? 202 PHE A CD2 1 ATOM 1519 C CE1 . PHE A 1 198 ? 76.481 160.306 10.914 1.00 35.21 ? 202 PHE A CE1 1 ATOM 1520 C CE2 . PHE A 1 198 ? 77.689 158.518 11.932 1.00 33.70 ? 202 PHE A CE2 1 ATOM 1521 C CZ . PHE A 1 198 ? 77.422 159.866 11.817 1.00 33.13 ? 202 PHE A CZ 1 ATOM 1522 N N . HIS A 1 199 ? 74.588 154.967 11.503 1.00 27.49 ? 203 HIS A N 1 ATOM 1523 C CA . HIS A 1 199 ? 74.663 154.344 12.820 1.00 27.72 ? 203 HIS A CA 1 ATOM 1524 C C . HIS A 1 199 ? 76.029 154.390 13.488 1.00 31.25 ? 203 HIS A C 1 ATOM 1525 O O . HIS A 1 199 ? 76.084 154.491 14.721 1.00 31.73 ? 203 HIS A O 1 ATOM 1526 C CB . HIS A 1 199 ? 74.108 152.917 12.794 1.00 28.53 ? 203 HIS A CB 1 ATOM 1527 C CG . HIS A 1 199 ? 72.648 152.843 12.486 1.00 33.49 ? 203 HIS A CG 1 ATOM 1528 N ND1 . HIS A 1 199 ? 72.116 151.776 11.791 1.00 35.56 ? 203 HIS A ND1 1 ATOM 1529 C CD2 . HIS A 1 199 ? 71.658 153.720 12.765 1.00 36.67 ? 203 HIS A CD2 1 ATOM 1530 C CE1 . HIS A 1 199 ? 70.825 152.029 11.679 1.00 36.73 ? 203 HIS A CE1 1 ATOM 1531 N NE2 . HIS A 1 199 ? 70.505 153.189 12.248 1.00 37.96 ? 203 HIS A NE2 1 ATOM 1532 N N . ASN A 1 200 ? 77.120 154.298 12.690 1.00 25.88 ? 204 ASN A N 1 ATOM 1533 C CA . ASN A 1 200 ? 78.503 154.289 13.181 1.00 24.59 ? 204 ASN A CA 1 ATOM 1534 C C . ASN A 1 200 ? 79.530 154.565 12.089 1.00 28.30 ? 204 ASN A C 1 ATOM 1535 O O . ASN A 1 200 ? 79.217 154.498 10.898 1.00 27.72 ? 204 ASN A O 1 ATOM 1536 C CB . ASN A 1 200 ? 78.834 152.924 13.766 1.00 23.13 ? 204 ASN A CB 1 ATOM 1537 C CG . ASN A 1 200 ? 78.546 152.705 15.215 1.00 48.55 ? 204 ASN A CG 1 ATOM 1538 O OD1 . ASN A 1 200 ? 78.575 153.627 16.048 1.00 50.87 ? 204 ASN A OD1 1 ATOM 1539 N ND2 . ASN A 1 200 ? 78.296 151.442 15.522 1.00 36.39 ? 204 ASN A ND2 1 ATOM 1540 N N . PHE A 1 201 ? 80.792 154.787 12.518 1.00 24.32 ? 205 PHE A N 1 ATOM 1541 C CA . PHE A 1 201 ? 81.949 155.024 11.659 1.00 22.65 ? 205 PHE A CA 1 ATOM 1542 C C . PHE A 1 201 ? 82.858 153.808 11.615 1.00 26.61 ? 205 PHE A C 1 ATOM 1543 O O . PHE A 1 201 ? 82.925 153.054 12.582 1.00 27.04 ? 205 PHE A O 1 ATOM 1544 C CB . PHE A 1 201 ? 82.768 156.207 12.181 1.00 23.87 ? 205 PHE A CB 1 ATOM 1545 C CG . PHE A 1 201 ? 82.121 157.561 12.064 1.00 25.33 ? 205 PHE A CG 1 ATOM 1546 C CD1 . PHE A 1 201 ? 81.943 158.159 10.823 1.00 27.87 ? 205 PHE A CD1 1 ATOM 1547 C CD2 . PHE A 1 201 ? 81.767 158.279 13.201 1.00 27.62 ? 205 PHE A CD2 1 ATOM 1548 C CE1 . PHE A 1 201 ? 81.387 159.435 10.719 1.00 29.71 ? 205 PHE A CE1 1 ATOM 1549 C CE2 . PHE A 1 201 ? 81.209 159.552 13.096 1.00 31.15 ? 205 PHE A CE2 1 ATOM 1550 C CZ . PHE A 1 201 ? 81.022 160.123 11.856 1.00 29.31 ? 205 PHE A CZ 1 ATOM 1551 N N . THR A 1 202 ? 83.602 153.657 10.521 1.00 22.91 ? 206 THR A N 1 ATOM 1552 C CA . THR A 1 202 ? 84.564 152.579 10.356 1.00 23.14 ? 206 THR A CA 1 ATOM 1553 C C . THR A 1 202 ? 85.923 153.183 9.994 1.00 28.82 ? 206 THR A C 1 ATOM 1554 O O . THR A 1 202 ? 86.114 153.679 8.870 1.00 29.13 ? 206 THR A O 1 ATOM 1555 C CB . THR A 1 202 ? 84.033 151.545 9.365 1.00 30.75 ? 206 THR A CB 1 ATOM 1556 O OG1 . THR A 1 202 ? 82.804 151.033 9.871 1.00 32.63 ? 206 THR A OG1 1 ATOM 1557 C CG2 . THR A 1 202 ? 85.020 150.407 9.097 1.00 28.20 ? 206 THR A CG2 1 ATOM 1558 N N . LEU A 1 203 ? 86.856 153.170 10.963 1.00 24.95 ? 207 LEU A N 1 ATOM 1559 C CA . LEU A 1 203 ? 88.193 153.702 10.742 1.00 24.51 ? 207 LEU A CA 1 ATOM 1560 C C . LEU A 1 203 ? 89.174 152.575 10.395 1.00 30.05 ? 207 LEU A C 1 ATOM 1561 O O . LEU A 1 203 ? 89.122 151.520 11.009 1.00 28.63 ? 207 LEU A O 1 ATOM 1562 C CB . LEU A 1 203 ? 88.673 154.550 11.942 1.00 24.44 ? 207 LEU A CB 1 ATOM 1563 C CG . LEU A 1 203 ? 90.091 155.152 11.854 1.00 28.65 ? 207 LEU A CG 1 ATOM 1564 C CD1 . LEU A 1 203 ? 90.179 156.277 10.818 1.00 28.18 ? 207 LEU A CD1 1 ATOM 1565 C CD2 . LEU A 1 203 ? 90.587 155.608 13.202 1.00 30.22 ? 207 LEU A CD2 1 ATOM 1566 N N . CYS A 1 204 ? 90.031 152.799 9.378 1.00 29.81 ? 208 CYS A N 1 ATOM 1567 C CA . CYS A 1 204 ? 91.056 151.859 8.919 1.00 31.92 ? 208 CYS A CA 1 ATOM 1568 C C . CYS A 1 204 ? 92.401 152.558 8.836 1.00 33.66 ? 208 CYS A C 1 ATOM 1569 O O . CYS A 1 204 ? 92.458 153.695 8.376 1.00 32.69 ? 208 CYS A O 1 ATOM 1570 C CB . CYS A 1 204 ? 90.684 151.245 7.573 1.00 33.84 ? 208 CYS A CB 1 ATOM 1571 S SG . CYS A 1 204 ? 89.050 150.463 7.536 1.00 38.56 ? 208 CYS A SG 1 ATOM 1572 N N . TYR A 1 205 ? 93.479 151.882 9.279 1.00 29.13 ? 209 TYR A N 1 ATOM 1573 C CA . TYR A 1 205 ? 94.851 152.388 9.179 1.00 28.62 ? 209 TYR A CA 1 ATOM 1574 C C . TYR A 1 205 ? 95.654 151.413 8.330 1.00 30.58 ? 209 TYR A C 1 ATOM 1575 O O . TYR A 1 205 ? 95.749 150.227 8.658 1.00 30.43 ? 209 TYR A O 1 ATOM 1576 C CB . TYR A 1 205 ? 95.499 152.730 10.542 1.00 30.80 ? 209 TYR A CB 1 ATOM 1577 C CG . TYR A 1 205 ? 95.530 151.620 11.573 1.00 34.01 ? 209 TYR A CG 1 ATOM 1578 C CD1 . TYR A 1 205 ? 94.440 151.386 12.407 1.00 35.61 ? 209 TYR A CD1 1 ATOM 1579 C CD2 . TYR A 1 205 ? 96.688 150.882 11.794 1.00 36.66 ? 209 TYR A CD2 1 ATOM 1580 C CE1 . TYR A 1 205 ? 94.474 150.388 13.380 1.00 38.15 ? 209 TYR A CE1 1 ATOM 1581 C CE2 . TYR A 1 205 ? 96.739 149.888 12.769 1.00 38.89 ? 209 TYR A CE2 1 ATOM 1582 C CZ . TYR A 1 205 ? 95.631 149.647 13.566 1.00 47.54 ? 209 TYR A CZ 1 ATOM 1583 O OH . TYR A 1 205 ? 95.672 148.659 14.525 1.00 50.20 ? 209 TYR A OH 1 ATOM 1584 N N . ILE A 1 206 ? 96.147 151.903 7.185 1.00 26.20 ? 210 ILE A N 1 ATOM 1585 C CA . ILE A 1 206 ? 96.843 151.100 6.180 1.00 27.27 ? 210 ILE A CA 1 ATOM 1586 C C . ILE A 1 206 ? 98.362 151.356 6.055 1.00 33.80 ? 210 ILE A C 1 ATOM 1587 O O . ILE A 1 206 ? 98.793 152.428 5.628 1.00 33.10 ? 210 ILE A O 1 ATOM 1588 C CB . ILE A 1 206 ? 96.088 151.174 4.824 1.00 29.42 ? 210 ILE A CB 1 ATOM 1589 C CG1 . ILE A 1 206 ? 94.605 150.753 4.975 1.00 28.03 ? 210 ILE A CG1 1 ATOM 1590 C CG2 . ILE A 1 206 ? 96.777 150.336 3.750 1.00 32.38 ? 210 ILE A CG2 1 ATOM 1591 C CD1 . ILE A 1 206 ? 93.600 151.819 4.680 1.00 29.41 ? 210 ILE A CD1 1 ATOM 1592 N N . LYS A 1 207 ? 99.156 150.334 6.398 1.00 33.38 ? 211 LYS A N 1 ATOM 1593 C CA . LYS A 1 207 ? 100.613 150.338 6.333 1.00 36.15 ? 211 LYS A CA 1 ATOM 1594 C C . LYS A 1 207 ? 101.022 149.292 5.280 1.00 45.14 ? 211 LYS A C 1 ATOM 1595 O O . LYS A 1 207 ? 101.365 148.153 5.616 1.00 46.67 ? 211 LYS A O 1 ATOM 1596 C CB . LYS A 1 207 ? 101.202 150.039 7.724 1.00 39.19 ? 211 LYS A CB 1 ATOM 1597 C CG . LYS A 1 207 ? 102.713 150.138 7.825 1.00 49.08 ? 211 LYS A CG 1 ATOM 1598 C CD . LYS A 1 207 ? 103.224 149.297 8.980 1.00 61.29 ? 211 LYS A CD 1 ATOM 1599 C CE . LYS A 1 207 ? 104.671 148.903 8.816 1.00 81.16 ? 211 LYS A CE 1 ATOM 1600 N NZ . LYS A 1 207 ? 104.849 147.797 7.836 1.00 93.07 ? 211 LYS A NZ 1 ATOM 1601 N N . GLU A 1 208 ? 100.971 149.706 3.990 1.00 43.50 ? 212 GLU A N 1 ATOM 1602 C CA . GLU A 1 208 ? 101.274 148.912 2.787 1.00 45.67 ? 212 GLU A CA 1 ATOM 1603 C C . GLU A 1 208 ? 100.236 147.786 2.607 1.00 49.01 ? 212 GLU A C 1 ATOM 1604 O O . GLU A 1 208 ? 99.039 148.071 2.505 1.00 45.88 ? 212 GLU A O 1 ATOM 1605 C CB . GLU A 1 208 ? 102.730 148.386 2.771 1.00 50.72 ? 212 GLU A CB 1 ATOM 1606 C CG . GLU A 1 208 ? 103.801 149.440 3.010 1.00 67.99 ? 212 GLU A CG 1 ATOM 1607 C CD . GLU A 1 208 ? 104.167 149.674 4.466 1.00 102.73 ? 212 GLU A CD 1 ATOM 1608 O OE1 . GLU A 1 208 ? 104.417 148.681 5.189 1.00 106.69 ? 212 GLU A OE1 1 ATOM 1609 O OE2 . GLU A 1 208 ? 104.180 150.853 4.889 1.00 98.60 ? 212 GLU A OE2 1 ATOM 1610 N N . THR A 1 209 ? 100.682 146.519 2.613 1.00 48.37 ? 213 THR A N 1 ATOM 1611 C CA . THR A 1 209 ? 99.829 145.336 2.487 1.00 48.68 ? 213 THR A CA 1 ATOM 1612 C C . THR A 1 209 ? 98.964 145.101 3.737 1.00 50.58 ? 213 THR A C 1 ATOM 1613 O O . THR A 1 209 ? 97.962 144.389 3.654 1.00 49.66 ? 213 THR A O 1 ATOM 1614 C CB . THR A 1 209 ? 100.674 144.113 2.139 1.00 66.26 ? 213 THR A CB 1 ATOM 1615 O OG1 . THR A 1 209 ? 101.827 144.080 2.988 1.00 71.66 ? 213 THR A OG1 1 ATOM 1616 C CG2 . THR A 1 209 ? 101.093 144.095 0.675 1.00 67.61 ? 213 THR A CG2 1 ATOM 1617 N N . GLU A 1 210 ? 99.354 145.706 4.884 1.00 46.34 ? 214 GLU A N 1 ATOM 1618 C CA . GLU A 1 210 ? 98.668 145.638 6.181 1.00 44.47 ? 214 GLU A CA 1 ATOM 1619 C C . GLU A 1 210 ? 97.504 146.635 6.248 1.00 45.08 ? 214 GLU A C 1 ATOM 1620 O O . GLU A 1 210 ? 97.599 147.733 5.698 1.00 44.04 ? 214 GLU A O 1 ATOM 1621 C CB . GLU A 1 210 ? 99.644 145.916 7.336 1.00 46.94 ? 214 GLU A CB 1 ATOM 1622 C CG . GLU A 1 210 ? 100.700 144.847 7.547 1.00 62.82 ? 214 GLU A CG 1 ATOM 1623 C CD . GLU A 1 210 ? 101.893 144.942 6.615 1.00 96.64 ? 214 GLU A CD 1 ATOM 1624 O OE1 . GLU A 1 210 ? 102.761 145.815 6.846 1.00 99.27 ? 214 GLU A OE1 1 ATOM 1625 O OE2 . GLU A 1 210 ? 101.954 144.149 5.648 1.00 95.51 ? 214 GLU A OE2 1 ATOM 1626 N N . LYS A 1 211 ? 96.410 146.244 6.928 1.00 39.55 ? 215 LYS A N 1 ATOM 1627 C CA . LYS A 1 211 ? 95.199 147.043 7.117 1.00 36.41 ? 215 LYS A CA 1 ATOM 1628 C C . LYS A 1 211 ? 94.430 146.526 8.327 1.00 40.97 ? 215 LYS A C 1 ATOM 1629 O O . LYS A 1 211 ? 94.139 145.330 8.407 1.00 42.36 ? 215 LYS A O 1 ATOM 1630 C CB . LYS A 1 211 ? 94.301 146.995 5.858 1.00 36.90 ? 215 LYS A CB 1 ATOM 1631 C CG . LYS A 1 211 ? 92.907 147.628 6.015 1.00 38.51 ? 215 LYS A CG 1 ATOM 1632 C CD . LYS A 1 211 ? 92.148 147.559 4.705 1.00 46.68 ? 215 LYS A CD 1 ATOM 1633 C CE . LYS A 1 211 ? 90.817 148.261 4.718 1.00 54.96 ? 215 LYS A CE 1 ATOM 1634 N NZ . LYS A 1 211 ? 89.980 147.854 3.555 1.00 64.19 ? 215 LYS A NZ 1 ATOM 1635 N N . ASP A 1 212 ? 94.087 147.431 9.256 1.00 35.87 ? 216 ASP A N 1 ATOM 1636 C CA . ASP A 1 212 ? 93.278 147.106 10.425 1.00 34.83 ? 216 ASP A CA 1 ATOM 1637 C C . ASP A 1 212 ? 92.165 148.122 10.510 1.00 35.74 ? 216 ASP A C 1 ATOM 1638 O O . ASP A 1 212 ? 92.417 149.320 10.377 1.00 32.56 ? 216 ASP A O 1 ATOM 1639 C CB . ASP A 1 212 ? 94.102 147.087 11.721 1.00 37.87 ? 216 ASP A CB 1 ATOM 1640 C CG . ASP A 1 212 ? 95.403 146.325 11.618 1.00 47.89 ? 216 ASP A CG 1 ATOM 1641 O OD1 . ASP A 1 212 ? 96.368 146.878 11.043 1.00 49.30 ? 216 ASP A OD1 1 ATOM 1642 O OD2 . ASP A 1 212 ? 95.456 145.173 12.102 1.00 52.73 ? 216 ASP A OD2 1 ATOM 1643 N N . CYS A 1 213 ? 90.929 147.633 10.683 1.00 34.01 ? 217 CYS A N 1 ATOM 1644 C CA . CYS A 1 213 ? 89.756 148.486 10.797 1.00 33.62 ? 217 CYS A CA 1 ATOM 1645 C C . CYS A 1 213 ? 89.144 148.498 12.194 1.00 35.45 ? 217 CYS A C 1 ATOM 1646 O O . CYS A 1 213 ? 89.476 147.653 13.034 1.00 35.95 ? 217 CYS A O 1 ATOM 1647 C CB . CYS A 1 213 ? 88.730 148.204 9.705 1.00 34.83 ? 217 CYS A CB 1 ATOM 1648 S SG . CYS A 1 213 ? 89.357 148.488 8.025 1.00 40.02 ? 217 CYS A SG 1 ATOM 1649 N N . LEU A 1 214 ? 88.317 149.515 12.462 1.00 29.61 ? 218 LEU A N 1 ATOM 1650 C CA . LEU A 1 214 ? 87.690 149.764 13.753 1.00 28.57 ? 218 LEU A CA 1 ATOM 1651 C C . LEU A 1 214 ? 86.196 150.065 13.604 1.00 32.99 ? 218 LEU A C 1 ATOM 1652 O O . LEU A 1 214 ? 85.621 149.902 12.523 1.00 32.51 ? 218 LEU A O 1 ATOM 1653 C CB . LEU A 1 214 ? 88.387 150.963 14.419 1.00 28.02 ? 218 LEU A CB 1 ATOM 1654 C CG . LEU A 1 214 ? 89.784 150.735 14.950 1.00 33.29 ? 218 LEU A CG 1 ATOM 1655 C CD1 . LEU A 1 214 ? 90.837 151.194 13.950 1.00 33.19 ? 218 LEU A CD1 1 ATOM 1656 C CD2 . LEU A 1 214 ? 89.980 151.484 16.240 1.00 37.20 ? 218 LEU A CD2 1 ATOM 1657 N N . ASN A 1 215 ? 85.574 150.492 14.711 1.00 30.16 ? 219 ASN A N 1 ATOM 1658 C CA . ASN A 1 215 ? 84.171 150.872 14.795 1.00 29.55 ? 219 ASN A CA 1 ATOM 1659 C C . ASN A 1 215 ? 84.063 152.020 15.786 1.00 32.65 ? 219 ASN A C 1 ATOM 1660 O O . ASN A 1 215 ? 84.343 151.848 16.979 1.00 33.31 ? 219 ASN A O 1 ATOM 1661 C CB . ASN A 1 215 ? 83.294 149.684 15.203 1.00 29.85 ? 219 ASN A CB 1 ATOM 1662 C CG . ASN A 1 215 ? 82.170 149.385 14.244 1.00 49.52 ? 219 ASN A CG 1 ATOM 1663 O OD1 . ASN A 1 215 ? 82.304 149.469 13.009 1.00 39.51 ? 219 ASN A OD1 1 ATOM 1664 N ND2 . ASN A 1 215 ? 81.055 148.939 14.800 1.00 45.09 ? 219 ASN A ND2 1 ATOM 1665 N N . LEU A 1 216 ? 83.726 153.208 15.276 1.00 27.43 ? 220 LEU A N 1 ATOM 1666 C CA . LEU A 1 216 ? 83.611 154.407 16.099 1.00 27.15 ? 220 LEU A CA 1 ATOM 1667 C C . LEU A 1 216 ? 82.174 154.888 16.235 1.00 31.17 ? 220 LEU A C 1 ATOM 1668 O O . LEU A 1 216 ? 81.423 154.894 15.252 1.00 30.47 ? 220 LEU A O 1 ATOM 1669 C CB . LEU A 1 216 ? 84.478 155.552 15.554 1.00 26.03 ? 220 LEU A CB 1 ATOM 1670 C CG . LEU A 1 216 ? 85.949 155.300 15.267 1.00 28.92 ? 220 LEU A CG 1 ATOM 1671 C CD1 . LEU A 1 216 ? 86.547 156.477 14.523 1.00 29.10 ? 220 LEU A CD1 1 ATOM 1672 C CD2 . LEU A 1 216 ? 86.726 155.033 16.514 1.00 28.97 ? 220 LEU A CD2 1 ATOM 1673 N N . ASP A 1 217 ? 81.822 155.334 17.454 1.00 27.93 ? 221 ASP A N 1 ATOM 1674 C CA . ASP A 1 217 ? 80.526 155.896 17.823 1.00 28.74 ? 221 ASP A CA 1 ATOM 1675 C C . ASP A 1 217 ? 80.196 157.122 16.964 1.00 32.67 ? 221 ASP A C 1 ATOM 1676 O O . ASP A 1 217 ? 81.060 157.986 16.769 1.00 32.48 ? 221 ASP A O 1 ATOM 1677 C CB . ASP A 1 217 ? 80.554 156.301 19.297 1.00 32.02 ? 221 ASP A CB 1 ATOM 1678 C CG . ASP A 1 217 ? 79.230 156.793 19.813 1.00 40.69 ? 221 ASP A CG 1 ATOM 1679 O OD1 . ASP A 1 217 ? 78.400 155.949 20.214 1.00 41.94 ? 221 ASP A OD1 1 ATOM 1680 O OD2 . ASP A 1 217 ? 79.016 158.015 19.805 1.00 45.48 ? 221 ASP A OD2 1 ATOM 1681 N N . LYS A 1 218 ? 78.930 157.208 16.490 1.00 28.55 ? 222 LYS A N 1 ATOM 1682 C CA . LYS A 1 218 ? 78.416 158.297 15.643 1.00 27.67 ? 222 LYS A CA 1 ATOM 1683 C C . LYS A 1 218 ? 78.691 159.706 16.167 1.00 30.83 ? 222 LYS A C 1 ATOM 1684 O O . LYS A 1 218 ? 78.789 160.637 15.367 1.00 30.23 ? 222 LYS A O 1 ATOM 1685 C CB . LYS A 1 218 ? 76.925 158.101 15.285 1.00 30.97 ? 222 LYS A CB 1 ATOM 1686 C CG . LYS A 1 218 ? 75.967 157.970 16.459 1.00 47.79 ? 222 LYS A CG 1 ATOM 1687 C CD . LYS A 1 218 ? 74.669 157.269 16.051 1.00 62.55 ? 222 LYS A CD 1 ATOM 1688 C CE . LYS A 1 218 ? 73.549 158.216 15.671 1.00 78.53 ? 222 LYS A CE 1 ATOM 1689 N NZ . LYS A 1 218 ? 72.220 157.539 15.686 1.00 85.70 ? 222 LYS A NZ 1 ATOM 1690 N N . ASN A 1 219 ? 78.857 159.846 17.499 1.00 27.90 ? 223 ASN A N 1 ATOM 1691 C CA . ASN A 1 219 ? 79.110 161.121 18.166 1.00 28.82 ? 223 ASN A CA 1 ATOM 1692 C C . ASN A 1 219 ? 80.546 161.601 18.234 1.00 33.07 ? 223 ASN A C 1 ATOM 1693 O O . ASN A 1 219 ? 80.758 162.785 18.510 1.00 33.98 ? 223 ASN A O 1 ATOM 1694 C CB . ASN A 1 219 ? 78.438 161.187 19.519 1.00 27.01 ? 223 ASN A CB 1 ATOM 1695 C CG . ASN A 1 219 ? 76.980 161.403 19.367 1.00 49.66 ? 223 ASN A CG 1 ATOM 1696 O OD1 . ASN A 1 219 ? 76.534 162.511 19.058 1.00 50.19 ? 223 ASN A OD1 1 ATOM 1697 N ND2 . ASN A 1 219 ? 76.223 160.326 19.457 1.00 41.35 ? 223 ASN A ND2 1 ATOM 1698 N N . LEU A 1 220 ? 81.533 160.726 18.006 1.00 28.58 ? 224 LEU A N 1 ATOM 1699 C CA . LEU A 1 220 ? 82.894 161.239 18.067 1.00 28.67 ? 224 LEU A CA 1 ATOM 1700 C C . LEU A 1 220 ? 83.357 161.917 16.791 1.00 33.89 ? 224 LEU A C 1 ATOM 1701 O O . LEU A 1 220 ? 82.816 161.649 15.720 1.00 32.94 ? 224 LEU A O 1 ATOM 1702 C CB . LEU A 1 220 ? 83.940 160.331 18.746 1.00 28.16 ? 224 LEU A CB 1 ATOM 1703 C CG . LEU A 1 220 ? 83.940 158.867 18.403 1.00 31.39 ? 224 LEU A CG 1 ATOM 1704 C CD1 . LEU A 1 220 ? 84.699 158.623 17.141 1.00 30.38 ? 224 LEU A CD1 1 ATOM 1705 C CD2 . LEU A 1 220 ? 84.563 158.072 19.515 1.00 33.26 ? 224 LEU A CD2 1 ATOM 1706 N N . ILE A 1 221 ? 84.266 162.889 16.937 1.00 32.46 ? 225 ILE A N 1 ATOM 1707 C CA . ILE A 1 221 ? 84.793 163.716 15.855 1.00 32.30 ? 225 ILE A CA 1 ATOM 1708 C C . ILE A 1 221 ? 86.321 163.765 15.873 1.00 37.75 ? 225 ILE A C 1 ATOM 1709 O O . ILE A 1 221 ? 86.917 164.568 15.154 1.00 38.32 ? 225 ILE A O 1 ATOM 1710 C CB . ILE A 1 221 ? 84.153 165.129 15.873 1.00 37.22 ? 225 ILE A CB 1 ATOM 1711 C CG1 . ILE A 1 221 ? 84.410 165.864 17.202 1.00 39.06 ? 225 ILE A CG1 1 ATOM 1712 C CG2 . ILE A 1 221 ? 82.659 165.063 15.550 1.00 40.48 ? 225 ILE A CG2 1 ATOM 1713 C CD1 . ILE A 1 221 ? 84.922 167.236 17.032 1.00 46.03 ? 225 ILE A CD1 1 ATOM 1714 N N . LYS A 1 222 ? 86.950 162.900 16.694 1.00 34.19 ? 226 LYS A N 1 ATOM 1715 C CA . LYS A 1 222 ? 88.403 162.799 16.828 1.00 33.91 ? 226 LYS A CA 1 ATOM 1716 C C . LYS A 1 222 ? 88.798 161.387 17.285 1.00 39.26 ? 226 LYS A C 1 ATOM 1717 O O . LYS A 1 222 ? 88.051 160.754 18.039 1.00 39.37 ? 226 LYS A O 1 ATOM 1718 C CB . LYS A 1 222 ? 88.930 163.870 17.808 1.00 36.77 ? 226 LYS A CB 1 ATOM 1719 C CG . LYS A 1 222 ? 90.453 163.969 17.913 1.00 30.96 ? 226 LYS A CG 1 ATOM 1720 C CD . LYS A 1 222 ? 90.865 164.934 19.002 1.00 31.08 ? 226 LYS A CD 1 ATOM 1721 C CE . LYS A 1 222 ? 92.292 164.726 19.428 1.00 40.10 ? 226 LYS A CE 1 ATOM 1722 N NZ . LYS A 1 222 ? 92.407 164.596 20.907 1.00 51.66 ? 226 LYS A NZ 1 ATOM 1723 N N . TYR A 1 223 ? 89.969 160.896 16.824 1.00 36.31 ? 227 TYR A N 1 ATOM 1724 C CA . TYR A 1 223 ? 90.500 159.600 17.243 1.00 36.84 ? 227 TYR A CA 1 ATOM 1725 C C . TYR A 1 223 ? 92.017 159.564 17.355 1.00 43.67 ? 227 TYR A C 1 ATOM 1726 O O . TYR A 1 223 ? 92.704 160.147 16.522 1.00 43.87 ? 227 TYR A O 1 ATOM 1727 C CB . TYR A 1 223 ? 89.958 158.441 16.418 1.00 36.39 ? 227 TYR A CB 1 ATOM 1728 C CG . TYR A 1 223 ? 89.975 157.139 17.185 1.00 38.91 ? 227 TYR A CG 1 ATOM 1729 C CD1 . TYR A 1 223 ? 89.194 156.968 18.326 1.00 41.98 ? 227 TYR A CD1 1 ATOM 1730 C CD2 . TYR A 1 223 ? 90.771 156.074 16.774 1.00 39.57 ? 227 TYR A CD2 1 ATOM 1731 C CE1 . TYR A 1 223 ? 89.200 155.767 19.035 1.00 44.00 ? 227 TYR A CE1 1 ATOM 1732 C CE2 . TYR A 1 223 ? 90.768 154.860 17.461 1.00 41.44 ? 227 TYR A CE2 1 ATOM 1733 C CZ . TYR A 1 223 ? 89.979 154.710 18.591 1.00 51.33 ? 227 TYR A CZ 1 ATOM 1734 O OH . TYR A 1 223 ? 89.976 153.521 19.282 1.00 54.95 ? 227 TYR A OH 1 ATOM 1735 N N . ASP A 1 224 ? 92.530 158.908 18.412 1.00 42.05 ? 228 ASP A N 1 ATOM 1736 C CA . ASP A 1 224 ? 93.958 158.805 18.717 1.00 43.36 ? 228 ASP A CA 1 ATOM 1737 C C . ASP A 1 224 ? 94.466 157.431 18.359 1.00 44.61 ? 228 ASP A C 1 ATOM 1738 O O . ASP A 1 224 ? 93.858 156.436 18.754 1.00 44.13 ? 228 ASP A O 1 ATOM 1739 C CB . ASP A 1 224 ? 94.193 159.058 20.218 1.00 48.84 ? 228 ASP A CB 1 ATOM 1740 C CG . ASP A 1 224 ? 93.628 160.357 20.783 1.00 70.79 ? 228 ASP A CG 1 ATOM 1741 O OD1 . ASP A 1 224 ? 93.164 161.205 19.988 1.00 72.07 ? 228 ASP A OD1 1 ATOM 1742 O OD2 . ASP A 1 224 ? 93.679 160.538 22.017 1.00 82.48 ? 228 ASP A OD2 1 ATOM 1743 N N . LEU A 1 225 ? 95.584 157.367 17.628 1.00 40.17 ? 229 LEU A N 1 ATOM 1744 C CA . LEU A 1 225 ? 96.169 156.091 17.216 1.00 39.64 ? 229 LEU A CA 1 ATOM 1745 C C . LEU A 1 225 ? 97.534 155.820 17.828 1.00 44.06 ? 229 LEU A C 1 ATOM 1746 O O . LEU A 1 225 ? 98.537 156.391 17.401 1.00 42.68 ? 229 LEU A O 1 ATOM 1747 C CB . LEU A 1 225 ? 96.192 155.931 15.686 1.00 38.20 ? 229 LEU A CB 1 ATOM 1748 C CG . LEU A 1 225 ? 94.883 155.471 15.048 1.00 41.34 ? 229 LEU A CG 1 ATOM 1749 C CD1 . LEU A 1 225 ? 94.822 155.873 13.602 1.00 40.73 ? 229 LEU A CD1 1 ATOM 1750 C CD2 . LEU A 1 225 ? 94.693 153.968 15.177 1.00 43.47 ? 229 LEU A CD2 1 ATOM 1751 N N . GLN A 1 226 ? 97.562 154.940 18.838 1.00 42.55 ? 230 GLN A N 1 ATOM 1752 C CA . GLN A 1 226 ? 98.789 154.564 19.526 1.00 45.22 ? 230 GLN A CA 1 ATOM 1753 C C . GLN A 1 226 ? 99.383 153.270 18.999 1.00 51.26 ? 230 GLN A C 1 ATOM 1754 O O . GLN A 1 226 ? 98.753 152.581 18.190 1.00 48.69 ? 230 GLN A O 1 ATOM 1755 C CB . GLN A 1 226 ? 98.579 154.520 21.041 1.00 48.24 ? 230 GLN A CB 1 ATOM 1756 C CG . GLN A 1 226 ? 98.992 155.814 21.737 1.00 64.89 ? 230 GLN A CG 1 ATOM 1757 C CD . GLN A 1 226 ? 98.145 157.021 21.385 1.00 78.69 ? 230 GLN A CD 1 ATOM 1758 O OE1 . GLN A 1 226 ? 98.671 158.092 21.070 1.00 71.11 ? 230 GLN A OE1 1 ATOM 1759 N NE2 . GLN A 1 226 ? 96.821 156.891 21.475 1.00 69.34 ? 230 GLN A NE2 1 ATOM 1760 N N . ASN A 1 227 ? 100.613 152.956 19.465 1.00 52.31 ? 231 ASN A N 1 ATOM 1761 C CA . ASN A 1 227 ? 101.427 151.793 19.090 1.00 54.09 ? 231 ASN A CA 1 ATOM 1762 C C . ASN A 1 227 ? 101.589 151.707 17.571 1.00 55.33 ? 231 ASN A C 1 ATOM 1763 O O . ASN A 1 227 ? 101.044 150.808 16.927 1.00 53.56 ? 231 ASN A O 1 ATOM 1764 C CB . ASN A 1 227 ? 100.922 150.485 19.738 1.00 56.08 ? 231 ASN A CB 1 ATOM 1765 C CG . ASN A 1 227 ? 101.782 149.281 19.429 1.00 82.70 ? 231 ASN A CG 1 ATOM 1766 O OD1 . ASN A 1 227 ? 102.861 149.087 20.000 1.00 82.02 ? 231 ASN A OD1 1 ATOM 1767 N ND2 . ASN A 1 227 ? 101.337 148.468 18.484 1.00 72.11 ? 231 ASN A ND2 1 ATOM 1768 N N . LEU A 1 228 ? 102.284 152.701 17.002 1.00 51.72 ? 232 LEU A N 1 ATOM 1769 C CA . LEU A 1 228 ? 102.532 152.766 15.559 1.00 50.77 ? 232 LEU A CA 1 ATOM 1770 C C . LEU A 1 228 ? 104.028 152.732 15.265 1.00 59.09 ? 232 LEU A C 1 ATOM 1771 O O . LEU A 1 228 ? 104.831 153.108 16.129 1.00 61.40 ? 232 LEU A O 1 ATOM 1772 C CB . LEU A 1 228 ? 101.852 153.989 14.900 1.00 47.67 ? 232 LEU A CB 1 ATOM 1773 C CG . LEU A 1 228 ? 100.313 154.048 14.953 1.00 48.50 ? 232 LEU A CG 1 ATOM 1774 C CD1 . LEU A 1 228 ? 99.800 155.371 14.436 1.00 46.43 ? 232 LEU A CD1 1 ATOM 1775 C CD2 . LEU A 1 228 ? 99.682 152.925 14.160 1.00 48.97 ? 232 LEU A CD2 1 ATOM 1776 N N . LYS A 1 229 ? 104.401 152.234 14.066 1.00 55.85 ? 233 LYS A N 1 ATOM 1777 C CA . LYS A 1 229 ? 105.797 152.138 13.642 1.00 58.37 ? 233 LYS A CA 1 ATOM 1778 C C . LYS A 1 229 ? 106.352 153.556 13.411 1.00 61.57 ? 233 LYS A C 1 ATOM 1779 O O . LYS A 1 229 ? 105.694 154.348 12.723 1.00 58.88 ? 233 LYS A O 1 ATOM 1780 C CB . LYS A 1 229 ? 105.939 151.267 12.382 1.00 61.13 ? 233 LYS A CB 1 ATOM 1781 C CG . LYS A 1 229 ? 107.316 150.626 12.249 1.00 80.61 ? 233 LYS A CG 1 ATOM 1782 C CD . LYS A 1 229 ? 107.548 150.041 10.864 1.00 92.28 ? 233 LYS A CD 1 ATOM 1783 C CE . LYS A 1 229 ? 108.727 149.097 10.818 1.00 110.05 ? 233 LYS A CE 1 ATOM 1784 N NZ . LYS A 1 229 ? 108.385 147.746 11.339 1.00 121.58 ? 233 LYS A NZ 1 ATOM 1785 N N . PRO A 1 230 ? 107.511 153.918 14.027 1.00 59.50 ? 234 PRO A N 1 ATOM 1786 C CA . PRO A 1 230 ? 108.045 155.282 13.849 1.00 59.25 ? 234 PRO A CA 1 ATOM 1787 C C . PRO A 1 230 ? 108.495 155.572 12.422 1.00 64.42 ? 234 PRO A C 1 ATOM 1788 O O . PRO A 1 230 ? 108.933 154.648 11.734 1.00 66.00 ? 234 PRO A O 1 ATOM 1789 C CB . PRO A 1 230 ? 109.200 155.338 14.841 1.00 64.25 ? 234 PRO A CB 1 ATOM 1790 C CG . PRO A 1 230 ? 109.629 153.931 14.989 1.00 70.89 ? 234 PRO A CG 1 ATOM 1791 C CD . PRO A 1 230 ? 108.386 153.113 14.900 1.00 63.91 ? 234 PRO A CD 1 ATOM 1792 N N . TYR A 1 231 ? 108.367 156.846 11.975 1.00 59.77 ? 235 TYR A N 1 ATOM 1793 C CA . TYR A 1 231 ? 108.729 157.300 10.624 1.00 59.85 ? 235 TYR A CA 1 ATOM 1794 C C . TYR A 1 231 ? 108.244 156.308 9.547 1.00 59.46 ? 235 TYR A C 1 ATOM 1795 O O . TYR A 1 231 ? 109.032 155.647 8.867 1.00 60.05 ? 235 TYR A O 1 ATOM 1796 C CB . TYR A 1 231 ? 110.230 157.659 10.535 1.00 66.27 ? 235 TYR A CB 1 ATOM 1797 C CG . TYR A 1 231 ? 110.713 158.167 9.190 1.00 71.04 ? 235 TYR A CG 1 ATOM 1798 C CD1 . TYR A 1 231 ? 109.974 159.104 8.466 1.00 70.71 ? 235 TYR A CD1 1 ATOM 1799 C CD2 . TYR A 1 231 ? 111.940 157.763 8.670 1.00 76.19 ? 235 TYR A CD2 1 ATOM 1800 C CE1 . TYR A 1 231 ? 110.416 159.577 7.230 1.00 72.96 ? 235 TYR A CE1 1 ATOM 1801 C CE2 . TYR A 1 231 ? 112.400 158.239 7.443 1.00 78.47 ? 235 TYR A CE2 1 ATOM 1802 C CZ . TYR A 1 231 ? 111.634 159.146 6.726 1.00 85.72 ? 235 TYR A CZ 1 ATOM 1803 O OH . TYR A 1 231 ? 112.095 159.617 5.520 1.00 90.86 ? 235 TYR A OH 1 ATOM 1804 N N . THR A 1 232 ? 106.914 156.161 9.484 1.00 51.95 ? 236 THR A N 1 ATOM 1805 C CA . THR A 1 232 ? 106.199 155.257 8.590 1.00 49.76 ? 236 THR A CA 1 ATOM 1806 C C . THR A 1 232 ? 104.978 155.979 8.017 1.00 46.72 ? 236 THR A C 1 ATOM 1807 O O . THR A 1 232 ? 104.263 156.645 8.761 1.00 43.66 ? 236 THR A O 1 ATOM 1808 C CB . THR A 1 232 ? 105.857 153.960 9.352 1.00 62.94 ? 236 THR A CB 1 ATOM 1809 O OG1 . THR A 1 232 ? 107.072 153.343 9.792 1.00 65.54 ? 236 THR A OG1 1 ATOM 1810 C CG2 . THR A 1 232 ? 105.052 152.968 8.518 1.00 64.02 ? 236 THR A CG2 1 ATOM 1811 N N . LYS A 1 233 ? 104.755 155.859 6.696 1.00 41.70 ? 237 LYS A N 1 ATOM 1812 C CA . LYS A 1 233 ? 103.627 156.501 6.021 1.00 38.36 ? 237 LYS A CA 1 ATOM 1813 C C . LYS A 1 233 ? 102.339 155.698 6.196 1.00 38.60 ? 237 LYS A C 1 ATOM 1814 O O . LYS A 1 233 ? 102.253 154.541 5.764 1.00 38.66 ? 237 LYS A O 1 ATOM 1815 C CB . LYS A 1 233 ? 103.939 156.785 4.540 1.00 40.90 ? 237 LYS A CB 1 ATOM 1816 C CG . LYS A 1 233 ? 103.419 158.139 4.067 1.00 44.07 ? 237 LYS A CG 1 ATOM 1817 C CD . LYS A 1 233 ? 104.011 158.558 2.723 1.00 47.67 ? 237 LYS A CD 1 ATOM 1818 C CE . LYS A 1 233 ? 103.611 159.966 2.341 1.00 42.85 ? 237 LYS A CE 1 ATOM 1819 N NZ . LYS A 1 233 ? 104.324 160.437 1.127 1.00 44.11 ? 237 LYS A NZ 1 ATOM 1820 N N . TYR A 1 234 ? 101.358 156.315 6.874 1.00 31.68 ? 238 TYR A N 1 ATOM 1821 C CA . TYR A 1 234 ? 100.058 155.719 7.160 1.00 29.21 ? 238 TYR A CA 1 ATOM 1822 C C . TYR A 1 234 ? 98.968 156.344 6.337 1.00 30.35 ? 238 TYR A C 1 ATOM 1823 O O . TYR A 1 234 ? 99.037 157.530 5.993 1.00 30.19 ? 238 TYR A O 1 ATOM 1824 C CB . TYR A 1 234 ? 99.715 155.820 8.657 1.00 30.41 ? 238 TYR A CB 1 ATOM 1825 C CG . TYR A 1 234 ? 100.342 154.725 9.497 1.00 34.66 ? 238 TYR A CG 1 ATOM 1826 C CD1 . TYR A 1 234 ? 101.631 154.862 10.008 1.00 38.72 ? 238 TYR A CD1 1 ATOM 1827 C CD2 . TYR A 1 234 ? 99.656 153.541 9.760 1.00 35.21 ? 238 TYR A CD2 1 ATOM 1828 C CE1 . TYR A 1 234 ? 102.226 153.845 10.753 1.00 41.63 ? 238 TYR A CE1 1 ATOM 1829 C CE2 . TYR A 1 234 ? 100.240 152.517 10.503 1.00 38.06 ? 238 TYR A CE2 1 ATOM 1830 C CZ . TYR A 1 234 ? 101.523 152.677 11.006 1.00 49.06 ? 238 TYR A CZ 1 ATOM 1831 O OH . TYR A 1 234 ? 102.096 151.680 11.765 1.00 53.23 ? 238 TYR A OH 1 ATOM 1832 N N . VAL A 1 235 ? 97.964 155.531 5.998 1.00 25.08 ? 239 VAL A N 1 ATOM 1833 C CA . VAL A 1 235 ? 96.791 155.958 5.233 1.00 22.87 ? 239 VAL A CA 1 ATOM 1834 C C . VAL A 1 235 ? 95.537 155.608 6.046 1.00 25.69 ? 239 VAL A C 1 ATOM 1835 O O . VAL A 1 235 ? 95.340 154.440 6.389 1.00 24.62 ? 239 VAL A O 1 ATOM 1836 C CB . VAL A 1 235 ? 96.745 155.390 3.785 1.00 25.93 ? 239 VAL A CB 1 ATOM 1837 C CG1 . VAL A 1 235 ? 95.495 155.861 3.052 1.00 24.45 ? 239 VAL A CG1 1 ATOM 1838 C CG2 . VAL A 1 235 ? 97.992 155.767 2.997 1.00 26.95 ? 239 VAL A CG2 1 ATOM 1839 N N . LEU A 1 236 ? 94.724 156.621 6.389 1.00 22.30 ? 240 LEU A N 1 ATOM 1840 C CA . LEU A 1 236 ? 93.497 156.384 7.131 1.00 22.47 ? 240 LEU A CA 1 ATOM 1841 C C . LEU A 1 236 ? 92.294 156.419 6.215 1.00 29.06 ? 240 LEU A C 1 ATOM 1842 O O . LEU A 1 236 ? 92.155 157.334 5.403 1.00 29.71 ? 240 LEU A O 1 ATOM 1843 C CB . LEU A 1 236 ? 93.260 157.384 8.282 1.00 22.50 ? 240 LEU A CB 1 ATOM 1844 C CG . LEU A 1 236 ? 94.239 157.546 9.451 1.00 28.09 ? 240 LEU A CG 1 ATOM 1845 C CD1 . LEU A 1 236 ? 94.870 156.240 9.884 1.00 29.18 ? 240 LEU A CD1 1 ATOM 1846 C CD2 . LEU A 1 236 ? 95.247 158.594 9.153 1.00 31.51 ? 240 LEU A CD2 1 ATOM 1847 N N . SER A 1 237 ? 91.413 155.437 6.365 1.00 26.48 ? 241 SER A N 1 ATOM 1848 C CA . SER A 1 237 ? 90.157 155.394 5.645 1.00 26.79 ? 241 SER A CA 1 ATOM 1849 C C . SER A 1 237 ? 89.069 155.630 6.693 1.00 31.97 ? 241 SER A C 1 ATOM 1850 O O . SER A 1 237 ? 89.141 155.074 7.792 1.00 32.67 ? 241 SER A O 1 ATOM 1851 C CB . SER A 1 237 ? 89.968 154.040 4.974 1.00 31.97 ? 241 SER A CB 1 ATOM 1852 O OG . SER A 1 237 ? 88.731 153.439 5.336 1.00 45.45 ? 241 SER A OG 1 ATOM 1853 N N . LEU A 1 238 ? 88.076 156.457 6.369 1.00 28.05 ? 242 LEU A N 1 ATOM 1854 C CA . LEU A 1 238 ? 86.971 156.714 7.291 1.00 27.31 ? 242 LEU A CA 1 ATOM 1855 C C . LEU A 1 238 ? 85.671 156.900 6.521 1.00 32.07 ? 242 LEU A C 1 ATOM 1856 O O . LEU A 1 238 ? 85.578 157.766 5.643 1.00 32.24 ? 242 LEU A O 1 ATOM 1857 C CB . LEU A 1 238 ? 87.259 157.904 8.237 1.00 26.90 ? 242 LEU A CB 1 ATOM 1858 C CG . LEU A 1 238 ? 86.090 158.403 9.102 1.00 30.25 ? 242 LEU A CG 1 ATOM 1859 C CD1 . LEU A 1 238 ? 85.802 157.449 10.241 1.00 30.85 ? 242 LEU A CD1 1 ATOM 1860 C CD2 . LEU A 1 238 ? 86.347 159.793 9.616 1.00 29.51 ? 242 LEU A CD2 1 ATOM 1861 N N . HIS A 1 239 ? 84.677 156.066 6.853 1.00 28.00 ? 243 HIS A N 1 ATOM 1862 C CA . HIS A 1 239 ? 83.349 156.093 6.254 1.00 28.11 ? 243 HIS A CA 1 ATOM 1863 C C . HIS A 1 239 ? 82.315 155.798 7.321 1.00 31.17 ? 243 HIS A C 1 ATOM 1864 O O . HIS A 1 239 ? 82.635 155.165 8.331 1.00 30.38 ? 243 HIS A O 1 ATOM 1865 C CB . HIS A 1 239 ? 83.240 155.097 5.080 1.00 29.32 ? 243 HIS A CB 1 ATOM 1866 C CG . HIS A 1 239 ? 83.213 153.657 5.485 1.00 32.63 ? 243 HIS A CG 1 ATOM 1867 N ND1 . HIS A 1 239 ? 82.035 153.039 5.882 1.00 34.87 ? 243 HIS A ND1 1 ATOM 1868 C CD2 . HIS A 1 239 ? 84.218 152.754 5.531 1.00 34.31 ? 243 HIS A CD2 1 ATOM 1869 C CE1 . HIS A 1 239 ? 82.363 151.791 6.172 1.00 34.31 ? 243 HIS A CE1 1 ATOM 1870 N NE2 . HIS A 1 239 ? 83.665 151.570 5.972 1.00 34.47 ? 243 HIS A NE2 1 ATOM 1871 N N . ALA A 1 240 ? 81.075 156.243 7.088 1.00 27.67 ? 244 ALA A N 1 ATOM 1872 C CA . ALA A 1 240 ? 79.958 156.015 7.997 1.00 27.22 ? 244 ALA A CA 1 ATOM 1873 C C . ALA A 1 240 ? 79.023 154.981 7.383 1.00 29.63 ? 244 ALA A C 1 ATOM 1874 O O . ALA A 1 240 ? 78.812 155.013 6.168 1.00 30.79 ? 244 ALA A O 1 ATOM 1875 C CB . ALA A 1 240 ? 79.210 157.314 8.234 1.00 28.94 ? 244 ALA A CB 1 ATOM 1876 N N . TYR A 1 241 ? 78.479 154.059 8.200 1.00 23.45 ? 245 TYR A N 1 ATOM 1877 C CA . TYR A 1 241 ? 77.548 153.048 7.710 1.00 23.19 ? 245 TYR A CA 1 ATOM 1878 C C . TYR A 1 241 ? 76.196 153.132 8.404 1.00 28.57 ? 245 TYR A C 1 ATOM 1879 O O . TYR A 1 241 ? 76.122 153.572 9.555 1.00 28.87 ? 245 TYR A O 1 ATOM 1880 C CB . TYR A 1 241 ? 78.132 151.633 7.809 1.00 23.67 ? 245 TYR A CB 1 ATOM 1881 C CG . TYR A 1 241 ? 78.260 151.099 9.217 1.00 26.47 ? 245 TYR A CG 1 ATOM 1882 C CD1 . TYR A 1 241 ? 77.209 150.409 9.819 1.00 29.88 ? 245 TYR A CD1 1 ATOM 1883 C CD2 . TYR A 1 241 ? 79.439 151.260 9.945 1.00 26.29 ? 245 TYR A CD2 1 ATOM 1884 C CE1 . TYR A 1 241 ? 77.310 149.939 11.129 1.00 30.90 ? 245 TYR A CE1 1 ATOM 1885 C CE2 . TYR A 1 241 ? 79.566 150.752 11.239 1.00 26.77 ? 245 TYR A CE2 1 ATOM 1886 C CZ . TYR A 1 241 ? 78.494 150.098 11.827 1.00 34.82 ? 245 TYR A CZ 1 ATOM 1887 O OH . TYR A 1 241 ? 78.578 149.613 13.105 1.00 38.24 ? 245 TYR A OH 1 ATOM 1888 N N . ILE A 1 242 ? 75.129 152.686 7.705 1.00 25.74 ? 246 ILE A N 1 ATOM 1889 C CA . ILE A 1 242 ? 73.756 152.619 8.212 1.00 26.42 ? 246 ILE A CA 1 ATOM 1890 C C . ILE A 1 242 ? 73.227 151.210 8.035 1.00 31.36 ? 246 ILE A C 1 ATOM 1891 O O . ILE A 1 242 ? 73.415 150.614 6.972 1.00 30.19 ? 246 ILE A O 1 ATOM 1892 C CB . ILE A 1 242 ? 72.805 153.694 7.607 1.00 30.63 ? 246 ILE A CB 1 ATOM 1893 C CG1 . ILE A 1 242 ? 71.459 153.772 8.392 1.00 32.12 ? 246 ILE A CG1 1 ATOM 1894 C CG2 . ILE A 1 242 ? 72.605 153.520 6.082 1.00 31.95 ? 246 ILE A CG2 1 ATOM 1895 C CD1 . ILE A 1 242 ? 70.553 154.973 8.116 1.00 32.78 ? 246 ILE A CD1 1 ATOM 1896 N N . ILE A 1 243 ? 72.575 150.668 9.071 1.00 30.22 ? 247 ILE A N 1 ATOM 1897 C CA . ILE A 1 243 ? 71.992 149.336 8.943 1.00 31.16 ? 247 ILE A CA 1 ATOM 1898 C C . ILE A 1 243 ? 70.511 149.405 8.546 1.00 37.12 ? 247 ILE A C 1 ATOM 1899 O O . ILE A 1 243 ? 69.612 149.458 9.395 1.00 37.39 ? 247 ILE A O 1 ATOM 1900 C CB . ILE A 1 243 ? 72.358 148.309 10.042 1.00 33.70 ? 247 ILE A CB 1 ATOM 1901 C CG1 . ILE A 1 243 ? 73.782 148.564 10.583 1.00 32.47 ? 247 ILE A CG1 1 ATOM 1902 C CG2 . ILE A 1 243 ? 72.241 146.891 9.469 1.00 34.41 ? 247 ILE A CG2 1 ATOM 1903 C CD1 . ILE A 1 243 ? 73.983 148.244 12.040 1.00 40.09 ? 247 ILE A CD1 1 ATOM 1904 N N . ALA A 1 244 ? 70.294 149.469 7.223 1.00 34.39 ? 248 ALA A N 1 ATOM 1905 C CA . ALA A 1 244 ? 68.991 149.531 6.582 1.00 37.23 ? 248 ALA A CA 1 ATOM 1906 C C . ALA A 1 244 ? 68.471 148.083 6.375 1.00 43.71 ? 248 ALA A C 1 ATOM 1907 O O . ALA A 1 244 ? 68.759 147.229 7.218 1.00 43.46 ? 248 ALA A O 1 ATOM 1908 C CB . ALA A 1 244 ? 69.128 150.267 5.260 1.00 38.37 ? 248 ALA A CB 1 ATOM 1909 N N . LYS A 1 245 ? 67.730 147.790 5.272 1.00 42.00 ? 249 LYS A N 1 ATOM 1910 C CA . LYS A 1 245 ? 67.250 146.430 4.965 1.00 43.00 ? 249 LYS A CA 1 ATOM 1911 C C . LYS A 1 245 ? 68.470 145.535 4.650 1.00 46.81 ? 249 LYS A C 1 ATOM 1912 O O . LYS A 1 245 ? 68.337 144.320 4.472 1.00 48.41 ? 249 LYS A O 1 ATOM 1913 C CB . LYS A 1 245 ? 66.271 146.441 3.772 1.00 47.32 ? 249 LYS A CB 1 ATOM 1914 C CG . LYS A 1 245 ? 64.881 146.994 4.084 1.00 51.84 ? 249 LYS A CG 1 ATOM 1915 C CD . LYS A 1 245 ? 64.111 147.294 2.805 1.00 57.06 ? 249 LYS A CD 1 ATOM 1916 C CE . LYS A 1 245 ? 62.636 147.502 3.029 1.00 67.31 ? 249 LYS A CE 1 ATOM 1917 N NZ . LYS A 1 245 ? 61.862 147.366 1.760 1.00 75.84 ? 249 LYS A NZ 1 ATOM 1918 N N . VAL A 1 246 ? 69.657 146.173 4.591 1.00 40.61 ? 250 VAL A N 1 ATOM 1919 C CA . VAL A 1 246 ? 70.999 145.646 4.334 1.00 38.39 ? 250 VAL A CA 1 ATOM 1920 C C . VAL A 1 246 ? 71.978 146.713 4.902 1.00 38.31 ? 250 VAL A C 1 ATOM 1921 O O . VAL A 1 246 ? 71.562 147.862 5.073 1.00 38.63 ? 250 VAL A O 1 ATOM 1922 C CB . VAL A 1 246 ? 71.184 145.371 2.802 1.00 43.59 ? 250 VAL A CB 1 ATOM 1923 C CG1 . VAL A 1 246 ? 71.231 146.659 1.983 1.00 43.53 ? 250 VAL A CG1 1 ATOM 1924 C CG2 . VAL A 1 246 ? 72.404 144.503 2.517 1.00 42.69 ? 250 VAL A CG2 1 ATOM 1925 N N . GLN A 1 247 ? 73.234 146.358 5.222 1.00 31.69 ? 251 GLN A N 1 ATOM 1926 C CA . GLN A 1 247 ? 74.172 147.380 5.710 1.00 29.89 ? 251 GLN A CA 1 ATOM 1927 C C . GLN A 1 247 ? 74.632 148.228 4.527 1.00 33.39 ? 251 GLN A C 1 ATOM 1928 O O . GLN A 1 247 ? 75.181 147.687 3.566 1.00 33.68 ? 251 GLN A O 1 ATOM 1929 C CB . GLN A 1 247 ? 75.378 146.761 6.448 1.00 30.13 ? 251 GLN A CB 1 ATOM 1930 C CG . GLN A 1 247 ? 76.573 147.718 6.638 1.00 39.18 ? 251 GLN A CG 1 ATOM 1931 C CD . GLN A 1 247 ? 77.438 147.409 7.840 1.00 56.64 ? 251 GLN A CD 1 ATOM 1932 O OE1 . GLN A 1 247 ? 77.002 146.791 8.827 1.00 53.52 ? 251 GLN A OE1 1 ATOM 1933 N NE2 . GLN A 1 247 ? 78.669 147.907 7.818 1.00 43.76 ? 251 GLN A NE2 1 ATOM 1934 N N . ARG A 1 248 ? 74.384 149.545 4.587 1.00 29.42 ? 252 ARG A N 1 ATOM 1935 C CA . ARG A 1 248 ? 74.776 150.480 3.523 1.00 28.91 ? 252 ARG A CA 1 ATOM 1936 C C . ARG A 1 248 ? 75.940 151.357 3.988 1.00 32.90 ? 252 ARG A C 1 ATOM 1937 O O . ARG A 1 248 ? 75.828 152.074 4.981 1.00 31.84 ? 252 ARG A O 1 ATOM 1938 C CB . ARG A 1 248 ? 73.588 151.332 3.019 1.00 27.35 ? 252 ARG A CB 1 ATOM 1939 C CG . ARG A 1 248 ? 72.332 150.527 2.719 1.00 28.80 ? 252 ARG A CG 1 ATOM 1940 C CD . ARG A 1 248 ? 71.429 151.220 1.726 1.00 31.94 ? 252 ARG A CD 1 ATOM 1941 N NE . ARG A 1 248 ? 70.878 150.261 0.767 1.00 35.41 ? 252 ARG A NE 1 ATOM 1942 C CZ . ARG A 1 248 ? 69.704 149.649 0.889 1.00 46.56 ? 252 ARG A CZ 1 ATOM 1943 N NH1 . ARG A 1 248 ? 68.927 149.890 1.936 1.00 30.98 ? 252 ARG A NH1 1 ATOM 1944 N NH2 . ARG A 1 248 ? 69.302 148.787 -0.028 1.00 37.05 ? 252 ARG A NH2 1 ATOM 1945 N N . ASN A 1 249 ? 77.069 151.255 3.288 1.00 30.62 ? 253 ASN A N 1 ATOM 1946 C CA . ASN A 1 249 ? 78.282 152.014 3.582 1.00 29.54 ? 253 ASN A CA 1 ATOM 1947 C C . ASN A 1 249 ? 78.354 153.280 2.735 1.00 32.35 ? 253 ASN A C 1 ATOM 1948 O O . ASN A 1 249 ? 78.007 153.276 1.547 1.00 32.03 ? 253 ASN A O 1 ATOM 1949 C CB . ASN A 1 249 ? 79.532 151.161 3.304 1.00 33.51 ? 253 ASN A CB 1 ATOM 1950 C CG . ASN A 1 249 ? 79.779 150.039 4.268 1.00 66.35 ? 253 ASN A CG 1 ATOM 1951 O OD1 . ASN A 1 249 ? 79.645 150.208 5.479 1.00 61.65 ? 253 ASN A OD1 1 ATOM 1952 N ND2 . ASN A 1 249 ? 80.179 148.872 3.749 1.00 69.73 ? 253 ASN A ND2 1 ATOM 1953 N N . GLY A 1 250 ? 78.828 154.345 3.356 1.00 28.33 ? 254 GLY A N 1 ATOM 1954 C CA . GLY A 1 250 ? 79.058 155.605 2.674 1.00 29.12 ? 254 GLY A CA 1 ATOM 1955 C C . GLY A 1 250 ? 80.436 155.557 2.060 1.00 32.68 ? 254 GLY A C 1 ATOM 1956 O O . GLY A 1 250 ? 81.223 154.666 2.412 1.00 30.53 ? 254 GLY A O 1 ATOM 1957 N N . SER A 1 251 ? 80.741 156.491 1.125 1.00 30.98 ? 255 SER A N 1 ATOM 1958 C CA . SER A 1 251 ? 82.077 156.525 0.515 1.00 31.03 ? 255 SER A CA 1 ATOM 1959 C C . SER A 1 251 ? 83.139 156.879 1.575 1.00 33.30 ? 255 SER A C 1 ATOM 1960 O O . SER A 1 251 ? 82.816 157.518 2.580 1.00 31.48 ? 255 SER A O 1 ATOM 1961 C CB . SER A 1 251 ? 82.130 157.437 -0.712 1.00 36.57 ? 255 SER A CB 1 ATOM 1962 O OG . SER A 1 251 ? 82.162 158.827 -0.428 1.00 45.47 ? 255 SER A OG 1 ATOM 1963 N N . ALA A 1 252 ? 84.360 156.357 1.414 1.00 30.24 ? 256 ALA A N 1 ATOM 1964 C CA . ALA A 1 252 ? 85.405 156.579 2.405 1.00 29.72 ? 256 ALA A CA 1 ATOM 1965 C C . ALA A 1 252 ? 86.242 157.816 2.149 1.00 36.04 ? 256 ALA A C 1 ATOM 1966 O O . ALA A 1 252 ? 86.560 158.150 1.002 1.00 37.34 ? 256 ALA A O 1 ATOM 1967 C CB . ALA A 1 252 ? 86.286 155.351 2.537 1.00 30.16 ? 256 ALA A CB 1 ATOM 1968 N N . ALA A 1 253 ? 86.581 158.507 3.235 1.00 32.61 ? 257 ALA A N 1 ATOM 1969 C CA . ALA A 1 253 ? 87.395 159.708 3.205 1.00 32.75 ? 257 ALA A CA 1 ATOM 1970 C C . ALA A 1 253 ? 88.821 159.287 3.518 1.00 35.22 ? 257 ALA A C 1 ATOM 1971 O O . ALA A 1 253 ? 89.091 158.759 4.605 1.00 35.14 ? 257 ALA A O 1 ATOM 1972 C CB . ALA A 1 253 ? 86.882 160.697 4.240 1.00 33.72 ? 257 ALA A CB 1 ATOM 1973 N N . MET A 1 254 ? 89.714 159.455 2.543 1.00 30.62 ? 258 MET A N 1 ATOM 1974 C CA . MET A 1 254 ? 91.122 159.092 2.683 1.00 30.66 ? 258 MET A CA 1 ATOM 1975 C C . MET A 1 254 ? 91.907 160.179 3.406 1.00 34.33 ? 258 MET A C 1 ATOM 1976 O O . MET A 1 254 ? 91.522 161.351 3.403 1.00 33.36 ? 258 MET A O 1 ATOM 1977 C CB . MET A 1 254 ? 91.764 158.733 1.335 1.00 34.42 ? 258 MET A CB 1 ATOM 1978 C CG . MET A 1 254 ? 91.123 157.540 0.626 1.00 37.76 ? 258 MET A CG 1 ATOM 1979 S SD . MET A 1 254 ? 91.412 155.973 1.448 1.00 40.03 ? 258 MET A SD 1 ATOM 1980 C CE . MET A 1 254 ? 90.537 154.932 0.414 1.00 37.03 ? 258 MET A CE 1 ATOM 1981 N N . CYS A 1 255 ? 93.006 159.767 4.039 1.00 32.21 ? 259 CYS A N 1 ATOM 1982 C CA . CYS A 1 255 ? 93.827 160.583 4.921 1.00 32.63 ? 259 CYS A CA 1 ATOM 1983 C C . CYS A 1 255 ? 95.245 160.072 4.890 1.00 37.71 ? 259 CYS A C 1 ATOM 1984 O O . CYS A 1 255 ? 95.445 158.862 5.005 1.00 38.18 ? 259 CYS A O 1 ATOM 1985 C CB . CYS A 1 255 ? 93.260 160.435 6.330 1.00 32.53 ? 259 CYS A CB 1 ATOM 1986 S SG . CYS A 1 255 ? 93.312 161.930 7.332 1.00 37.12 ? 259 CYS A SG 1 ATOM 1987 N N . HIS A 1 256 ? 96.237 160.958 4.834 1.00 34.21 ? 260 HIS A N 1 ATOM 1988 C CA . HIS A 1 256 ? 97.611 160.473 4.951 1.00 34.41 ? 260 HIS A CA 1 ATOM 1989 C C . HIS A 1 256 ? 98.476 161.283 5.893 1.00 40.23 ? 260 HIS A C 1 ATOM 1990 O O . HIS A 1 256 ? 98.323 162.504 5.998 1.00 40.07 ? 260 HIS A O 1 ATOM 1991 C CB . HIS A 1 256 ? 98.294 160.120 3.617 1.00 35.16 ? 260 HIS A CB 1 ATOM 1992 C CG . HIS A 1 256 ? 98.641 161.279 2.743 1.00 38.37 ? 260 HIS A CG 1 ATOM 1993 N ND1 . HIS A 1 256 ? 98.145 161.377 1.464 1.00 39.93 ? 260 HIS A ND1 1 ATOM 1994 C CD2 . HIS A 1 256 ? 99.478 162.318 2.965 1.00 40.65 ? 260 HIS A CD2 1 ATOM 1995 C CE1 . HIS A 1 256 ? 98.664 162.484 0.960 1.00 40.29 ? 260 HIS A CE1 1 ATOM 1996 N NE2 . HIS A 1 256 ? 99.470 163.084 1.830 1.00 41.06 ? 260 HIS A NE2 1 ATOM 1997 N N . PHE A 1 257 ? 99.343 160.585 6.620 1.00 38.03 ? 261 PHE A N 1 ATOM 1998 C CA . PHE A 1 257 ? 100.280 161.189 7.557 1.00 39.52 ? 261 PHE A CA 1 ATOM 1999 C C . PHE A 1 257 ? 101.472 160.258 7.770 1.00 45.39 ? 261 PHE A C 1 ATOM 2000 O O . PHE A 1 257 ? 101.378 159.053 7.512 1.00 44.58 ? 261 PHE A O 1 ATOM 2001 C CB . PHE A 1 257 ? 99.598 161.557 8.889 1.00 40.61 ? 261 PHE A CB 1 ATOM 2002 C CG . PHE A 1 257 ? 99.525 160.428 9.882 1.00 42.53 ? 261 PHE A CG 1 ATOM 2003 C CD1 . PHE A 1 257 ? 98.508 159.489 9.816 1.00 44.49 ? 261 PHE A CD1 1 ATOM 2004 C CD2 . PHE A 1 257 ? 100.481 160.296 10.879 1.00 47.26 ? 261 PHE A CD2 1 ATOM 2005 C CE1 . PHE A 1 257 ? 98.441 158.443 10.735 1.00 46.09 ? 261 PHE A CE1 1 ATOM 2006 C CE2 . PHE A 1 257 ? 100.425 159.235 11.790 1.00 50.89 ? 261 PHE A CE2 1 ATOM 2007 C CZ . PHE A 1 257 ? 99.407 158.315 11.710 1.00 47.47 ? 261 PHE A CZ 1 ATOM 2008 N N . THR A 1 258 ? 102.592 160.823 8.244 1.00 43.82 ? 262 THR A N 1 ATOM 2009 C CA . THR A 1 258 ? 103.801 160.053 8.523 1.00 45.53 ? 262 THR A CA 1 ATOM 2010 C C . THR A 1 258 ? 104.369 160.338 9.916 1.00 48.94 ? 262 THR A C 1 ATOM 2011 O O . THR A 1 258 ? 104.580 161.497 10.283 1.00 48.50 ? 262 THR A O 1 ATOM 2012 C CB . THR A 1 258 ? 104.781 159.951 7.320 1.00 55.31 ? 262 THR A CB 1 ATOM 2013 O OG1 . THR A 1 258 ? 106.126 159.803 7.792 1.00 58.14 ? 262 THR A OG1 1 ATOM 2014 C CG2 . THR A 1 258 ? 104.663 161.118 6.323 1.00 52.20 ? 262 THR A CG2 1 ATOM 2015 N N . THR A 1 259 ? 104.566 159.253 10.691 1.00 45.08 ? 263 THR A N 1 ATOM 2016 C CA . THR A 1 259 ? 105.057 159.235 12.066 1.00 46.22 ? 263 THR A CA 1 ATOM 2017 C C . THR A 1 259 ? 106.406 159.948 12.284 1.00 53.84 ? 263 THR A C 1 ATOM 2018 O O . THR A 1 259 ? 107.149 160.176 11.321 1.00 54.79 ? 263 THR A O 1 ATOM 2019 C CB . THR A 1 259 ? 104.942 157.832 12.666 1.00 51.02 ? 263 THR A CB 1 ATOM 2020 O OG1 . THR A 1 259 ? 105.553 156.893 11.785 1.00 49.36 ? 263 THR A OG1 1 ATOM 2021 C CG2 . THR A 1 259 ? 103.499 157.427 12.926 1.00 46.68 ? 263 THR A CG2 1 ATOM 2022 N N . LYS A 1 260 ? 106.692 160.341 13.546 1.00 51.39 ? 264 LYS A N 1 ATOM 2023 C CA . LYS A 1 260 ? 107.896 161.089 13.929 1.00 67.04 ? 264 LYS A CA 1 ATOM 2024 C C . LYS A 1 260 ? 109.136 160.216 14.113 1.00 93.27 ? 264 LYS A C 1 ATOM 2025 O O . LYS A 1 260 ? 109.062 159.152 14.720 1.00 57.76 ? 264 LYS A O 1 ATOM 2026 C CB . LYS A 1 260 ? 107.635 161.956 15.173 1.00 69.51 ? 264 LYS A CB 1 ATOM 2027 C CG . LYS A 1 260 ? 106.484 162.942 15.004 1.00 74.51 ? 264 LYS A CG 1 ATOM 2028 C CD . LYS A 1 260 ? 106.588 164.111 15.968 1.00 84.54 ? 264 LYS A CD 1 ATOM 2029 C CE . LYS A 1 260 ? 105.403 165.043 15.877 1.00 94.48 ? 264 LYS A CE 1 ATOM 2030 N NZ . LYS A 1 260 ? 105.351 165.784 14.584 1.00 104.85 ? 264 LYS A NZ 1 HETATM 2031 C C1 . NAG B 2 . ? 78.062 150.993 16.858 1.00 35.70 ? 1265 NAG A C1 1 HETATM 2032 C C2 . NAG B 2 . ? 77.052 149.848 16.881 1.00 38.17 ? 1265 NAG A C2 1 HETATM 2033 C C3 . NAG B 2 . ? 76.945 149.350 18.324 1.00 36.14 ? 1265 NAG A C3 1 HETATM 2034 C C4 . NAG B 2 . ? 78.314 148.923 18.848 1.00 34.08 ? 1265 NAG A C4 1 HETATM 2035 C C5 . NAG B 2 . ? 79.336 150.054 18.697 1.00 33.79 ? 1265 NAG A C5 1 HETATM 2036 C C6 . NAG B 2 . ? 80.762 149.640 18.992 1.00 32.08 ? 1265 NAG A C6 1 HETATM 2037 C C7 . NAG B 2 . ? 74.960 149.639 15.580 1.00 47.80 ? 1265 NAG A C7 1 HETATM 2038 C C8 . NAG B 2 . ? 73.638 150.271 15.271 1.00 48.26 ? 1265 NAG A C8 1 HETATM 2039 N N2 . NAG B 2 . ? 75.765 150.333 16.410 1.00 42.94 ? 1265 NAG A N2 1 HETATM 2040 O O3 . NAG B 2 . ? 76.032 148.258 18.408 1.00 35.41 ? 1265 NAG A O3 1 HETATM 2041 O O4 . NAG B 2 . ? 78.175 148.571 20.219 1.00 31.86 ? 1265 NAG A O4 1 HETATM 2042 O O5 . NAG B 2 . ? 79.332 150.548 17.348 1.00 34.16 ? 1265 NAG A O5 1 HETATM 2043 O O6 . NAG B 2 . ? 81.370 148.957 17.902 1.00 30.79 ? 1265 NAG A O6 1 HETATM 2044 O O7 . NAG B 2 . ? 75.286 148.551 15.108 1.00 50.33 ? 1265 NAG A O7 1 HETATM 2045 C C1 . NAG C 2 . ? 39.878 151.127 -10.014 1.00 94.94 ? 1266 NAG A C1 1 HETATM 2046 C C2 . NAG C 2 . ? 40.145 151.765 -8.640 1.00 96.94 ? 1266 NAG A C2 1 HETATM 2047 C C3 . NAG C 2 . ? 39.088 152.837 -8.357 1.00 95.85 ? 1266 NAG A C3 1 HETATM 2048 C C4 . NAG C 2 . ? 39.009 153.851 -9.494 1.00 95.79 ? 1266 NAG A C4 1 HETATM 2049 C C5 . NAG C 2 . ? 38.739 153.141 -10.819 1.00 95.55 ? 1266 NAG A C5 1 HETATM 2050 C C6 . NAG C 2 . ? 38.810 154.063 -12.017 1.00 94.18 ? 1266 NAG A C6 1 HETATM 2051 C C7 . NAG C 2 . ? 40.793 150.872 -6.412 1.00 98.37 ? 1266 NAG A C7 1 HETATM 2052 C C8 . NAG C 2 . ? 40.647 149.715 -5.470 1.00 97.88 ? 1266 NAG A C8 1 HETATM 2053 N N2 . NAG C 2 . ? 40.128 150.763 -7.581 1.00 98.33 ? 1266 NAG A N2 1 HETATM 2054 O O3 . NAG C 2 . ? 39.376 153.513 -7.137 1.00 94.47 ? 1266 NAG A O3 1 HETATM 2055 O O4 . NAG C 2 . ? 37.958 154.775 -9.229 1.00 95.13 ? 1266 NAG A O4 1 HETATM 2056 O O5 . NAG C 2 . ? 39.727 152.120 -11.037 1.00 95.95 ? 1266 NAG A O5 1 HETATM 2057 O O6 . NAG C 2 . ? 40.149 154.437 -12.333 1.00 92.66 ? 1266 NAG A O6 1 HETATM 2058 O O7 . NAG C 2 . ? 41.479 151.853 -6.134 1.00 98.69 ? 1266 NAG A O7 1 HETATM 2059 C C1 . NAG D 2 . ? 22.398 136.214 -6.191 1.00 85.16 ? 1267 NAG A C1 1 HETATM 2060 C C2 . NAG D 2 . ? 22.731 135.770 -4.767 1.00 84.33 ? 1267 NAG A C2 1 HETATM 2061 C C3 . NAG D 2 . ? 21.677 136.396 -3.848 1.00 85.31 ? 1267 NAG A C3 1 HETATM 2062 C C4 . NAG D 2 . ? 21.590 137.907 -4.063 1.00 87.32 ? 1267 NAG A C4 1 HETATM 2063 C C5 . NAG D 2 . ? 21.305 138.230 -5.529 1.00 87.17 ? 1267 NAG A C5 1 HETATM 2064 C C6 . NAG D 2 . ? 21.320 139.709 -5.841 1.00 87.77 ? 1267 NAG A C6 1 HETATM 2065 C C7 . NAG D 2 . ? 23.735 133.517 -4.665 1.00 78.04 ? 1267 NAG A C7 1 HETATM 2066 C C8 . NAG D 2 . ? 23.453 132.046 -4.612 1.00 77.13 ? 1267 NAG A C8 1 HETATM 2067 N N2 . NAG D 2 . ? 22.659 134.318 -4.710 1.00 81.07 ? 1267 NAG A N2 1 HETATM 2068 O O3 . NAG D 2 . ? 21.986 136.119 -2.485 1.00 83.77 ? 1267 NAG A O3 1 HETATM 2069 O O4 . NAG D 2 . ? 20.553 138.445 -3.249 1.00 89.25 ? 1267 NAG A O4 1 HETATM 2070 O O5 . NAG D 2 . ? 22.315 137.630 -6.354 1.00 86.62 ? 1267 NAG A O5 1 HETATM 2071 O O6 . NAG D 2 . ? 21.086 139.943 -7.225 1.00 88.16 ? 1267 NAG A O6 1 HETATM 2072 O O7 . NAG D 2 . ? 24.881 133.957 -4.660 1.00 77.47 ? 1267 NAG A O7 1 HETATM 2073 C C1 . NAG E 2 . ? 33.668 131.459 -24.178 1.00 55.63 ? 1268 NAG A C1 1 HETATM 2074 C C2 . NAG E 2 . ? 34.964 130.697 -23.874 1.00 54.16 ? 1268 NAG A C2 1 HETATM 2075 C C3 . NAG E 2 . ? 36.048 130.936 -24.929 1.00 55.05 ? 1268 NAG A C3 1 HETATM 2076 C C4 . NAG E 2 . ? 35.476 130.813 -26.335 1.00 55.24 ? 1268 NAG A C4 1 HETATM 2077 C C5 . NAG E 2 . ? 34.313 131.788 -26.492 1.00 57.67 ? 1268 NAG A C5 1 HETATM 2078 C C6 . NAG E 2 . ? 33.682 131.764 -27.865 1.00 59.98 ? 1268 NAG A C6 1 HETATM 2079 C C7 . NAG E 2 . ? 36.092 130.398 -21.695 1.00 54.81 ? 1268 NAG A C7 1 HETATM 2080 C C8 . NAG E 2 . ? 36.324 131.013 -20.347 1.00 54.45 ? 1268 NAG A C8 1 HETATM 2081 N N2 . NAG E 2 . ? 35.424 131.159 -22.574 1.00 53.69 ? 1268 NAG A N2 1 HETATM 2082 O O3 . NAG E 2 . ? 37.104 130.000 -24.755 1.00 56.16 ? 1268 NAG A O3 1 HETATM 2083 O O4 . NAG E 2 . ? 36.490 131.072 -27.301 1.00 53.58 ? 1268 NAG A O4 1 HETATM 2084 O O5 . NAG E 2 . ? 33.279 131.442 -25.556 1.00 57.58 ? 1268 NAG A O5 1 HETATM 2085 O O6 . NAG E 2 . ? 32.516 132.576 -27.927 1.00 60.91 ? 1268 NAG A O6 1 HETATM 2086 O O7 . NAG E 2 . ? 36.481 129.265 -21.969 1.00 56.29 ? 1268 NAG A O7 1 HETATM 2087 C C1 . NAG F 2 . ? 80.480 147.734 4.563 1.00 72.51 ? 1269 NAG A C1 1 HETATM 2088 C C2 . NAG F 2 . ? 80.571 146.437 3.753 1.00 75.58 ? 1269 NAG A C2 1 HETATM 2089 C C3 . NAG F 2 . ? 81.370 145.295 4.397 1.00 76.08 ? 1269 NAG A C3 1 HETATM 2090 C C4 . NAG F 2 . ? 82.540 145.813 5.235 1.00 75.28 ? 1269 NAG A C4 1 HETATM 2091 C C5 . NAG F 2 . ? 82.071 146.957 6.127 1.00 75.05 ? 1269 NAG A C5 1 HETATM 2092 C C6 . NAG F 2 . ? 83.109 147.503 7.078 1.00 74.47 ? 1269 NAG A C6 1 HETATM 2093 C C7 . NAG F 2 . ? 78.544 145.920 2.437 1.00 78.53 ? 1269 NAG A C7 1 HETATM 2094 C C8 . NAG F 2 . ? 77.154 145.361 2.504 1.00 78.12 ? 1269 NAG A C8 1 HETATM 2095 N N2 . NAG F 2 . ? 79.178 146.043 3.610 1.00 77.17 ? 1269 NAG A N2 1 HETATM 2096 O O3 . NAG F 2 . ? 81.840 144.405 3.391 1.00 76.62 ? 1269 NAG A O3 1 HETATM 2097 O O4 . NAG F 2 . ? 83.038 144.752 6.045 1.00 75.06 ? 1269 NAG A O4 1 HETATM 2098 O O5 . NAG F 2 . ? 81.661 148.046 5.292 1.00 74.49 ? 1269 NAG A O5 1 HETATM 2099 O O6 . NAG F 2 . ? 82.547 148.569 7.836 1.00 73.48 ? 1269 NAG A O6 1 HETATM 2100 O O7 . NAG F 2 . ? 79.065 146.238 1.372 1.00 80.05 ? 1269 NAG A O7 1 # loop_ _atom_site_anisotrop.id _atom_site_anisotrop.type_symbol _atom_site_anisotrop.pdbx_label_atom_id _atom_site_anisotrop.pdbx_label_alt_id _atom_site_anisotrop.pdbx_label_comp_id _atom_site_anisotrop.pdbx_label_asym_id _atom_site_anisotrop.pdbx_label_seq_id _atom_site_anisotrop.pdbx_PDB_ins_code _atom_site_anisotrop.U[1][1] _atom_site_anisotrop.U[2][2] _atom_site_anisotrop.U[3][3] _atom_site_anisotrop.U[1][2] _atom_site_anisotrop.U[1][3] _atom_site_anisotrop.U[2][3] _atom_site_anisotrop.pdbx_auth_seq_id _atom_site_anisotrop.pdbx_auth_comp_id _atom_site_anisotrop.pdbx_auth_asym_id _atom_site_anisotrop.pdbx_auth_atom_id 1 N N . THR A 6 ? 1.1418 1.2362 1.4410 -0.2378 -0.4008 0.0387 10 THR A N 2 C CA . THR A 6 ? 1.1044 1.2446 1.4291 -0.2531 -0.3856 0.0363 10 THR A CA 3 C C . THR A 6 ? 1.1188 1.2832 1.4571 -0.2389 -0.3376 0.0176 10 THR A C 4 O O . THR A 6 ? 1.1246 1.2511 1.4274 -0.2257 -0.3192 0.0075 10 THR A O 5 C CB . THR A 6 ? 1.2272 1.3103 1.4753 -0.2804 -0.3980 0.0405 10 THR A CB 6 O OG1 . THR A 6 ? 1.2463 1.2747 1.4261 -0.2780 -0.3668 0.0272 10 THR A OG1 7 C CG2 . THR A 6 ? 1.2613 1.2899 1.4674 -0.2952 -0.4464 0.0585 10 THR A CG2 8 N N . CYS A 7 ? 1.0335 1.2572 1.4207 -0.2424 -0.3179 0.0130 11 CYS A N 9 C CA . CYS A 7 ? 0.9917 1.2328 1.3871 -0.2312 -0.2755 -0.0039 11 CYS A CA 10 C C . CYS A 7 ? 1.0382 1.2269 1.3602 -0.2401 -0.2579 -0.0143 11 CYS A C 11 O O . CYS A 7 ? 1.0222 1.1978 1.3294 -0.2289 -0.2313 -0.0259 11 CYS A O 12 C CB . CYS A 7 ? 0.9574 1.2641 1.4157 -0.2329 -0.2593 -0.0064 11 CYS A CB 13 S SG . CYS A 7 ? 0.9962 1.3693 1.5517 -0.2162 -0.2688 0.0070 11 CYS A SG 14 N N . ASP A 8 ? 1.0145 1.1670 1.2863 -0.2599 -0.2745 -0.0076 12 ASP A N 15 C CA . ASP A 8 ? 1.0287 1.1242 1.2263 -0.2671 -0.2588 -0.0129 12 ASP A CA 16 C C . ASP A 8 ? 1.1023 1.1406 1.2572 -0.2558 -0.2566 -0.0145 12 ASP A C 17 O O . ASP A 8 ? 1.1049 1.1149 1.2241 -0.2524 -0.2305 -0.0227 12 ASP A O 18 C CB . ASP A 8 ? 1.0920 1.1495 1.2366 -0.2898 -0.2795 -0.0018 12 ASP A CB 19 C CG . ASP A 8 ? 1.2691 1.2667 1.3357 -0.2955 -0.2590 -0.0047 12 ASP A CG 20 O OD1 . ASP A 8 ? 1.2547 1.2647 1.3258 -0.2853 -0.2258 -0.0168 12 ASP A OD1 21 O OD2 . ASP A 8 ? 1.3933 1.3301 1.3934 -0.3103 -0.2760 0.0067 12 ASP A OD2 22 N N . GLU A 9 ? 1.0651 1.0878 1.2259 -0.2498 -0.2838 -0.0063 13 GLU A N 23 C CA . GLU A 9 ? 1.0863 1.0507 1.2050 -0.2385 -0.2840 -0.0085 13 GLU A CA 24 C C . GLU A 9 ? 1.0654 1.0612 1.2209 -0.2187 -0.2569 -0.0211 13 GLU A C 25 O O . GLU A 9 ? 1.0595 1.0208 1.1785 -0.2144 -0.2331 -0.0302 13 GLU A O 26 C CB . GLU A 9 ? 1.1538 1.0900 1.2647 -0.2393 -0.3261 0.0052 13 GLU A CB 27 C CG . GLU A 9 ? 1.3657 1.2234 1.4161 -0.2309 -0.3328 0.0041 13 GLU A CG 28 C CD . GLU A 9 ? 1.7228 1.5440 1.7562 -0.2351 -0.3795 0.0190 13 GLU A CD 29 O OE1 . GLU A 9 ? 1.6749 1.4831 1.6911 -0.2552 -0.4071 0.0322 13 GLU A OE1 30 O OE2 . GLU A 9 ? 1.6739 1.4777 1.7089 -0.2188 -0.3900 0.0180 13 GLU A OE2 31 N N . LYS A 10 ? 0.9707 1.0291 1.1963 -0.2074 -0.2591 -0.0202 14 LYS A N 32 C CA . LYS A 10 ? 0.9353 1.0180 1.1905 -0.1889 -0.2342 -0.0299 14 LYS A CA 33 C C . LYS A 10 ? 0.9634 1.0577 1.2136 -0.1916 -0.1981 -0.0432 14 LYS A C 34 O O . LYS A 10 ? 0.9634 1.0417 1.1994 -0.1824 -0.1780 -0.0519 14 LYS A O 35 C CB . LYS A 10 ? 0.9318 1.0756 1.2611 -0.1759 -0.2407 -0.0232 14 LYS A CB 36 C CG . LYS A 10 ? 0.9894 1.1388 1.3334 -0.1540 -0.2190 -0.0297 14 LYS A CG 37 C CD . LYS A 10 ? 1.0352 1.2404 1.4502 -0.1381 -0.2195 -0.0211 14 LYS A CD 38 C CE . LYS A 10 ? 1.1181 1.3126 1.5303 -0.1157 -0.1975 -0.0261 14 LYS A CE 39 N NZ . LYS A 10 ? 1.1954 1.4395 1.6746 -0.0966 -0.1925 -0.0156 14 LYS A NZ 40 N N . TYR A 11 ? 0.8950 1.0144 1.1536 -0.2052 -0.1911 -0.0443 15 TYR A N 41 C CA . TYR A 11 ? 0.8596 0.9926 1.1165 -0.2082 -0.1607 -0.0556 15 TYR A CA 42 C C . TYR A 11 ? 0.9063 1.0056 1.1129 -0.2210 -0.1524 -0.0569 15 TYR A C 43 O O . TYR A 11 ? 0.8791 0.9982 1.0911 -0.2250 -0.1324 -0.0638 15 TYR A O 44 C CB . TYR A 11 ? 0.8359 1.0271 1.1465 -0.2086 -0.1512 -0.0586 15 TYR A CB 45 C CG . TYR A 11 ? 0.8530 1.0770 1.2153 -0.1934 -0.1524 -0.0556 15 TYR A CG 46 C CD1 . TYR A 11 ? 0.8792 1.0957 1.2428 -0.1789 -0.1348 -0.0612 15 TYR A CD1 47 C CD2 . TYR A 11 ? 0.8606 1.1221 1.2697 -0.1937 -0.1697 -0.0455 15 TYR A CD2 48 C CE1 . TYR A 11 ? 0.8895 1.1300 1.2949 -0.1622 -0.1321 -0.0566 15 TYR A CE1 49 C CE2 . TYR A 11 ? 0.8685 1.1618 1.3298 -0.1768 -0.1675 -0.0401 15 TYR A CE2 50 C CZ . TYR A 11 ? 0.9614 1.2418 1.4183 -0.1597 -0.1474 -0.0455 15 TYR A CZ 51 O OH . TYR A 11 ? 0.9739 1.2793 1.4761 -0.1404 -0.1417 -0.0385 15 TYR A OH 52 N N . ALA A 12 ? 0.8881 0.9325 1.0433 -0.2260 -0.1659 -0.0497 16 ALA A N 53 C CA . ALA A 12 ? 0.8993 0.9031 1.0013 -0.2355 -0.1547 -0.0479 16 ALA A CA 54 C C . ALA A 12 ? 0.9175 0.9199 1.0133 -0.2315 -0.1233 -0.0565 16 ALA A C 55 O O . ALA A 12 ? 0.9050 0.9070 0.9849 -0.2374 -0.1080 -0.0563 16 ALA A O 56 C CB . ALA A 12 ? 0.9708 0.9031 1.0127 -0.2392 -0.1721 -0.0382 16 ALA A CB 57 N N . ASN A 13 ? 0.8582 0.8611 0.9666 -0.2221 -0.1143 -0.0631 17 ASN A N 58 C CA . ASN A 13 ? 0.8363 0.8394 0.9418 -0.2213 -0.0878 -0.0697 17 ASN A CA 59 C C . ASN A 13 ? 0.8504 0.9034 1.0015 -0.2183 -0.0758 -0.0788 17 ASN A C 60 O O . ASN A 13 ? 0.8391 0.8900 0.9885 -0.2188 -0.0587 -0.0836 17 ASN A O 61 C CB . ASN A 13 ? 0.8498 0.7979 0.9155 -0.2179 -0.0812 -0.0696 17 ASN A CB 62 C CG . ASN A 13 ? 1.0969 0.9807 1.1095 -0.2194 -0.0942 -0.0612 17 ASN A CG 63 O OD1 . ASN A 13 ? 1.0145 0.8854 1.0228 -0.2169 -0.1192 -0.0575 17 ASN A OD1 64 N ND2 . ASN A 13 ? 1.0236 0.8594 0.9926 -0.2223 -0.0769 -0.0574 17 ASN A ND2 65 N N . ILE A 14 ? 0.7870 0.8810 0.9759 -0.2166 -0.0839 -0.0801 18 ILE A N 66 C CA . ILE A 14 ? 0.7563 0.8883 0.9817 -0.2138 -0.0720 -0.0876 18 ILE A CA 67 C C . ILE A 14 ? 0.7852 0.9257 1.0071 -0.2213 -0.0529 -0.0929 18 ILE A C 68 O O . ILE A 14 ? 0.7813 0.9199 0.9891 -0.2279 -0.0496 -0.0903 18 ILE A O 69 C CB . ILE A 14 ? 0.7767 0.9466 1.0393 -0.2128 -0.0809 -0.0865 18 ILE A CB 70 C CG1 . ILE A 14 ? 0.7626 0.9596 1.0583 -0.2067 -0.0677 -0.0927 18 ILE A CG1 71 C CG2 . ILE A 14 ? 0.7763 0.9568 1.0321 -0.2238 -0.0829 -0.0852 18 ILE A CG2 72 C CD1 . ILE A 14 ? 0.8461 1.0794 1.1833 -0.2040 -0.0725 -0.0907 18 ILE A CD1 73 N N . THR A 15 ? 0.7198 0.8659 0.9507 -0.2205 -0.0412 -0.0986 19 THR A N 74 C CA . THR A 15 ? 0.6936 0.8497 0.9254 -0.2292 -0.0276 -0.1022 19 THR A CA 75 C C . THR A 15 ? 0.6875 0.8694 0.9423 -0.2306 -0.0231 -0.1083 19 THR A C 76 O O . THR A 15 ? 0.6720 0.8600 0.9420 -0.2233 -0.0252 -0.1098 19 THR A O 77 C CB . THR A 15 ? 0.8334 0.9679 1.0488 -0.2327 -0.0188 -0.1025 19 THR A CB 78 O OG1 . THR A 15 ? 0.8495 0.9757 1.0651 -0.2282 -0.0174 -0.1063 19 THR A OG1 79 C CG2 . THR A 15 ? 0.8367 0.9383 1.0248 -0.2316 -0.0192 -0.0972 19 THR A CG2 80 N N . VAL A 16 ? 0.6201 0.8138 0.8765 -0.2391 -0.0160 -0.1109 20 VAL A N 81 C CA . VAL A 16 ? 0.6015 0.8102 0.8707 -0.2422 -0.0116 -0.1175 20 VAL A CA 82 C C . VAL A 16 ? 0.6600 0.8636 0.9230 -0.2520 -0.0056 -0.1193 20 VAL A C 83 O O . VAL A 16 ? 0.6567 0.8604 0.9146 -0.2580 -0.0045 -0.1147 20 VAL A O 84 C CB . VAL A 16 ? 0.6285 0.8550 0.9012 -0.2438 -0.0137 -0.1186 20 VAL A CB 85 C CG1 . VAL A 16 ? 0.6108 0.8464 0.8874 -0.2490 -0.0080 -0.1262 20 VAL A CG1 86 C CG2 . VAL A 16 ? 0.6274 0.8605 0.9092 -0.2379 -0.0219 -0.1169 20 VAL A CG2 87 N N . ASP A 17 ? 0.6260 0.8227 0.8888 -0.2543 -0.0016 -0.1248 21 ASP A N 88 C CA . ASP A 17 ? 0.6358 0.8234 0.8888 -0.2668 -0.0001 -0.1261 21 ASP A CA 89 C C . ASP A 17 ? 0.6568 0.8502 0.9121 -0.2697 0.0006 -0.1326 21 ASP A C 90 O O . ASP A 17 ? 0.6438 0.8351 0.9032 -0.2624 0.0051 -0.1378 21 ASP A O 91 C CB . ASP A 17 ? 0.7006 0.8575 0.9346 -0.2699 0.0037 -0.1259 21 ASP A CB 92 C CG . ASP A 17 ? 0.9243 1.0699 1.1481 -0.2706 0.0033 -0.1206 21 ASP A CG 93 O OD1 . ASP A 17 ? 0.9287 1.0871 1.1585 -0.2765 0.0007 -0.1161 21 ASP A OD1 94 O OD2 . ASP A 17 ? 1.0596 1.1806 1.2671 -0.2644 0.0076 -0.1206 21 ASP A OD2 95 N N . TYR A 18 ? 0.6043 0.8054 0.8583 -0.2798 -0.0035 -0.1319 22 TYR A N 96 C CA . TYR A 18 ? 0.5940 0.7958 0.8441 -0.2826 -0.0042 -0.1389 22 TYR A CA 97 C C . TYR A 18 ? 0.6552 0.8274 0.8862 -0.2939 -0.0064 -0.1421 22 TYR A C 98 O O . TYR A 18 ? 0.6587 0.8257 0.8853 -0.3058 -0.0134 -0.1358 22 TYR A O 99 C CB . TYR A 18 ? 0.5887 0.8157 0.8464 -0.2835 -0.0079 -0.1355 22 TYR A CB 100 C CG . TYR A 18 ? 0.5918 0.8348 0.8542 -0.2730 -0.0045 -0.1340 22 TYR A CG 101 C CD1 . TYR A 18 ? 0.6113 0.8547 0.8696 -0.2677 -0.0017 -0.1419 22 TYR A CD1 102 C CD2 . TYR A 18 ? 0.5962 0.8476 0.8629 -0.2699 -0.0038 -0.1241 22 TYR A CD2 103 C CE1 . TYR A 18 ? 0.6200 0.8734 0.8773 -0.2615 -0.0015 -0.1392 22 TYR A CE1 104 C CE2 . TYR A 18 ? 0.5995 0.8542 0.8602 -0.2622 -0.0022 -0.1215 22 TYR A CE2 105 C CZ . TYR A 18 ? 0.6778 0.9341 0.9333 -0.2590 -0.0026 -0.1286 22 TYR A CZ 106 O OH . TYR A 18 ? 0.6611 0.9166 0.9057 -0.2549 -0.0039 -0.1247 22 TYR A OH 107 N N . LEU A 19 ? 0.6154 0.7639 0.8326 -0.2911 0.0001 -0.1509 23 LEU A N 108 C CA . LEU A 19 ? 0.6420 0.7469 0.8293 -0.3014 -0.0001 -0.1543 23 LEU A CA 109 C C . LEU A 19 ? 0.6717 0.7679 0.8477 -0.3036 -0.0015 -0.1638 23 LEU A C 110 O O . LEU A 19 ? 0.6632 0.7613 0.8427 -0.2938 0.0089 -0.1719 23 LEU A O 111 C CB . LEU A 19 ? 0.6743 0.7432 0.8455 -0.2943 0.0141 -0.1555 23 LEU A CB 112 C CG . LEU A 19 ? 0.7493 0.8183 0.9235 -0.2898 0.0168 -0.1472 23 LEU A CG 113 C CD1 . LEU A 19 ? 0.7278 0.8288 0.9331 -0.2720 0.0229 -0.1465 23 LEU A CD1 114 C CD2 . LEU A 19 ? 0.8292 0.8416 0.9645 -0.2924 0.0264 -0.1453 23 LEU A CD2 115 N N . TYR A 20 ? 0.6252 0.7133 0.7889 -0.3168 -0.0153 -0.1622 24 TYR A N 116 C CA . TYR A 20 ? 0.6305 0.7060 0.7782 -0.3190 -0.0194 -0.1712 24 TYR A CA 117 C C . TYR A 20 ? 0.7417 0.7533 0.8471 -0.3248 -0.0143 -0.1798 24 TYR A C 118 O O . TYR A 20 ? 0.7761 0.7476 0.8563 -0.3357 -0.0178 -0.1747 24 TYR A O 119 C CB . TYR A 20 ? 0.6386 0.7335 0.7936 -0.3296 -0.0386 -0.1638 24 TYR A CB 120 C CG . TYR A 20 ? 0.6500 0.7479 0.7964 -0.3265 -0.0432 -0.1716 24 TYR A CG 121 C CD1 . TYR A 20 ? 0.6385 0.7690 0.7983 -0.3125 -0.0342 -0.1756 24 TYR A CD1 122 C CD2 . TYR A 20 ? 0.6909 0.7560 0.8111 -0.3385 -0.0585 -0.1737 24 TYR A CD2 123 C CE1 . TYR A 20 ? 0.6430 0.7742 0.7893 -0.3089 -0.0376 -0.1822 24 TYR A CE1 124 C CE2 . TYR A 20 ? 0.6990 0.7660 0.8090 -0.3343 -0.0639 -0.1806 24 TYR A CE2 125 C CZ . TYR A 20 ? 0.7591 0.8594 0.8814 -0.3186 -0.0520 -0.1852 24 TYR A CZ 126 O OH . TYR A 20 ? 0.7830 0.8811 0.8883 -0.3132 -0.0554 -0.1923 24 TYR A OH 127 N N . ASN A 21 ? 0.7051 0.7008 0.7964 -0.3185 -0.0054 -0.1927 25 ASN A N 128 C CA . ASN A 21 ? 0.7452 0.6721 0.7903 -0.3235 0.0015 -0.2023 25 ASN A CA 129 C C . ASN A 21 ? 0.7928 0.7072 0.8165 -0.3322 -0.0160 -0.2077 25 ASN A C 130 O O . ASN A 21 ? 0.7520 0.6939 0.7854 -0.3244 -0.0148 -0.2153 25 ASN A O 131 C CB . ASN A 21 ? 0.7385 0.6522 0.7828 -0.3100 0.0268 -0.2131 25 ASN A CB 132 C CG . ASN A 21 ? 1.0052 0.8387 0.9982 -0.3135 0.0401 -0.2227 25 ASN A CG 133 O OD1 . ASN A 21 ? 0.8465 0.6318 0.7971 -0.3256 0.0276 -0.2269 25 ASN A OD1 134 N ND2 . ASN A 21 ? 0.9516 0.7656 0.9466 -0.3025 0.0663 -0.2254 25 ASN A ND2 135 N N . LYS A 22 ? 0.7929 0.6647 0.7850 -0.3489 -0.0336 -0.2028 26 LYS A N 136 C CA . LYS A 22 ? 0.8092 0.6657 0.7808 -0.3589 -0.0558 -0.2050 26 LYS A CA 137 C C . LYS A 22 ? 0.8963 0.7017 0.8255 -0.3540 -0.0459 -0.2235 26 LYS A C 138 O O . LYS A 22 ? 0.8894 0.7045 0.8136 -0.3530 -0.0583 -0.2288 26 LYS A O 139 C CB . LYS A 22 ? 0.8813 0.6970 0.8258 -0.3814 -0.0793 -0.1935 26 LYS A CB 140 C CG . LYS A 22 ? 0.9753 0.8377 0.9578 -0.3896 -0.0897 -0.1755 26 LYS A CG 141 C CD . LYS A 22 ? 1.0457 0.8924 1.0233 -0.3883 -0.0722 -0.1708 26 LYS A CD 142 C CE . LYS A 22 ? 1.1337 0.8908 1.0470 -0.4024 -0.0705 -0.1697 26 LYS A CE 143 N NZ . LYS A 22 ? 1.1932 0.9012 1.0764 -0.3873 -0.0410 -0.1821 26 LYS A NZ 144 N N . GLU A 23 ? 0.8834 0.6338 0.7821 -0.3497 -0.0215 -0.2326 27 GLU A N 145 C CA . GLU A 23 ? 0.9116 0.6042 0.7671 -0.3452 -0.0056 -0.2508 27 GLU A CA 146 C C . GLU A 23 ? 0.8981 0.6413 0.7821 -0.3302 0.0080 -0.2616 27 GLU A C 147 O O . GLU A 23 ? 0.9061 0.6250 0.7601 -0.3292 0.0070 -0.2754 27 GLU A O 148 C CB . GLU A 23 ? 0.9782 0.6008 0.7995 -0.3432 0.0218 -0.2541 27 GLU A CB 149 C CG . GLU A 23 ? 1.2119 0.7558 0.9797 -0.3596 0.0118 -0.2455 27 GLU A CG 150 C CD . GLU A 23 ? 1.6003 1.0651 1.3260 -0.3554 0.0431 -0.2466 27 GLU A CD 151 O OE1 . GLU A 23 ? 1.5810 1.0475 1.3198 -0.3394 0.0743 -0.2558 27 GLU A OE1 152 O OE2 . GLU A 23 ? 1.5823 0.9820 1.2610 -0.3685 0.0373 -0.2366 27 GLU A OE2 153 N N . THR A 24 ? 0.7973 0.6032 0.7321 -0.3195 0.0205 -0.2556 28 THR A N 154 C CA . THR A 24 ? 0.7555 0.6065 0.7141 -0.3080 0.0326 -0.2638 28 THR A CA 155 C C . THR A 24 ? 0.7619 0.6756 0.7462 -0.3056 0.0148 -0.2573 28 THR A C 156 O O . THR A 24 ? 0.7382 0.6737 0.7224 -0.2986 0.0212 -0.2653 28 THR A O 157 C CB . THR A 24 ? 0.8321 0.7125 0.8286 -0.2984 0.0541 -0.2600 28 THR A CB 158 O OG1 . THR A 24 ? 0.8535 0.7773 0.8874 -0.2978 0.0445 -0.2433 28 THR A OG1 159 C CG2 . THR A 24 ? 0.8168 0.6373 0.7910 -0.2964 0.0786 -0.2659 28 THR A CG2 160 N N . LYS A 25 ? 0.6994 0.6398 0.7038 -0.3113 -0.0052 -0.2419 29 LYS A N 161 C CA . LYS A 25 ? 0.6556 0.6557 0.6898 -0.3075 -0.0185 -0.2314 29 LYS A CA 162 C C . LYS A 25 ? 0.6676 0.7193 0.7383 -0.2973 -0.0059 -0.2260 29 LYS A C 163 O O . LYS A 25 ? 0.6450 0.7355 0.7283 -0.2906 -0.0081 -0.2212 29 LYS A O 164 C CB . LYS A 25 ? 0.6787 0.6734 0.6873 -0.3044 -0.0263 -0.2394 29 LYS A CB 165 C CG . LYS A 25 ? 0.7513 0.7110 0.7346 -0.3150 -0.0490 -0.2380 29 LYS A CG 166 C CD . LYS A 25 ? 0.8248 0.7931 0.7919 -0.3078 -0.0583 -0.2419 29 LYS A CD 167 C CE . LYS A 25 ? 0.9178 0.8660 0.8719 -0.3173 -0.0864 -0.2358 29 LYS A CE 168 N NZ . LYS A 25 ? 0.9152 0.8970 0.8748 -0.3057 -0.0952 -0.2314 29 LYS A NZ 169 N N . LEU A 26 ? 0.6129 0.6599 0.6971 -0.2956 0.0071 -0.2255 30 LEU A N 170 C CA . LEU A 26 ? 0.5769 0.6654 0.6939 -0.2875 0.0159 -0.2198 30 LEU A CA 171 C C . LEU A 26 ? 0.6140 0.7170 0.7579 -0.2883 0.0129 -0.2063 30 LEU A C 172 O O . LEU A 26 ? 0.6362 0.7075 0.7687 -0.2950 0.0107 -0.2039 30 LEU A O 173 C CB . LEU A 26 ? 0.5820 0.6580 0.6959 -0.2827 0.0346 -0.2311 30 LEU A CB 174 C CG . LEU A 26 ? 0.6561 0.7167 0.7402 -0.2822 0.0410 -0.2463 30 LEU A CG 175 C CD1 . LEU A 26 ? 0.6757 0.7104 0.7551 -0.2809 0.0616 -0.2577 30 LEU A CD1 176 C CD2 . LEU A 26 ? 0.6762 0.7771 0.7645 -0.2783 0.0365 -0.2428 30 LEU A CD2 177 N N . PHE A 27 ? 0.5237 0.6683 0.6960 -0.2822 0.0126 -0.1973 31 PHE A N 178 C CA . PHE A 27 ? 0.5036 0.6619 0.6984 -0.2814 0.0104 -0.1855 31 PHE A CA 179 C C . PHE A 27 ? 0.5600 0.7199 0.7703 -0.2738 0.0217 -0.1861 31 PHE A C 180 O O . PHE A 27 ? 0.5544 0.7231 0.7695 -0.2693 0.0289 -0.1922 31 PHE A O 181 C CB . PHE A 27 ? 0.4936 0.6897 0.7060 -0.2788 0.0030 -0.1743 31 PHE A CB 182 C CG . PHE A 27 ? 0.5048 0.7082 0.7182 -0.2854 -0.0077 -0.1662 31 PHE A CG 183 C CD1 . PHE A 27 ? 0.5465 0.7465 0.7687 -0.2927 -0.0135 -0.1574 31 PHE A CD1 184 C CD2 . PHE A 27 ? 0.5124 0.7277 0.7190 -0.2841 -0.0115 -0.1659 31 PHE A CD2 185 C CE1 . PHE A 27 ? 0.5565 0.7684 0.7865 -0.3008 -0.0242 -0.1480 31 PHE A CE1 186 C CE2 . PHE A 27 ? 0.5436 0.7726 0.7604 -0.2891 -0.0214 -0.1555 31 PHE A CE2 187 C CZ . PHE A 27 ? 0.5307 0.7601 0.7623 -0.2984 -0.0283 -0.1464 31 PHE A CZ 188 N N . THR A 28 ? 0.5293 0.6815 0.7479 -0.2727 0.0227 -0.1788 32 THR A N 189 C CA . THR A 28 ? 0.5331 0.6918 0.7722 -0.2630 0.0312 -0.1750 32 THR A CA 190 C C . THR A 28 ? 0.6022 0.7864 0.8573 -0.2608 0.0215 -0.1639 32 THR A C 191 O O . THR A 28 ? 0.6076 0.7857 0.8539 -0.2672 0.0148 -0.1588 32 THR A O 192 C CB . THR A 28 ? 0.6130 0.7310 0.8386 -0.2610 0.0435 -0.1753 32 THR A CB 193 O OG1 . THR A 28 ? 0.5528 0.6420 0.7623 -0.2614 0.0563 -0.1856 32 THR A OG1 194 C CG2 . THR A 28 ? 0.6049 0.7329 0.8547 -0.2483 0.0513 -0.1674 32 THR A CG2 195 N N . ALA A 29 ? 0.5596 0.7691 0.8361 -0.2533 0.0199 -0.1600 33 ALA A N 196 C CA . ALA A 29 ? 0.5539 0.7775 0.8394 -0.2503 0.0113 -0.1501 33 ALA A CA 197 C C . ALA A 29 ? 0.6264 0.8427 0.9246 -0.2410 0.0156 -0.1457 33 ALA A C 198 O O . ALA A 29 ? 0.6064 0.8320 0.9244 -0.2336 0.0203 -0.1459 33 ALA A O 199 C CB . ALA A 29 ? 0.5462 0.7927 0.8380 -0.2489 0.0043 -0.1473 33 ALA A CB 200 N N . LYS A 30 ? 0.6225 0.8216 0.9093 -0.2413 0.0150 -0.1411 34 LYS A N 201 C CA . LYS A 30 ? 0.6433 0.8312 0.9355 -0.2304 0.0196 -0.1360 34 LYS A CA 202 C C . LYS A 30 ? 0.6981 0.9004 0.9994 -0.2252 0.0081 -0.1289 34 LYS A C 203 O O . LYS A 30 ? 0.6905 0.8886 0.9774 -0.2316 0.0020 -0.1267 34 LYS A O 204 C CB . LYS A 30 ? 0.7019 0.8523 0.9653 -0.2341 0.0269 -0.1354 34 LYS A CB 205 C CG . LYS A 30 ? 0.9236 1.0571 1.1845 -0.2207 0.0336 -0.1294 34 LYS A CG 206 C CD . LYS A 30 ? 1.1360 1.2346 1.3808 -0.2149 0.0516 -0.1298 34 LYS A CD 207 C CE . LYS A 30 ? 1.3388 1.4308 1.5928 -0.1953 0.0611 -0.1222 34 LYS A CE 208 N NZ . LYS A 30 ? 1.4808 1.5445 1.7288 -0.1854 0.0835 -0.1209 34 LYS A NZ 209 N N . LEU A 31 ? 0.6637 0.8812 0.9891 -0.2141 0.0049 -0.1246 35 LEU A N 210 C CA . LEU A 31 ? 0.6704 0.8948 1.0013 -0.2088 -0.0089 -0.1173 35 LEU A CA 211 C C . LEU A 31 ? 0.7784 0.9780 1.0945 -0.2006 -0.0067 -0.1137 35 LEU A C 212 O O . LEU A 31 ? 0.7905 0.9803 1.1115 -0.1905 0.0038 -0.1124 35 LEU A O 213 C CB . LEU A 31 ? 0.6618 0.9126 1.0263 -0.2020 -0.0167 -0.1125 35 LEU A CB 214 C CG . LEU A 31 ? 0.7020 0.9745 1.0796 -0.2099 -0.0154 -0.1171 35 LEU A CG 215 C CD1 . LEU A 31 ? 0.7004 1.0001 1.1168 -0.2044 -0.0211 -0.1110 35 LEU A CD1 216 C CD2 . LEU A 31 ? 0.7266 0.9985 1.0804 -0.2217 -0.0245 -0.1184 35 LEU A CD2 217 N N . ASN A 32 ? 0.7741 0.9584 1.0674 -0.2048 -0.0137 -0.1120 36 ASN A N 218 C CA . ASN A 32 ? 0.8172 0.9724 1.0881 -0.1989 -0.0114 -0.1101 36 ASN A CA 219 C C . ASN A 32 ? 0.9163 1.0708 1.1969 -0.1843 -0.0227 -0.1037 36 ASN A C 220 O O . ASN A 32 ? 0.9239 1.0661 1.1900 -0.1849 -0.0346 -0.1011 36 ASN A O 221 C CB . ASN A 32 ? 0.8461 0.9818 1.0877 -0.2109 -0.0108 -0.1116 36 ASN A CB 222 C CG . ASN A 32 ? 1.1441 1.2847 1.3815 -0.2259 -0.0037 -0.1154 36 ASN A CG 223 O OD1 . ASN A 32 ? 1.1112 1.2594 1.3466 -0.2355 -0.0058 -0.1145 36 ASN A OD1 224 N ND2 . ASN A 32 ? 1.0017 1.1345 1.2356 -0.2278 0.0051 -0.1185 36 ASN A ND2 225 N N . VAL A 33 ? 0.8955 1.0622 1.2018 -0.1708 -0.0187 -0.1001 37 VAL A N 226 C CA . VAL A 33 ? 0.9146 1.0877 1.2410 -0.1542 -0.0294 -0.0916 37 VAL A CA 227 C C . VAL A 33 ? 1.0016 1.1650 1.3332 -0.1372 -0.0124 -0.0883 37 VAL A C 228 O O . VAL A 33 ? 0.9971 1.1584 1.3297 -0.1390 0.0061 -0.0914 37 VAL A O 229 C CB . VAL A 33 ? 0.9470 1.1586 1.3150 -0.1549 -0.0457 -0.0856 37 VAL A CB 230 C CG1 . VAL A 33 ? 0.9428 1.1474 1.2917 -0.1669 -0.0653 -0.0849 37 VAL A CG1 231 C CG2 . VAL A 33 ? 0.9211 1.1611 1.3171 -0.1607 -0.0339 -0.0890 37 VAL A CG2 232 N N . ASN A 34 ? 0.9917 1.1436 1.3222 -0.1199 -0.0181 -0.0812 38 ASN A N 233 C CA . ASN A 34 ? 1.0175 1.1562 1.3494 -0.0996 -0.0003 -0.0754 38 ASN A CA 234 C C . ASN A 34 ? 1.0526 1.2329 1.4450 -0.0873 0.0050 -0.0662 38 ASN A C 235 O O . ASN A 34 ? 1.0477 1.2236 1.4442 -0.0845 0.0289 -0.0668 38 ASN A O 236 C CB . ASN A 34 ? 1.0636 1.1742 1.3709 -0.0835 -0.0080 -0.0707 38 ASN A CB 237 C CG . ASN A 34 ? 1.3621 1.4303 1.6109 -0.0962 -0.0119 -0.0799 38 ASN A CG 238 O OD1 . ASN A 34 ? 1.3045 1.3672 1.5444 -0.1006 -0.0319 -0.0808 38 ASN A OD1 239 N ND2 . ASN A 34 ? 1.2574 1.2913 1.4629 -0.1042 0.0074 -0.0863 38 ASN A ND2 240 N N . GLU A 35 ? 0.9992 1.2169 1.4366 -0.0824 -0.0176 -0.0575 39 GLU A N 241 C CA . GLU A 35 ? 0.9878 1.2531 1.4921 -0.0727 -0.0173 -0.0464 39 GLU A CA 242 C C . GLU A 35 ? 1.0204 1.3104 1.5474 -0.0879 -0.0062 -0.0524 39 GLU A C 243 O O . GLU A 35 ? 0.9976 1.2799 1.4969 -0.1088 -0.0115 -0.0637 39 GLU A O 244 C CB . GLU A 35 ? 1.0031 1.2991 1.5437 -0.0701 -0.0510 -0.0352 39 GLU A CB 245 C CG . GLU A 35 ? 1.1025 1.3986 1.6242 -0.0941 -0.0775 -0.0410 39 GLU A CG 246 C CD . GLU A 35 ? 1.2651 1.5152 1.7285 -0.0983 -0.0920 -0.0463 39 GLU A CD 247 O OE1 . GLU A 35 ? 1.1261 1.3377 1.5429 -0.0974 -0.0742 -0.0555 39 GLU A OE1 248 O OE2 . GLU A 35 ? 1.1259 1.3744 1.5867 -0.1048 -0.1211 -0.0410 39 GLU A OE2 249 N N . ASN A 36 ? 0.9833 1.3016 1.5608 -0.0760 0.0104 -0.0442 40 ASN A N 250 C CA . ASN A 36 ? 0.9591 1.2981 1.5592 -0.0885 0.0229 -0.0499 40 ASN A CA 251 C C . ASN A 36 ? 0.9816 1.3659 1.6195 -0.1034 -0.0050 -0.0468 40 ASN A C 252 O O . ASN A 36 ? 0.9737 1.3993 1.6696 -0.0956 -0.0160 -0.0328 40 ASN A O 253 C CB . ASN A 36 ? 0.9849 1.3236 1.6130 -0.0715 0.0577 -0.0438 40 ASN A CB 254 C CG . ASN A 36 ? 1.2565 1.5456 1.8318 -0.0787 0.0858 -0.0569 40 ASN A CG 255 O OD1 . ASN A 36 ? 1.1954 1.4868 1.7820 -0.0851 0.1033 -0.0622 40 ASN A OD1 256 N ND2 . ASN A 36 ? 1.1293 1.3685 1.6421 -0.0800 0.0895 -0.0627 40 ASN A ND2 257 N N . VAL A 37 ? 0.9237 1.2965 1.5236 -0.1253 -0.0179 -0.0585 41 VAL A N 258 C CA . VAL A 37 ? 0.9071 1.3047 1.5169 -0.1435 -0.0439 -0.0577 41 VAL A CA 259 C C . VAL A 37 ? 0.9488 1.3781 1.5926 -0.1540 -0.0350 -0.0600 41 VAL A C 260 O O . VAL A 37 ? 0.9471 1.3681 1.5914 -0.1506 -0.0066 -0.0673 41 VAL A O 261 C CB . VAL A 37 ? 0.9542 1.3171 1.5019 -0.1584 -0.0547 -0.0679 41 VAL A CB 262 C CG1 . VAL A 37 ? 0.9320 1.2949 1.4590 -0.1774 -0.0497 -0.0792 41 VAL A CG1 263 C CG2 . VAL A 37 ? 0.9652 1.3219 1.5017 -0.1609 -0.0857 -0.0594 41 VAL A CG2 264 N N . GLU A 38 ? 0.8964 1.3565 1.5645 -0.1673 -0.0591 -0.0533 42 GLU A N 265 C CA . GLU A 38 ? 0.8774 1.3667 1.5742 -0.1802 -0.0530 -0.0555 42 GLU A CA 266 C C . GLU A 38 ? 0.9203 1.3937 1.5677 -0.2034 -0.0656 -0.0656 42 GLU A C 267 O O . GLU A 38 ? 0.9156 1.3741 1.5316 -0.2117 -0.0909 -0.0617 42 GLU A O 268 C CB . GLU A 38 ? 0.8957 1.4351 1.6616 -0.1794 -0.0709 -0.0373 42 GLU A CB 269 C CG . GLU A 38 ? 1.0360 1.5997 1.8630 -0.1547 -0.0506 -0.0256 42 GLU A CG 270 C CD . GLU A 38 ? 1.2778 1.8873 2.1732 -0.1454 -0.0738 -0.0027 42 GLU A CD 271 O OE1 . GLU A 38 ? 1.2035 1.8332 2.1081 -0.1633 -0.1097 0.0055 42 GLU A OE1 272 O OE2 . GLU A 38 ? 1.1821 1.8018 2.1161 -0.1195 -0.0575 0.0082 42 GLU A OE2 273 N N . CYS A 39 ? 0.8776 1.3485 1.5135 -0.2131 -0.0465 -0.0782 43 CYS A N 274 C CA . CYS A 39 ? 0.8769 1.3322 1.4643 -0.2331 -0.0547 -0.0876 43 CYS A CA 275 C C . CYS A 39 ? 0.9125 1.3945 1.5225 -0.2480 -0.0555 -0.0877 43 CYS A C 276 O O . CYS A 39 ? 0.8986 1.3949 1.5410 -0.2437 -0.0322 -0.0923 43 CYS A O 277 C CB . CYS A 39 ? 0.8819 1.3019 1.4201 -0.2329 -0.0346 -0.1039 43 CYS A CB 278 S SG . CYS A 39 ? 0.9438 1.3314 1.4531 -0.2195 -0.0323 -0.1042 43 CYS A SG 279 N N . GLY A 40 ? 0.8738 1.3561 1.4610 -0.2661 -0.0806 -0.0824 44 GLY A N 280 C CA . GLY A 40 ? 1.1527 1.6565 1.7515 -0.2853 -0.0867 -0.0810 44 GLY A CA 281 C C . GLY A 40 ? 1.1366 1.6903 1.8168 -0.2824 -0.0856 -0.0693 44 GLY A C 282 O O . GLY A 40 ? 0.4805 1.0462 1.1947 -0.2721 -0.0559 -0.0758 44 GLY A O 283 N N . CYS A 44 ? 0.8874 1.2524 1.4253 -0.2068 0.0496 -0.1290 48 CYS A N 284 C CA . CYS A 44 ? 0.8950 1.2301 1.3994 -0.2009 0.0477 -0.1291 48 CYS A CA 285 C C . CYS A 44 ? 0.9468 1.2660 1.4662 -0.1827 0.0666 -0.1220 48 CYS A C 286 O O . CYS A 44 ? 0.9517 1.2737 1.4788 -0.1721 0.0578 -0.1117 48 CYS A O 287 C CB . CYS A 44 ? 0.8981 1.2425 1.3919 -0.2043 0.0208 -0.1221 48 CYS A CB 288 S SG . CYS A 44 ? 0.9369 1.2970 1.4135 -0.2226 -0.0011 -0.1240 48 CYS A SG 289 N N . THR A 45 ? 0.8962 1.1913 1.4127 -0.1785 0.0942 -0.1276 49 THR A N 290 C CA . THR A 45 ? 0.9106 1.1778 1.4303 -0.1606 0.1191 -0.1206 49 THR A CA 291 C C . THR A 45 ? 0.9360 1.1616 1.4063 -0.1589 0.1164 -0.1210 49 THR A C 292 O O . THR A 45 ? 0.9249 1.1239 1.3496 -0.1732 0.1100 -0.1316 49 THR A O 293 C CB . THR A 45 ? 1.0585 1.2949 1.5718 -0.1591 0.1509 -0.1278 49 THR A CB 294 O OG1 . THR A 45 ? 1.0702 1.2699 1.5292 -0.1755 0.1497 -0.1442 49 THR A OG1 295 C CG2 . THR A 45 ? 1.0335 1.3135 1.6045 -0.1585 0.1580 -0.1244 49 THR A CG2 296 N N . ASN A 46 ? 0.8839 1.1072 1.3650 -0.1419 0.1192 -0.1083 50 ASN A N 297 C CA . ASN A 46 ? 0.8934 1.0775 1.3288 -0.1389 0.1176 -0.1065 50 ASN A CA 298 C C . ASN A 46 ? 0.8831 1.0779 1.2971 -0.1542 0.0887 -0.1115 50 ASN A C 299 O O . ASN A 46 ? 0.8951 1.0544 1.2625 -0.1618 0.0870 -0.1155 50 ASN A O 300 C CB . ASN A 46 ? 0.9554 1.0733 1.3366 -0.1409 0.1424 -0.1118 50 ASN A CB 301 C CG . ASN A 46 ? 1.3877 1.4569 1.7240 -0.1327 0.1510 -0.1053 50 ASN A CG 302 O OD1 . ASN A 46 ? 1.3444 1.4256 1.6834 -0.1257 0.1382 -0.0987 50 ASN A OD1 303 N ND2 . ASN A 46 ? 1.3601 1.3652 1.6457 -0.1349 0.1730 -0.1075 50 ASN A ND2 304 N N . ASN A 47 ? 0.7748 1.0158 1.2220 -0.1589 0.0667 -0.1097 51 ASN A N 305 C CA . ASN A 47 ? 0.7399 0.9906 1.1700 -0.1715 0.0418 -0.1123 51 ASN A CA 306 C C . ASN A 47 ? 0.7636 0.9981 1.1576 -0.1893 0.0408 -0.1241 51 ASN A C 307 O O . ASN A 47 ? 0.7640 0.9889 1.1315 -0.1974 0.0297 -0.1255 51 ASN A O 308 C CB . ASN A 47 ? 0.7432 0.9775 1.1551 -0.1639 0.0332 -0.1060 51 ASN A CB 309 C CG . ASN A 47 ? 0.9288 1.1840 1.3756 -0.1473 0.0249 -0.0937 51 ASN A CG 310 O OD1 . ASN A 47 ? 0.8514 1.1428 1.3441 -0.1434 0.0200 -0.0876 51 ASN A OD1 311 N ND2 . ASN A 47 ? 0.8110 1.0437 1.2360 -0.1383 0.0213 -0.0894 51 ASN A ND2 312 N N . GLU A 48 ? 0.6972 0.9284 1.0915 -0.1946 0.0531 -0.1320 52 GLU A N 313 C CA . GLU A 48 ? 0.6829 0.8982 1.0447 -0.2096 0.0522 -0.1429 52 GLU A CA 314 C C . GLU A 48 ? 0.6830 0.9221 1.0575 -0.2168 0.0496 -0.1493 52 GLU A C 315 O O . GLU A 48 ? 0.6675 0.9159 1.0669 -0.2120 0.0613 -0.1500 52 GLU A O 316 C CB . GLU A 48 ? 0.7309 0.8996 1.0616 -0.2106 0.0707 -0.1484 52 GLU A CB 317 C CG . GLU A 48 ? 0.9033 1.0377 1.2064 -0.2078 0.0738 -0.1428 52 GLU A CG 318 C CD . GLU A 48 ? 1.2359 1.3133 1.4984 -0.2108 0.0911 -0.1462 52 GLU A CD 319 O OE1 . GLU A 48 ? 1.0737 1.1343 1.3371 -0.2073 0.1084 -0.1505 52 GLU A OE1 320 O OE2 . GLU A 48 ? 1.2584 1.3029 1.4844 -0.2174 0.0881 -0.1437 52 GLU A OE2 321 N N . VAL A 49 ? 0.6113 0.8580 0.9670 -0.2279 0.0363 -0.1534 53 VAL A N 322 C CA . VAL A 49 ? 0.5838 0.8442 0.9370 -0.2358 0.0347 -0.1604 53 VAL A CA 323 C C . VAL A 49 ? 0.6364 0.8674 0.9554 -0.2429 0.0429 -0.1722 53 VAL A C 324 O O . VAL A 49 ? 0.6174 0.8378 0.9138 -0.2478 0.0356 -0.1720 53 VAL A O 325 C CB . VAL A 49 ? 0.6076 0.8889 0.9556 -0.2416 0.0167 -0.1554 53 VAL A CB 326 C CG1 . VAL A 49 ? 0.5961 0.8849 0.9331 -0.2500 0.0172 -0.1625 53 VAL A CG1 327 C CG2 . VAL A 49 ? 0.6014 0.9020 0.9762 -0.2358 0.0046 -0.1430 53 VAL A CG2 328 N N . HIS A 50 ? 0.6223 0.8377 0.9383 -0.2432 0.0582 -0.1815 54 HIS A N 329 C CA . HIS A 50 ? 0.6457 0.8235 0.9249 -0.2495 0.0658 -0.1934 54 HIS A CA 330 C C . HIS A 50 ? 0.6786 0.8609 0.9366 -0.2573 0.0614 -0.2033 54 HIS A C 331 O O . HIS A 50 ? 0.6550 0.8656 0.9252 -0.2587 0.0570 -0.2022 54 HIS A O 332 C CB . HIS A 50 ? 0.6917 0.8349 0.9687 -0.2446 0.0888 -0.1987 54 HIS A CB 333 C CG . HIS A 50 ? 0.7640 0.8876 1.0473 -0.2356 0.0978 -0.1892 54 HIS A CG 334 N ND1 . HIS A 50 ? 0.8153 0.9031 1.0650 -0.2397 0.0936 -0.1873 54 HIS A ND1 335 C CD2 . HIS A 50 ? 0.7943 0.9281 1.1112 -0.2227 0.1108 -0.1802 54 HIS A CD2 336 C CE1 . HIS A 50 ? 0.8296 0.9022 1.0862 -0.2294 0.1053 -0.1782 54 HIS A CE1 337 N NE2 . HIS A 50 ? 0.8219 0.9219 1.1201 -0.2173 0.1166 -0.1734 54 HIS A NE2 338 N N . ASN A 51 ? 0.6507 0.7998 0.8726 -0.2628 0.0623 -0.2127 55 ASN A N 339 C CA . ASN A 51 ? 0.6433 0.7850 0.8355 -0.2683 0.0607 -0.2241 55 ASN A CA 340 C C . ASN A 51 ? 0.6598 0.8340 0.8499 -0.2696 0.0473 -0.2187 55 ASN A C 341 O O . ASN A 51 ? 0.6585 0.8400 0.8364 -0.2717 0.0495 -0.2244 55 ASN A O 342 C CB . ASN A 51 ? 0.6482 0.7745 0.8349 -0.2689 0.0782 -0.2367 55 ASN A CB 343 C CG . ASN A 51 ? 1.0005 1.0842 1.1819 -0.2662 0.0976 -0.2424 55 ASN A CG 344 O OD1 . ASN A 51 ? 0.9357 0.9841 1.0986 -0.2665 0.0970 -0.2405 55 ASN A OD1 345 N ND2 . ASN A 51 ? 0.9336 1.0203 1.1311 -0.2646 0.1154 -0.2480 55 ASN A ND2 346 N N . LEU A 52 ? 0.5949 0.7832 0.7916 -0.2689 0.0352 -0.2073 56 LEU A N 347 C CA . LEU A 52 ? 0.5730 0.7841 0.7635 -0.2683 0.0261 -0.1998 56 LEU A CA 348 C C . LEU A 52 ? 0.6217 0.8219 0.7858 -0.2698 0.0218 -0.2026 56 LEU A C 349 O O . LEU A 52 ? 0.6218 0.8103 0.7869 -0.2725 0.0168 -0.2011 56 LEU A O 350 C CB . LEU A 52 ? 0.5604 0.7912 0.7741 -0.2656 0.0180 -0.1846 56 LEU A CB 351 C CG . LEU A 52 ? 0.6117 0.8544 0.8533 -0.2624 0.0183 -0.1791 56 LEU A CG 352 C CD1 . LEU A 52 ? 0.6088 0.8582 0.8641 -0.2596 0.0112 -0.1671 56 LEU A CD1 353 C CD2 . LEU A 52 ? 0.6401 0.8979 0.8815 -0.2636 0.0158 -0.1773 56 LEU A CD2 354 N N . THR A 53 ? 0.5670 0.7694 0.7057 -0.2684 0.0231 -0.2056 57 THR A N 355 C CA . THR A 53 ? 0.5655 0.7613 0.6801 -0.2665 0.0194 -0.2062 57 THR A CA 356 C C . THR A 53 ? 0.5919 0.8110 0.7246 -0.2630 0.0127 -0.1885 57 THR A C 357 O O . THR A 53 ? 0.5764 0.8107 0.7193 -0.2604 0.0136 -0.1779 57 THR A O 358 C CB . THR A 53 ? 0.6767 0.8642 0.7529 -0.2641 0.0258 -0.2136 57 THR A CB 359 O OG1 . THR A 53 ? 0.6968 0.8634 0.7598 -0.2689 0.0342 -0.2299 57 THR A OG1 360 C CG2 . THR A 53 ? 0.6540 0.8332 0.7027 -0.2590 0.0231 -0.2140 57 THR A CG2 361 N N . GLU A 54 ? 0.5382 0.7572 0.6740 -0.2636 0.0055 -0.1849 58 GLU A N 362 C CA . GLU A 54 ? 0.5179 0.7604 0.6751 -0.2610 0.0007 -0.1676 58 GLU A CA 363 C C . GLU A 54 ? 0.5521 0.8056 0.6940 -0.2509 0.0089 -0.1581 58 GLU A C 364 O O . GLU A 54 ? 0.5564 0.7971 0.6638 -0.2466 0.0146 -0.1658 58 GLU A O 365 C CB . GLU A 54 ? 0.5437 0.7848 0.7062 -0.2650 -0.0104 -0.1658 58 GLU A CB 366 C CG . GLU A 54 ? 0.6832 0.9150 0.8163 -0.2589 -0.0107 -0.1718 58 GLU A CG 367 C CD . GLU A 54 ? 0.9226 1.1616 1.0667 -0.2607 -0.0247 -0.1643 58 GLU A CD 368 O OE1 . GLU A 54 ? 0.8789 1.0921 1.0134 -0.2707 -0.0367 -0.1734 58 GLU A OE1 369 O OE2 . GLU A 54 ? 0.7465 1.0135 0.9065 -0.2520 -0.0234 -0.1485 58 GLU A OE2 370 N N . CYS A 55 ? 0.5043 0.7744 0.6649 -0.2473 0.0115 -0.1416 59 CYS A N 371 C CA . CYS A 55 ? 0.5069 0.7793 0.6492 -0.2367 0.0223 -0.1285 59 CYS A CA 372 C C . CYS A 55 ? 0.5282 0.7805 0.6290 -0.2343 0.0298 -0.1330 59 CYS A C 373 O O . CYS A 55 ? 0.5258 0.7677 0.5925 -0.2256 0.0397 -0.1263 59 CYS A O 374 C CB . CYS A 55 ? 0.5272 0.8100 0.6687 -0.2285 0.0240 -0.1212 59 CYS A CB 375 S SG . CYS A 55 ? 0.5756 0.8887 0.7721 -0.2330 0.0146 -0.1070 59 CYS A SG 376 N N . LYS A 56 ? 0.4792 0.7248 0.5818 -0.2423 0.0254 -0.1425 60 LYS A N 377 C CA . LYS A 56 ? 0.4862 0.7154 0.5551 -0.2448 0.0284 -0.1460 60 LYS A CA 378 C C . LYS A 56 ? 0.5363 0.7677 0.6242 -0.2494 0.0225 -0.1396 60 LYS A C 379 O O . LYS A 56 ? 0.5245 0.7681 0.6496 -0.2526 0.0163 -0.1428 60 LYS A O 380 C CB . LYS A 56 ? 0.5008 0.7217 0.5570 -0.2511 0.0278 -0.1654 60 LYS A CB 381 C CG . LYS A 56 ? 0.5743 0.7829 0.5977 -0.2464 0.0332 -0.1740 60 LYS A CG 382 C CD . LYS A 56 ? 0.7624 0.9504 0.7494 -0.2522 0.0378 -0.1916 60 LYS A CD 383 C CE . LYS A 56 ? 0.9259 1.1138 0.9321 -0.2627 0.0365 -0.2043 60 LYS A CE 384 N NZ . LYS A 56 ? 0.9501 1.1199 0.9164 -0.2694 0.0432 -0.2157 60 LYS A NZ 385 N N . ASN A 57 ? 0.4998 0.7142 0.5573 -0.2496 0.0237 -0.1299 61 ASN A N 386 C CA . ASN A 57 ? 0.4996 0.7112 0.5698 -0.2546 0.0145 -0.1239 61 ASN A CA 387 C C . ASN A 57 ? 0.5562 0.7736 0.6334 -0.2640 0.0067 -0.1349 61 ASN A C 388 O O . ASN A 57 ? 0.5616 0.7693 0.6072 -0.2685 0.0098 -0.1415 61 ASN A O 389 C CB . ASN A 57 ? 0.5134 0.6954 0.5427 -0.2529 0.0169 -0.1079 61 ASN A CB 390 C CG . ASN A 57 ? 0.7461 0.9221 0.7803 -0.2438 0.0259 -0.0941 61 ASN A CG 391 O OD1 . ASN A 57 ? 0.7957 0.9950 0.8672 -0.2398 0.0287 -0.0957 61 ASN A OD1 392 N ND2 . ASN A 57 ? 0.5749 0.7155 0.5692 -0.2411 0.0314 -0.0792 61 ASN A ND2 393 N N . ALA A 58 ? 0.5081 0.7414 0.6276 -0.2661 -0.0014 -0.1369 62 ALA A N 394 C CA . ALA A 58 ? 0.5085 0.7540 0.6495 -0.2728 -0.0071 -0.1444 62 ALA A CA 395 C C . ALA A 58 ? 0.5841 0.8317 0.7414 -0.2749 -0.0206 -0.1333 62 ALA A C 396 O O . ALA A 58 ? 0.5789 0.8204 0.7416 -0.2696 -0.0236 -0.1246 62 ALA A O 397 C CB . ALA A 58 ? 0.5009 0.7604 0.6783 -0.2701 -0.0014 -0.1560 62 ALA A CB 398 N N . SER A 59 ? 0.5679 0.8226 0.7317 -0.2835 -0.0297 -0.1328 63 SER A N 399 C CA . SER A 59 ? 0.5849 0.8413 0.7641 -0.2863 -0.0469 -0.1207 63 SER A CA 400 C C . SER A 59 ? 0.6347 0.9219 0.8712 -0.2850 -0.0510 -0.1233 63 SER A C 401 O O . SER A 59 ? 0.6161 0.9195 0.8705 -0.2882 -0.0427 -0.1328 63 SER A O 402 C CB . SER A 59 ? 0.6659 0.9004 0.8009 -0.2989 -0.0589 -0.1117 63 SER A CB 403 O OG . SER A 59 ? 0.8253 1.0487 0.9618 -0.3014 -0.0783 -0.0976 63 SER A OG 404 N N . VAL A 60 ? 0.6106 0.9027 0.8743 -0.2785 -0.0612 -0.1147 64 VAL A N 405 C CA . VAL A 60 ? 0.6071 0.9273 0.9263 -0.2735 -0.0646 -0.1133 64 VAL A CA 406 C C . VAL A 60 ? 0.6848 1.0066 1.0162 -0.2752 -0.0886 -0.0982 64 VAL A C 407 O O . VAL A 60 ? 0.6962 0.9913 0.9996 -0.2729 -0.0974 -0.0912 64 VAL A O 408 C CB . VAL A 60 ? 0.6459 0.9704 0.9904 -0.2602 -0.0484 -0.1203 64 VAL A CB 409 C CG1 . VAL A 60 ? 0.6518 0.9585 0.9861 -0.2521 -0.0523 -0.1147 64 VAL A CG1 410 C CG2 . VAL A 60 ? 0.6383 0.9887 1.0350 -0.2541 -0.0429 -0.1204 64 VAL A CG2 411 N N . SER A 61 ? 0.6530 1.0029 1.0229 -0.2808 -0.0999 -0.0924 65 SER A N 412 C CA . SER A 61 ? 0.6804 1.0341 1.0660 -0.2837 -0.1275 -0.0764 65 SER A CA 413 C C . SER A 61 ? 0.7269 1.1060 1.1704 -0.2667 -0.1261 -0.0724 65 SER A C 414 O O . SER A 61 ? 0.7111 1.1235 1.2040 -0.2614 -0.1134 -0.0750 65 SER A O 415 C CB . SER A 61 ? 0.7536 1.1226 1.1451 -0.3024 -0.1449 -0.0689 65 SER A CB 416 O OG . SER A 61 ? 0.9380 1.2714 1.2799 -0.3151 -0.1702 -0.0569 65 SER A OG 417 N N . ILE A 62 ? 0.6951 1.0524 1.1266 -0.2565 -0.1348 -0.0670 66 ILE A N 418 C CA . ILE A 62 ? 0.6907 1.0605 1.1619 -0.2378 -0.1313 -0.0638 66 ILE A CA 419 C C . ILE A 62 ? 0.7956 1.1771 1.2960 -0.2352 -0.1601 -0.0473 66 ILE A C 420 O O . ILE A 62 ? 0.8237 1.1767 1.2883 -0.2443 -0.1847 -0.0394 66 ILE A O 421 C CB . ILE A 62 ? 0.7246 1.0589 1.1583 -0.2281 -0.1182 -0.0710 66 ILE A CB 422 C CG1 . ILE A 62 ? 0.7049 1.0342 1.1207 -0.2300 -0.0917 -0.0854 66 ILE A CG1 423 C CG2 . ILE A 62 ? 0.7364 1.0708 1.1939 -0.2095 -0.1163 -0.0671 66 ILE A CG2 424 C CD1 . ILE A 62 ? 0.7736 1.0686 1.1454 -0.2291 -0.0849 -0.0899 66 ILE A CD1 425 N N . SER A 63 ? 0.7633 1.1823 1.3266 -0.2214 -0.1562 -0.0412 67 SER A N 426 C CA . SER A 63 ? 0.7882 1.2268 1.3928 -0.2142 -0.1819 -0.0241 67 SER A CA 427 C C . SER A 63 ? 0.8507 1.3080 1.5008 -0.1880 -0.1634 -0.0216 67 SER A C 428 O O . SER A 63 ? 0.8247 1.2803 1.4754 -0.1791 -0.1309 -0.0325 67 SER A O 429 C CB . SER A 63 ? 0.8408 1.3200 1.4884 -0.2301 -0.2023 -0.0122 67 SER A CB 430 O OG . SER A 63 ? 0.9391 1.4605 1.6389 -0.2272 -0.1771 -0.0158 67 SER A OG 431 N N . HIS A 64 ? 0.8472 1.3160 1.5291 -0.1755 -0.1848 -0.0063 68 HIS A N 432 C CA . HIS A 64 ? 0.8554 1.3393 1.5786 -0.1478 -0.1707 0.0005 68 HIS A CA 433 C C . HIS A 64 ? 0.9231 1.4381 1.6984 -0.1414 -0.2043 0.0221 68 HIS A C 434 O O . HIS A 64 ? 0.9326 1.4356 1.6876 -0.1582 -0.2408 0.0289 68 HIS A O 435 C CB . HIS A 64 ? 0.8829 1.3146 1.5486 -0.1344 -0.1576 -0.0095 68 HIS A CB 436 C CG . HIS A 64 ? 0.9358 1.3708 1.6258 -0.1067 -0.1337 -0.0059 68 HIS A CG 437 N ND1 . HIS A 64 ? 0.9876 1.4120 1.6810 -0.0873 -0.1475 0.0046 68 HIS A ND1 438 C CD2 . HIS A 64 ? 0.9499 1.3893 1.6529 -0.0956 -0.0966 -0.0111 68 HIS A CD2 439 C CE1 . HIS A 64 ? 0.9874 1.4121 1.6961 -0.0642 -0.1170 0.0062 68 HIS A CE1 440 N NE2 . HIS A 64 ? 0.9711 1.4022 1.6846 -0.0688 -0.0855 -0.0026 68 HIS A NE2 441 N N . ASN A 65 ? 0.8849 1.4367 1.7251 -0.1174 -0.1925 0.0344 69 ASN A N 442 C CA . ASN A 65 ? 0.9039 1.4937 1.8057 -0.1080 -0.2239 0.0576 69 ASN A CA 443 C C . ASN A 65 ? 0.9890 1.5357 1.8458 -0.1028 -0.2573 0.0620 69 ASN A C 444 O O . ASN A 65 ? 1.0034 1.5684 1.8901 -0.1072 -0.2974 0.0796 69 ASN A O 445 C CB . ASN A 65 ? 0.9254 1.5596 1.9038 -0.0785 -0.1974 0.0708 69 ASN A CB 446 C CG . ASN A 65 ? 1.2747 1.8706 2.2185 -0.0515 -0.1588 0.0615 69 ASN A CG 447 O OD1 . ASN A 65 ? 1.2210 1.7686 2.1082 -0.0414 -0.1647 0.0562 69 ASN A OD1 448 N ND2 . ASN A 65 ? 1.1782 1.7900 2.1519 -0.0398 -0.1170 0.0600 69 ASN A ND2 449 N N . SER A 66 ? 0.9554 1.4418 1.7380 -0.0958 -0.2417 0.0460 70 SER A N 450 C CA . SER A 66 ? 0.9904 1.4221 1.7156 -0.0904 -0.2654 0.0454 70 SER A CA 451 C C . SER A 66 ? 1.0467 1.4373 1.7132 -0.1187 -0.2980 0.0423 70 SER A C 452 O O . SER A 66 ? 1.0742 1.4111 1.6871 -0.1169 -0.3187 0.0419 70 SER A O 453 C CB . SER A 66 ? 1.0474 1.4304 1.7156 -0.0750 -0.2323 0.0292 70 SER A CB 454 O OG . SER A 66 ? 1.1436 1.5047 1.7667 -0.0932 -0.2100 0.0112 70 SER A OG 455 N N . CYS A 67 ? 0.9818 1.3901 1.6512 -0.1441 -0.3002 0.0401 71 CYS A N 456 C CA . CYS A 67 ? 1.0058 1.3702 1.6139 -0.1708 -0.3267 0.0390 71 CYS A CA 457 C C . CYS A 67 ? 1.0371 1.4411 1.6811 -0.1950 -0.3492 0.0507 71 CYS A C 458 O O . CYS A 67 ? 0.9974 1.4625 1.7080 -0.1939 -0.3335 0.0534 71 CYS A O 459 C CB . CYS A 67 ? 1.0081 1.3227 1.5422 -0.1788 -0.2995 0.0190 71 CYS A CB 460 S SG . CYS A 67 ? 1.0077 1.3599 1.5643 -0.1813 -0.2540 0.0037 71 CYS A SG 461 N N . THR A 68 ? 1.0252 1.3892 1.6208 -0.2176 -0.3853 0.0582 72 THR A N 462 C CA . THR A 68 ? 1.0259 1.4178 1.6435 -0.2448 -0.4119 0.0710 72 THR A CA 463 C C . THR A 68 ? 1.0653 1.4260 1.6201 -0.2685 -0.3972 0.0590 72 THR A C 464 O O . THR A 68 ? 1.0591 1.3726 1.5517 -0.2640 -0.3716 0.0431 72 THR A O 465 C CB . THR A 68 ? 1.1752 1.5407 1.7797 -0.2568 -0.4670 0.0915 72 THR A CB 466 O OG1 . THR A 68 ? 1.2081 1.4824 1.7066 -0.2711 -0.4792 0.0865 72 THR A OG1 467 C CG2 . THR A 68 ? 1.1686 1.5524 1.8217 -0.2298 -0.4827 0.1027 72 THR A CG2 468 N N . ALA A 69 ? 1.0183 1.4036 1.5873 -0.2945 -0.4145 0.0680 73 ALA A N 469 C CA . ALA A 69 ? 1.0183 1.3702 1.5217 -0.3184 -0.4048 0.0595 73 ALA A CA 470 C C . ALA A 69 ? 1.1184 1.3764 1.5170 -0.3298 -0.4246 0.0619 73 ALA A C 471 O O . ALA A 69 ? 1.1525 1.3810 1.5404 -0.3276 -0.4577 0.0744 73 ALA A O 472 C CB . ALA A 69 ? 1.0287 1.4228 1.5675 -0.3448 -0.4244 0.0713 73 ALA A CB 473 N N . PRO A 70 ? 1.0799 1.2850 1.3985 -0.3393 -0.4035 0.0508 74 PRO A N 474 C CA . PRO A 70 ? 1.0364 1.2612 1.3497 -0.3417 -0.3654 0.0352 74 PRO A CA 475 C C . PRO A 70 ? 1.0232 1.2755 1.3698 -0.3153 -0.3247 0.0175 74 PRO A C 476 O O . PRO A 70 ? 1.0252 1.2539 1.3626 -0.2970 -0.3194 0.0143 74 PRO A O 477 C CB . PRO A 70 ? 1.1030 1.2455 1.3090 -0.3560 -0.3622 0.0340 74 PRO A CB 478 C CG . PRO A 70 ? 1.2061 1.2848 1.3663 -0.3475 -0.3779 0.0399 74 PRO A CG 479 C CD . PRO A 70 ? 1.1615 1.2715 1.3796 -0.3477 -0.4174 0.0550 74 PRO A CD 480 N N . ASP A 71 ? 0.9247 1.2192 1.3012 -0.3153 -0.2962 0.0058 75 ASP A N 481 C CA . ASP A 71 ? 0.8727 1.1871 1.2711 -0.2953 -0.2573 -0.0111 75 ASP A CA 482 C C . ASP A 71 ? 0.8935 1.1512 1.2192 -0.2920 -0.2394 -0.0207 75 ASP A C 483 O O . ASP A 71 ? 0.9186 1.1287 1.1779 -0.3067 -0.2476 -0.0167 75 ASP A O 484 C CB . ASP A 71 ? 0.8663 1.2213 1.2925 -0.3019 -0.2344 -0.0211 75 ASP A CB 485 C CG . ASP A 71 ? 0.9914 1.4115 1.5051 -0.2963 -0.2322 -0.0170 75 ASP A CG 486 O OD1 . ASP A 71 ? 1.0107 1.4533 1.5689 -0.2938 -0.2580 -0.0012 75 ASP A OD1 487 O OD2 . ASP A 71 ? 1.0410 1.4875 1.5780 -0.2947 -0.2049 -0.0284 75 ASP A OD2 488 N N . LYS A 72 ? 0.7931 1.0546 1.1301 -0.2734 -0.2135 -0.0321 76 LYS A N 489 C CA . LYS A 72 ? 0.7807 0.9990 1.0612 -0.2704 -0.1938 -0.0406 76 LYS A CA 490 C C . LYS A 72 ? 0.7829 1.0159 1.0554 -0.2764 -0.1698 -0.0517 76 LYS A C 491 O O . LYS A 72 ? 0.7396 1.0111 1.0550 -0.2693 -0.1518 -0.0612 76 LYS A O 492 C CB . LYS A 72 ? 0.7916 1.0049 1.0832 -0.2516 -0.1785 -0.0472 76 LYS A CB 493 C CG . LYS A 72 ? 0.8319 0.9919 1.0618 -0.2519 -0.1681 -0.0496 76 LYS A CG 494 C CD . LYS A 72 ? 0.7762 0.9394 0.9951 -0.2499 -0.1384 -0.0608 76 LYS A CD 495 C CE . LYS A 72 ? 0.7525 0.8639 0.9093 -0.2542 -0.1314 -0.0575 76 LYS A CE 496 N NZ . LYS A 72 ? 0.8306 0.9466 0.9824 -0.2506 -0.1042 -0.0656 76 LYS A NZ 497 N N . THR A 73 ? 0.7442 0.9405 0.9565 -0.2883 -0.1685 -0.0500 77 THR A N 498 C CA . THR A 73 ? 0.7112 0.9142 0.9064 -0.2923 -0.1459 -0.0602 77 THR A CA 499 C C . THR A 73 ? 0.7456 0.9313 0.9227 -0.2802 -0.1227 -0.0673 77 THR A C 500 O O . THR A 73 ? 0.7725 0.9137 0.9040 -0.2789 -0.1221 -0.0609 77 THR A O 501 C CB . THR A 73 ? 0.7802 0.9540 0.9198 -0.3101 -0.1545 -0.0537 77 THR A CB 502 O OG1 . THR A 73 ? 0.7763 0.9813 0.9477 -0.3232 -0.1728 -0.0497 77 THR A OG1 503 C CG2 . THR A 73 ? 0.7096 0.8756 0.8145 -0.3104 -0.1291 -0.0633 77 THR A CG2 504 N N . LEU A 74 ? 0.6546 0.8732 0.8690 -0.2718 -0.1041 -0.0792 78 LEU A N 505 C CA . LEU A 74 ? 0.6327 0.8437 0.8406 -0.2628 -0.0846 -0.0855 78 LEU A CA 506 C C . LEU A 74 ? 0.6626 0.8780 0.8530 -0.2656 -0.0671 -0.0933 78 LEU A C 507 O O . LEU A 74 ? 0.6306 0.8713 0.8412 -0.2683 -0.0619 -0.1020 78 LEU A O 508 C CB . LEU A 74 ? 0.6100 0.8449 0.8639 -0.2523 -0.0788 -0.0916 78 LEU A CB 509 C CG . LEU A 74 ? 0.6541 0.8838 0.9048 -0.2465 -0.0610 -0.0979 78 LEU A CG 510 C CD1 . LEU A 74 ? 0.6747 0.8703 0.8938 -0.2446 -0.0610 -0.0909 78 LEU A CD1 511 C CD2 . LEU A 74 ? 0.6765 0.9232 0.9630 -0.2388 -0.0551 -0.1035 78 LEU A CD2 512 N N . ILE A 75 ? 0.6375 0.8260 0.7902 -0.2637 -0.0567 -0.0895 79 ILE A N 513 C CA . ILE A 75 ? 0.6260 0.8167 0.7605 -0.2634 -0.0401 -0.0945 79 ILE A CA 514 C C . ILE A 75 ? 0.6394 0.8485 0.8031 -0.2567 -0.0279 -0.1013 79 ILE A C 515 O O . ILE A 75 ? 0.6478 0.8468 0.8143 -0.2522 -0.0248 -0.0963 79 ILE A O 516 C CB . ILE A 75 ? 0.6996 0.8509 0.7766 -0.2640 -0.0335 -0.0836 79 ILE A CB 517 C CG1 . ILE A 75 ? 0.7431 0.8656 0.7782 -0.2745 -0.0478 -0.0756 79 ILE A CG1 518 C CG2 . ILE A 75 ? 0.6958 0.8519 0.7587 -0.2594 -0.0147 -0.0869 79 ILE A CG2 519 C CD1 . ILE A 75 ? 0.8262 0.9679 0.8631 -0.2849 -0.0541 -0.0829 79 ILE A CD1 520 N N . LEU A 76 ? 0.5562 0.7876 0.7378 -0.2575 -0.0216 -0.1127 80 LEU A N 521 C CA . LEU A 76 ? 0.5321 0.7758 0.7352 -0.2545 -0.0131 -0.1188 80 LEU A CA 522 C C . LEU A 76 ? 0.5584 0.7993 0.7408 -0.2533 -0.0031 -0.1176 80 LEU A C 523 O O . LEU A 76 ? 0.5593 0.8010 0.7243 -0.2549 0.0003 -0.1234 80 LEU A O 524 C CB . LEU A 76 ? 0.5226 0.7821 0.7515 -0.2559 -0.0121 -0.1310 80 LEU A CB 525 C CG . LEU A 76 ? 0.5926 0.8599 0.8482 -0.2544 -0.0193 -0.1305 80 LEU A CG 526 C CD1 . LEU A 76 ? 0.5926 0.8701 0.8689 -0.2545 -0.0123 -0.1411 80 LEU A CD1 527 C CD2 . LEU A 76 ? 0.6322 0.8935 0.9008 -0.2491 -0.0225 -0.1246 80 LEU A CD2 528 N N . ASP A 77 ? 0.4935 0.7302 0.6768 -0.2500 0.0024 -0.1089 81 ASP A N 529 C CA . ASP A 77 ? 0.4805 0.7200 0.6536 -0.2467 0.0126 -0.1041 81 ASP A CA 530 C C . ASP A 77 ? 0.4985 0.7577 0.7002 -0.2498 0.0114 -0.1114 81 ASP A C 531 O O . ASP A 77 ? 0.4921 0.7570 0.7150 -0.2519 0.0109 -0.1070 81 ASP A O 532 C CB . ASP A 77 ? 0.5205 0.7449 0.6833 -0.2418 0.0211 -0.0887 81 ASP A CB 533 C CG . ASP A 77 ? 0.6603 0.8854 0.8104 -0.2349 0.0353 -0.0787 81 ASP A CG 534 O OD1 . ASP A 77 ? 0.6511 0.8931 0.8052 -0.2340 0.0361 -0.0844 81 ASP A OD1 535 O OD2 . ASP A 77 ? 0.7651 0.9712 0.9006 -0.2292 0.0469 -0.0646 81 ASP A OD2 536 N N . VAL A 78 ? 0.4353 0.6990 0.6325 -0.2519 0.0100 -0.1230 82 VAL A N 537 C CA . VAL A 78 ? 0.4133 0.6835 0.6268 -0.2566 0.0065 -0.1315 82 VAL A CA 538 C C . VAL A 78 ? 0.4338 0.7153 0.6556 -0.2565 0.0070 -0.1240 82 VAL A C 539 O O . VAL A 78 ? 0.4381 0.7229 0.6453 -0.2499 0.0131 -0.1181 82 VAL A O 540 C CB . VAL A 78 ? 0.4608 0.7231 0.6619 -0.2589 0.0064 -0.1469 82 VAL A CB 541 C CG1 . VAL A 78 ? 0.4607 0.7158 0.6693 -0.2645 0.0030 -0.1557 82 VAL A CG1 542 C CG2 . VAL A 78 ? 0.4598 0.7190 0.6649 -0.2593 0.0056 -0.1506 82 VAL A CG2 543 N N . PRO A 79 ? 0.3595 0.6462 0.6040 -0.2639 0.0007 -0.1220 83 PRO A N 544 C CA . PRO A 79 ? 0.3474 0.6505 0.6081 -0.2662 -0.0020 -0.1122 83 PRO A CA 545 C C . PRO A 79 ? 0.3829 0.6861 0.6345 -0.2672 -0.0082 -0.1186 83 PRO A C 546 O O . PRO A 79 ? 0.3782 0.6631 0.6070 -0.2673 -0.0088 -0.1332 83 PRO A O 547 C CB . PRO A 79 ? 0.3678 0.6709 0.6495 -0.2779 -0.0093 -0.1088 83 PRO A CB 548 C CG . PRO A 79 ? 0.4209 0.7058 0.6943 -0.2782 -0.0078 -0.1164 83 PRO A CG 549 C CD . PRO A 79 ? 0.3686 0.6449 0.6230 -0.2711 -0.0041 -0.1269 83 PRO A CD 550 N N . PRO A 80 ? 0.3352 0.6574 0.6050 -0.2682 -0.0133 -0.1078 84 PRO A N 551 C CA . PRO A 80 ? 0.3411 0.6594 0.5991 -0.2685 -0.0222 -0.1139 84 PRO A CA 552 C C . PRO A 80 ? 0.4055 0.6999 0.6558 -0.2831 -0.0374 -0.1253 84 PRO A C 553 O O . PRO A 80 ? 0.4067 0.6920 0.6657 -0.2939 -0.0415 -0.1250 84 PRO A O 554 C CB . PRO A 80 ? 0.3633 0.7138 0.6517 -0.2649 -0.0244 -0.0948 84 PRO A CB 555 C CG . PRO A 80 ? 0.4098 0.7770 0.7198 -0.2604 -0.0108 -0.0799 84 PRO A CG 556 C CD . PRO A 80 ? 0.3498 0.6981 0.6532 -0.2686 -0.0109 -0.0887 84 PRO A CD 557 N N . GLY A 81 ? 0.6720 1.0965 0.4772 -0.4653 -0.0112 -0.0440 85 GLY A N 558 C CA . GLY A 81 ? 0.6967 1.1542 0.4778 -0.5029 -0.0076 -0.0501 85 GLY A CA 559 C C . GLY A 81 ? 0.7444 1.1937 0.5437 -0.4766 -0.0127 -0.0400 85 GLY A C 560 O O . GLY A 81 ? 0.7456 1.1348 0.5463 -0.4615 -0.0288 -0.0053 85 GLY A O 561 N N . VAL A 82 ? 0.6838 1.1975 0.5054 -0.4696 -0.0013 -0.0769 86 VAL A N 562 C CA . VAL A 82 ? 0.6556 1.1708 0.5017 -0.4459 -0.0067 -0.0756 86 VAL A CA 563 C C . VAL A 82 ? 0.7223 1.2016 0.5312 -0.4799 -0.0170 -0.0404 86 VAL A C 564 O O . VAL A 82 ? 0.7021 1.1373 0.5243 -0.4522 -0.0281 -0.0143 86 VAL A O 565 C CB . VAL A 82 ? 0.6833 1.2815 0.5682 -0.4399 0.0016 -0.1333 86 VAL A CB 566 C CG1 . VAL A 82 ? 0.6688 1.2803 0.5765 -0.4315 -0.0046 -0.1401 86 VAL A CG1 567 C CG2 . VAL A 82 ? 0.6512 1.2610 0.5828 -0.3922 -0.0028 -0.1569 86 VAL A CG2 568 N N . GLU A 83 ? 0.7171 1.2100 0.4758 -0.5429 -0.0170 -0.0352 87 GLU A N 569 C CA . GLU A 83 ? 0.7546 1.2097 0.4675 -0.5864 -0.0349 0.0040 87 GLU A CA 570 C C . GLU A 83 ? 0.8245 1.1764 0.5299 -0.5722 -0.0646 0.0564 87 GLU A C 571 O O . GLU A 83 ? 0.8603 1.1669 0.5379 -0.5976 -0.0889 0.0919 87 GLU A O 572 C CB . GLU A 83 ? 0.8287 1.3337 0.4816 -0.6706 -0.0304 -0.0033 87 GLU A CB 573 C CG . GLU A 83 ? 0.9458 1.4893 0.5881 -0.6953 -0.0158 -0.0296 87 GLU A CG 574 C CD . GLU A 83 ? 1.1693 1.6331 0.7941 -0.6986 -0.0353 0.0074 87 GLU A CD 575 O OE1 . GLU A 83 ? 1.0896 1.4779 0.6742 -0.7333 -0.0678 0.0587 87 GLU A OE1 576 O OE2 . GLU A 83 ? 1.0307 1.5115 0.6832 -0.6711 -0.0214 -0.0186 87 GLU A OE2 577 N N . LYS A 84 ? 0.7546 1.0752 0.4904 -0.5317 -0.0655 0.0559 88 LYS A N 578 C CA . LYS A 84 ? 0.7682 1.0070 0.5153 -0.5138 -0.0941 0.0880 88 LYS A CA 579 C C . LYS A 84 ? 0.7978 1.0142 0.5876 -0.4604 -0.0978 0.0935 88 LYS A C 580 O O . LYS A 84 ? 0.8057 0.9665 0.6163 -0.4426 -0.1219 0.1098 88 LYS A O 581 C CB . LYS A 84 ? 0.7803 1.0082 0.5409 -0.5047 -0.0936 0.0777 88 LYS A CB 582 C CG . LYS A 84 ? 0.8219 1.0503 0.5345 -0.5681 -0.1008 0.0837 88 LYS A CG 583 C CD . LYS A 84 ? 0.8815 1.0966 0.6116 -0.5584 -0.1022 0.0724 88 LYS A CD 584 C CE . LYS A 84 ? 1.0566 1.2520 0.7373 -0.6270 -0.1197 0.0887 88 LYS A CE 585 N NZ . LYS A 84 ? 1.1619 1.3195 0.8690 -0.6143 -0.1343 0.0844 88 LYS A NZ 586 N N . PHE A 85 ? 0.7251 0.9877 0.5322 -0.4374 -0.0771 0.0759 89 PHE A N 587 C CA . PHE A 85 ? 0.6923 0.9430 0.5346 -0.3944 -0.0777 0.0808 89 PHE A CA 588 C C . PHE A 85 ? 0.7525 1.0155 0.5866 -0.4057 -0.0790 0.0854 89 PHE A C 589 O O . PHE A 85 ? 0.7447 1.0596 0.5675 -0.4273 -0.0661 0.0644 89 PHE A O 590 C CB . PHE A 85 ? 0.6667 0.9533 0.5424 -0.3549 -0.0592 0.0594 89 PHE A CB 591 C CG . PHE A 85 ? 0.6819 0.9702 0.5655 -0.3445 -0.0546 0.0501 89 PHE A CG 592 C CD1 . PHE A 85 ? 0.7206 0.9786 0.6236 -0.3274 -0.0641 0.0573 89 PHE A CD1 593 C CD2 . PHE A 85 ? 0.7055 1.0340 0.5840 -0.3512 -0.0413 0.0268 89 PHE A CD2 594 C CE1 . PHE A 85 ? 0.7315 0.9998 0.6456 -0.3199 -0.0594 0.0427 89 PHE A CE1 595 C CE2 . PHE A 85 ? 0.7394 1.0718 0.6246 -0.3429 -0.0370 0.0174 89 PHE A CE2 596 C CZ . PHE A 85 ? 0.7178 1.0200 0.6192 -0.3287 -0.0457 0.0261 89 PHE A CZ 597 N N . GLN A 86 ? 0.7167 0.9408 0.5632 -0.3901 -0.0941 0.1056 90 GLN A N 598 C CA . GLN A 86 ? 0.7130 0.9459 0.5550 -0.3980 -0.0968 0.1108 90 GLN A CA 599 C C . GLN A 86 ? 0.6938 0.9175 0.5755 -0.3554 -0.0949 0.1123 90 GLN A C 600 O O . GLN A 86 ? 0.6787 0.8671 0.5794 -0.3350 -0.1058 0.1227 90 GLN A O 601 C CB . GLN A 86 ? 0.7926 0.9829 0.5970 -0.4380 -0.1250 0.1403 90 GLN A CB 602 C CG . GLN A 86 ? 1.0768 1.2665 0.8784 -0.4430 -0.1332 0.1506 90 GLN A CG 603 C CD . GLN A 86 ? 1.4382 1.5595 1.2234 -0.4592 -0.1732 0.1857 90 GLN A CD 604 O OE1 . GLN A 86 ? 1.3712 1.4620 1.1888 -0.4276 -0.1864 0.1921 90 GLN A OE1 605 N NE2 . GLN A 86 ? 1.4272 1.5217 1.1636 -0.5112 -0.1981 0.2088 90 GLN A NE2 606 N N . LEU A 87 ? 0.6073 0.8672 0.5059 -0.3449 -0.0835 0.0976 91 LEU A N 607 C CA . LEU A 87 ? 0.5706 0.8213 0.5017 -0.3130 -0.0840 0.1027 91 LEU A CA 608 C C . LEU A 87 ? 0.6447 0.8705 0.5684 -0.3232 -0.0980 0.1192 91 LEU A C 609 O O . LEU A 87 ? 0.6556 0.9026 0.5639 -0.3468 -0.0989 0.1144 91 LEU A O 610 C CB . LEU A 87 ? 0.5376 0.8258 0.4967 -0.2969 -0.0761 0.0818 91 LEU A CB 611 C CG . LEU A 87 ? 0.5622 0.8376 0.5510 -0.2705 -0.0803 0.0916 91 LEU A CG 612 C CD1 . LEU A 87 ? 0.5584 0.8136 0.5485 -0.2571 -0.0787 0.1075 91 LEU A CD1 613 C CD2 . LEU A 87 ? 0.5622 0.8639 0.5840 -0.2568 -0.0853 0.0718 91 LEU A CD2 614 N N . HIS A 88 ? 0.6063 0.7934 0.5426 -0.3083 -0.1106 0.1338 92 HIS A N 615 C CA . HIS A 88 ? 0.6278 0.7818 0.5638 -0.3131 -0.1318 0.1491 92 HIS A CA 616 C C . HIS A 88 ? 0.6255 0.7848 0.5959 -0.2862 -0.1267 0.1461 92 HIS A C 617 O O . HIS A 88 ? 0.5804 0.7525 0.5750 -0.2647 -0.1146 0.1382 92 HIS A O 618 C CB . HIS A 88 ? 0.6787 0.7856 0.6169 -0.3150 -0.1583 0.1584 92 HIS A CB 619 C CG . HIS A 88 ? 0.7551 0.8198 0.7068 -0.3125 -0.1908 0.1703 92 HIS A CG 620 N ND1 . HIS A 88 ? 0.8242 0.8602 0.7395 -0.3464 -0.2182 0.1939 92 HIS A ND1 621 C CD2 . HIS A 88 ? 0.7701 0.8214 0.7692 -0.2829 -0.2029 0.1583 92 HIS A CD2 622 C CE1 . HIS A 88 ? 0.8342 0.8317 0.7779 -0.3315 -0.2497 0.1986 92 HIS A CE1 623 N NE2 . HIS A 88 ? 0.8043 0.8128 0.8033 -0.2915 -0.2407 0.1732 92 HIS A NE2 624 N N . ASP A 89 ? 0.5998 0.7527 0.5685 -0.2927 -0.1366 0.1532 93 ASP A N 625 C CA . ASP A 89 ? 0.5817 0.7381 0.5820 -0.2715 -0.1340 0.1507 93 ASP A CA 626 C C . ASP A 89 ? 0.6541 0.7756 0.6731 -0.2618 -0.1574 0.1538 93 ASP A C 627 O O . ASP A 89 ? 0.6807 0.7710 0.6854 -0.2765 -0.1847 0.1665 93 ASP A O 628 C CB . ASP A 89 ? 0.6066 0.7807 0.6015 -0.2828 -0.1331 0.1501 93 ASP A CB 629 C CG . ASP A 89 ? 0.7364 0.9157 0.7647 -0.2630 -0.1294 0.1469 93 ASP A CG 630 O OD1 . ASP A 89 ? 0.7325 0.8984 0.7828 -0.2467 -0.1325 0.1475 93 ASP A OD1 631 O OD2 . ASP A 89 ? 0.8277 1.0302 0.8640 -0.2660 -0.1243 0.1389 93 ASP A OD2 632 N N . CYS A 90 ? 0.6060 0.7373 0.6590 -0.2403 -0.1506 0.1390 94 CYS A N 633 C CA . CYS A 90 ? 0.6284 0.7420 0.7188 -0.2259 -0.1733 0.1248 94 CYS A CA 634 C C . CYS A 90 ? 0.6458 0.7721 0.7683 -0.2127 -0.1737 0.1146 94 CYS A C 635 O O . CYS A 90 ? 0.6407 0.7705 0.8080 -0.1970 -0.1881 0.0898 94 CYS A O 636 C CB . CYS A 90 ? 0.6359 0.7703 0.7524 -0.2144 -0.1658 0.1012 94 CYS A CB 637 S SG . CYS A 90 ? 0.6557 0.8464 0.7613 -0.2158 -0.1236 0.0977 94 CYS A SG 638 N N . THR A 91 ? 0.5793 0.7184 0.6875 -0.2181 -0.1590 0.1266 95 THR A N 639 C CA . THR A 91 ? 0.5586 0.7124 0.6957 -0.2082 -0.1567 0.1176 95 THR A CA 640 C C . THR A 91 ? 0.6494 0.7749 0.8116 -0.1999 -0.1908 0.1099 95 THR A C 641 O O . THR A 91 ? 0.6718 0.7586 0.8087 -0.2121 -0.2179 0.1292 95 THR A O 642 C CB . THR A 91 ? 0.5218 0.6879 0.6433 -0.2158 -0.1414 0.1308 95 THR A CB 643 O OG1 . THR A 91 ? 0.5078 0.6924 0.6161 -0.2202 -0.1215 0.1352 95 THR A OG1 644 C CG2 . THR A 91 ? 0.4185 0.6021 0.5689 -0.2085 -0.1355 0.1226 95 THR A CG2 645 N N . GLN A 92 ? 0.6088 0.7584 0.8218 -0.1828 -0.1923 0.0789 96 GLN A N 646 C CA . GLN A 92 ? 0.6363 0.7668 0.8924 -0.1678 -0.2284 0.0597 96 GLN A CA 647 C C . GLN A 92 ? 0.6715 0.7943 0.9142 -0.1727 -0.2304 0.0767 96 GLN A C 648 O O . GLN A 92 ? 0.6355 0.7944 0.8766 -0.1759 -0.1985 0.0761 96 GLN A O 649 C CB . GLN A 92 ? 0.6459 0.8282 0.9677 -0.1504 -0.2217 0.0087 96 GLN A CB 650 C CG . GLN A 92 ? 0.9492 1.1440 1.3011 -0.1424 -0.2293 -0.0212 96 GLN A CG 651 C CD . GLN A 92 ? 1.2932 1.4462 1.7001 -0.1219 -0.2865 -0.0474 96 GLN A CD 652 O OE1 . GLN A 92 ? 1.2788 1.4525 1.7554 -0.1017 -0.3088 -0.0930 96 GLN A OE1 653 N NE2 . GLN A 92 ? 1.2055 1.3005 1.5879 -0.1279 -0.3147 -0.0230 96 GLN A NE2 654 N N . VAL A 93 ? 0.6533 0.7272 0.8823 -0.1781 -0.2709 0.0953 97 VAL A N 655 C CA . VAL A 93 ? 0.6485 0.7153 0.8594 -0.1872 -0.2781 0.1124 97 VAL A CA 656 C C . VAL A 93 ? 0.6759 0.7786 0.9305 -0.1706 -0.2641 0.0870 97 VAL A C 657 O O . VAL A 93 ? 0.6556 0.7738 0.8940 -0.1790 -0.2471 0.0978 97 VAL A O 658 C CB . VAL A 93 ? 0.7487 0.7583 0.9324 -0.2037 -0.3312 0.1392 97 VAL A CB 659 C CG1 . VAL A 93 ? 0.7754 0.7602 0.8993 -0.2347 -0.3369 0.1703 97 VAL A CG1 660 C CG2 . VAL A 93 ? 0.7847 0.7565 1.0242 -0.1813 -0.3850 0.1190 97 VAL A CG2 661 N N . GLU A 94 ? 0.6350 0.7576 0.9496 -0.1489 -0.2716 0.0478 98 GLU A N 662 C CA . GLU A 94 ? 0.6145 0.7810 0.9761 -0.1368 -0.2588 0.0156 98 GLU A CA 663 C C . GLU A 94 ? 0.6082 0.8283 0.9586 -0.1496 -0.2062 0.0147 98 GLU A C 664 O O . GLU A 94 ? 0.5869 0.8388 0.9573 -0.1507 -0.1913 0.0020 98 GLU A O 665 C CB . GLU A 94 ? 0.6517 0.8354 1.0897 -0.1123 -0.2866 -0.0379 98 GLU A CB 666 C CG . GLU A 94 ? 0.8559 1.0802 1.3201 -0.1094 -0.2690 -0.0708 98 GLU A CG 667 C CD . GLU A 94 ? 1.3487 1.5270 1.8071 -0.1053 -0.2990 -0.0627 98 GLU A CD 668 O OE1 . GLU A 94 ? 1.4965 1.6064 1.9070 -0.1152 -0.3268 -0.0167 98 GLU A OE1 669 O OE2 . GLU A 94 ? 1.2639 1.4815 1.7647 -0.0968 -0.2935 -0.1045 98 GLU A OE2 670 N N . LYS A 95 ? 0.5472 0.7728 0.8645 -0.1618 -0.1830 0.0307 99 LYS A N 671 C CA . LYS A 95 ? 0.5210 0.7853 0.8229 -0.1785 -0.1446 0.0377 99 LYS A CA 672 C C . LYS A 95 ? 0.5564 0.7953 0.8095 -0.1908 -0.1346 0.0763 99 LYS A C 673 O O . LYS A 95 ? 0.5406 0.7975 0.7795 -0.2040 -0.1137 0.0869 99 LYS A O 674 C CB . LYS A 95 ? 0.5499 0.8586 0.8667 -0.1838 -0.1284 0.0123 99 LYS A CB 675 C CG . LYS A 95 ? 0.7724 1.1388 1.1483 -0.1784 -0.1276 -0.0410 99 LYS A CG 676 C CD . LYS A 95 ? 0.9261 1.3630 1.3100 -0.1972 -0.1007 -0.0688 99 LYS A CD 677 C CE . LYS A 95 ? 1.0989 1.5334 1.4945 -0.1856 -0.1119 -0.0872 99 LYS A CE 678 N NZ . LYS A 95 ? 1.2204 1.6619 1.6890 -0.1570 -0.1448 -0.1421 99 LYS A NZ 679 N N . ALA A 96 ? 0.5134 0.7156 0.7434 -0.1900 -0.1531 0.0940 100 ALA A N 680 C CA . ALA A 96 ? 0.5016 0.6932 0.6953 -0.2017 -0.1465 0.1162 100 ALA A CA 681 C C . ALA A 96 ? 0.5252 0.7331 0.7249 -0.2067 -0.1314 0.1209 100 ALA A C 682 O O . ALA A 96 ? 0.5166 0.7257 0.7028 -0.2127 -0.1253 0.1287 100 ALA A O 683 C CB . ALA A 96 ? 0.5326 0.6986 0.7008 -0.2095 -0.1697 0.1271 100 ALA A CB 684 N N . ASP A 97 ? 0.4641 0.6835 0.6905 -0.2035 -0.1301 0.1126 101 ASP A N 685 C CA . ASP A 97 ? 0.4542 0.6827 0.6951 -0.2082 -0.1230 0.1157 101 ASP A CA 686 C C . ASP A 97 ? 0.5135 0.7507 0.7576 -0.2195 -0.1114 0.1250 101 ASP A C 687 O O . ASP A 97 ? 0.5035 0.7356 0.7591 -0.2256 -0.1145 0.1334 101 ASP A O 688 C CB . ASP A 97 ? 0.4787 0.7158 0.7458 -0.2033 -0.1277 0.1035 101 ASP A CB 689 C CG . ASP A 97 ? 0.6321 0.8895 0.9228 -0.2016 -0.1224 0.0872 101 ASP A CG 690 O OD1 . ASP A 97 ? 0.6365 0.8997 0.9262 -0.1983 -0.1229 0.0774 101 ASP A OD1 691 O OD2 . ASP A 97 ? 0.7232 0.9971 1.0385 -0.2043 -0.1182 0.0780 101 ASP A OD2 692 N N . THR A 98 ? 0.4934 0.7457 0.7298 -0.2257 -0.1023 0.1224 102 THR A N 693 C CA . THR A 98 ? 0.5114 0.7799 0.7402 -0.2481 -0.0926 0.1347 102 THR A CA 694 C C . THR A 98 ? 0.5883 0.8638 0.7923 -0.2547 -0.0868 0.1402 102 THR A C 695 O O . THR A 98 ? 0.6106 0.9051 0.8003 -0.2796 -0.0804 0.1521 102 THR A O 696 C CB . THR A 98 ? 0.6068 0.9152 0.8537 -0.2633 -0.0810 0.1184 102 THR A CB 697 O OG1 . THR A 98 ? 0.6112 0.9493 0.8710 -0.2536 -0.0754 0.0873 102 THR A OG1 698 C CG2 . THR A 98 ? 0.5764 0.8813 0.8497 -0.2582 -0.0858 0.1117 102 THR A CG2 699 N N . THR A 99 ? 0.5424 0.8053 0.7384 -0.2377 -0.0905 0.1323 103 THR A N 700 C CA . THR A 99 ? 0.5497 0.8208 0.7262 -0.2417 -0.0849 0.1331 103 THR A CA 701 C C . THR A 99 ? 0.5916 0.8336 0.7499 -0.2309 -0.0932 0.1411 103 THR A C 702 O O . THR A 99 ? 0.5898 0.8128 0.7492 -0.2216 -0.1028 0.1392 103 THR A O 703 C CB . THR A 99 ? 0.7173 1.0185 0.9115 -0.2365 -0.0800 0.1024 103 THR A CB 704 O OG1 . THR A 99 ? 0.7832 1.0549 0.9878 -0.2154 -0.0975 0.0924 103 THR A OG1 705 C CG2 . THR A 99 ? 0.6968 1.0470 0.9173 -0.2494 -0.0688 0.0794 103 THR A CG2 706 N N . ILE A 100 ? 0.5389 0.7851 0.6780 -0.2367 -0.0889 0.1476 104 ILE A N 707 C CA . ILE A 100 ? 0.5254 0.7549 0.6468 -0.2304 -0.0934 0.1498 104 ILE A CA 708 C C . ILE A 100 ? 0.5669 0.8122 0.6793 -0.2323 -0.0857 0.1409 104 ILE A C 709 O O . ILE A 100 ? 0.5570 0.8302 0.6668 -0.2446 -0.0762 0.1414 104 ILE A O 710 C CB . ILE A 100 ? 0.5684 0.7886 0.6855 -0.2329 -0.1005 0.1620 104 ILE A CB 711 C CG1 . ILE A 100 ? 0.5697 0.7809 0.7073 -0.2272 -0.1108 0.1576 104 ILE A CG1 712 C CG2 . ILE A 100 ? 0.5699 0.7885 0.6696 -0.2303 -0.1006 0.1577 104 ILE A CG2 713 C CD1 . ILE A 100 ? 0.7295 0.9331 0.8858 -0.2257 -0.1278 0.1600 104 ILE A CD1 714 N N . CYS A 101 ? 0.5419 0.7724 0.6492 -0.2248 -0.0920 0.1325 105 CYS A N 715 C CA . CYS A 101 ? 0.5521 0.7922 0.6567 -0.2239 -0.0893 0.1207 105 CYS A CA 716 C C . CYS A 101 ? 0.5922 0.8105 0.6707 -0.2260 -0.0940 0.1297 105 CYS A C 717 O O . CYS A 101 ? 0.5973 0.7923 0.6665 -0.2284 -0.1057 0.1344 105 CYS A O 718 C CB . CYS A 101 ? 0.5725 0.8109 0.7069 -0.2138 -0.1016 0.0971 105 CYS A CB 719 S SG . CYS A 101 ? 0.6378 0.8857 0.7843 -0.2092 -0.1056 0.0736 105 CYS A SG 720 N N . LEU A 102 ? 0.5312 0.7633 0.5957 -0.2300 -0.0851 0.1316 106 LEU A N 721 C CA . LEU A 102 ? 0.5317 0.7543 0.5748 -0.2337 -0.0867 0.1332 106 LEU A CA 722 C C . LEU A 102 ? 0.5999 0.8320 0.6398 -0.2337 -0.0823 0.1233 106 LEU A C 723 O O . LEU A 102 ? 0.6080 0.8679 0.6560 -0.2338 -0.0730 0.1174 106 LEU A O 724 C CB . LEU A 102 ? 0.5271 0.7585 0.5652 -0.2350 -0.0853 0.1388 106 LEU A CB 725 C CG . LEU A 102 ? 0.5932 0.8206 0.6454 -0.2332 -0.0924 0.1408 106 LEU A CG 726 C CD1 . LEU A 102 ? 0.6024 0.8363 0.6662 -0.2298 -0.1006 0.1405 106 LEU A CD1 727 C CD2 . LEU A 102 ? 0.6379 0.8612 0.6827 -0.2404 -0.0963 0.1326 106 LEU A CD2 728 N N . LYS A 103 ? 0.5636 0.7772 0.5903 -0.2386 -0.0898 0.1206 107 LYS A N 729 C CA . LYS A 103 ? 0.5640 0.7806 0.5935 -0.2380 -0.0902 0.1082 107 LYS A CA 730 C C . LYS A 103 ? 0.6362 0.8406 0.6378 -0.2513 -0.0925 0.1122 107 LYS A C 731 O O . LYS A 103 ? 0.6550 0.8386 0.6376 -0.2661 -0.1031 0.1217 107 LYS A O 732 C CB . LYS A 103 ? 0.6052 0.8001 0.6634 -0.2313 -0.1103 0.0962 107 LYS A CB 733 C CG . LYS A 103 ? 0.7719 0.9657 0.8517 -0.2267 -0.1201 0.0747 107 LYS A CG 734 C CD . LYS A 103 ? 0.9176 1.0594 1.0168 -0.2259 -0.1587 0.0735 107 LYS A CD 735 C CE . LYS A 103 ? 0.9921 1.1353 1.1420 -0.2083 -0.1760 0.0525 107 LYS A CE 736 N NZ . LYS A 103 ? 1.0048 1.1769 1.2157 -0.1911 -0.1842 0.0064 107 LYS A NZ 737 N N . TRP A 104 ? 0.5880 0.8112 0.5846 -0.2510 -0.0826 0.1032 108 TRP A N 738 C CA . TRP A 104 ? 0.6005 0.8171 0.5725 -0.2667 -0.0840 0.1023 108 TRP A CA 739 C C . TRP A 104 ? 0.6772 0.8602 0.6544 -0.2734 -0.1036 0.1003 108 TRP A C 740 O O . TRP A 104 ? 0.6587 0.8454 0.6677 -0.2584 -0.1076 0.0849 108 TRP A O 741 C CB . TRP A 104 ? 0.5679 0.8167 0.5350 -0.2632 -0.0690 0.0919 108 TRP A CB 742 C CG . TRP A 104 ? 0.5611 0.8322 0.5253 -0.2603 -0.0631 0.0916 108 TRP A CG 743 C CD1 . TRP A 104 ? 0.5853 0.8701 0.5617 -0.2482 -0.0626 0.0973 108 TRP A CD1 744 C CD2 . TRP A 104 ? 0.5608 0.8466 0.5151 -0.2720 -0.0623 0.0803 108 TRP A CD2 745 N NE1 . TRP A 104 ? 0.5728 0.8694 0.5550 -0.2455 -0.0682 0.0907 108 TRP A NE1 746 C CE2 . TRP A 104 ? 0.5955 0.9007 0.5692 -0.2580 -0.0653 0.0739 108 TRP A CE2 747 C CE3 . TRP A 104 ? 0.5943 0.8837 0.5263 -0.2979 -0.0620 0.0724 108 TRP A CE3 748 C CZ2 . TRP A 104 ? 0.5863 0.9201 0.5718 -0.2610 -0.0682 0.0491 108 TRP A CZ2 749 C CZ3 . TRP A 104 ? 0.6107 0.9394 0.5441 -0.3085 -0.0573 0.0487 108 TRP A CZ3 750 C CH2 . TRP A 104 ? 0.5991 0.9525 0.5658 -0.2862 -0.0603 0.0319 108 TRP A CH2 751 N N . LYS A 105 ? 0.6832 0.8360 0.6324 -0.2992 -0.1199 0.1136 109 LYS A N 752 C CA . LYS A 105 ? 0.7347 0.8403 0.6857 -0.3122 -0.1509 0.1193 109 LYS A CA 753 C C . LYS A 105 ? 0.8218 0.9303 0.7462 -0.3352 -0.1473 0.1175 109 LYS A C 754 O O . LYS A 105 ? 0.8253 0.9639 0.7151 -0.3565 -0.1287 0.1184 109 LYS A O 755 C CB . LYS A 105 ? 0.8131 0.8727 0.7438 -0.3356 -0.1826 0.1448 109 LYS A CB 756 C CG . LYS A 105 ? 1.0139 1.0569 0.9828 -0.3104 -0.1984 0.1428 109 LYS A CG 757 C CD . LYS A 105 ? 1.1781 1.1859 1.2016 -0.2894 -0.2330 0.1256 109 LYS A CD 758 C CE . LYS A 105 ? 1.3301 1.3067 1.3960 -0.2721 -0.2675 0.1210 109 LYS A CE 759 N NZ . LYS A 105 ? 1.4985 1.4074 1.5339 -0.3018 -0.3156 0.1568 109 LYS A NZ 760 N N . ASN A 106 ? 0.7930 0.8763 0.7413 -0.3302 -0.1660 0.1080 110 ASN A N 761 C CA . ASN A 106 ? 0.8141 0.8912 0.7429 -0.3528 -0.1686 0.1061 110 ASN A CA 762 C C . ASN A 106 ? 0.9342 0.9465 0.8300 -0.3958 -0.2114 0.1377 110 ASN A C 763 O O . ASN A 106 ? 0.9646 0.9186 0.8918 -0.3909 -0.2552 0.1422 110 ASN A O 764 C CB . ASN A 106 ? 0.8171 0.9001 0.7980 -0.3243 -0.1722 0.0765 110 ASN A CB 765 C CG . ASN A 106 ? 1.1510 1.2117 1.1299 -0.3427 -0.1878 0.0713 110 ASN A CG 766 O OD1 . ASN A 106 ? 1.1821 1.2157 1.2105 -0.3284 -0.2164 0.0529 110 ASN A OD1 767 N ND2 . ASN A 106 ? 0.9802 1.0587 0.9102 -0.3734 -0.1697 0.0801 110 ASN A ND2 768 N N . ILE A 107 ? 0.9177 0.9435 0.7533 -0.4403 -0.2031 0.1575 111 ILE A N 769 C CA . ILE A 107 ? 0.9970 0.9705 0.7838 -0.4963 -0.2434 0.1948 111 ILE A CA 770 C C . ILE A 107 ? 1.1131 1.0478 0.8722 -0.5400 -0.2704 0.2095 111 ILE A C 771 O O . ILE A 107 ? 1.1882 1.0576 0.9134 -0.5863 -0.3201 0.2475 111 ILE A O 772 C CB . ILE A 107 ? 1.0429 1.0528 0.7781 -0.5335 -0.2292 0.2085 111 ILE A CB 773 C CG1 . ILE A 107 ? 1.0235 1.1182 0.7291 -0.5564 -0.1828 0.1828 111 ILE A CG1 774 C CG2 . ILE A 107 ? 1.0039 1.0220 0.7722 -0.4928 -0.2224 0.2036 111 ILE A CG2 775 C CD1 . ILE A 107 ? 1.1869 1.3179 0.8272 -0.6259 -0.1817 0.1946 111 ILE A CD1 776 N N . GLU A 108 ? 1.0344 1.0055 0.8066 -0.5281 -0.2423 0.1820 112 GLU A N 777 C CA . GLU A 108 ? 1.0853 1.0258 0.8387 -0.5650 -0.2630 0.1897 112 GLU A CA 778 C C . GLU A 108 ? 1.0742 1.0390 0.8839 -0.5169 -0.2426 0.1508 112 GLU A C 779 O O . GLU A 108 ? 0.9999 1.0291 0.8332 -0.4760 -0.1989 0.1211 112 GLU A O 780 C CB . GLU A 108 ? 1.1310 1.1217 0.8116 -0.6301 -0.2386 0.1955 112 GLU A CB 781 C CG . GLU A 108 ? 1.4166 1.3517 1.0516 -0.6980 -0.2798 0.2274 112 GLU A CG 782 C CD . GLU A 108 ? 1.8237 1.8251 1.3962 -0.7623 -0.2489 0.2192 112 GLU A CD 783 O OE1 . GLU A 108 ? 1.7829 1.8713 1.3302 -0.7758 -0.2061 0.1974 112 GLU A OE1 784 O OE2 . GLU A 108 ? 1.8257 1.7963 1.3807 -0.7995 -0.2687 0.2289 112 GLU A OE2 785 N N . THR A 109 ? 1.0664 0.9793 0.8981 -0.5243 -0.2780 0.1514 113 THR A N 786 C CA . THR A 109 ? 1.0178 0.9584 0.9046 -0.4836 -0.2611 0.1107 113 THR A CA 787 C C . THR A 109 ? 1.0174 1.0316 0.8722 -0.4959 -0.2107 0.0909 113 THR A C 788 O O . THR A 109 ? 1.0389 1.0669 0.8322 -0.5486 -0.2022 0.1075 113 THR A O 789 C CB . THR A 109 ? 1.1660 1.0286 1.0988 -0.4854 -0.3204 0.1105 113 THR A CB 790 O OG1 . THR A 109 ? 1.1412 1.0436 1.1296 -0.4482 -0.3008 0.0643 113 THR A OG1 791 C CG2 . THR A 109 ? 1.2204 1.0153 1.0947 -0.5578 -0.3636 0.1542 113 THR A CG2 792 N N . PHE A 110 ? 0.9003 0.9680 0.7979 -0.4500 -0.1789 0.0524 114 PHE A N 793 C CA . PHE A 110 ? 0.8557 0.9901 0.7374 -0.4518 -0.1383 0.0282 114 PHE A CA 794 C C . PHE A 110 ? 0.9004 1.0498 0.8368 -0.4171 -0.1360 -0.0057 114 PHE A C 795 O O . PHE A 110 ? 0.8935 1.0287 0.8838 -0.3832 -0.1525 -0.0192 114 PHE A O 796 C CB . PHE A 110 ? 0.8082 1.0104 0.6757 -0.4332 -0.0977 0.0180 114 PHE A CB 797 C CG . PHE A 110 ? 0.7711 0.9855 0.6758 -0.3859 -0.0911 0.0126 114 PHE A CG 798 C CD1 . PHE A 110 ? 0.7552 1.0081 0.6977 -0.3490 -0.0755 -0.0137 114 PHE A CD1 799 C CD2 . PHE A 110 ? 0.7981 0.9921 0.6962 -0.3844 -0.1001 0.0335 114 PHE A CD2 800 C CE1 . PHE A 110 ? 0.7281 0.9999 0.6975 -0.3170 -0.0692 -0.0175 114 PHE A CE1 801 C CE2 . PHE A 110 ? 0.7941 1.0034 0.7240 -0.3465 -0.0929 0.0280 114 PHE A CE2 802 C CZ . PHE A 110 ? 0.7264 0.9754 0.6896 -0.3159 -0.0774 0.0034 114 PHE A CZ 803 N N . THR A 111 ? 0.8513 1.0385 0.7776 -0.4270 -0.1151 -0.0255 115 THR A N 804 C CA . THR A 111 ? 0.8363 1.0460 0.8111 -0.4002 -0.1116 -0.0607 115 THR A CA 805 C C . THR A 111 ? 0.8493 1.1348 0.8462 -0.3582 -0.0760 -0.0887 115 THR A C 806 O O . THR A 111 ? 0.8283 1.1388 0.8720 -0.3341 -0.0755 -0.1200 115 THR A O 807 C CB . THR A 111 ? 0.9418 1.1443 0.8991 -0.4351 -0.1155 -0.0666 115 THR A CB 808 O OG1 . THR A 111 ? 0.8963 1.1550 0.8058 -0.4545 -0.0798 -0.0699 115 THR A OG1 809 C CG2 . THR A 111 ? 1.0093 1.1243 0.9491 -0.4821 -0.1640 -0.0339 115 THR A CG2 810 N N . CYS A 112 ? 0.8037 1.1268 0.7698 -0.3522 -0.0507 -0.0790 116 CYS A N 811 C CA . CYS A 112 ? 0.7702 1.1545 0.7481 -0.3204 -0.0265 -0.0942 116 CYS A CA 812 C C . CYS A 112 ? 0.8191 1.2075 0.8405 -0.2953 -0.0345 -0.1046 116 CYS A C 813 O O . CYS A 112 ? 0.8259 1.1685 0.8643 -0.2957 -0.0569 -0.0940 116 CYS A O 814 C CB . CYS A 112 ? 0.7633 1.1653 0.7113 -0.3186 -0.0143 -0.0773 116 CYS A CB 815 S SG . CYS A 112 ? 0.8198 1.2525 0.7345 -0.3418 -0.0006 -0.0876 116 CYS A SG 816 N N . ASP A 113 ? 0.7699 1.2197 0.8100 -0.2774 -0.0177 -0.1287 117 ASP A N 817 C CA . ASP A 113 ? 0.7632 1.2437 0.8439 -0.2606 -0.0187 -0.1485 117 ASP A CA 818 C C . ASP A 113 ? 0.7916 1.2722 0.8509 -0.2568 -0.0140 -0.1206 117 ASP A C 819 O O . ASP A 113 ? 0.7765 1.2709 0.7975 -0.2595 -0.0027 -0.0989 117 ASP A O 820 C CB . ASP A 113 ? 0.7738 1.3343 0.8698 -0.2545 0.0003 -0.1822 117 ASP A CB 821 C CG . ASP A 113 ? 0.9619 1.5756 1.1125 -0.2449 0.0005 -0.2228 117 ASP A CG 822 O OD1 . ASP A 113 ? 0.9745 1.5846 1.1377 -0.2407 -0.0045 -0.2178 117 ASP A OD1 823 O OD2 . ASP A 113 ? 1.0464 1.7152 1.2301 -0.2428 0.0072 -0.2654 117 ASP A OD2 824 N N . THR A 114 ? 0.7450 1.2061 0.8345 -0.2499 -0.0278 -0.1234 118 THR A N 825 C CA . THR A 114 ? 0.7301 1.1884 0.8043 -0.2475 -0.0249 -0.0991 118 THR A CA 826 C C . THR A 114 ? 0.7595 1.2890 0.8252 -0.2481 -0.0050 -0.1035 118 THR A C 827 O O . THR A 114 ? 0.7508 1.2763 0.7894 -0.2514 -0.0022 -0.0742 118 THR A O 828 C CB . THR A 114 ? 0.8378 1.2522 0.9472 -0.2411 -0.0486 -0.1017 118 THR A CB 829 O OG1 . THR A 114 ? 0.8219 1.2591 0.9956 -0.2300 -0.0609 -0.1486 118 THR A OG1 830 C CG2 . THR A 114 ? 0.8605 1.1959 0.9482 -0.2533 -0.0714 -0.0725 118 THR A CG2 831 N N . GLN A 115 ? 0.6993 1.2957 0.7852 -0.2499 0.0067 -0.1387 119 GLN A N 832 C CA . GLN A 115 ? 0.6852 1.3584 0.7534 -0.2632 0.0236 -0.1410 119 GLN A CA 833 C C . GLN A 115 ? 0.7171 1.3823 0.7269 -0.2725 0.0247 -0.0981 119 GLN A C 834 O O . GLN A 115 ? 0.7243 1.4284 0.7066 -0.2895 0.0277 -0.0803 119 GLN A O 835 C CB . GLN A 115 ? 0.7034 1.4611 0.8060 -0.2686 0.0359 -0.1936 119 GLN A CB 836 C CG . GLN A 115 ? 0.9422 1.7194 1.0249 -0.2717 0.0424 -0.1982 119 GLN A CG 837 C CD . GLN A 115 ? 1.1907 2.0701 1.2979 -0.2837 0.0579 -0.2474 119 GLN A CD 838 O OE1 . GLN A 115 ? 1.1471 2.0562 1.3196 -0.2738 0.0566 -0.3031 119 GLN A OE1 839 N NE2 . GLN A 115 ? 1.0807 2.0169 1.1388 -0.3068 0.0684 -0.2299 119 GLN A NE2 840 N N . ASN A 116 ? 0.6551 1.2717 0.6491 -0.2645 0.0178 -0.0839 120 ASN A N 841 C CA . ASN A 116 ? 0.6545 1.2618 0.6108 -0.2668 0.0112 -0.0549 120 ASN A CA 842 C C . ASN A 116 ? 0.6922 1.2430 0.6384 -0.2610 -0.0012 -0.0258 120 ASN A C 843 O O . ASN A 116 ? 0.6918 1.2308 0.6216 -0.2584 -0.0132 -0.0092 120 ASN A O 844 C CB . ASN A 116 ? 0.6871 1.3018 0.6398 -0.2634 0.0133 -0.0712 120 ASN A CB 845 C CG . ASN A 116 ? 1.0809 1.7386 1.0575 -0.2654 0.0256 -0.1093 120 ASN A CG 846 O OD1 . ASN A 116 ? 1.0546 1.6859 1.0563 -0.2609 0.0255 -0.1293 120 ASN A OD1 847 N ND2 . ASN A 116 ? 0.9865 1.7119 0.9568 -0.2757 0.0332 -0.1213 120 ASN A ND2 848 N N . ILE A 117 ? 0.6355 1.1560 0.5981 -0.2583 -0.0019 -0.0241 121 ILE A N 849 C CA . ILE A 117 ? 0.6256 1.1003 0.5816 -0.2551 -0.0116 -0.0009 121 ILE A CA 850 C C . ILE A 117 ? 0.6827 1.1641 0.6354 -0.2586 -0.0151 0.0195 121 ILE A C 851 O O . ILE A 117 ? 0.6848 1.1881 0.6539 -0.2624 -0.0084 0.0083 121 ILE A O 852 C CB . ILE A 117 ? 0.6647 1.0961 0.6331 -0.2554 -0.0154 -0.0072 121 ILE A CB 853 C CG1 . ILE A 117 ? 0.6737 1.0990 0.6350 -0.2623 -0.0137 -0.0214 121 ILE A CG1 854 C CG2 . ILE A 117 ? 0.6838 1.0791 0.6445 -0.2559 -0.0237 0.0145 121 ILE A CG2 855 C CD1 . ILE A 117 ? 0.7754 1.1567 0.7307 -0.2763 -0.0226 -0.0170 121 ILE A CD1 856 N N . THR A 118 ? 0.6344 1.1009 0.5713 -0.2586 -0.0285 0.0449 122 THR A N 857 C CA . THR A 118 ? 0.6347 1.0991 0.5646 -0.2666 -0.0370 0.0704 122 THR A CA 858 C C . THR A 118 ? 0.6722 1.0909 0.6097 -0.2571 -0.0503 0.0854 122 THR A C 859 O O . THR A 118 ? 0.6634 1.0644 0.6063 -0.2474 -0.0598 0.0799 122 THR A O 860 C CB . THR A 118 ? 0.7307 1.2273 0.6355 -0.2849 -0.0475 0.0896 122 THR A CB 861 O OG1 . THR A 118 ? 0.6936 1.1736 0.5926 -0.2768 -0.0686 0.0970 122 THR A OG1 862 C CG2 . THR A 118 ? 0.7116 1.2715 0.6108 -0.3011 -0.0285 0.0684 122 THR A CG2 863 N N . TYR A 119 ? 0.6240 1.0330 0.5669 -0.2608 -0.0494 0.0967 123 TYR A N 864 C CA . TYR A 119 ? 0.6186 0.9907 0.5718 -0.2531 -0.0598 0.1074 123 TYR A CA 865 C C . TYR A 119 ? 0.7111 1.0764 0.6587 -0.2619 -0.0777 0.1359 123 TYR A C 866 O O . TYR A 119 ? 0.7223 1.1126 0.6568 -0.2804 -0.0728 0.1473 123 TYR A O 867 C CB . TYR A 119 ? 0.6171 0.9772 0.5833 -0.2507 -0.0491 0.0984 123 TYR A CB 868 C CG . TYR A 119 ? 0.6304 0.9868 0.6021 -0.2480 -0.0413 0.0765 123 TYR A CG 869 C CD1 . TYR A 119 ? 0.6550 1.0387 0.6377 -0.2497 -0.0327 0.0571 123 TYR A CD1 870 C CD2 . TYR A 119 ? 0.6417 0.9709 0.6093 -0.2487 -0.0454 0.0731 123 TYR A CD2 871 C CE1 . TYR A 119 ? 0.6650 1.0353 0.6596 -0.2474 -0.0342 0.0379 123 TYR A CE1 872 C CE2 . TYR A 119 ? 0.6623 0.9791 0.6295 -0.2545 -0.0454 0.0604 123 TYR A CE2 873 C CZ . TYR A 119 ? 0.7471 1.0774 0.7306 -0.2515 -0.0428 0.0444 123 TYR A CZ 874 O OH . TYR A 119 ? 0.7640 1.0725 0.7536 -0.2572 -0.0511 0.0329 123 TYR A OH 875 N N . ARG A 120 ? 0.6877 1.0243 0.6482 -0.2524 -0.1009 0.1439 124 ARG A N 876 C CA . ARG A 120 ? 0.7189 1.0354 0.6800 -0.2611 -0.1285 0.1736 124 ARG A CA 877 C C . ARG A 120 ? 0.7670 1.0550 0.7560 -0.2487 -0.1372 0.1706 124 ARG A C 878 O O . ARG A 120 ? 0.7476 1.0339 0.7574 -0.2328 -0.1333 0.1441 124 ARG A O 879 C CB . ARG A 120 ? 0.7662 1.0712 0.7278 -0.2608 -0.1646 0.1857 124 ARG A CB 880 C CG . ARG A 120 ? 1.0018 1.3386 0.9327 -0.2756 -0.1591 0.1897 124 ARG A CG 881 C CD . ARG A 120 ? 1.2943 1.6121 1.2290 -0.2735 -0.2040 0.2029 124 ARG A CD 882 N NE . ARG A 120 ? 1.5761 1.8608 1.4989 -0.2957 -0.2470 0.2481 124 ARG A NE 883 C CZ . ARG A 120 ? 1.8670 2.1023 1.8266 -0.2818 -0.2947 0.2563 124 ARG A CZ 884 N NH1 . ARG A 120 ? 1.7047 1.9316 1.7187 -0.2449 -0.3012 0.2142 124 ARG A NH1 885 N NH2 . ARG A 120 ? 1.8026 2.0007 1.7475 -0.3083 -0.3389 0.3034 124 ARG A NH2 886 N N . PHE A 121 ? 0.7357 1.0087 0.7237 -0.2609 -0.1481 0.1957 125 PHE A N 887 C CA . PHE A 121 ? 0.7217 0.9702 0.7386 -0.2502 -0.1574 0.1928 125 PHE A CA 888 C C . PHE A 121 ? 0.8097 1.0266 0.8366 -0.2597 -0.1971 0.2223 125 PHE A C 889 O O . PHE A 121 ? 0.8358 1.0533 0.8319 -0.2870 -0.2084 0.2552 125 PHE A O 890 C CB . PHE A 121 ? 0.7241 0.9823 0.7348 -0.2563 -0.1300 0.1917 125 PHE A CB 891 C CG . PHE A 121 ? 0.7129 0.9856 0.7218 -0.2471 -0.1028 0.1660 125 PHE A CG 892 C CD1 . PHE A 121 ? 0.7590 1.0566 0.7514 -0.2534 -0.0845 0.1578 125 PHE A CD1 893 C CD2 . PHE A 121 ? 0.7196 0.9813 0.7438 -0.2365 -0.0998 0.1502 125 PHE A CD2 894 C CE1 . PHE A 121 ? 0.7566 1.0551 0.7521 -0.2465 -0.0702 0.1373 125 PHE A CE1 895 C CE2 . PHE A 121 ? 0.7483 1.0132 0.7641 -0.2362 -0.0844 0.1355 125 PHE A CE2 896 C CZ . PHE A 121 ? 0.7317 1.0086 0.7354 -0.2400 -0.0728 0.1308 125 PHE A CZ 897 N N . GLN A 122 ? 0.7790 0.9714 0.8494 -0.2420 -0.2202 0.2100 126 GLN A N 898 C CA . GLN A 122 ? 0.8297 0.9810 0.9239 -0.2475 -0.2666 0.2345 126 GLN A CA 899 C C . GLN A 122 ? 0.8779 1.0234 1.0061 -0.2360 -0.2604 0.2183 126 GLN A C 900 O O . GLN A 122 ? 0.8442 1.0043 1.0107 -0.2124 -0.2556 0.1771 126 GLN A O 901 C CB . GLN A 122 ? 0.8815 1.0069 1.0152 -0.2312 -0.3192 0.2258 126 GLN A CB 902 C CG . GLN A 122 ? 1.1685 1.3079 1.2740 -0.2356 -0.3217 0.2298 126 GLN A CG 903 C CD . GLN A 122 ? 1.5115 1.6242 1.6631 -0.2170 -0.3804 0.2180 126 GLN A CD 904 O OE1 . GLN A 122 ? 1.4682 1.5793 1.6881 -0.1871 -0.4025 0.1741 126 GLN A OE1 905 N NE2 . GLN A 122 ? 1.4510 1.5499 1.5700 -0.2348 -0.4078 0.2506 126 GLN A NE2 906 N N . CYS A 123 ? 0.8679 1.0034 0.9780 -0.2573 -0.2556 0.2472 127 CYS A N 907 C CA . CYS A 123 ? 0.8618 0.9935 1.0026 -0.2470 -0.2493 0.2323 127 CYS A CA 908 C C . CYS A 123 ? 0.9810 1.0716 1.1710 -0.2420 -0.2980 0.2382 127 CYS A C 909 O O . CYS A 123 ? 0.9720 1.0633 1.2173 -0.2145 -0.3177 0.1998 127 CYS A O 910 C CB . CYS A 123 ? 0.8423 0.9989 0.9534 -0.2598 -0.2073 0.2364 127 CYS A CB 911 S SG . CYS A 123 ? 0.8387 1.0326 0.9339 -0.2448 -0.1632 0.2027 127 CYS A SG 912 N N . GLY A 124 ? 1.0003 1.0588 1.1747 -0.2704 -0.3229 0.2816 128 GLY A N 913 C CA . GLY A 124 ? 1.0524 1.0578 1.2767 -0.2680 -0.3839 0.2929 128 GLY A CA 914 C C . GLY A 124 ? 1.1632 1.1396 1.3809 -0.2741 -0.4293 0.3139 128 GLY A C 915 O O . GLY A 124 ? 1.1396 1.1278 1.3898 -0.2439 -0.4375 0.2770 128 GLY A O 916 N N . ASN A 125 ? 1.1946 1.1453 1.3579 -0.3203 -0.4513 0.3734 129 ASN A N 917 C CA . ASN A 125 ? 1.2585 1.1834 1.3933 -0.3405 -0.4940 0.4080 129 ASN A CA 918 C C . ASN A 125 ? 1.3205 1.2987 1.3698 -0.3787 -0.4451 0.4311 129 ASN A C 919 O O . ASN A 125 ? 1.3684 1.3374 1.3796 -0.4047 -0.4729 0.4634 129 ASN A O 920 C CB . ASN A 125 ? 1.3503 1.1972 1.4921 -0.3729 -0.5759 0.4628 129 ASN A CB 921 C CG . ASN A 125 ? 1.6205 1.4112 1.8631 -0.3305 -0.6411 0.4327 129 ASN A CG 922 O OD1 . ASN A 125 ? 1.5146 1.3232 1.8221 -0.2793 -0.6433 0.3725 129 ASN A OD1 923 N ND2 . ASN A 125 ? 1.5657 1.2914 1.8277 -0.3541 -0.6992 0.4704 129 ASN A ND2 924 N N . MET A 126 ? 1.2269 1.2634 1.2527 -0.3812 -0.3763 0.4099 130 MET A N 925 C CA . MET A 126 ? 1.2115 1.3114 1.1751 -0.4122 -0.3272 0.4148 130 MET A CA 926 C C . MET A 126 ? 1.1735 1.3046 1.1409 -0.3797 -0.3004 0.3780 130 MET A C 927 O O . MET A 126 ? 1.1148 1.2493 1.1232 -0.3362 -0.2816 0.3356 130 MET A O 928 C CB . MET A 126 ? 1.2071 1.3531 1.1636 -0.4206 -0.2749 0.3967 130 MET A CB 929 C CG . MET A 126 ? 1.3202 1.4553 1.2575 -0.4671 -0.2911 0.4339 130 MET A CG 930 S SD . MET A 126 ? 1.3931 1.6228 1.2695 -0.5245 -0.2391 0.4333 130 MET A SD 931 C CE . MET A 126 ? 1.4457 1.6738 1.2548 -0.5875 -0.2787 0.4895 130 MET A CE 932 N N . ILE A 127 ? 1.1274 1.2850 1.0490 -0.4062 -0.2989 0.3947 131 ILE A N 933 C CA . ILE A 127 ? 1.0750 1.2646 0.9956 -0.3817 -0.2743 0.3628 131 ILE A CA 934 C C . ILE A 127 ? 1.0666 1.3286 0.9526 -0.4010 -0.2187 0.3453 131 ILE A C 935 O O . ILE A 127 ? 1.0997 1.3990 0.9418 -0.4498 -0.2131 0.3689 131 ILE A O 936 C CB . ILE A 127 ? 1.1645 1.3259 1.0782 -0.3842 -0.3227 0.3828 131 ILE A CB 937 C CG1 . ILE A 127 ? 1.1940 1.2874 1.1691 -0.3521 -0.3812 0.3800 131 ILE A CG1 938 C CG2 . ILE A 127 ? 1.1242 1.3262 1.0342 -0.3620 -0.2927 0.3476 131 ILE A CG2 939 C CD1 . ILE A 127 ? 1.3835 1.4286 1.3587 -0.3637 -0.4521 0.4134 131 ILE A CD1 940 N N . PHE A 128 ? 0.9362 1.2210 0.8459 -0.3657 -0.1811 0.3008 132 PHE A N 941 C CA . PHE A 128 ? 0.8907 1.2377 0.7888 -0.3724 -0.1354 0.2720 132 PHE A CA 942 C C . PHE A 128 ? 0.8967 1.2630 0.7940 -0.3545 -0.1230 0.2475 132 PHE A C 943 O O . PHE A 128 ? 0.8799 1.2127 0.7967 -0.3252 -0.1367 0.2387 132 PHE A O 944 C CB . PHE A 128 ? 0.8659 1.2127 0.7968 -0.3482 -0.1103 0.2429 132 PHE A CB 945 C CG . PHE A 128 ? 0.8983 1.2292 0.8364 -0.3612 -0.1184 0.2601 132 PHE A CG 946 C CD1 . PHE A 128 ? 0.9618 1.3390 0.8797 -0.4006 -0.1049 0.2665 132 PHE A CD1 947 C CD2 . PHE A 128 ? 0.9157 1.1947 0.8833 -0.3370 -0.1384 0.2643 132 PHE A CD2 948 C CE1 . PHE A 128 ? 0.9908 1.3547 0.9149 -0.4155 -0.1119 0.2817 132 PHE A CE1 949 C CE2 . PHE A 128 ? 0.9663 1.2306 0.9436 -0.3485 -0.1462 0.2785 132 PHE A CE2 950 C CZ . PHE A 128 ? 0.9684 1.2716 0.9226 -0.3873 -0.1331 0.2892 132 PHE A CZ 951 N N . ASP A 129 ? 0.8361 1.2645 0.7160 -0.3735 -0.0959 0.2297 133 ASP A N 952 C CA . ASP A 129 ? 0.8081 1.2613 0.6908 -0.3584 -0.0807 0.2015 133 ASP A CA 953 C C . ASP A 129 ? 0.8082 1.3065 0.7153 -0.3512 -0.0466 0.1579 133 ASP A C 954 O O . ASP A 129 ? 0.8196 1.3851 0.7195 -0.3795 -0.0295 0.1426 133 ASP A O 955 C CB . ASP A 129 ? 0.8727 1.3620 0.7166 -0.3899 -0.0903 0.2182 133 ASP A CB 956 C CG . ASP A 129 ? 1.0793 1.5320 0.8925 -0.4158 -0.1343 0.2702 133 ASP A CG 957 O OD1 . ASP A 129 ? 1.0931 1.4916 0.9206 -0.3908 -0.1664 0.2806 133 ASP A OD1 958 O OD2 . ASP A 129 ? 1.2067 1.6892 0.9829 -0.4647 -0.1401 0.2981 133 ASP A OD2 959 N N . ASN A 130 ? 0.7090 1.1727 0.6480 -0.3170 -0.0413 0.1363 134 ASN A N 960 C CA . ASN A 130 ? 0.6752 1.1579 0.6480 -0.3031 -0.0240 0.0968 134 ASN A CA 961 C C . ASN A 130 ? 0.6942 1.1181 0.6843 -0.2746 -0.0319 0.0934 134 ASN A C 962 O O . ASN A 130 ? 0.6868 1.0695 0.6693 -0.2684 -0.0443 0.1158 134 ASN A O 963 C CB . ASN A 130 ? 0.7012 1.2157 0.6907 -0.3160 -0.0157 0.0858 134 ASN A CB 964 C CG . ASN A 130 ? 1.0410 1.5983 1.0755 -0.3065 -0.0033 0.0337 134 ASN A CG 965 O OD1 . ASN A 130 ? 1.0218 1.6325 1.0673 -0.3125 0.0072 0.0020 134 ASN A OD1 966 N ND2 . ASN A 130 ? 0.9272 1.4639 0.9954 -0.2906 -0.0085 0.0197 134 ASN A ND2 967 N N . LYS A 131 ? 0.6358 1.0587 0.6518 -0.2615 -0.0283 0.0633 135 LYS A N 968 C CA . LYS A 131 ? 0.6232 0.9932 0.6486 -0.2462 -0.0396 0.0620 135 LYS A CA 969 C C . LYS A 131 ? 0.6802 1.0195 0.7131 -0.2421 -0.0483 0.0750 135 LYS A C 970 O O . LYS A 131 ? 0.6823 0.9817 0.7048 -0.2391 -0.0577 0.0880 135 LYS A O 971 C CB . LYS A 131 ? 0.6468 1.0189 0.7038 -0.2383 -0.0443 0.0295 135 LYS A CB 972 C CG . LYS A 131 ? 0.7272 1.0419 0.7799 -0.2348 -0.0617 0.0360 135 LYS A CG 973 C CD . LYS A 131 ? 0.8334 1.1419 0.9173 -0.2300 -0.0746 0.0077 135 LYS A CD 974 C CE . LYS A 131 ? 1.0507 1.2997 1.1153 -0.2395 -0.0949 0.0241 135 LYS A CE 975 N NZ . LYS A 131 ? 1.2373 1.4577 1.3398 -0.2358 -0.1229 0.0025 135 LYS A NZ 976 N N . GLU A 132 ? 0.6358 1.0028 0.6867 -0.2457 -0.0438 0.0672 136 GLU A N 977 C CA . GLU A 132 ? 0.6326 0.9783 0.6936 -0.2423 -0.0506 0.0765 136 GLU A CA 978 C C . GLU A 132 ? 0.6861 1.0623 0.7399 -0.2580 -0.0424 0.0889 136 GLU A C 979 O O . GLU A 132 ? 0.6934 1.1233 0.7434 -0.2760 -0.0305 0.0792 136 GLU A O 980 C CB . GLU A 132 ? 0.6553 0.9875 0.7551 -0.2291 -0.0635 0.0512 136 GLU A CB 981 C CG . GLU A 132 ? 0.7996 1.1873 0.9438 -0.2278 -0.0586 0.0091 136 GLU A CG 982 C CD . GLU A 132 ? 1.0756 1.4403 1.2682 -0.2102 -0.0821 -0.0153 136 GLU A CD 983 O OE1 . GLU A 132 ? 0.7958 1.1401 0.9878 -0.2084 -0.0877 -0.0009 136 GLU A OE1 984 O OE2 . GLU A 132 ? 1.0878 1.4506 1.3227 -0.1973 -0.1001 -0.0492 136 GLU A OE2 985 N N . ILE A 133 ? 0.6404 0.9859 0.6903 -0.2564 -0.0502 0.1105 137 ILE A N 986 C CA . ILE A 133 ? 0.6476 1.0082 0.6904 -0.2741 -0.0489 0.1285 137 ILE A CA 987 C C . ILE A 133 ? 0.6984 1.0450 0.7637 -0.2671 -0.0524 0.1250 137 ILE A C 988 O O . ILE A 133 ? 0.6790 0.9903 0.7558 -0.2486 -0.0614 0.1207 137 ILE A O 989 C CB . ILE A 133 ? 0.6971 1.0324 0.7150 -0.2817 -0.0624 0.1619 137 ILE A CB 990 C CG1 . ILE A 133 ? 0.6871 0.9754 0.7147 -0.2615 -0.0763 0.1674 137 ILE A CG1 991 C CG2 . ILE A 133 ? 0.7160 1.0706 0.7112 -0.2914 -0.0616 0.1655 137 ILE A CG2 992 C CD1 . ILE A 133 ? 0.7853 1.0498 0.8142 -0.2657 -0.0980 0.1910 137 ILE A CD1 993 N N . LYS A 134 ? 0.6778 1.0552 0.7457 -0.2870 -0.0465 0.1277 138 LYS A N 994 C CA . LYS A 134 ? 0.6732 1.0448 0.7651 -0.2818 -0.0484 0.1210 138 LYS A CA 995 C C . LYS A 134 ? 0.7261 1.0987 0.8025 -0.3069 -0.0515 0.1496 138 LYS A C 996 O O . LYS A 134 ? 0.7429 1.1527 0.7970 -0.3400 -0.0457 0.1600 138 LYS A O 997 C CB . LYS A 134 ? 0.7137 1.1355 0.8430 -0.2794 -0.0387 0.0760 138 LYS A CB 998 C CG . LYS A 134 ? 1.0764 1.4816 1.2331 -0.2519 -0.0489 0.0474 138 LYS A CG 999 C CD . LYS A 134 ? 1.2725 1.7280 1.4837 -0.2446 -0.0490 -0.0071 138 LYS A CD 1000 C CE . LYS A 134 ? 1.4766 1.9011 1.7190 -0.2183 -0.0711 -0.0307 138 LYS A CE 1001 N NZ . LYS A 134 ? 1.6258 2.0973 1.9395 -0.2054 -0.0811 -0.0930 138 LYS A NZ 1002 N N . LEU A 135 ? 0.6791 1.0103 0.7653 -0.2955 -0.0639 0.1641 139 LEU A N 1003 C CA . LEU A 135 ? 0.7035 1.0241 0.7846 -0.3166 -0.0739 0.1905 139 LEU A CA 1004 C C . LEU A 135 ? 0.7352 1.0702 0.8430 -0.3139 -0.0665 0.1726 139 LEU A C 1005 O O . LEU A 135 ? 0.6993 1.0211 0.8300 -0.2859 -0.0668 0.1518 139 LEU A O 1006 C CB . LEU A 135 ? 0.7096 0.9755 0.7939 -0.3030 -0.0984 0.2131 139 LEU A CB 1007 C CG . LEU A 135 ? 0.7930 1.0439 0.8566 -0.3101 -0.1144 0.2332 139 LEU A CG 1008 C CD1 . LEU A 135 ? 0.7672 1.0087 0.8345 -0.2825 -0.1116 0.2149 139 LEU A CD1 1009 C CD2 . LEU A 135 ? 0.8634 1.0719 0.9381 -0.3148 -0.1483 0.2588 139 LEU A CD2 1010 N N . GLU A 136 ? 0.7158 1.0800 0.8180 -0.3474 -0.0622 0.1809 140 GLU A N 1011 C CA . GLU A 136 ? 0.7059 1.0954 0.8353 -0.3496 -0.0531 0.1593 140 GLU A CA 1012 C C . GLU A 136 ? 0.7792 1.1460 0.9026 -0.3738 -0.0662 0.1908 140 GLU A C 1013 O O . GLU A 136 ? 0.8012 1.1410 0.8976 -0.3974 -0.0844 0.2290 140 GLU A O 1014 C CB . GLU A 136 ? 0.7291 1.2027 0.8655 -0.3740 -0.0296 0.1220 140 GLU A CB 1015 C CG . GLU A 136 ? 0.8447 1.3403 1.0088 -0.3436 -0.0231 0.0786 140 GLU A CG 1016 C CD . GLU A 136 ? 1.1039 1.6917 1.2802 -0.3674 -0.0026 0.0343 140 GLU A CD 1017 O OE1 . GLU A 136 ? 0.9131 1.5706 1.0969 -0.4021 0.0130 0.0129 140 GLU A OE1 1018 O OE2 . GLU A 136 ? 1.0757 1.6730 1.2593 -0.3520 -0.0018 0.0144 140 GLU A OE2 1019 N N . ASN A 137 ? 0.7350 1.1101 0.8868 -0.3688 -0.0620 0.1744 141 ASN A N 1020 C CA . ASN A 137 ? 0.7585 1.1147 0.9131 -0.3915 -0.0741 0.1981 141 ASN A CA 1021 C C . ASN A 137 ? 0.7927 1.0769 0.9575 -0.3701 -0.1036 0.2247 141 ASN A C 1022 O O . ASN A 137 ? 0.8230 1.0777 0.9874 -0.3933 -0.1258 0.2540 141 ASN A O 1023 C CB . ASN A 137 ? 0.8085 1.1976 0.9256 -0.4549 -0.0735 0.2249 141 ASN A CB 1024 C CG . ASN A 137 ? 1.0686 1.5526 1.1780 -0.4902 -0.0421 0.1909 141 ASN A CG 1025 O OD1 . ASN A 137 ? 0.9615 1.4935 1.1086 -0.4676 -0.0217 0.1388 141 ASN A OD1 1026 N ND2 . ASN A 137 ? 1.0141 1.5320 1.0767 -0.5518 -0.0420 0.2177 141 ASN A ND2 1027 N N . LEU A 138 ? 0.6946 0.9548 0.8722 -0.3295 -0.1069 0.2110 142 LEU A N 1028 C CA . LEU A 138 ? 0.6827 0.8954 0.8805 -0.3081 -0.1315 0.2192 142 LEU A CA 1029 C C . LEU A 138 ? 0.7120 0.9189 0.9444 -0.2972 -0.1349 0.2064 142 LEU A C 1030 O O . LEU A 138 ? 0.6866 0.9213 0.9266 -0.2919 -0.1167 0.1856 142 LEU A O 1031 C CB . LEU A 138 ? 0.6560 0.8628 0.8522 -0.2777 -0.1286 0.2025 142 LEU A CB 1032 C CG . LEU A 138 ? 0.7282 0.9365 0.8949 -0.2842 -0.1283 0.2133 142 LEU A CG 1033 C CD1 . LEU A 138 ? 0.6967 0.9047 0.8610 -0.2592 -0.1221 0.1940 142 LEU A CD1 1034 C CD2 . LEU A 138 ? 0.8035 0.9790 0.9702 -0.2963 -0.1589 0.2402 142 LEU A CD2 1035 N N . GLU A 139 ? 0.6827 0.8554 0.9431 -0.2929 -0.1618 0.2146 143 GLU A N 1036 C CA . GLU A 139 ? 0.6684 0.8399 0.9660 -0.2827 -0.1655 0.1989 143 GLU A CA 1037 C C . GLU A 139 ? 0.6560 0.8408 0.9676 -0.2503 -0.1571 0.1672 143 GLU A C 1038 O O . GLU A 139 ? 0.6361 0.8148 0.9476 -0.2379 -0.1650 0.1606 143 GLU A O 1039 C CB . GLU A 139 ? 0.7233 0.8547 1.0562 -0.2897 -0.2030 0.2133 143 GLU A CB 1040 C CG . GLU A 139 ? 0.8858 1.0180 1.2653 -0.2776 -0.2091 0.1921 143 GLU A CG 1041 C CD . GLU A 139 ? 1.2800 1.3689 1.6958 -0.2933 -0.2499 0.2108 143 GLU A CD 1042 O OE1 . GLU A 139 ? 1.2617 1.3420 1.6592 -0.3297 -0.2525 0.2396 143 GLU A OE1 1043 O OE2 . GLU A 139 ? 1.2919 1.3572 1.7571 -0.2722 -0.2830 0.1945 143 GLU A OE2 1044 N N . PRO A 140 ? 0.5759 0.7816 0.8969 -0.2406 -0.1437 0.1474 144 PRO A N 1045 C CA . PRO A 140 ? 0.5369 0.7556 0.8601 -0.2211 -0.1411 0.1241 144 PRO A CA 1046 C C . PRO A 140 ? 0.5647 0.7861 0.9232 -0.2117 -0.1572 0.1046 144 PRO A C 1047 O O . PRO A 140 ? 0.5759 0.7828 0.9726 -0.2133 -0.1749 0.1050 144 PRO A O 1048 C CB . PRO A 140 ? 0.5486 0.7835 0.8791 -0.2178 -0.1331 0.1121 144 PRO A CB 1049 C CG . PRO A 140 ? 0.6207 0.8609 0.9484 -0.2326 -0.1236 0.1221 144 PRO A CG 1050 C CD . PRO A 140 ? 0.5918 0.8134 0.9206 -0.2512 -0.1334 0.1449 144 PRO A CD 1051 N N . GLU A 141 ? 0.4984 0.7428 0.8472 -0.2055 -0.1536 0.0842 145 GLU A N 1052 C CA . GLU A 141 ? 0.4950 0.7689 0.8792 -0.2001 -0.1634 0.0493 145 GLU A CA 1053 C C . GLU A 141 ? 0.5857 0.8531 1.0048 -0.1931 -0.1828 0.0368 145 GLU A C 1054 O O . GLU A 141 ? 0.5805 0.8665 1.0587 -0.1843 -0.2008 0.0023 145 GLU A O 1055 C CB . GLU A 141 ? 0.5061 0.7979 0.9308 -0.1971 -0.1682 0.0287 145 GLU A CB 1056 C CG . GLU A 141 ? 0.6301 0.9349 1.0248 -0.2026 -0.1550 0.0334 145 GLU A CG 1057 C CD . GLU A 141 ? 0.8333 1.1668 1.2662 -0.2008 -0.1589 0.0072 145 GLU A CD 1058 O OE1 . GLU A 141 ? 0.8007 1.1800 1.2552 -0.2038 -0.1617 -0.0286 145 GLU A OE1 1059 O OE2 . GLU A 141 ? 0.6214 0.9409 1.0627 -0.1988 -0.1574 0.0177 145 GLU A OE2 1060 N N . HIS A 142 ? 0.5767 0.8213 0.9657 -0.1955 -0.1824 0.0596 146 HIS A N 1061 C CA . HIS A 142 ? 0.6041 0.8366 1.0212 -0.1884 -0.2055 0.0520 146 HIS A CA 1062 C C . HIS A 142 ? 0.6536 0.9060 1.0353 -0.1904 -0.1918 0.0455 146 HIS A C 1063 O O . HIS A 142 ? 0.6432 0.9013 0.9715 -0.2000 -0.1680 0.0608 146 HIS A O 1064 C CB . HIS A 142 ? 0.6552 0.8351 1.0662 -0.1960 -0.2243 0.0942 146 HIS A CB 1065 C CG . HIS A 142 ? 0.7323 0.8857 1.1806 -0.2005 -0.2459 0.1041 146 HIS A CG 1066 N ND1 . HIS A 142 ? 0.7857 0.9186 1.3025 -0.1902 -0.2881 0.0866 146 HIS A ND1 1067 C CD2 . HIS A 142 ? 0.7666 0.9127 1.1964 -0.2151 -0.2327 0.1267 146 HIS A CD2 1068 C CE1 . HIS A 142 ? 0.8019 0.9097 1.3342 -0.2015 -0.2994 0.1049 146 HIS A CE1 1069 N NE2 . HIS A 142 ? 0.7924 0.9110 1.2710 -0.2181 -0.2641 0.1290 146 HIS A NE2 1070 N N . GLU A 143 ? 0.6168 0.8768 1.0332 -0.1811 -0.2117 0.0212 147 GLU A N 1071 C CA . GLU A 143 ? 0.6047 0.8861 0.9930 -0.1839 -0.2008 0.0113 147 GLU A CA 1072 C C . GLU A 143 ? 0.6780 0.9241 1.0709 -0.1774 -0.2228 0.0292 147 GLU A C 1073 O O . GLU A 143 ? 0.6886 0.9097 1.1359 -0.1659 -0.2606 0.0232 147 GLU A O 1074 C CB . GLU A 143 ? 0.6047 0.9563 1.0125 -0.1877 -0.1918 -0.0448 147 GLU A CB 1075 C CG . GLU A 143 ? 0.7216 1.1153 1.2161 -0.1742 -0.2156 -0.1055 147 GLU A CG 1076 C CD . GLU A 143 ? 0.9382 1.4216 1.4311 -0.1916 -0.1951 -0.1610 147 GLU A CD 1077 O OE1 . GLU A 143 ? 0.7996 1.3153 1.2496 -0.2151 -0.1710 -0.1581 147 GLU A OE1 1078 O OE2 . GLU A 143 ? 0.8395 1.3618 1.3665 -0.1868 -0.2038 -0.2042 147 GLU A OE2 1079 N N . TYR A 144 ? 0.6461 0.8842 0.9813 -0.1864 -0.2038 0.0552 148 TYR A N 1080 C CA . TYR A 144 ? 0.6708 0.8791 0.9967 -0.1852 -0.2210 0.0776 148 TYR A CA 1081 C C . TYR A 144 ? 0.7111 0.9469 1.0208 -0.1837 -0.2106 0.0574 148 TYR A C 1082 O O . TYR A 144 ? 0.6882 0.9527 0.9602 -0.1935 -0.1804 0.0498 148 TYR A O 1083 C CB . TYR A 144 ? 0.7035 0.8795 0.9798 -0.2013 -0.2108 0.1287 148 TYR A CB 1084 C CG . TYR A 144 ? 0.7470 0.8990 1.0387 -0.2089 -0.2222 0.1489 148 TYR A CG 1085 C CD1 . TYR A 144 ? 0.8187 0.9325 1.1466 -0.2112 -0.2646 0.1637 148 TYR A CD1 1086 C CD2 . TYR A 144 ? 0.7381 0.9028 1.0119 -0.2150 -0.1962 0.1524 148 TYR A CD2 1087 C CE1 . TYR A 144 ? 0.8643 0.9551 1.2054 -0.2234 -0.2767 0.1833 148 TYR A CE1 1088 C CE2 . TYR A 144 ? 0.7648 0.9130 1.0536 -0.2240 -0.2046 0.1676 148 TYR A CE2 1089 C CZ . TYR A 144 ? 0.8997 1.0122 1.2205 -0.2299 -0.2429 0.1834 148 TYR A CZ 1090 O OH . TYR A 144 ? 0.9218 1.0166 1.2567 -0.2436 -0.2532 0.1996 148 TYR A OH 1091 N N . LYS A 145 ? 0.6859 0.9113 1.0283 -0.1726 -0.2413 0.0472 149 LYS A N 1092 C CA . LYS A 145 ? 0.6802 0.9349 1.0163 -0.1696 -0.2355 0.0223 149 LYS A CA 1093 C C . LYS A 145 ? 0.7523 0.9752 1.0376 -0.1777 -0.2328 0.0662 149 LYS A C 1094 O O . LYS A 145 ? 0.7760 0.9603 1.0722 -0.1761 -0.2669 0.0915 149 LYS A O 1095 C CB . LYS A 145 ? 0.7267 1.0029 1.1437 -0.1488 -0.2738 -0.0316 149 LYS A CB 1096 C CG . LYS A 145 ? 0.9437 1.2638 1.3602 -0.1468 -0.2653 -0.0682 149 LYS A CG 1097 C CD . LYS A 145 ? 1.0858 1.4572 1.5956 -0.1273 -0.2949 -0.1459 149 LYS A CD 1098 C CE . LYS A 145 ? 1.2044 1.6440 1.7123 -0.1331 -0.2750 -0.1951 149 LYS A CE 1099 N NZ . LYS A 145 ? 1.3161 1.7238 1.8198 -0.1216 -0.2975 -0.1790 149 LYS A NZ 1100 N N . CYS A 146 ? 0.7085 0.9478 0.9386 -0.1900 -0.1960 0.0759 150 CYS A N 1101 C CA . CYS A 146 ? 0.7232 0.9480 0.9090 -0.1982 -0.1881 0.1064 150 CYS A CA 1102 C C . CYS A 146 ? 0.7278 0.9801 0.9128 -0.1938 -0.1843 0.0784 150 CYS A C 1103 O O . CYS A 146 ? 0.7011 0.9876 0.8756 -0.1996 -0.1616 0.0515 150 CYS A O 1104 C CB . CYS A 146 ? 0.7286 0.9526 0.8675 -0.2118 -0.1562 0.1293 150 CYS A CB 1105 S SG . CYS A 146 ? 0.8014 1.0011 0.9377 -0.2218 -0.1601 0.1629 150 CYS A SG 1106 N N . ASP A 147 ? 0.6836 0.9215 0.8801 -0.1873 -0.2110 0.0846 151 ASP A N 1107 C CA . ASP A 147 ? 0.6712 0.9350 0.8709 -0.1816 -0.2111 0.0574 151 ASP A CA 1108 C C . ASP A 147 ? 0.6925 0.9526 0.8344 -0.1947 -0.1885 0.0870 151 ASP A C 1109 O O . ASP A 147 ? 0.6975 0.9333 0.8124 -0.2054 -0.1917 0.1268 151 ASP A O 1110 C CB . ASP A 147 ? 0.7306 0.9805 0.9867 -0.1633 -0.2620 0.0413 151 ASP A CB 1111 C CG . ASP A 147 ? 0.9518 1.2127 1.2845 -0.1457 -0.2907 -0.0022 151 ASP A CG 1112 O OD1 . ASP A 147 ? 0.9573 1.2731 1.3091 -0.1456 -0.2673 -0.0514 151 ASP A OD1 1113 O OD2 . ASP A 147 ? 1.0724 1.2894 1.4476 -0.1354 -0.3405 0.0112 151 ASP A OD2 1114 N N . SER A 148 ? 0.6203 0.9110 0.7447 -0.1980 -0.1654 0.0641 152 SER A N 1115 C CA . SER A 148 ? 0.6092 0.9010 0.6883 -0.2084 -0.1446 0.0832 152 SER A CA 1116 C C . SER A 148 ? 0.6374 0.9569 0.7173 -0.2060 -0.1411 0.0549 152 SER A C 1117 O O . SER A 148 ? 0.6153 0.9648 0.7204 -0.2035 -0.1409 0.0153 152 SER A O 1118 C CB . SER A 148 ? 0.6412 0.9330 0.6892 -0.2209 -0.1143 0.0917 152 SER A CB 1119 O OG . SER A 148 ? 0.7406 1.0337 0.7590 -0.2279 -0.0998 0.1054 152 SER A OG 1120 N N . GLU A 149 ? 0.5990 0.9181 0.6518 -0.2102 -0.1360 0.0705 153 GLU A N 1121 C CA . GLU A 149 ? 0.5911 0.9369 0.6409 -0.2091 -0.1301 0.0453 153 GLU A CA 1122 C C . GLU A 149 ? 0.6271 0.9769 0.6377 -0.2206 -0.1060 0.0599 153 GLU A C 1123 O O . GLU A 149 ? 0.6218 0.9600 0.6142 -0.2271 -0.1010 0.0873 153 GLU A O 1124 C CB . GLU A 149 ? 0.6305 0.9763 0.7113 -0.1941 -0.1668 0.0359 153 GLU A CB 1125 C CG . GLU A 149 ? 0.8340 1.1551 0.8927 -0.1993 -0.1877 0.0781 153 GLU A CG 1126 C CD . GLU A 149 ? 1.2275 1.5222 1.3236 -0.1870 -0.2432 0.0837 153 GLU A CD 1127 O OE1 . GLU A 149 ? 1.1427 1.4238 1.2851 -0.1738 -0.2667 0.0678 153 GLU A OE1 1128 O OE2 . GLU A 149 ? 1.2697 1.5542 1.3488 -0.1931 -0.2679 0.1073 153 GLU A OE2 1129 N N . ILE A 150 ? 0.5696 0.9428 0.5723 -0.2252 -0.0912 0.0355 154 ILE A N 1130 C CA . ILE A 150 ? 0.5567 0.9363 0.5331 -0.2338 -0.0724 0.0403 154 ILE A CA 1131 C C . ILE A 150 ? 0.5933 0.9959 0.5719 -0.2286 -0.0790 0.0258 154 ILE A C 1132 O O . ILE A 150 ? 0.5783 0.9999 0.5764 -0.2235 -0.0866 -0.0032 154 ILE A O 1133 C CB . ILE A 150 ? 0.5891 0.9645 0.5498 -0.2491 -0.0529 0.0318 154 ILE A CB 1134 C CG1 . ILE A 150 ? 0.5900 0.9427 0.5510 -0.2549 -0.0538 0.0432 154 ILE A CG1 1135 C CG2 . ILE A 150 ? 0.6031 0.9773 0.5517 -0.2529 -0.0419 0.0365 154 ILE A CG2 1136 C CD1 . ILE A 150 ? 0.6856 1.0248 0.6275 -0.2758 -0.0469 0.0420 154 ILE A CD1 1137 N N . LEU A 151 ? 0.5662 0.9749 0.5283 -0.2312 -0.0774 0.0420 155 LEU A N 1138 C CA . LEU A 151 ? 0.5877 1.0195 0.5460 -0.2288 -0.0841 0.0334 155 LEU A CA 1139 C C . LEU A 151 ? 0.6352 1.0877 0.5789 -0.2374 -0.0576 0.0192 155 LEU A C 1140 O O . LEU A 151 ? 0.6339 1.0823 0.5717 -0.2445 -0.0424 0.0250 155 LEU A O 1141 C CB . LEU A 151 ? 0.6235 1.0539 0.5686 -0.2337 -0.1072 0.0648 155 LEU A CB 1142 C CG . LEU A 151 ? 0.7169 1.1151 0.6704 -0.2333 -0.1400 0.0942 155 LEU A CG 1143 C CD1 . LEU A 151 ? 0.7713 1.1711 0.6974 -0.2519 -0.1655 0.1304 155 LEU A CD1 1144 C CD2 . LEU A 151 ? 0.7609 1.1428 0.7553 -0.2129 -0.1710 0.0741 155 LEU A CD2 1145 N N . TYR A 152 ? 0.5816 1.0575 0.5273 -0.2351 -0.0564 -0.0038 156 TYR A N 1146 C CA . TYR A 152 ? 0.5717 1.0697 0.5091 -0.2421 -0.0367 -0.0209 156 TYR A CA 1147 C C . TYR A 152 ? 0.6633 1.1902 0.5963 -0.2379 -0.0486 -0.0229 156 TYR A C 1148 O O . TYR A 152 ? 0.6763 1.2071 0.6219 -0.2279 -0.0680 -0.0340 156 TYR A O 1149 C CB . TYR A 152 ? 0.5693 1.0683 0.5100 -0.2500 -0.0244 -0.0479 156 TYR A CB 1150 C CG . TYR A 152 ? 0.5750 1.0894 0.5110 -0.2585 -0.0092 -0.0648 156 TYR A CG 1151 C CD1 . TYR A 152 ? 0.5999 1.1036 0.5382 -0.2628 -0.0015 -0.0600 156 TYR A CD1 1152 C CD2 . TYR A 152 ? 0.5772 1.1199 0.5150 -0.2609 -0.0053 -0.0918 156 TYR A CD2 1153 C CE1 . TYR A 152 ? 0.6059 1.1225 0.5509 -0.2684 0.0071 -0.0807 156 TYR A CE1 1154 C CE2 . TYR A 152 ? 0.5889 1.1438 0.5251 -0.2698 0.0074 -0.1082 156 TYR A CE2 1155 C CZ . TYR A 152 ? 0.6907 1.2304 0.6317 -0.2729 0.0123 -0.1019 156 TYR A CZ 1156 O OH . TYR A 152 ? 0.7218 1.2725 0.6717 -0.2794 0.0196 -0.1228 156 TYR A OH 1157 N N . ASN A 153 ? 0.6354 1.1873 0.5540 -0.2467 -0.0413 -0.0147 157 ASN A N 1158 C CA . ASN A 153 ? 0.6564 1.2395 0.5609 -0.2506 -0.0559 -0.0090 157 ASN A CA 1159 C C . ASN A 153 ? 0.7681 1.3262 0.6690 -0.2476 -0.0962 0.0209 157 ASN A C 1160 O O . ASN A 153 ? 0.7794 1.3415 0.6844 -0.2405 -0.1231 0.0177 157 ASN A O 1161 C CB . ASN A 153 ? 0.6124 1.2197 0.5253 -0.2437 -0.0500 -0.0420 157 ASN A CB 1162 C CG . ASN A 153 ? 0.7500 1.3739 0.6701 -0.2486 -0.0193 -0.0702 157 ASN A CG 1163 O OD1 . ASN A 153 ? 0.6785 1.3164 0.5995 -0.2568 -0.0046 -0.0714 157 ASN A OD1 1164 N ND2 . ASN A 153 ? 0.5820 1.2088 0.5126 -0.2454 -0.0126 -0.0979 157 ASN A ND2 1165 N N . ASN A 154 ? 0.7625 1.2900 0.6622 -0.2513 -0.1053 0.0474 158 ASN A N 1166 C CA . ASN A 154 ? 0.8103 1.3017 0.7139 -0.2495 -0.1487 0.0776 158 ASN A CA 1167 C C . ASN A 154 ? 0.8957 1.3635 0.8429 -0.2225 -0.1737 0.0519 158 ASN A C 1168 O O . ASN A 154 ? 0.9344 1.3712 0.9004 -0.2149 -0.2198 0.0673 158 ASN A O 1169 C CB . ASN A 154 ? 0.8702 1.3698 0.7407 -0.2722 -0.1814 0.1143 158 ASN A CB 1170 C CG . ASN A 154 ? 1.1901 1.7380 1.0203 -0.3055 -0.1535 0.1270 158 ASN A CG 1171 O OD1 . ASN A 154 ? 1.1513 1.7466 0.9726 -0.3108 -0.1313 0.1046 158 ASN A OD1 1172 N ND2 . ASN A 154 ? 1.0833 1.6290 0.8915 -0.3314 -0.1556 0.1585 158 ASN A ND2 1173 N N . HIS A 155 ? 0.8332 1.3195 0.7997 -0.2118 -0.1456 0.0097 159 HIS A N 1174 C CA . HIS A 155 ? 0.8314 1.3212 0.8413 -0.1936 -0.1576 -0.0304 159 HIS A CA 1175 C C . HIS A 155 ? 0.8212 1.2967 0.8419 -0.1954 -0.1425 -0.0347 159 HIS A C 1176 O O . HIS A 155 ? 0.7995 1.2792 0.7979 -0.2092 -0.1066 -0.0347 159 HIS A O 1177 C CB . HIS A 155 ? 0.8347 1.3649 0.8476 -0.1952 -0.1296 -0.0736 159 HIS A CB 1178 C CG . HIS A 155 ? 0.9069 1.4611 0.9318 -0.1850 -0.1509 -0.0926 159 HIS A CG 1179 N ND1 . HIS A 155 ? 0.9192 1.5123 0.9439 -0.1891 -0.1257 -0.1293 159 HIS A ND1 1180 C CD2 . HIS A 155 ? 0.9739 1.5149 1.0090 -0.1740 -0.1983 -0.0764 159 HIS A CD2 1181 C CE1 . HIS A 155 ? 0.9345 1.5424 0.9722 -0.1768 -0.1544 -0.1391 159 HIS A CE1 1182 N NE2 . HIS A 155 ? 0.9751 1.5501 1.0193 -0.1675 -0.2016 -0.1069 159 HIS A NE2 1183 N N . LYS A 156 ? 0.7493 1.2093 0.8088 -0.1816 -0.1730 -0.0430 160 LYS A N 1184 C CA . LYS A 156 ? 0.7136 1.1695 0.7848 -0.1850 -0.1579 -0.0526 160 LYS A CA 1185 C C . LYS A 156 ? 0.7150 1.2172 0.7979 -0.1928 -0.1320 -0.1040 160 LYS A C 1186 O O . LYS A 156 ? 0.7126 1.2501 0.8344 -0.1816 -0.1475 -0.1493 160 LYS A O 1187 C CB . LYS A 156 ? 0.7616 1.1942 0.8794 -0.1681 -0.2000 -0.0540 160 LYS A CB 1188 C CG . LYS A 156 ? 0.9093 1.3477 1.0424 -0.1724 -0.1838 -0.0700 160 LYS A CG 1189 C CD . LYS A 156 ? 1.0170 1.4540 1.2183 -0.1516 -0.2252 -0.0995 160 LYS A CD 1190 C CE . LYS A 156 ? 1.1244 1.6232 1.3835 -0.1413 -0.2309 -0.1754 160 LYS A CE 1191 N NZ . LYS A 156 ? 1.2428 1.7508 1.5788 -0.1217 -0.2669 -0.2155 160 LYS A NZ 1192 N N . PHE A 157 ? 0.6363 1.1404 0.6868 -0.2155 -0.0967 -0.0983 161 PHE A N 1193 C CA . PHE A 157 ? 0.6189 1.1666 0.6664 -0.2378 -0.0730 -0.1386 161 PHE A CA 1194 C C . PHE A 157 ? 0.6933 1.2477 0.7410 -0.2552 -0.0643 -0.1453 161 PHE A C 1195 O O . PHE A 157 ? 0.6924 1.2959 0.7396 -0.2811 -0.0491 -0.1835 161 PHE A O 1196 C CB . PHE A 157 ? 0.6342 1.1798 0.6384 -0.2597 -0.0464 -0.1275 161 PHE A CB 1197 C CG . PHE A 157 ? 0.6455 1.1458 0.6140 -0.2722 -0.0343 -0.0848 161 PHE A CG 1198 C CD1 . PHE A 157 ? 0.6774 1.1482 0.6392 -0.2572 -0.0392 -0.0522 161 PHE A CD1 1199 C CD2 . PHE A 157 ? 0.6753 1.1679 0.6187 -0.3028 -0.0213 -0.0809 161 PHE A CD2 1200 C CE1 . PHE A 157 ? 0.6905 1.1295 0.6341 -0.2655 -0.0307 -0.0262 161 PHE A CE1 1201 C CE2 . PHE A 157 ? 0.7181 1.1639 0.6398 -0.3100 -0.0200 -0.0457 161 PHE A CE2 1202 C CZ . PHE A 157 ? 0.6870 1.1089 0.6153 -0.2879 -0.0243 -0.0236 161 PHE A CZ 1203 N N . THR A 158 ? 0.6699 1.1806 0.7130 -0.2471 -0.0721 -0.1079 162 THR A N 1204 C CA . THR A 158 ? 0.6750 1.1871 0.7174 -0.2613 -0.0668 -0.1086 162 THR A CA 1205 C C . THR A 158 ? 0.7271 1.2000 0.7891 -0.2395 -0.0869 -0.0809 162 THR A C 1206 O O . THR A 158 ? 0.7166 1.1538 0.7757 -0.2229 -0.1005 -0.0483 162 THR A O 1207 C CB . THR A 158 ? 0.8440 1.3459 0.8346 -0.2984 -0.0431 -0.0896 162 THR A CB 1208 O OG1 . THR A 158 ? 0.8515 1.3727 0.8421 -0.3185 -0.0404 -0.1005 162 THR A OG1 1209 C CG2 . THR A 158 ? 0.8585 1.3014 0.8209 -0.2937 -0.0417 -0.0403 162 THR A CG2 1210 N N . ASN A 159 ? 0.6986 1.1851 0.7791 -0.2448 -0.0888 -0.0958 163 ASN A N 1211 C CA . ASN A 159 ? 0.7003 1.1539 0.8033 -0.2278 -0.1076 -0.0750 163 ASN A CA 1212 C C . ASN A 159 ? 0.7461 1.2209 0.8505 -0.2455 -0.0969 -0.0892 163 ASN A C 1213 O O . ASN A 159 ? 0.7444 1.2701 0.8384 -0.2728 -0.0799 -0.1226 163 ASN A O 1214 C CB . ASN A 159 ? 0.7373 1.1881 0.9000 -0.1973 -0.1470 -0.0930 163 ASN A CB 1215 C CG . ASN A 159 ? 1.1354 1.6436 1.3640 -0.1885 -0.1629 -0.1617 163 ASN A CG 1216 O OD1 . ASN A 159 ? 1.0669 1.6309 1.2969 -0.2100 -0.1403 -0.2007 163 ASN A OD1 1217 N ND2 . ASN A 159 ? 1.1298 1.6262 1.4168 -0.1590 -0.2076 -0.1779 163 ASN A ND2 1218 N N . ALA A 160 ? 0.7036 1.1432 0.8148 -0.2362 -0.1063 -0.0624 164 ALA A N 1219 C CA . ALA A 160 ? 0.6999 1.1560 0.8131 -0.2510 -0.0993 -0.0717 164 ALA A CA 1220 C C . ALA A 160 ? 0.7468 1.1679 0.8933 -0.2283 -0.1206 -0.0539 164 ALA A C 1221 O O . ALA A 160 ? 0.7543 1.1303 0.9030 -0.2110 -0.1366 -0.0205 164 ALA A O 1222 C CB . ALA A 160 ? 0.7179 1.1535 0.7693 -0.2802 -0.0779 -0.0384 164 ALA A CB 1223 N N . SER A 161 ? 0.6870 1.1345 0.8568 -0.2343 -0.1210 -0.0772 165 SER A N 1224 C CA . SER A 161 ? 0.6778 1.0958 0.8790 -0.2178 -0.1391 -0.0634 165 SER A CA 1225 C C . SER A 161 ? 0.7002 1.1174 0.8680 -0.2382 -0.1203 -0.0470 165 SER A C 1226 O O . SER A 161 ? 0.6890 1.1513 0.8340 -0.2665 -0.1030 -0.0690 165 SER A O 1227 C CB . SER A 161 ? 0.7266 1.1829 1.0075 -0.2003 -0.1654 -0.1189 165 SER A CB 1228 O OG . SER A 161 ? 0.8779 1.2957 1.1986 -0.1729 -0.2028 -0.1110 165 SER A OG 1229 N N . LYS A 162 ? 0.6484 1.0165 0.8094 -0.2288 -0.1256 -0.0072 166 LYS A N 1230 C CA . LYS A 162 ? 0.6380 1.0005 0.7741 -0.2437 -0.1139 0.0081 166 LYS A CA 1231 C C . LYS A 162 ? 0.6596 1.0083 0.8361 -0.2284 -0.1289 0.0095 166 LYS A C 1232 O O . LYS A 162 ? 0.6559 0.9642 0.8459 -0.2126 -0.1433 0.0356 166 LYS A O 1233 C CB . LYS A 162 ? 0.6760 0.9990 0.7587 -0.2536 -0.1016 0.0501 166 LYS A CB 1234 C CG . LYS A 162 ? 0.8338 1.1486 0.8919 -0.2706 -0.0977 0.0636 166 LYS A CG 1235 C CD . LYS A 162 ? 0.9237 1.2778 0.9526 -0.3058 -0.0919 0.0453 166 LYS A CD 1236 C CE . LYS A 162 ? 1.0922 1.4604 1.1193 -0.3207 -0.0952 0.0431 166 LYS A CE 1237 N NZ . LYS A 162 ? 1.2741 1.5983 1.2584 -0.3365 -0.1035 0.0805 166 LYS A NZ 1238 N N . ILE A 163 ? 0.5976 0.9876 0.7946 -0.2378 -0.1270 -0.0224 167 ILE A N 1239 C CA . ILE A 163 ? 0.5849 0.9693 0.8232 -0.2259 -0.1399 -0.0277 167 ILE A CA 1240 C C . ILE A 163 ? 0.6257 0.9881 0.8193 -0.2402 -0.1260 0.0061 167 ILE A C 1241 O O . ILE A 163 ? 0.6318 1.0189 0.7863 -0.2662 -0.1132 0.0031 167 ILE A O 1242 C CB . ILE A 163 ? 0.6175 1.0694 0.9161 -0.2258 -0.1483 -0.0919 167 ILE A CB 1243 C CG1 . ILE A 163 ? 0.6267 1.0951 0.9872 -0.2041 -0.1726 -0.1317 167 ILE A CG1 1244 C CG2 . ILE A 163 ? 0.6172 1.0629 0.9562 -0.2157 -0.1601 -0.0965 167 ILE A CG2 1245 C CD1 . ILE A 163 ? 0.7176 1.2826 1.1311 -0.2120 -0.1719 -0.2138 167 ILE A CD1 1246 N N . ILE A 164 ? 0.5685 0.8846 0.7663 -0.2270 -0.1322 0.0390 168 ILE A N 1247 C CA . ILE A 164 ? 0.5634 0.8578 0.7318 -0.2342 -0.1240 0.0657 168 ILE A CA 1248 C C . ILE A 164 ? 0.5894 0.8808 0.7951 -0.2252 -0.1326 0.0618 168 ILE A C 1249 O O . ILE A 164 ? 0.5975 0.8712 0.8398 -0.2114 -0.1472 0.0644 168 ILE A O 1250 C CB . ILE A 164 ? 0.6080 0.8623 0.7494 -0.2299 -0.1194 0.1011 168 ILE A CB 1251 C CG1 . ILE A 164 ? 0.6168 0.8698 0.7326 -0.2333 -0.1139 0.1046 168 ILE A CG1 1252 C CG2 . ILE A 164 ? 0.6142 0.8512 0.7354 -0.2346 -0.1160 0.1176 168 ILE A CG2 1253 C CD1 . ILE A 164 ? 0.7154 0.9549 0.8419 -0.2233 -0.1197 0.1159 168 ILE A CD1 1254 N N . LYS A 165 ? 0.5229 0.8241 0.7155 -0.2356 -0.1277 0.0618 169 LYS A N 1255 C CA . LYS A 165 ? 0.5123 0.8131 0.7350 -0.2292 -0.1331 0.0583 169 LYS A CA 1256 C C . LYS A 165 ? 0.5604 0.8244 0.7645 -0.2259 -0.1301 0.0902 169 LYS A C 1257 O O . LYS A 165 ? 0.5861 0.8381 0.7537 -0.2335 -0.1272 0.1041 169 LYS A O 1258 C CB . LYS A 165 ? 0.5426 0.8916 0.7653 -0.2461 -0.1309 0.0301 169 LYS A CB 1259 C CG . LYS A 165 ? 0.6336 1.0307 0.9194 -0.2397 -0.1386 -0.0178 169 LYS A CG 1260 C CD . LYS A 165 ? 0.6369 1.0599 0.9319 -0.2481 -0.1378 -0.0296 169 LYS A CD 1261 C CE . LYS A 165 ? 0.6045 1.0595 0.9751 -0.2340 -0.1492 -0.0719 169 LYS A CE 1262 N NZ . LYS A 165 ? 0.6625 1.0607 1.0684 -0.2108 -0.1629 -0.0483 169 LYS A NZ 1263 N N . THR A 166 ? 0.4828 0.7312 0.7166 -0.2164 -0.1344 0.0977 170 THR A N 1264 C CA . THR A 166 ? 0.4782 0.7085 0.7047 -0.2154 -0.1297 0.1159 170 THR A CA 1265 C C . THR A 166 ? 0.5171 0.7565 0.7519 -0.2153 -0.1317 0.1075 170 THR A C 1266 O O . THR A 166 ? 0.5411 0.7822 0.8064 -0.2118 -0.1340 0.1038 170 THR A O 1267 C CB . THR A 166 ? 0.6468 0.8626 0.8902 -0.2165 -0.1320 0.1310 170 THR A CB 1268 O OG1 . THR A 166 ? 0.7009 0.9138 0.9838 -0.2135 -0.1476 0.1230 170 THR A OG1 1269 C CG2 . THR A 166 ? 0.6455 0.8529 0.8660 -0.2215 -0.1294 0.1457 170 THR A CG2 1270 N N . ASP A 167 ? 0.4281 0.6706 0.6342 -0.2225 -0.1351 0.1069 171 ASP A N 1271 C CA . ASP A 167 ? 0.4135 0.6600 0.6163 -0.2267 -0.1443 0.1041 171 ASP A CA 1272 C C . ASP A 167 ? 0.4407 0.6939 0.6810 -0.2174 -0.1442 0.0957 171 ASP A C 1273 O O . ASP A 167 ? 0.4232 0.6684 0.6861 -0.2095 -0.1377 0.0991 171 ASP A O 1274 C CB . ASP A 167 ? 0.4501 0.6684 0.6276 -0.2271 -0.1570 0.1184 171 ASP A CB 1275 C CG . ASP A 167 ? 0.5715 0.7790 0.7366 -0.2343 -0.1803 0.1230 171 ASP A CG 1276 O OD1 . ASP A 167 ? 0.5718 0.8027 0.7354 -0.2454 -0.1828 0.1163 171 ASP A OD1 1277 O OD2 . ASP A 167 ? 0.6466 0.8235 0.8088 -0.2283 -0.2002 0.1304 171 ASP A OD2 1278 N N . PHE A 168 ? 0.4063 0.6766 0.6484 -0.2234 -0.1520 0.0860 172 PHE A N 1279 C CA . PHE A 168 ? 0.3934 0.6718 0.6710 -0.2150 -0.1525 0.0759 172 PHE A CA 1280 C C . PHE A 168 ? 0.4514 0.7104 0.7441 -0.2031 -0.1509 0.0824 172 PHE A C 1281 O O . PHE A 168 ? 0.4699 0.7137 0.7485 -0.1997 -0.1621 0.0869 172 PHE A O 1282 C CB . PHE A 168 ? 0.4251 0.7224 0.6902 -0.2260 -0.1652 0.0690 172 PHE A CB 1283 C CG . PHE A 168 ? 0.4381 0.7820 0.7054 -0.2420 -0.1618 0.0469 172 PHE A CG 1284 C CD1 . PHE A 168 ? 0.4948 0.8592 0.7251 -0.2641 -0.1615 0.0455 172 PHE A CD1 1285 C CD2 . PHE A 168 ? 0.4508 0.8273 0.7615 -0.2377 -0.1591 0.0210 172 PHE A CD2 1286 C CE1 . PHE A 168 ? 0.5052 0.9329 0.7442 -0.2831 -0.1559 0.0124 172 PHE A CE1 1287 C CE2 . PHE A 168 ? 0.4842 0.9189 0.8087 -0.2524 -0.1561 -0.0125 172 PHE A CE2 1288 C CZ . PHE A 168 ? 0.4741 0.9395 0.7638 -0.2757 -0.1534 -0.0195 172 PHE A CZ 1289 N N . GLY A 169 ? 0.3873 0.6496 0.7100 -0.2007 -0.1402 0.0803 173 GLY A N 1290 C CA . GLY A 169 ? 0.3847 0.6491 0.7222 -0.1994 -0.1334 0.0788 173 GLY A CA 1291 C C . GLY A 169 ? 0.4364 0.7141 0.7991 -0.1929 -0.1386 0.0621 173 GLY A C 1292 O O . GLY A 169 ? 0.4339 0.7156 0.8000 -0.1898 -0.1488 0.0560 173 GLY A O 1293 N N . SER A 170 ? 0.4642 0.8074 0.6338 -0.0694 -0.1074 0.1097 174 SER A N 1294 C CA . SER A 170 ? 0.4463 0.7575 0.5751 -0.0586 -0.0886 0.0946 174 SER A CA 1295 C C . SER A 170 ? 0.4610 0.7677 0.6185 -0.0354 -0.0882 0.0979 174 SER A C 1296 O O . SER A 170 ? 0.4674 0.7837 0.6524 -0.0346 -0.1098 0.1157 174 SER A O 1297 C CB . SER A 170 ? 0.5120 0.8029 0.5830 -0.0783 -0.0956 0.0946 174 SER A CB 1298 O OG . SER A 170 ? 0.6479 0.9385 0.6897 -0.1024 -0.0958 0.0908 174 SER A OG 1299 N N . PRO A 171 ? 0.3766 0.6672 0.5277 -0.0178 -0.0650 0.0818 175 PRO A N 1300 C CA . PRO A 171 ? 0.3700 0.6523 0.5442 0.0013 -0.0629 0.0824 175 PRO A CA 1301 C C . PRO A 171 ? 0.4412 0.7011 0.5794 -0.0013 -0.0695 0.0840 175 PRO A C 1302 O O . PRO A 171 ? 0.4447 0.6993 0.5457 -0.0186 -0.0788 0.0880 175 PRO A O 1303 C CB . PRO A 171 ? 0.3744 0.6504 0.5528 0.0157 -0.0355 0.0639 175 PRO A CB 1304 C CG . PRO A 171 ? 0.4170 0.6898 0.5599 0.0044 -0.0244 0.0543 175 PRO A CG 1305 C CD . PRO A 171 ? 0.3715 0.6486 0.4923 -0.0160 -0.0412 0.0637 175 PRO A CD 1306 N N . GLY A 172 ? 0.4096 0.6564 0.5593 0.0139 -0.0632 0.0802 176 GLY A N 1307 C CA . GLY A 172 ? 0.4255 0.6515 0.5454 0.0125 -0.0654 0.0791 176 GLY A CA 1308 C C . GLY A 172 ? 0.5302 0.7514 0.6318 -0.0029 -0.0869 0.0953 176 GLY A C 1309 O O . GLY A 172 ? 0.5610 0.7930 0.6846 -0.0089 -0.1071 0.1137 176 GLY A O 1310 N N . GLU A 173 ? 0.4795 0.6853 0.5413 -0.0107 -0.0835 0.0900 177 GLU A N 1311 C CA . GLU A 173 ? 0.4517 0.6482 0.4897 -0.0050 -0.0641 0.0716 177 GLU A CA 1312 C C . GLU A 173 ? 0.4672 0.6517 0.5214 0.0099 -0.0566 0.0651 177 GLU A C 1313 O O . GLU A 173 ? 0.4733 0.6514 0.5525 0.0143 -0.0664 0.0754 177 GLU A O 1314 C CB . GLU A 173 ? 0.4786 0.6684 0.4762 -0.0205 -0.0644 0.0701 177 GLU A CB 1315 C CG . GLU A 173 ? 0.6636 0.8427 0.6525 -0.0307 -0.0777 0.0819 177 GLU A CG 1316 C CD . GLU A 173 ? 0.9082 1.0824 0.8599 -0.0461 -0.0722 0.0770 177 GLU A CD 1317 O OE1 . GLU A 173 ? 0.7813 0.9600 0.7090 -0.0591 -0.0681 0.0737 177 GLU A OE1 1318 O OE2 . GLU A 173 ? 0.7884 0.9538 0.7358 -0.0466 -0.0710 0.0760 177 GLU A OE2 1319 N N . PRO A 174 ? 0.3949 0.5741 0.4346 0.0165 -0.0405 0.0491 178 PRO A N 1320 C CA . PRO A 174 ? 0.3892 0.5541 0.4374 0.0257 -0.0341 0.0419 178 PRO A CA 1321 C C . PRO A 174 ? 0.4330 0.5858 0.4647 0.0168 -0.0418 0.0457 178 PRO A C 1322 O O . PRO A 174 ? 0.4230 0.5806 0.4329 0.0041 -0.0478 0.0506 178 PRO A O 1323 C CB . PRO A 174 ? 0.4008 0.5663 0.4333 0.0311 -0.0177 0.0259 178 PRO A CB 1324 C CG . PRO A 174 ? 0.4470 0.6255 0.4667 0.0270 -0.0156 0.0262 178 PRO A CG 1325 C CD . PRO A 174 ? 0.3992 0.5830 0.4138 0.0151 -0.0289 0.0381 178 PRO A CD 1326 N N . GLN A 175 ? 0.3986 0.5338 0.4404 0.0219 -0.0397 0.0426 179 GLN A N 1327 C CA . GLN A 175 ? 0.4084 0.5286 0.4362 0.0125 -0.0456 0.0454 179 GLN A CA 1328 C C . GLN A 175 ? 0.4385 0.5569 0.4453 0.0106 -0.0345 0.0290 179 GLN A C 1329 O O . GLN A 175 ? 0.4553 0.5636 0.4669 0.0185 -0.0240 0.0172 179 GLN A O 1330 C CB . GLN A 175 ? 0.4507 0.5483 0.5048 0.0188 -0.0506 0.0530 179 GLN A CB 1331 C CG . GLN A 175 ? 0.7337 0.8087 0.7739 0.0083 -0.0558 0.0561 179 GLN A CG 1332 C CD . GLN A 175 ? 1.0652 1.1155 1.1345 0.0154 -0.0636 0.0687 179 GLN A CD 1333 O OE1 . GLN A 175 ? 1.0237 1.0706 1.0978 0.0092 -0.0813 0.0897 179 GLN A OE1 1334 N NE2 . GLN A 175 ? 0.9806 1.0115 1.0698 0.0281 -0.0504 0.0567 179 GLN A NE2 1335 N N . ILE A 176 ? 0.3478 0.4774 0.3321 -0.0006 -0.0362 0.0280 180 ILE A N 1336 C CA . ILE A 176 ? 0.3283 0.4619 0.2975 -0.0034 -0.0297 0.0155 180 ILE A CA 1337 C C . ILE A 176 ? 0.3788 0.4935 0.3437 -0.0120 -0.0319 0.0129 180 ILE A C 1338 O O . ILE A 176 ? 0.3973 0.5081 0.3576 -0.0238 -0.0390 0.0212 180 ILE A O 1339 C CB . ILE A 176 ? 0.3465 0.5035 0.3030 -0.0092 -0.0289 0.0148 180 ILE A CB 1340 C CG1 . ILE A 176 ? 0.3333 0.5024 0.2910 0.0006 -0.0233 0.0133 180 ILE A CG1 1341 C CG2 . ILE A 176 ? 0.3440 0.5088 0.2917 -0.0148 -0.0276 0.0064 180 ILE A CG2 1342 C CD1 . ILE A 176 ? 0.3990 0.5853 0.3495 -0.0033 -0.0206 0.0142 180 ILE A CD1 1343 N N . ILE A 177 ? 0.3238 0.4243 0.2862 -0.0087 -0.0248 0.0007 181 ILE A N 1344 C CA . ILE A 177 ? 0.3367 0.4154 0.2908 -0.0194 -0.0252 -0.0048 181 ILE A CA 1345 C C . ILE A 177 ? 0.3847 0.4836 0.3232 -0.0345 -0.0304 -0.0055 181 ILE A C 1346 O O . ILE A 177 ? 0.3911 0.4854 0.3270 -0.0474 -0.0360 0.0009 181 ILE A O 1347 C CB . ILE A 177 ? 0.3833 0.4407 0.3311 -0.0163 -0.0139 -0.0211 181 ILE A CB 1348 C CG1 . ILE A 177 ? 0.3715 0.4187 0.3388 0.0006 -0.0034 -0.0239 181 ILE A CG1 1349 C CG2 . ILE A 177 ? 0.4255 0.4533 0.3643 -0.0291 -0.0134 -0.0271 181 ILE A CG2 1350 C CD1 . ILE A 177 ? 0.4371 0.4616 0.4306 0.0080 -0.0034 -0.0168 181 ILE A CD1 1351 N N . PHE A 178 ? 0.3252 0.4483 0.2564 -0.0327 -0.0289 -0.0116 182 PHE A N 1352 C CA . PHE A 178 ? 0.3160 0.4658 0.2428 -0.0433 -0.0337 -0.0115 182 PHE A CA 1353 C C . PHE A 178 ? 0.3859 0.5635 0.3140 -0.0347 -0.0333 -0.0124 182 PHE A C 1354 O O . PHE A 178 ? 0.3772 0.5498 0.3021 -0.0230 -0.0292 -0.0148 182 PHE A O 1355 C CB . PHE A 178 ? 0.3525 0.4940 0.2679 -0.0599 -0.0369 -0.0192 182 PHE A CB 1356 C CG . PHE A 178 ? 0.3774 0.5117 0.2768 -0.0616 -0.0359 -0.0310 182 PHE A CG 1357 C CD1 . PHE A 178 ? 0.3963 0.5581 0.2916 -0.0600 -0.0407 -0.0317 182 PHE A CD1 1358 C CD2 . PHE A 178 ? 0.4310 0.5294 0.3175 -0.0676 -0.0305 -0.0412 182 PHE A CD2 1359 C CE1 . PHE A 178 ? 0.4283 0.5820 0.3015 -0.0657 -0.0418 -0.0410 182 PHE A CE1 1360 C CE2 . PHE A 178 ? 0.4871 0.5760 0.3511 -0.0738 -0.0279 -0.0540 182 PHE A CE2 1361 C CZ . PHE A 178 ? 0.4562 0.5734 0.3111 -0.0741 -0.0346 -0.0531 182 PHE A CZ 1362 N N . CYS A 179 ? 0.3616 0.5679 0.2967 -0.0409 -0.0369 -0.0099 183 CYS A N 1363 C CA . CYS A 179 ? 0.3610 0.5955 0.3030 -0.0341 -0.0390 -0.0090 183 CYS A CA 1364 C C . CYS A 179 ? 0.3808 0.6450 0.3354 -0.0456 -0.0451 -0.0084 183 CYS A C 1365 O O . CYS A 179 ? 0.3663 0.6431 0.3329 -0.0534 -0.0415 -0.0061 183 CYS A O 1366 C CB . CYS A 179 ? 0.3620 0.6040 0.3122 -0.0190 -0.0327 -0.0043 183 CYS A CB 1367 S SG . CYS A 179 ? 0.4100 0.6649 0.3729 -0.0228 -0.0252 -0.0001 183 CYS A SG 1368 N N . ARG A 180 ? 0.3368 0.6109 0.2861 -0.0501 -0.0546 -0.0106 184 ARG A N 1369 C CA . ARG A 180 ? 0.3388 0.6444 0.3023 -0.0634 -0.0642 -0.0096 184 ARG A CA 1370 C C . ARG A 180 ? 0.3833 0.7132 0.3518 -0.0583 -0.0766 -0.0050 184 ARG A C 1371 O O . ARG A 180 ? 0.3938 0.7058 0.3398 -0.0523 -0.0795 -0.0056 184 ARG A O 1372 C CB . ARG A 180 ? 0.3759 0.6633 0.3216 -0.0854 -0.0684 -0.0168 184 ARG A CB 1373 C CG . ARG A 180 ? 0.5214 0.7806 0.4354 -0.0900 -0.0726 -0.0246 184 ARG A CG 1374 C CD . ARG A 180 ? 0.6022 0.8348 0.4973 -0.1114 -0.0727 -0.0339 184 ARG A CD 1375 N NE . ARG A 180 ? 0.6125 0.8095 0.4752 -0.1144 -0.0698 -0.0446 184 ARG A NE 1376 C CZ . ARG A 180 ? 0.7712 0.9294 0.6142 -0.1274 -0.0634 -0.0556 184 ARG A CZ 1377 N NH1 . ARG A 180 ? 0.6012 0.7498 0.4523 -0.1388 -0.0618 -0.0550 184 ARG A NH1 1378 N NH2 . ARG A 180 ? 0.5636 0.6894 0.3776 -0.1300 -0.0567 -0.0678 184 ARG A NH2 1379 N N . SER A 181 ? 0.3282 0.6993 0.3266 -0.0624 -0.0846 0.0004 185 SER A N 1380 C CA . SER A 181 ? 0.3354 0.7345 0.3445 -0.0590 -0.1013 0.0087 185 SER A CA 1381 C C . SER A 181 ? 0.4472 0.8416 0.4302 -0.0824 -0.1167 0.0043 185 SER A C 1382 O O . SER A 181 ? 0.4541 0.8438 0.4325 -0.1017 -0.1150 -0.0032 185 SER A O 1383 C CB . SER A 181 ? 0.3550 0.8036 0.4152 -0.0538 -0.1035 0.0165 185 SER A CB 1384 O OG . SER A 181 ? 0.4643 0.9423 0.5412 -0.0486 -0.1231 0.0283 185 SER A OG 1385 N N . GLU A 182 ? 0.4549 0.8460 0.4155 -0.0833 -0.1310 0.0086 186 GLU A N 1386 C CA . GLU A 182 ? 0.5073 0.8914 0.4352 -0.1091 -0.1459 0.0032 186 GLU A CA 1387 C C . GLU A 182 ? 0.5961 1.0188 0.5337 -0.1150 -0.1728 0.0174 186 GLU A C 1388 O O . GLU A 182 ? 0.6276 1.0514 0.5387 -0.1404 -0.1891 0.0145 186 GLU A O 1389 C CB . GLU A 182 ? 0.5541 0.8842 0.4292 -0.1146 -0.1353 -0.0099 186 GLU A CB 1390 C CG . GLU A 182 ? 0.7052 1.0011 0.5733 -0.1188 -0.1161 -0.0235 186 GLU A CG 1391 C CD . GLU A 182 ? 1.0473 1.2915 0.8739 -0.1217 -0.1025 -0.0374 186 GLU A CD 1392 O OE1 . GLU A 182 ? 0.9631 1.1922 0.7813 -0.1045 -0.0935 -0.0363 186 GLU A OE1 1393 O OE2 . GLU A 182 ? 1.0254 1.2435 0.8298 -0.1415 -0.0991 -0.0502 186 GLU A OE2 1394 N N . ALA A 183 ? 0.5456 0.9995 0.5227 -0.0920 -0.1779 0.0331 187 ALA A N 1395 C CA . ALA A 183 ? 0.5599 1.0563 0.5624 -0.0901 -0.2046 0.0522 187 ALA A CA 1396 C C . ALA A 183 ? 0.5844 1.1206 0.6550 -0.0648 -0.1988 0.0632 187 ALA A C 1397 O O . ALA A 183 ? 0.5477 1.0739 0.6345 -0.0527 -0.1738 0.0543 187 ALA A O 1398 C CB . ALA A 183 ? 0.5964 1.0689 0.5585 -0.0850 -0.2156 0.0613 187 ALA A CB 1399 N N . ALA A 184 ? 0.5585 1.1395 0.6697 -0.0578 -0.2217 0.0825 188 ALA A N 1400 C CA . ALA A 184 ? 0.5322 1.1523 0.7147 -0.0324 -0.2149 0.0927 188 ALA A CA 1401 C C . ALA A 184 ? 0.5570 1.1472 0.7381 -0.0024 -0.1979 0.0961 188 ALA A C 1402 O O . ALA A 184 ? 0.5152 1.1188 0.7424 0.0177 -0.1787 0.0950 188 ALA A O 1403 C CB . ALA A 184 ? 0.5593 1.2358 0.7902 -0.0323 -0.2464 0.1143 188 ALA A CB 1404 N N . HIS A 185 ? 0.5346 1.0827 0.6604 -0.0019 -0.2029 0.0987 189 HIS A N 1405 C CA . HIS A 185 ? 0.5193 1.0348 0.6357 0.0221 -0.1884 0.1022 189 HIS A CA 1406 C C . HIS A 185 ? 0.5402 1.0024 0.5970 0.0151 -0.1695 0.0854 189 HIS A C 1407 O O . HIS A 185 ? 0.5444 0.9754 0.5780 0.0275 -0.1624 0.0887 189 HIS A O 1408 C CB . HIS A 185 ? 0.5583 1.0772 0.6724 0.0318 -0.2137 0.1261 189 HIS A CB 1409 C CG . HIS A 185 ? 0.6066 1.1815 0.7805 0.0362 -0.2391 0.1458 189 HIS A CG 1410 N ND1 . HIS A 185 ? 0.6076 1.2134 0.8545 0.0621 -0.2296 0.1528 189 HIS A ND1 1411 C CD2 . HIS A 185 ? 0.6519 1.2579 0.8244 0.0166 -0.2725 0.1587 189 HIS A CD2 1412 C CE1 . HIS A 185 ? 0.6113 1.2688 0.9052 0.0602 -0.2578 0.1711 189 HIS A CE1 1413 N NE2 . HIS A 185 ? 0.6431 1.3037 0.8936 0.0321 -0.2863 0.1762 189 HIS A NE2 1414 N N . GLN A 186 ? 0.4703 0.9220 0.5055 -0.0045 -0.1608 0.0682 190 GLN A N 1415 C CA . GLN A 186 ? 0.4649 0.8693 0.4521 -0.0100 -0.1435 0.0532 190 GLN A CA 1416 C C . GLN A 186 ? 0.4726 0.8653 0.4642 -0.0142 -0.1224 0.0373 190 GLN A C 1417 O O . GLN A 186 ? 0.4588 0.8766 0.4774 -0.0225 -0.1223 0.0344 190 GLN A O 1418 C CB . GLN A 186 ? 0.5242 0.9046 0.4559 -0.0300 -0.1559 0.0504 190 GLN A CB 1419 C CG . GLN A 186 ? 0.7154 1.0784 0.6180 -0.0544 -0.1514 0.0328 190 GLN A CG 1420 C CD . GLN A 186 ? 0.8399 1.1573 0.7112 -0.0535 -0.1281 0.0168 190 GLN A CD 1421 O OE1 . GLN A 186 ? 0.7340 1.0373 0.6013 -0.0636 -0.1179 0.0036 190 GLN A OE1 1422 N NE2 . GLN A 186 ? 0.7313 1.0246 0.5824 -0.0416 -0.1195 0.0186 190 GLN A NE2 1423 N N . GLY A 187 ? 0.4134 0.7684 0.3783 -0.0092 -0.1056 0.0287 191 GLY A N 1424 C CA . GLY A 187 ? 0.3916 0.7287 0.3547 -0.0126 -0.0881 0.0167 191 GLY A CA 1425 C C . GLY A 187 ? 0.4435 0.7397 0.3706 -0.0128 -0.0778 0.0085 191 GLY A C 1426 O O . GLY A 187 ? 0.4545 0.7369 0.3673 -0.0028 -0.0754 0.0121 191 GLY A O 1427 N N . VAL A 188 ? 0.3824 0.6588 0.2972 -0.0242 -0.0709 -0.0022 192 VAL A N 1428 C CA . VAL A 188 ? 0.3778 0.6178 0.2676 -0.0233 -0.0594 -0.0108 192 VAL A CA 1429 C C . VAL A 188 ? 0.3629 0.5899 0.2660 -0.0176 -0.0468 -0.0133 192 VAL A C 1430 O O . VAL A 188 ? 0.3445 0.5789 0.2614 -0.0245 -0.0473 -0.0132 192 VAL A O 1431 C CB . VAL A 188 ? 0.4710 0.6908 0.3294 -0.0410 -0.0624 -0.0212 192 VAL A CB 1432 C CG1 . VAL A 188 ? 0.4787 0.6624 0.3265 -0.0418 -0.0467 -0.0331 192 VAL A CG1 1433 C CG2 . VAL A 188 ? 0.5001 0.7178 0.3303 -0.0441 -0.0700 -0.0189 192 VAL A CG2 1434 N N . ILE A 189 ? 0.2943 0.5033 0.1928 -0.0067 -0.0364 -0.0142 193 ILE A N 1435 C CA . ILE A 189 ? 0.2773 0.4735 0.1872 -0.0021 -0.0275 -0.0147 193 ILE A CA 1436 C C . ILE A 189 ? 0.3547 0.5224 0.2537 -0.0021 -0.0189 -0.0230 193 ILE A C 1437 O O . ILE A 189 ? 0.3582 0.5171 0.2427 0.0013 -0.0134 -0.0270 193 ILE A O 1438 C CB . ILE A 189 ? 0.2945 0.4998 0.2176 0.0095 -0.0227 -0.0077 193 ILE A CB 1439 C CG1 . ILE A 189 ? 0.2919 0.4860 0.2246 0.0098 -0.0179 -0.0061 193 ILE A CG1 1440 C CG2 . ILE A 189 ? 0.3076 0.5090 0.2209 0.0190 -0.0189 -0.0064 193 ILE A CG2 1441 C CD1 . ILE A 189 ? 0.3932 0.5951 0.3340 0.0145 -0.0143 -0.0005 193 ILE A CD1 1442 N N . THR A 190 ? 0.3250 0.4771 0.2315 -0.0065 -0.0169 -0.0255 194 THR A N 1443 C CA . THR A 190 ? 0.3428 0.4674 0.2492 -0.0039 -0.0067 -0.0334 194 THR A CA 1444 C C . THR A 190 ? 0.3770 0.4959 0.3081 0.0028 -0.0060 -0.0257 194 THR A C 1445 O O . THR A 190 ? 0.3494 0.4741 0.2871 -0.0028 -0.0141 -0.0177 194 THR A O 1446 C CB . THR A 190 ? 0.4995 0.6037 0.3874 -0.0167 -0.0049 -0.0454 194 THR A CB 1447 O OG1 . THR A 190 ? 0.5525 0.6291 0.4403 -0.0119 0.0103 -0.0561 194 THR A OG1 1448 C CG2 . THR A 190 ? 0.4827 0.5820 0.3757 -0.0275 -0.0121 -0.0432 194 THR A CG2 1449 N N . TRP A 191 ? 0.3520 0.4615 0.2967 0.0134 0.0032 -0.0269 195 TRP A N 1450 C CA . TRP A 191 ? 0.3440 0.4522 0.3159 0.0204 0.0007 -0.0167 195 TRP A CA 1451 C C . TRP A 191 ? 0.3859 0.4759 0.3803 0.0301 0.0118 -0.0217 195 TRP A C 1452 O O . TRP A 191 ? 0.3834 0.4597 0.3690 0.0309 0.0257 -0.0360 195 TRP A O 1453 C CB . TRP A 191 ? 0.3078 0.4379 0.2842 0.0249 -0.0021 -0.0082 195 TRP A CB 1454 C CG . TRP A 191 ? 0.3210 0.4545 0.2940 0.0318 0.0091 -0.0148 195 TRP A CG 1455 C CD1 . TRP A 191 ? 0.3585 0.4906 0.3518 0.0397 0.0177 -0.0155 195 TRP A CD1 1456 C CD2 . TRP A 191 ? 0.3223 0.4604 0.2704 0.0299 0.0127 -0.0206 195 TRP A CD2 1457 N NE1 . TRP A 191 ? 0.3536 0.4879 0.3326 0.0412 0.0285 -0.0226 195 TRP A NE1 1458 C CE2 . TRP A 191 ? 0.3764 0.5126 0.3256 0.0354 0.0245 -0.0247 195 TRP A CE2 1459 C CE3 . TRP A 191 ? 0.3388 0.4846 0.2664 0.0237 0.0058 -0.0209 195 TRP A CE3 1460 C CZ2 . TRP A 191 ? 0.3771 0.5137 0.3012 0.0338 0.0292 -0.0282 195 TRP A CZ2 1461 C CZ3 . TRP A 191 ? 0.3684 0.5174 0.2763 0.0242 0.0082 -0.0230 195 TRP A CZ3 1462 C CH2 . TRP A 191 ? 0.3846 0.5264 0.2876 0.0286 0.0196 -0.0263 195 TRP A CH2 1463 N N . ASN A 192 ? 0.3376 0.4292 0.3621 0.0365 0.0057 -0.0093 196 ASN A N 1464 C CA . ASN A 192 ? 0.3479 0.4305 0.4083 0.0489 0.0138 -0.0094 196 ASN A CA 1465 C C . ASN A 192 ? 0.3888 0.4968 0.4671 0.0544 0.0114 -0.0008 196 ASN A C 1466 O O . ASN A 192 ? 0.3674 0.4911 0.4369 0.0479 -0.0024 0.0111 196 ASN A O 1467 C CB . ASN A 192 ? 0.3374 0.4037 0.4229 0.0511 0.0032 0.0030 196 ASN A CB 1468 C CG . ASN A 192 ? 0.4207 0.4550 0.4956 0.0465 0.0085 -0.0062 196 ASN A CG 1469 O OD1 . ASN A 192 ? 0.2813 0.2994 0.3435 0.0461 0.0256 -0.0253 196 ASN A OD1 1470 N ND2 . ASN A 192 ? 0.3207 0.3421 0.3981 0.0408 -0.0058 0.0072 196 ASN A ND2 1471 N N . PRO A 193 ? 0.3509 0.4626 0.4530 0.0640 0.0263 -0.0077 197 PRO A N 1472 C CA . PRO A 193 ? 0.3318 0.4686 0.4509 0.0664 0.0243 -0.0001 197 PRO A CA 1473 C C . PRO A 193 ? 0.3928 0.5435 0.5431 0.0671 0.0046 0.0204 197 PRO A C 1474 O O . PRO A 193 ? 0.4170 0.5563 0.5913 0.0716 -0.0037 0.0291 197 PRO A O 1475 C CB . PRO A 193 ? 0.3639 0.4999 0.5072 0.0755 0.0468 -0.0132 197 PRO A CB 1476 C CG . PRO A 193 ? 0.4501 0.5601 0.6069 0.0817 0.0567 -0.0222 197 PRO A CG 1477 C CD . PRO A 193 ? 0.3982 0.4913 0.5112 0.0709 0.0482 -0.0247 197 PRO A CD 1478 N N . PRO A 194 ? 0.3317 0.5046 0.4808 0.0613 -0.0035 0.0290 198 PRO A N 1479 C CA . PRO A 194 ? 0.3288 0.5158 0.5035 0.0580 -0.0245 0.0493 198 PRO A CA 1480 C C . PRO A 194 ? 0.3921 0.5904 0.6273 0.0708 -0.0240 0.0561 198 PRO A C 1481 O O . PRO A 194 ? 0.3893 0.5880 0.6454 0.0811 -0.0026 0.0420 198 PRO A O 1482 C CB . PRO A 194 ? 0.3347 0.5387 0.4851 0.0460 -0.0283 0.0513 198 PRO A CB 1483 C CG . PRO A 194 ? 0.3796 0.5840 0.5177 0.0498 -0.0070 0.0345 198 PRO A CG 1484 C CD . PRO A 194 ? 0.3343 0.5176 0.4566 0.0557 0.0052 0.0213 198 PRO A CD 1485 N N . GLN A 195 ? 0.3568 0.5654 0.6208 0.0690 -0.0475 0.0783 199 GLN A N 1486 C CA . GLN A 195 ? 0.3682 0.5908 0.6994 0.0826 -0.0524 0.0899 199 GLN A CA 1487 C C . GLN A 195 ? 0.4361 0.6929 0.8065 0.0846 -0.0476 0.0903 199 GLN A C 1488 O O . GLN A 195 ? 0.4474 0.7147 0.8785 0.1007 -0.0380 0.0899 199 GLN A O 1489 C CB . GLN A 195 ? 0.4004 0.6193 0.7503 0.0805 -0.0824 0.1168 199 GLN A CB 1490 C CG . GLN A 195 ? 0.5934 0.7864 0.9780 0.0979 -0.0782 0.1186 199 GLN A CG 1491 C CD . GLN A 195 ? 0.9363 1.1294 1.3542 0.0990 -0.1096 0.1499 199 GLN A CD 1492 O OE1 . GLN A 195 ? 0.8810 1.0668 1.2603 0.0814 -0.1332 0.1666 199 GLN A OE1 1493 N NE2 . GLN A 195 ? 0.9100 1.1106 1.4015 0.1195 -0.1100 0.1592 199 GLN A NE2 1494 N N . ARG A 196 ? 0.3748 0.6484 0.7145 0.0681 -0.0528 0.0909 200 ARG A N 1495 C CA . ARG A 196 ? 0.3559 0.6621 0.7285 0.0654 -0.0492 0.0915 200 ARG A CA 1496 C C . ARG A 196 ? 0.3714 0.6753 0.7312 0.0687 -0.0165 0.0672 200 ARG A C 1497 O O . ARG A 196 ? 0.3724 0.6499 0.6995 0.0738 0.0016 0.0507 200 ARG A O 1498 C CB . ARG A 196 ? 0.3634 0.6857 0.7095 0.0429 -0.0721 0.1052 200 ARG A CB 1499 C CG . ARG A 196 ? 0.4795 0.8351 0.8802 0.0390 -0.0976 0.1286 200 ARG A CG 1500 C CD . ARG A 196 ? 0.5717 0.9307 0.9342 0.0138 -0.1275 0.1462 200 ARG A CD 1501 N NE . ARG A 196 ? 0.6932 1.0321 1.0412 0.0130 -0.1483 0.1622 200 ARG A NE 1502 C CZ . ARG A 196 ? 0.8410 1.1515 1.1259 0.0022 -0.1476 0.1570 200 ARG A CZ 1503 N NH1 . ARG A 196 ? 0.6236 0.9232 0.8577 -0.0063 -0.1283 0.1368 200 ARG A NH1 1504 N NH2 . ARG A 196 ? 0.6698 0.9628 0.9445 -0.0003 -0.1659 0.1727 200 ARG A NH2 1505 N N . SER A 197 ? 0.2963 0.6281 0.6815 0.0636 -0.0099 0.0660 201 SER A N 1506 C CA . SER A 197 ? 0.2773 0.6079 0.6484 0.0627 0.0200 0.0457 201 SER A CA 1507 C C . SER A 197 ? 0.2899 0.6055 0.5920 0.0466 0.0202 0.0401 201 SER A C 1508 O O . SER A 197 ? 0.2829 0.6061 0.5678 0.0321 0.0005 0.0515 201 SER A O 1509 C CB . SER A 197 ? 0.3187 0.6859 0.7468 0.0616 0.0269 0.0478 201 SER A CB 1510 O OG . SER A 197 ? 0.4578 0.8417 0.9598 0.0793 0.0274 0.0539 201 SER A OG 1511 N N . PHE A 198 ? 0.2277 0.5207 0.4901 0.0484 0.0423 0.0229 202 PHE A N 1512 C CA . PHE A 198 ? 0.2102 0.4863 0.4122 0.0371 0.0448 0.0176 202 PHE A CA 1513 C C . PHE A 198 ? 0.2582 0.5212 0.4366 0.0375 0.0717 0.0015 202 PHE A C 1514 O O . PHE A 198 ? 0.2481 0.5128 0.4515 0.0454 0.0905 -0.0082 202 PHE A O 1515 C CB . PHE A 198 ? 0.2251 0.4801 0.3884 0.0374 0.0317 0.0203 202 PHE A CB 1516 C CG . PHE A 198 ? 0.2483 0.4834 0.4020 0.0484 0.0414 0.0106 202 PHE A CG 1517 C CD1 . PHE A 198 ? 0.2916 0.5259 0.4802 0.0587 0.0376 0.0135 202 PHE A CD1 1518 C CD2 . PHE A 198 ? 0.2802 0.4956 0.3892 0.0473 0.0528 -0.0004 202 PHE A CD2 1519 C CE1 . PHE A 198 ? 0.3166 0.5286 0.4926 0.0659 0.0478 0.0026 202 PHE A CE1 1520 C CE2 . PHE A 198 ? 0.3288 0.5264 0.4252 0.0534 0.0597 -0.0094 202 PHE A CE2 1521 C CZ . PHE A 198 ? 0.3119 0.5067 0.4402 0.0618 0.0585 -0.0093 202 PHE A CZ 1522 N N . HIS A 199 ? 0.2224 0.4701 0.3520 0.0285 0.0743 -0.0010 203 HIS A N 1523 C CA . HIS A 199 ? 0.2403 0.4727 0.3403 0.0262 0.0960 -0.0124 203 HIS A CA 1524 C C . HIS A 199 ? 0.3102 0.5155 0.3618 0.0293 0.0968 -0.0172 203 HIS A C 1525 O O . HIS A 199 ? 0.3269 0.5190 0.3596 0.0294 0.1135 -0.0270 203 HIS A O 1526 C CB . HIS A 199 ? 0.2538 0.4891 0.3412 0.0128 0.1015 -0.0106 203 HIS A CB 1527 C CG . HIS A 199 ? 0.2901 0.5554 0.4270 0.0071 0.1052 -0.0082 203 HIS A CG 1528 N ND1 . HIS A 199 ? 0.3130 0.5884 0.4497 -0.0077 0.0987 -0.0019 203 HIS A ND1 1529 C CD2 . HIS A 199 ? 0.3051 0.5928 0.4954 0.0142 0.1144 -0.0113 203 HIS A CD2 1530 C CE1 . HIS A 199 ? 0.2992 0.6068 0.4898 -0.0103 0.1020 -0.0001 203 HIS A CE1 1531 N NE2 . HIS A 199 ? 0.2993 0.6162 0.5269 0.0041 0.1119 -0.0053 203 HIS A NE2 1532 N N . ASN A 200 ? 0.2512 0.4497 0.2825 0.0299 0.0792 -0.0103 204 ASN A N 1533 C CA . ASN A 200 ? 0.2543 0.4335 0.2467 0.0327 0.0762 -0.0123 204 ASN A CA 1534 C C . ASN A 200 ? 0.3023 0.4824 0.2906 0.0343 0.0582 -0.0055 204 ASN A C 1535 O O . ASN A 200 ? 0.2858 0.4770 0.2904 0.0304 0.0479 0.0014 204 ASN A O 1536 C CB . ASN A 200 ? 0.2525 0.4173 0.2089 0.0274 0.0822 -0.0115 204 ASN A CB 1537 C CG . ASN A 200 ? 0.5857 0.7381 0.5208 0.0242 0.0989 -0.0183 204 ASN A CG 1538 O OD1 . ASN A 200 ? 0.6174 0.7655 0.5501 0.0262 0.1067 -0.0265 204 ASN A OD1 1539 N ND2 . ASN A 200 ? 0.4417 0.5844 0.3563 0.0172 0.1054 -0.0152 204 ASN A ND2 1540 N N . PHE A 201 ? 0.2639 0.4328 0.2274 0.0375 0.0545 -0.0072 205 PHE A N 1541 C CA . PHE A 201 ? 0.2442 0.4144 0.2018 0.0381 0.0410 -0.0026 205 PHE A CA 1542 C C . PHE A 201 ? 0.3047 0.4682 0.2382 0.0378 0.0400 0.0003 205 PHE A C 1543 O O . PHE A 201 ? 0.3197 0.4732 0.2347 0.0388 0.0468 -0.0005 205 PHE A O 1544 C CB . PHE A 201 ? 0.2626 0.4284 0.2159 0.0412 0.0377 -0.0067 205 PHE A CB 1545 C CG . PHE A 201 ? 0.2723 0.4392 0.2511 0.0433 0.0380 -0.0092 205 PHE A CG 1546 C CD1 . PHE A 201 ? 0.2946 0.4691 0.2952 0.0424 0.0267 -0.0016 205 PHE A CD1 1547 C CD2 . PHE A 201 ? 0.3044 0.4617 0.2833 0.0454 0.0498 -0.0191 205 PHE A CD2 1548 C CE1 . PHE A 201 ? 0.3098 0.4822 0.3370 0.0462 0.0255 -0.0014 205 PHE A CE1 1549 C CE2 . PHE A 201 ? 0.3410 0.4953 0.3472 0.0494 0.0522 -0.0223 205 PHE A CE2 1550 C CZ . PHE A 201 ? 0.3064 0.4682 0.3391 0.0512 0.0391 -0.0122 205 PHE A CZ 1551 N N . THR A 202 ? 0.2565 0.4240 0.1902 0.0362 0.0324 0.0038 206 THR A N 1552 C CA . THR A 202 ? 0.2664 0.4278 0.1851 0.0382 0.0334 0.0055 206 THR A CA 1553 C C . THR A 202 ? 0.3352 0.5040 0.2557 0.0406 0.0261 0.0060 206 THR A C 1554 O O . THR A 202 ? 0.3345 0.5101 0.2623 0.0350 0.0219 0.0064 206 THR A O 1555 C CB . THR A 202 ? 0.3648 0.5219 0.2815 0.0313 0.0376 0.0063 206 THR A CB 1556 O OG1 . THR A 202 ? 0.3901 0.5428 0.3068 0.0277 0.0443 0.0059 206 THR A OG1 1557 C CG2 . THR A 202 ? 0.3401 0.4866 0.2449 0.0347 0.0424 0.0063 206 THR A CG2 1558 N N . LEU A 203 ? 0.2888 0.4573 0.2020 0.0468 0.0236 0.0068 207 LEU A N 1559 C CA . LEU A 203 ? 0.2774 0.4574 0.1965 0.0482 0.0166 0.0075 207 LEU A CA 1560 C C . LEU A 203 ? 0.3458 0.5278 0.2683 0.0544 0.0193 0.0104 207 LEU A C 1561 O O . LEU A 203 ? 0.3336 0.5052 0.2489 0.0607 0.0225 0.0141 207 LEU A O 1562 C CB . LEU A 203 ? 0.2779 0.4603 0.1904 0.0484 0.0097 0.0067 207 LEU A CB 1563 C CG . LEU A 203 ? 0.3235 0.5214 0.2438 0.0473 0.0007 0.0078 207 LEU A CG 1564 C CD1 . LEU A 203 ? 0.3120 0.5158 0.2429 0.0396 -0.0010 0.0047 207 LEU A CD1 1565 C CD2 . LEU A 203 ? 0.3475 0.5459 0.2548 0.0453 -0.0074 0.0082 207 LEU A CD2 1566 N N . CYS A 204 ? 0.3349 0.5285 0.2693 0.0521 0.0198 0.0086 208 CYS A N 1567 C CA . CYS A 204 ? 0.3565 0.5545 0.3019 0.0586 0.0261 0.0089 208 CYS A CA 1568 C C . CYS A 204 ? 0.3651 0.5856 0.3281 0.0591 0.0207 0.0092 208 CYS A C 1569 O O . CYS A 204 ? 0.3501 0.5787 0.3131 0.0489 0.0168 0.0065 208 CYS A O 1570 C CB . CYS A 204 ? 0.3853 0.5739 0.3267 0.0518 0.0386 0.0032 208 CYS A CB 1571 S SG . CYS A 204 ? 0.4589 0.6248 0.3815 0.0464 0.0437 0.0026 208 CYS A SG 1572 N N . TYR A 205 ? 0.2983 0.5295 0.2791 0.0705 0.0198 0.0137 209 TYR A N 1573 C CA . TYR A 205 ? 0.2743 0.5330 0.2800 0.0711 0.0154 0.0145 209 TYR A CA 1574 C C . TYR A 205 ? 0.2889 0.5539 0.3192 0.0793 0.0306 0.0114 209 TYR A C 1575 O O . TYR A 205 ? 0.2876 0.5425 0.3263 0.0933 0.0352 0.0157 209 TYR A O 1576 C CB . TYR A 205 ? 0.2953 0.5686 0.3064 0.0752 -0.0027 0.0234 209 TYR A CB 1577 C CG . TYR A 205 ? 0.3391 0.6037 0.3493 0.0887 -0.0087 0.0342 209 TYR A CG 1578 C CD1 . TYR A 205 ? 0.3780 0.6180 0.3571 0.0873 -0.0114 0.0370 209 TYR A CD1 1579 C CD2 . TYR A 205 ? 0.3560 0.6385 0.3984 0.1022 -0.0129 0.0432 209 TYR A CD2 1580 C CE1 . TYR A 205 ? 0.4160 0.6447 0.3888 0.0970 -0.0178 0.0488 209 TYR A CE1 1581 C CE2 . TYR A 205 ? 0.3882 0.6604 0.4292 0.1146 -0.0216 0.0569 209 TYR A CE2 1582 C CZ . TYR A 205 ? 0.5202 0.7636 0.5226 0.1107 -0.0245 0.0600 209 TYR A CZ 1583 O OH . TYR A 205 ? 0.5607 0.7903 0.5564 0.1204 -0.0334 0.0751 209 TYR A OH 1584 N N . ILE A 206 ? 0.2265 0.5035 0.2654 0.0692 0.0409 0.0031 210 ILE A N 1585 C CA . ILE A 206 ? 0.2322 0.5129 0.2910 0.0728 0.0617 -0.0046 210 ILE A CA 1586 C C . ILE A 206 ? 0.2892 0.6057 0.3895 0.0766 0.0646 -0.0050 210 ILE A C 1587 O O . ILE A 206 ? 0.2738 0.6083 0.3754 0.0620 0.0626 -0.0082 210 ILE A O 1588 C CB . ILE A 206 ? 0.2755 0.5367 0.3058 0.0553 0.0765 -0.0154 210 ILE A CB 1589 C CG1 . ILE A 206 ? 0.2787 0.5096 0.2768 0.0527 0.0731 -0.0139 210 ILE A CG1 1590 C CG2 . ILE A 206 ? 0.3089 0.5689 0.3526 0.0554 0.1025 -0.0270 210 ILE A CG2 1591 C CD1 . ILE A 206 ? 0.3066 0.5319 0.2791 0.0362 0.0622 -0.0125 210 ILE A CD1 1592 N N . LYS A 207 ? 0.2685 0.5946 0.4051 0.0961 0.0701 -0.0012 211 LYS A N 1593 C CA . LYS A 207 ? 0.2737 0.6379 0.4620 0.1040 0.0742 -0.0004 211 LYS A CA 1594 C C . LYS A 207 ? 0.3827 0.7395 0.5931 0.1117 0.1060 -0.0129 211 LYS A C 1595 O O . LYS A 207 ? 0.3937 0.7455 0.6339 0.1336 0.1122 -0.0084 211 LYS A O 1596 C CB . LYS A 207 ? 0.2958 0.6794 0.5138 0.1218 0.0509 0.0174 211 LYS A CB 1597 C CG . LYS A 207 ? 0.3850 0.8162 0.6637 0.1299 0.0485 0.0221 211 LYS A CG 1598 C CD . LYS A 207 ? 0.5246 0.9668 0.8373 0.1530 0.0299 0.0414 211 LYS A CD 1599 C CE . LYS A 207 ? 0.7366 1.2227 1.1243 0.1686 0.0357 0.0454 211 LYS A CE 1600 N NZ . LYS A 207 ? 0.8831 1.3542 1.2989 0.1842 0.0704 0.0334 211 LYS A NZ 1601 N N . GLU A 208 ? 0.3691 0.7219 0.5618 0.0921 0.1268 -0.0286 212 GLU A N 1602 C CA . GLU A 208 ? 0.3980 0.7391 0.5980 0.0905 0.1619 -0.0457 212 GLU A CA 1603 C C . GLU A 208 ? 0.4666 0.7610 0.6346 0.0949 0.1725 -0.0503 212 GLU A C 1604 O O . GLU A 208 ? 0.4520 0.7209 0.5702 0.0801 0.1626 -0.0495 212 GLU A O 1605 C CB . GLU A 208 ? 0.4276 0.8026 0.6967 0.1090 0.1783 -0.0481 212 GLU A CB 1606 C CG . GLU A 208 ? 0.6170 1.0429 0.9232 0.1035 0.1667 -0.0428 212 GLU A CG 1607 C CD . GLU A 208 ? 1.0384 1.4912 1.3737 0.1187 0.1319 -0.0215 212 GLU A CD 1608 O OE1 . GLU A 208 ? 1.0773 1.5301 1.4462 0.1444 0.1266 -0.0107 212 GLU A OE1 1609 O OE2 . GLU A 208 ? 0.9850 1.4555 1.3057 0.1034 0.1095 -0.0150 212 GLU A OE2 1610 N N . THR A 209 ? 0.4516 0.7349 0.6512 0.1155 0.1917 -0.0542 213 THR A N 1611 C CA . THR A 209 ? 0.4799 0.7164 0.6534 0.1203 0.2041 -0.0591 213 THR A CA 1612 C C . THR A 209 ? 0.5151 0.7352 0.6713 0.1307 0.1759 -0.0406 213 THR A C 1613 O O . THR A 209 ? 0.5283 0.7092 0.6494 0.1267 0.1808 -0.0435 213 THR A O 1614 C CB . THR A 209 ? 0.6908 0.9187 0.9081 0.1404 0.2350 -0.0690 213 THR A CB 1615 O OG1 . THR A 209 ? 0.7241 0.9904 1.0083 0.1663 0.2238 -0.0545 213 THR A OG1 1616 C CG2 . THR A 209 ? 0.7109 0.9353 0.9225 0.1227 0.2727 -0.0943 213 THR A CG2 1617 N N . GLU A 210 ? 0.4443 0.6941 0.6223 0.1409 0.1473 -0.0225 214 GLU A N 1618 C CA . GLU A 210 ? 0.4301 0.6690 0.5904 0.1480 0.1201 -0.0046 214 GLU A CA 1619 C C . GLU A 210 ? 0.4570 0.6884 0.5672 0.1260 0.1052 -0.0051 214 GLU A C 1620 O O . GLU A 210 ? 0.4403 0.6903 0.5428 0.1095 0.1034 -0.0111 214 GLU A O 1621 C CB . GLU A 210 ? 0.4360 0.7104 0.6372 0.1640 0.0960 0.0139 214 GLU A CB 1622 C CG . GLU A 210 ? 0.6154 0.8978 0.8736 0.1908 0.1038 0.0212 214 GLU A CG 1623 C CD . GLU A 210 ? 1.0162 1.3303 1.3253 0.1946 0.1262 0.0089 214 GLU A CD 1624 O OE1 . GLU A 210 ? 1.0238 1.3839 1.3640 0.1919 0.1128 0.0142 214 GLU A OE1 1625 O OE2 . GLU A 210 ? 1.0067 1.2990 1.3233 0.1980 0.1588 -0.0074 214 GLU A OE2 1626 N N . LYS A 211 ? 0.4067 0.6104 0.4856 0.1260 0.0955 0.0019 215 LYS A N 1627 C CA . LYS A 211 ? 0.3831 0.5785 0.4217 0.1089 0.0829 0.0023 215 LYS A CA 1628 C C . LYS A 211 ? 0.4535 0.6289 0.4743 0.1158 0.0703 0.0143 215 LYS A C 1629 O O . LYS A 211 ? 0.4818 0.6295 0.4984 0.1237 0.0800 0.0157 215 LYS A O 1630 C CB . LYS A 211 ? 0.4061 0.5812 0.4147 0.0901 0.0987 -0.0118 215 LYS A CB 1631 C CG . LYS A 211 ? 0.4411 0.6066 0.4156 0.0750 0.0865 -0.0098 215 LYS A CG 1632 C CD . LYS A 211 ? 0.5580 0.7084 0.5072 0.0552 0.0984 -0.0210 215 LYS A CD 1633 C CE . LYS A 211 ? 0.6717 0.8192 0.5974 0.0408 0.0853 -0.0177 215 LYS A CE 1634 N NZ . LYS A 211 ? 0.8029 0.9329 0.7033 0.0215 0.0944 -0.0256 215 LYS A NZ 1635 N N . ASP A 212 ? 0.3897 0.5760 0.3972 0.1108 0.0508 0.0219 216 ASP A N 1636 C CA . ASP A 212 ? 0.3904 0.5583 0.3745 0.1123 0.0405 0.0316 216 ASP A CA 1637 C C . ASP A 212 ? 0.4110 0.5782 0.3688 0.0963 0.0356 0.0266 216 ASP A C 1638 O O . ASP A 212 ? 0.3626 0.5500 0.3245 0.0890 0.0283 0.0234 216 ASP A O 1639 C CB . ASP A 212 ? 0.4209 0.6015 0.4165 0.1235 0.0218 0.0473 216 ASP A CB 1640 C CG . ASP A 212 ? 0.5305 0.7228 0.5665 0.1416 0.0229 0.0546 216 ASP A CG 1641 O OD1 . ASP A 212 ? 0.5281 0.7503 0.5948 0.1427 0.0242 0.0500 216 ASP A OD1 1642 O OD2 . ASP A 212 ? 0.5975 0.7690 0.6371 0.1549 0.0232 0.0654 216 ASP A OD2 1643 N N . CYS A 213 ? 0.4049 0.5484 0.3390 0.0907 0.0409 0.0256 217 CYS A N 1644 C CA . CYS A 213 ? 0.4059 0.5492 0.3225 0.0777 0.0382 0.0213 217 CYS A CA 1645 C C . CYS A 213 ? 0.4385 0.5724 0.3361 0.0772 0.0319 0.0277 217 CYS A C 1646 O O . CYS A 213 ? 0.4511 0.5730 0.3419 0.0849 0.0291 0.0372 217 CYS A O 1647 C CB . CYS A 213 ? 0.4275 0.5597 0.3364 0.0667 0.0493 0.0132 217 CYS A CB 1648 S SG . CYS A 213 ? 0.4859 0.6286 0.4059 0.0597 0.0565 0.0042 217 CYS A SG 1649 N N . LEU A 214 ? 0.3654 0.5045 0.2550 0.0680 0.0298 0.0230 218 LEU A N 1650 C CA . LEU A 214 ? 0.3614 0.4927 0.2313 0.0642 0.0278 0.0249 218 LEU A CA 1651 C C . LEU A 214 ? 0.4200 0.5468 0.2867 0.0550 0.0374 0.0178 218 LEU A C 1652 O O . LEU A 214 ? 0.4096 0.5383 0.2874 0.0513 0.0426 0.0140 218 LEU A O 1653 C CB . LEU A 214 ? 0.3501 0.4957 0.2190 0.0625 0.0166 0.0244 218 LEU A CB 1654 C CG . LEU A 214 ? 0.4130 0.5673 0.2846 0.0692 0.0035 0.0338 218 LEU A CG 1655 C CD1 . LEU A 214 ? 0.3950 0.5713 0.2947 0.0728 -0.0005 0.0318 218 LEU A CD1 1656 C CD2 . LEU A 214 ? 0.4693 0.6246 0.3195 0.0617 -0.0065 0.0352 218 LEU A CD2 1657 N N . ASN A 215 ? 0.3907 0.5126 0.2426 0.0501 0.0399 0.0158 219 ASN A N 1658 C CA . ASN A 215 ? 0.3820 0.5034 0.2375 0.0428 0.0507 0.0087 219 ASN A CA 1659 C C . ASN A 215 ? 0.4234 0.5461 0.2711 0.0394 0.0518 0.0024 219 ASN A C 1660 O O . ASN A 215 ? 0.4446 0.5561 0.2648 0.0361 0.0519 0.0042 219 ASN A O 1661 C CB . ASN A 215 ? 0.3957 0.5014 0.2370 0.0380 0.0617 0.0112 219 ASN A CB 1662 C CG . ASN A 215 ? 0.6369 0.7480 0.4967 0.0322 0.0690 0.0077 219 ASN A CG 1663 O OD1 . ASN A 215 ? 0.5014 0.6217 0.3780 0.0326 0.0639 0.0073 219 ASN A OD1 1664 N ND2 . ASN A 215 ? 0.5847 0.6897 0.4388 0.0243 0.0812 0.0058 219 ASN A ND2 1665 N N . LEU A 216 ? 0.3463 0.4801 0.2157 0.0392 0.0519 -0.0044 220 LEU A N 1666 C CA . LEU A 216 ? 0.3452 0.4763 0.2099 0.0360 0.0558 -0.0131 220 LEU A CA 1667 C C . LEU A 216 ? 0.3899 0.5216 0.2729 0.0340 0.0714 -0.0217 220 LEU A C 1668 O O . LEU A 216 ? 0.3671 0.5103 0.2804 0.0365 0.0717 -0.0197 220 LEU A O 1669 C CB . LEU A 216 ? 0.3243 0.4635 0.2011 0.0379 0.0445 -0.0145 220 LEU A CB 1670 C CG . LEU A 216 ? 0.3607 0.5069 0.2312 0.0400 0.0297 -0.0072 220 LEU A CG 1671 C CD1 . LEU A 216 ? 0.3546 0.5097 0.2414 0.0391 0.0218 -0.0093 220 LEU A CD1 1672 C CD2 . LEU A 216 ? 0.3732 0.5130 0.2144 0.0365 0.0243 -0.0047 220 LEU A CD2 1673 N N . ASP A 217 ? 0.3585 0.4788 0.2240 0.0285 0.0844 -0.0313 221 ASP A N 1674 C CA . ASP A 217 ? 0.3624 0.4826 0.2472 0.0271 0.1042 -0.0425 221 ASP A CA 1675 C C . ASP A 217 ? 0.3946 0.5249 0.3218 0.0349 0.1016 -0.0455 221 ASP A C 1676 O O . ASP A 217 ? 0.3947 0.5207 0.3186 0.0364 0.0911 -0.0461 221 ASP A O 1677 C CB . ASP A 217 ? 0.4218 0.5233 0.2714 0.0176 0.1189 -0.0546 221 ASP A CB 1678 C CG . ASP A 217 ? 0.5257 0.6257 0.3947 0.0157 0.1453 -0.0689 221 ASP A CG 1679 O OD1 . ASP A 217 ? 0.5426 0.6436 0.4074 0.0100 0.1598 -0.0695 221 ASP A OD1 1680 O OD2 . ASP A 217 ? 0.5799 0.6773 0.4707 0.0198 0.1529 -0.0797 221 ASP A OD2 1681 N N . LYS A 218 ? 0.3244 0.4679 0.2924 0.0388 0.1105 -0.0461 222 LYS A N 1682 C CA . LYS A 218 ? 0.2942 0.4480 0.3091 0.0473 0.1065 -0.0450 222 LYS A CA 1683 C C . LYS A 218 ? 0.3389 0.4766 0.3560 0.0505 0.1134 -0.0561 222 LYS A C 1684 O O . LYS A 218 ? 0.3218 0.4610 0.3660 0.0570 0.1027 -0.0514 222 LYS A O 1685 C CB . LYS A 218 ? 0.3137 0.4875 0.3757 0.0504 0.1156 -0.0433 222 LYS A CB 1686 C CG . LYS A 218 ? 0.5261 0.6977 0.5920 0.0473 0.1438 -0.0570 222 LYS A CG 1687 C CD . LYS A 218 ? 0.6914 0.8886 0.7968 0.0459 0.1496 -0.0521 222 LYS A CD 1688 C CE . LYS A 218 ? 0.8641 1.0815 1.0383 0.0567 0.1555 -0.0529 222 LYS A CE 1689 N NZ . LYS A 218 ? 0.9333 1.1774 1.1456 0.0526 0.1680 -0.0523 222 LYS A NZ 1690 N N . ASN A 219 ? 0.3192 0.4382 0.3028 0.0435 0.1306 -0.0706 223 ASN A N 1691 C CA . ASN A 219 ? 0.3402 0.4380 0.3168 0.0425 0.1413 -0.0852 223 ASN A CA 1692 C C . ASN A 219 ? 0.4104 0.4948 0.3514 0.0360 0.1249 -0.0843 223 ASN A C 1693 O O . ASN A 219 ? 0.4280 0.4942 0.3690 0.0349 0.1308 -0.0950 223 ASN A O 1694 C CB . ASN A 219 ? 0.3280 0.4108 0.2874 0.0351 0.1715 -0.1040 223 ASN A CB 1695 C CG . ASN A 219 ? 0.5922 0.6876 0.6072 0.0448 0.1918 -0.1093 223 ASN A CG 1696 O OD1 . ASN A 219 ? 0.5856 0.6779 0.6437 0.0557 0.1984 -0.1144 223 ASN A OD1 1697 N ND2 . ASN A 219 ? 0.4792 0.5914 0.5003 0.0418 0.1994 -0.1055 223 ASN A ND2 1698 N N . LEU A 220 ? 0.3600 0.4527 0.2733 0.0315 0.1058 -0.0724 224 LEU A N 1699 C CA . LEU A 220 ? 0.3721 0.4577 0.2594 0.0250 0.0903 -0.0714 224 LEU A CA 1700 C C . LEU A 220 ? 0.4262 0.5197 0.3417 0.0310 0.0740 -0.0625 224 LEU A C 1701 O O . LEU A 220 ? 0.3985 0.5065 0.3464 0.0393 0.0685 -0.0523 224 LEU A O 1702 C CB . LEU A 220 ? 0.3801 0.4669 0.2229 0.0155 0.0790 -0.0659 224 LEU A CB 1703 C CG . LEU A 220 ? 0.4167 0.5178 0.2583 0.0197 0.0717 -0.0521 224 LEU A CG 1704 C CD1 . LEU A 220 ? 0.3914 0.5096 0.2531 0.0265 0.0531 -0.0393 224 LEU A CD1 1705 C CD2 . LEU A 220 ? 0.4578 0.5515 0.2545 0.0102 0.0678 -0.0490 224 LEU A CD2 1706 N N . ILE A 221 ? 0.4166 0.4984 0.3183 0.0242 0.0677 -0.0673 225 ILE A N 1707 C CA . ILE A 221 ? 0.4072 0.4909 0.3290 0.0259 0.0541 -0.0602 225 ILE A CA 1708 C C . ILE A 221 ? 0.4831 0.5722 0.3792 0.0151 0.0380 -0.0570 225 ILE A C 1709 O O . ILE A 221 ? 0.4878 0.5753 0.3930 0.0119 0.0286 -0.0535 225 ILE A O 1710 C CB . ILE A 221 ? 0.4699 0.5306 0.4135 0.0291 0.0656 -0.0697 225 ILE A CB 1711 C CG1 . ILE A 221 ? 0.5129 0.5466 0.4245 0.0178 0.0802 -0.0893 225 ILE A CG1 1712 C CG2 . ILE A 221 ? 0.4959 0.5609 0.4815 0.0429 0.0774 -0.0680 225 ILE A CG2 1713 C CD1 . ILE A 221 ? 0.6085 0.6196 0.5210 0.0121 0.0782 -0.0950 225 ILE A CD1 1714 N N . LYS A 222 ? 0.4457 0.5420 0.3115 0.0088 0.0341 -0.0566 226 LYS A N 1715 C CA . LYS A 222 ? 0.4443 0.5524 0.2915 -0.0007 0.0174 -0.0518 226 LYS A CA 1716 C C . LYS A 222 ? 0.5122 0.6357 0.3439 0.0011 0.0105 -0.0427 226 LYS A C 1717 O O . LYS A 222 ? 0.5216 0.6363 0.3379 0.0022 0.0206 -0.0453 226 LYS A O 1718 C CB . LYS A 222 ? 0.4962 0.5856 0.3154 -0.0168 0.0186 -0.0648 226 LYS A CB 1719 C CG . LYS A 222 ? 0.4217 0.5271 0.2276 -0.0293 -0.0007 -0.0596 226 LYS A CG 1720 C CD . LYS A 222 ? 0.4415 0.5264 0.2130 -0.0493 0.0004 -0.0736 226 LYS A CD 1721 C CE . LYS A 222 ? 0.5541 0.6608 0.3087 -0.0637 -0.0211 -0.0666 226 LYS A CE 1722 N NZ . LYS A 222 ? 0.7203 0.8148 0.4277 -0.0805 -0.0227 -0.0733 226 LYS A NZ 1723 N N . TYR A 223 ? 0.4654 0.6110 0.3033 0.0014 -0.0056 -0.0318 227 TYR A N 1724 C CA . TYR A 223 ? 0.4709 0.6298 0.2993 0.0048 -0.0142 -0.0210 227 TYR A CA 1725 C C . TYR A 223 ? 0.5497 0.7303 0.3793 -0.0008 -0.0328 -0.0133 227 TYR A C 1726 O O . TYR A 223 ? 0.5407 0.7349 0.3912 -0.0026 -0.0380 -0.0129 227 TYR A O 1727 C CB . TYR A 223 ? 0.4566 0.6220 0.3043 0.0187 -0.0092 -0.0129 227 TYR A CB 1728 C CG . TYR A 223 ? 0.4947 0.6585 0.3251 0.0223 -0.0113 -0.0045 227 TYR A CG 1729 C CD1 . TYR A 223 ? 0.5499 0.6948 0.3505 0.0164 -0.0028 -0.0089 227 TYR A CD1 1730 C CD2 . TYR A 223 ? 0.4936 0.6725 0.3375 0.0311 -0.0202 0.0078 227 TYR A CD2 1731 C CE1 . TYR A 223 ? 0.5839 0.7235 0.3644 0.0177 -0.0055 0.0010 227 TYR A CE1 1732 C CE2 . TYR A 223 ? 0.5242 0.6971 0.3534 0.0355 -0.0228 0.0177 227 TYR A CE2 1733 C CZ . TYR A 223 ? 0.6674 0.8200 0.4630 0.0280 -0.0167 0.0154 227 TYR A CZ 1734 O OH . TYR A 223 ? 0.7227 0.8656 0.4995 0.0303 -0.0201 0.0272 227 TYR A OH 1735 N N . ASP A 224 ? 0.5352 0.7196 0.3429 -0.0049 -0.0436 -0.0062 228 ASP A N 1736 C CA . ASP A 224 ? 0.5422 0.7514 0.3540 -0.0106 -0.0646 0.0037 228 ASP A CA 1737 C C . ASP A 224 ? 0.5437 0.7720 0.3792 0.0054 -0.0718 0.0199 228 ASP A C 1738 O O . ASP A 224 ? 0.5463 0.7614 0.3691 0.0129 -0.0676 0.0259 228 ASP A O 1739 C CB . ASP A 224 ? 0.6294 0.8285 0.3979 -0.0285 -0.0751 0.0028 228 ASP A CB 1740 C CG . ASP A 224 ? 0.9267 1.0989 0.6641 -0.0461 -0.0638 -0.0163 228 ASP A CG 1741 O OD1 . ASP A 224 ? 0.9399 1.1031 0.6952 -0.0433 -0.0504 -0.0274 228 ASP A OD1 1742 O OD2 . ASP A 224 ? 1.0938 1.2521 0.7879 -0.0636 -0.0683 -0.0199 228 ASP A OD2 1743 N N . LEU A 225 ? 0.4657 0.7237 0.3368 0.0100 -0.0809 0.0263 229 LEU A N 1744 C CA . LEU A 225 ? 0.4429 0.7191 0.3441 0.0271 -0.0849 0.0402 229 LEU A CA 1745 C C . LEU A 225 ? 0.4834 0.7899 0.4008 0.0260 -0.1079 0.0546 229 LEU A C 1746 O O . LEU A 225 ? 0.4468 0.7824 0.3925 0.0211 -0.1150 0.0541 229 LEU A O 1747 C CB . LEU A 225 ? 0.4102 0.6952 0.3461 0.0374 -0.0703 0.0357 229 LEU A CB 1748 C CG . LEU A 225 ? 0.4612 0.7207 0.3888 0.0446 -0.0517 0.0297 229 LEU A CG 1749 C CD1 . LEU A 225 ? 0.4451 0.7097 0.3929 0.0443 -0.0400 0.0222 229 LEU A CD1 1750 C CD2 . LEU A 225 ? 0.4898 0.7413 0.4204 0.0592 -0.0486 0.0394 229 LEU A CD2 1751 N N . GLN A 226 ? 0.4719 0.7723 0.3724 0.0295 -0.1204 0.0689 230 GLN A N 1752 C CA . GLN A 226 ? 0.4906 0.8200 0.4076 0.0295 -0.1468 0.0874 230 GLN A CA 1753 C C . GLN A 226 ? 0.5456 0.8918 0.5103 0.0542 -0.1480 0.1028 230 GLN A C 1754 O O . GLN A 226 ? 0.5154 0.8442 0.4903 0.0691 -0.1272 0.0979 230 GLN A O 1755 C CB . GLN A 226 ? 0.5517 0.8641 0.4170 0.0141 -0.1643 0.0962 230 GLN A CB 1756 C CG . GLN A 226 ? 0.7696 1.0891 0.6068 -0.0133 -0.1776 0.0881 230 GLN A CG 1757 C CD . GLN A 226 ? 0.9601 1.2557 0.7742 -0.0258 -0.1554 0.0627 230 GLN A CD 1758 O OE1 . GLN A 226 ? 0.8562 1.1655 0.6801 -0.0384 -0.1575 0.0528 230 GLN A OE1 1759 N NE2 . GLN A 226 ? 0.8638 1.1228 0.6480 -0.0233 -0.1343 0.0524 230 GLN A NE2 1760 N N . ASN A 227 ? 0.5373 0.9175 0.5328 0.0576 -0.1727 0.1213 231 ASN A N 1761 C CA . ASN A 227 ? 0.5337 0.9359 0.5856 0.0824 -0.1770 0.1383 231 ASN A CA 1762 C C . ASN A 227 ? 0.5303 0.9437 0.6283 0.0961 -0.1503 0.1240 231 ASN A C 1763 O O . ASN A 227 ? 0.5133 0.9037 0.6180 0.1125 -0.1300 0.1210 231 ASN A O 1764 C CB . ASN A 227 ? 0.5752 0.9469 0.6088 0.0963 -0.1814 0.1557 231 ASN A CB 1765 C CG . ASN A 227 ? 0.8861 1.2759 0.9803 0.1236 -0.1862 0.1745 231 ASN A CG 1766 O OD1 . ASN A 227 ? 0.8552 1.2783 0.9828 0.1280 -0.2136 0.1957 231 ASN A OD1 1767 N ND2 . ASN A 227 ? 0.7527 1.1217 0.8654 0.1422 -0.1591 0.1665 231 ASN A ND2 1768 N N . LEU A 228 ? 0.4658 0.9110 0.5883 0.0852 -0.1491 0.1138 232 LEU A N 1769 C CA . LEU A 228 ? 0.4368 0.8945 0.5977 0.0924 -0.1238 0.0996 232 LEU A CA 1770 C C . LEU A 228 ? 0.5020 1.0131 0.7300 0.0986 -0.1315 0.1072 232 LEU A C 1771 O O . LEU A 228 ? 0.5172 1.0593 0.7566 0.0896 -0.1590 0.1201 232 LEU A O 1772 C CB . LEU A 228 ? 0.4135 0.8554 0.5422 0.0730 -0.1086 0.0786 232 LEU A CB 1773 C CG . LEU A 228 ? 0.4582 0.8518 0.5330 0.0691 -0.0961 0.0691 232 LEU A CG 1774 C CD1 . LEU A 228 ? 0.4432 0.8262 0.4947 0.0507 -0.0870 0.0527 232 LEU A CD1 1775 C CD2 . LEU A 228 ? 0.4691 0.8408 0.5508 0.0865 -0.0751 0.0668 232 LEU A CD2 1776 N N . LYS A 229 ? 0.4422 0.9647 0.7151 0.1129 -0.1068 0.0993 233 LYS A N 1777 C CA . LYS A 229 ? 0.4326 1.0076 0.7778 0.1206 -0.1068 0.1036 233 LYS A CA 1778 C C . LYS A 229 ? 0.4625 1.0678 0.8090 0.0945 -0.1112 0.0937 233 LYS A C 1779 O O . LYS A 229 ? 0.4487 1.0305 0.7579 0.0786 -0.0945 0.0761 233 LYS A O 1780 C CB . LYS A 229 ? 0.4553 1.0273 0.8401 0.1398 -0.0728 0.0930 233 LYS A CB 1781 C CG . LYS A 229 ? 0.6572 1.2784 1.1272 0.1593 -0.0730 0.1034 233 LYS A CG 1782 C CD . LYS A 229 ? 0.7930 1.4131 1.2999 0.1715 -0.0326 0.0860 233 LYS A CD 1783 C CE . LYS A 229 ? 0.9759 1.6345 1.5709 0.1988 -0.0284 0.0968 233 LYS A CE 1784 N NZ . LYS A 229 ? 1.1305 1.7573 1.7317 0.2265 -0.0323 0.1121 233 LYS A NZ 1785 N N . PRO A 230 ? 0.4064 1.0618 0.7925 0.0879 -0.1360 0.1062 234 PRO A N 1786 C CA . PRO A 230 ? 0.3949 1.0769 0.7795 0.0598 -0.1405 0.0966 234 PRO A CA 1787 C C . PRO A 230 ? 0.4428 1.1428 0.8622 0.0569 -0.1092 0.0797 234 PRO A C 1788 O O . PRO A 230 ? 0.4404 1.1560 0.9111 0.0783 -0.0897 0.0794 234 PRO A O 1789 C CB . PRO A 230 ? 0.4271 1.1614 0.8527 0.0557 -0.1752 0.1164 234 PRO A CB 1790 C CG . PRO A 230 ? 0.4873 1.2380 0.9680 0.0881 -0.1787 0.1345 234 PRO A CG 1791 C CD . PRO A 230 ? 0.4344 1.1247 0.8693 0.1044 -0.1626 0.1311 234 PRO A CD 1792 N N . TYR A 231 ? 0.3963 1.0900 0.7849 0.0296 -0.1029 0.0654 235 TYR A N 1793 C CA . TYR A 231 ? 0.3869 1.0922 0.7947 0.0197 -0.0740 0.0495 235 TYR A CA 1794 C C . TYR A 231 ? 0.3881 1.0693 0.8018 0.0395 -0.0412 0.0404 235 TYR A C 1795 O O . TYR A 231 ? 0.3665 1.0778 0.8372 0.0522 -0.0217 0.0377 235 TYR A O 1796 C CB . TYR A 231 ? 0.4238 1.1956 0.8985 0.0102 -0.0792 0.0528 235 TYR A CB 1797 C CG . TYR A 231 ? 0.4725 1.2597 0.9670 -0.0041 -0.0484 0.0366 235 TYR A CG 1798 C CD1 . TYR A 231 ? 0.5014 1.2479 0.9374 -0.0262 -0.0342 0.0227 235 TYR A CD1 1799 C CD2 . TYR A 231 ? 0.4927 1.3365 1.0657 0.0026 -0.0342 0.0363 235 TYR A CD2 1800 C CE1 . TYR A 231 ? 0.5224 1.2800 0.9697 -0.0427 -0.0069 0.0097 235 TYR A CE1 1801 C CE2 . TYR A 231 ? 0.5121 1.3698 1.0995 -0.0140 -0.0034 0.0204 235 TYR A CE2 1802 C CZ . TYR A 231 ? 0.6412 1.4541 1.1616 -0.0380 0.0096 0.0076 235 TYR A CZ 1803 O OH . TYR A 231 ? 0.7000 1.5238 1.2285 -0.0573 0.0390 -0.0062 235 TYR A OH 1804 N N . THR A 232 ? 0.3310 0.9572 0.6859 0.0420 -0.0358 0.0359 236 THR A N 1805 C CA . THR A 232 ? 0.3178 0.9111 0.6616 0.0562 -0.0088 0.0273 236 THR A CA 1806 C C . THR A 232 ? 0.3164 0.8633 0.5954 0.0392 -0.0004 0.0165 236 THR A C 1807 O O . THR A 232 ? 0.2989 0.8236 0.5366 0.0302 -0.0186 0.0199 236 THR A O 1808 C CB . THR A 232 ? 0.4872 1.0658 0.8384 0.0831 -0.0169 0.0395 236 THR A CB 1809 O OG1 . THR A 232 ? 0.4821 1.1068 0.9014 0.0996 -0.0259 0.0520 236 THR A OG1 1810 C CG2 . THR A 232 ? 0.5192 1.0590 0.8545 0.0960 0.0100 0.0303 236 THR A CG2 1811 N N . LYS A 233 ? 0.2601 0.7929 0.5312 0.0338 0.0272 0.0037 237 LYS A N 1812 C CA . LYS A 233 ? 0.2503 0.7422 0.4651 0.0176 0.0336 -0.0038 237 LYS A CA 1813 C C . LYS A 233 ? 0.2782 0.7288 0.4595 0.0308 0.0343 -0.0025 237 LYS A C 1814 O O . LYS A 233 ? 0.2779 0.7203 0.4707 0.0450 0.0511 -0.0059 237 LYS A O 1815 C CB . LYS A 233 ? 0.2822 0.7762 0.4956 0.0009 0.0597 -0.0161 237 LYS A CB 1816 C CG . LYS A 233 ? 0.3438 0.8171 0.5136 -0.0252 0.0546 -0.0180 237 LYS A CG 1817 C CD . LYS A 233 ? 0.3862 0.8685 0.5564 -0.0465 0.0772 -0.0274 237 LYS A CD 1818 C CE . LYS A 233 ? 0.3454 0.8071 0.4755 -0.0726 0.0686 -0.0254 237 LYS A CE 1819 N NZ . LYS A 233 ? 0.3580 0.8306 0.4873 -0.0967 0.0891 -0.0327 237 LYS A NZ 1820 N N . TYR A 234 ? 0.2121 0.6372 0.3544 0.0255 0.0172 0.0017 238 TYR A N 1821 C CA . TYR A 234 ? 0.2035 0.5923 0.3141 0.0347 0.0160 0.0033 238 TYR A CA 1822 C C . TYR A 234 ? 0.2406 0.5996 0.3129 0.0203 0.0217 -0.0022 238 TYR A C 1823 O O . TYR A 234 ? 0.2422 0.6016 0.3033 0.0031 0.0178 -0.0038 238 TYR A O 1824 C CB . TYR A 234 ? 0.2245 0.6078 0.3232 0.0409 -0.0060 0.0125 238 TYR A CB 1825 C CG . TYR A 234 ? 0.2635 0.6629 0.3906 0.0600 -0.0131 0.0224 238 TYR A CG 1826 C CD1 . TYR A 234 ? 0.2892 0.7278 0.4540 0.0614 -0.0254 0.0295 238 TYR A CD1 1827 C CD2 . TYR A 234 ? 0.2813 0.6570 0.3997 0.0757 -0.0087 0.0263 238 TYR A CD2 1828 C CE1 . TYR A 234 ? 0.3105 0.7650 0.5061 0.0801 -0.0350 0.0422 238 TYR A CE1 1829 C CE2 . TYR A 234 ? 0.3049 0.6913 0.4497 0.0939 -0.0163 0.0381 238 TYR A CE2 1830 C CZ . TYR A 234 ? 0.4179 0.8440 0.6023 0.0969 -0.0306 0.0471 238 TYR A CZ 1831 O OH . TYR A 234 ? 0.4571 0.8946 0.6708 0.1157 -0.0420 0.0625 238 TYR A OH 1832 N N . VAL A 235 ? 0.1889 0.5216 0.2424 0.0266 0.0301 -0.0039 239 VAL A N 1833 C CA . VAL A 235 ? 0.1811 0.4868 0.2011 0.0142 0.0325 -0.0063 239 VAL A CA 1834 C C . VAL A 235 ? 0.2304 0.5134 0.2321 0.0233 0.0241 -0.0021 239 VAL A C 1835 O O . VAL A 235 ? 0.2180 0.4943 0.2233 0.0364 0.0291 -0.0014 239 VAL A O 1836 C CB . VAL A 235 ? 0.2253 0.5230 0.2369 0.0055 0.0524 -0.0139 239 VAL A CB 1837 C CG1 . VAL A 235 ? 0.2265 0.4990 0.2034 -0.0089 0.0488 -0.0125 239 VAL A CG1 1838 C CG2 . VAL A 235 ? 0.2247 0.5455 0.2537 -0.0056 0.0644 -0.0196 239 VAL A CG2 1839 N N . LEU A 236 ? 0.1974 0.4679 0.1819 0.0164 0.0128 0.0004 240 LEU A N 1840 C CA . LEU A 236 ? 0.2108 0.4621 0.1810 0.0233 0.0081 0.0027 240 LEU A CA 1841 C C . LEU A 236 ? 0.3050 0.5389 0.2603 0.0158 0.0114 0.0027 240 LEU A C 1842 O O . LEU A 236 ? 0.3160 0.5472 0.2655 0.0033 0.0084 0.0039 240 LEU A O 1843 C CB . LEU A 236 ? 0.2144 0.4620 0.1787 0.0225 -0.0039 0.0041 240 LEU A CB 1844 C CG . LEU A 236 ? 0.2779 0.5403 0.2489 0.0254 -0.0130 0.0055 240 LEU A CG 1845 C CD1 . LEU A 236 ? 0.2835 0.5576 0.2675 0.0383 -0.0119 0.0099 240 LEU A CD1 1846 C CD2 . LEU A 236 ? 0.3130 0.5912 0.2932 0.0135 -0.0177 0.0040 240 LEU A CD2 1847 N N . SER A 237 ? 0.2786 0.5003 0.2272 0.0222 0.0158 0.0028 241 SER A N 1848 C CA . SER A 237 ? 0.2908 0.4994 0.2278 0.0146 0.0160 0.0041 241 SER A CA 1849 C C . SER A 237 ? 0.3589 0.5596 0.2962 0.0212 0.0104 0.0064 241 SER A C 1850 O O . SER A 237 ? 0.3684 0.5674 0.3055 0.0311 0.0123 0.0057 241 SER A O 1851 C CB . SER A 237 ? 0.3616 0.5624 0.2909 0.0134 0.0277 0.0006 241 SER A CB 1852 O OG . SER A 237 ? 0.5382 0.7272 0.4613 0.0157 0.0275 0.0021 241 SER A OG 1853 N N . LEU A 238 ? 0.3104 0.5063 0.2492 0.0153 0.0040 0.0098 242 LEU A N 1854 C CA . LEU A 238 ? 0.3010 0.4909 0.2458 0.0215 0.0028 0.0102 242 LEU A CA 1855 C C . LEU A 238 ? 0.3593 0.5475 0.3117 0.0155 -0.0016 0.0156 242 LEU A C 1856 O O . LEU A 238 ? 0.3599 0.5486 0.3163 0.0076 -0.0104 0.0216 242 LEU A O 1857 C CB . LEU A 238 ? 0.2951 0.4829 0.2442 0.0249 -0.0009 0.0079 242 LEU A CB 1858 C CG . LEU A 238 ? 0.3375 0.5171 0.2948 0.0299 0.0018 0.0056 242 LEU A CG 1859 C CD1 . LEU A 238 ? 0.3494 0.5258 0.2970 0.0358 0.0104 0.0013 242 LEU A CD1 1860 C CD2 . LEU A 238 ? 0.3295 0.5015 0.2902 0.0292 -0.0008 0.0022 242 LEU A CD2 1861 N N . HIS A 239 ? 0.3074 0.4943 0.2623 0.0179 0.0034 0.0150 243 HIS A N 1862 C CA . HIS A 239 ? 0.3033 0.4940 0.2709 0.0121 -0.0017 0.0208 243 HIS A CA 1863 C C . HIS A 239 ? 0.3375 0.5289 0.3179 0.0194 0.0060 0.0177 243 HIS A C 1864 O O . HIS A 239 ? 0.3335 0.5187 0.3021 0.0254 0.0160 0.0115 243 HIS A O 1865 C CB . HIS A 239 ? 0.3236 0.5142 0.2762 -0.0011 -0.0024 0.0228 243 HIS A CB 1866 C CG . HIS A 239 ? 0.3722 0.5559 0.3119 0.0003 0.0099 0.0164 243 HIS A CG 1867 N ND1 . HIS A 239 ? 0.3978 0.5825 0.3447 -0.0009 0.0133 0.0166 243 HIS A ND1 1868 C CD2 . HIS A 239 ? 0.4020 0.5768 0.3250 0.0029 0.0196 0.0106 243 HIS A CD2 1869 C CE1 . HIS A 239 ? 0.4005 0.5730 0.3301 0.0000 0.0246 0.0113 243 HIS A CE1 1870 N NE2 . HIS A 239 ? 0.4092 0.5749 0.3258 0.0036 0.0285 0.0079 243 HIS A NE2 1871 N N . ALA A 240 ? 0.2818 0.4818 0.2877 0.0180 0.0011 0.0231 244 ALA A N 1872 C CA . ALA A 240 ? 0.2684 0.4731 0.2928 0.0232 0.0109 0.0196 244 ALA A CA 1873 C C . ALA A 240 ? 0.2944 0.5086 0.3227 0.0127 0.0095 0.0236 244 ALA A C 1874 O O . ALA A 240 ? 0.3059 0.5272 0.3366 0.0020 -0.0041 0.0322 244 ALA A O 1875 C CB . ALA A 240 ? 0.2763 0.4869 0.3364 0.0307 0.0085 0.0220 244 ALA A CB 1876 N N . TYR A 241 ? 0.2178 0.4305 0.2427 0.0127 0.0230 0.0178 245 TYR A N 1877 C CA . TYR A 241 ? 0.2108 0.4314 0.2390 0.0003 0.0231 0.0204 245 TYR A CA 1878 C C . TYR A 241 ? 0.2622 0.4988 0.3244 0.0018 0.0314 0.0194 245 TYR A C 1879 O O . TYR A 241 ? 0.2647 0.4978 0.3342 0.0122 0.0447 0.0124 245 TYR A O 1880 C CB . TYR A 241 ? 0.2355 0.4374 0.2266 -0.0054 0.0324 0.0152 245 TYR A CB 1881 C CG . TYR A 241 ? 0.2798 0.4684 0.2575 0.0021 0.0485 0.0087 245 TYR A CG 1882 C CD1 . TYR A 241 ? 0.3205 0.5112 0.3038 -0.0040 0.0598 0.0067 245 TYR A CD1 1883 C CD2 . TYR A 241 ? 0.2891 0.4634 0.2465 0.0126 0.0516 0.0058 245 TYR A CD2 1884 C CE1 . TYR A 241 ? 0.3445 0.5202 0.3096 0.0000 0.0745 0.0020 245 TYR A CE1 1885 C CE2 . TYR A 241 ? 0.3057 0.4664 0.2452 0.0167 0.0632 0.0024 245 TYR A CE2 1886 C CZ . TYR A 241 ? 0.4074 0.5670 0.3484 0.0100 0.0751 0.0007 245 TYR A CZ 1887 O OH . TYR A 241 ? 0.4637 0.6074 0.3817 0.0110 0.0866 -0.0014 245 TYR A OH 1888 N N . ILE A 242 ? 0.2137 0.4685 0.2959 -0.0108 0.0246 0.0256 246 ILE A N 1889 C CA . ILE A 242 ? 0.2019 0.4786 0.3232 -0.0123 0.0326 0.0253 246 ILE A CA 1890 C C . ILE A 242 ? 0.2699 0.5465 0.3751 -0.0302 0.0375 0.0239 246 ILE A C 1891 O O . ILE A 242 ? 0.2635 0.5360 0.3476 -0.0448 0.0252 0.0284 246 ILE A O 1892 C CB . ILE A 242 ? 0.2263 0.5332 0.4044 -0.0091 0.0173 0.0366 246 ILE A CB 1893 C CG1 . ILE A 242 ? 0.2197 0.5520 0.4488 -0.0056 0.0316 0.0335 246 ILE A CG1 1894 C CG2 . ILE A 242 ? 0.2391 0.5583 0.4164 -0.0258 -0.0088 0.0509 246 ILE A CG2 1895 C CD1 . ILE A 242 ? 0.1955 0.5570 0.4929 0.0051 0.0216 0.0434 246 ILE A CD1 1896 N N . ILE A 243 ? 0.2531 0.5309 0.3641 -0.0313 0.0570 0.0168 247 ILE A N 1897 C CA . ILE A 243 ? 0.2704 0.5463 0.3671 -0.0503 0.0627 0.0156 247 ILE A CA 1898 C C . ILE A 243 ? 0.3157 0.6306 0.4639 -0.0621 0.0569 0.0216 247 ILE A C 1899 O O . ILE A 243 ? 0.3026 0.6350 0.4830 -0.0608 0.0729 0.0173 247 ILE A O 1900 C CB . ILE A 243 ? 0.3261 0.5718 0.3824 -0.0516 0.0842 0.0069 247 ILE A CB 1901 C CG1 . ILE A 243 ? 0.3322 0.5489 0.3525 -0.0358 0.0866 0.0038 247 ILE A CG1 1902 C CG2 . ILE A 243 ? 0.3504 0.5802 0.3769 -0.0717 0.0844 0.0072 247 ILE A CG2 1903 C CD1 . ILE A 243 ? 0.4432 0.6401 0.4399 -0.0309 0.1059 -0.0023 247 ILE A CD1 1904 N N . ALA A 244 ? 0.2731 0.6034 0.4301 -0.0745 0.0331 0.0320 248 ALA A N 1905 C CA . ALA A 244 ? 0.2795 0.6502 0.4850 -0.0887 0.0188 0.0420 248 ALA A CA 1906 C C . ALA A 244 ? 0.3709 0.7374 0.5524 -0.1158 0.0240 0.0383 248 ALA A C 1907 O O . ALA A 244 ? 0.3883 0.7271 0.5361 -0.1168 0.0464 0.0273 248 ALA A O 1908 C CB . ALA A 244 ? 0.2864 0.6701 0.5014 -0.0924 -0.0120 0.0567 248 ALA A CB 1909 N N . LYS A 245 ? 0.3368 0.7275 0.5317 -0.1395 0.0025 0.0480 249 LYS A N 1910 C CA . LYS A 245 ? 0.3607 0.7443 0.5287 -0.1694 0.0061 0.0437 249 LYS A CA 1911 C C . LYS A 245 ? 0.4525 0.7818 0.5442 -0.1757 0.0136 0.0339 249 LYS A C 1912 O O . LYS A 245 ? 0.4915 0.7995 0.5484 -0.1981 0.0216 0.0272 249 LYS A O 1913 C CB . LYS A 245 ? 0.3931 0.8154 0.5895 -0.1955 -0.0228 0.0573 249 LYS A CB 1914 C CG . LYS A 245 ? 0.4032 0.8837 0.6828 -0.1938 -0.0285 0.0671 249 LYS A CG 1915 C CD . LYS A 245 ? 0.4450 0.9665 0.7565 -0.2149 -0.0658 0.0862 249 LYS A CD 1916 C CE . LYS A 245 ? 0.5262 1.1091 0.9221 -0.2200 -0.0717 0.0960 249 LYS A CE 1917 N NZ . LYS A 245 ? 0.6163 1.2358 1.0295 -0.2512 -0.1094 0.1142 249 LYS A NZ 1918 N N . VAL A 246 ? 0.3885 0.6961 0.4585 -0.1554 0.0121 0.0331 250 VAL A N 1919 C CA . VAL A 246 ? 0.3952 0.6571 0.4062 -0.1528 0.0195 0.0248 250 VAL A CA 1920 C C . VAL A 246 ? 0.3942 0.6504 0.4112 -0.1223 0.0220 0.0251 250 VAL A C 1921 O O . VAL A 246 ? 0.3738 0.6593 0.4347 -0.1098 0.0127 0.0327 250 VAL A O 1922 C CB . VAL A 246 ? 0.4736 0.7288 0.4537 -0.1776 0.0015 0.0272 250 VAL A CB 1923 C CG1 . VAL A 246 ? 0.4567 0.7379 0.4592 -0.1738 -0.0240 0.0406 250 VAL A CG1 1924 C CG2 . VAL A 246 ? 0.4984 0.7046 0.4192 -0.1798 0.0160 0.0149 250 VAL A CG2 1925 N N . GLN A 247 ? 0.3355 0.5554 0.3131 -0.1105 0.0344 0.0173 251 GLN A N 1926 C CA . GLN A 247 ? 0.3118 0.5291 0.2947 -0.0856 0.0344 0.0179 251 GLN A CA 1927 C C . GLN A 247 ? 0.3534 0.5791 0.3360 -0.0883 0.0148 0.0245 251 GLN A C 1928 O O . GLN A 247 ? 0.3743 0.5827 0.3227 -0.1022 0.0120 0.0219 251 GLN A O 1929 C CB . GLN A 247 ? 0.3388 0.5204 0.2857 -0.0725 0.0508 0.0099 251 GLN A CB 1930 C CG . GLN A 247 ? 0.4553 0.6332 0.4003 -0.0525 0.0473 0.0104 251 GLN A CG 1931 C CD . GLN A 247 ? 0.6894 0.8457 0.6169 -0.0361 0.0608 0.0062 251 GLN A CD 1932 O OE1 . GLN A 247 ? 0.6545 0.8018 0.5770 -0.0360 0.0730 0.0045 251 GLN A OE1 1933 N NE2 . GLN A 247 ? 0.5315 0.6810 0.4501 -0.0234 0.0575 0.0058 251 GLN A NE2 1934 N N . ARG A 248 ? 0.2831 0.5326 0.3023 -0.0764 0.0029 0.0329 252 ARG A N 1935 C CA . ARG A 248 ? 0.2741 0.5303 0.2940 -0.0791 -0.0170 0.0421 252 ARG A CA 1936 C C . ARG A 248 ? 0.3307 0.5743 0.3451 -0.0583 -0.0128 0.0394 252 ARG A C 1937 O O . ARG A 248 ? 0.3065 0.5562 0.3470 -0.0404 -0.0066 0.0383 252 ARG A O 1938 C CB . ARG A 248 ? 0.2269 0.5181 0.2940 -0.0841 -0.0385 0.0575 252 ARG A CB 1939 C CG . ARG A 248 ? 0.2335 0.5452 0.3158 -0.1048 -0.0438 0.0610 252 ARG A CG 1940 C CD . ARG A 248 ? 0.2508 0.5951 0.3677 -0.1171 -0.0734 0.0800 252 ARG A CD 1941 N NE . ARG A 248 ? 0.3007 0.6500 0.3947 -0.1496 -0.0852 0.0828 252 ARG A NE 1942 C CZ . ARG A 248 ? 0.4246 0.7989 0.5458 -0.1638 -0.0870 0.0848 252 ARG A CZ 1943 N NH1 . ARG A 248 ? 0.2011 0.5995 0.3764 -0.1473 -0.0756 0.0840 252 ARG A NH1 1944 N NH2 . ARG A 248 ? 0.3132 0.6881 0.4063 -0.1968 -0.0985 0.0862 252 ARG A NH2 1945 N N . ASN A 249 ? 0.3197 0.5450 0.2988 -0.0628 -0.0139 0.0367 253 ASN A N 1946 C CA . ASN A 249 ? 0.3118 0.5269 0.2836 -0.0474 -0.0109 0.0342 253 ASN A CA 1947 C C . ASN A 249 ? 0.3403 0.5655 0.3233 -0.0504 -0.0300 0.0458 253 ASN A C 1948 O O . ASN A 249 ? 0.3376 0.5679 0.3114 -0.0695 -0.0450 0.0543 253 ASN A O 1949 C CB . ASN A 249 ? 0.3830 0.5748 0.3155 -0.0502 0.0012 0.0243 253 ASN A CB 1950 C CG . ASN A 249 ? 0.8081 0.9838 0.7291 -0.0419 0.0196 0.0150 253 ASN A CG 1951 O OD1 . ASN A 249 ? 0.7434 0.9208 0.6782 -0.0275 0.0257 0.0140 253 ASN A OD1 1952 N ND2 . ASN A 249 ? 0.8670 1.0230 0.7596 -0.0519 0.0294 0.0080 253 ASN A ND2 1953 N N . GLY A 250 ? 0.2843 0.5092 0.2831 -0.0337 -0.0297 0.0465 254 GLY A N 1954 C CA . GLY A 250 ? 0.2906 0.5183 0.2976 -0.0348 -0.0458 0.0575 254 GLY A CA 1955 C C . GLY A 250 ? 0.3530 0.5657 0.3231 -0.0418 -0.0428 0.0530 254 GLY A C 1956 O O . GLY A 250 ? 0.3365 0.5387 0.2850 -0.0392 -0.0268 0.0408 254 GLY A O 1957 N N . SER A 251 ? 0.3338 0.5453 0.2981 -0.0509 -0.0575 0.0636 255 SER A N 1958 C CA . SER A 251 ? 0.3495 0.5489 0.2807 -0.0594 -0.0521 0.0586 255 SER A CA 1959 C C . SER A 251 ? 0.3779 0.5726 0.3146 -0.0413 -0.0389 0.0485 255 SER A C 1960 O O . SER A 251 ? 0.3456 0.5427 0.3078 -0.0255 -0.0390 0.0487 255 SER A O 1961 C CB . SER A 251 ? 0.4243 0.6216 0.3435 -0.0767 -0.0705 0.0732 255 SER A CB 1962 O OG . SER A 251 ? 0.5299 0.7260 0.4720 -0.0665 -0.0809 0.0831 255 SER A OG 1963 N N . ALA A 252 ? 0.3488 0.5375 0.2629 -0.0440 -0.0261 0.0385 256 ALA A N 1964 C CA . ALA A 252 ? 0.3400 0.5286 0.2605 -0.0290 -0.0163 0.0303 256 ALA A CA 1965 C C . ALA A 252 ? 0.4202 0.6084 0.3407 -0.0323 -0.0222 0.0340 256 ALA A C 1966 O O . ALA A 252 ? 0.4432 0.6287 0.3470 -0.0489 -0.0269 0.0390 256 ALA A O 1967 C CB . ALA A 252 ? 0.3508 0.5368 0.2581 -0.0262 0.0002 0.0189 256 ALA A CB 1968 N N . ALA A 253 ? 0.3716 0.5603 0.3070 -0.0191 -0.0215 0.0313 257 ALA A N 1969 C CA . ALA A 253 ? 0.3739 0.5602 0.3101 -0.0222 -0.0261 0.0333 257 ALA A CA 1970 C C . ALA A 253 ? 0.4044 0.5990 0.3347 -0.0207 -0.0153 0.0237 257 ALA A C 1971 O O . ALA A 253 ? 0.3997 0.5988 0.3366 -0.0080 -0.0093 0.0171 257 ALA A O 1972 C CB . ALA A 253 ? 0.3820 0.5619 0.3372 -0.0107 -0.0304 0.0340 257 ALA A CB 1973 N N . MET A 254 ? 0.3491 0.5468 0.2676 -0.0345 -0.0127 0.0238 258 MET A N 1974 C CA . MET A 254 ? 0.3444 0.5553 0.2653 -0.0339 -0.0017 0.0153 258 MET A CA 1975 C C . MET A 254 ? 0.3858 0.6018 0.3169 -0.0328 -0.0068 0.0149 258 MET A C 1976 O O . MET A 254 ? 0.3779 0.5822 0.3076 -0.0379 -0.0167 0.0208 258 MET A O 1977 C CB . MET A 254 ? 0.3963 0.6099 0.3016 -0.0507 0.0082 0.0128 258 MET A CB 1978 C CG . MET A 254 ? 0.4461 0.6523 0.3363 -0.0550 0.0159 0.0099 258 MET A CG 1979 S SD . MET A 254 ? 0.4688 0.6796 0.3724 -0.0356 0.0310 -0.0006 258 MET A SD 1980 C CE . MET A 254 ? 0.4444 0.6393 0.3231 -0.0482 0.0381 -0.0035 258 MET A CE 1981 N N . CYS A 255 ? 0.3493 0.5823 0.2921 -0.0264 -0.0006 0.0084 259 CYS A N 1982 C CA . CYS A 255 ? 0.3485 0.5902 0.3010 -0.0261 -0.0061 0.0067 259 CYS A CA 1983 C C . CYS A 255 ? 0.3989 0.6667 0.3671 -0.0264 0.0014 0.0022 259 CYS A C 1984 O O . CYS A 255 ? 0.3987 0.6757 0.3764 -0.0151 0.0093 -0.0004 259 CYS A O 1985 C CB . CYS A 255 ? 0.3484 0.5843 0.3033 -0.0120 -0.0114 0.0055 259 CYS A CB 1986 S SG . CYS A 255 ? 0.4112 0.6362 0.3629 -0.0169 -0.0210 0.0038 259 CYS A SG 1987 N N . HIS A 256 ? 0.3482 0.6286 0.3231 -0.0382 -0.0009 0.0014 260 HIS A N 1988 C CA . HIS A 256 ? 0.3318 0.6439 0.3315 -0.0368 0.0054 -0.0024 260 HIS A CA 1989 C C . HIS A 256 ? 0.3959 0.7246 0.4079 -0.0417 -0.0057 -0.0022 260 HIS A C 1990 O O . HIS A 256 ? 0.4033 0.7178 0.4013 -0.0546 -0.0135 -0.0014 260 HIS A O 1991 C CB . HIS A 256 ? 0.3354 0.6598 0.3405 -0.0473 0.0225 -0.0065 260 HIS A CB 1992 C CG . HIS A 256 ? 0.3815 0.7024 0.3738 -0.0708 0.0236 -0.0056 260 HIS A CG 1993 N ND1 . HIS A 256 ? 0.4161 0.7185 0.3825 -0.0854 0.0310 -0.0044 260 HIS A ND1 1994 C CD2 . HIS A 256 ? 0.4037 0.7370 0.4038 -0.0841 0.0182 -0.0052 260 HIS A CD2 1995 C CE1 . HIS A 256 ? 0.4236 0.7253 0.3818 -0.1062 0.0298 -0.0020 260 HIS A CE1 1996 N NE2 . HIS A 256 ? 0.4206 0.7402 0.3993 -0.1061 0.0230 -0.0031 260 HIS A NE2 1997 N N . PHE A 257 ? 0.3501 0.7070 0.3880 -0.0315 -0.0079 -0.0020 261 PHE A N 1998 C CA . PHE A 257 ? 0.3568 0.7360 0.4087 -0.0378 -0.0209 -0.0009 261 PHE A CA 1999 C C . PHE A 257 ? 0.4037 0.8240 0.4968 -0.0277 -0.0195 0.0015 261 PHE A C 2000 O O . PHE A 257 ? 0.3879 0.8111 0.4950 -0.0110 -0.0095 0.0022 261 PHE A O 2001 C CB . PHE A 257 ? 0.3846 0.7440 0.4143 -0.0347 -0.0360 0.0006 261 PHE A CB 2002 C CG . PHE A 257 ? 0.4044 0.7709 0.4405 -0.0169 -0.0423 0.0054 261 PHE A CG 2003 C CD1 . PHE A 257 ? 0.4397 0.7856 0.4651 -0.0017 -0.0351 0.0066 261 PHE A CD1 2004 C CD2 . PHE A 257 ? 0.4499 0.8438 0.5021 -0.0171 -0.0569 0.0104 261 PHE A CD2 2005 C CE1 . PHE A 257 ? 0.4582 0.8066 0.4863 0.0132 -0.0407 0.0125 261 PHE A CE1 2006 C CE2 . PHE A 257 ? 0.4932 0.8914 0.5490 -0.0014 -0.0649 0.0182 261 PHE A CE2 2007 C CZ . PHE A 257 ? 0.4625 0.8360 0.5052 0.0138 -0.0559 0.0191 261 PHE A CZ 2008 N N . THR A 258 ? 0.3659 0.8178 0.4811 -0.0383 -0.0298 0.0030 262 THR A N 2009 C CA . THR A 258 ? 0.3561 0.8537 0.5201 -0.0287 -0.0320 0.0076 262 THR A CA 2010 C C . THR A 258 ? 0.3899 0.9083 0.5613 -0.0321 -0.0576 0.0153 262 THR A C 2011 O O . THR A 258 ? 0.3901 0.9075 0.5451 -0.0533 -0.0686 0.0129 262 THR A O 2012 C CB . THR A 258 ? 0.4575 0.9859 0.6582 -0.0348 -0.0117 0.0020 262 THR A CB 2013 O OG1 . THR A 258 ? 0.4586 1.0390 0.7115 -0.0337 -0.0199 0.0070 262 THR A OG1 2014 C CG2 . THR A 258 ? 0.4321 0.9445 0.6067 -0.0603 -0.0015 -0.0052 262 THR A CG2 2015 N N . THR A 259 ? 0.3291 0.8623 0.5214 -0.0124 -0.0676 0.0253 263 THR A N 2016 C CA . THR A 259 ? 0.3355 0.8881 0.5325 -0.0137 -0.0948 0.0364 263 THR A CA 2017 C C . THR A 259 ? 0.4045 1.0053 0.6360 -0.0318 -0.1089 0.0392 263 THR A C 2018 O O . THR A 259 ? 0.3955 1.0238 0.6623 -0.0378 -0.0944 0.0338 263 THR A O 2019 C CB . THR A 259 ? 0.3909 0.9449 0.6028 0.0120 -0.1013 0.0490 263 THR A CB 2020 O OG1 . THR A 259 ? 0.3443 0.9226 0.6086 0.0302 -0.0840 0.0499 263 THR A OG1 2021 C CG2 . THR A 259 ? 0.3694 0.8721 0.5321 0.0207 -0.0955 0.0468 263 THR A CG2 2022 N N . LYS A 260 ? 0.3752 0.9850 0.5924 -0.0439 -0.1365 0.0468 264 LYS A N 2023 C CA . LYS A 260 ? 0.5499 1.2042 0.7930 -0.0660 -0.1548 0.0501 264 LYS A CA 2024 C C . LYS A 260 ? 0.8376 1.5539 1.1524 -0.0525 -0.1677 0.0658 264 LYS A C 2025 O O . LYS A 260 ? 0.3825 1.1023 0.7097 -0.0308 -0.1794 0.0801 264 LYS A O 2026 C CB . LYS A 260 ? 0.6058 1.2393 0.7960 -0.0897 -0.1783 0.0496 264 LYS A CB 2027 C CG . LYS A 260 ? 0.7097 1.2837 0.8378 -0.1029 -0.1640 0.0333 264 LYS A CG 2028 C CD . LYS A 260 ? 0.8552 1.4155 0.9416 -0.1340 -0.1811 0.0273 264 LYS A CD 2029 C CE . LYS A 260 ? 1.0205 1.5187 1.0508 -0.1432 -0.1655 0.0114 264 LYS A CE 2030 N NZ . LYS A 260 ? 1.1522 1.6397 1.1919 -0.1490 -0.1449 0.0023 264 LYS A NZ # 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 5 ? ? ? A . n A 1 2 THR 2 6 ? ? ? A . n A 1 3 GLY 3 7 ? ? ? A . n A 1 4 LYS 4 8 ? ? ? A . n A 1 5 PRO 5 9 ? ? ? A . n A 1 6 THR 6 10 10 THR THR A . n A 1 7 CYS 7 11 11 CYS CYS A . n A 1 8 ASP 8 12 12 ASP ASP A . n A 1 9 GLU 9 13 13 GLU GLU A . n A 1 10 LYS 10 14 14 LYS LYS A . n A 1 11 TYR 11 15 15 TYR TYR A . n A 1 12 ALA 12 16 16 ALA ALA A . n A 1 13 ASN 13 17 17 ASN ASN A . n A 1 14 ILE 14 18 18 ILE ILE A . n A 1 15 THR 15 19 19 THR THR A . n A 1 16 VAL 16 20 20 VAL VAL A . n A 1 17 ASP 17 21 21 ASP ASP A . n A 1 18 TYR 18 22 22 TYR TYR A . n A 1 19 LEU 19 23 23 LEU LEU A . n A 1 20 TYR 20 24 24 TYR TYR A . n A 1 21 ASN 21 25 25 ASN ASN A . n A 1 22 LYS 22 26 26 LYS LYS A . n A 1 23 GLU 23 27 27 GLU GLU A . n A 1 24 THR 24 28 28 THR THR A . n A 1 25 LYS 25 29 29 LYS LYS A . n A 1 26 LEU 26 30 30 LEU LEU A . n A 1 27 PHE 27 31 31 PHE PHE A . n A 1 28 THR 28 32 32 THR THR A . n A 1 29 ALA 29 33 33 ALA ALA A . n A 1 30 LYS 30 34 34 LYS LYS A . n A 1 31 LEU 31 35 35 LEU LEU A . n A 1 32 ASN 32 36 36 ASN ASN A . n A 1 33 VAL 33 37 37 VAL VAL A . n A 1 34 ASN 34 38 38 ASN ASN A . n A 1 35 GLU 35 39 39 GLU GLU A . n A 1 36 ASN 36 40 40 ASN ASN A . n A 1 37 VAL 37 41 41 VAL VAL A . n A 1 38 GLU 38 42 42 GLU GLU A . n A 1 39 CYS 39 43 43 CYS CYS A . n A 1 40 GLY 40 44 44 GLY GLY A . n A 1 41 ASN 41 45 ? ? ? A . n A 1 42 ASN 42 46 ? ? ? A . n A 1 43 THR 43 47 ? ? ? A . n A 1 44 CYS 44 48 48 CYS CYS A . n A 1 45 THR 45 49 49 THR THR A . n A 1 46 ASN 46 50 50 ASN ASN A . n A 1 47 ASN 47 51 51 ASN ASN A . n A 1 48 GLU 48 52 52 GLU GLU A . n A 1 49 VAL 49 53 53 VAL VAL A . n A 1 50 HIS 50 54 54 HIS HIS A . n A 1 51 ASN 51 55 55 ASN ASN A . n A 1 52 LEU 52 56 56 LEU LEU A . n A 1 53 THR 53 57 57 THR THR A . n A 1 54 GLU 54 58 58 GLU GLU A . n A 1 55 CYS 55 59 59 CYS CYS A . n A 1 56 LYS 56 60 60 LYS LYS A . n A 1 57 ASN 57 61 61 ASN ASN A . n A 1 58 ALA 58 62 62 ALA ALA A . n A 1 59 SER 59 63 63 SER SER A . n A 1 60 VAL 60 64 64 VAL VAL A . n A 1 61 SER 61 65 65 SER SER A . n A 1 62 ILE 62 66 66 ILE ILE A . n A 1 63 SER 63 67 67 SER SER A . n A 1 64 HIS 64 68 68 HIS HIS A . n A 1 65 ASN 65 69 69 ASN ASN A . n A 1 66 SER 66 70 70 SER SER A . n A 1 67 CYS 67 71 71 CYS CYS A . n A 1 68 THR 68 72 72 THR THR A . n A 1 69 ALA 69 73 73 ALA ALA A . n A 1 70 PRO 70 74 74 PRO PRO A . n A 1 71 ASP 71 75 75 ASP ASP A . n A 1 72 LYS 72 76 76 LYS LYS A . n A 1 73 THR 73 77 77 THR THR A . n A 1 74 LEU 74 78 78 LEU LEU A . n A 1 75 ILE 75 79 79 ILE ILE A . n A 1 76 LEU 76 80 80 LEU LEU A . n A 1 77 ASP 77 81 81 ASP ASP A . n A 1 78 VAL 78 82 82 VAL VAL A . n A 1 79 PRO 79 83 83 PRO PRO A . n A 1 80 PRO 80 84 84 PRO PRO A . n A 1 81 GLY 81 85 85 GLY GLY A . n A 1 82 VAL 82 86 86 VAL VAL A . n A 1 83 GLU 83 87 87 GLU GLU A . n A 1 84 LYS 84 88 88 LYS LYS A . n A 1 85 PHE 85 89 89 PHE PHE A . n A 1 86 GLN 86 90 90 GLN GLN A . n A 1 87 LEU 87 91 91 LEU LEU A . n A 1 88 HIS 88 92 92 HIS HIS A . n A 1 89 ASP 89 93 93 ASP ASP A . n A 1 90 CYS 90 94 94 CYS CYS A . n A 1 91 THR 91 95 95 THR THR A . n A 1 92 GLN 92 96 96 GLN GLN A . n A 1 93 VAL 93 97 97 VAL VAL A . n A 1 94 GLU 94 98 98 GLU GLU A . n A 1 95 LYS 95 99 99 LYS LYS A . n A 1 96 ALA 96 100 100 ALA ALA A . n A 1 97 ASP 97 101 101 ASP ASP A . n A 1 98 THR 98 102 102 THR THR A . n A 1 99 THR 99 103 103 THR THR A . n A 1 100 ILE 100 104 104 ILE ILE A . n A 1 101 CYS 101 105 105 CYS CYS A . n A 1 102 LEU 102 106 106 LEU LEU A . n A 1 103 LYS 103 107 107 LYS LYS A . n A 1 104 TRP 104 108 108 TRP TRP A . n A 1 105 LYS 105 109 109 LYS LYS A . n A 1 106 ASN 106 110 110 ASN ASN A . n A 1 107 ILE 107 111 111 ILE ILE A . n A 1 108 GLU 108 112 112 GLU GLU A . n A 1 109 THR 109 113 113 THR THR A . n A 1 110 PHE 110 114 114 PHE PHE A . n A 1 111 THR 111 115 115 THR THR A . n A 1 112 CYS 112 116 116 CYS CYS A . n A 1 113 ASP 113 117 117 ASP ASP A . n A 1 114 THR 114 118 118 THR THR A . n A 1 115 GLN 115 119 119 GLN GLN A . n A 1 116 ASN 116 120 120 ASN ASN A . n A 1 117 ILE 117 121 121 ILE ILE A . n A 1 118 THR 118 122 122 THR THR A . n A 1 119 TYR 119 123 123 TYR TYR A . n A 1 120 ARG 120 124 124 ARG ARG A . n A 1 121 PHE 121 125 125 PHE PHE A . n A 1 122 GLN 122 126 126 GLN GLN A . n A 1 123 CYS 123 127 127 CYS CYS A . n A 1 124 GLY 124 128 128 GLY GLY A . n A 1 125 ASN 125 129 129 ASN ASN A . n A 1 126 MET 126 130 130 MET MET A . n A 1 127 ILE 127 131 131 ILE ILE A . n A 1 128 PHE 128 132 132 PHE PHE A . n A 1 129 ASP 129 133 133 ASP ASP A . n A 1 130 ASN 130 134 134 ASN ASN A . n A 1 131 LYS 131 135 135 LYS LYS A . n A 1 132 GLU 132 136 136 GLU GLU A . n A 1 133 ILE 133 137 137 ILE ILE A . n A 1 134 LYS 134 138 138 LYS LYS A . n A 1 135 LEU 135 139 139 LEU LEU A . n A 1 136 GLU 136 140 140 GLU GLU A . n A 1 137 ASN 137 141 141 ASN ASN A . n A 1 138 LEU 138 142 142 LEU LEU A . n A 1 139 GLU 139 143 143 GLU GLU A . n A 1 140 PRO 140 144 144 PRO PRO A . n A 1 141 GLU 141 145 145 GLU GLU A . n A 1 142 HIS 142 146 146 HIS HIS A . n A 1 143 GLU 143 147 147 GLU GLU A . n A 1 144 TYR 144 148 148 TYR TYR A . n A 1 145 LYS 145 149 149 LYS LYS A . n A 1 146 CYS 146 150 150 CYS CYS A . n A 1 147 ASP 147 151 151 ASP ASP A . n A 1 148 SER 148 152 152 SER SER A . n A 1 149 GLU 149 153 153 GLU GLU A . n A 1 150 ILE 150 154 154 ILE ILE A . n A 1 151 LEU 151 155 155 LEU LEU A . n A 1 152 TYR 152 156 156 TYR TYR A . n A 1 153 ASN 153 157 157 ASN ASN A . n A 1 154 ASN 154 158 158 ASN ASN A . n A 1 155 HIS 155 159 159 HIS HIS A . n A 1 156 LYS 156 160 160 LYS LYS A . n A 1 157 PHE 157 161 161 PHE PHE A . n A 1 158 THR 158 162 162 THR THR A . n A 1 159 ASN 159 163 163 ASN ASN A . n A 1 160 ALA 160 164 164 ALA ALA A . n A 1 161 SER 161 165 165 SER SER A . n A 1 162 LYS 162 166 166 LYS LYS A . n A 1 163 ILE 163 167 167 ILE ILE A . n A 1 164 ILE 164 168 168 ILE ILE A . n A 1 165 LYS 165 169 169 LYS LYS A . n A 1 166 THR 166 170 170 THR THR A . n A 1 167 ASP 167 171 171 ASP ASP A . n A 1 168 PHE 168 172 172 PHE PHE A . n A 1 169 GLY 169 173 173 GLY GLY A . n A 1 170 SER 170 174 174 SER SER A . n A 1 171 PRO 171 175 175 PRO PRO A . n A 1 172 GLY 172 176 176 GLY GLY A . n A 1 173 GLU 173 177 177 GLU GLU A . n A 1 174 PRO 174 178 178 PRO PRO A . n A 1 175 GLN 175 179 179 GLN GLN A . n A 1 176 ILE 176 180 180 ILE ILE A . n A 1 177 ILE 177 181 181 ILE ILE A . n A 1 178 PHE 178 182 182 PHE PHE A . n A 1 179 CYS 179 183 183 CYS CYS A . n A 1 180 ARG 180 184 184 ARG ARG A . n A 1 181 SER 181 185 185 SER SER A . n A 1 182 GLU 182 186 186 GLU GLU A . n A 1 183 ALA 183 187 187 ALA ALA A . n A 1 184 ALA 184 188 188 ALA ALA A . n A 1 185 HIS 185 189 189 HIS HIS A . n A 1 186 GLN 186 190 190 GLN GLN A . n A 1 187 GLY 187 191 191 GLY GLY A . n A 1 188 VAL 188 192 192 VAL VAL A . n A 1 189 ILE 189 193 193 ILE ILE A . n A 1 190 THR 190 194 194 THR THR A . n A 1 191 TRP 191 195 195 TRP TRP A . n A 1 192 ASN 192 196 196 ASN ASN A . n A 1 193 PRO 193 197 197 PRO PRO A . n A 1 194 PRO 194 198 198 PRO PRO A . n A 1 195 GLN 195 199 199 GLN GLN A . n A 1 196 ARG 196 200 200 ARG ARG A . n A 1 197 SER 197 201 201 SER SER A . n A 1 198 PHE 198 202 202 PHE PHE A . n A 1 199 HIS 199 203 203 HIS HIS A . n A 1 200 ASN 200 204 204 ASN ASN A . n A 1 201 PHE 201 205 205 PHE PHE A . n A 1 202 THR 202 206 206 THR THR A . n A 1 203 LEU 203 207 207 LEU LEU A . n A 1 204 CYS 204 208 208 CYS CYS A . n A 1 205 TYR 205 209 209 TYR TYR A . n A 1 206 ILE 206 210 210 ILE ILE A . n A 1 207 LYS 207 211 211 LYS LYS A . n A 1 208 GLU 208 212 212 GLU GLU A . n A 1 209 THR 209 213 213 THR THR A . n A 1 210 GLU 210 214 214 GLU GLU A . n A 1 211 LYS 211 215 215 LYS LYS A . n A 1 212 ASP 212 216 216 ASP ASP A . n A 1 213 CYS 213 217 217 CYS CYS A . n A 1 214 LEU 214 218 218 LEU LEU A . n A 1 215 ASN 215 219 219 ASN ASN A . n A 1 216 LEU 216 220 220 LEU LEU A . n A 1 217 ASP 217 221 221 ASP ASP A . n A 1 218 LYS 218 222 222 LYS LYS A . n A 1 219 ASN 219 223 223 ASN ASN A . n A 1 220 LEU 220 224 224 LEU LEU A . n A 1 221 ILE 221 225 225 ILE ILE A . n A 1 222 LYS 222 226 226 LYS LYS A . n A 1 223 TYR 223 227 227 TYR TYR A . n A 1 224 ASP 224 228 228 ASP ASP A . n A 1 225 LEU 225 229 229 LEU LEU A . n A 1 226 GLN 226 230 230 GLN GLN A . n A 1 227 ASN 227 231 231 ASN ASN A . n A 1 228 LEU 228 232 232 LEU LEU A . n A 1 229 LYS 229 233 233 LYS LYS A . n A 1 230 PRO 230 234 234 PRO PRO A . n A 1 231 TYR 231 235 235 TYR TYR A . n A 1 232 THR 232 236 236 THR THR A . n A 1 233 LYS 233 237 237 LYS LYS A . n A 1 234 TYR 234 238 238 TYR TYR A . n A 1 235 VAL 235 239 239 VAL VAL A . n A 1 236 LEU 236 240 240 LEU LEU A . n A 1 237 SER 237 241 241 SER SER A . n A 1 238 LEU 238 242 242 LEU LEU A . n A 1 239 HIS 239 243 243 HIS HIS A . n A 1 240 ALA 240 244 244 ALA ALA A . n A 1 241 TYR 241 245 245 TYR TYR A . n A 1 242 ILE 242 246 246 ILE ILE A . n A 1 243 ILE 243 247 247 ILE ILE A . n A 1 244 ALA 244 248 248 ALA ALA A . n A 1 245 LYS 245 249 249 LYS LYS A . n A 1 246 VAL 246 250 250 VAL VAL A . n A 1 247 GLN 247 251 251 GLN GLN A . n A 1 248 ARG 248 252 252 ARG ARG A . n A 1 249 ASN 249 253 253 ASN ASN A . n A 1 250 GLY 250 254 254 GLY GLY A . n A 1 251 SER 251 255 255 SER SER A . n A 1 252 ALA 252 256 256 ALA ALA A . n A 1 253 ALA 253 257 257 ALA ALA A . n A 1 254 MET 254 258 258 MET MET A . n A 1 255 CYS 255 259 259 CYS CYS A . n A 1 256 HIS 256 260 260 HIS HIS A . n A 1 257 PHE 257 261 261 PHE PHE A . n A 1 258 THR 258 262 262 THR THR A . n A 1 259 THR 259 263 263 THR THR A . n A 1 260 LYS 260 264 264 LYS LYS A . n A 1 261 GLY 261 265 ? ? ? A . n A 1 262 THR 262 266 ? ? ? A . n A 1 263 LYS 263 267 ? ? ? A . n A 1 264 HIS 264 268 ? ? ? A . n A 1 265 HIS 265 269 ? ? ? A . n A 1 266 HIS 266 270 ? ? ? A . n A 1 267 HIS 267 271 ? ? ? A . n A 1 268 HIS 268 272 ? ? ? A . n A 1 269 HIS 269 273 ? ? ? A . n # loop_ _pdbx_nonpoly_scheme.asym_id _pdbx_nonpoly_scheme.entity_id _pdbx_nonpoly_scheme.mon_id _pdbx_nonpoly_scheme.ndb_seq_num _pdbx_nonpoly_scheme.pdb_seq_num _pdbx_nonpoly_scheme.auth_seq_num _pdbx_nonpoly_scheme.pdb_mon_id _pdbx_nonpoly_scheme.auth_mon_id _pdbx_nonpoly_scheme.pdb_strand_id _pdbx_nonpoly_scheme.pdb_ins_code B 2 NAG 1 1265 1265 NAG NAG A . C 2 NAG 1 1266 1266 NAG NAG A . D 2 NAG 1 1267 1267 NAG NAG A . E 2 NAG 1 1268 1268 NAG NAG A . F 2 NAG 1 1269 1269 NAG NAG A . # loop_ _pdbx_struct_mod_residue.id _pdbx_struct_mod_residue.label_asym_id _pdbx_struct_mod_residue.label_comp_id _pdbx_struct_mod_residue.label_seq_id _pdbx_struct_mod_residue.auth_asym_id _pdbx_struct_mod_residue.auth_comp_id _pdbx_struct_mod_residue.auth_seq_id _pdbx_struct_mod_residue.PDB_ins_code _pdbx_struct_mod_residue.parent_comp_id _pdbx_struct_mod_residue.details 1 A ASN 51 A ASN 55 ? ASN 'GLYCOSYLATION SITE' 2 A ASN 57 A ASN 61 ? ASN 'GLYCOSYLATION SITE' 3 A ASN 159 A ASN 163 ? ASN 'GLYCOSYLATION SITE' 4 A ASN 200 A ASN 204 ? ASN 'GLYCOSYLATION SITE' 5 A ASN 249 A ASN 253 ? ASN 'GLYCOSYLATION SITE' # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details author_and_software_defined_assembly _pdbx_struct_assembly.method_details PISA _pdbx_struct_assembly.oligomeric_details monomeric _pdbx_struct_assembly.oligomeric_count 1 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E,F # _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 2016-03-23 2 'Structure model' 1 1 2016-03-30 3 'Structure model' 1 2 2016-05-18 # _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' 'Database references' 2 3 'Structure model' 'Database references' # loop_ _pdbx_refine_tls.pdbx_refine_id _pdbx_refine_tls.id _pdbx_refine_tls.details _pdbx_refine_tls.method _pdbx_refine_tls.origin_x _pdbx_refine_tls.origin_y _pdbx_refine_tls.origin_z _pdbx_refine_tls.T[1][1] _pdbx_refine_tls.T[2][2] _pdbx_refine_tls.T[3][3] _pdbx_refine_tls.T[1][2] _pdbx_refine_tls.T[1][3] _pdbx_refine_tls.T[2][3] _pdbx_refine_tls.L[1][1] _pdbx_refine_tls.L[2][2] _pdbx_refine_tls.L[3][3] _pdbx_refine_tls.L[1][2] _pdbx_refine_tls.L[1][3] _pdbx_refine_tls.L[2][3] _pdbx_refine_tls.S[1][1] _pdbx_refine_tls.S[1][2] _pdbx_refine_tls.S[1][3] _pdbx_refine_tls.S[2][1] _pdbx_refine_tls.S[2][2] _pdbx_refine_tls.S[2][3] _pdbx_refine_tls.S[3][1] _pdbx_refine_tls.S[3][2] _pdbx_refine_tls.S[3][3] 'X-RAY DIFFRACTION' 1 ? refined 24.6644 141.1058 -19.4156 -0.2322 0.0509 0.1123 -0.2334 -0.0199 -0.1268 -1.4865 4.4807 3.1530 0.3052 -0.7025 -1.2918 0.0475 0.1109 0.3791 -0.1215 0.0348 0.6105 -0.1909 -0.3466 -0.0823 'X-RAY DIFFRACTION' 2 ? refined 52.8747 145.9984 -10.1238 -0.0819 0.1718 -0.0684 -0.2382 -0.0791 0.1275 8.5996 3.3533 4.6280 4.2918 4.8487 4.1820 -0.0740 0.2713 0.2230 -0.0384 -0.1557 -0.1520 0.0476 -0.1792 0.2297 'X-RAY DIFFRACTION' 3 ? refined 89.3693 156.8899 10.1905 -0.0960 0.1018 -0.1622 0.0351 0.0006 0.0032 2.7775 4.0196 2.9257 2.1266 -0.5695 -0.2799 -0.1264 -0.0930 0.0734 0.1836 0.0459 -0.0409 -0.0205 0.2553 0.0805 # loop_ _pdbx_refine_tls_group.pdbx_refine_id _pdbx_refine_tls_group.id _pdbx_refine_tls_group.refine_tls_id _pdbx_refine_tls_group.beg_auth_asym_id _pdbx_refine_tls_group.beg_auth_seq_id _pdbx_refine_tls_group.beg_label_asym_id _pdbx_refine_tls_group.beg_label_seq_id _pdbx_refine_tls_group.end_auth_asym_id _pdbx_refine_tls_group.end_auth_seq_id _pdbx_refine_tls_group.end_label_asym_id _pdbx_refine_tls_group.end_label_seq_id _pdbx_refine_tls_group.selection _pdbx_refine_tls_group.selection_details 'X-RAY DIFFRACTION' 1 1 ? ? ? ? ? ? ? ? ? '{ A|10 - A|84 }' 'X-RAY DIFFRACTION' 2 2 ? ? ? ? ? ? ? ? ? '{ A|85 - A|173 }' 'X-RAY DIFFRACTION' 3 3 ? ? ? ? ? ? ? ? ? '{ A|174 - A|264 }' # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal BUSTER refinement 2.11.2 ? 1 HKL-2000 'data reduction' . ? 2 HKL-2000 'data scaling' . ? 3 PHASER phasing . ? 4 # _pdbx_entry_details.entry_id 5FN6 _pdbx_entry_details.compound_details ? _pdbx_entry_details.source_details ? _pdbx_entry_details.nonpolymer_details ? _pdbx_entry_details.sequence_details ;ETG N-TERMINAL RESIDUES DERIVED FROM THE EXPRESSION VECTOR. GTKHHHHHH C-TERMINAL RESIDUES DERIVED FROM THE EXPRESSION VECTOR. ; # 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 127 ? ? -91.75 -77.77 2 1 ASP A 171 ? ? -4.28 150.62 3 1 GLU A 212 ? ? 66.40 -119.65 4 1 ALA A 248 ? ? -86.68 -145.43 # loop_ _pdbx_unobs_or_zero_occ_residues.id _pdbx_unobs_or_zero_occ_residues.PDB_model_num _pdbx_unobs_or_zero_occ_residues.polymer_flag _pdbx_unobs_or_zero_occ_residues.occupancy_flag _pdbx_unobs_or_zero_occ_residues.auth_asym_id _pdbx_unobs_or_zero_occ_residues.auth_comp_id _pdbx_unobs_or_zero_occ_residues.auth_seq_id _pdbx_unobs_or_zero_occ_residues.PDB_ins_code _pdbx_unobs_or_zero_occ_residues.label_asym_id _pdbx_unobs_or_zero_occ_residues.label_comp_id _pdbx_unobs_or_zero_occ_residues.label_seq_id 1 1 Y 1 A GLU 5 ? A GLU 1 2 1 Y 1 A THR 6 ? A THR 2 3 1 Y 1 A GLY 7 ? A GLY 3 4 1 Y 1 A LYS 8 ? A LYS 4 5 1 Y 1 A PRO 9 ? A PRO 5 6 1 Y 1 A ASN 45 ? A ASN 41 7 1 Y 1 A ASN 46 ? A ASN 42 8 1 Y 1 A THR 47 ? A THR 43 9 1 Y 1 A GLY 265 ? A GLY 261 10 1 Y 1 A THR 266 ? A THR 262 11 1 Y 1 A LYS 267 ? A LYS 263 12 1 Y 1 A HIS 268 ? A HIS 264 13 1 Y 1 A HIS 269 ? A HIS 265 14 1 Y 1 A HIS 270 ? A HIS 266 15 1 Y 1 A HIS 271 ? A HIS 267 16 1 Y 1 A HIS 272 ? A HIS 268 17 1 Y 1 A HIS 273 ? A HIS 269 # _pdbx_entity_nonpoly.entity_id 2 _pdbx_entity_nonpoly.name N-ACETYL-D-GLUCOSAMINE _pdbx_entity_nonpoly.comp_id NAG #