data_4UY2 # _entry.id 4UY2 # _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 4UY2 PDBE EBI-61626 WWPDB D_1290061626 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.content_type _pdbx_database_related.details PDB 4UXU unspecified ;CRYSTAL STRUCTURE OF THE EXTRACELLULAR DOMAIN OF THE HUMAN ALPHA9 NICOTINIC ACETYLCHOLINE RECEPTOR IN COMPLEX WITH METHYLLYCACONITINE ; PDB 4D01 unspecified 'CRYSTAL STRUCTURE OF THE EXTRACELLULAR DOMAIN OF THE HUMAN ALPHA9 NICOTINIC ACETYLCHOLINE RECEPTOR' # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 4UY2 _pdbx_database_status.deposit_site PDBE _pdbx_database_status.process_site PDBE _pdbx_database_status.SG_entry . _pdbx_database_status.recvd_initial_deposition_date 2014-08-28 _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 'Giastas, P.' 1 'Zouridakis, M.' 2 'Zarkadas, E.' 3 'Tzartos, S.J.' 4 # _citation.id primary _citation.title 'Crystal Structures of Free and Antagonist-Bound States of Human Alpha9 Nicotinic Receptor Extracellular Domain' _citation.journal_abbrev Nat.Struct.Mol.Biol. _citation.journal_volume 21 _citation.page_first 976 _citation.page_last ? _citation.year 2014 _citation.journal_id_ASTM ? _citation.country US _citation.journal_id_ISSN 1545-9993 _citation.journal_id_CSD ? _citation.book_publisher ? _citation.pdbx_database_id_PubMed 25282151 _citation.pdbx_database_id_DOI 10.1038/NSMB.2900 # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Zouridakis, M.' 1 primary 'Giastas, P.' 2 primary 'Zarkadas, E.' 3 primary 'Chroni-Tzartou, D.' 4 primary 'Bregestovski, P.' 5 primary 'Tzartos, S.J.' 6 # _cell.entry_id 4UY2 _cell.length_a 42.319 _cell.length_b 119.348 _cell.length_c 79.107 _cell.angle_alpha 90.00 _cell.angle_beta 103.02 _cell.angle_gamma 90.00 _cell.Z_PDB 4 _cell.pdbx_unique_axis ? # _symmetry.entry_id 4UY2 _symmetry.space_group_name_H-M 'P 1 21 1' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 4 # 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 'NEURONAL ACETYLCHOLINE RECEPTOR SUBUNIT ALPHA-9' 25307.029 2 ? ? 'EXTRACELLULAR DOMAIN, RESIDUES 26-237' ? 2 polymer nat 'ALPHA-BUNGAROTOXIN ISOFORM V31' 8033.334 2 ? ? ? ? 3 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 4 ? ? ? ? # loop_ _entity_name_com.entity_id _entity_name_com.name 1 'ALPHA9 NICOTINIC ACETYLCHOLINE RECEPTOR, NICOTINIC ACETYLCHOLINE RECEPTOR SUBUNIT ALPHA-9, NACHR ALPHA-9' 2 'ALPHA-BTX V31, ALPHA-BGT(V31), BGTX V31, LONG NEUROTOXIN 1' # loop_ _entity_poly.entity_id _entity_poly.type _entity_poly.nstd_linkage _entity_poly.nstd_monomer _entity_poly.pdbx_seq_one_letter_code _entity_poly.pdbx_seq_one_letter_code_can _entity_poly.pdbx_strand_id _entity_poly.pdbx_target_identifier 1 'polypeptide(L)' no no ;ADGKYAQKLFNDLFEDYSNALRPVEDTDKVLNVTLQITLSQIKDMDERNQILTAYLWIRQIWHDAYLTWDRDQYDGLDSI RIPSDLVWRPDIVLYNKADDESSEPVNTNVVLRYDGLITWDAPAITKSSCVVDVTYFPFDNQQCNLTFGSWTYNGNQVDI FNALDSGDLSDFIEDVEWEVHGMPAVKNVISYGCCSEPYPDVTFTLLLKRRSHHHHHH ; ;ADGKYAQKLFNDLFEDYSNALRPVEDTDKVLNVTLQITLSQIKDMDERNQILTAYLWIRQIWHDAYLTWDRDQYDGLDSI RIPSDLVWRPDIVLYNKADDESSEPVNTNVVLRYDGLITWDAPAITKSSCVVDVTYFPFDNQQCNLTFGSWTYNGNQVDI FNALDSGDLSDFIEDVEWEVHGMPAVKNVISYGCCSEPYPDVTFTLLLKRRSHHHHHH ; A,B ? 2 'polypeptide(L)' no no IVCHTTATSPISAVTCPPGENLCYRKMWCDVFCSSRGKVVELGCAATCPSKKPYEEVTCCSTDKCNPHPKQRPG IVCHTTATSPISAVTCPPGENLCYRKMWCDVFCSSRGKVVELGCAATCPSKKPYEEVTCCSTDKCNPHPKQRPG C,D ? # loop_ _entity_poly_seq.entity_id _entity_poly_seq.num _entity_poly_seq.mon_id _entity_poly_seq.hetero 1 1 ALA n 1 2 ASP n 1 3 GLY n 1 4 LYS n 1 5 TYR n 1 6 ALA n 1 7 GLN n 1 8 LYS n 1 9 LEU n 1 10 PHE n 1 11 ASN n 1 12 ASP n 1 13 LEU n 1 14 PHE n 1 15 GLU n 1 16 ASP n 1 17 TYR n 1 18 SER n 1 19 ASN n 1 20 ALA n 1 21 LEU n 1 22 ARG n 1 23 PRO n 1 24 VAL n 1 25 GLU n 1 26 ASP n 1 27 THR n 1 28 ASP n 1 29 LYS n 1 30 VAL n 1 31 LEU n 1 32 ASN n 1 33 VAL n 1 34 THR n 1 35 LEU n 1 36 GLN n 1 37 ILE n 1 38 THR n 1 39 LEU n 1 40 SER n 1 41 GLN n 1 42 ILE n 1 43 LYS n 1 44 ASP n 1 45 MET n 1 46 ASP n 1 47 GLU n 1 48 ARG n 1 49 ASN n 1 50 GLN n 1 51 ILE n 1 52 LEU n 1 53 THR n 1 54 ALA n 1 55 TYR n 1 56 LEU n 1 57 TRP n 1 58 ILE n 1 59 ARG n 1 60 GLN n 1 61 ILE n 1 62 TRP n 1 63 HIS n 1 64 ASP n 1 65 ALA n 1 66 TYR n 1 67 LEU n 1 68 THR n 1 69 TRP n 1 70 ASP n 1 71 ARG n 1 72 ASP n 1 73 GLN n 1 74 TYR n 1 75 ASP n 1 76 GLY n 1 77 LEU n 1 78 ASP n 1 79 SER n 1 80 ILE n 1 81 ARG n 1 82 ILE n 1 83 PRO n 1 84 SER n 1 85 ASP n 1 86 LEU n 1 87 VAL n 1 88 TRP n 1 89 ARG n 1 90 PRO n 1 91 ASP n 1 92 ILE n 1 93 VAL n 1 94 LEU n 1 95 TYR n 1 96 ASN n 1 97 LYS n 1 98 ALA n 1 99 ASP n 1 100 ASP n 1 101 GLU n 1 102 SER n 1 103 SER n 1 104 GLU n 1 105 PRO n 1 106 VAL n 1 107 ASN n 1 108 THR n 1 109 ASN n 1 110 VAL n 1 111 VAL n 1 112 LEU n 1 113 ARG n 1 114 TYR n 1 115 ASP n 1 116 GLY n 1 117 LEU n 1 118 ILE n 1 119 THR n 1 120 TRP n 1 121 ASP n 1 122 ALA n 1 123 PRO n 1 124 ALA n 1 125 ILE n 1 126 THR n 1 127 LYS n 1 128 SER n 1 129 SER n 1 130 CYS n 1 131 VAL n 1 132 VAL n 1 133 ASP n 1 134 VAL n 1 135 THR n 1 136 TYR n 1 137 PHE n 1 138 PRO n 1 139 PHE n 1 140 ASP n 1 141 ASN n 1 142 GLN n 1 143 GLN n 1 144 CYS n 1 145 ASN n 1 146 LEU n 1 147 THR n 1 148 PHE n 1 149 GLY n 1 150 SER n 1 151 TRP n 1 152 THR n 1 153 TYR n 1 154 ASN n 1 155 GLY n 1 156 ASN n 1 157 GLN n 1 158 VAL n 1 159 ASP n 1 160 ILE n 1 161 PHE n 1 162 ASN n 1 163 ALA n 1 164 LEU n 1 165 ASP n 1 166 SER n 1 167 GLY n 1 168 ASP n 1 169 LEU n 1 170 SER n 1 171 ASP n 1 172 PHE n 1 173 ILE n 1 174 GLU n 1 175 ASP n 1 176 VAL n 1 177 GLU n 1 178 TRP n 1 179 GLU n 1 180 VAL n 1 181 HIS n 1 182 GLY n 1 183 MET n 1 184 PRO n 1 185 ALA n 1 186 VAL n 1 187 LYS n 1 188 ASN n 1 189 VAL n 1 190 ILE n 1 191 SER n 1 192 TYR n 1 193 GLY n 1 194 CYS n 1 195 CYS n 1 196 SER n 1 197 GLU n 1 198 PRO n 1 199 TYR n 1 200 PRO n 1 201 ASP n 1 202 VAL n 1 203 THR n 1 204 PHE n 1 205 THR n 1 206 LEU n 1 207 LEU n 1 208 LEU n 1 209 LYS n 1 210 ARG n 1 211 ARG n 1 212 SER n 1 213 HIS n 1 214 HIS n 1 215 HIS n 1 216 HIS n 1 217 HIS n 1 218 HIS n 2 1 ILE n 2 2 VAL n 2 3 CYS n 2 4 HIS n 2 5 THR n 2 6 THR n 2 7 ALA n 2 8 THR n 2 9 SER n 2 10 PRO n 2 11 ILE n 2 12 SER n 2 13 ALA n 2 14 VAL n 2 15 THR n 2 16 CYS n 2 17 PRO n 2 18 PRO n 2 19 GLY n 2 20 GLU n 2 21 ASN n 2 22 LEU n 2 23 CYS n 2 24 TYR n 2 25 ARG n 2 26 LYS n 2 27 MET n 2 28 TRP n 2 29 CYS n 2 30 ASP n 2 31 VAL n 2 32 PHE n 2 33 CYS n 2 34 SER n 2 35 SER n 2 36 ARG n 2 37 GLY n 2 38 LYS n 2 39 VAL n 2 40 VAL n 2 41 GLU n 2 42 LEU n 2 43 GLY n 2 44 CYS n 2 45 ALA n 2 46 ALA n 2 47 THR n 2 48 CYS n 2 49 PRO n 2 50 SER n 2 51 LYS n 2 52 LYS n 2 53 PRO n 2 54 TYR n 2 55 GLU n 2 56 GLU n 2 57 VAL n 2 58 THR n 2 59 CYS n 2 60 CYS n 2 61 SER n 2 62 THR n 2 63 ASP n 2 64 LYS n 2 65 CYS n 2 66 ASN n 2 67 PRO n 2 68 HIS n 2 69 PRO n 2 70 LYS n 2 71 GLN n 2 72 ARG n 2 73 PRO n 2 74 GLY 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 ? _entity_src_gen.pdbx_host_org_scientific_name 'KOMAGATAELLA PASTORIS' _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 4922 _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 X33 _entity_src_gen.pdbx_host_org_variant ? _entity_src_gen.pdbx_host_org_cell_line ? _entity_src_gen.pdbx_host_org_atcc ? _entity_src_gen.pdbx_host_org_culture_collection ? _entity_src_gen.pdbx_host_org_cell ? _entity_src_gen.pdbx_host_org_organelle ? _entity_src_gen.pdbx_host_org_cellular_location ? _entity_src_gen.pdbx_host_org_vector_type 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 PPICZAA _entity_src_gen.plasmid_details ? _entity_src_gen.pdbx_description ? # _entity_src_nat.entity_id 2 _entity_src_nat.pdbx_src_id 1 _entity_src_nat.pdbx_alt_source_flag sample _entity_src_nat.pdbx_beg_seq_num ? _entity_src_nat.pdbx_end_seq_num ? _entity_src_nat.common_name 'MANY-BANDED KRAIT' _entity_src_nat.pdbx_organism_scientific 'BUNGARUS MULTICINCTUS' _entity_src_nat.pdbx_ncbi_taxonomy_id 8616 _entity_src_nat.genus ? _entity_src_nat.species ? _entity_src_nat.strain ? _entity_src_nat.tissue ? _entity_src_nat.tissue_fraction ? _entity_src_nat.pdbx_secretion ? _entity_src_nat.pdbx_fragment ? _entity_src_nat.pdbx_variant ? _entity_src_nat.pdbx_cell_line ? _entity_src_nat.pdbx_atcc ? _entity_src_nat.pdbx_cellular_location ? _entity_src_nat.pdbx_organ ? _entity_src_nat.pdbx_organelle ? _entity_src_nat.pdbx_cell ? _entity_src_nat.pdbx_plasmid_name ? _entity_src_nat.pdbx_plasmid_details ? _entity_src_nat.details ? # loop_ _struct_ref.id _struct_ref.db_name _struct_ref.db_code _struct_ref.entity_id _struct_ref.pdbx_seq_one_letter_code _struct_ref.pdbx_align_begin _struct_ref.pdbx_db_accession _struct_ref.pdbx_db_isoform 1 UNP ACHA9_HUMAN 1 ? ? Q9UGM1 ? 2 UNP NXL1V_BUNMU 2 ? ? P60616 ? # loop_ _struct_ref_seq.align_id _struct_ref_seq.ref_id _struct_ref_seq.pdbx_PDB_id_code _struct_ref_seq.pdbx_strand_id _struct_ref_seq.seq_align_beg _struct_ref_seq.pdbx_seq_align_beg_ins_code _struct_ref_seq.seq_align_end _struct_ref_seq.pdbx_seq_align_end_ins_code _struct_ref_seq.pdbx_db_accession _struct_ref_seq.db_align_beg _struct_ref_seq.pdbx_db_align_beg_ins_code _struct_ref_seq.db_align_end _struct_ref_seq.pdbx_db_align_end_ins_code _struct_ref_seq.pdbx_auth_seq_align_beg _struct_ref_seq.pdbx_auth_seq_align_end 1 1 4UY2 A 1 ? 212 ? Q9UGM1 26 ? 237 ? 1 212 2 1 4UY2 B 1 ? 212 ? Q9UGM1 26 ? 237 ? 1 212 3 2 4UY2 C 1 ? 74 ? P60616 22 ? 95 ? 1 74 4 2 4UY2 D 1 ? 74 ? P60616 22 ? 95 ? 1 74 # 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 4UY2 HIS A 213 ? UNP Q9UGM1 ? ? 'expression tag' 213 1 1 4UY2 HIS A 214 ? UNP Q9UGM1 ? ? 'expression tag' 214 2 1 4UY2 HIS A 215 ? UNP Q9UGM1 ? ? 'expression tag' 215 3 1 4UY2 HIS A 216 ? UNP Q9UGM1 ? ? 'expression tag' 216 4 1 4UY2 HIS A 217 ? UNP Q9UGM1 ? ? 'expression tag' 217 5 1 4UY2 HIS A 218 ? UNP Q9UGM1 ? ? 'expression tag' 218 6 2 4UY2 HIS B 213 ? UNP Q9UGM1 ? ? 'expression tag' 213 7 2 4UY2 HIS B 214 ? UNP Q9UGM1 ? ? 'expression tag' 214 8 2 4UY2 HIS B 215 ? UNP Q9UGM1 ? ? 'expression tag' 215 9 2 4UY2 HIS B 216 ? UNP Q9UGM1 ? ? 'expression tag' 216 10 2 4UY2 HIS B 217 ? UNP Q9UGM1 ? ? 'expression tag' 217 11 2 4UY2 HIS B 218 ? UNP Q9UGM1 ? ? 'expression tag' 218 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 4UY2 _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 2.78 _exptl_crystal.density_percent_sol 55.8 _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 7.0 _exptl_crystal_grow.pdbx_pH_range ? _exptl_crystal_grow.pdbx_details '0.1 M MES PH 6.0, 0.2 M NACL, 30% W/V JEFFAMINE ED2003' # _diffrn.id 1 _diffrn.ambient_temp 100 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector PIXEL _diffrn_detector.type 'DECTRIS PILATUS 2M' _diffrn_detector.pdbx_collection_date 2013-08-30 _diffrn_detector.details ? # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator ? _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 1.0000 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source SYNCHROTRON _diffrn_source.type 'SLS BEAMLINE X06DA' _diffrn_source.pdbx_synchrotron_site SLS _diffrn_source.pdbx_synchrotron_beamline X06DA _diffrn_source.pdbx_wavelength 1.0000 _diffrn_source.pdbx_wavelength_list ? # _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 _reflns.entry_id 4UY2 _reflns.observed_criterion_sigma_I 1.0 _reflns.observed_criterion_sigma_F ? _reflns.d_resolution_low 47.00 _reflns.d_resolution_high 2.70 _reflns.number_obs 21021 _reflns.number_all ? _reflns.percent_possible_obs 99.5 _reflns.pdbx_Rmerge_I_obs 0.11 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI 9.90 _reflns.B_iso_Wilson_estimate 67.36 _reflns.pdbx_redundancy 5.1 # _reflns_shell.pdbx_diffrn_id 1 _reflns_shell.pdbx_ordinal 1 _reflns_shell.d_res_high 2.70 _reflns_shell.d_res_low 2.80 _reflns_shell.percent_possible_all 97.0 _reflns_shell.Rmerge_I_obs 1.45 _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs 1.00 _reflns_shell.pdbx_redundancy 5.2 # _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.entry_id 4UY2 _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.ls_number_reflns_obs 20942 _refine.ls_number_reflns_all ? _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F 1.12 _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 47.185 _refine.ls_d_res_high 2.697 _refine.ls_percent_reflns_obs 97.81 _refine.ls_R_factor_obs 0.2617 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.2581 _refine.ls_R_factor_R_free 0.3312 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 4.9 _refine.ls_number_reflns_R_free 2009 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc ? _refine.correlation_coeff_Fo_to_Fc_free ? _refine.B_iso_mean 104 _refine.aniso_B[1][1] ? _refine.aniso_B[2][2] ? _refine.aniso_B[3][3] ? _refine.aniso_B[1][2] ? _refine.aniso_B[1][3] ? _refine.aniso_B[2][3] ? _refine.solvent_model_details 'FLAT BULK SOLVENT MODEL' _refine.solvent_model_param_ksol ? _refine.solvent_model_param_bsol ? _refine.pdbx_solvent_vdw_probe_radii 1.11 _refine.pdbx_solvent_ion_probe_radii ? _refine.pdbx_solvent_shrinkage_radii 0.90 _refine.pdbx_ls_cross_valid_method ? _refine.details ? _refine.pdbx_starting_model 'PDB ENTRIES 1D01, 2QC1' _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_stereochemistry_target_values ML _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details ? _refine.pdbx_overall_ESU_R ? _refine.pdbx_overall_ESU_R_Free ? _refine.overall_SU_ML 0.54 _refine.pdbx_overall_phase_error 46.62 _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 ? # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 4412 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 56 _refine_hist.number_atoms_solvent 0 _refine_hist.number_atoms_total 4468 _refine_hist.d_res_high 2.697 _refine_hist.d_res_low 47.185 # 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 f_bond_d 0.017 ? ? 4598 'X-RAY DIFFRACTION' ? f_angle_d 2.425 ? ? 6272 'X-RAY DIFFRACTION' ? f_dihedral_angle_d 18.072 ? ? 1656 'X-RAY DIFFRACTION' ? f_chiral_restr 0.101 ? ? 710 'X-RAY DIFFRACTION' ? f_plane_restr 0.014 ? ? 800 'X-RAY DIFFRACTION' ? # loop_ _refine_ls_shell.pdbx_refine_id _refine_ls_shell.pdbx_total_number_of_bins_used _refine_ls_shell.d_res_high _refine_ls_shell.d_res_low _refine_ls_shell.number_reflns_R_work _refine_ls_shell.R_factor_R_work _refine_ls_shell.percent_reflns_obs _refine_ls_shell.R_factor_R_free _refine_ls_shell.R_factor_R_free_error _refine_ls_shell.percent_reflns_R_free _refine_ls_shell.number_reflns_R_free _refine_ls_shell.number_reflns_all _refine_ls_shell.R_factor_all 'X-RAY DIFFRACTION' . 2.6970 2.7645 2627 0.4276 94.00 0.4782 . . 131 . . 'X-RAY DIFFRACTION' . 2.7645 2.8392 2768 0.4120 98.00 0.4787 . . 154 . . 'X-RAY DIFFRACTION' . 2.8392 2.9227 2782 0.4077 98.00 0.4660 . . 143 . . 'X-RAY DIFFRACTION' . 2.9227 3.0171 2810 0.3767 99.00 0.4227 . . 139 . . 'X-RAY DIFFRACTION' . 3.0171 3.1249 2701 0.3516 98.00 0.4095 . . 146 . . 'X-RAY DIFFRACTION' . 3.1249 3.2500 2843 0.3195 98.00 0.4075 . . 144 . . 'X-RAY DIFFRACTION' . 3.2500 3.3978 2721 0.3091 99.00 0.4445 . . 143 . . 'X-RAY DIFFRACTION' . 3.3978 3.5769 2806 0.2798 99.00 0.3711 . . 149 . . 'X-RAY DIFFRACTION' . 3.5769 3.8009 2758 0.2613 98.00 0.2886 . . 148 . . 'X-RAY DIFFRACTION' . 3.8009 4.0943 2764 0.2395 99.00 0.2953 . . 146 . . 'X-RAY DIFFRACTION' . 4.0943 4.5060 2767 0.2093 98.00 0.3179 . . 145 . . 'X-RAY DIFFRACTION' . 4.5060 5.1573 2726 0.2032 96.00 0.2500 . . 143 . . 'X-RAY DIFFRACTION' . 5.1573 6.4950 2761 0.2364 98.00 0.3197 . . 146 . . 'X-RAY DIFFRACTION' . 6.4950 47.1918 2792 0.2075 98.00 0.2658 . . 132 . . # _struct.entry_id 4UY2 _struct.title 'Crystal structure of the complex of the extracellular domain of human alpha9 nAChR with alpha-bungarotoxin.' _struct.pdbx_descriptor 'NEURONAL ACETYLCHOLINE RECEPTOR SUBUNIT ALPHA-9, ALPHA-BUNGAROTOXIN ISOFORM V31' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 4UY2 _struct_keywords.pdbx_keywords 'TOXIN-BINDING PROTEIN/TOXIN' _struct_keywords.text 'TOXIN-BINDING PROTEIN-TOXIN COMPLEX, LIGAND BINDING DOMAIN, CYS-LOOP RECEPTOR' # loop_ _struct_asym.id _struct_asym.pdbx_blank_PDB_chainid_flag _struct_asym.pdbx_modified _struct_asym.entity_id _struct_asym.details A N N 1 ? B N N 1 ? C N N 2 ? D N N 2 ? E N N 3 ? F N N 3 ? G N N 3 ? H N N 3 ? # _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 TYR A 5 ? LEU A 9 ? TYR A 5 LEU A 9 5 ? 5 HELX_P HELX_P2 2 ARG A 71 ? ASP A 75 ? ARG A 71 ASP A 75 5 ? 5 HELX_P HELX_P3 3 ASP A 85 ? VAL A 87 ? ASP A 85 VAL A 87 5 ? 3 HELX_P HELX_P4 4 ASP B 70 ? TYR B 74 ? ASP B 70 TYR B 74 5 ? 5 HELX_P HELX_P5 5 ASP B 85 ? VAL B 87 ? ASP B 85 VAL B 87 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 130 SG ? ? ? 1_555 A CYS 144 SG ? ? A CYS 130 A CYS 144 1_555 ? ? ? ? ? ? ? 2.030 ? disulf2 disulf ? ? B CYS 130 SG ? ? ? 1_555 B CYS 144 SG ? ? B CYS 130 B CYS 144 1_555 ? ? ? ? ? ? ? 2.049 ? disulf3 disulf ? ? C CYS 3 SG ? ? ? 1_555 C CYS 16 SG ? ? C CYS 3 C CYS 16 1_555 ? ? ? ? ? ? ? 2.041 ? disulf4 disulf ? ? C CYS 3 SG ? ? ? 1_555 C CYS 23 SG ? ? C CYS 3 C CYS 23 1_555 ? ? ? ? ? ? ? 2.046 ? disulf5 disulf ? ? C CYS 16 SG ? ? ? 1_555 C CYS 44 SG ? ? C CYS 16 C CYS 44 1_555 ? ? ? ? ? ? ? 2.023 ? disulf6 disulf ? ? C CYS 29 SG ? ? ? 1_555 C CYS 33 SG ? ? C CYS 29 C CYS 33 1_555 ? ? ? ? ? ? ? 2.062 ? disulf7 disulf ? ? C CYS 48 SG ? ? ? 1_555 C CYS 59 SG ? ? C CYS 48 C CYS 59 1_555 ? ? ? ? ? ? ? 2.042 ? disulf8 disulf ? ? C CYS 60 SG ? ? ? 1_555 C CYS 65 SG ? ? C CYS 60 C CYS 65 1_555 ? ? ? ? ? ? ? 2.032 ? disulf9 disulf ? ? D CYS 3 SG ? ? ? 1_555 D CYS 16 SG ? ? D CYS 3 D CYS 16 1_555 ? ? ? ? ? ? ? 2.048 ? disulf10 disulf ? ? D CYS 3 SG ? ? ? 1_555 D CYS 23 SG ? ? D CYS 3 D CYS 23 1_555 ? ? ? ? ? ? ? 2.051 ? disulf11 disulf ? ? D CYS 16 SG ? ? ? 1_555 D CYS 44 SG ? ? D CYS 16 D CYS 44 1_555 ? ? ? ? ? ? ? 2.020 ? disulf12 disulf ? ? D CYS 29 SG ? ? ? 1_555 D CYS 33 SG ? ? D CYS 29 D CYS 33 1_555 ? ? ? ? ? ? ? 2.030 ? disulf13 disulf ? ? D CYS 48 SG ? ? ? 1_555 D CYS 59 SG ? ? D CYS 48 D CYS 59 1_555 ? ? ? ? ? ? ? 2.031 ? disulf14 disulf ? ? D CYS 60 SG ? ? ? 1_555 D CYS 65 SG ? ? D CYS 60 D CYS 65 1_555 ? ? ? ? ? ? ? 2.031 ? covale1 covale ? ? A ASN 32 ND2 ? ? ? 1_555 E NAG . C1 ? ? A ASN 32 A NAG 1214 1_555 ? ? ? ? ? ? ? 1.420 ? covale2 covale ? ? A ASN 145 ND2 ? ? ? 1_555 F NAG . C1 ? ? A ASN 145 A NAG 1215 1_555 ? ? ? ? ? ? ? 1.428 ? covale3 covale ? ? B ASN 32 ND2 ? ? ? 1_555 G NAG . C1 ? ? B ASN 32 B NAG 1214 1_555 ? ? ? ? ? ? ? 1.455 ? covale4 covale ? ? B ASN 145 ND2 ? ? ? 1_555 H NAG . C1 ? ? B ASN 145 B NAG 1215 1_555 ? ? ? ? ? ? ? 1.428 ? # 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 PHE 137 A . ? PHE 137 A PRO 138 A ? PRO 138 A 1 10.32 2 PHE 137 B . ? PHE 137 B PRO 138 B ? PRO 138 B 1 -0.51 3 SER 9 C . ? SER 9 C PRO 10 C ? PRO 10 C 1 -8.52 4 SER 9 D . ? SER 9 D PRO 10 D ? PRO 10 D 1 -6.04 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details AA ? 8 ? AB ? 6 ? AC ? 7 ? BA ? 8 ? BB ? 6 ? BC ? 7 ? CA ? 2 ? CB ? 3 ? DA ? 2 ? DB ? 3 ? # 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 AA 3 4 ? anti-parallel AA 4 5 ? anti-parallel AA 5 6 ? anti-parallel AA 6 7 ? anti-parallel AA 7 8 ? anti-parallel AB 1 2 ? anti-parallel AB 2 3 ? anti-parallel AB 3 4 ? anti-parallel AB 4 5 ? anti-parallel AB 5 6 ? parallel AC 1 2 ? anti-parallel AC 2 3 ? anti-parallel AC 3 4 ? anti-parallel AC 4 5 ? anti-parallel AC 5 6 ? anti-parallel AC 6 7 ? anti-parallel BA 1 2 ? anti-parallel BA 2 3 ? anti-parallel BA 3 4 ? anti-parallel BA 4 5 ? anti-parallel BA 5 6 ? anti-parallel BA 6 7 ? anti-parallel BA 7 8 ? anti-parallel BB 1 2 ? anti-parallel BB 2 3 ? anti-parallel BB 3 4 ? anti-parallel BB 4 5 ? anti-parallel BB 5 6 ? parallel BC 1 2 ? anti-parallel BC 2 3 ? anti-parallel BC 3 4 ? anti-parallel BC 4 5 ? anti-parallel BC 5 6 ? anti-parallel BC 6 7 ? anti-parallel CA 1 2 ? anti-parallel CB 1 2 ? anti-parallel CB 2 3 ? anti-parallel DA 1 2 ? anti-parallel DB 1 2 ? anti-parallel DB 2 3 ? 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 SER A 79 ? PRO A 83 ? SER A 79 PRO A 83 AA 2 ASN A 109 ? ARG A 113 ? ASN A 109 ARG A 113 AA 3 LEU A 117 ? TRP A 120 ? LEU A 117 TRP A 120 AA 4 ILE A 51 ? HIS A 63 ? ILE A 51 HIS A 63 AA 5 PRO A 123 ? VAL A 132 ? PRO A 123 VAL A 132 AA 6 GLN A 142 ? SER A 150 ? GLN A 142 SER A 150 AA 7 TYR A 199 ? LEU A 208 ? TYR A 199 LEU A 208 AA 8 LYS A 187 ? ILE A 190 ? LYS A 187 ILE A 190 AB 1 SER A 79 ? PRO A 83 ? SER A 79 PRO A 83 AB 2 ASN A 109 ? ARG A 113 ? ASN A 109 ARG A 113 AB 3 LEU A 117 ? TRP A 120 ? LEU A 117 TRP A 120 AB 4 ILE A 51 ? HIS A 63 ? ILE A 51 HIS A 63 AB 5 LEU A 31 ? ASP A 46 ? LEU A 31 ASP A 46 AB 6 VAL A 158 ? ASN A 162 ? VAL A 158 ASN A 162 AC 1 SER A 79 ? PRO A 83 ? SER A 79 PRO A 83 AC 2 ASN A 109 ? ARG A 113 ? ASN A 109 ARG A 113 AC 3 LEU A 117 ? TRP A 120 ? LEU A 117 TRP A 120 AC 4 ILE A 51 ? HIS A 63 ? ILE A 51 HIS A 63 AC 5 PRO A 123 ? VAL A 132 ? PRO A 123 VAL A 132 AC 6 GLN A 142 ? SER A 150 ? GLN A 142 SER A 150 AC 7 ILE A 92 ? LEU A 94 ? ILE A 92 LEU A 94 BA 1 SER B 79 ? PRO B 83 ? SER B 79 PRO B 83 BA 2 ASN B 109 ? ARG B 113 ? ASN B 109 ARG B 113 BA 3 LEU B 117 ? TRP B 120 ? LEU B 117 TRP B 120 BA 4 ILE B 51 ? HIS B 63 ? ILE B 51 HIS B 63 BA 5 PRO B 123 ? ASP B 133 ? PRO B 123 ASP B 133 BA 6 ASN B 141 ? SER B 150 ? ASN B 141 SER B 150 BA 7 TYR B 199 ? LEU B 207 ? TYR B 199 LEU B 207 BA 8 ALA B 185 ? ILE B 190 ? ALA B 185 ILE B 190 BB 1 SER B 79 ? PRO B 83 ? SER B 79 PRO B 83 BB 2 ASN B 109 ? ARG B 113 ? ASN B 109 ARG B 113 BB 3 LEU B 117 ? TRP B 120 ? LEU B 117 TRP B 120 BB 4 ILE B 51 ? HIS B 63 ? ILE B 51 HIS B 63 BB 5 LEU B 31 ? ASP B 46 ? LEU B 31 ASP B 46 BB 6 VAL B 158 ? ASN B 162 ? VAL B 158 ASN B 162 BC 1 SER B 79 ? PRO B 83 ? SER B 79 PRO B 83 BC 2 ASN B 109 ? ARG B 113 ? ASN B 109 ARG B 113 BC 3 LEU B 117 ? TRP B 120 ? LEU B 117 TRP B 120 BC 4 ILE B 51 ? HIS B 63 ? ILE B 51 HIS B 63 BC 5 PRO B 123 ? ASP B 133 ? PRO B 123 ASP B 133 BC 6 ASN B 141 ? SER B 150 ? ASN B 141 SER B 150 BC 7 ILE B 92 ? LEU B 94 ? ILE B 92 LEU B 94 CA 1 VAL C 2 ? THR C 5 ? VAL C 2 THR C 5 CA 2 SER C 12 ? THR C 15 ? SER C 12 THR C 15 CB 1 VAL C 39 ? ALA C 45 ? VAL C 39 ALA C 45 CB 2 LEU C 22 ? TRP C 28 ? LEU C 22 TRP C 28 CB 3 THR C 58 ? CYS C 60 ? THR C 58 CYS C 60 DA 1 VAL D 2 ? THR D 5 ? VAL D 2 THR D 5 DA 2 SER D 12 ? THR D 15 ? SER D 12 THR D 15 DB 1 VAL D 39 ? ALA D 45 ? VAL D 39 ALA D 45 DB 2 LEU D 22 ? TRP D 28 ? LEU D 22 TRP D 28 DB 3 THR D 58 ? CYS D 60 ? THR D 58 CYS D 60 # 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 ILE A 82 ? N ILE A 82 O VAL A 110 ? O VAL A 110 AA 2 3 N ARG A 113 ? N ARG A 113 O LEU A 117 ? O LEU A 117 AA 3 4 N TRP A 120 ? N TRP A 120 O GLN A 60 ? O GLN A 60 AA 4 5 N LEU A 56 ? N LEU A 56 O ALA A 124 ? O ALA A 124 AA 5 6 N VAL A 131 ? N VAL A 131 O GLN A 143 ? O GLN A 143 AA 6 7 N PHE A 148 ? N PHE A 148 O VAL A 202 ? O VAL A 202 AA 7 8 N ASP A 201 ? N ASP A 201 O ASN A 188 ? O ASN A 188 AB 1 2 N ILE A 82 ? N ILE A 82 O VAL A 110 ? O VAL A 110 AB 2 3 N ARG A 113 ? N ARG A 113 O LEU A 117 ? O LEU A 117 AB 3 4 N TRP A 120 ? N TRP A 120 O GLN A 60 ? O GLN A 60 AB 4 5 N ILE A 61 ? N ILE A 61 O THR A 34 ? O THR A 34 AB 5 6 N VAL A 33 ? N VAL A 33 O ASP A 159 ? O ASP A 159 AC 1 2 N ILE A 82 ? N ILE A 82 O VAL A 110 ? O VAL A 110 AC 2 3 N ARG A 113 ? N ARG A 113 O LEU A 117 ? O LEU A 117 AC 3 4 N TRP A 120 ? N TRP A 120 O GLN A 60 ? O GLN A 60 AC 4 5 N LEU A 56 ? N LEU A 56 O ALA A 124 ? O ALA A 124 AC 5 6 N VAL A 131 ? N VAL A 131 O GLN A 143 ? O GLN A 143 AC 6 7 N GLY A 149 ? N GLY A 149 O VAL A 93 ? O VAL A 93 BA 1 2 N ILE B 82 ? N ILE B 82 O VAL B 110 ? O VAL B 110 BA 2 3 N ARG B 113 ? N ARG B 113 O LEU B 117 ? O LEU B 117 BA 3 4 N TRP B 120 ? N TRP B 120 O GLN B 60 ? O GLN B 60 BA 4 5 N LEU B 56 ? N LEU B 56 O ALA B 124 ? O ALA B 124 BA 5 6 N ASP B 133 ? N ASP B 133 O ASN B 141 ? O ASN B 141 BA 6 7 N PHE B 148 ? N PHE B 148 O VAL B 202 ? O VAL B 202 BA 7 8 N THR B 203 ? N THR B 203 O VAL B 186 ? O VAL B 186 BB 1 2 N ILE B 82 ? N ILE B 82 O VAL B 110 ? O VAL B 110 BB 2 3 N ARG B 113 ? N ARG B 113 O LEU B 117 ? O LEU B 117 BB 3 4 N TRP B 120 ? N TRP B 120 O GLN B 60 ? O GLN B 60 BB 4 5 N ILE B 61 ? N ILE B 61 O THR B 34 ? O THR B 34 BB 5 6 N VAL B 33 ? N VAL B 33 O ASP B 159 ? O ASP B 159 BC 1 2 N ILE B 82 ? N ILE B 82 O VAL B 110 ? O VAL B 110 BC 2 3 N ARG B 113 ? N ARG B 113 O LEU B 117 ? O LEU B 117 BC 3 4 N TRP B 120 ? N TRP B 120 O GLN B 60 ? O GLN B 60 BC 4 5 N LEU B 56 ? N LEU B 56 O ALA B 124 ? O ALA B 124 BC 5 6 N ASP B 133 ? N ASP B 133 O ASN B 141 ? O ASN B 141 BC 6 7 N GLY B 149 ? N GLY B 149 O VAL B 93 ? O VAL B 93 CA 1 2 N THR C 5 ? N THR C 5 O SER C 12 ? O SER C 12 CB 1 2 N ALA C 45 ? N ALA C 45 O LEU C 22 ? O LEU C 22 CB 2 3 N ARG C 25 ? N ARG C 25 O THR C 58 ? O THR C 58 DA 1 2 N THR D 5 ? N THR D 5 O SER D 12 ? O SER D 12 DB 1 2 N ALA D 45 ? N ALA D 45 O LEU D 22 ? O LEU D 22 DB 2 3 N ARG D 25 ? N ARG D 25 O THR D 58 ? O THR D 58 # 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 ? ? ? ? 4 'Binding site for Mono-Saccharide NAG A1214 bound to ASN A 32' AC2 Software ? ? ? ? 4 'Binding site for Mono-Saccharide NAG A1215 bound to ASN A 145' AC3 Software ? ? ? ? 4 'Binding site for Mono-Saccharide NAG B1214 bound to ASN B 32' AC4 Software ? ? ? ? 4 'Binding site for Mono-Saccharide NAG B1215 bound to ASN B 145' # loop_ _struct_site_gen.id _struct_site_gen.site_id _struct_site_gen.pdbx_num_res _struct_site_gen.label_comp_id _struct_site_gen.label_asym_id _struct_site_gen.label_seq_id _struct_site_gen.pdbx_auth_ins_code _struct_site_gen.auth_comp_id _struct_site_gen.auth_asym_id _struct_site_gen.auth_seq_id _struct_site_gen.label_atom_id _struct_site_gen.label_alt_id _struct_site_gen.symmetry _struct_site_gen.details 1 AC1 4 VAL A 30 ? VAL A 30 . ? 1_555 ? 2 AC1 4 ASN A 32 ? ASN A 32 . ? 1_555 ? 3 AC1 4 PHE A 161 ? PHE A 161 . ? 1_555 ? 4 AC1 4 PRO D 73 ? PRO D 73 . ? 1_656 ? 5 AC2 4 VAL A 131 ? VAL A 131 . ? 1_555 ? 6 AC2 4 GLN A 143 ? GLN A 143 . ? 1_555 ? 7 AC2 4 ASN A 145 ? ASN A 145 . ? 1_555 ? 8 AC2 4 THR A 203 ? THR A 203 . ? 1_555 ? 9 AC3 4 VAL B 30 ? VAL B 30 . ? 1_555 ? 10 AC3 4 ASN B 32 ? ASN B 32 . ? 1_555 ? 11 AC3 4 LYS C 64 ? LYS C 64 . ? 1_454 ? 12 AC3 4 PRO C 73 ? PRO C 73 . ? 1_454 ? 13 AC4 4 VAL B 131 ? VAL B 131 . ? 1_555 ? 14 AC4 4 GLN B 143 ? GLN B 143 . ? 1_555 ? 15 AC4 4 ASN B 145 ? ASN B 145 . ? 1_555 ? 16 AC4 4 ASN B 188 ? ASN B 188 . ? 1_555 ? # _database_PDB_matrix.entry_id 4UY2 _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 4UY2 _atom_sites.fract_transf_matrix[1][1] 0.023630 _atom_sites.fract_transf_matrix[1][2] 0.000000 _atom_sites.fract_transf_matrix[1][3] 0.005464 _atom_sites.fract_transf_matrix[2][1] 0.000000 _atom_sites.fract_transf_matrix[2][2] 0.008379 _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] 0.012975 _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 . TYR A 1 5 ? -2.152 21.983 10.002 1.00 130.63 ? 5 TYR A N 1 ATOM 2 C CA . TYR A 1 5 ? -1.445 20.719 9.855 1.00 129.43 ? 5 TYR A CA 1 ATOM 3 C C . TYR A 1 5 ? -0.381 20.535 10.886 1.00 123.73 ? 5 TYR A C 1 ATOM 4 O O . TYR A 1 5 ? 0.031 21.470 11.568 1.00 123.27 ? 5 TYR A O 1 ATOM 5 C CB . TYR A 1 5 ? -0.773 20.607 8.484 1.00 134.25 ? 5 TYR A CB 1 ATOM 6 C CG . TYR A 1 5 ? -1.575 19.844 7.472 1.00 141.25 ? 5 TYR A CG 1 ATOM 7 C CD1 . TYR A 1 5 ? -2.550 20.486 6.720 1.00 147.31 ? 5 TYR A CD1 1 ATOM 8 C CD2 . TYR A 1 5 ? -1.376 18.479 7.280 1.00 138.48 ? 5 TYR A CD2 1 ATOM 9 C CE1 . TYR A 1 5 ? -3.301 19.802 5.800 1.00 147.14 ? 5 TYR A CE1 1 ATOM 10 C CE2 . TYR A 1 5 ? -2.123 17.779 6.353 1.00 142.29 ? 5 TYR A CE2 1 ATOM 11 C CZ . TYR A 1 5 ? -3.087 18.450 5.616 1.00 149.06 ? 5 TYR A CZ 1 ATOM 12 O OH . TYR A 1 5 ? -3.845 17.775 4.686 1.00 154.38 ? 5 TYR A OH 1 ATOM 13 N N . ALA A 1 6 ? 0.085 19.302 10.970 1.00 123.90 ? 6 ALA A N 1 ATOM 14 C CA . ALA A 1 6 ? 1.096 18.948 11.943 1.00 128.22 ? 6 ALA A CA 1 ATOM 15 C C . ALA A 1 6 ? 2.436 19.618 11.635 1.00 133.98 ? 6 ALA A C 1 ATOM 16 O O . ALA A 1 6 ? 3.347 19.513 12.432 1.00 134.14 ? 6 ALA A O 1 ATOM 17 C CB . ALA A 1 6 ? 1.273 17.438 12.007 1.00 124.07 ? 6 ALA A CB 1 ATOM 18 N N . GLN A 1 7 ? 2.590 20.256 10.476 1.00 136.20 ? 7 GLN A N 1 ATOM 19 C CA . GLN A 1 7 ? 3.823 21.013 10.216 1.00 141.88 ? 7 GLN A CA 1 ATOM 20 C C . GLN A 1 7 ? 3.930 22.250 11.112 1.00 137.50 ? 7 GLN A C 1 ATOM 21 O O . GLN A 1 7 ? 4.999 22.756 11.293 1.00 144.97 ? 7 GLN A O 1 ATOM 22 C CB . GLN A 1 7 ? 3.914 21.402 8.722 1.00 160.44 ? 7 GLN A CB 1 ATOM 23 C CG . GLN A 1 7 ? 4.886 22.572 8.245 1.00 176.86 ? 7 GLN A CG 1 ATOM 24 C CD . GLN A 1 7 ? 6.375 22.538 8.756 1.00 181.29 ? 7 GLN A CD 1 ATOM 25 O OE1 . GLN A 1 7 ? 6.813 23.381 9.558 1.00 177.62 ? 7 GLN A OE1 1 ATOM 26 N NE2 . GLN A 1 7 ? 7.141 21.564 8.272 1.00 175.66 ? 7 GLN A NE2 1 ATOM 27 N N . LYS A 1 8 ? 2.853 22.681 11.764 1.00 122.54 ? 8 LYS A N 1 ATOM 28 C CA . LYS A 1 8 ? 2.947 23.835 12.681 1.00 112.43 ? 8 LYS A CA 1 ATOM 29 C C . LYS A 1 8 ? 3.010 23.268 14.094 1.00 123.57 ? 8 LYS A C 1 ATOM 30 O O . LYS A 1 8 ? 3.163 23.988 15.092 1.00 132.91 ? 8 LYS A O 1 ATOM 31 C CB . LYS A 1 8 ? 1.777 24.828 12.510 1.00 101.65 ? 8 LYS A CB 1 ATOM 32 C CG . LYS A 1 8 ? 1.684 25.962 13.573 1.00 103.35 ? 8 LYS A CG 1 ATOM 33 C CD . LYS A 1 8 ? 3.046 26.656 13.769 1.00 108.70 ? 8 LYS A CD 1 ATOM 34 C CE . LYS A 1 8 ? 3.077 27.878 14.690 1.00 115.61 ? 8 LYS A CE 1 ATOM 35 N NZ . LYS A 1 8 ? 1.802 28.627 14.599 1.00 118.17 ? 8 LYS A NZ 1 ATOM 36 N N . LEU A 1 9 ? 3.016 21.945 14.159 1.00 124.72 ? 9 LEU A N 1 ATOM 37 C CA . LEU A 1 9 ? 3.473 21.291 15.360 1.00 122.22 ? 9 LEU A CA 1 ATOM 38 C C . LEU A 1 9 ? 4.957 21.124 15.193 1.00 125.69 ? 9 LEU A C 1 ATOM 39 O O . LEU A 1 9 ? 5.740 21.413 16.086 1.00 127.93 ? 9 LEU A O 1 ATOM 40 C CB . LEU A 1 9 ? 2.778 19.948 15.533 1.00 121.98 ? 9 LEU A CB 1 ATOM 41 C CG . LEU A 1 9 ? 3.520 18.910 16.348 1.00 130.63 ? 9 LEU A CG 1 ATOM 42 C CD1 . LEU A 1 9 ? 3.599 19.426 17.761 1.00 133.72 ? 9 LEU A CD1 1 ATOM 43 C CD2 . LEU A 1 9 ? 2.773 17.597 16.279 1.00 133.41 ? 9 LEU A CD2 1 ATOM 44 N N . PHE A 1 10 ? 5.325 20.660 14.011 1.00 123.08 ? 10 PHE A N 1 ATOM 45 C CA . PHE A 1 10 ? 6.694 20.594 13.579 1.00 122.14 ? 10 PHE A CA 1 ATOM 46 C C . PHE A 1 10 ? 7.168 22.041 13.307 1.00 132.51 ? 10 PHE A C 1 ATOM 47 O O . PHE A 1 10 ? 8.174 22.200 12.658 1.00 138.65 ? 10 PHE A O 1 ATOM 48 C CB . PHE A 1 10 ? 6.873 19.637 12.361 1.00 110.58 ? 10 PHE A CB 1 ATOM 49 C CG . PHE A 1 10 ? 8.297 19.595 11.799 1.00 104.14 ? 10 PHE A CG 1 ATOM 50 C CD1 . PHE A 1 10 ? 8.704 20.468 10.779 1.00 109.02 ? 10 PHE A CD1 1 ATOM 51 C CD2 . PHE A 1 10 ? 9.211 18.662 12.263 1.00 85.06 ? 10 PHE A CD2 1 ATOM 52 C CE1 . PHE A 1 10 ? 10.004 20.457 10.299 1.00 103.81 ? 10 PHE A CE1 1 ATOM 53 C CE2 . PHE A 1 10 ? 10.514 18.632 11.767 1.00 81.68 ? 10 PHE A CE2 1 ATOM 54 C CZ . PHE A 1 10 ? 10.909 19.529 10.789 1.00 90.61 ? 10 PHE A CZ 1 ATOM 55 N N . ASN A 1 11 ? 6.418 23.103 13.630 1.00 142.34 ? 11 ASN A N 1 ATOM 56 C CA . ASN A 1 11 ? 6.924 24.462 13.289 1.00 159.02 ? 11 ASN A CA 1 ATOM 57 C C . ASN A 1 11 ? 8.379 24.632 13.687 1.00 179.61 ? 11 ASN A C 1 ATOM 58 O O . ASN A 1 11 ? 9.264 24.723 12.830 1.00 176.03 ? 11 ASN A O 1 ATOM 59 C CB . ASN A 1 11 ? 6.082 25.551 13.945 1.00 152.11 ? 11 ASN A CB 1 ATOM 60 C CG . ASN A 1 11 ? 5.797 25.277 15.417 1.00 138.28 ? 11 ASN A CG 1 ATOM 61 O OD1 . ASN A 1 11 ? 5.832 24.127 15.858 1.00 124.68 ? 11 ASN A OD1 1 ATOM 62 N ND2 . ASN A 1 11 ? 5.611 26.339 16.197 1.00 139.36 ? 11 ASN A ND2 1 ATOM 63 N N . ASP A 1 12 ? 8.559 24.781 15.002 1.00 200.38 ? 12 ASP A N 1 ATOM 64 C CA . ASP A 1 12 ? 8.829 23.630 15.857 1.00 204.58 ? 12 ASP A CA 1 ATOM 65 C C . ASP A 1 12 ? 9.407 23.572 17.235 1.00 196.83 ? 12 ASP A C 1 ATOM 66 O O . ASP A 1 12 ? 9.648 24.522 17.978 1.00 201.14 ? 12 ASP A O 1 ATOM 67 C CB . ASP A 1 12 ? 9.578 22.568 15.034 1.00 216.99 ? 12 ASP A CB 1 ATOM 68 C CG . ASP A 1 12 ? 10.840 23.023 14.394 1.00 227.98 ? 12 ASP A CG 1 ATOM 69 O OD1 . ASP A 1 12 ? 11.473 23.997 14.780 1.00 231.68 ? 12 ASP A OD1 1 ATOM 70 O OD2 . ASP A 1 12 ? 11.151 22.396 13.366 1.00 231.98 ? 12 ASP A OD2 1 ATOM 71 N N . LEU A 1 13 ? 9.258 22.325 17.587 1.00 154.78 ? 13 LEU A N 1 ATOM 72 C CA . LEU A 1 13 ? 9.771 21.644 18.695 1.00 134.97 ? 13 LEU A CA 1 ATOM 73 C C . LEU A 1 13 ? 11.296 21.648 18.553 1.00 140.51 ? 13 LEU A C 1 ATOM 74 O O . LEU A 1 13 ? 12.002 21.239 19.462 1.00 149.65 ? 13 LEU A O 1 ATOM 75 C CB . LEU A 1 13 ? 9.142 20.257 18.675 1.00 112.76 ? 13 LEU A CB 1 ATOM 76 C CG . LEU A 1 13 ? 7.596 20.349 18.651 1.00 96.34 ? 13 LEU A CG 1 ATOM 77 C CD1 . LEU A 1 13 ? 6.873 18.975 18.684 1.00 66.43 ? 13 LEU A CD1 1 ATOM 78 C CD2 . LEU A 1 13 ? 7.035 21.287 19.713 1.00 94.83 ? 13 LEU A CD2 1 ATOM 79 N N . PHE A 1 14 ? 11.777 22.168 17.411 1.00 137.74 ? 14 PHE A N 1 ATOM 80 C CA . PHE A 1 14 ? 13.157 22.052 16.998 1.00 141.42 ? 14 PHE A CA 1 ATOM 81 C C . PHE A 1 14 ? 13.906 23.427 16.861 1.00 169.66 ? 14 PHE A C 1 ATOM 82 O O . PHE A 1 14 ? 15.017 23.389 16.393 1.00 169.14 ? 14 PHE A O 1 ATOM 83 C CB . PHE A 1 14 ? 13.233 21.300 15.623 1.00 107.85 ? 14 PHE A CB 1 ATOM 84 C CG . PHE A 1 14 ? 12.545 19.943 15.596 1.00 93.85 ? 14 PHE A CG 1 ATOM 85 C CD1 . PHE A 1 14 ? 13.224 18.824 15.976 1.00 100.18 ? 14 PHE A CD1 1 ATOM 86 C CD2 . PHE A 1 14 ? 11.205 19.805 15.232 1.00 83.40 ? 14 PHE A CD2 1 ATOM 87 C CE1 . PHE A 1 14 ? 12.591 17.589 15.966 1.00 93.76 ? 14 PHE A CE1 1 ATOM 88 C CE2 . PHE A 1 14 ? 10.583 18.582 15.247 1.00 85.69 ? 14 PHE A CE2 1 ATOM 89 C CZ . PHE A 1 14 ? 11.275 17.472 15.606 1.00 81.11 ? 14 PHE A CZ 1 ATOM 90 N N . GLU A 1 15 ? 13.399 24.609 17.264 1.00 165.64 ? 15 GLU A N 1 ATOM 91 C CA . GLU A 1 15 ? 14.326 25.791 17.373 1.00 179.52 ? 15 GLU A CA 1 ATOM 92 C C . GLU A 1 15 ? 15.017 25.731 18.739 1.00 188.49 ? 15 GLU A C 1 ATOM 93 O O . GLU A 1 15 ? 16.223 25.978 18.878 1.00 191.75 ? 15 GLU A O 1 ATOM 94 C CB . GLU A 1 15 ? 13.660 27.182 17.205 1.00 170.39 ? 15 GLU A CB 1 ATOM 95 C CG . GLU A 1 15 ? 12.261 27.333 17.809 1.00 178.38 ? 15 GLU A CG 1 ATOM 96 C CD . GLU A 1 15 ? 11.174 26.767 16.936 1.00 185.78 ? 15 GLU A CD 1 ATOM 97 O OE1 . GLU A 1 15 ? 11.461 25.791 16.249 1.00 186.88 ? 15 GLU A OE1 1 ATOM 98 O OE2 . GLU A 1 15 ? 10.033 27.283 16.927 1.00 187.73 ? 15 GLU A OE2 1 ATOM 99 N N . ASP A 1 16 ? 14.223 25.438 19.758 1.00 183.74 ? 16 ASP A N 1 ATOM 100 C CA . ASP A 1 16 ? 14.779 25.260 21.086 1.00 183.84 ? 16 ASP A CA 1 ATOM 101 C C . ASP A 1 16 ? 14.824 23.764 21.318 1.00 181.66 ? 16 ASP A C 1 ATOM 102 O O . ASP A 1 16 ? 14.055 23.211 22.084 1.00 180.59 ? 16 ASP A O 1 ATOM 103 C CB . ASP A 1 16 ? 13.941 25.980 22.151 1.00 185.03 ? 16 ASP A CB 1 ATOM 104 C CG . ASP A 1 16 ? 14.414 25.696 23.569 1.00 185.92 ? 16 ASP A CG 1 ATOM 105 O OD1 . ASP A 1 16 ? 15.639 25.664 23.772 1.00 184.72 ? 16 ASP A OD1 1 ATOM 106 O OD2 . ASP A 1 16 ? 13.578 25.562 24.486 1.00 184.82 ? 16 ASP A OD2 1 ATOM 107 N N . TYR A 1 17 ? 15.737 23.151 20.575 1.00 176.42 ? 17 TYR A N 1 ATOM 108 C CA . TYR A 1 17 ? 16.126 21.740 20.639 1.00 159.34 ? 17 TYR A CA 1 ATOM 109 C C . TYR A 1 17 ? 17.009 21.410 19.442 1.00 151.08 ? 17 TYR A C 1 ATOM 110 O O . TYR A 1 17 ? 16.668 21.720 18.303 1.00 151.00 ? 17 TYR A O 1 ATOM 111 C CB . TYR A 1 17 ? 14.923 20.789 20.634 1.00 149.38 ? 17 TYR A CB 1 ATOM 112 C CG . TYR A 1 17 ? 15.301 19.311 20.639 1.00 142.86 ? 17 TYR A CG 1 ATOM 113 C CD1 . TYR A 1 17 ? 16.480 18.862 21.228 1.00 144.50 ? 17 TYR A CD1 1 ATOM 114 C CD2 . TYR A 1 17 ? 14.493 18.374 20.025 1.00 139.93 ? 17 TYR A CD2 1 ATOM 115 C CE1 . TYR A 1 17 ? 16.828 17.532 21.208 1.00 145.84 ? 17 TYR A CE1 1 ATOM 116 C CE2 . TYR A 1 17 ? 14.826 17.043 20.010 1.00 141.58 ? 17 TYR A CE2 1 ATOM 117 C CZ . TYR A 1 17 ? 15.993 16.631 20.599 1.00 146.05 ? 17 TYR A CZ 1 ATOM 118 O OH . TYR A 1 17 ? 16.320 15.312 20.580 1.00 148.59 ? 17 TYR A OH 1 ATOM 119 N N . SER A 1 18 ? 18.133 20.755 19.715 1.00 143.76 ? 18 SER A N 1 ATOM 120 C CA . SER A 1 18 ? 18.892 20.021 18.712 1.00 134.62 ? 18 SER A CA 1 ATOM 121 C C . SER A 1 18 ? 19.456 18.819 19.453 1.00 120.82 ? 18 SER A C 1 ATOM 122 O O . SER A 1 18 ? 19.711 18.891 20.654 1.00 105.98 ? 18 SER A O 1 ATOM 123 C CB . SER A 1 18 ? 19.982 20.883 18.048 1.00 132.70 ? 18 SER A CB 1 ATOM 124 O OG . SER A 1 18 ? 19.488 21.548 16.882 1.00 126.02 ? 18 SER A OG 1 ATOM 125 N N . ASN A 1 19 ? 19.651 17.731 18.717 1.00 128.62 ? 19 ASN A N 1 ATOM 126 C CA . ASN A 1 19 ? 19.935 16.402 19.254 1.00 138.04 ? 19 ASN A CA 1 ATOM 127 C C . ASN A 1 19 ? 21.057 16.247 20.271 1.00 146.95 ? 19 ASN A C 1 ATOM 128 O O . ASN A 1 19 ? 21.343 15.129 20.695 1.00 156.35 ? 19 ASN A O 1 ATOM 129 C CB . ASN A 1 19 ? 20.307 15.497 18.083 1.00 141.75 ? 19 ASN A CB 1 ATOM 130 C CG . ASN A 1 19 ? 21.549 15.999 17.351 1.00 151.07 ? 19 ASN A CG 1 ATOM 131 O OD1 . ASN A 1 19 ? 21.658 17.185 17.018 1.00 156.80 ? 19 ASN A OD1 1 ATOM 132 N ND2 . ASN A 1 19 ? 22.508 15.105 17.133 1.00 152.06 ? 19 ASN A ND2 1 ATOM 133 N N . ALA A 1 20 ? 21.659 17.338 20.721 1.00 130.24 ? 20 ALA A N 1 ATOM 134 C CA . ALA A 1 20 ? 22.872 17.177 21.506 1.00 117.52 ? 20 ALA A CA 1 ATOM 135 C C . ALA A 1 20 ? 22.629 16.857 22.961 1.00 113.71 ? 20 ALA A C 1 ATOM 136 O O . ALA A 1 20 ? 23.105 15.839 23.469 1.00 113.71 ? 20 ALA A O 1 ATOM 137 C CB . ALA A 1 20 ? 23.719 18.422 21.399 1.00 114.44 ? 20 ALA A CB 1 ATOM 138 N N . LEU A 1 21 ? 21.815 17.664 23.620 1.00 103.90 ? 21 LEU A N 1 ATOM 139 C CA . LEU A 1 21 ? 21.706 17.495 25.049 1.00 102.07 ? 21 LEU A CA 1 ATOM 140 C C . LEU A 1 21 ? 20.464 16.720 25.451 1.00 96.19 ? 21 LEU A C 1 ATOM 141 O O . LEU A 1 21 ? 19.391 16.877 24.865 1.00 95.24 ? 21 LEU A O 1 ATOM 142 C CB . LEU A 1 21 ? 21.758 18.863 25.742 1.00 107.78 ? 21 LEU A CB 1 ATOM 143 C CG . LEU A 1 21 ? 20.729 19.981 25.573 1.00 106.55 ? 21 LEU A CG 1 ATOM 144 C CD1 . LEU A 1 21 ? 19.853 20.065 26.819 1.00 110.61 ? 21 LEU A CD1 1 ATOM 145 C CD2 . LEU A 1 21 ? 21.451 21.312 25.335 1.00 98.47 ? 21 LEU A CD2 1 ATOM 146 N N . ARG A 1 22 ? 20.655 15.853 26.442 1.00 100.16 ? 22 ARG A N 1 ATOM 147 C CA . ARG A 1 22 ? 19.632 14.931 26.892 1.00 102.03 ? 22 ARG A CA 1 ATOM 148 C C . ARG A 1 22 ? 18.411 15.695 27.339 1.00 111.31 ? 22 ARG A C 1 ATOM 149 O O . ARG A 1 22 ? 18.513 16.628 28.154 1.00 107.23 ? 22 ARG A O 1 ATOM 150 C CB . ARG A 1 22 ? 20.136 14.067 28.037 1.00 104.28 ? 22 ARG A CB 1 ATOM 151 C CG . ARG A 1 22 ? 21.280 13.150 27.700 1.00 108.05 ? 22 ARG A CG 1 ATOM 152 C CD . ARG A 1 22 ? 21.876 12.633 28.982 1.00 107.23 ? 22 ARG A CD 1 ATOM 153 N NE . ARG A 1 22 ? 20.821 12.174 29.881 1.00 106.93 ? 22 ARG A NE 1 ATOM 154 C CZ . ARG A 1 22 ? 20.803 12.416 31.191 1.00 105.21 ? 22 ARG A CZ 1 ATOM 155 N NH1 . ARG A 1 22 ? 21.783 13.103 31.760 1.00 108.30 ? 22 ARG A NH1 1 ATOM 156 N NH2 . ARG A 1 22 ? 19.805 11.974 31.936 1.00 95.39 ? 22 ARG A NH2 1 ATOM 157 N N . PRO A 1 23 ? 17.246 15.284 26.814 1.00 123.69 ? 23 PRO A N 1 ATOM 158 C CA . PRO A 1 23 ? 15.951 15.928 27.011 1.00 125.55 ? 23 PRO A CA 1 ATOM 159 C C . PRO A 1 23 ? 15.357 15.617 28.363 1.00 123.73 ? 23 PRO A C 1 ATOM 160 O O . PRO A 1 23 ? 14.222 15.160 28.463 1.00 128.26 ? 23 PRO A O 1 ATOM 161 C CB . PRO A 1 23 ? 15.103 15.333 25.902 1.00 124.70 ? 23 PRO A CB 1 ATOM 162 C CG . PRO A 1 23 ? 15.647 13.975 25.731 1.00 123.65 ? 23 PRO A CG 1 ATOM 163 C CD . PRO A 1 23 ? 17.132 14.117 25.921 1.00 124.93 ? 23 PRO A CD 1 ATOM 164 N N . VAL A 1 24 ? 16.140 15.843 29.403 1.00 115.28 ? 24 VAL A N 1 ATOM 165 C CA . VAL A 1 24 ? 15.587 15.821 30.730 1.00 115.90 ? 24 VAL A CA 1 ATOM 166 C C . VAL A 1 24 ? 15.573 17.269 31.194 1.00 133.54 ? 24 VAL A C 1 ATOM 167 O O . VAL A 1 24 ? 16.296 18.110 30.652 1.00 122.17 ? 24 VAL A O 1 ATOM 168 C CB . VAL A 1 24 ? 16.386 14.926 31.702 1.00 100.64 ? 24 VAL A CB 1 ATOM 169 C CG1 . VAL A 1 24 ? 16.121 13.449 31.436 1.00 88.26 ? 24 VAL A CG1 1 ATOM 170 C CG2 . VAL A 1 24 ? 17.881 15.232 31.632 1.00 102.47 ? 24 VAL A CG2 1 ATOM 171 N N . GLU A 1 25 ? 14.690 17.549 32.143 1.00 185.03 ? 25 GLU A N 1 ATOM 172 C CA . GLU A 1 25 ? 14.467 18.877 32.706 1.00 191.43 ? 25 GLU A CA 1 ATOM 173 C C . GLU A 1 25 ? 15.742 19.515 33.297 1.00 192.87 ? 25 GLU A C 1 ATOM 174 O O . GLU A 1 25 ? 15.939 20.723 33.183 1.00 206.31 ? 25 GLU A O 1 ATOM 175 C CB . GLU A 1 25 ? 13.371 18.768 33.775 1.00 196.40 ? 25 GLU A CB 1 ATOM 176 C CG . GLU A 1 25 ? 13.854 18.105 35.067 1.00 200.81 ? 25 GLU A CG 1 ATOM 177 C CD . GLU A 1 25 ? 14.476 16.729 34.843 1.00 201.11 ? 25 GLU A CD 1 ATOM 178 O OE1 . GLU A 1 25 ? 14.214 16.085 33.799 1.00 199.46 ? 25 GLU A OE1 1 ATOM 179 O OE2 . GLU A 1 25 ? 15.313 16.327 35.670 1.00 202.07 ? 25 GLU A OE2 1 ATOM 180 N N . ASP A 1 26 ? 16.605 18.701 33.912 1.00 174.22 ? 26 ASP A N 1 ATOM 181 C CA . ASP A 1 26 ? 17.949 19.127 34.322 1.00 170.52 ? 26 ASP A CA 1 ATOM 182 C C . ASP A 1 26 ? 18.851 17.903 34.409 1.00 157.28 ? 26 ASP A C 1 ATOM 183 O O . ASP A 1 26 ? 18.368 16.775 34.530 1.00 158.86 ? 26 ASP A O 1 ATOM 184 C CB . ASP A 1 26 ? 17.953 19.884 35.665 1.00 170.09 ? 26 ASP A CB 1 ATOM 185 C CG . ASP A 1 26 ? 17.455 19.041 36.858 1.00 167.26 ? 26 ASP A CG 1 ATOM 186 O OD1 . ASP A 1 26 ? 17.663 17.807 36.920 1.00 162.70 ? 26 ASP A OD1 1 ATOM 187 O OD2 . ASP A 1 26 ? 16.851 19.643 37.768 1.00 169.51 ? 26 ASP A OD2 1 ATOM 188 N N . THR A 1 27 ? 20.157 18.126 34.378 1.00 164.11 ? 27 THR A N 1 ATOM 189 C CA . THR A 1 27 ? 21.077 17.068 33.988 1.00 165.43 ? 27 THR A CA 1 ATOM 190 C C . THR A 1 27 ? 21.142 15.783 34.835 1.00 176.35 ? 27 THR A C 1 ATOM 191 O O . THR A 1 27 ? 21.068 14.696 34.274 1.00 177.10 ? 27 THR A O 1 ATOM 192 C CB . THR A 1 27 ? 22.520 17.629 33.884 1.00 177.39 ? 27 THR A CB 1 ATOM 193 O OG1 . THR A 1 27 ? 23.413 16.587 33.468 1.00 178.36 ? 27 THR A OG1 1 ATOM 194 C CG2 . THR A 1 27 ? 22.989 18.232 35.201 1.00 175.69 ? 27 THR A CG2 1 ATOM 195 N N . ASP A 1 28 ? 21.222 15.863 36.157 1.00 179.83 ? 28 ASP A N 1 ATOM 196 C CA . ASP A 1 28 ? 21.612 14.655 36.884 1.00 172.11 ? 28 ASP A CA 1 ATOM 197 C C . ASP A 1 28 ? 20.465 13.798 37.386 1.00 160.59 ? 28 ASP A C 1 ATOM 198 O O . ASP A 1 28 ? 20.612 13.041 38.351 1.00 163.69 ? 28 ASP A O 1 ATOM 199 C CB . ASP A 1 28 ? 22.534 15.023 38.045 1.00 174.02 ? 28 ASP A CB 1 ATOM 200 C CG . ASP A 1 28 ? 22.102 16.282 38.755 1.00 172.88 ? 28 ASP A CG 1 ATOM 201 O OD1 . ASP A 1 28 ? 21.449 17.149 38.127 1.00 168.82 ? 28 ASP A OD1 1 ATOM 202 O OD2 . ASP A 1 28 ? 22.448 16.415 39.946 1.00 172.88 ? 28 ASP A OD2 1 ATOM 203 N N . LYS A 1 29 ? 19.334 13.898 36.707 1.00 141.73 ? 29 LYS A N 1 ATOM 204 C CA . LYS A 1 29 ? 18.331 12.856 36.798 1.00 131.22 ? 29 LYS A CA 1 ATOM 205 C C . LYS A 1 29 ? 18.567 11.962 35.593 1.00 123.41 ? 29 LYS A C 1 ATOM 206 O O . LYS A 1 29 ? 19.462 12.231 34.806 1.00 106.93 ? 29 LYS A O 1 ATOM 207 C CB . LYS A 1 29 ? 16.923 13.440 36.885 1.00 131.03 ? 29 LYS A CB 1 ATOM 208 C CG . LYS A 1 29 ? 16.904 14.797 37.577 1.00 134.59 ? 29 LYS A CG 1 ATOM 209 C CD . LYS A 1 29 ? 15.632 15.003 38.398 1.00 133.70 ? 29 LYS A CD 1 ATOM 210 C CE . LYS A 1 29 ? 15.570 16.426 38.917 1.00 138.23 ? 29 LYS A CE 1 ATOM 211 N NZ . LYS A 1 29 ? 14.177 16.857 39.194 1.00 133.39 ? 29 LYS A NZ 1 ATOM 212 N N . VAL A 1 30 ? 17.814 10.881 35.459 1.00 126.82 ? 30 VAL A N 1 ATOM 213 C CA . VAL A 1 30 ? 18.139 9.900 34.427 1.00 124.04 ? 30 VAL A CA 1 ATOM 214 C C . VAL A 1 30 ? 17.065 9.666 33.342 1.00 126.96 ? 30 VAL A C 1 ATOM 215 O O . VAL A 1 30 ? 15.873 9.666 33.606 1.00 138.46 ? 30 VAL A O 1 ATOM 216 C CB . VAL A 1 30 ? 18.517 8.562 35.134 1.00 100.96 ? 30 VAL A CB 1 ATOM 217 C CG1 . VAL A 1 30 ? 17.625 7.388 34.722 1.00 102.34 ? 30 VAL A CG1 1 ATOM 218 C CG2 . VAL A 1 30 ? 19.991 8.273 34.936 1.00 101.35 ? 30 VAL A CG2 1 ATOM 219 N N . LEU A 1 31 ? 17.513 9.455 32.109 1.00 110.31 ? 31 LEU A N 1 ATOM 220 C CA . LEU A 1 31 ? 16.620 9.156 30.997 1.00 88.51 ? 31 LEU A CA 1 ATOM 221 C C . LEU A 1 31 ? 16.634 7.673 30.735 1.00 92.41 ? 31 LEU A C 1 ATOM 222 O O . LEU A 1 31 ? 17.585 7.153 30.175 1.00 108.27 ? 31 LEU A O 1 ATOM 223 C CB . LEU A 1 31 ? 17.033 9.910 29.718 1.00 79.99 ? 31 LEU A CB 1 ATOM 224 C CG . LEU A 1 31 ? 16.021 9.975 28.544 1.00 68.01 ? 31 LEU A CG 1 ATOM 225 C CD1 . LEU A 1 31 ? 16.394 11.072 27.578 1.00 67.06 ? 31 LEU A CD1 1 ATOM 226 C CD2 . LEU A 1 31 ? 15.791 8.655 27.775 1.00 59.53 ? 31 LEU A CD2 1 ATOM 227 N N . ASN A 1 32 ? 15.586 6.965 31.112 1.00 88.88 ? 32 ASN A N 1 ATOM 228 C CA . ASN A 1 32 ? 15.610 5.555 30.766 1.00 93.12 ? 32 ASN A CA 1 ATOM 229 C C . ASN A 1 32 ? 15.112 5.260 29.361 1.00 96.84 ? 32 ASN A C 1 ATOM 230 O O . ASN A 1 32 ? 14.508 6.094 28.685 1.00 100.98 ? 32 ASN A O 1 ATOM 231 C CB . ASN A 1 32 ? 14.798 4.692 31.740 1.00 103.15 ? 32 ASN A CB 1 ATOM 232 C CG . ASN A 1 32 ? 15.130 4.928 33.207 1.00 123.34 ? 32 ASN A CG 1 ATOM 233 O OD1 . ASN A 1 32 ? 16.282 4.860 33.637 1.00 135.26 ? 32 ASN A OD1 1 ATOM 234 N ND2 . ASN A 1 32 ? 14.107 5.201 33.976 1.00 123.96 ? 32 ASN A ND2 1 ATOM 235 N N . VAL A 1 33 ? 15.414 4.046 28.922 1.00 86.10 ? 33 VAL A N 1 ATOM 236 C CA . VAL A 1 33 ? 15.131 3.616 27.566 1.00 77.17 ? 33 VAL A CA 1 ATOM 237 C C . VAL A 1 33 ? 14.741 2.160 27.608 1.00 77.64 ? 33 VAL A C 1 ATOM 238 O O . VAL A 1 33 ? 15.351 1.337 28.298 1.00 65.55 ? 33 VAL A O 1 ATOM 239 C CB . VAL A 1 33 ? 16.329 3.824 26.595 1.00 80.24 ? 33 VAL A CB 1 ATOM 240 C CG1 . VAL A 1 33 ? 16.195 2.937 25.340 1.00 71.69 ? 33 VAL A CG1 1 ATOM 241 C CG2 . VAL A 1 33 ? 16.558 5.337 26.253 1.00 58.60 ? 33 VAL A CG2 1 ATOM 242 N N . THR A 1 34 ? 13.685 1.843 26.894 1.00 95.11 ? 34 THR A N 1 ATOM 243 C CA . THR A 1 34 ? 13.264 0.469 26.833 1.00 90.42 ? 34 THR A CA 1 ATOM 244 C C . THR A 1 34 ? 13.847 -0.093 25.555 1.00 82.93 ? 34 THR A C 1 ATOM 245 O O . THR A 1 34 ? 13.790 0.558 24.508 1.00 76.72 ? 34 THR A O 1 ATOM 246 C CB . THR A 1 34 ? 11.728 0.334 26.849 1.00 80.80 ? 34 THR A CB 1 ATOM 247 O OG1 . THR A 1 34 ? 11.181 1.226 27.837 1.00 78.37 ? 34 THR A OG1 1 ATOM 248 C CG2 . THR A 1 34 ? 11.310 -1.130 27.116 1.00 60.61 ? 34 THR A CG2 1 ATOM 249 N N . LEU A 1 35 ? 14.473 -1.253 25.649 1.00 65.38 ? 35 LEU A N 1 ATOM 250 C CA . LEU A 1 35 ? 15.009 -1.862 24.458 1.00 65.81 ? 35 LEU A CA 1 ATOM 251 C C . LEU A 1 35 ? 14.661 -3.304 24.245 1.00 69.24 ? 35 LEU A C 1 ATOM 252 O O . LEU A 1 35 ? 14.889 -4.163 25.129 1.00 61.07 ? 35 LEU A O 1 ATOM 253 C CB . LEU A 1 35 ? 16.546 -1.744 24.417 1.00 72.52 ? 35 LEU A CB 1 ATOM 254 C CG . LEU A 1 35 ? 17.091 -2.273 23.067 1.00 56.84 ? 35 LEU A CG 1 ATOM 255 C CD1 . LEU A 1 35 ? 17.971 -1.301 22.395 1.00 46.76 ? 35 LEU A CD1 1 ATOM 256 C CD2 . LEU A 1 35 ? 17.866 -3.563 23.296 1.00 49.24 ? 35 LEU A CD2 1 ATOM 257 N N . GLN A 1 36 ? 14.133 -3.574 23.051 1.00 60.32 ? 36 GLN A N 1 ATOM 258 C CA . GLN A 1 36 ? 14.071 -4.955 22.573 1.00 69.97 ? 36 GLN A CA 1 ATOM 259 C C . GLN A 1 36 ? 14.200 -5.184 21.060 1.00 69.91 ? 36 GLN A C 1 ATOM 260 O O . GLN A 1 36 ? 13.703 -4.443 20.220 1.00 53.37 ? 36 GLN A O 1 ATOM 261 C CB . GLN A 1 36 ? 12.859 -5.685 23.150 1.00 73.28 ? 36 GLN A CB 1 ATOM 262 C CG . GLN A 1 36 ? 12.635 -7.012 22.484 1.00 91.98 ? 36 GLN A CG 1 ATOM 263 C CD . GLN A 1 36 ? 11.679 -7.907 23.183 1.00 96.91 ? 36 GLN A CD 1 ATOM 264 O OE1 . GLN A 1 36 ? 11.775 -8.055 24.377 1.00 109.69 ? 36 GLN A OE1 1 ATOM 265 N NE2 . GLN A 1 36 ? 10.577 -8.239 22.501 1.00 117.38 ? 36 GLN A NE2 1 ATOM 266 N N . ILE A 1 37 ? 14.998 -6.203 20.788 1.00 73.35 ? 37 ILE A N 1 ATOM 267 C CA . ILE A 1 37 ? 15.216 -6.797 19.500 1.00 90.64 ? 37 ILE A CA 1 ATOM 268 C C . ILE A 1 37 ? 14.077 -7.732 19.044 1.00 102.97 ? 37 ILE A C 1 ATOM 269 O O . ILE A 1 37 ? 13.409 -8.375 19.848 1.00 102.32 ? 37 ILE A O 1 ATOM 270 C CB . ILE A 1 37 ? 16.544 -7.585 19.536 1.00 83.77 ? 37 ILE A CB 1 ATOM 271 C CG1 . ILE A 1 37 ? 16.350 -8.868 20.329 1.00 81.48 ? 37 ILE A CG1 1 ATOM 272 C CG2 . ILE A 1 37 ? 17.680 -6.752 20.176 1.00 70.87 ? 37 ILE A CG2 1 ATOM 273 C CD1 . ILE A 1 37 ? 17.577 -9.641 20.438 1.00 74.36 ? 37 ILE A CD1 1 ATOM 274 N N . THR A 1 38 ? 13.808 -7.759 17.746 1.00 127.22 ? 38 THR A N 1 ATOM 275 C CA . THR A 1 38 ? 12.910 -8.772 17.230 1.00 135.71 ? 38 THR A CA 1 ATOM 276 C C . THR A 1 38 ? 13.734 -9.540 16.193 1.00 135.57 ? 38 THR A C 1 ATOM 277 O O . THR A 1 38 ? 13.974 -9.060 15.087 1.00 140.54 ? 38 THR A O 1 ATOM 278 C CB . THR A 1 38 ? 11.586 -8.191 16.644 1.00 92.22 ? 38 THR A CB 1 ATOM 279 O OG1 . THR A 1 38 ? 11.776 -7.858 15.275 1.00 109.97 ? 38 THR A OG1 1 ATOM 280 C CG2 . THR A 1 38 ? 11.123 -6.945 17.413 1.00 78.23 ? 38 THR A CG2 1 ATOM 281 N N . LEU A 1 39 ? 14.205 -10.723 16.582 1.00 115.99 ? 39 LEU A N 1 ATOM 282 C CA . LEU A 1 39 ? 14.987 -11.548 15.680 1.00 90.70 ? 39 LEU A CA 1 ATOM 283 C C . LEU A 1 39 ? 14.097 -11.949 14.508 1.00 81.08 ? 39 LEU A C 1 ATOM 284 O O . LEU A 1 39 ? 12.993 -12.476 14.688 1.00 77.59 ? 39 LEU A O 1 ATOM 285 C CB . LEU A 1 39 ? 15.527 -12.789 16.400 1.00 77.48 ? 39 LEU A CB 1 ATOM 286 C CG . LEU A 1 39 ? 16.246 -13.878 15.589 1.00 81.32 ? 39 LEU A CG 1 ATOM 287 C CD1 . LEU A 1 39 ? 17.634 -13.406 15.200 1.00 77.60 ? 39 LEU A CD1 1 ATOM 288 C CD2 . LEU A 1 39 ? 16.358 -15.237 16.294 1.00 79.63 ? 39 LEU A CD2 1 ATOM 289 N N . SER A 1 40 ? 14.623 -11.723 13.309 1.00 83.49 ? 40 SER A N 1 ATOM 290 C CA . SER A 1 40 ? 13.933 -12.038 12.067 1.00 84.66 ? 40 SER A CA 1 ATOM 291 C C . SER A 1 40 ? 14.581 -13.216 11.358 1.00 100.45 ? 40 SER A C 1 ATOM 292 O O . SER A 1 40 ? 13.898 -14.131 10.914 1.00 97.79 ? 40 SER A O 1 ATOM 293 C CB . SER A 1 40 ? 13.931 -10.824 11.135 1.00 72.74 ? 40 SER A CB 1 ATOM 294 O OG . SER A 1 40 ? 13.215 -9.731 11.686 1.00 85.48 ? 40 SER A OG 1 ATOM 295 N N . GLN A 1 41 ? 15.907 -13.216 11.276 1.00 101.03 ? 41 GLN A N 1 ATOM 296 C CA . GLN A 1 41 ? 16.572 -14.292 10.574 1.00 91.66 ? 41 GLN A CA 1 ATOM 297 C C . GLN A 1 41 ? 18.010 -14.472 10.929 1.00 65.82 ? 41 GLN A C 1 ATOM 298 O O . GLN A 1 41 ? 18.766 -13.479 10.962 1.00 50.32 ? 41 GLN A O 1 ATOM 299 C CB . GLN A 1 41 ? 16.470 -14.033 9.073 1.00 116.36 ? 41 GLN A CB 1 ATOM 300 C CG . GLN A 1 41 ? 17.645 -14.528 8.164 1.00 171.50 ? 41 GLN A CG 1 ATOM 301 C CD . GLN A 1 41 ? 17.693 -16.039 7.930 1.00 168.08 ? 41 GLN A CD 1 ATOM 302 O OE1 . GLN A 1 41 ? 17.247 -16.836 8.765 1.00 170.35 ? 41 GLN A OE1 1 ATOM 303 N NE2 . GLN A 1 41 ? 18.272 -16.438 6.797 1.00 156.57 ? 41 GLN A NE2 1 ATOM 304 N N . ILE A 1 42 ? 18.374 -15.759 11.044 1.00 56.56 ? 42 ILE A N 1 ATOM 305 C CA . ILE A 1 42 ? 19.756 -16.245 11.045 1.00 75.22 ? 42 ILE A CA 1 ATOM 306 C C . ILE A 1 42 ? 20.357 -16.323 9.633 1.00 84.13 ? 42 ILE A C 1 ATOM 307 O O . ILE A 1 42 ? 20.254 -17.355 8.962 1.00 91.96 ? 42 ILE A O 1 ATOM 308 C CB . ILE A 1 42 ? 19.846 -17.647 11.654 1.00 83.98 ? 42 ILE A CB 1 ATOM 309 C CG1 . ILE A 1 42 ? 19.383 -17.618 13.100 1.00 84.99 ? 42 ILE A CG1 1 ATOM 310 C CG2 . ILE A 1 42 ? 21.279 -18.157 11.638 1.00 96.09 ? 42 ILE A CG2 1 ATOM 311 C CD1 . ILE A 1 42 ? 19.519 -18.967 13.799 1.00 88.99 ? 42 ILE A CD1 1 ATOM 312 N N . LYS A 1 43 ? 21.008 -15.240 9.204 1.00 76.83 ? 43 LYS A N 1 ATOM 313 C CA . LYS A 1 43 ? 21.489 -15.105 7.818 1.00 65.11 ? 43 LYS A CA 1 ATOM 314 C C . LYS A 1 43 ? 22.548 -16.128 7.439 1.00 66.42 ? 43 LYS A C 1 ATOM 315 O O . LYS A 1 43 ? 22.663 -16.488 6.271 1.00 55.94 ? 43 LYS A O 1 ATOM 316 C CB . LYS A 1 43 ? 22.058 -13.703 7.576 1.00 51.44 ? 43 LYS A CB 1 ATOM 317 C CG . LYS A 1 43 ? 22.726 -13.552 6.249 1.00 64.56 ? 43 LYS A CG 1 ATOM 318 C CD . LYS A 1 43 ? 21.689 -13.707 5.145 1.00 79.02 ? 43 LYS A CD 1 ATOM 319 C CE . LYS A 1 43 ? 22.323 -13.910 3.780 1.00 93.71 ? 43 LYS A CE 1 ATOM 320 N NZ . LYS A 1 43 ? 21.341 -13.612 2.707 1.00 94.06 ? 43 LYS A NZ 1 ATOM 321 N N . ASP A 1 44 ? 23.328 -16.558 8.429 1.00 73.09 ? 44 ASP A N 1 ATOM 322 C CA . ASP A 1 44 ? 24.409 -17.494 8.219 1.00 74.23 ? 44 ASP A CA 1 ATOM 323 C C . ASP A 1 44 ? 25.004 -17.813 9.579 1.00 69.33 ? 44 ASP A C 1 ATOM 324 O O . ASP A 1 44 ? 25.473 -16.913 10.294 1.00 68.49 ? 44 ASP A O 1 ATOM 325 C CB . ASP A 1 44 ? 25.476 -16.903 7.268 1.00 84.47 ? 44 ASP A CB 1 ATOM 326 C CG . ASP A 1 44 ? 26.648 -17.842 7.019 1.00 103.98 ? 44 ASP A CG 1 ATOM 327 O OD1 . ASP A 1 44 ? 26.553 -19.057 7.291 1.00 120.50 ? 44 ASP A OD1 1 ATOM 328 O OD2 . ASP A 1 44 ? 27.699 -17.343 6.580 1.00 111.00 ? 44 ASP A OD2 1 ATOM 329 N N . MET A 1 45 ? 25.024 -19.088 9.932 1.00 51.37 ? 45 MET A N 1 ATOM 330 C CA . MET A 1 45 ? 25.786 -19.455 11.079 1.00 53.83 ? 45 MET A CA 1 ATOM 331 C C . MET A 1 45 ? 27.125 -19.912 10.567 1.00 73.53 ? 45 MET A C 1 ATOM 332 O O . MET A 1 45 ? 27.317 -21.092 10.280 1.00 84.08 ? 45 MET A O 1 ATOM 333 C CB . MET A 1 45 ? 25.104 -20.546 11.913 1.00 71.15 ? 45 MET A CB 1 ATOM 334 C CG . MET A 1 45 ? 25.830 -20.830 13.269 1.00 82.92 ? 45 MET A CG 1 ATOM 335 S SD . MET A 1 45 ? 25.907 -19.297 14.232 1.00 83.45 ? 45 MET A SD 1 ATOM 336 C CE . MET A 1 45 ? 27.612 -19.270 14.731 1.00 64.00 ? 45 MET A CE 1 ATOM 337 N N . ASP A 1 46 ? 28.035 -18.954 10.420 1.00 81.09 ? 46 ASP A N 1 ATOM 338 C CA . ASP A 1 46 ? 29.423 -19.230 10.051 1.00 78.60 ? 46 ASP A CA 1 ATOM 339 C C . ASP A 1 46 ? 30.035 -20.078 11.136 1.00 72.53 ? 46 ASP A C 1 ATOM 340 O O . ASP A 1 46 ? 30.543 -19.572 12.125 1.00 65.83 ? 46 ASP A O 1 ATOM 341 C CB . ASP A 1 46 ? 30.177 -17.918 9.877 1.00 77.00 ? 46 ASP A CB 1 ATOM 342 C CG . ASP A 1 46 ? 31.486 -18.075 9.166 1.00 72.47 ? 46 ASP A CG 1 ATOM 343 O OD1 . ASP A 1 46 ? 32.105 -19.163 9.272 1.00 75.07 ? 46 ASP A OD1 1 ATOM 344 O OD2 . ASP A 1 46 ? 31.865 -17.091 8.478 1.00 59.27 ? 46 ASP A OD2 1 ATOM 345 N N . GLU A 1 47 ? 29.994 -21.382 10.939 1.00 70.91 ? 47 GLU A N 1 ATOM 346 C CA . GLU A 1 47 ? 30.461 -22.301 11.954 1.00 67.60 ? 47 GLU A CA 1 ATOM 347 C C . GLU A 1 47 ? 31.947 -22.164 12.162 1.00 90.62 ? 47 GLU A C 1 ATOM 348 O O . GLU A 1 47 ? 32.384 -22.204 13.308 1.00 98.06 ? 47 GLU A O 1 ATOM 349 C CB . GLU A 1 47 ? 30.126 -23.743 11.589 1.00 80.35 ? 47 GLU A CB 1 ATOM 350 C CG . GLU A 1 47 ? 28.706 -24.166 11.916 1.00 92.92 ? 47 GLU A CG 1 ATOM 351 C CD . GLU A 1 47 ? 28.589 -25.665 12.111 1.00 107.66 ? 47 GLU A CD 1 ATOM 352 O OE1 . GLU A 1 47 ? 28.951 -26.420 11.178 1.00 120.99 ? 47 GLU A OE1 1 ATOM 353 O OE2 . GLU A 1 47 ? 28.135 -26.095 13.190 1.00 108.47 ? 47 GLU A OE2 1 ATOM 354 N N . ARG A 1 48 ? 32.738 -22.046 11.083 1.00 94.76 ? 48 ARG A N 1 ATOM 355 C CA . ARG A 1 48 ? 34.180 -22.279 11.226 1.00 92.79 ? 48 ARG A CA 1 ATOM 356 C C . ARG A 1 48 ? 34.976 -21.018 11.598 1.00 81.12 ? 48 ARG A C 1 ATOM 357 O O . ARG A 1 48 ? 36.132 -21.110 11.975 1.00 92.72 ? 48 ARG A O 1 ATOM 358 C CB . ARG A 1 48 ? 34.752 -22.902 9.935 1.00 108.79 ? 48 ARG A CB 1 ATOM 359 C CG . ARG A 1 48 ? 35.750 -22.026 9.141 1.00 106.46 ? 48 ARG A CG 1 ATOM 360 C CD . ARG A 1 48 ? 36.727 -22.871 8.321 1.00 106.70 ? 48 ARG A CD 1 ATOM 361 N NE . ARG A 1 48 ? 37.976 -22.138 8.080 1.00 114.76 ? 48 ARG A NE 1 ATOM 362 C CZ . ARG A 1 48 ? 39.108 -22.673 7.612 1.00 108.43 ? 48 ARG A CZ 1 ATOM 363 N NH1 . ARG A 1 48 ? 39.194 -23.970 7.312 1.00 116.85 ? 48 ARG A NH1 1 ATOM 364 N NH2 . ARG A 1 48 ? 40.166 -21.895 7.464 1.00 90.69 ? 48 ARG A NH2 1 ATOM 365 N N . ASN A 1 49 ? 34.335 -19.861 11.571 1.00 67.84 ? 49 ASN A N 1 ATOM 366 C CA . ASN A 1 49 ? 34.855 -18.689 12.266 1.00 75.98 ? 49 ASN A CA 1 ATOM 367 C C . ASN A 1 49 ? 34.106 -18.343 13.554 1.00 95.72 ? 49 ASN A C 1 ATOM 368 O O . ASN A 1 49 ? 34.488 -17.410 14.257 1.00 108.23 ? 49 ASN A O 1 ATOM 369 C CB . ASN A 1 49 ? 34.843 -17.488 11.339 1.00 79.80 ? 49 ASN A CB 1 ATOM 370 C CG . ASN A 1 49 ? 35.803 -17.634 10.170 1.00 84.47 ? 49 ASN A CG 1 ATOM 371 O OD1 . ASN A 1 49 ? 36.193 -18.745 9.787 1.00 81.81 ? 49 ASN A OD1 1 ATOM 372 N ND2 . ASN A 1 49 ? 36.207 -16.494 9.609 1.00 67.59 ? 49 ASN A ND2 1 ATOM 373 N N . GLN A 1 50 ? 33.044 -19.099 13.846 1.00 97.00 ? 50 GLN A N 1 ATOM 374 C CA . GLN A 1 50 ? 32.080 -18.829 14.927 1.00 81.83 ? 50 GLN A CA 1 ATOM 375 C C . GLN A 1 50 ? 31.519 -17.418 14.912 1.00 84.13 ? 50 GLN A C 1 ATOM 376 O O . GLN A 1 50 ? 31.485 -16.732 15.931 1.00 88.66 ? 50 GLN A O 1 ATOM 377 C CB . GLN A 1 50 ? 32.689 -19.083 16.284 1.00 76.67 ? 50 GLN A CB 1 ATOM 378 C CG . GLN A 1 50 ? 32.169 -20.343 16.932 1.00 92.88 ? 50 GLN A CG 1 ATOM 379 C CD . GLN A 1 50 ? 32.605 -21.576 16.181 1.00 108.81 ? 50 GLN A CD 1 ATOM 380 O OE1 . GLN A 1 50 ? 33.629 -21.562 15.509 1.00 124.54 ? 50 GLN A OE1 1 ATOM 381 N NE2 . GLN A 1 50 ? 31.862 -22.660 16.324 1.00 117.77 ? 50 GLN A NE2 1 ATOM 382 N N . ILE A 1 51 ? 31.063 -17.000 13.747 1.00 77.20 ? 51 ILE A N 1 ATOM 383 C CA . ILE A 1 51 ? 30.440 -15.716 13.612 1.00 76.57 ? 51 ILE A CA 1 ATOM 384 C C . ILE A 1 51 ? 28.987 -15.995 13.270 1.00 87.95 ? 51 ILE A C 1 ATOM 385 O O . ILE A 1 51 ? 28.694 -16.909 12.502 1.00 98.61 ? 51 ILE A O 1 ATOM 386 C CB . ILE A 1 51 ? 31.092 -14.858 12.518 1.00 67.49 ? 51 ILE A CB 1 ATOM 387 C CG1 . ILE A 1 51 ? 32.438 -14.327 12.978 1.00 70.92 ? 51 ILE A CG1 1 ATOM 388 C CG2 . ILE A 1 51 ? 30.243 -13.652 12.258 1.00 78.44 ? 51 ILE A CG2 1 ATOM 389 C CD1 . ILE A 1 51 ? 32.332 -13.336 14.116 1.00 78.34 ? 51 ILE A CD1 1 ATOM 390 N N . LEU A 1 52 ? 28.074 -15.267 13.898 1.00 77.34 ? 52 LEU A N 1 ATOM 391 C CA . LEU A 1 52 ? 26.689 -15.349 13.516 1.00 69.22 ? 52 LEU A CA 1 ATOM 392 C C . LEU A 1 52 ? 26.324 -14.073 12.782 1.00 76.41 ? 52 LEU A C 1 ATOM 393 O O . LEU A 1 52 ? 26.554 -12.963 13.268 1.00 90.60 ? 52 LEU A O 1 ATOM 394 C CB . LEU A 1 52 ? 25.779 -15.533 14.717 1.00 66.94 ? 52 LEU A CB 1 ATOM 395 C CG . LEU A 1 52 ? 24.309 -15.266 14.370 1.00 70.16 ? 52 LEU A CG 1 ATOM 396 C CD1 . LEU A 1 52 ? 23.606 -16.574 13.966 1.00 69.96 ? 52 LEU A CD1 1 ATOM 397 C CD2 . LEU A 1 52 ? 23.570 -14.541 15.478 1.00 73.43 ? 52 LEU A CD2 1 ATOM 398 N N . THR A 1 53 ? 25.716 -14.230 11.624 1.00 67.45 ? 53 THR A N 1 ATOM 399 C CA . THR A 1 53 ? 25.194 -13.100 10.936 1.00 55.93 ? 53 THR A CA 1 ATOM 400 C C . THR A 1 53 ? 23.661 -13.136 11.086 1.00 71.77 ? 53 THR A C 1 ATOM 401 O O . THR A 1 53 ? 23.064 -14.211 10.999 1.00 84.75 ? 53 THR A O 1 ATOM 402 C CB . THR A 1 53 ? 25.576 -13.124 9.484 1.00 53.56 ? 53 THR A CB 1 ATOM 403 O OG1 . THR A 1 53 ? 27.000 -13.347 9.325 1.00 58.13 ? 53 THR A OG1 1 ATOM 404 C CG2 . THR A 1 53 ? 25.171 -11.798 8.871 1.00 52.99 ? 53 THR A CG2 1 ATOM 405 N N . ALA A 1 54 ? 23.035 -11.999 11.403 1.00 59.23 ? 54 ALA A N 1 ATOM 406 C CA . ALA A 1 54 ? 21.607 -11.987 11.687 1.00 45.88 ? 54 ALA A CA 1 ATOM 407 C C . ALA A 1 54 ? 20.952 -10.698 11.248 1.00 65.33 ? 54 ALA A C 1 ATOM 408 O O . ALA A 1 54 ? 21.544 -9.603 11.361 1.00 72.33 ? 54 ALA A O 1 ATOM 409 C CB . ALA A 1 54 ? 21.342 -12.219 13.205 1.00 70.66 ? 54 ALA A CB 1 ATOM 410 N N . TYR A 1 55 ? 19.709 -10.825 10.788 1.00 60.45 ? 55 TYR A N 1 ATOM 411 C CA . TYR A 1 55 ? 18.900 -9.672 10.447 1.00 73.72 ? 55 TYR A CA 1 ATOM 412 C C . TYR A 1 55 ? 18.018 -9.382 11.635 1.00 65.31 ? 55 TYR A C 1 ATOM 413 O O . TYR A 1 55 ? 17.443 -10.325 12.213 1.00 56.32 ? 55 TYR A O 1 ATOM 414 C CB . TYR A 1 55 ? 18.040 -9.927 9.187 1.00 98.90 ? 55 TYR A CB 1 ATOM 415 C CG . TYR A 1 55 ? 18.753 -10.112 7.841 1.00 90.07 ? 55 TYR A CG 1 ATOM 416 C CD1 . TYR A 1 55 ? 19.814 -9.296 7.456 1.00 101.00 ? 55 TYR A CD1 1 ATOM 417 C CD2 . TYR A 1 55 ? 18.351 -11.112 6.964 1.00 87.84 ? 55 TYR A CD2 1 ATOM 418 C CE1 . TYR A 1 55 ? 20.450 -9.467 6.228 1.00 108.20 ? 55 TYR A CE1 1 ATOM 419 C CE2 . TYR A 1 55 ? 18.971 -11.290 5.740 1.00 101.80 ? 55 TYR A CE2 1 ATOM 420 C CZ . TYR A 1 55 ? 20.024 -10.467 5.365 1.00 107.88 ? 55 TYR A CZ 1 ATOM 421 O OH . TYR A 1 55 ? 20.644 -10.654 4.131 1.00 102.95 ? 55 TYR A OH 1 ATOM 422 N N . LEU A 1 56 ? 17.959 -8.107 12.044 1.00 54.76 ? 56 LEU A N 1 ATOM 423 C CA . LEU A 1 56 ? 17.075 -7.738 13.150 1.00 66.02 ? 56 LEU A CA 1 ATOM 424 C C . LEU A 1 56 ? 16.393 -6.385 13.014 1.00 76.28 ? 56 LEU A C 1 ATOM 425 O O . LEU A 1 56 ? 16.877 -5.474 12.291 1.00 61.95 ? 56 LEU A O 1 ATOM 426 C CB . LEU A 1 56 ? 17.806 -7.690 14.487 1.00 54.21 ? 56 LEU A CB 1 ATOM 427 C CG . LEU A 1 56 ? 18.752 -8.741 15.015 1.00 58.19 ? 56 LEU A CG 1 ATOM 428 C CD1 . LEU A 1 56 ? 19.283 -8.183 16.328 1.00 61.30 ? 56 LEU A CD1 1 ATOM 429 C CD2 . LEU A 1 56 ? 18.112 -10.096 15.194 1.00 52.87 ? 56 LEU A CD2 1 ATOM 430 N N . TRP A 1 57 ? 15.328 -6.269 13.819 1.00 73.93 ? 57 TRP A N 1 ATOM 431 C CA . TRP A 1 57 ? 14.616 -5.029 14.125 1.00 78.95 ? 57 TRP A CA 1 ATOM 432 C C . TRP A 1 57 ? 14.842 -4.664 15.616 1.00 60.97 ? 57 TRP A C 1 ATOM 433 O O . TRP A 1 57 ? 14.738 -5.533 16.492 1.00 42.87 ? 57 TRP A O 1 ATOM 434 C CB . TRP A 1 57 ? 13.114 -5.185 13.869 1.00 65.86 ? 57 TRP A CB 1 ATOM 435 C CG . TRP A 1 57 ? 12.792 -5.266 12.485 1.00 55.34 ? 57 TRP A CG 1 ATOM 436 C CD1 . TRP A 1 57 ? 12.635 -6.399 11.752 1.00 61.46 ? 57 TRP A CD1 1 ATOM 437 C CD2 . TRP A 1 57 ? 12.602 -4.163 11.595 1.00 58.76 ? 57 TRP A CD2 1 ATOM 438 N NE1 . TRP A 1 57 ? 12.338 -6.062 10.439 1.00 83.84 ? 57 TRP A NE1 1 ATOM 439 C CE2 . TRP A 1 57 ? 12.323 -4.695 10.324 1.00 72.81 ? 57 TRP A CE2 1 ATOM 440 C CE3 . TRP A 1 57 ? 12.643 -2.774 11.755 1.00 57.78 ? 57 TRP A CE3 1 ATOM 441 C CZ2 . TRP A 1 57 ? 12.079 -3.897 9.226 1.00 72.51 ? 57 TRP A CZ2 1 ATOM 442 C CZ3 . TRP A 1 57 ? 12.402 -1.982 10.664 1.00 68.42 ? 57 TRP A CZ3 1 ATOM 443 C CH2 . TRP A 1 57 ? 12.123 -2.542 9.413 1.00 75.21 ? 57 TRP A CH2 1 ATOM 444 N N . ILE A 1 58 ? 15.117 -3.387 15.881 1.00 43.25 ? 58 ILE A N 1 ATOM 445 C CA . ILE A 1 58 ? 15.555 -2.924 17.174 1.00 78.56 ? 58 ILE A CA 1 ATOM 446 C C . ILE A 1 58 ? 14.648 -1.846 17.672 1.00 88.52 ? 58 ILE A C 1 ATOM 447 O O . ILE A 1 58 ? 14.595 -0.747 17.107 1.00 83.36 ? 58 ILE A O 1 ATOM 448 C CB . ILE A 1 58 ? 16.999 -2.406 17.151 1.00 74.37 ? 58 ILE A CB 1 ATOM 449 C CG1 . ILE A 1 58 ? 17.954 -3.590 16.934 1.00 81.39 ? 58 ILE A CG1 1 ATOM 450 C CG2 . ILE A 1 58 ? 17.313 -1.682 18.458 1.00 71.11 ? 58 ILE A CG2 1 ATOM 451 C CD1 . ILE A 1 58 ? 19.437 -3.228 16.967 1.00 82.68 ? 58 ILE A CD1 1 ATOM 452 N N . ARG A 1 59 ? 13.907 -2.210 18.717 1.00 102.24 ? 59 ARG A N 1 ATOM 453 C CA . ARG A 1 59 ? 12.983 -1.321 19.391 1.00 86.78 ? 59 ARG A CA 1 ATOM 454 C C . ARG A 1 59 ? 13.621 -0.548 20.518 1.00 70.58 ? 59 ARG A C 1 ATOM 455 O O . ARG A 1 59 ? 14.121 -1.135 21.464 1.00 70.48 ? 59 ARG A O 1 ATOM 456 C CB . ARG A 1 59 ? 11.819 -2.130 19.931 1.00 78.67 ? 59 ARG A CB 1 ATOM 457 C CG . ARG A 1 59 ? 10.536 -1.709 19.406 1.00 60.05 ? 59 ARG A CG 1 ATOM 458 C CD . ARG A 1 59 ? 9.364 -2.222 20.175 1.00 75.18 ? 59 ARG A CD 1 ATOM 459 N NE . ARG A 1 59 ? 8.188 -1.863 19.394 1.00 97.41 ? 59 ARG A NE 1 ATOM 460 C CZ . ARG A 1 59 ? 7.767 -0.615 19.283 1.00 96.87 ? 59 ARG A CZ 1 ATOM 461 N NH1 . ARG A 1 59 ? 8.418 0.330 19.945 1.00 97.27 ? 59 ARG A NH1 1 ATOM 462 N NH2 . ARG A 1 59 ? 6.723 -0.323 18.530 1.00 79.88 ? 59 ARG A NH2 1 ATOM 463 N N . GLN A 1 60 ? 13.552 0.772 20.411 1.00 50.28 ? 60 GLN A N 1 ATOM 464 C CA . GLN A 1 60 ? 14.024 1.665 21.446 1.00 63.31 ? 60 GLN A CA 1 ATOM 465 C C . GLN A 1 60 ? 13.004 2.724 21.782 1.00 78.63 ? 60 GLN A C 1 ATOM 466 O O . GLN A 1 60 ? 12.655 3.503 20.918 1.00 83.48 ? 60 GLN A O 1 ATOM 467 C CB . GLN A 1 60 ? 15.306 2.371 21.014 1.00 64.35 ? 60 GLN A CB 1 ATOM 468 C CG . GLN A 1 60 ? 16.524 1.485 20.657 1.00 65.78 ? 60 GLN A CG 1 ATOM 469 C CD . GLN A 1 60 ? 17.530 2.321 19.933 1.00 80.62 ? 60 GLN A CD 1 ATOM 470 O OE1 . GLN A 1 60 ? 17.977 3.338 20.460 1.00 81.43 ? 60 GLN A OE1 1 ATOM 471 N NE2 . GLN A 1 60 ? 17.804 1.979 18.670 1.00 95.21 ? 60 GLN A NE2 1 ATOM 472 N N . ILE A 1 61 ? 12.635 2.859 23.054 1.00 81.55 ? 61 ILE A N 1 ATOM 473 C CA . ILE A 1 61 ? 11.582 3.808 23.414 1.00 73.56 ? 61 ILE A CA 1 ATOM 474 C C . ILE A 1 61 ? 12.037 4.711 24.554 1.00 67.58 ? 61 ILE A C 1 ATOM 475 O O . ILE A 1 61 ? 12.697 4.240 25.479 1.00 59.31 ? 61 ILE A O 1 ATOM 476 C CB . ILE A 1 61 ? 10.306 3.087 23.857 1.00 68.40 ? 61 ILE A CB 1 ATOM 477 C CG1 . ILE A 1 61 ? 10.144 1.740 23.163 1.00 63.72 ? 61 ILE A CG1 1 ATOM 478 C CG2 . ILE A 1 61 ? 9.147 3.931 23.626 1.00 45.69 ? 61 ILE A CG2 1 ATOM 479 C CD1 . ILE A 1 61 ? 8.954 0.975 23.631 1.00 44.25 ? 61 ILE A CD1 1 ATOM 480 N N . TRP A 1 62 ? 11.734 6.004 24.469 1.00 60.37 ? 62 TRP A N 1 ATOM 481 C CA . TRP A 1 62 ? 12.193 6.939 25.492 1.00 58.20 ? 62 TRP A CA 1 ATOM 482 C C . TRP A 1 62 ? 11.455 8.270 25.444 1.00 84.57 ? 62 TRP A C 1 ATOM 483 O O . TRP A 1 62 ? 10.821 8.600 24.433 1.00 97.83 ? 62 TRP A O 1 ATOM 484 C CB . TRP A 1 62 ? 13.685 7.188 25.366 1.00 63.88 ? 62 TRP A CB 1 ATOM 485 C CG . TRP A 1 62 ? 14.089 8.028 24.197 1.00 61.98 ? 62 TRP A CG 1 ATOM 486 C CD1 . TRP A 1 62 ? 14.301 9.388 24.181 1.00 65.86 ? 62 TRP A CD1 1 ATOM 487 C CD2 . TRP A 1 62 ? 14.398 7.560 22.890 1.00 73.07 ? 62 TRP A CD2 1 ATOM 488 N NE1 . TRP A 1 62 ? 14.681 9.805 22.917 1.00 79.07 ? 62 TRP A NE1 1 ATOM 489 C CE2 . TRP A 1 62 ? 14.749 8.702 22.105 1.00 83.11 ? 62 TRP A CE2 1 ATOM 490 C CE3 . TRP A 1 62 ? 14.383 6.292 22.288 1.00 72.07 ? 62 TRP A CE3 1 ATOM 491 C CZ2 . TRP A 1 62 ? 15.089 8.605 20.753 1.00 80.11 ? 62 TRP A CZ2 1 ATOM 492 C CZ3 . TRP A 1 62 ? 14.726 6.196 20.953 1.00 77.45 ? 62 TRP A CZ3 1 ATOM 493 C CH2 . TRP A 1 62 ? 15.072 7.354 20.194 1.00 80.37 ? 62 TRP A CH2 1 ATOM 494 N N . HIS A 1 63 ? 11.557 9.049 26.523 1.00 94.75 ? 63 HIS A N 1 ATOM 495 C CA . HIS A 1 63 ? 10.829 10.317 26.604 1.00 98.28 ? 63 HIS A CA 1 ATOM 496 C C . HIS A 1 63 ? 11.751 11.492 26.401 1.00 88.81 ? 63 HIS A C 1 ATOM 497 O O . HIS A 1 63 ? 12.860 11.525 26.916 1.00 100.04 ? 63 HIS A O 1 ATOM 498 C CB . HIS A 1 63 ? 10.090 10.475 27.946 1.00 105.21 ? 63 HIS A CB 1 ATOM 499 C CG . HIS A 1 63 ? 8.927 9.549 28.133 1.00 100.65 ? 63 HIS A CG 1 ATOM 500 N ND1 . HIS A 1 63 ? 9.069 8.252 28.608 1.00 103.50 ? 63 HIS A ND1 1 ATOM 501 C CD2 . HIS A 1 63 ? 7.597 9.726 27.940 1.00 90.00 ? 63 HIS A CD2 1 ATOM 502 C CE1 . HIS A 1 63 ? 7.887 7.680 28.680 1.00 102.79 ? 63 HIS A CE1 1 ATOM 503 N NE2 . HIS A 1 63 ? 6.969 8.552 28.273 1.00 96.61 ? 63 HIS A NE2 1 ATOM 504 N N . ASP A 1 64 ? 11.265 12.450 25.636 1.00 91.68 ? 64 ASP A N 1 ATOM 505 C CA . ASP A 1 64 ? 11.972 13.677 25.345 1.00 88.78 ? 64 ASP A CA 1 ATOM 506 C C . ASP A 1 64 ? 11.151 14.826 25.896 1.00 99.50 ? 64 ASP A C 1 ATOM 507 O O . ASP A 1 64 ? 10.112 15.186 25.336 1.00 113.31 ? 64 ASP A O 1 ATOM 508 C CB . ASP A 1 64 ? 12.182 13.814 23.839 1.00 93.66 ? 64 ASP A CB 1 ATOM 509 C CG . ASP A 1 64 ? 13.020 15.018 23.465 1.00 102.39 ? 64 ASP A CG 1 ATOM 510 O OD1 . ASP A 1 64 ? 12.693 16.148 23.908 1.00 101.81 ? 64 ASP A OD1 1 ATOM 511 O OD2 . ASP A 1 64 ? 13.998 14.834 22.699 1.00 111.63 ? 64 ASP A OD2 1 ATOM 512 N N . ALA A 1 65 ? 11.611 15.395 27.000 1.00 98.08 ? 65 ALA A N 1 ATOM 513 C CA . ALA A 1 65 ? 10.824 16.365 27.752 1.00 101.36 ? 65 ALA A CA 1 ATOM 514 C C . ALA A 1 65 ? 10.610 17.646 26.982 1.00 101.28 ? 65 ALA A C 1 ATOM 515 O O . ALA A 1 65 ? 9.776 18.461 27.355 1.00 111.90 ? 65 ALA A O 1 ATOM 516 C CB . ALA A 1 65 ? 11.501 16.674 29.084 1.00 108.32 ? 65 ALA A CB 1 ATOM 517 N N . TYR A 1 66 ? 11.376 17.835 25.918 1.00 101.44 ? 66 TYR A N 1 ATOM 518 C CA . TYR A 1 66 ? 11.274 19.059 25.130 1.00 111.35 ? 66 TYR A CA 1 ATOM 519 C C . TYR A 1 66 ? 10.339 18.963 23.895 1.00 100.08 ? 66 TYR A C 1 ATOM 520 O O . TYR A 1 66 ? 9.959 19.984 23.300 1.00 94.96 ? 66 TYR A O 1 ATOM 521 C CB . TYR A 1 66 ? 12.682 19.495 24.731 1.00 115.67 ? 66 TYR A CB 1 ATOM 522 C CG . TYR A 1 66 ? 13.547 19.870 25.925 1.00 113.24 ? 66 TYR A CG 1 ATOM 523 C CD1 . TYR A 1 66 ? 14.108 18.884 26.738 1.00 115.64 ? 66 TYR A CD1 1 ATOM 524 C CD2 . TYR A 1 66 ? 13.791 21.202 26.247 1.00 112.33 ? 66 TYR A CD2 1 ATOM 525 C CE1 . TYR A 1 66 ? 14.903 19.208 27.827 1.00 115.95 ? 66 TYR A CE1 1 ATOM 526 C CE2 . TYR A 1 66 ? 14.587 21.539 27.335 1.00 117.74 ? 66 TYR A CE2 1 ATOM 527 C CZ . TYR A 1 66 ? 15.142 20.535 28.122 1.00 121.56 ? 66 TYR A CZ 1 ATOM 528 O OH . TYR A 1 66 ? 15.934 20.849 29.208 1.00 122.15 ? 66 TYR A OH 1 ATOM 529 N N . LEU A 1 67 ? 9.990 17.740 23.503 1.00 96.96 ? 67 LEU A N 1 ATOM 530 C CA . LEU A 1 67 ? 9.099 17.531 22.364 1.00 97.05 ? 67 LEU A CA 1 ATOM 531 C C . LEU A 1 67 ? 7.651 17.240 22.730 1.00 112.03 ? 67 LEU A C 1 ATOM 532 O O . LEU A 1 67 ? 7.036 16.340 22.151 1.00 111.64 ? 67 LEU A O 1 ATOM 533 C CB . LEU A 1 67 ? 9.628 16.387 21.513 1.00 88.14 ? 67 LEU A CB 1 ATOM 534 C CG . LEU A 1 67 ? 11.083 16.649 21.147 1.00 93.15 ? 67 LEU A CG 1 ATOM 535 C CD1 . LEU A 1 67 ? 11.630 15.501 20.335 1.00 97.31 ? 67 LEU A CD1 1 ATOM 536 C CD2 . LEU A 1 67 ? 11.208 17.969 20.402 1.00 87.67 ? 67 LEU A CD2 1 ATOM 537 N N . THR A 1 68 ? 7.115 17.995 23.685 1.00 119.03 ? 68 THR A N 1 ATOM 538 C CA . THR A 1 68 ? 5.717 17.847 24.103 1.00 119.04 ? 68 THR A CA 1 ATOM 539 C C . THR A 1 68 ? 4.821 18.947 23.566 1.00 119.55 ? 68 THR A C 1 ATOM 540 O O . THR A 1 68 ? 5.192 20.123 23.528 1.00 124.26 ? 68 THR A O 1 ATOM 541 C CB . THR A 1 68 ? 5.560 17.824 25.619 1.00 112.51 ? 68 THR A CB 1 ATOM 542 O OG1 . THR A 1 68 ? 5.996 19.079 26.154 1.00 117.68 ? 68 THR A OG1 1 ATOM 543 C CG2 . THR A 1 68 ? 6.356 16.688 26.209 1.00 105.93 ? 68 THR A CG2 1 ATOM 544 N N . TRP A 1 69 ? 3.620 18.553 23.179 1.00 118.28 ? 69 TRP A N 1 ATOM 545 C CA . TRP A 1 69 ? 2.616 19.514 22.775 1.00 121.14 ? 69 TRP A CA 1 ATOM 546 C C . TRP A 1 69 ? 1.258 19.029 23.203 1.00 121.22 ? 69 TRP A C 1 ATOM 547 O O . TRP A 1 69 ? 0.975 17.824 23.223 1.00 116.59 ? 69 TRP A O 1 ATOM 548 C CB . TRP A 1 69 ? 2.638 19.740 21.271 1.00 123.89 ? 69 TRP A CB 1 ATOM 549 C CG . TRP A 1 69 ? 1.918 18.677 20.509 1.00 124.10 ? 69 TRP A CG 1 ATOM 550 C CD1 . TRP A 1 69 ? 0.610 18.690 20.107 1.00 123.61 ? 69 TRP A CD1 1 ATOM 551 C CD2 . TRP A 1 69 ? 2.452 17.416 20.095 1.00 118.50 ? 69 TRP A CD2 1 ATOM 552 N NE1 . TRP A 1 69 ? 0.308 17.524 19.442 1.00 116.71 ? 69 TRP A NE1 1 ATOM 553 C CE2 . TRP A 1 69 ? 1.423 16.727 19.424 1.00 115.44 ? 69 TRP A CE2 1 ATOM 554 C CE3 . TRP A 1 69 ? 3.708 16.810 20.214 1.00 113.30 ? 69 TRP A CE3 1 ATOM 555 C CZ2 . TRP A 1 69 ? 1.613 15.469 18.871 1.00 110.48 ? 69 TRP A CZ2 1 ATOM 556 C CZ3 . TRP A 1 69 ? 3.893 15.561 19.669 1.00 109.20 ? 69 TRP A CZ3 1 ATOM 557 C CH2 . TRP A 1 69 ? 2.851 14.900 19.005 1.00 108.04 ? 69 TRP A CH2 1 ATOM 558 N N . ASP A 1 70 ? 0.424 19.982 23.576 1.00 119.87 ? 70 ASP A N 1 ATOM 559 C CA . ASP A 1 70 ? -0.935 19.660 23.918 1.00 120.18 ? 70 ASP A CA 1 ATOM 560 C C . ASP A 1 70 ? -1.739 19.417 22.658 1.00 123.35 ? 70 ASP A C 1 ATOM 561 O O . ASP A 1 70 ? -1.777 20.261 21.763 1.00 130.40 ? 70 ASP A O 1 ATOM 562 C CB . ASP A 1 70 ? -1.530 20.783 24.736 1.00 116.72 ? 70 ASP A CB 1 ATOM 563 C CG . ASP A 1 70 ? -2.941 20.523 25.082 1.00 113.23 ? 70 ASP A CG 1 ATOM 564 O OD1 . ASP A 1 70 ? -3.290 19.331 25.299 1.00 107.62 ? 70 ASP A OD1 1 ATOM 565 O OD2 . ASP A 1 70 ? -3.682 21.518 25.170 1.00 115.19 ? 70 ASP A OD2 1 ATOM 566 N N . ARG A 1 71 ? -2.380 18.254 22.588 1.00 123.91 ? 71 ARG A N 1 ATOM 567 C CA . ARG A 1 71 ? -2.989 17.839 21.331 1.00 124.63 ? 71 ARG A CA 1 ATOM 568 C C . ARG A 1 71 ? -4.284 18.588 20.986 1.00 133.52 ? 71 ARG A C 1 ATOM 569 O O . ARG A 1 71 ? -4.441 19.048 19.856 1.00 133.33 ? 71 ARG A O 1 ATOM 570 C CB . ARG A 1 71 ? -3.230 16.332 21.358 1.00 120.47 ? 71 ARG A CB 1 ATOM 571 C CG . ARG A 1 71 ? -3.928 15.829 22.594 1.00 121.79 ? 71 ARG A CG 1 ATOM 572 C CD . ARG A 1 71 ? -4.255 14.367 22.416 1.00 124.50 ? 71 ARG A CD 1 ATOM 573 N NE . ARG A 1 71 ? -4.928 13.796 23.577 1.00 124.79 ? 71 ARG A NE 1 ATOM 574 C CZ . ARG A 1 71 ? -5.271 12.516 23.683 1.00 125.42 ? 71 ARG A CZ 1 ATOM 575 N NH1 . ARG A 1 71 ? -4.956 11.658 22.719 1.00 117.68 ? 71 ARG A NH1 1 ATOM 576 N NH2 . ARG A 1 71 ? -5.914 12.088 24.763 1.00 130.43 ? 71 ARG A NH2 1 ATOM 577 N N . ASP A 1 72 ? -5.192 18.705 21.956 1.00 148.35 ? 72 ASP A N 1 ATOM 578 C CA . ASP A 1 72 ? -6.511 19.315 21.756 1.00 156.00 ? 72 ASP A CA 1 ATOM 579 C C . ASP A 1 72 ? -6.375 20.567 20.885 1.00 161.31 ? 72 ASP A C 1 ATOM 580 O O . ASP A 1 72 ? -7.156 20.771 19.962 1.00 169.62 ? 72 ASP A O 1 ATOM 581 C CB . ASP A 1 72 ? -7.219 19.603 23.094 1.00 161.52 ? 72 ASP A CB 1 ATOM 582 C CG . ASP A 1 72 ? -6.400 20.456 24.032 1.00 163.57 ? 72 ASP A CG 1 ATOM 583 O OD1 . ASP A 1 72 ? -5.575 21.242 23.540 1.00 166.57 ? 72 ASP A OD1 1 ATOM 584 O OD2 . ASP A 1 72 ? -6.594 20.343 25.263 1.00 159.79 ? 72 ASP A OD2 1 ATOM 585 N N . GLN A 1 73 ? -5.353 21.378 21.156 1.00 155.26 ? 73 GLN A N 1 ATOM 586 C CA . GLN A 1 73 ? -5.254 22.712 20.578 1.00 156.19 ? 73 GLN A CA 1 ATOM 587 C C . GLN A 1 73 ? -4.278 22.726 19.408 1.00 162.21 ? 73 GLN A C 1 ATOM 588 O O . GLN A 1 73 ? -3.925 23.793 18.911 1.00 161.63 ? 73 GLN A O 1 ATOM 589 C CB . GLN A 1 73 ? -4.847 23.765 21.612 1.00 156.17 ? 73 GLN A CB 1 ATOM 590 C CG . GLN A 1 73 ? -5.896 24.029 22.673 1.00 153.62 ? 73 GLN A CG 1 ATOM 591 C CD . GLN A 1 73 ? -5.521 25.177 23.577 1.00 155.69 ? 73 GLN A CD 1 ATOM 592 O OE1 . GLN A 1 73 ? -4.451 25.764 23.429 1.00 155.76 ? 73 GLN A OE1 1 ATOM 593 N NE2 . GLN A 1 73 ? -6.374 25.473 24.554 1.00 151.52 ? 73 GLN A NE2 1 ATOM 594 N N . TYR A 1 74 ? -3.829 21.546 18.982 1.00 156.71 ? 74 TYR A N 1 ATOM 595 C CA . TYR A 1 74 ? -3.260 21.407 17.635 1.00 153.90 ? 74 TYR A CA 1 ATOM 596 C C . TYR A 1 74 ? -4.176 20.511 16.793 1.00 146.31 ? 74 TYR A C 1 ATOM 597 O O . TYR A 1 74 ? -3.711 19.614 16.088 1.00 132.62 ? 74 TYR A O 1 ATOM 598 C CB . TYR A 1 74 ? -1.856 20.794 17.698 1.00 155.61 ? 74 TYR A CB 1 ATOM 599 C CG . TYR A 1 74 ? -0.746 21.766 18.035 1.00 159.92 ? 74 TYR A CG 1 ATOM 600 C CD1 . TYR A 1 74 ? -0.976 22.870 18.848 1.00 166.35 ? 74 TYR A CD1 1 ATOM 601 C CD2 . TYR A 1 74 ? 0.533 21.584 17.534 1.00 157.09 ? 74 TYR A CD2 1 ATOM 602 C CE1 . TYR A 1 74 ? 0.044 23.762 19.155 1.00 166.86 ? 74 TYR A CE1 1 ATOM 603 C CE2 . TYR A 1 74 ? 1.555 22.469 17.834 1.00 157.94 ? 74 TYR A CE2 1 ATOM 604 C CZ . TYR A 1 74 ? 1.307 23.554 18.641 1.00 160.78 ? 74 TYR A CZ 1 ATOM 605 O OH . TYR A 1 74 ? 2.325 24.431 18.932 1.00 158.46 ? 74 TYR A OH 1 ATOM 606 N N . ASP A 1 75 ? -5.466 20.835 16.802 1.00 143.69 ? 75 ASP A N 1 ATOM 607 C CA . ASP A 1 75 ? -6.514 20.041 16.151 1.00 145.85 ? 75 ASP A CA 1 ATOM 608 C C . ASP A 1 75 ? -6.448 18.539 16.521 1.00 141.89 ? 75 ASP A C 1 ATOM 609 O O . ASP A 1 75 ? -6.819 17.673 15.722 1.00 140.03 ? 75 ASP A O 1 ATOM 610 C CB . ASP A 1 75 ? -6.474 20.210 14.636 1.00 144.41 ? 75 ASP A CB 1 ATOM 611 C CG . ASP A 1 75 ? -7.845 19.994 13.996 1.00 144.46 ? 75 ASP A CG 1 ATOM 612 O OD1 . ASP A 1 75 ? -8.668 19.263 14.586 1.00 143.18 ? 75 ASP A OD1 1 ATOM 613 O OD2 . ASP A 1 75 ? -8.108 20.562 12.914 1.00 144.82 ? 75 ASP A OD2 1 ATOM 614 N N . GLY A 1 76 ? -5.981 18.254 17.739 1.00 150.92 ? 76 GLY A N 1 ATOM 615 C CA . GLY A 1 76 ? -5.956 16.913 18.314 1.00 146.49 ? 76 GLY A CA 1 ATOM 616 C C . GLY A 1 76 ? -5.075 15.846 17.694 1.00 142.71 ? 76 GLY A C 1 ATOM 617 O O . GLY A 1 76 ? -5.366 14.653 17.798 1.00 149.43 ? 76 GLY A O 1 ATOM 618 N N . LEU A 1 77 ? -3.975 16.257 17.078 1.00 139.08 ? 77 LEU A N 1 ATOM 619 C CA . LEU A 1 77 ? -3.085 15.294 16.450 1.00 123.97 ? 77 LEU A CA 1 ATOM 620 C C . LEU A 1 77 ? -2.221 14.613 17.512 1.00 113.06 ? 77 LEU A C 1 ATOM 621 O O . LEU A 1 77 ? -1.434 15.259 18.219 1.00 94.34 ? 77 LEU A O 1 ATOM 622 C CB . LEU A 1 77 ? -2.226 15.949 15.369 1.00 127.37 ? 77 LEU A CB 1 ATOM 623 C CG . LEU A 1 77 ? -2.899 15.961 13.991 1.00 133.10 ? 77 LEU A CG 1 ATOM 624 C CD1 . LEU A 1 77 ? -4.109 16.896 13.920 1.00 130.86 ? 77 LEU A CD1 1 ATOM 625 C CD2 . LEU A 1 77 ? -1.901 16.293 12.906 1.00 138.77 ? 77 LEU A CD2 1 ATOM 626 N N . ASP A 1 78 ? -2.405 13.301 17.623 1.00 111.04 ? 78 ASP A N 1 ATOM 627 C CA . ASP A 1 78 ? -1.757 12.513 18.653 1.00 109.04 ? 78 ASP A CA 1 ATOM 628 C C . ASP A 1 78 ? -0.267 12.502 18.431 1.00 121.38 ? 78 ASP A C 1 ATOM 629 O O . ASP A 1 78 ? 0.486 12.885 19.304 1.00 115.53 ? 78 ASP A O 1 ATOM 630 C CB . ASP A 1 78 ? -2.320 11.066 18.639 1.00 121.65 ? 78 ASP A CB 1 ATOM 631 C CG . ASP A 1 78 ? -1.412 10.020 19.356 1.00 132.97 ? 78 ASP A CG 1 ATOM 632 O OD1 . ASP A 1 78 ? -0.301 10.322 19.834 1.00 127.72 ? 78 ASP A OD1 1 ATOM 633 O OD2 . ASP A 1 78 ? -1.822 8.842 19.439 1.00 136.41 ? 78 ASP A OD2 1 ATOM 634 N N . SER A 1 79 ? 0.167 12.066 17.261 1.00 135.74 ? 79 SER A N 1 ATOM 635 C CA . SER A 1 79 ? 1.599 11.898 17.041 1.00 125.51 ? 79 SER A CA 1 ATOM 636 C C . SER A 1 79 ? 2.160 11.924 15.617 1.00 124.53 ? 79 SER A C 1 ATOM 637 O O . SER A 1 79 ? 1.543 11.395 14.700 1.00 137.79 ? 79 SER A O 1 ATOM 638 C CB . SER A 1 79 ? 2.000 10.574 17.641 1.00 129.34 ? 79 SER A CB 1 ATOM 639 O OG . SER A 1 79 ? 3.044 10.014 16.857 1.00 141.57 ? 79 SER A OG 1 ATOM 640 N N . ILE A 1 80 ? 3.417 12.339 15.481 1.00 97.78 ? 80 ILE A N 1 ATOM 641 C CA . ILE A 1 80 ? 4.063 12.467 14.183 1.00 74.51 ? 80 ILE A CA 1 ATOM 642 C C . ILE A 1 80 ? 5.248 11.551 14.021 1.00 78.03 ? 80 ILE A C 1 ATOM 643 O O . ILE A 1 80 ? 5.830 11.098 15.007 1.00 87.23 ? 80 ILE A O 1 ATOM 644 C CB . ILE A 1 80 ? 4.557 13.896 13.938 1.00 71.82 ? 80 ILE A CB 1 ATOM 645 C CG1 . ILE A 1 80 ? 5.583 14.296 14.974 1.00 74.77 ? 80 ILE A CG1 1 ATOM 646 C CG2 . ILE A 1 80 ? 3.424 14.880 14.019 1.00 82.73 ? 80 ILE A CG2 1 ATOM 647 C CD1 . ILE A 1 80 ? 5.925 15.774 14.881 1.00 81.28 ? 80 ILE A CD1 1 ATOM 648 N N . ARG A 1 81 ? 5.539 11.192 12.770 1.00 77.13 ? 81 ARG A N 1 ATOM 649 C CA . ARG A 1 81 ? 6.759 10.458 12.462 1.00 77.51 ? 81 ARG A CA 1 ATOM 650 C C . ARG A 1 81 ? 7.796 11.475 12.036 1.00 75.13 ? 81 ARG A C 1 ATOM 651 O O . ARG A 1 81 ? 7.456 12.393 11.305 1.00 73.93 ? 81 ARG A O 1 ATOM 652 C CB . ARG A 1 81 ? 6.543 9.382 11.400 1.00 77.39 ? 81 ARG A CB 1 ATOM 653 C CG . ARG A 1 81 ? 5.519 8.320 11.774 1.00 94.73 ? 81 ARG A CG 1 ATOM 654 C CD . ARG A 1 81 ? 5.405 7.265 10.673 1.00 116.23 ? 81 ARG A CD 1 ATOM 655 N NE . ARG A 1 81 ? 4.436 6.208 10.968 1.00 128.63 ? 81 ARG A NE 1 ATOM 656 C CZ . ARG A 1 81 ? 4.041 5.292 10.086 1.00 138.97 ? 81 ARG A CZ 1 ATOM 657 N NH1 . ARG A 1 81 ? 4.517 5.317 8.841 1.00 147.84 ? 81 ARG A NH1 1 ATOM 658 N NH2 . ARG A 1 81 ? 3.157 4.364 10.440 1.00 132.62 ? 81 ARG A NH2 1 ATOM 659 N N . ILE A 1 82 ? 9.023 11.360 12.566 1.00 78.30 ? 82 ILE A N 1 ATOM 660 C CA . ILE A 1 82 ? 10.123 12.281 12.220 1.00 86.03 ? 82 ILE A CA 1 ATOM 661 C C . ILE A 1 82 ? 11.523 11.594 12.212 1.00 99.51 ? 82 ILE A C 1 ATOM 662 O O . ILE A 1 82 ? 11.689 10.524 12.800 1.00 83.88 ? 82 ILE A O 1 ATOM 663 C CB . ILE A 1 82 ? 10.145 13.512 13.177 1.00 94.60 ? 82 ILE A CB 1 ATOM 664 C CG1 . ILE A 1 82 ? 9.941 13.093 14.623 1.00 94.68 ? 82 ILE A CG1 1 ATOM 665 C CG2 . ILE A 1 82 ? 9.089 14.546 12.768 1.00 86.82 ? 82 ILE A CG2 1 ATOM 666 C CD1 . ILE A 1 82 ? 9.935 14.270 15.566 1.00 99.51 ? 82 ILE A CD1 1 ATOM 667 N N . PRO A 1 83 ? 12.511 12.189 11.494 1.00 108.45 ? 83 PRO A N 1 ATOM 668 C CA . PRO A 1 83 ? 13.887 11.689 11.327 1.00 113.37 ? 83 PRO A CA 1 ATOM 669 C C . PRO A 1 83 ? 14.652 11.395 12.592 1.00 117.81 ? 83 PRO A C 1 ATOM 670 O O . PRO A 1 83 ? 14.854 12.270 13.437 1.00 133.91 ? 83 PRO A O 1 ATOM 671 C CB . PRO A 1 83 ? 14.568 12.831 10.569 1.00 113.80 ? 83 PRO A CB 1 ATOM 672 C CG . PRO A 1 83 ? 13.490 13.338 9.710 1.00 111.43 ? 83 PRO A CG 1 ATOM 673 C CD . PRO A 1 83 ? 12.219 13.240 10.501 1.00 111.59 ? 83 PRO A CD 1 ATOM 674 N N . SER A 1 84 ? 15.152 10.167 12.673 1.00 109.69 ? 84 SER A N 1 ATOM 675 C CA . SER A 1 84 ? 15.903 9.756 13.841 1.00 102.93 ? 84 SER A CA 1 ATOM 676 C C . SER A 1 84 ? 17.136 10.634 14.080 1.00 102.95 ? 84 SER A C 1 ATOM 677 O O . SER A 1 84 ? 17.411 11.003 15.218 1.00 108.38 ? 84 SER A O 1 ATOM 678 C CB . SER A 1 84 ? 16.280 8.273 13.715 1.00 97.55 ? 84 SER A CB 1 ATOM 679 O OG . SER A 1 84 ? 17.431 8.079 12.928 1.00 104.25 ? 84 SER A OG 1 ATOM 680 N N . ASP A 1 85 ? 17.817 11.054 13.020 1.00 101.90 ? 85 ASP A N 1 ATOM 681 C CA . ASP A 1 85 ? 19.011 11.879 13.191 1.00 98.23 ? 85 ASP A CA 1 ATOM 682 C C . ASP A 1 85 ? 18.619 13.273 13.695 1.00 103.87 ? 85 ASP A C 1 ATOM 683 O O . ASP A 1 85 ? 19.481 14.114 13.948 1.00 110.26 ? 85 ASP A O 1 ATOM 684 C CB . ASP A 1 85 ? 19.879 11.945 11.905 1.00 124.95 ? 85 ASP A CB 1 ATOM 685 C CG . ASP A 1 85 ? 19.218 12.677 10.729 1.00 129.46 ? 85 ASP A CG 1 ATOM 686 O OD1 . ASP A 1 85 ? 18.112 13.241 10.873 1.00 126.82 ? 85 ASP A OD1 1 ATOM 687 O OD2 . ASP A 1 85 ? 19.856 12.702 9.647 1.00 124.65 ? 85 ASP A OD2 1 ATOM 688 N N . LEU A 1 86 ? 17.318 13.514 13.845 1.00 92.54 ? 86 LEU A N 1 ATOM 689 C CA . LEU A 1 86 ? 16.832 14.852 14.160 1.00 95.99 ? 86 LEU A CA 1 ATOM 690 C C . LEU A 1 86 ? 16.339 14.916 15.584 1.00 99.78 ? 86 LEU A C 1 ATOM 691 O O . LEU A 1 86 ? 16.042 15.991 16.104 1.00 105.85 ? 86 LEU A O 1 ATOM 692 C CB . LEU A 1 86 ? 15.698 15.245 13.199 1.00 96.26 ? 86 LEU A CB 1 ATOM 693 C CG . LEU A 1 86 ? 15.337 16.710 12.952 1.00 100.02 ? 86 LEU A CG 1 ATOM 694 C CD1 . LEU A 1 86 ? 16.566 17.575 12.839 1.00 114.31 ? 86 LEU A CD1 1 ATOM 695 C CD2 . LEU A 1 86 ? 14.516 16.819 11.690 1.00 94.66 ? 86 LEU A CD2 1 ATOM 696 N N . VAL A 1 87 ? 16.272 13.766 16.230 1.00 87.89 ? 87 VAL A N 1 ATOM 697 C CA . VAL A 1 87 ? 15.938 13.770 17.628 1.00 90.84 ? 87 VAL A CA 1 ATOM 698 C C . VAL A 1 87 ? 17.094 13.193 18.417 1.00 87.31 ? 87 VAL A C 1 ATOM 699 O O . VAL A 1 87 ? 17.861 12.398 17.876 1.00 87.11 ? 87 VAL A O 1 ATOM 700 C CB . VAL A 1 87 ? 14.639 12.959 17.901 1.00 80.71 ? 87 VAL A CB 1 ATOM 701 C CG1 . VAL A 1 87 ? 13.448 13.713 17.390 1.00 72.56 ? 87 VAL A CG1 1 ATOM 702 C CG2 . VAL A 1 87 ? 14.704 11.564 17.265 1.00 77.48 ? 87 VAL A CG2 1 ATOM 703 N N . TRP A 1 88 ? 17.205 13.579 19.691 1.00 88.85 ? 88 TRP A N 1 ATOM 704 C CA . TRP A 1 88 ? 18.183 12.982 20.567 1.00 79.99 ? 88 TRP A CA 1 ATOM 705 C C . TRP A 1 88 ? 17.870 11.503 20.587 1.00 80.99 ? 88 TRP A C 1 ATOM 706 O O . TRP A 1 88 ? 16.701 11.104 20.681 1.00 79.04 ? 88 TRP A O 1 ATOM 707 C CB . TRP A 1 88 ? 18.134 13.569 21.991 1.00 84.78 ? 88 TRP A CB 1 ATOM 708 C CG . TRP A 1 88 ? 19.208 13.018 22.898 1.00 89.87 ? 88 TRP A CG 1 ATOM 709 C CD1 . TRP A 1 88 ? 20.490 13.474 23.030 1.00 91.56 ? 88 TRP A CD1 1 ATOM 710 C CD2 . TRP A 1 88 ? 19.097 11.870 23.744 1.00 85.74 ? 88 TRP A CD2 1 ATOM 711 N NE1 . TRP A 1 88 ? 21.169 12.696 23.928 1.00 96.70 ? 88 TRP A NE1 1 ATOM 712 C CE2 . TRP A 1 88 ? 20.338 11.704 24.380 1.00 89.51 ? 88 TRP A CE2 1 ATOM 713 C CE3 . TRP A 1 88 ? 18.060 10.975 24.036 1.00 80.46 ? 88 TRP A CE3 1 ATOM 714 C CZ2 . TRP A 1 88 ? 20.579 10.676 25.277 1.00 80.62 ? 88 TRP A CZ2 1 ATOM 715 C CZ3 . TRP A 1 88 ? 18.296 9.957 24.925 1.00 86.01 ? 88 TRP A CZ3 1 ATOM 716 C CH2 . TRP A 1 88 ? 19.551 9.814 25.538 1.00 86.73 ? 88 TRP A CH2 1 ATOM 717 N N . ARG A 1 89 ? 18.926 10.707 20.476 1.00 86.86 ? 89 ARG A N 1 ATOM 718 C CA . ARG A 1 89 ? 18.875 9.251 20.567 1.00 95.14 ? 89 ARG A CA 1 ATOM 719 C C . ARG A 1 89 ? 19.895 8.769 21.605 1.00 90.58 ? 89 ARG A C 1 ATOM 720 O O . ARG A 1 89 ? 20.964 9.379 21.798 1.00 85.17 ? 89 ARG A O 1 ATOM 721 C CB . ARG A 1 89 ? 19.167 8.558 19.219 1.00 95.68 ? 89 ARG A CB 1 ATOM 722 C CG . ARG A 1 89 ? 18.200 8.762 18.051 1.00 92.00 ? 89 ARG A CG 1 ATOM 723 C CD . ARG A 1 89 ? 19.014 9.003 16.787 1.00 85.93 ? 89 ARG A CD 1 ATOM 724 N NE . ARG A 1 89 ? 19.687 10.315 16.787 1.00 107.33 ? 89 ARG A NE 1 ATOM 725 C CZ . ARG A 1 89 ? 20.972 10.559 17.083 1.00 130.38 ? 89 ARG A CZ 1 ATOM 726 N NH1 . ARG A 1 89 ? 21.818 9.581 17.416 1.00 132.54 ? 89 ARG A NH1 1 ATOM 727 N NH2 . ARG A 1 89 ? 21.420 11.811 17.036 1.00 133.59 ? 89 ARG A NH2 1 ATOM 728 N N . PRO A 1 90 ? 19.547 7.709 22.321 1.00 100.39 ? 90 PRO A N 1 ATOM 729 C CA . PRO A 1 90 ? 20.601 7.148 23.155 1.00 108.13 ? 90 PRO A CA 1 ATOM 730 C C . PRO A 1 90 ? 21.548 6.472 22.178 1.00 104.31 ? 90 PRO A C 1 ATOM 731 O O . PRO A 1 90 ? 21.112 5.525 21.513 1.00 119.78 ? 90 PRO A O 1 ATOM 732 C CB . PRO A 1 90 ? 19.863 6.144 24.036 1.00 106.85 ? 90 PRO A CB 1 ATOM 733 C CG . PRO A 1 90 ? 18.666 5.721 23.185 1.00 98.17 ? 90 PRO A CG 1 ATOM 734 C CD . PRO A 1 90 ? 18.294 6.936 22.383 1.00 99.57 ? 90 PRO A CD 1 ATOM 735 N N . ASP A 1 91 ? 22.785 6.922 22.026 1.00 70.85 ? 91 ASP A N 1 ATOM 736 C CA . ASP A 1 91 ? 23.559 6.310 20.970 1.00 66.49 ? 91 ASP A CA 1 ATOM 737 C C . ASP A 1 91 ? 23.841 4.838 21.283 1.00 63.06 ? 91 ASP A C 1 ATOM 738 O O . ASP A 1 91 ? 24.972 4.437 21.403 1.00 88.03 ? 91 ASP A O 1 ATOM 739 C CB . ASP A 1 91 ? 24.854 7.090 20.713 1.00 73.82 ? 91 ASP A CB 1 ATOM 740 C CG . ASP A 1 91 ? 24.599 8.424 20.000 1.00 105.32 ? 91 ASP A CG 1 ATOM 741 O OD1 . ASP A 1 91 ? 24.039 8.410 18.873 1.00 117.11 ? 91 ASP A OD1 1 ATOM 742 O OD2 . ASP A 1 91 ? 24.943 9.491 20.548 1.00 112.30 ? 91 ASP A OD2 1 ATOM 743 N N . ILE A 1 92 ? 22.777 4.041 21.358 1.00 54.15 ? 92 ILE A N 1 ATOM 744 C CA . ILE A 1 92 ? 22.837 2.620 21.690 1.00 65.14 ? 92 ILE A CA 1 ATOM 745 C C . ILE A 1 92 ? 23.250 1.721 20.544 1.00 65.82 ? 92 ILE A C 1 ATOM 746 O O . ILE A 1 92 ? 22.554 1.623 19.551 1.00 79.16 ? 92 ILE A O 1 ATOM 747 C CB . ILE A 1 92 ? 21.503 2.105 22.208 1.00 71.32 ? 92 ILE A CB 1 ATOM 748 C CG1 . ILE A 1 92 ? 21.308 2.615 23.630 1.00 66.69 ? 92 ILE A CG1 1 ATOM 749 C CG2 . ILE A 1 92 ? 21.483 0.568 22.234 1.00 68.09 ? 92 ILE A CG2 1 ATOM 750 C CD1 . ILE A 1 92 ? 20.247 1.863 24.368 1.00 59.46 ? 92 ILE A CD1 1 ATOM 751 N N . VAL A 1 93 ? 24.388 1.062 20.733 1.00 56.21 ? 93 VAL A N 1 ATOM 752 C CA . VAL A 1 93 ? 25.097 0.283 19.723 1.00 53.54 ? 93 VAL A CA 1 ATOM 753 C C . VAL A 1 93 ? 25.232 -1.209 20.048 1.00 57.14 ? 93 VAL A C 1 ATOM 754 O O . VAL A 1 93 ? 24.467 -1.697 20.846 1.00 69.51 ? 93 VAL A O 1 ATOM 755 C CB . VAL A 1 93 ? 26.435 0.881 19.486 1.00 59.93 ? 93 VAL A CB 1 ATOM 756 C CG1 . VAL A 1 93 ? 26.326 2.398 19.573 1.00 49.04 ? 93 VAL A CG1 1 ATOM 757 C CG2 . VAL A 1 93 ? 27.431 0.298 20.455 1.00 69.79 ? 93 VAL A CG2 1 ATOM 758 N N . LEU A 1 94 ? 26.001 -1.972 19.266 1.00 62.48 ? 94 LEU A N 1 ATOM 759 C CA . LEU A 1 94 ? 26.274 -3.363 19.621 1.00 67.60 ? 94 LEU A CA 1 ATOM 760 C C . LEU A 1 94 ? 27.680 -3.489 20.277 1.00 96.90 ? 94 LEU A C 1 ATOM 761 O O . LEU A 1 94 ? 28.689 -3.296 19.613 1.00 106.72 ? 94 LEU A O 1 ATOM 762 C CB . LEU A 1 94 ? 26.117 -4.284 18.372 1.00 46.86 ? 94 LEU A CB 1 ATOM 763 C CG . LEU A 1 94 ? 26.015 -5.789 18.722 1.00 56.92 ? 94 LEU A CG 1 ATOM 764 C CD1 . LEU A 1 94 ? 24.623 -6.111 19.054 1.00 46.31 ? 94 LEU A CD1 1 ATOM 765 C CD2 . LEU A 1 94 ? 26.464 -6.802 17.686 1.00 46.92 ? 94 LEU A CD2 1 ATOM 766 N N . TYR A 1 95 ? 27.735 -3.816 21.571 1.00 87.28 ? 95 TYR A N 1 ATOM 767 C CA . TYR A 1 95 ? 28.998 -4.046 22.303 1.00 72.16 ? 95 TYR A CA 1 ATOM 768 C C . TYR A 1 95 ? 29.685 -5.311 21.852 1.00 76.73 ? 95 TYR A C 1 ATOM 769 O O . TYR A 1 95 ? 30.889 -5.371 21.761 1.00 87.58 ? 95 TYR A O 1 ATOM 770 C CB . TYR A 1 95 ? 28.765 -4.182 23.821 1.00 70.06 ? 95 TYR A CB 1 ATOM 771 C CG . TYR A 1 95 ? 28.734 -2.900 24.633 1.00 69.32 ? 95 TYR A CG 1 ATOM 772 C CD1 . TYR A 1 95 ? 28.498 -1.664 24.018 1.00 74.33 ? 95 TYR A CD1 1 ATOM 773 C CD2 . TYR A 1 95 ? 28.879 -2.931 26.032 1.00 54.50 ? 95 TYR A CD2 1 ATOM 774 C CE1 . TYR A 1 95 ? 28.450 -0.473 24.766 1.00 76.86 ? 95 TYR A CE1 1 ATOM 775 C CE2 . TYR A 1 95 ? 28.804 -1.738 26.814 1.00 60.30 ? 95 TYR A CE2 1 ATOM 776 C CZ . TYR A 1 95 ? 28.607 -0.507 26.161 1.00 68.23 ? 95 TYR A CZ 1 ATOM 777 O OH . TYR A 1 95 ? 28.536 0.689 26.874 1.00 62.38 ? 95 TYR A OH 1 ATOM 778 N N . ASN A 1 96 ? 28.895 -6.323 21.547 1.00 78.17 ? 96 ASN A N 1 ATOM 779 C CA . ASN A 1 96 ? 29.394 -7.649 21.193 1.00 80.50 ? 96 ASN A CA 1 ATOM 780 C C . ASN A 1 96 ? 30.013 -7.853 19.735 1.00 88.10 ? 96 ASN A C 1 ATOM 781 O O . ASN A 1 96 ? 30.585 -8.931 19.408 1.00 67.17 ? 96 ASN A O 1 ATOM 782 C CB . ASN A 1 96 ? 28.208 -8.588 21.362 1.00 58.10 ? 96 ASN A CB 1 ATOM 783 C CG . ASN A 1 96 ? 28.598 -10.014 21.253 1.00 71.49 ? 96 ASN A CG 1 ATOM 784 O OD1 . ASN A 1 96 ? 29.757 -10.385 21.492 1.00 83.08 ? 96 ASN A OD1 1 ATOM 785 N ND2 . ASN A 1 96 ? 27.649 -10.834 20.826 1.00 58.89 ? 96 ASN A ND2 1 ATOM 786 N N . LYS A 1 97 ? 29.925 -6.798 18.915 1.00 85.89 ? 97 LYS A N 1 ATOM 787 C CA . LYS A 1 97 ? 30.250 -6.767 17.473 1.00 86.30 ? 97 LYS A CA 1 ATOM 788 C C . LYS A 1 97 ? 31.483 -7.566 17.050 1.00 82.28 ? 97 LYS A C 1 ATOM 789 O O . LYS A 1 97 ? 32.249 -8.002 17.895 1.00 89.00 ? 97 LYS A O 1 ATOM 790 C CB . LYS A 1 97 ? 30.445 -5.301 17.068 1.00 82.84 ? 97 LYS A CB 1 ATOM 791 C CG . LYS A 1 97 ? 30.101 -4.944 15.677 1.00 98.80 ? 97 LYS A CG 1 ATOM 792 C CD . LYS A 1 97 ? 30.001 -3.417 15.508 1.00 113.02 ? 97 LYS A CD 1 ATOM 793 C CE . LYS A 1 97 ? 30.955 -2.668 16.438 1.00 119.66 ? 97 LYS A CE 1 ATOM 794 N NZ . LYS A 1 97 ? 30.539 -1.243 16.624 1.00 124.16 ? 97 LYS A NZ 1 ATOM 795 N N . ALA A 1 98 ? 31.657 -7.802 15.751 1.00 74.88 ? 98 ALA A N 1 ATOM 796 C CA . ALA A 1 98 ? 32.911 -8.395 15.258 1.00 71.97 ? 98 ALA A CA 1 ATOM 797 C C . ALA A 1 98 ? 33.408 -7.758 13.927 1.00 95.50 ? 98 ALA A C 1 ATOM 798 O O . ALA A 1 98 ? 34.619 -7.758 13.627 1.00 84.07 ? 98 ALA A O 1 ATOM 799 C CB . ALA A 1 98 ? 32.750 -9.925 15.114 1.00 66.31 ? 98 ALA A CB 1 ATOM 800 N N . ASP A 1 99 ? 32.463 -7.188 13.175 1.00 86.57 ? 99 ASP A N 1 ATOM 801 C CA . ASP A 1 99 ? 32.723 -6.548 11.902 1.00 85.08 ? 99 ASP A CA 1 ATOM 802 C C . ASP A 1 99 ? 31.917 -5.254 11.831 1.00 93.41 ? 99 ASP A C 1 ATOM 803 O O . ASP A 1 99 ? 32.422 -4.170 12.120 1.00 100.04 ? 99 ASP A O 1 ATOM 804 N N . PRO A 1 105 ? 21.771 0.041 10.833 1.00 96.42 ? 105 PRO A N 1 ATOM 805 C CA . PRO A 1 105 ? 22.523 0.140 9.571 1.00 104.78 ? 105 PRO A CA 1 ATOM 806 C C . PRO A 1 105 ? 21.676 0.445 8.299 1.00 128.59 ? 105 PRO A C 1 ATOM 807 O O . PRO A 1 105 ? 21.755 -0.361 7.379 1.00 120.62 ? 105 PRO A O 1 ATOM 808 C CB . PRO A 1 105 ? 23.191 -1.248 9.453 1.00 105.57 ? 105 PRO A CB 1 ATOM 809 C CG . PRO A 1 105 ? 23.137 -1.899 10.868 1.00 69.76 ? 105 PRO A CG 1 ATOM 810 C CD . PRO A 1 105 ? 22.342 -0.960 11.767 1.00 82.57 ? 105 PRO A CD 1 ATOM 811 N N . VAL A 1 106 ? 20.886 1.533 8.291 1.00 140.17 ? 106 VAL A N 1 ATOM 812 C CA . VAL A 1 106 ? 19.990 2.026 7.188 1.00 144.04 ? 106 VAL A CA 1 ATOM 813 C C . VAL A 1 106 ? 18.888 2.874 7.851 1.00 134.54 ? 106 VAL A C 1 ATOM 814 O O . VAL A 1 106 ? 18.027 2.356 8.564 1.00 131.26 ? 106 VAL A O 1 ATOM 815 C CB . VAL A 1 106 ? 19.349 0.908 6.284 1.00 106.26 ? 106 VAL A CB 1 ATOM 816 C CG1 . VAL A 1 106 ? 17.904 1.246 5.904 1.00 111.27 ? 106 VAL A CG1 1 ATOM 817 C CG2 . VAL A 1 106 ? 20.176 0.708 5.016 1.00 92.42 ? 106 VAL A CG2 1 ATOM 818 N N . ASN A 1 107 ? 18.924 4.182 7.614 1.00 125.50 ? 107 ASN A N 1 ATOM 819 C CA . ASN A 1 107 ? 18.242 5.110 8.510 1.00 109.38 ? 107 ASN A CA 1 ATOM 820 C C . ASN A 1 107 ? 16.704 5.138 8.332 1.00 105.80 ? 107 ASN A C 1 ATOM 821 O O . ASN A 1 107 ? 16.183 4.863 7.257 1.00 103.94 ? 107 ASN A O 1 ATOM 822 C CB . ASN A 1 107 ? 18.846 6.513 8.312 1.00 102.58 ? 107 ASN A CB 1 ATOM 823 C CG . ASN A 1 107 ? 18.536 7.450 9.454 1.00 93.83 ? 107 ASN A CG 1 ATOM 824 O OD1 . ASN A 1 107 ? 18.212 6.991 10.542 1.00 101.04 ? 107 ASN A OD1 1 ATOM 825 N ND2 . ASN A 1 107 ? 18.642 8.767 9.222 1.00 82.54 ? 107 ASN A ND2 1 ATOM 826 N N . THR A 1 108 ? 15.984 5.411 9.421 1.00 113.30 ? 108 THR A N 1 ATOM 827 C CA . THR A 1 108 ? 14.521 5.422 9.431 1.00 95.24 ? 108 THR A CA 1 ATOM 828 C C . THR A 1 108 ? 13.975 6.517 10.344 1.00 100.63 ? 108 THR A C 1 ATOM 829 O O . THR A 1 108 ? 14.712 7.382 10.813 1.00 100.56 ? 108 THR A O 1 ATOM 830 C CB . THR A 1 108 ? 13.908 4.120 9.909 1.00 80.22 ? 108 THR A CB 1 ATOM 831 O OG1 . THR A 1 108 ? 14.090 4.037 11.315 1.00 90.24 ? 108 THR A OG1 1 ATOM 832 C CG2 . THR A 1 108 ? 14.537 2.908 9.239 1.00 75.11 ? 108 THR A CG2 1 ATOM 833 N N . ASN A 1 109 ? 12.680 6.444 10.640 1.00 99.68 ? 109 ASN A N 1 ATOM 834 C CA . ASN A 1 109 ? 12.016 7.534 11.353 1.00 107.11 ? 109 ASN A CA 1 ATOM 835 C C . ASN A 1 109 ? 11.261 7.114 12.624 1.00 94.65 ? 109 ASN A C 1 ATOM 836 O O . ASN A 1 109 ? 10.946 5.931 12.855 1.00 84.58 ? 109 ASN A O 1 ATOM 837 C CB . ASN A 1 109 ? 11.040 8.222 10.393 1.00 130.73 ? 109 ASN A CB 1 ATOM 838 C CG . ASN A 1 109 ? 11.750 8.971 9.248 1.00 147.60 ? 109 ASN A CG 1 ATOM 839 O OD1 . ASN A 1 109 ? 12.307 10.045 9.431 1.00 150.12 ? 109 ASN A OD1 1 ATOM 840 N ND2 . ASN A 1 109 ? 11.729 8.377 8.057 1.00 147.20 ? 109 ASN A ND2 1 ATOM 841 N N . VAL A 1 110 ? 10.976 8.109 13.452 1.00 91.92 ? 110 VAL A N 1 ATOM 842 C CA . VAL A 1 110 ? 10.475 7.842 14.796 1.00 89.50 ? 110 VAL A CA 1 ATOM 843 C C . VAL A 1 110 ? 9.065 8.361 15.031 1.00 97.57 ? 110 VAL A C 1 ATOM 844 O O . VAL A 1 110 ? 8.700 9.458 14.607 1.00 106.60 ? 110 VAL A O 1 ATOM 845 C CB . VAL A 1 110 ? 11.394 8.452 15.875 1.00 89.57 ? 110 VAL A CB 1 ATOM 846 C CG1 . VAL A 1 110 ? 12.849 7.957 15.709 1.00 92.57 ? 110 VAL A CG1 1 ATOM 847 C CG2 . VAL A 1 110 ? 11.329 9.973 15.856 1.00 79.83 ? 110 VAL A CG2 1 ATOM 848 N N . VAL A 1 111 ? 8.285 7.573 15.752 1.00 90.98 ? 111 VAL A N 1 ATOM 849 C CA . VAL A 1 111 ? 6.931 7.961 16.105 1.00 89.24 ? 111 VAL A CA 1 ATOM 850 C C . VAL A 1 111 ? 6.936 8.807 17.368 1.00 96.92 ? 111 VAL A C 1 ATOM 851 O O . VAL A 1 111 ? 6.860 8.246 18.454 1.00 111.90 ? 111 VAL A O 1 ATOM 852 C CB . VAL A 1 111 ? 6.082 6.710 16.392 1.00 92.61 ? 111 VAL A CB 1 ATOM 853 C CG1 . VAL A 1 111 ? 4.645 7.085 16.672 1.00 96.28 ? 111 VAL A CG1 1 ATOM 854 C CG2 . VAL A 1 111 ? 6.205 5.698 15.276 1.00 85.21 ? 111 VAL A CG2 1 ATOM 855 N N . LEU A 1 112 ? 6.984 10.134 17.266 1.00 91.76 ? 112 LEU A N 1 ATOM 856 C CA . LEU A 1 112 ? 6.967 10.951 18.497 1.00 91.61 ? 112 LEU A CA 1 ATOM 857 C C . LEU A 1 112 ? 5.557 11.218 18.976 1.00 87.85 ? 112 LEU A C 1 ATOM 858 O O . LEU A 1 112 ? 4.802 11.780 18.231 1.00 97.27 ? 112 LEU A O 1 ATOM 859 C CB . LEU A 1 112 ? 7.669 12.291 18.274 1.00 87.67 ? 112 LEU A CB 1 ATOM 860 C CG . LEU A 1 112 ? 7.382 13.331 19.382 1.00 80.55 ? 112 LEU A CG 1 ATOM 861 C CD1 . LEU A 1 112 ? 8.032 13.011 20.763 1.00 72.54 ? 112 LEU A CD1 1 ATOM 862 C CD2 . LEU A 1 112 ? 7.635 14.780 18.936 1.00 68.57 ? 112 LEU A CD2 1 ATOM 863 N N . ARG A 1 113 ? 5.246 10.983 20.248 1.00 86.62 ? 113 ARG A N 1 ATOM 864 C CA . ARG A 1 113 ? 3.873 11.168 20.755 1.00 81.26 ? 113 ARG A CA 1 ATOM 865 C C . ARG A 1 113 ? 3.668 12.563 21.375 1.00 93.10 ? 113 ARG A C 1 ATOM 866 O O . ARG A 1 113 ? 4.628 13.321 21.516 1.00 95.99 ? 113 ARG A O 1 ATOM 867 C CB . ARG A 1 113 ? 3.545 10.061 21.765 1.00 71.06 ? 113 ARG A CB 1 ATOM 868 C CG . ARG A 1 113 ? 2.040 9.753 21.964 1.00 70.66 ? 113 ARG A CG 1 ATOM 869 C CD . ARG A 1 113 ? 1.764 8.407 22.704 1.00 83.23 ? 113 ARG A CD 1 ATOM 870 N NE . ARG A 1 113 ? 2.352 8.390 24.048 1.00 85.44 ? 113 ARG A NE 1 ATOM 871 C CZ . ARG A 1 113 ? 2.344 7.341 24.869 1.00 86.83 ? 113 ARG A CZ 1 ATOM 872 N NH1 . ARG A 1 113 ? 1.741 6.214 24.511 1.00 101.12 ? 113 ARG A NH1 1 ATOM 873 N NH2 . ARG A 1 113 ? 2.940 7.411 26.050 1.00 66.09 ? 113 ARG A NH2 1 ATOM 874 N N . TYR A 1 114 ? 2.411 12.915 21.675 1.00 104.20 ? 114 TYR A N 1 ATOM 875 C CA . TYR A 1 114 ? 2.052 14.247 22.200 1.00 103.78 ? 114 TYR A CA 1 ATOM 876 C C . TYR A 1 114 ? 2.665 14.446 23.577 1.00 100.91 ? 114 TYR A C 1 ATOM 877 O O . TYR A 1 114 ? 2.944 15.577 23.983 1.00 108.87 ? 114 TYR A O 1 ATOM 878 C CB . TYR A 1 114 ? 0.524 14.455 22.272 1.00 96.19 ? 114 TYR A CB 1 ATOM 879 C CG . TYR A 1 114 ? -0.162 13.660 23.363 1.00 96.55 ? 114 TYR A CG 1 ATOM 880 C CD1 . TYR A 1 114 ? -0.178 14.115 24.682 1.00 106.59 ? 114 TYR A CD1 1 ATOM 881 C CD2 . TYR A 1 114 ? -0.792 12.456 23.078 1.00 100.02 ? 114 TYR A CD2 1 ATOM 882 C CE1 . TYR A 1 114 ? -0.792 13.387 25.688 1.00 118.60 ? 114 TYR A CE1 1 ATOM 883 C CE2 . TYR A 1 114 ? -1.413 11.719 24.078 1.00 110.17 ? 114 TYR A CE2 1 ATOM 884 C CZ . TYR A 1 114 ? -1.416 12.188 25.385 1.00 120.21 ? 114 TYR A CZ 1 ATOM 885 O OH . TYR A 1 114 ? -2.041 11.450 26.377 1.00 122.90 ? 114 TYR A OH 1 ATOM 886 N N . ASP A 1 115 ? 2.832 13.340 24.298 1.00 88.00 ? 115 ASP A N 1 ATOM 887 C CA . ASP A 1 115 ? 3.441 13.364 25.613 1.00 94.60 ? 115 ASP A CA 1 ATOM 888 C C . ASP A 1 115 ? 4.965 13.281 25.574 1.00 102.51 ? 115 ASP A C 1 ATOM 889 O O . ASP A 1 115 ? 5.582 13.000 26.594 1.00 113.29 ? 115 ASP A O 1 ATOM 890 C CB . ASP A 1 115 ? 2.902 12.215 26.456 1.00 93.31 ? 115 ASP A CB 1 ATOM 891 C CG . ASP A 1 115 ? 3.255 10.875 25.883 1.00 89.95 ? 115 ASP A CG 1 ATOM 892 O OD1 . ASP A 1 115 ? 3.457 10.817 24.671 1.00 93.37 ? 115 ASP A OD1 1 ATOM 893 O OD2 . ASP A 1 115 ? 3.323 9.883 26.626 1.00 85.64 ? 115 ASP A OD2 1 ATOM 894 N N . GLY A 1 116 ? 5.565 13.467 24.399 1.00 90.63 ? 116 GLY A N 1 ATOM 895 C CA . GLY A 1 116 ? 7.018 13.494 24.250 1.00 77.46 ? 116 GLY A CA 1 ATOM 896 C C . GLY A 1 116 ? 7.651 12.104 24.265 1.00 74.65 ? 116 GLY A C 1 ATOM 897 O O . GLY A 1 116 ? 8.880 11.976 24.384 1.00 80.41 ? 116 GLY A O 1 ATOM 898 N N . LEU A 1 117 ? 6.816 11.067 24.109 1.00 72.83 ? 117 LEU A N 1 ATOM 899 C CA . LEU A 1 117 ? 7.271 9.674 23.950 1.00 72.21 ? 117 LEU A CA 1 ATOM 900 C C . LEU A 1 117 ? 7.665 9.328 22.521 1.00 93.87 ? 117 LEU A C 1 ATOM 901 O O . LEU A 1 117 ? 6.937 9.608 21.569 1.00 109.37 ? 117 LEU A O 1 ATOM 902 C CB . LEU A 1 117 ? 6.193 8.694 24.393 1.00 68.64 ? 117 LEU A CB 1 ATOM 903 C CG . LEU A 1 117 ? 6.592 7.269 24.019 1.00 74.05 ? 117 LEU A CG 1 ATOM 904 C CD1 . LEU A 1 117 ? 7.650 6.846 24.975 1.00 81.91 ? 117 LEU A CD1 1 ATOM 905 C CD2 . LEU A 1 117 ? 5.434 6.302 24.153 1.00 66.71 ? 117 LEU A CD2 1 ATOM 906 N N . ILE A 1 118 ? 8.825 8.703 22.387 1.00 95.27 ? 118 ILE A N 1 ATOM 907 C CA . ILE A 1 118 ? 9.394 8.377 21.092 1.00 83.02 ? 118 ILE A CA 1 ATOM 908 C C . ILE A 1 118 ? 9.587 6.888 20.893 1.00 90.68 ? 118 ILE A C 1 ATOM 909 O O . ILE A 1 118 ? 10.080 6.186 21.773 1.00 98.82 ? 118 ILE A O 1 ATOM 910 C CB . ILE A 1 118 ? 10.713 9.126 20.925 1.00 72.65 ? 118 ILE A CB 1 ATOM 911 C CG1 . ILE A 1 118 ? 10.396 10.532 20.406 1.00 67.63 ? 118 ILE A CG1 1 ATOM 912 C CG2 . ILE A 1 118 ? 11.687 8.358 20.030 1.00 72.78 ? 118 ILE A CG2 1 ATOM 913 C CD1 . ILE A 1 118 ? 11.595 11.405 20.245 1.00 69.63 ? 118 ILE A CD1 1 ATOM 914 N N . THR A 1 119 ? 9.125 6.410 19.749 1.00 92.78 ? 119 THR A N 1 ATOM 915 C CA . THR A 1 119 ? 9.262 5.016 19.362 1.00 90.72 ? 119 THR A CA 1 ATOM 916 C C . THR A 1 119 ? 9.962 4.809 18.035 1.00 79.18 ? 119 THR A C 1 ATOM 917 O O . THR A 1 119 ? 9.422 5.135 16.981 1.00 83.28 ? 119 THR A O 1 ATOM 918 C CB . THR A 1 119 ? 7.943 4.349 19.280 1.00 98.14 ? 119 THR A CB 1 ATOM 919 O OG1 . THR A 1 119 ? 7.367 4.324 20.589 1.00 98.74 ? 119 THR A OG1 1 ATOM 920 C CG2 . THR A 1 119 ? 8.149 2.954 18.782 1.00 93.19 ? 119 THR A CG2 1 ATOM 921 N N . TRP A 1 120 ? 11.171 4.267 18.144 1.00 76.57 ? 120 TRP A N 1 ATOM 922 C CA . TRP A 1 120 ? 12.125 4.020 17.071 1.00 62.64 ? 120 TRP A CA 1 ATOM 923 C C . TRP A 1 120 ? 12.361 2.509 16.874 1.00 67.56 ? 120 TRP A C 1 ATOM 924 O O . TRP A 1 120 ? 13.098 1.883 17.645 1.00 81.21 ? 120 TRP A O 1 ATOM 925 C CB . TRP A 1 120 ? 13.440 4.730 17.407 1.00 57.29 ? 120 TRP A CB 1 ATOM 926 C CG . TRP A 1 120 ? 14.408 4.830 16.307 1.00 80.57 ? 120 TRP A CG 1 ATOM 927 C CD1 . TRP A 1 120 ? 14.140 4.817 14.956 1.00 76.19 ? 120 TRP A CD1 1 ATOM 928 C CD2 . TRP A 1 120 ? 15.841 4.942 16.438 1.00 94.22 ? 120 TRP A CD2 1 ATOM 929 N NE1 . TRP A 1 120 ? 15.324 4.931 14.247 1.00 88.38 ? 120 TRP A NE1 1 ATOM 930 C CE2 . TRP A 1 120 ? 16.377 5.013 15.131 1.00 101.39 ? 120 TRP A CE2 1 ATOM 931 C CE3 . TRP A 1 120 ? 16.720 5.006 17.535 1.00 86.08 ? 120 TRP A CE3 1 ATOM 932 C CZ2 . TRP A 1 120 ? 17.760 5.140 14.899 1.00 101.11 ? 120 TRP A CZ2 1 ATOM 933 C CZ3 . TRP A 1 120 ? 18.083 5.137 17.304 1.00 78.76 ? 120 TRP A CZ3 1 ATOM 934 C CH2 . TRP A 1 120 ? 18.589 5.197 16.002 1.00 87.33 ? 120 TRP A CH2 1 ATOM 935 N N . ASP A 1 121 ? 11.727 1.902 15.880 1.00 74.36 ? 121 ASP A N 1 ATOM 936 C CA . ASP A 1 121 ? 12.178 0.588 15.422 1.00 81.11 ? 121 ASP A CA 1 ATOM 937 C C . ASP A 1 121 ? 13.132 0.826 14.252 1.00 76.21 ? 121 ASP A C 1 ATOM 938 O O . ASP A 1 121 ? 13.069 1.865 13.589 1.00 66.79 ? 121 ASP A O 1 ATOM 939 C CB . ASP A 1 121 ? 11.017 -0.304 15.016 1.00 90.51 ? 121 ASP A CB 1 ATOM 940 C CG . ASP A 1 121 ? 9.841 -0.129 15.919 1.00 103.97 ? 121 ASP A CG 1 ATOM 941 O OD1 . ASP A 1 121 ? 10.086 0.048 17.106 1.00 117.69 ? 121 ASP A OD1 1 ATOM 942 O OD2 . ASP A 1 121 ? 8.682 -0.175 15.474 1.00 102.32 ? 121 ASP A OD2 1 ATOM 943 N N . ALA A 1 122 ? 14.074 -0.086 14.061 1.00 77.69 ? 122 ALA A N 1 ATOM 944 C CA . ALA A 1 122 ? 15.111 0.129 13.062 1.00 71.62 ? 122 ALA A CA 1 ATOM 945 C C . ALA A 1 122 ? 15.816 -1.196 12.740 1.00 69.45 ? 122 ALA A C 1 ATOM 946 O O . ALA A 1 122 ? 15.796 -2.138 13.530 1.00 60.83 ? 122 ALA A O 1 ATOM 947 C CB . ALA A 1 122 ? 16.076 1.181 13.519 1.00 48.54 ? 122 ALA A CB 1 ATOM 948 N N . PRO A 1 123 ? 16.366 -1.316 11.533 1.00 67.15 ? 123 PRO A N 1 ATOM 949 C CA . PRO A 1 123 ? 16.716 -2.720 11.331 1.00 56.34 ? 123 PRO A CA 1 ATOM 950 C C . PRO A 1 123 ? 18.184 -2.862 11.434 1.00 53.81 ? 123 PRO A C 1 ATOM 951 O O . PRO A 1 123 ? 18.831 -1.841 11.174 1.00 51.08 ? 123 PRO A O 1 ATOM 952 C CB . PRO A 1 123 ? 16.170 -3.024 9.911 1.00 53.88 ? 123 PRO A CB 1 ATOM 953 C CG . PRO A 1 123 ? 16.187 -1.659 9.209 1.00 60.17 ? 123 PRO A CG 1 ATOM 954 C CD . PRO A 1 123 ? 16.331 -0.554 10.275 1.00 62.52 ? 123 PRO A CD 1 ATOM 955 N N . ALA A 1 124 ? 18.707 -4.056 11.706 1.00 52.56 ? 124 ALA A N 1 ATOM 956 C CA . ALA A 1 124 ? 20.148 -4.176 11.875 1.00 83.51 ? 124 ALA A CA 1 ATOM 957 C C . ALA A 1 124 ? 20.684 -5.436 11.202 1.00 82.21 ? 124 ALA A C 1 ATOM 958 O O . ALA A 1 124 ? 19.920 -6.421 10.983 1.00 67.76 ? 124 ALA A O 1 ATOM 959 C CB . ALA A 1 124 ? 20.541 -4.166 13.416 1.00 63.46 ? 124 ALA A CB 1 ATOM 960 N N . ILE A 1 125 ? 21.971 -5.367 10.822 1.00 71.45 ? 125 ILE A N 1 ATOM 961 C CA . ILE A 1 125 ? 22.738 -6.578 10.595 1.00 68.90 ? 125 ILE A CA 1 ATOM 962 C C . ILE A 1 125 ? 23.884 -6.639 11.551 1.00 80.92 ? 125 ILE A C 1 ATOM 963 O O . ILE A 1 125 ? 24.597 -5.653 11.723 1.00 103.83 ? 125 ILE A O 1 ATOM 964 C CB . ILE A 1 125 ? 23.292 -6.685 9.170 1.00 72.16 ? 125 ILE A CB 1 ATOM 965 C CG1 . ILE A 1 125 ? 22.193 -6.377 8.127 1.00 82.30 ? 125 ILE A CG1 1 ATOM 966 C CG2 . ILE A 1 125 ? 23.823 -8.107 8.933 1.00 58.94 ? 125 ILE A CG2 1 ATOM 967 C CD1 . ILE A 1 125 ? 22.640 -6.521 6.674 1.00 82.12 ? 125 ILE A CD1 1 ATOM 968 N N . THR A 1 126 ? 24.089 -7.815 12.140 1.00 70.45 ? 126 THR A N 1 ATOM 969 C CA . THR A 1 126 ? 25.113 -7.983 13.146 1.00 54.64 ? 126 THR A CA 1 ATOM 970 C C . THR A 1 126 ? 25.984 -9.196 12.908 1.00 70.34 ? 126 THR A C 1 ATOM 971 O O . THR A 1 126 ? 25.495 -10.316 12.687 1.00 64.94 ? 126 THR A O 1 ATOM 972 C CB . THR A 1 126 ? 24.512 -8.129 14.527 1.00 62.82 ? 126 THR A CB 1 ATOM 973 O OG1 . THR A 1 126 ? 23.801 -9.373 14.620 1.00 66.50 ? 126 THR A OG1 1 ATOM 974 C CG2 . THR A 1 126 ? 23.588 -6.988 14.825 1.00 74.93 ? 126 THR A CG2 1 ATOM 975 N N . LYS A 1 127 ? 27.287 -8.978 13.028 1.00 74.06 ? 127 LYS A N 1 ATOM 976 C CA . LYS A 1 127 ? 28.200 -10.085 13.038 1.00 78.33 ? 127 LYS A CA 1 ATOM 977 C C . LYS A 1 127 ? 28.671 -10.104 14.458 1.00 86.03 ? 127 LYS A C 1 ATOM 978 O O . LYS A 1 127 ? 29.260 -9.134 14.937 1.00 107.03 ? 127 LYS A O 1 ATOM 979 C CB . LYS A 1 127 ? 29.362 -9.936 12.034 1.00 85.66 ? 127 LYS A CB 1 ATOM 980 C CG . LYS A 1 127 ? 29.084 -9.212 10.685 1.00 96.78 ? 127 LYS A CG 1 ATOM 981 C CD . LYS A 1 127 ? 29.070 -10.223 9.508 1.00 85.53 ? 127 LYS A CD 1 ATOM 982 C CE . LYS A 1 127 ? 29.788 -9.809 8.151 1.00 105.83 ? 127 LYS A CE 1 ATOM 983 N NZ . LYS A 1 127 ? 31.035 -8.917 7.951 1.00 91.69 ? 127 LYS A NZ 1 ATOM 984 N N . SER A 1 128 ? 28.367 -11.192 15.155 1.00 58.65 ? 128 SER A N 1 ATOM 985 C CA . SER A 1 128 ? 28.660 -11.211 16.545 1.00 59.01 ? 128 SER A CA 1 ATOM 986 C C . SER A 1 128 ? 29.335 -12.554 16.745 1.00 83.23 ? 128 SER A C 1 ATOM 987 O O . SER A 1 128 ? 29.129 -13.443 15.928 1.00 90.01 ? 128 SER A O 1 ATOM 988 C CB . SER A 1 128 ? 27.379 -11.040 17.398 1.00 53.94 ? 128 SER A CB 1 ATOM 989 O OG . SER A 1 128 ? 26.598 -12.238 17.498 1.00 49.86 ? 128 SER A OG 1 ATOM 990 N N . SER A 1 129 ? 30.134 -12.711 17.804 1.00 82.75 ? 129 SER A N 1 ATOM 991 C CA . SER A 1 129 ? 30.864 -13.956 18.002 1.00 77.41 ? 129 SER A CA 1 ATOM 992 C C . SER A 1 129 ? 30.039 -14.966 18.752 1.00 72.37 ? 129 SER A C 1 ATOM 993 O O . SER A 1 129 ? 29.168 -14.594 19.509 1.00 91.60 ? 129 SER A O 1 ATOM 994 C CB . SER A 1 129 ? 32.161 -13.702 18.736 1.00 84.53 ? 129 SER A CB 1 ATOM 995 O OG . SER A 1 129 ? 32.700 -12.471 18.300 1.00 95.53 ? 129 SER A OG 1 ATOM 996 N N . CYS A 1 130 ? 30.224 -16.241 18.433 1.00 67.97 ? 130 CYS A N 1 ATOM 997 C CA . CYS A 1 130 ? 29.502 -17.314 19.102 1.00 71.69 ? 130 CYS A CA 1 ATOM 998 C C . CYS A 1 130 ? 30.470 -18.258 19.752 1.00 85.89 ? 130 CYS A C 1 ATOM 999 O O . CYS A 1 130 ? 31.645 -18.270 19.381 1.00 101.13 ? 130 CYS A O 1 ATOM 1000 C CB . CYS A 1 130 ? 28.640 -18.074 18.122 1.00 51.76 ? 130 CYS A CB 1 ATOM 1001 S SG . CYS A 1 130 ? 27.483 -16.982 17.382 1.00 96.57 ? 130 CYS A SG 1 ATOM 1002 N N . VAL A 1 131 ? 29.980 -19.071 20.693 1.00 82.11 ? 131 VAL A N 1 ATOM 1003 C CA . VAL A 1 131 ? 30.838 -20.020 21.398 1.00 72.59 ? 131 VAL A CA 1 ATOM 1004 C C . VAL A 1 131 ? 30.170 -21.382 21.480 1.00 89.80 ? 131 VAL A C 1 ATOM 1005 O O . VAL A 1 131 ? 28.943 -21.460 21.614 1.00 99.33 ? 131 VAL A O 1 ATOM 1006 C CB . VAL A 1 131 ? 31.139 -19.526 22.829 1.00 81.26 ? 131 VAL A CB 1 ATOM 1007 C CG1 . VAL A 1 131 ? 32.135 -20.442 23.547 1.00 81.20 ? 131 VAL A CG1 1 ATOM 1008 C CG2 . VAL A 1 131 ? 31.631 -18.085 22.804 1.00 85.87 ? 131 VAL A CG2 1 ATOM 1009 N N . VAL A 1 132 ? 30.957 -22.448 21.355 1.00 85.18 ? 132 VAL A N 1 ATOM 1010 C CA . VAL A 1 132 ? 30.477 -23.797 21.618 1.00 104.16 ? 132 VAL A CA 1 ATOM 1011 C C . VAL A 1 132 ? 31.022 -24.322 22.933 1.00 140.19 ? 132 VAL A C 1 ATOM 1012 O O . VAL A 1 132 ? 32.154 -24.028 23.299 1.00 143.32 ? 132 VAL A O 1 ATOM 1013 C CB . VAL A 1 132 ? 30.901 -24.787 20.511 1.00 104.86 ? 132 VAL A CB 1 ATOM 1014 C CG1 . VAL A 1 132 ? 30.150 -24.517 19.228 1.00 109.88 ? 132 VAL A CG1 1 ATOM 1015 C CG2 . VAL A 1 132 ? 32.401 -24.693 20.263 1.00 106.84 ? 132 VAL A CG2 1 ATOM 1016 N N . ASP A 1 133 ? 30.207 -25.070 23.666 1.00 174.29 ? 133 ASP A N 1 ATOM 1017 C CA . ASP A 1 133 ? 30.689 -26.031 24.674 1.00 186.10 ? 133 ASP A CA 1 ATOM 1018 C C . ASP A 1 133 ? 29.553 -27.016 24.646 1.00 197.68 ? 133 ASP A C 1 ATOM 1019 O O . ASP A 1 133 ? 28.430 -26.673 24.997 1.00 198.99 ? 133 ASP A O 1 ATOM 1020 C CB . ASP A 1 133 ? 30.901 -25.488 26.080 1.00 181.39 ? 133 ASP A CB 1 ATOM 1021 C CG . ASP A 1 133 ? 31.008 -26.622 27.110 1.00 180.32 ? 133 ASP A CG 1 ATOM 1022 O OD1 . ASP A 1 133 ? 31.130 -27.808 26.704 1.00 182.24 ? 133 ASP A OD1 1 ATOM 1023 O OD2 . ASP A 1 133 ? 30.940 -26.360 28.326 1.00 179.65 ? 133 ASP A OD2 1 ATOM 1024 N N . VAL A 1 134 ? 29.817 -28.235 24.216 1.00 203.32 ? 134 VAL A N 1 ATOM 1025 C CA . VAL A 1 134 ? 28.686 -29.107 23.996 1.00 201.02 ? 134 VAL A CA 1 ATOM 1026 C C . VAL A 1 134 ? 28.527 -30.363 24.882 1.00 181.09 ? 134 VAL A C 1 ATOM 1027 O O . VAL A 1 134 ? 29.083 -31.430 24.652 1.00 186.35 ? 134 VAL A O 1 ATOM 1028 C CB . VAL A 1 134 ? 28.680 -29.376 22.425 1.00 179.08 ? 134 VAL A CB 1 ATOM 1029 C CG1 . VAL A 1 134 ? 28.988 -30.806 21.992 1.00 178.25 ? 134 VAL A CG1 1 ATOM 1030 C CG2 . VAL A 1 134 ? 27.417 -28.806 21.792 1.00 178.10 ? 134 VAL A CG2 1 ATOM 1031 N N . THR A 1 135 ? 27.834 -30.134 25.997 1.00 170.74 ? 135 THR A N 1 ATOM 1032 C CA . THR A 1 135 ? 26.573 -30.779 26.372 1.00 162.73 ? 135 THR A CA 1 ATOM 1033 C C . THR A 1 135 ? 25.828 -29.674 27.129 1.00 162.79 ? 135 THR A C 1 ATOM 1034 O O . THR A 1 135 ? 26.465 -28.702 27.479 1.00 139.43 ? 135 THR A O 1 ATOM 1035 C CB . THR A 1 135 ? 26.686 -32.077 27.187 1.00 159.03 ? 135 THR A CB 1 ATOM 1036 O OG1 . THR A 1 135 ? 25.398 -32.707 27.219 1.00 166.39 ? 135 THR A OG1 1 ATOM 1037 C CG2 . THR A 1 135 ? 27.121 -31.847 28.591 1.00 163.55 ? 135 THR A CG2 1 ATOM 1038 N N . TYR A 1 136 ? 24.607 -29.953 27.591 1.00 178.16 ? 136 TYR A N 1 ATOM 1039 C CA . TYR A 1 136 ? 23.342 -29.236 27.334 1.00 185.04 ? 136 TYR A CA 1 ATOM 1040 C C . TYR A 1 136 ? 22.825 -29.851 26.017 1.00 185.95 ? 136 TYR A C 1 ATOM 1041 O O . TYR A 1 136 ? 22.027 -29.240 25.296 1.00 180.98 ? 136 TYR A O 1 ATOM 1042 C CB . TYR A 1 136 ? 23.415 -27.680 27.216 1.00 204.67 ? 136 TYR A CB 1 ATOM 1043 C CG . TYR A 1 136 ? 24.212 -26.855 28.243 1.00 207.50 ? 136 TYR A CG 1 ATOM 1044 C CD1 . TYR A 1 136 ? 23.611 -26.339 29.391 1.00 210.28 ? 136 TYR A CD1 1 ATOM 1045 C CD2 . TYR A 1 136 ? 25.510 -26.436 27.969 1.00 207.76 ? 136 TYR A CD2 1 ATOM 1046 C CE1 . TYR A 1 136 ? 24.351 -25.550 30.295 1.00 208.93 ? 136 TYR A CE1 1 ATOM 1047 C CE2 . TYR A 1 136 ? 26.247 -25.691 28.853 1.00 207.70 ? 136 TYR A CE2 1 ATOM 1048 C CZ . TYR A 1 136 ? 25.671 -25.231 30.000 1.00 207.92 ? 136 TYR A CZ 1 ATOM 1049 O OH . TYR A 1 136 ? 26.441 -24.455 30.833 1.00 208.59 ? 136 TYR A OH 1 ATOM 1050 N N . PHE A 1 137 ? 23.304 -31.068 25.727 1.00 187.65 ? 137 PHE A N 1 ATOM 1051 C CA . PHE A 1 137 ? 22.873 -31.847 24.569 1.00 188.00 ? 137 PHE A CA 1 ATOM 1052 C C . PHE A 1 137 ? 21.350 -31.803 24.499 1.00 193.19 ? 137 PHE A C 1 ATOM 1053 O O . PHE A 1 137 ? 20.690 -31.841 25.539 1.00 199.21 ? 137 PHE A O 1 ATOM 1054 C CB . PHE A 1 137 ? 23.350 -33.303 24.656 1.00 179.19 ? 137 PHE A CB 1 ATOM 1055 C CG . PHE A 1 137 ? 24.808 -33.511 24.352 1.00 173.23 ? 137 PHE A CG 1 ATOM 1056 C CD1 . PHE A 1 137 ? 25.513 -32.653 23.553 1.00 172.10 ? 137 PHE A CD1 1 ATOM 1057 C CD2 . PHE A 1 137 ? 25.471 -34.605 24.883 1.00 176.48 ? 137 PHE A CD2 1 ATOM 1058 C CE1 . PHE A 1 137 ? 26.846 -32.902 23.278 1.00 174.40 ? 137 PHE A CE1 1 ATOM 1059 C CE2 . PHE A 1 137 ? 26.826 -34.840 24.627 1.00 177.62 ? 137 PHE A CE2 1 ATOM 1060 C CZ . PHE A 1 137 ? 27.499 -33.976 23.826 1.00 174.16 ? 137 PHE A CZ 1 ATOM 1061 N N . PRO A 1 138 ? 20.762 -31.760 23.295 1.00 201.43 ? 138 PRO A N 1 ATOM 1062 C CA . PRO A 1 138 ? 21.093 -31.907 21.858 1.00 203.39 ? 138 PRO A CA 1 ATOM 1063 C C . PRO A 1 138 ? 22.566 -31.847 21.352 1.00 234.66 ? 138 PRO A C 1 ATOM 1064 O O . PRO A 1 138 ? 23.308 -30.937 21.718 1.00 231.51 ? 138 PRO A O 1 ATOM 1065 C CB . PRO A 1 138 ? 20.267 -30.789 21.217 1.00 203.08 ? 138 PRO A CB 1 ATOM 1066 C CG . PRO A 1 138 ? 19.757 -29.887 22.303 1.00 201.09 ? 138 PRO A CG 1 ATOM 1067 C CD . PRO A 1 138 ? 19.761 -30.703 23.547 1.00 198.19 ? 138 PRO A CD 1 ATOM 1068 N N . PHE A 1 139 ? 22.935 -32.836 20.520 1.00 236.22 ? 139 PHE A N 1 ATOM 1069 C CA . PHE A 1 139 ? 24.243 -32.992 19.832 1.00 240.43 ? 139 PHE A CA 1 ATOM 1070 C C . PHE A 1 139 ? 25.139 -31.704 19.779 1.00 231.72 ? 139 PHE A C 1 ATOM 1071 O O . PHE A 1 139 ? 26.262 -31.732 20.293 1.00 232.03 ? 139 PHE A O 1 ATOM 1072 C CB . PHE A 1 139 ? 23.930 -33.607 18.427 1.00 225.62 ? 139 PHE A CB 1 ATOM 1073 C CG . PHE A 1 139 ? 25.125 -33.921 17.557 1.00 214.46 ? 139 PHE A CG 1 ATOM 1074 C CD1 . PHE A 1 139 ? 26.039 -34.881 17.926 1.00 210.95 ? 139 PHE A CD1 1 ATOM 1075 C CD2 . PHE A 1 139 ? 25.236 -33.366 16.289 1.00 208.11 ? 139 PHE A CD2 1 ATOM 1076 C CE1 . PHE A 1 139 ? 27.098 -35.184 17.099 1.00 207.91 ? 139 PHE A CE1 1 ATOM 1077 C CE2 . PHE A 1 139 ? 26.288 -33.692 15.454 1.00 204.52 ? 139 PHE A CE2 1 ATOM 1078 C CZ . PHE A 1 139 ? 27.216 -34.594 15.858 1.00 204.13 ? 139 PHE A CZ 1 ATOM 1079 N N . ASP A 1 140 ? 24.624 -30.581 19.252 1.00 219.66 ? 140 ASP A N 1 ATOM 1080 C CA . ASP A 1 140 ? 25.393 -29.315 19.088 1.00 187.98 ? 140 ASP A CA 1 ATOM 1081 C C . ASP A 1 140 ? 24.737 -28.006 19.511 1.00 187.21 ? 140 ASP A C 1 ATOM 1082 O O . ASP A 1 140 ? 24.029 -27.409 18.686 1.00 185.87 ? 140 ASP A O 1 ATOM 1083 C CB . ASP A 1 140 ? 25.744 -29.007 17.617 1.00 173.38 ? 140 ASP A CB 1 ATOM 1084 C CG . ASP A 1 140 ? 26.235 -30.179 16.836 1.00 165.39 ? 140 ASP A CG 1 ATOM 1085 O OD1 . ASP A 1 140 ? 26.945 -31.043 17.382 1.00 169.33 ? 140 ASP A OD1 1 ATOM 1086 O OD2 . ASP A 1 140 ? 25.845 -30.245 15.652 1.00 159.93 ? 140 ASP A OD2 1 ATOM 1087 N N . ASN A 1 141 ? 25.016 -27.474 20.699 1.00 182.14 ? 141 ASN A N 1 ATOM 1088 C CA . ASN A 1 141 ? 24.466 -26.151 20.928 1.00 175.69 ? 141 ASN A CA 1 ATOM 1089 C C . ASN A 1 141 ? 25.571 -25.125 20.706 1.00 159.89 ? 141 ASN A C 1 ATOM 1090 O O . ASN A 1 141 ? 26.755 -25.355 20.958 1.00 167.31 ? 141 ASN A O 1 ATOM 1091 C CB . ASN A 1 141 ? 23.834 -25.944 22.332 1.00 166.87 ? 141 ASN A CB 1 ATOM 1092 C CG . ASN A 1 141 ? 24.650 -26.537 23.477 1.00 168.44 ? 141 ASN A CG 1 ATOM 1093 O OD1 . ASN A 1 141 ? 24.747 -27.752 23.619 1.00 167.91 ? 141 ASN A OD1 1 ATOM 1094 N ND2 . ASN A 1 141 ? 25.203 -25.670 24.326 1.00 166.73 ? 141 ASN A ND2 1 ATOM 1095 N N . GLN A 1 142 ? 25.131 -23.973 20.231 1.00 126.23 ? 142 GLN A N 1 ATOM 1096 C CA . GLN A 1 142 ? 25.983 -22.839 19.943 1.00 105.34 ? 142 GLN A CA 1 ATOM 1097 C C . GLN A 1 142 ? 25.384 -21.650 20.640 1.00 95.59 ? 142 GLN A C 1 ATOM 1098 O O . GLN A 1 142 ? 24.168 -21.455 20.638 1.00 93.99 ? 142 GLN A O 1 ATOM 1099 C CB . GLN A 1 142 ? 26.124 -22.568 18.453 1.00 112.13 ? 142 GLN A CB 1 ATOM 1100 C CG . GLN A 1 142 ? 27.397 -23.124 17.873 1.00 117.64 ? 142 GLN A CG 1 ATOM 1101 C CD . GLN A 1 142 ? 27.800 -22.390 16.643 1.00 117.71 ? 142 GLN A CD 1 ATOM 1102 O OE1 . GLN A 1 142 ? 26.995 -21.678 16.048 1.00 117.77 ? 142 GLN A OE1 1 ATOM 1103 N NE2 . GLN A 1 142 ? 29.062 -22.510 16.275 1.00 117.85 ? 142 GLN A NE2 1 ATOM 1104 N N . GLN A 1 143 ? 26.216 -20.906 21.337 1.00 84.80 ? 143 GLN A N 1 ATOM 1105 C CA . GLN A 1 143 ? 25.684 -19.805 22.093 1.00 82.44 ? 143 GLN A CA 1 ATOM 1106 C C . GLN A 1 143 ? 26.077 -18.540 21.388 1.00 65.37 ? 143 GLN A C 1 ATOM 1107 O O . GLN A 1 143 ? 27.245 -18.313 21.086 1.00 63.65 ? 143 GLN A O 1 ATOM 1108 C CB . GLN A 1 143 ? 26.192 -19.844 23.544 1.00 87.12 ? 143 GLN A CB 1 ATOM 1109 C CG . GLN A 1 143 ? 25.390 -18.947 24.475 1.00 93.79 ? 143 GLN A CG 1 ATOM 1110 C CD . GLN A 1 143 ? 26.102 -18.661 25.770 1.00 105.99 ? 143 GLN A CD 1 ATOM 1111 O OE1 . GLN A 1 143 ? 27.205 -19.150 26.013 1.00 118.15 ? 143 GLN A OE1 1 ATOM 1112 N NE2 . GLN A 1 143 ? 25.493 -17.838 26.599 1.00 103.38 ? 143 GLN A NE2 1 ATOM 1113 N N . CYS A 1 144 ? 25.126 -17.693 21.121 1.00 49.62 ? 144 CYS A N 1 ATOM 1114 C CA . CYS A 1 144 ? 25.530 -16.467 20.472 1.00 70.25 ? 144 CYS A CA 1 ATOM 1115 C C . CYS A 1 144 ? 24.977 -15.348 21.290 1.00 60.73 ? 144 CYS A C 1 ATOM 1116 O O . CYS A 1 144 ? 23.768 -15.194 21.392 1.00 68.31 ? 144 CYS A O 1 ATOM 1117 C CB . CYS A 1 144 ? 25.048 -16.418 19.000 1.00 74.97 ? 144 CYS A CB 1 ATOM 1118 S SG . CYS A 1 144 ? 25.701 -17.744 17.986 1.00 154.65 ? 144 CYS A SG 1 ATOM 1119 N N . ASN A 1 145 ? 25.839 -14.563 21.891 1.00 48.39 ? 145 ASN A N 1 ATOM 1120 C CA . ASN A 1 145 ? 25.318 -13.510 22.753 1.00 66.54 ? 145 ASN A CA 1 ATOM 1121 C C . ASN A 1 145 ? 25.237 -12.278 21.969 1.00 47.20 ? 145 ASN A C 1 ATOM 1122 O O . ASN A 1 145 ? 26.086 -12.042 21.148 1.00 56.04 ? 145 ASN A O 1 ATOM 1123 C CB . ASN A 1 145 ? 26.186 -13.239 23.991 1.00 73.03 ? 145 ASN A CB 1 ATOM 1124 C CG . ASN A 1 145 ? 25.930 -14.191 25.132 1.00 82.31 ? 145 ASN A CG 1 ATOM 1125 O OD1 . ASN A 1 145 ? 25.212 -15.190 25.008 1.00 68.62 ? 145 ASN A OD1 1 ATOM 1126 N ND2 . ASN A 1 145 ? 26.538 -13.871 26.274 1.00 99.68 ? 145 ASN A ND2 1 ATOM 1127 N N . LEU A 1 146 ? 24.266 -11.448 22.262 1.00 58.44 ? 146 LEU A N 1 ATOM 1128 C CA . LEU A 1 146 ? 24.210 -10.146 21.629 1.00 78.19 ? 146 LEU A CA 1 ATOM 1129 C C . LEU A 1 146 ? 24.153 -9.079 22.701 1.00 70.70 ? 146 LEU A C 1 ATOM 1130 O O . LEU A 1 146 ? 23.133 -8.915 23.365 1.00 75.88 ? 146 LEU A O 1 ATOM 1131 C CB . LEU A 1 146 ? 22.987 -10.051 20.705 1.00 82.68 ? 146 LEU A CB 1 ATOM 1132 C CG . LEU A 1 146 ? 23.031 -10.994 19.511 1.00 71.56 ? 146 LEU A CG 1 ATOM 1133 C CD1 . LEU A 1 146 ? 21.646 -11.229 19.003 1.00 73.84 ? 146 LEU A CD1 1 ATOM 1134 C CD2 . LEU A 1 146 ? 23.886 -10.350 18.455 1.00 76.32 ? 146 LEU A CD2 1 ATOM 1135 N N . THR A 1 147 ? 25.238 -8.356 22.893 1.00 54.20 ? 147 THR A N 1 ATOM 1136 C CA . THR A 1 147 ? 25.200 -7.408 23.971 1.00 50.95 ? 147 THR A CA 1 ATOM 1137 C C . THR A 1 147 ? 25.044 -5.948 23.577 1.00 48.20 ? 147 THR A C 1 ATOM 1138 O O . THR A 1 147 ? 25.914 -5.366 22.961 1.00 65.45 ? 147 THR A O 1 ATOM 1139 C CB . THR A 1 147 ? 26.429 -7.578 24.805 1.00 49.27 ? 147 THR A CB 1 ATOM 1140 O OG1 . THR A 1 147 ? 26.357 -8.860 25.474 1.00 53.93 ? 147 THR A OG1 1 ATOM 1141 C CG2 . THR A 1 147 ? 26.478 -6.490 25.863 1.00 52.95 ? 147 THR A CG2 1 ATOM 1142 N N . PHE A 1 148 ? 23.963 -5.319 24.006 1.00 51.06 ? 148 PHE A N 1 ATOM 1143 C CA . PHE A 1 148 ? 23.743 -3.925 23.596 1.00 68.77 ? 148 PHE A CA 1 ATOM 1144 C C . PHE A 1 148 ? 23.936 -2.961 24.741 1.00 67.79 ? 148 PHE A C 1 ATOM 1145 O O . PHE A 1 148 ? 23.482 -3.254 25.880 1.00 48.99 ? 148 PHE A O 1 ATOM 1146 C CB . PHE A 1 148 ? 22.312 -3.722 23.060 1.00 71.40 ? 148 PHE A CB 1 ATOM 1147 C CG . PHE A 1 148 ? 21.947 -4.645 21.945 1.00 75.03 ? 148 PHE A CG 1 ATOM 1148 C CD1 . PHE A 1 148 ? 21.718 -5.996 22.194 1.00 81.78 ? 148 PHE A CD1 1 ATOM 1149 C CD2 . PHE A 1 148 ? 21.849 -4.185 20.659 1.00 53.93 ? 148 PHE A CD2 1 ATOM 1150 C CE1 . PHE A 1 148 ? 21.409 -6.866 21.180 1.00 57.44 ? 148 PHE A CE1 1 ATOM 1151 C CE2 . PHE A 1 148 ? 21.548 -5.051 19.660 1.00 61.89 ? 148 PHE A CE2 1 ATOM 1152 C CZ . PHE A 1 148 ? 21.330 -6.406 19.935 1.00 56.64 ? 148 PHE A CZ 1 ATOM 1153 N N . GLY A 1 149 ? 24.592 -1.835 24.461 1.00 46.72 ? 149 GLY A N 1 ATOM 1154 C CA . GLY A 1 149 ? 24.588 -0.769 25.439 1.00 47.10 ? 149 GLY A CA 1 ATOM 1155 C C . GLY A 1 149 ? 24.968 0.536 24.804 1.00 47.67 ? 149 GLY A C 1 ATOM 1156 O O . GLY A 1 149 ? 25.571 0.506 23.775 1.00 47.89 ? 149 GLY A O 1 ATOM 1157 N N . SER A 1 150 ? 24.804 1.658 25.487 1.00 48.12 ? 150 SER A N 1 ATOM 1158 C CA . SER A 1 150 ? 25.078 2.941 24.877 1.00 48.81 ? 150 SER A CA 1 ATOM 1159 C C . SER A 1 150 ? 26.498 3.150 24.499 1.00 59.88 ? 150 SER A C 1 ATOM 1160 O O . SER A 1 150 ? 27.401 2.499 25.018 1.00 96.06 ? 150 SER A O 1 ATOM 1161 C CB . SER A 1 150 ? 24.682 4.071 25.799 1.00 49.31 ? 150 SER A CB 1 ATOM 1162 O OG . SER A 1 150 ? 25.152 5.292 25.233 1.00 54.97 ? 150 SER A OG 1 ATOM 1163 N N . TRP A 1 151 ? 26.729 4.068 23.581 1.00 58.73 ? 151 TRP A N 1 ATOM 1164 C CA . TRP A 1 151 ? 28.108 4.275 23.122 1.00 86.52 ? 151 TRP A CA 1 ATOM 1165 C C . TRP A 1 151 ? 28.742 5.414 23.873 1.00 107.82 ? 151 TRP A C 1 ATOM 1166 O O . TRP A 1 151 ? 29.960 5.487 23.969 1.00 119.57 ? 151 TRP A O 1 ATOM 1167 C CB . TRP A 1 151 ? 28.154 4.521 21.605 1.00 86.93 ? 151 TRP A CB 1 ATOM 1168 C CG . TRP A 1 151 ? 29.492 4.808 21.018 1.00 79.86 ? 151 TRP A CG 1 ATOM 1169 C CD1 . TRP A 1 151 ? 30.036 6.035 20.762 1.00 83.69 ? 151 TRP A CD1 1 ATOM 1170 C CD2 . TRP A 1 151 ? 30.451 3.838 20.578 1.00 86.16 ? 151 TRP A CD2 1 ATOM 1171 N NE1 . TRP A 1 151 ? 31.286 5.890 20.198 1.00 94.84 ? 151 TRP A NE1 1 ATOM 1172 C CE2 . TRP A 1 151 ? 31.570 4.551 20.081 1.00 98.72 ? 151 TRP A CE2 1 ATOM 1173 C CE3 . TRP A 1 151 ? 30.480 2.433 20.566 1.00 86.08 ? 151 TRP A CE3 1 ATOM 1174 C CZ2 . TRP A 1 151 ? 32.722 3.900 19.583 1.00 100.56 ? 151 TRP A CZ2 1 ATOM 1175 C CZ3 . TRP A 1 151 ? 31.626 1.781 20.066 1.00 88.92 ? 151 TRP A CZ3 1 ATOM 1176 C CH2 . TRP A 1 151 ? 32.732 2.521 19.590 1.00 94.94 ? 151 TRP A CH2 1 ATOM 1177 N N . THR A 1 152 ? 27.918 6.296 24.429 1.00 120.62 ? 152 THR A N 1 ATOM 1178 C CA . THR A 1 152 ? 28.454 7.517 25.013 1.00 128.29 ? 152 THR A CA 1 ATOM 1179 C C . THR A 1 152 ? 27.962 7.909 26.427 1.00 118.20 ? 152 THR A C 1 ATOM 1180 O O . THR A 1 152 ? 28.389 8.948 26.940 1.00 102.88 ? 152 THR A O 1 ATOM 1181 C CB . THR A 1 152 ? 28.174 8.719 24.050 1.00 108.75 ? 152 THR A CB 1 ATOM 1182 O OG1 . THR A 1 152 ? 26.785 9.052 24.083 1.00 110.66 ? 152 THR A OG1 1 ATOM 1183 C CG2 . THR A 1 152 ? 28.553 8.395 22.591 1.00 95.01 ? 152 THR A CG2 1 ATOM 1184 N N . TYR A 1 153 ? 27.096 7.089 27.046 1.00 93.97 ? 153 TYR A N 1 ATOM 1185 C CA . TYR A 1 153 ? 26.382 7.449 28.291 1.00 76.63 ? 153 TYR A CA 1 ATOM 1186 C C . TYR A 1 153 ? 26.284 6.354 29.396 1.00 91.48 ? 153 TYR A C 1 ATOM 1187 O O . TYR A 1 153 ? 25.660 5.292 29.157 1.00 82.12 ? 153 TYR A O 1 ATOM 1188 C CB . TYR A 1 153 ? 24.933 7.877 27.954 1.00 78.74 ? 153 TYR A CB 1 ATOM 1189 C CG . TYR A 1 153 ? 24.782 9.198 27.225 1.00 84.17 ? 153 TYR A CG 1 ATOM 1190 C CD1 . TYR A 1 153 ? 24.980 10.412 27.882 1.00 93.90 ? 153 TYR A CD1 1 ATOM 1191 C CD2 . TYR A 1 153 ? 24.392 9.234 25.908 1.00 76.74 ? 153 TYR A CD2 1 ATOM 1192 C CE1 . TYR A 1 153 ? 24.833 11.630 27.223 1.00 95.65 ? 153 TYR A CE1 1 ATOM 1193 C CE2 . TYR A 1 153 ? 24.243 10.443 25.242 1.00 91.63 ? 153 TYR A CE2 1 ATOM 1194 C CZ . TYR A 1 153 ? 24.464 11.640 25.902 1.00 97.76 ? 153 TYR A CZ 1 ATOM 1195 O OH . TYR A 1 153 ? 24.315 12.844 25.226 1.00 106.55 ? 153 TYR A OH 1 ATOM 1196 N N . ASN A 1 154 ? 26.838 6.621 30.597 1.00 91.30 ? 154 ASN A N 1 ATOM 1197 C CA . ASN A 1 154 ? 26.638 5.742 31.783 1.00 95.40 ? 154 ASN A CA 1 ATOM 1198 C C . ASN A 1 154 ? 25.185 5.579 32.177 1.00 87.81 ? 154 ASN A C 1 ATOM 1199 O O . ASN A 1 154 ? 24.331 6.387 31.790 1.00 88.93 ? 154 ASN A O 1 ATOM 1200 C CB . ASN A 1 154 ? 27.386 6.242 33.004 1.00 100.17 ? 154 ASN A CB 1 ATOM 1201 C CG . ASN A 1 154 ? 27.189 7.706 33.217 1.00 110.59 ? 154 ASN A CG 1 ATOM 1202 O OD1 . ASN A 1 154 ? 26.071 8.159 33.447 1.00 116.32 ? 154 ASN A OD1 1 ATOM 1203 N ND2 . ASN A 1 154 ? 28.258 8.474 33.087 1.00 111.93 ? 154 ASN A ND2 1 ATOM 1204 N N . GLY A 1 155 ? 24.911 4.553 32.972 1.00 77.89 ? 155 GLY A N 1 ATOM 1205 C CA . GLY A 1 155 ? 23.593 4.392 33.576 1.00 80.34 ? 155 GLY A CA 1 ATOM 1206 C C . GLY A 1 155 ? 23.105 5.565 34.432 1.00 92.17 ? 155 GLY A C 1 ATOM 1207 O O . GLY A 1 155 ? 22.000 5.527 34.987 1.00 90.74 ? 155 GLY A O 1 ATOM 1208 N N . ASN A 1 156 ? 23.956 6.577 34.596 1.00 102.25 ? 156 ASN A N 1 ATOM 1209 C CA . ASN A 1 156 ? 23.646 7.742 35.427 1.00 114.50 ? 156 ASN A CA 1 ATOM 1210 C C . ASN A 1 156 ? 23.235 8.904 34.549 1.00 108.71 ? 156 ASN A C 1 ATOM 1211 O O . ASN A 1 156 ? 22.785 9.946 35.030 1.00 104.64 ? 156 ASN A O 1 ATOM 1212 C CB . ASN A 1 156 ? 24.847 8.134 36.301 1.00 125.53 ? 156 ASN A CB 1 ATOM 1213 C CG . ASN A 1 156 ? 24.442 8.947 37.511 1.00 129.61 ? 156 ASN A CG 1 ATOM 1214 O OD1 . ASN A 1 156 ? 24.281 10.166 37.441 1.00 135.31 ? 156 ASN A OD1 1 ATOM 1215 N ND2 . ASN A 1 156 ? 24.271 8.266 38.634 1.00 128.67 ? 156 ASN A ND2 1 ATOM 1216 N N . GLN A 1 157 ? 23.443 8.724 33.252 1.00 107.03 ? 157 GLN A N 1 ATOM 1217 C CA . GLN A 1 157 ? 22.834 9.579 32.251 1.00 100.39 ? 157 GLN A CA 1 ATOM 1218 C C . GLN A 1 157 ? 21.695 8.841 31.554 1.00 94.51 ? 157 GLN A C 1 ATOM 1219 O O . GLN A 1 157 ? 20.626 9.399 31.339 1.00 89.28 ? 157 GLN A O 1 ATOM 1220 C CB . GLN A 1 157 ? 23.879 10.014 31.230 1.00 106.65 ? 157 GLN A CB 1 ATOM 1221 C CG . GLN A 1 157 ? 25.054 10.800 31.818 1.00 107.40 ? 157 GLN A CG 1 ATOM 1222 C CD . GLN A 1 157 ? 26.382 10.462 31.164 1.00 94.80 ? 157 GLN A CD 1 ATOM 1223 O OE1 . GLN A 1 157 ? 26.776 9.294 31.075 1.00 82.10 ? 157 GLN A OE1 1 ATOM 1224 N NE2 . GLN A 1 157 ? 27.052 11.486 30.647 1.00 93.74 ? 157 GLN A NE2 1 ATOM 1225 N N . VAL A 1 158 ? 21.940 7.577 31.211 1.00 89.15 ? 158 VAL A N 1 ATOM 1226 C CA . VAL A 1 158 ? 20.973 6.745 30.500 1.00 77.21 ? 158 VAL A CA 1 ATOM 1227 C C . VAL A 1 158 ? 20.943 5.309 31.023 1.00 78.59 ? 158 VAL A C 1 ATOM 1228 O O . VAL A 1 158 ? 21.937 4.599 30.915 1.00 84.07 ? 158 VAL A O 1 ATOM 1229 C CB . VAL A 1 158 ? 21.299 6.721 28.972 1.00 83.06 ? 158 VAL A CB 1 ATOM 1230 C CG1 . VAL A 1 158 ? 20.369 5.771 28.229 1.00 87.74 ? 158 VAL A CG1 1 ATOM 1231 C CG2 . VAL A 1 158 ? 21.251 8.139 28.355 1.00 71.60 ? 158 VAL A CG2 1 ATOM 1232 N N . ASP A 1 159 ? 19.819 4.856 31.572 1.00 73.72 ? 159 ASP A N 1 ATOM 1233 C CA . ASP A 1 159 ? 19.729 3.451 32.005 1.00 84.26 ? 159 ASP A CA 1 ATOM 1234 C C . ASP A 1 159 ? 18.927 2.756 30.936 1.00 84.68 ? 159 ASP A C 1 ATOM 1235 O O . ASP A 1 159 ? 18.048 3.377 30.345 1.00 85.89 ? 159 ASP A O 1 ATOM 1236 C CB . ASP A 1 159 ? 19.057 3.293 33.382 1.00 95.78 ? 159 ASP A CB 1 ATOM 1237 C CG . ASP A 1 159 ? 19.261 1.896 34.009 1.00 95.39 ? 159 ASP A CG 1 ATOM 1238 O OD1 . ASP A 1 159 ? 19.653 0.944 33.308 1.00 88.61 ? 159 ASP A OD1 1 ATOM 1239 O OD2 . ASP A 1 159 ? 18.962 1.734 35.207 1.00 101.09 ? 159 ASP A OD2 1 ATOM 1240 N N . ILE A 1 160 ? 19.241 1.496 30.647 1.00 75.35 ? 160 ILE A N 1 ATOM 1241 C CA . ILE A 1 160 ? 18.574 0.853 29.538 1.00 70.33 ? 160 ILE A CA 1 ATOM 1242 C C . ILE A 1 160 ? 17.981 -0.491 29.973 1.00 78.58 ? 160 ILE A C 1 ATOM 1243 O O . ILE A 1 160 ? 18.689 -1.340 30.511 1.00 70.31 ? 160 ILE A O 1 ATOM 1244 C CB . ILE A 1 160 ? 19.536 0.697 28.310 1.00 91.35 ? 160 ILE A CB 1 ATOM 1245 C CG1 . ILE A 1 160 ? 20.557 -0.409 28.494 1.00 100.46 ? 160 ILE A CG1 1 ATOM 1246 C CG2 . ILE A 1 160 ? 20.208 2.032 27.953 1.00 83.26 ? 160 ILE A CG2 1 ATOM 1247 C CD1 . ILE A 1 160 ? 20.263 -1.591 27.637 1.00 98.65 ? 160 ILE A CD1 1 ATOM 1248 N N . PHE A 1 161 ? 16.659 -0.639 29.785 1.00 90.44 ? 161 PHE A N 1 ATOM 1249 C CA . PHE A 1 161 ? 15.891 -1.844 30.169 1.00 88.38 ? 161 PHE A CA 1 ATOM 1250 C C . PHE A 1 161 ? 15.356 -2.677 28.985 1.00 82.92 ? 161 PHE A C 1 ATOM 1251 O O . PHE A 1 161 ? 14.847 -2.120 28.001 1.00 84.77 ? 161 PHE A O 1 ATOM 1252 C CB . PHE A 1 161 ? 14.698 -1.429 31.038 1.00 93.28 ? 161 PHE A CB 1 ATOM 1253 C CG . PHE A 1 161 ? 15.077 -0.568 32.182 1.00 100.57 ? 161 PHE A CG 1 ATOM 1254 C CD1 . PHE A 1 161 ? 15.618 -1.118 33.327 1.00 106.09 ? 161 PHE A CD1 1 ATOM 1255 C CD2 . PHE A 1 161 ? 14.953 0.810 32.094 1.00 107.51 ? 161 PHE A CD2 1 ATOM 1256 C CE1 . PHE A 1 161 ? 15.989 -0.311 34.385 1.00 111.45 ? 161 PHE A CE1 1 ATOM 1257 C CE2 . PHE A 1 161 ? 15.331 1.621 33.153 1.00 114.77 ? 161 PHE A CE2 1 ATOM 1258 C CZ . PHE A 1 161 ? 15.853 1.062 34.297 1.00 112.14 ? 161 PHE A CZ 1 ATOM 1259 N N . ASN A 1 162 ? 15.452 -4.003 29.090 1.00 68.02 ? 162 ASN A N 1 ATOM 1260 C CA . ASN A 1 162 ? 14.729 -4.895 28.174 1.00 79.27 ? 162 ASN A CA 1 ATOM 1261 C C . ASN A 1 162 ? 13.203 -4.895 28.363 1.00 86.31 ? 162 ASN A C 1 ATOM 1262 O O . ASN A 1 162 ? 12.714 -4.925 29.487 1.00 82.30 ? 162 ASN A O 1 ATOM 1263 C CB . ASN A 1 162 ? 15.255 -6.309 28.329 1.00 82.70 ? 162 ASN A CB 1 ATOM 1264 C CG . ASN A 1 162 ? 15.467 -6.655 29.758 1.00 100.02 ? 162 ASN A CG 1 ATOM 1265 O OD1 . ASN A 1 162 ? 15.849 -5.785 30.535 1.00 108.20 ? 162 ASN A OD1 1 ATOM 1266 N ND2 . ASN A 1 162 ? 15.189 -7.903 30.140 1.00 108.10 ? 162 ASN A ND2 1 ATOM 1267 N N . ALA A 1 163 ? 12.455 -4.912 27.259 1.00 101.12 ? 163 ALA A N 1 ATOM 1268 C CA . ALA A 1 163 ? 10.977 -4.918 27.299 1.00 108.31 ? 163 ALA A CA 1 ATOM 1269 C C . ALA A 1 163 ? 10.430 -6.192 27.939 1.00 116.43 ? 163 ALA A C 1 ATOM 1270 O O . ALA A 1 163 ? 9.362 -6.197 28.553 1.00 125.69 ? 163 ALA A O 1 ATOM 1271 C CB . ALA A 1 163 ? 10.415 -4.757 25.922 1.00 106.90 ? 163 ALA A CB 1 ATOM 1272 N N . LEU A 1 164 ? 11.165 -7.276 27.759 1.00 113.63 ? 164 LEU A N 1 ATOM 1273 C CA . LEU A 1 164 ? 10.966 -8.476 28.547 1.00 106.50 ? 164 LEU A CA 1 ATOM 1274 C C . LEU A 1 164 ? 12.175 -9.399 28.468 1.00 92.37 ? 164 LEU A C 1 ATOM 1275 O O . LEU A 1 164 ? 13.096 -9.214 27.645 1.00 86.18 ? 164 LEU A O 1 ATOM 1276 C CB . LEU A 1 164 ? 9.664 -9.208 28.159 1.00 93.51 ? 164 LEU A CB 1 ATOM 1277 C CG . LEU A 1 164 ? 9.239 -9.593 26.743 1.00 90.57 ? 164 LEU A CG 1 ATOM 1278 C CD1 . LEU A 1 164 ? 9.960 -10.798 26.176 1.00 97.21 ? 164 LEU A CD1 1 ATOM 1279 C CD2 . LEU A 1 164 ? 7.766 -9.910 26.860 1.00 86.76 ? 164 LEU A CD2 1 ATOM 1280 N N . ASP A 1 165 ? 12.139 -10.372 29.371 1.00 78.74 ? 165 ASP A N 1 ATOM 1281 C CA . ASP A 1 165 ? 13.236 -11.242 29.695 1.00 88.74 ? 165 ASP A CA 1 ATOM 1282 C C . ASP A 1 165 ? 13.302 -12.393 28.681 1.00 86.47 ? 165 ASP A C 1 ATOM 1283 O O . ASP A 1 165 ? 13.720 -13.523 28.974 1.00 84.54 ? 165 ASP A O 1 ATOM 1284 C CB . ASP A 1 165 ? 13.088 -11.748 31.152 1.00 111.65 ? 165 ASP A CB 1 ATOM 1285 C CG . ASP A 1 165 ? 13.117 -10.601 32.190 1.00 116.16 ? 165 ASP A CG 1 ATOM 1286 O OD1 . ASP A 1 165 ? 13.971 -9.698 32.061 1.00 122.38 ? 165 ASP A OD1 1 ATOM 1287 O OD2 . ASP A 1 165 ? 12.299 -10.609 33.139 1.00 108.93 ? 165 ASP A OD2 1 ATOM 1288 N N . SER A 1 166 ? 12.905 -12.080 27.464 1.00 83.97 ? 166 SER A N 1 ATOM 1289 C CA . SER A 1 166 ? 13.217 -12.936 26.344 1.00 94.00 ? 166 SER A CA 1 ATOM 1290 C C . SER A 1 166 ? 13.438 -11.985 25.226 1.00 94.03 ? 166 SER A C 1 ATOM 1291 O O . SER A 1 166 ? 12.952 -10.856 25.265 1.00 96.95 ? 166 SER A O 1 ATOM 1292 C CB . SER A 1 166 ? 12.093 -13.912 26.021 1.00 107.72 ? 166 SER A CB 1 ATOM 1293 O OG . SER A 1 166 ? 11.931 -14.847 27.076 1.00 118.53 ? 166 SER A OG 1 ATOM 1294 N N . GLY A 1 167 ? 14.178 -12.427 24.228 1.00 96.61 ? 167 GLY A N 1 ATOM 1295 C CA . GLY A 1 167 ? 14.271 -11.658 23.016 1.00 95.71 ? 167 GLY A CA 1 ATOM 1296 C C . GLY A 1 167 ? 13.151 -12.185 22.182 1.00 93.16 ? 167 GLY A C 1 ATOM 1297 O O . GLY A 1 167 ? 12.992 -13.410 22.067 1.00 91.24 ? 167 GLY A O 1 ATOM 1298 N N . ASP A 1 168 ? 12.365 -11.263 21.641 1.00 98.98 ? 168 ASP A N 1 ATOM 1299 C CA . ASP A 1 168 ? 11.223 -11.601 20.792 1.00 105.52 ? 168 ASP A CA 1 ATOM 1300 C C . ASP A 1 168 ? 11.516 -12.510 19.606 1.00 111.11 ? 168 ASP A C 1 ATOM 1301 O O . ASP A 1 168 ? 12.190 -12.097 18.654 1.00 100.10 ? 168 ASP A O 1 ATOM 1302 C CB . ASP A 1 168 ? 10.589 -10.337 20.229 1.00 105.01 ? 168 ASP A CB 1 ATOM 1303 C CG . ASP A 1 168 ? 9.384 -10.641 19.400 1.00 115.54 ? 168 ASP A CG 1 ATOM 1304 O OD1 . ASP A 1 168 ? 8.698 -11.626 19.727 1.00 117.72 ? 168 ASP A OD1 1 ATOM 1305 O OD2 . ASP A 1 168 ? 9.131 -9.914 18.420 1.00 125.38 ? 168 ASP A OD2 1 ATOM 1306 N N . LEU A 1 169 ? 11.060 -13.757 19.694 1.00 122.83 ? 169 LEU A N 1 ATOM 1307 C CA . LEU A 1 169 ? 11.052 -14.632 18.537 1.00 120.73 ? 169 LEU A CA 1 ATOM 1308 C C . LEU A 1 169 ? 9.837 -14.282 17.662 1.00 124.26 ? 169 LEU A C 1 ATOM 1309 O O . LEU A 1 169 ? 10.013 -13.862 16.529 1.00 136.68 ? 169 LEU A O 1 ATOM 1310 C CB . LEU A 1 169 ? 11.063 -16.106 18.941 1.00 113.72 ? 169 LEU A CB 1 ATOM 1311 C CG . LEU A 1 169 ? 12.238 -16.484 19.855 1.00 114.87 ? 169 LEU A CG 1 ATOM 1312 C CD1 . LEU A 1 169 ? 12.263 -17.981 20.128 1.00 118.67 ? 169 LEU A CD1 1 ATOM 1313 C CD2 . LEU A 1 169 ? 13.570 -16.001 19.307 1.00 108.29 ? 169 LEU A CD2 1 ATOM 1314 N N . SER A 1 170 ? 8.631 -14.399 18.219 1.00 114.92 ? 170 SER A N 1 ATOM 1315 C CA . SER A 1 170 ? 7.338 -14.250 17.503 1.00 127.72 ? 170 SER A CA 1 ATOM 1316 C C . SER A 1 170 ? 7.405 -14.151 15.973 1.00 130.90 ? 170 SER A C 1 ATOM 1317 O O . SER A 1 170 ? 6.867 -15.027 15.287 1.00 136.58 ? 170 SER A O 1 ATOM 1318 C CB . SER A 1 170 ? 6.544 -13.044 18.066 1.00 81.16 ? 170 SER A CB 1 ATOM 1319 O OG . SER A 1 170 ? 6.665 -11.825 17.339 1.00 69.28 ? 170 SER A OG 1 ATOM 1320 N N . ASP A 1 171 ? 8.042 -13.098 15.442 1.00 130.15 ? 171 ASP A N 1 ATOM 1321 C CA . ASP A 1 171 ? 8.280 -13.006 13.988 1.00 125.87 ? 171 ASP A CA 1 ATOM 1322 C C . ASP A 1 171 ? 9.653 -13.560 13.633 1.00 117.05 ? 171 ASP A C 1 ATOM 1323 O O . ASP A 1 171 ? 10.315 -13.072 12.731 1.00 107.77 ? 171 ASP A O 1 ATOM 1324 C CB . ASP A 1 171 ? 8.171 -11.568 13.446 1.00 124.19 ? 171 ASP A CB 1 ATOM 1325 C CG . ASP A 1 171 ? 7.035 -10.790 14.052 1.00 131.41 ? 171 ASP A CG 1 ATOM 1326 O OD1 . ASP A 1 171 ? 5.899 -11.319 14.079 1.00 140.84 ? 171 ASP A OD1 1 ATOM 1327 O OD2 . ASP A 1 171 ? 7.259 -9.623 14.438 1.00 131.58 ? 171 ASP A OD2 1 ATOM 1328 N N . PHE A 1 172 ? 10.061 -14.601 14.344 1.00 118.30 ? 172 PHE A N 1 ATOM 1329 C CA . PHE A 1 172 ? 11.243 -15.357 13.980 1.00 114.42 ? 172 PHE A CA 1 ATOM 1330 C C . PHE A 1 172 ? 10.863 -16.304 12.859 1.00 118.51 ? 172 PHE A C 1 ATOM 1331 O O . PHE A 1 172 ? 9.727 -16.774 12.780 1.00 117.65 ? 172 PHE A O 1 ATOM 1332 C CB . PHE A 1 172 ? 11.791 -16.089 15.209 1.00 108.34 ? 172 PHE A CB 1 ATOM 1333 C CG . PHE A 1 172 ? 12.702 -17.241 14.903 1.00 102.32 ? 172 PHE A CG 1 ATOM 1334 C CD1 . PHE A 1 172 ? 13.932 -17.046 14.287 1.00 98.18 ? 172 PHE A CD1 1 ATOM 1335 C CD2 . PHE A 1 172 ? 12.341 -18.530 15.296 1.00 103.05 ? 172 PHE A CD2 1 ATOM 1336 C CE1 . PHE A 1 172 ? 14.776 -18.129 14.033 1.00 100.07 ? 172 PHE A CE1 1 ATOM 1337 C CE2 . PHE A 1 172 ? 13.173 -19.615 15.052 1.00 104.87 ? 172 PHE A CE2 1 ATOM 1338 C CZ . PHE A 1 172 ? 14.394 -19.417 14.418 1.00 105.03 ? 172 PHE A CZ 1 ATOM 1339 N N . ILE A 1 173 ? 11.837 -16.580 11.999 1.00 124.27 ? 173 ILE A N 1 ATOM 1340 C CA . ILE A 1 173 ? 11.586 -17.205 10.712 1.00 125.87 ? 173 ILE A CA 1 ATOM 1341 C C . ILE A 1 173 ? 12.448 -18.478 10.611 1.00 126.29 ? 173 ILE A C 1 ATOM 1342 O O . ILE A 1 173 ? 13.542 -18.481 10.045 1.00 130.44 ? 173 ILE A O 1 ATOM 1343 C CB . ILE A 1 173 ? 11.857 -16.175 9.590 1.00 120.61 ? 173 ILE A CB 1 ATOM 1344 C CG1 . ILE A 1 173 ? 11.008 -14.916 9.862 1.00 113.21 ? 173 ILE A CG1 1 ATOM 1345 C CG2 . ILE A 1 173 ? 11.563 -16.765 8.243 1.00 116.57 ? 173 ILE A CG2 1 ATOM 1346 C CD1 . ILE A 1 173 ? 11.126 -13.789 8.887 1.00 100.32 ? 173 ILE A CD1 1 ATOM 1347 N N . GLU A 1 174 ? 11.916 -19.537 11.224 1.00 131.89 ? 174 GLU A N 1 ATOM 1348 C CA . GLU A 1 174 ? 12.492 -20.887 11.354 1.00 131.64 ? 174 GLU A CA 1 ATOM 1349 C C . GLU A 1 174 ? 13.505 -21.390 10.295 1.00 135.38 ? 174 GLU A C 1 ATOM 1350 O O . GLU A 1 174 ? 13.128 -22.030 9.311 1.00 133.02 ? 174 GLU A O 1 ATOM 1351 C CB . GLU A 1 174 ? 11.328 -21.872 11.447 1.00 133.44 ? 174 GLU A CB 1 ATOM 1352 C CG . GLU A 1 174 ? 10.059 -21.230 12.002 1.00 141.52 ? 174 GLU A CG 1 ATOM 1353 C CD . GLU A 1 174 ? 9.070 -22.237 12.551 1.00 153.03 ? 174 GLU A CD 1 ATOM 1354 O OE1 . GLU A 1 174 ? 9.317 -23.452 12.415 1.00 157.40 ? 174 GLU A OE1 1 ATOM 1355 O OE2 . GLU A 1 174 ? 8.034 -21.812 13.107 1.00 162.42 ? 174 GLU A OE2 1 ATOM 1356 N N . ASP A 1 175 ? 14.788 -21.113 10.511 1.00 125.06 ? 175 ASP A N 1 ATOM 1357 C CA . ASP A 1 175 ? 15.822 -21.597 9.611 1.00 126.99 ? 175 ASP A CA 1 ATOM 1358 C C . ASP A 1 175 ? 15.828 -23.126 9.575 1.00 127.36 ? 175 ASP A C 1 ATOM 1359 O O . ASP A 1 175 ? 15.390 -23.787 10.517 1.00 135.00 ? 175 ASP A O 1 ATOM 1360 C CB . ASP A 1 175 ? 17.180 -21.056 10.078 1.00 137.67 ? 175 ASP A CB 1 ATOM 1361 C CG . ASP A 1 175 ? 18.356 -21.568 9.251 1.00 146.37 ? 175 ASP A CG 1 ATOM 1362 O OD1 . ASP A 1 175 ? 18.428 -21.213 8.051 1.00 153.11 ? 175 ASP A OD1 1 ATOM 1363 O OD2 . ASP A 1 175 ? 19.223 -22.292 9.816 1.00 143.33 ? 175 ASP A OD2 1 ATOM 1364 N N . VAL A 1 176 ? 16.338 -23.682 8.481 1.00 122.63 ? 176 VAL A N 1 ATOM 1365 C CA . VAL A 1 176 ? 16.196 -25.108 8.203 1.00 113.66 ? 176 VAL A CA 1 ATOM 1366 C C . VAL A 1 176 ? 17.257 -25.941 8.919 1.00 112.42 ? 176 VAL A C 1 ATOM 1367 O O . VAL A 1 176 ? 16.994 -27.094 9.287 1.00 116.70 ? 176 VAL A O 1 ATOM 1368 C CB . VAL A 1 176 ? 16.243 -25.360 6.685 1.00 114.79 ? 176 VAL A CB 1 ATOM 1369 C CG1 . VAL A 1 176 ? 17.322 -24.506 6.052 1.00 112.92 ? 176 VAL A CG1 1 ATOM 1370 C CG2 . VAL A 1 176 ? 16.437 -26.843 6.343 1.00 116.20 ? 176 VAL A CG2 1 ATOM 1371 N N . GLU A 1 177 ? 18.457 -25.386 9.116 1.00 110.34 ? 177 GLU A N 1 ATOM 1372 C CA . GLU A 1 177 ? 19.446 -26.124 9.897 1.00 114.42 ? 177 GLU A CA 1 ATOM 1373 C C . GLU A 1 177 ? 19.607 -25.523 11.312 1.00 116.92 ? 177 GLU A C 1 ATOM 1374 O O . GLU A 1 177 ? 20.147 -26.159 12.168 1.00 108.31 ? 177 GLU A O 1 ATOM 1375 C CB . GLU A 1 177 ? 20.819 -26.267 9.219 1.00 120.98 ? 177 GLU A CB 1 ATOM 1376 C CG . GLU A 1 177 ? 21.328 -25.062 8.482 1.00 128.87 ? 177 GLU A CG 1 ATOM 1377 C CD . GLU A 1 177 ? 21.020 -25.089 6.989 1.00 134.41 ? 177 GLU A CD 1 ATOM 1378 O OE1 . GLU A 1 177 ? 20.257 -25.969 6.539 1.00 136.14 ? 177 GLU A OE1 1 ATOM 1379 O OE2 . GLU A 1 177 ? 21.535 -24.211 6.263 1.00 134.97 ? 177 GLU A OE2 1 ATOM 1380 N N . TRP A 1 178 ? 19.172 -24.304 11.600 1.00 125.31 ? 178 TRP A N 1 ATOM 1381 C CA . TRP A 1 178 ? 19.420 -23.797 12.970 1.00 127.97 ? 178 TRP A CA 1 ATOM 1382 C C . TRP A 1 178 ? 18.143 -23.401 13.780 1.00 136.51 ? 178 TRP A C 1 ATOM 1383 O O . TRP A 1 178 ? 17.270 -22.656 13.326 1.00 138.66 ? 178 TRP A O 1 ATOM 1384 C CB . TRP A 1 178 ? 20.443 -22.658 12.868 1.00 131.30 ? 178 TRP A CB 1 ATOM 1385 C CG . TRP A 1 178 ? 21.858 -23.227 12.610 1.00 138.42 ? 178 TRP A CG 1 ATOM 1386 C CD1 . TRP A 1 178 ? 22.546 -23.231 11.421 1.00 138.90 ? 178 TRP A CD1 1 ATOM 1387 C CD2 . TRP A 1 178 ? 22.720 -23.891 13.566 1.00 136.96 ? 178 TRP A CD2 1 ATOM 1388 N NE1 . TRP A 1 178 ? 23.771 -23.849 11.582 1.00 139.73 ? 178 TRP A NE1 1 ATOM 1389 C CE2 . TRP A 1 178 ? 23.901 -24.257 12.885 1.00 137.01 ? 178 TRP A CE2 1 ATOM 1390 C CE3 . TRP A 1 178 ? 22.605 -24.203 14.926 1.00 132.64 ? 178 TRP A CE3 1 ATOM 1391 C CZ2 . TRP A 1 178 ? 24.951 -24.919 13.517 1.00 133.59 ? 178 TRP A CZ2 1 ATOM 1392 C CZ3 . TRP A 1 178 ? 23.656 -24.861 15.549 1.00 133.22 ? 178 TRP A CZ3 1 ATOM 1393 C CH2 . TRP A 1 178 ? 24.809 -25.209 14.846 1.00 132.15 ? 178 TRP A CH2 1 ATOM 1394 N N . GLU A 1 179 ? 18.069 -23.935 15.001 1.00 139.17 ? 179 GLU A N 1 ATOM 1395 C CA . GLU A 1 179 ? 16.831 -23.980 15.820 1.00 126.90 ? 179 GLU A CA 1 ATOM 1396 C C . GLU A 1 179 ? 16.889 -23.189 17.104 1.00 109.34 ? 179 GLU A C 1 ATOM 1397 O O . GLU A 1 179 ? 17.447 -23.650 18.090 1.00 104.42 ? 179 GLU A O 1 ATOM 1398 C CB . GLU A 1 179 ? 16.409 -25.419 16.219 1.00 149.84 ? 179 GLU A CB 1 ATOM 1399 C CG . GLU A 1 179 ? 15.920 -26.290 15.095 1.00 158.76 ? 179 GLU A CG 1 ATOM 1400 C CD . GLU A 1 179 ? 15.636 -25.490 13.858 1.00 168.79 ? 179 GLU A CD 1 ATOM 1401 O OE1 . GLU A 1 179 ? 14.578 -24.831 13.742 1.00 170.04 ? 179 GLU A OE1 1 ATOM 1402 O OE2 . GLU A 1 179 ? 16.528 -25.526 12.989 1.00 169.16 ? 179 GLU A OE2 1 ATOM 1403 N N . VAL A 1 180 ? 16.286 -22.011 17.110 1.00 105.31 ? 180 VAL A N 1 ATOM 1404 C CA . VAL A 1 180 ? 16.258 -21.227 18.327 1.00 113.25 ? 180 VAL A CA 1 ATOM 1405 C C . VAL A 1 180 ? 15.502 -21.964 19.409 1.00 116.43 ? 180 VAL A C 1 ATOM 1406 O O . VAL A 1 180 ? 14.284 -22.147 19.343 1.00 116.86 ? 180 VAL A O 1 ATOM 1407 C CB . VAL A 1 180 ? 15.589 -19.883 18.107 1.00 111.28 ? 180 VAL A CB 1 ATOM 1408 C CG1 . VAL A 1 180 ? 15.293 -19.206 19.439 1.00 93.48 ? 180 VAL A CG1 1 ATOM 1409 C CG2 . VAL A 1 180 ? 16.452 -19.017 17.214 1.00 110.85 ? 180 VAL A CG2 1 ATOM 1410 N N . HIS A 1 181 ? 16.270 -22.357 20.418 1.00 128.79 ? 181 HIS A N 1 ATOM 1411 C CA . HIS A 1 181 ? 15.769 -23.005 21.615 1.00 136.93 ? 181 HIS A CA 1 ATOM 1412 C C . HIS A 1 181 ? 15.479 -21.996 22.697 1.00 139.22 ? 181 HIS A C 1 ATOM 1413 O O . HIS A 1 181 ? 14.496 -22.120 23.417 1.00 156.78 ? 181 HIS A O 1 ATOM 1414 C CB . HIS A 1 181 ? 16.759 -24.058 22.114 1.00 142.93 ? 181 HIS A CB 1 ATOM 1415 C CG . HIS A 1 181 ? 16.389 -25.447 21.702 1.00 154.02 ? 181 HIS A CG 1 ATOM 1416 N ND1 . HIS A 1 181 ? 15.087 -25.875 21.677 1.00 157.68 ? 181 HIS A ND1 1 ATOM 1417 C CD2 . HIS A 1 181 ? 17.151 -26.494 21.305 1.00 159.24 ? 181 HIS A CD2 1 ATOM 1418 C CE1 . HIS A 1 181 ? 15.050 -27.141 21.286 1.00 162.31 ? 181 HIS A CE1 1 ATOM 1419 N NE2 . HIS A 1 181 ? 16.285 -27.535 21.055 1.00 164.50 ? 181 HIS A NE2 1 ATOM 1420 N N . GLY A 1 182 ? 16.317 -20.983 22.808 1.00 105.93 ? 182 GLY A N 1 ATOM 1421 C CA . GLY A 1 182 ? 16.029 -19.941 23.768 1.00 98.62 ? 182 GLY A CA 1 ATOM 1422 C C . GLY A 1 182 ? 16.580 -18.622 23.308 1.00 89.26 ? 182 GLY A C 1 ATOM 1423 O O . GLY A 1 182 ? 17.495 -18.619 22.505 1.00 78.51 ? 182 GLY A O 1 ATOM 1424 N N . MET A 1 183 ? 15.993 -17.509 23.741 1.00 94.16 ? 183 MET A N 1 ATOM 1425 C CA . MET A 1 183 ? 16.683 -16.222 23.609 1.00 100.66 ? 183 MET A CA 1 ATOM 1426 C C . MET A 1 183 ? 16.485 -15.312 24.827 1.00 88.69 ? 183 MET A C 1 ATOM 1427 O O . MET A 1 183 ? 16.037 -14.166 24.677 1.00 78.43 ? 183 MET A O 1 ATOM 1428 C CB . MET A 1 183 ? 16.212 -15.464 22.368 1.00 120.60 ? 183 MET A CB 1 ATOM 1429 C CG . MET A 1 183 ? 17.281 -14.526 21.868 1.00 132.21 ? 183 MET A CG 1 ATOM 1430 S SD . MET A 1 183 ? 16.875 -13.123 20.819 1.00 75.59 ? 183 MET A SD 1 ATOM 1431 C CE . MET A 1 183 ? 18.584 -12.766 20.382 1.00 87.72 ? 183 MET A CE 1 ATOM 1432 N N . PRO A 1 184 ? 16.868 -15.782 26.025 1.00 85.94 ? 184 PRO A N 1 ATOM 1433 C CA . PRO A 1 184 ? 16.609 -15.009 27.256 1.00 81.34 ? 184 PRO A CA 1 ATOM 1434 C C . PRO A 1 184 ? 17.377 -13.685 27.300 1.00 77.01 ? 184 PRO A C 1 ATOM 1435 O O . PRO A 1 184 ? 18.341 -13.537 26.546 1.00 86.97 ? 184 PRO A O 1 ATOM 1436 C CB . PRO A 1 184 ? 17.071 -15.948 28.348 1.00 80.62 ? 184 PRO A CB 1 ATOM 1437 C CG . PRO A 1 184 ? 18.079 -16.845 27.667 1.00 76.32 ? 184 PRO A CG 1 ATOM 1438 C CD . PRO A 1 184 ? 17.601 -17.035 26.293 1.00 76.13 ? 184 PRO A CD 1 ATOM 1439 N N . ALA A 1 185 ? 16.889 -12.690 28.032 1.00 62.93 ? 185 ALA A N 1 ATOM 1440 C CA . ALA A 1 185 ? 17.656 -11.449 28.167 1.00 62.72 ? 185 ALA A CA 1 ATOM 1441 C C . ALA A 1 185 ? 18.105 -11.346 29.612 1.00 66.84 ? 185 ALA A C 1 ATOM 1442 O O . ALA A 1 185 ? 17.596 -12.063 30.441 1.00 68.07 ? 185 ALA A O 1 ATOM 1443 C CB . ALA A 1 185 ? 16.897 -10.250 27.752 1.00 49.35 ? 185 ALA A CB 1 ATOM 1444 N N . VAL A 1 186 ? 19.194 -10.604 29.830 1.00 77.63 ? 186 VAL A N 1 ATOM 1445 C CA . VAL A 1 186 ? 19.884 -10.394 31.115 1.00 71.63 ? 186 VAL A CA 1 ATOM 1446 C C . VAL A 1 186 ? 20.423 -8.969 31.210 1.00 71.39 ? 186 VAL A C 1 ATOM 1447 O O . VAL A 1 186 ? 20.850 -8.404 30.213 1.00 86.40 ? 186 VAL A O 1 ATOM 1448 C CB . VAL A 1 186 ? 21.008 -11.357 31.315 1.00 66.09 ? 186 VAL A CB 1 ATOM 1449 C CG1 . VAL A 1 186 ? 21.785 -10.950 32.498 1.00 69.51 ? 186 VAL A CG1 1 ATOM 1450 C CG2 . VAL A 1 186 ? 20.454 -12.760 31.524 1.00 75.68 ? 186 VAL A CG2 1 ATOM 1451 N N . LYS A 1 187 ? 20.336 -8.336 32.369 1.00 64.19 ? 187 LYS A N 1 ATOM 1452 C CA . LYS A 1 187 ? 20.802 -6.963 32.402 1.00 62.67 ? 187 LYS A CA 1 ATOM 1453 C C . LYS A 1 187 ? 22.014 -6.827 33.303 1.00 75.42 ? 187 LYS A C 1 ATOM 1454 O O . LYS A 1 187 ? 21.957 -7.171 34.486 1.00 99.43 ? 187 LYS A O 1 ATOM 1455 C CB . LYS A 1 187 ? 19.693 -6.027 32.855 1.00 56.39 ? 187 LYS A CB 1 ATOM 1456 C CG . LYS A 1 187 ? 20.159 -4.596 32.904 1.00 62.99 ? 187 LYS A CG 1 ATOM 1457 C CD . LYS A 1 187 ? 19.109 -3.651 33.497 1.00 70.60 ? 187 LYS A CD 1 ATOM 1458 C CE . LYS A 1 187 ? 19.679 -2.216 33.523 1.00 73.18 ? 187 LYS A CE 1 ATOM 1459 N NZ . LYS A 1 187 ? 18.825 -1.206 34.223 1.00 78.44 ? 187 LYS A NZ 1 ATOM 1460 N N . ASN A 1 188 ? 23.120 -6.331 32.768 1.00 63.78 ? 188 ASN A N 1 ATOM 1461 C CA . ASN A 1 188 ? 24.306 -6.199 33.590 1.00 60.83 ? 188 ASN A CA 1 ATOM 1462 C C . ASN A 1 188 ? 24.862 -4.781 33.575 1.00 67.81 ? 188 ASN A C 1 ATOM 1463 O O . ASN A 1 188 ? 24.445 -3.923 32.780 1.00 81.38 ? 188 ASN A O 1 ATOM 1464 C CB . ASN A 1 188 ? 25.347 -7.230 33.156 1.00 66.80 ? 188 ASN A CB 1 ATOM 1465 C CG . ASN A 1 188 ? 24.858 -8.667 33.363 1.00 81.69 ? 188 ASN A CG 1 ATOM 1466 O OD1 . ASN A 1 188 ? 23.941 -8.900 34.138 1.00 88.37 ? 188 ASN A OD1 1 ATOM 1467 N ND2 . ASN A 1 188 ? 25.484 -9.630 32.699 1.00 72.87 ? 188 ASN A ND2 1 ATOM 1468 N N . VAL A 1 189 ? 25.785 -4.527 34.484 1.00 67.92 ? 189 VAL A N 1 ATOM 1469 C CA . VAL A 1 189 ? 26.539 -3.291 34.431 1.00 73.90 ? 189 VAL A CA 1 ATOM 1470 C C . VAL A 1 189 ? 27.948 -3.665 34.190 1.00 70.37 ? 189 VAL A C 1 ATOM 1471 O O . VAL A 1 189 ? 28.350 -4.770 34.595 1.00 61.48 ? 189 VAL A O 1 ATOM 1472 C CB . VAL A 1 189 ? 26.466 -2.470 35.717 1.00 66.99 ? 189 VAL A CB 1 ATOM 1473 C CG1 . VAL A 1 189 ? 25.141 -1.761 35.804 1.00 73.81 ? 189 VAL A CG1 1 ATOM 1474 C CG2 . VAL A 1 189 ? 26.791 -3.347 36.911 1.00 56.08 ? 189 VAL A CG2 1 ATOM 1475 N N . ILE A 1 190 ? 28.647 -2.786 33.462 1.00 71.32 ? 190 ILE A N 1 ATOM 1476 C CA . ILE A 1 190 ? 30.074 -2.924 33.237 1.00 74.79 ? 190 ILE A CA 1 ATOM 1477 C C . ILE A 1 190 ? 30.768 -1.693 33.800 1.00 78.34 ? 190 ILE A C 1 ATOM 1478 O O . ILE A 1 190 ? 30.442 -0.530 33.503 1.00 70.92 ? 190 ILE A O 1 ATOM 1479 C CB . ILE A 1 190 ? 30.453 -3.058 31.764 1.00 89.79 ? 190 ILE A CB 1 ATOM 1480 C CG1 . ILE A 1 190 ? 29.385 -3.815 30.958 1.00 97.72 ? 190 ILE A CG1 1 ATOM 1481 C CG2 . ILE A 1 190 ? 31.835 -3.702 31.664 1.00 88.46 ? 190 ILE A CG2 1 ATOM 1482 C CD1 . ILE A 1 190 ? 29.361 -5.323 31.233 1.00 103.40 ? 190 ILE A CD1 1 ATOM 1483 N N . SER A 1 191 ? 31.775 -1.997 34.591 1.00 83.01 ? 191 SER A N 1 ATOM 1484 C CA . SER A 1 191 ? 32.493 -1.055 35.425 1.00 80.42 ? 191 SER A CA 1 ATOM 1485 C C . SER A 1 191 ? 33.421 -0.079 34.683 1.00 96.78 ? 191 SER A C 1 ATOM 1486 O O . SER A 1 191 ? 33.252 1.138 34.824 1.00 103.82 ? 191 SER A O 1 ATOM 1487 C CB . SER A 1 191 ? 33.208 -1.896 36.433 1.00 68.81 ? 191 SER A CB 1 ATOM 1488 O OG . SER A 1 191 ? 33.088 -3.241 35.943 1.00 65.36 ? 191 SER A OG 1 ATOM 1489 N N . TYR A 1 192 ? 34.411 -0.599 33.947 1.00 95.50 ? 192 TYR A N 1 ATOM 1490 C CA . TYR A 1 192 ? 35.332 0.224 33.118 1.00 98.43 ? 192 TYR A CA 1 ATOM 1491 C C . TYR A 1 192 ? 36.219 1.189 33.883 1.00 96.05 ? 192 TYR A C 1 ATOM 1492 O O . TYR A 1 192 ? 35.804 2.301 34.233 1.00 78.19 ? 192 TYR A O 1 ATOM 1493 C CB . TYR A 1 192 ? 34.555 1.034 32.030 1.00 112.39 ? 192 TYR A CB 1 ATOM 1494 C CG . TYR A 1 192 ? 34.065 0.218 30.839 1.00 89.64 ? 192 TYR A CG 1 ATOM 1495 C CD1 . TYR A 1 192 ? 34.968 -0.354 29.976 1.00 94.81 ? 192 TYR A CD1 1 ATOM 1496 C CD2 . TYR A 1 192 ? 32.724 -0.015 30.618 1.00 68.13 ? 192 TYR A CD2 1 ATOM 1497 C CE1 . TYR A 1 192 ? 34.562 -1.108 28.923 1.00 96.92 ? 192 TYR A CE1 1 ATOM 1498 C CE2 . TYR A 1 192 ? 32.322 -0.771 29.580 1.00 76.39 ? 192 TYR A CE2 1 ATOM 1499 C CZ . TYR A 1 192 ? 33.239 -1.321 28.729 1.00 97.42 ? 192 TYR A CZ 1 ATOM 1500 O OH . TYR A 1 192 ? 32.857 -2.082 27.644 1.00 108.78 ? 192 TYR A OH 1 ATOM 1501 N N . GLY A 1 193 ? 37.488 0.823 34.003 1.00 103.49 ? 193 GLY A N 1 ATOM 1502 C CA . GLY A 1 193 ? 38.391 1.523 34.900 1.00 105.16 ? 193 GLY A CA 1 ATOM 1503 C C . GLY A 1 193 ? 38.603 2.987 34.582 1.00 96.63 ? 193 GLY A C 1 ATOM 1504 O O . GLY A 1 193 ? 39.302 3.685 35.318 1.00 97.86 ? 193 GLY A O 1 ATOM 1505 N N . CYS A 1 194 ? 37.992 3.470 33.508 1.00 92.13 ? 194 CYS A N 1 ATOM 1506 C CA . CYS A 1 194 ? 38.299 4.821 33.059 1.00 115.93 ? 194 CYS A CA 1 ATOM 1507 C C . CYS A 1 194 ? 37.734 5.779 34.087 1.00 112.14 ? 194 CYS A C 1 ATOM 1508 O O . CYS A 1 194 ? 38.374 6.751 34.486 1.00 123.90 ? 194 CYS A O 1 ATOM 1509 C CB . CYS A 1 194 ? 37.673 5.108 31.685 1.00 119.02 ? 194 CYS A CB 1 ATOM 1510 S SG . CYS A 1 194 ? 35.896 4.877 31.716 1.00 136.43 ? 194 CYS A SG 1 ATOM 1511 N N . CYS A 1 195 ? 36.524 5.451 34.518 1.00 94.69 ? 195 CYS A N 1 ATOM 1512 C CA . CYS A 1 195 ? 35.717 6.287 35.397 1.00 113.08 ? 195 CYS A CA 1 ATOM 1513 C C . CYS A 1 195 ? 34.437 5.454 35.609 1.00 121.94 ? 195 CYS A C 1 ATOM 1514 O O . CYS A 1 195 ? 34.583 4.300 36.019 1.00 116.21 ? 195 CYS A O 1 ATOM 1515 C CB . CYS A 1 195 ? 35.560 7.666 34.771 1.00 99.81 ? 195 CYS A CB 1 ATOM 1516 S SG . CYS A 1 195 ? 34.944 7.741 33.039 1.00 148.05 ? 195 CYS A SG 1 ATOM 1517 N N . SER A 1 196 ? 33.197 5.918 35.416 1.00 158.95 ? 196 SER A N 1 ATOM 1518 C CA . SER A 1 196 ? 32.440 7.060 35.957 1.00 170.26 ? 196 SER A CA 1 ATOM 1519 C C . SER A 1 196 ? 31.086 6.416 35.987 1.00 178.26 ? 196 SER A C 1 ATOM 1520 O O . SER A 1 196 ? 30.377 6.481 34.986 1.00 187.01 ? 196 SER A O 1 ATOM 1521 C CB . SER A 1 196 ? 32.342 8.340 35.099 1.00 169.02 ? 196 SER A CB 1 ATOM 1522 O OG . SER A 1 196 ? 33.341 9.311 35.338 1.00 171.36 ? 196 SER A OG 1 ATOM 1523 N N . GLU A 1 197 ? 30.751 5.715 37.065 1.00 149.28 ? 197 GLU A N 1 ATOM 1524 C CA . GLU A 1 197 ? 29.467 5.020 37.180 1.00 113.15 ? 197 GLU A CA 1 ATOM 1525 C C . GLU A 1 197 ? 29.519 3.772 36.273 1.00 99.72 ? 197 GLU A C 1 ATOM 1526 O O . GLU A 1 197 ? 30.390 3.663 35.404 1.00 99.21 ? 197 GLU A O 1 ATOM 1527 C CB . GLU A 1 197 ? 28.288 5.936 36.800 1.00 93.08 ? 197 GLU A CB 1 ATOM 1528 C CG . GLU A 1 197 ? 28.416 7.485 37.076 1.00 147.34 ? 197 GLU A CG 1 ATOM 1529 C CD . GLU A 1 197 ? 29.274 7.926 38.284 1.00 155.70 ? 197 GLU A CD 1 ATOM 1530 O OE1 . GLU A 1 197 ? 29.485 7.158 39.256 1.00 163.07 ? 197 GLU A OE1 1 ATOM 1531 O OE2 . GLU A 1 197 ? 29.806 9.063 38.213 1.00 153.33 ? 197 GLU A OE2 1 ATOM 1532 N N . PRO A 1 198 ? 28.615 2.806 36.467 1.00 91.57 ? 198 PRO A N 1 ATOM 1533 C CA . PRO A 1 198 ? 28.662 1.687 35.518 1.00 91.94 ? 198 PRO A CA 1 ATOM 1534 C C . PRO A 1 198 ? 27.897 1.899 34.216 1.00 101.18 ? 198 PRO A C 1 ATOM 1535 O O . PRO A 1 198 ? 27.137 2.863 34.015 1.00 101.34 ? 198 PRO A O 1 ATOM 1536 C CB . PRO A 1 198 ? 28.053 0.524 36.309 1.00 92.06 ? 198 PRO A CB 1 ATOM 1537 C CG . PRO A 1 198 ? 27.169 1.136 37.276 1.00 99.79 ? 198 PRO A CG 1 ATOM 1538 C CD . PRO A 1 198 ? 27.725 2.519 37.602 1.00 102.20 ? 198 PRO A CD 1 ATOM 1539 N N . TYR A 1 199 ? 28.161 0.988 33.288 1.00 100.57 ? 199 TYR A N 1 ATOM 1540 C CA . TYR A 1 199 ? 27.583 1.062 31.953 1.00 70.31 ? 199 TYR A CA 1 ATOM 1541 C C . TYR A 1 199 ? 26.619 -0.105 31.857 1.00 66.05 ? 199 TYR A C 1 ATOM 1542 O O . TYR A 1 199 ? 27.025 -1.281 31.905 1.00 67.15 ? 199 TYR A O 1 ATOM 1543 C CB . TYR A 1 199 ? 28.679 1.008 30.892 1.00 59.78 ? 199 TYR A CB 1 ATOM 1544 C CG . TYR A 1 199 ? 29.380 2.345 30.700 1.00 66.25 ? 199 TYR A CG 1 ATOM 1545 C CD1 . TYR A 1 199 ? 28.663 3.463 30.313 1.00 74.41 ? 199 TYR A CD1 1 ATOM 1546 C CD2 . TYR A 1 199 ? 30.764 2.493 30.906 1.00 67.62 ? 199 TYR A CD2 1 ATOM 1547 C CE1 . TYR A 1 199 ? 29.277 4.688 30.132 1.00 71.60 ? 199 TYR A CE1 1 ATOM 1548 C CE2 . TYR A 1 199 ? 31.394 3.723 30.711 1.00 67.14 ? 199 TYR A CE2 1 ATOM 1549 C CZ . TYR A 1 199 ? 30.630 4.826 30.332 1.00 74.05 ? 199 TYR A CZ 1 ATOM 1550 O OH . TYR A 1 199 ? 31.171 6.084 30.117 1.00 76.03 ? 199 TYR A OH 1 ATOM 1551 N N . PRO A 1 200 ? 25.329 0.211 31.785 1.00 69.50 ? 200 PRO A N 1 ATOM 1552 C CA . PRO A 1 200 ? 24.241 -0.771 31.718 1.00 61.23 ? 200 PRO A CA 1 ATOM 1553 C C . PRO A 1 200 ? 24.281 -1.438 30.377 1.00 73.57 ? 200 PRO A C 1 ATOM 1554 O O . PRO A 1 200 ? 24.618 -0.769 29.366 1.00 69.80 ? 200 PRO A O 1 ATOM 1555 C CB . PRO A 1 200 ? 22.992 0.079 31.854 1.00 55.66 ? 200 PRO A CB 1 ATOM 1556 C CG . PRO A 1 200 ? 23.393 1.392 31.214 1.00 71.21 ? 200 PRO A CG 1 ATOM 1557 C CD . PRO A 1 200 ? 24.838 1.592 31.658 1.00 74.38 ? 200 PRO A CD 1 ATOM 1558 N N . ASP A 1 201 ? 23.990 -2.733 30.349 1.00 73.14 ? 201 ASP A N 1 ATOM 1559 C CA . ASP A 1 201 ? 23.989 -3.403 29.064 1.00 75.56 ? 201 ASP A CA 1 ATOM 1560 C C . ASP A 1 201 ? 23.068 -4.606 29.103 1.00 77.98 ? 201 ASP A C 1 ATOM 1561 O O . ASP A 1 201 ? 23.176 -5.436 30.032 1.00 67.72 ? 201 ASP A O 1 ATOM 1562 C CB . ASP A 1 201 ? 25.417 -3.826 28.662 1.00 66.00 ? 201 ASP A CB 1 ATOM 1563 C CG . ASP A 1 201 ? 25.895 -5.025 29.396 1.00 83.85 ? 201 ASP A CG 1 ATOM 1564 O OD1 . ASP A 1 201 ? 26.368 -4.896 30.538 1.00 105.17 ? 201 ASP A OD1 1 ATOM 1565 O OD2 . ASP A 1 201 ? 25.764 -6.116 28.830 1.00 87.04 ? 201 ASP A OD2 1 ATOM 1566 N N . VAL A 1 202 ? 22.253 -4.779 28.051 1.00 70.00 ? 202 VAL A N 1 ATOM 1567 C CA . VAL A 1 202 ? 21.420 -5.988 27.995 1.00 74.68 ? 202 VAL A CA 1 ATOM 1568 C C . VAL A 1 202 ? 22.034 -6.951 27.021 1.00 61.10 ? 202 VAL A C 1 ATOM 1569 O O . VAL A 1 202 ? 22.683 -6.532 26.048 1.00 46.22 ? 202 VAL A O 1 ATOM 1570 C CB . VAL A 1 202 ? 19.929 -5.755 27.541 1.00 86.01 ? 202 VAL A CB 1 ATOM 1571 C CG1 . VAL A 1 202 ? 19.247 -4.733 28.382 1.00 85.64 ? 202 VAL A CG1 1 ATOM 1572 C CG2 . VAL A 1 202 ? 19.854 -5.347 26.100 1.00 96.38 ? 202 VAL A CG2 1 ATOM 1573 N N . THR A 1 203 ? 21.854 -8.228 27.333 1.00 47.86 ? 203 THR A N 1 ATOM 1574 C CA . THR A 1 203 ? 22.386 -9.317 26.568 1.00 46.20 ? 203 THR A CA 1 ATOM 1575 C C . THR A 1 203 ? 21.334 -10.315 26.181 1.00 66.14 ? 203 THR A C 1 ATOM 1576 O O . THR A 1 203 ? 20.872 -11.141 26.966 1.00 60.42 ? 203 THR A O 1 ATOM 1577 C CB . THR A 1 203 ? 23.485 -10.017 27.309 1.00 63.10 ? 203 THR A CB 1 ATOM 1578 O OG1 . THR A 1 203 ? 24.674 -9.241 27.133 1.00 87.67 ? 203 THR A OG1 1 ATOM 1579 C CG2 . THR A 1 203 ? 23.751 -11.398 26.718 1.00 61.63 ? 203 THR A CG2 1 ATOM 1580 N N . PHE A 1 204 ? 20.946 -10.219 24.928 1.00 71.03 ? 204 PHE A N 1 ATOM 1581 C CA . PHE A 1 204 ? 20.159 -11.267 24.347 1.00 69.72 ? 204 PHE A CA 1 ATOM 1582 C C . PHE A 1 204 ? 21.069 -12.439 23.999 1.00 62.22 ? 204 PHE A C 1 ATOM 1583 O O . PHE A 1 204 ? 22.093 -12.265 23.338 1.00 66.60 ? 204 PHE A O 1 ATOM 1584 C CB . PHE A 1 204 ? 19.415 -10.736 23.140 1.00 74.80 ? 204 PHE A CB 1 ATOM 1585 C CG . PHE A 1 204 ? 18.517 -9.593 23.465 1.00 75.17 ? 204 PHE A CG 1 ATOM 1586 C CD1 . PHE A 1 204 ? 17.198 -9.827 23.863 1.00 72.72 ? 204 PHE A CD1 1 ATOM 1587 C CD2 . PHE A 1 204 ? 18.988 -8.294 23.405 1.00 70.36 ? 204 PHE A CD2 1 ATOM 1588 C CE1 . PHE A 1 204 ? 16.363 -8.789 24.185 1.00 75.54 ? 204 PHE A CE1 1 ATOM 1589 C CE2 . PHE A 1 204 ? 18.154 -7.242 23.712 1.00 75.47 ? 204 PHE A CE2 1 ATOM 1590 C CZ . PHE A 1 204 ? 16.836 -7.490 24.109 1.00 77.26 ? 204 PHE A CZ 1 ATOM 1591 N N . THR A 1 205 ? 20.695 -13.617 24.469 1.00 47.91 ? 205 THR A N 1 ATOM 1592 C CA . THR A 1 205 ? 21.537 -14.800 24.414 1.00 62.71 ? 205 THR A CA 1 ATOM 1593 C C . THR A 1 205 ? 20.883 -15.892 23.615 1.00 72.17 ? 205 THR A C 1 ATOM 1594 O O . THR A 1 205 ? 19.886 -16.455 24.043 1.00 85.38 ? 205 THR A O 1 ATOM 1595 C CB . THR A 1 205 ? 21.810 -15.293 25.828 1.00 76.47 ? 205 THR A CB 1 ATOM 1596 O OG1 . THR A 1 205 ? 22.644 -14.330 26.471 1.00 81.59 ? 205 THR A OG1 1 ATOM 1597 C CG2 . THR A 1 205 ? 22.442 -16.685 25.850 1.00 48.33 ? 205 THR A CG2 1 ATOM 1598 N N . LEU A 1 206 ? 21.443 -16.219 22.462 1.00 70.96 ? 206 LEU A N 1 ATOM 1599 C CA . LEU A 1 206 ? 20.708 -17.056 21.529 1.00 79.16 ? 206 LEU A CA 1 ATOM 1600 C C . LEU A 1 206 ? 21.276 -18.461 21.525 1.00 77.72 ? 206 LEU A C 1 ATOM 1601 O O . LEU A 1 206 ? 22.487 -18.650 21.376 1.00 79.01 ? 206 LEU A O 1 ATOM 1602 C CB . LEU A 1 206 ? 20.744 -16.398 20.146 1.00 81.73 ? 206 LEU A CB 1 ATOM 1603 C CG . LEU A 1 206 ? 19.811 -16.740 18.983 1.00 85.76 ? 206 LEU A CG 1 ATOM 1604 C CD1 . LEU A 1 206 ? 18.368 -16.924 19.396 1.00 92.76 ? 206 LEU A CD1 1 ATOM 1605 C CD2 . LEU A 1 206 ? 19.859 -15.552 18.064 1.00 79.59 ? 206 LEU A CD2 1 ATOM 1606 N N . LEU A 1 207 ? 20.408 -19.450 21.693 1.00 75.84 ? 207 LEU A N 1 ATOM 1607 C CA . LEU A 1 207 ? 20.876 -20.820 21.747 1.00 95.68 ? 207 LEU A CA 1 ATOM 1608 C C . LEU A 1 207 ? 20.199 -21.658 20.693 1.00 107.44 ? 207 LEU A C 1 ATOM 1609 O O . LEU A 1 207 ? 18.980 -21.796 20.702 1.00 120.57 ? 207 LEU A O 1 ATOM 1610 C CB . LEU A 1 207 ? 20.588 -21.444 23.101 1.00 105.58 ? 207 LEU A CB 1 ATOM 1611 C CG . LEU A 1 207 ? 21.549 -21.279 24.269 1.00 115.58 ? 207 LEU A CG 1 ATOM 1612 C CD1 . LEU A 1 207 ? 21.641 -19.817 24.671 1.00 112.10 ? 207 LEU A CD1 1 ATOM 1613 C CD2 . LEU A 1 207 ? 21.052 -22.138 25.434 1.00 125.19 ? 207 LEU A CD2 1 ATOM 1614 N N . LEU A 1 208 ? 20.999 -22.272 19.829 1.00 100.30 ? 208 LEU A N 1 ATOM 1615 C CA . LEU A 1 208 ? 20.483 -22.983 18.669 1.00 101.42 ? 208 LEU A CA 1 ATOM 1616 C C . LEU A 1 208 ? 20.859 -24.477 18.779 1.00 105.33 ? 208 LEU A C 1 ATOM 1617 O O . LEU A 1 208 ? 21.759 -24.802 19.535 1.00 108.31 ? 208 LEU A O 1 ATOM 1618 C CB . LEU A 1 208 ? 21.069 -22.349 17.389 1.00 94.71 ? 208 LEU A CB 1 ATOM 1619 C CG . LEU A 1 208 ? 21.298 -20.819 17.404 1.00 86.24 ? 208 LEU A CG 1 ATOM 1620 C CD1 . LEU A 1 208 ? 21.946 -20.352 16.158 1.00 66.32 ? 208 LEU A CD1 1 ATOM 1621 C CD2 . LEU A 1 208 ? 19.985 -20.049 17.588 1.00 92.56 ? 208 LEU A CD2 1 ATOM 1622 N N . LYS A 1 209 ? 20.233 -25.376 18.003 1.00 96.78 ? 209 LYS A N 1 ATOM 1623 C CA . LYS A 1 209 ? 20.845 -26.701 17.700 1.00 105.00 ? 209 LYS A CA 1 ATOM 1624 C C . LYS A 1 209 ? 20.554 -27.157 16.188 1.00 114.24 ? 209 LYS A C 1 ATOM 1625 O O . LYS A 1 209 ? 20.183 -26.328 15.400 1.00 115.44 ? 209 LYS A O 1 ATOM 1626 C CB . LYS A 1 209 ? 20.363 -27.707 18.786 1.00 126.11 ? 209 LYS A CB 1 ATOM 1627 C CG . LYS A 1 209 ? 20.345 -29.166 18.424 1.00 135.57 ? 209 LYS A CG 1 ATOM 1628 C CD . LYS A 1 209 ? 21.752 -29.628 17.990 1.00 150.12 ? 209 LYS A CD 1 ATOM 1629 C CE . LYS A 1 209 ? 21.737 -31.083 17.585 1.00 158.74 ? 209 LYS A CE 1 ATOM 1630 N NZ . LYS A 1 209 ? 22.775 -31.492 16.587 1.00 162.80 ? 209 LYS A NZ 1 ATOM 1631 N N . ARG A 1 210 ? 20.790 -28.409 15.769 1.00 116.48 ? 210 ARG A N 1 ATOM 1632 C CA . ARG A 1 210 ? 20.415 -28.929 14.466 1.00 124.81 ? 210 ARG A CA 1 ATOM 1633 C C . ARG A 1 210 ? 20.224 -30.503 14.235 1.00 152.48 ? 210 ARG A C 1 ATOM 1634 O O . ARG A 1 210 ? 21.014 -31.337 14.515 1.00 148.29 ? 210 ARG A O 1 ATOM 1635 C CB . ARG A 1 210 ? 21.408 -28.305 13.478 1.00 133.04 ? 210 ARG A CB 1 ATOM 1636 C CG . ARG A 1 210 ? 21.358 -28.749 11.995 1.00 146.47 ? 210 ARG A CG 1 ATOM 1637 C CD . ARG A 1 210 ? 19.966 -29.170 11.619 1.00 156.81 ? 210 ARG A CD 1 ATOM 1638 N NE . ARG A 1 210 ? 18.858 -28.217 11.681 1.00 169.14 ? 210 ARG A NE 1 ATOM 1639 C CZ . ARG A 1 210 ? 17.789 -28.149 12.499 1.00 176.56 ? 210 ARG A CZ 1 ATOM 1640 N NH1 . ARG A 1 210 ? 17.676 -28.736 13.670 1.00 178.21 ? 210 ARG A NH1 1 ATOM 1641 N NH2 . ARG A 1 210 ? 16.849 -27.303 12.221 1.00 175.42 ? 210 ARG A NH2 1 ATOM 1642 N N . ARG A 1 211 ? 19.088 -30.780 13.600 1.00 144.80 ? 211 ARG A N 1 ATOM 1643 C CA . ARG A 1 211 ? 18.504 -32.018 13.024 1.00 154.79 ? 211 ARG A CA 1 ATOM 1644 C C . ARG A 1 211 ? 19.473 -32.670 12.045 1.00 160.47 ? 211 ARG A C 1 ATOM 1645 O O . ARG A 1 211 ? 20.009 -32.033 11.143 1.00 164.59 ? 211 ARG A O 1 ATOM 1646 C CB . ARG A 1 211 ? 17.086 -31.750 12.310 1.00 151.87 ? 211 ARG A CB 1 ATOM 1647 C CG . ARG A 1 211 ? 16.896 -30.691 11.124 1.00 172.81 ? 211 ARG A CG 1 ATOM 1648 C CD . ARG A 1 211 ? 15.389 -30.264 10.695 1.00 177.90 ? 211 ARG A CD 1 ATOM 1649 N NE . ARG A 1 211 ? 14.608 -29.742 11.831 1.00 169.65 ? 211 ARG A NE 1 ATOM 1650 C CZ . ARG A 1 211 ? 14.195 -28.485 12.027 1.00 155.10 ? 211 ARG A CZ 1 ATOM 1651 N NH1 . ARG A 1 211 ? 14.338 -27.559 11.080 1.00 149.43 ? 211 ARG A NH1 1 ATOM 1652 N NH2 . ARG A 1 211 ? 13.555 -28.180 13.164 1.00 151.74 ? 211 ARG A NH2 1 ATOM 1653 N N . SER A 1 212 ? 19.709 -33.952 12.291 1.00 163.60 ? 212 SER A N 1 ATOM 1654 C CA . SER A 1 212 ? 20.620 -34.801 11.526 1.00 157.12 ? 212 SER A CA 1 ATOM 1655 C C . SER A 1 212 ? 19.915 -36.158 11.402 1.00 147.60 ? 212 SER A C 1 ATOM 1656 O O . SER A 1 212 ? 19.916 -36.805 10.344 1.00 143.92 ? 212 SER A O 1 ATOM 1657 C CB . SER A 1 212 ? 21.999 -34.971 12.219 1.00 148.64 ? 212 SER A CB 1 ATOM 1658 O OG . SER A 1 212 ? 22.465 -33.813 12.896 1.00 146.27 ? 212 SER A OG 1 ATOM 1659 N N . TYR B 1 5 ? 29.174 20.717 7.773 1.00 178.70 ? 5 TYR B N 1 ATOM 1660 C CA . TYR B 1 5 ? 29.317 19.840 6.620 1.00 181.56 ? 5 TYR B CA 1 ATOM 1661 C C . TYR B 1 5 ? 28.068 19.853 5.751 1.00 190.33 ? 5 TYR B C 1 ATOM 1662 O O . TYR B 1 5 ? 27.921 20.715 4.888 1.00 185.98 ? 5 TYR B O 1 ATOM 1663 C CB . TYR B 1 5 ? 29.626 18.403 7.059 1.00 176.67 ? 5 TYR B CB 1 ATOM 1664 C CG . TYR B 1 5 ? 28.960 17.936 8.350 1.00 175.14 ? 5 TYR B CG 1 ATOM 1665 C CD1 . TYR B 1 5 ? 29.580 18.119 9.580 1.00 174.30 ? 5 TYR B CD1 1 ATOM 1666 C CD2 . TYR B 1 5 ? 27.733 17.264 8.332 1.00 174.97 ? 5 TYR B CD2 1 ATOM 1667 C CE1 . TYR B 1 5 ? 28.984 17.674 10.757 1.00 173.60 ? 5 TYR B CE1 1 ATOM 1668 C CE2 . TYR B 1 5 ? 27.128 16.825 9.495 1.00 177.35 ? 5 TYR B CE2 1 ATOM 1669 C CZ . TYR B 1 5 ? 27.756 17.027 10.708 1.00 175.69 ? 5 TYR B CZ 1 ATOM 1670 O OH . TYR B 1 5 ? 27.151 16.578 11.866 1.00 172.05 ? 5 TYR B OH 1 ATOM 1671 N N . ALA B 1 6 ? 27.141 18.948 6.077 1.00 199.57 ? 6 ALA B N 1 ATOM 1672 C CA . ALA B 1 6 ? 25.942 18.623 5.302 1.00 208.30 ? 6 ALA B CA 1 ATOM 1673 C C . ALA B 1 6 ? 25.037 19.813 5.165 1.00 204.00 ? 6 ALA B C 1 ATOM 1674 O O . ALA B 1 6 ? 24.029 19.730 4.457 1.00 201.80 ? 6 ALA B O 1 ATOM 1675 C CB . ALA B 1 6 ? 25.174 17.474 5.949 1.00 212.45 ? 6 ALA B CB 1 ATOM 1676 N N . GLN B 1 7 ? 25.384 20.888 5.877 1.00 203.29 ? 7 GLN B N 1 ATOM 1677 C CA . GLN B 1 7 ? 24.782 22.203 5.719 1.00 195.88 ? 7 GLN B CA 1 ATOM 1678 C C . GLN B 1 7 ? 23.287 22.060 5.411 1.00 181.17 ? 7 GLN B C 1 ATOM 1679 O O . GLN B 1 7 ? 22.586 21.273 6.030 1.00 182.58 ? 7 GLN B O 1 ATOM 1680 C CB . GLN B 1 7 ? 25.577 22.977 4.629 1.00 185.04 ? 7 GLN B CB 1 ATOM 1681 C CG . GLN B 1 7 ? 25.326 22.646 3.125 1.00 204.14 ? 7 GLN B CG 1 ATOM 1682 C CD . GLN B 1 7 ? 25.668 21.226 2.690 1.00 202.41 ? 7 GLN B CD 1 ATOM 1683 O OE1 . GLN B 1 7 ? 26.824 20.822 2.683 1.00 200.22 ? 7 GLN B OE1 1 ATOM 1684 N NE2 . GLN B 1 7 ? 24.643 20.448 2.360 1.00 201.63 ? 7 GLN B NE2 1 ATOM 1685 N N . LYS B 1 8 ? 22.788 22.810 4.458 1.00 174.77 ? 8 LYS B N 1 ATOM 1686 C CA . LYS B 1 8 ? 21.802 22.217 3.605 1.00 166.29 ? 8 LYS B CA 1 ATOM 1687 C C . LYS B 1 8 ? 22.046 22.695 2.156 1.00 164.25 ? 8 LYS B C 1 ATOM 1688 O O . LYS B 1 8 ? 21.987 23.878 1.884 1.00 168.26 ? 8 LYS B O 1 ATOM 1689 C CB . LYS B 1 8 ? 20.400 22.452 4.204 1.00 163.62 ? 8 LYS B CB 1 ATOM 1690 C CG . LYS B 1 8 ? 19.484 23.399 3.613 1.00 165.58 ? 8 LYS B CG 1 ATOM 1691 C CD . LYS B 1 8 ? 18.115 23.014 4.027 1.00 166.75 ? 8 LYS B CD 1 ATOM 1692 C CE . LYS B 1 8 ? 16.990 23.818 3.499 1.00 169.41 ? 8 LYS B CE 1 ATOM 1693 N NZ . LYS B 1 8 ? 15.865 22.869 3.244 1.00 166.75 ? 8 LYS B NZ 1 ATOM 1694 N N . LEU B 1 9 ? 22.549 21.771 1.320 1.00 151.71 ? 9 LEU B N 1 ATOM 1695 C CA . LEU B 1 9 ? 22.418 21.767 -0.142 1.00 139.13 ? 9 LEU B CA 1 ATOM 1696 C C . LEU B 1 9 ? 21.242 20.856 -0.377 1.00 145.33 ? 9 LEU B C 1 ATOM 1697 O O . LEU B 1 9 ? 20.971 20.422 -1.480 1.00 139.01 ? 9 LEU B O 1 ATOM 1698 C CB . LEU B 1 9 ? 23.665 21.295 -0.904 1.00 130.87 ? 9 LEU B CB 1 ATOM 1699 C CG . LEU B 1 9 ? 24.677 22.365 -1.393 1.00 136.85 ? 9 LEU B CG 1 ATOM 1700 C CD1 . LEU B 1 9 ? 25.574 21.796 -2.498 1.00 133.45 ? 9 LEU B CD1 1 ATOM 1701 C CD2 . LEU B 1 9 ? 24.072 23.717 -1.851 1.00 135.11 ? 9 LEU B CD2 1 ATOM 1702 N N . PHE B 1 10 ? 20.631 20.494 0.746 1.00 147.14 ? 10 PHE B N 1 ATOM 1703 C CA . PHE B 1 10 ? 19.195 20.253 0.922 1.00 161.61 ? 10 PHE B CA 1 ATOM 1704 C C . PHE B 1 10 ? 18.551 21.650 0.743 1.00 176.73 ? 10 PHE B C 1 ATOM 1705 O O . PHE B 1 10 ? 17.335 21.841 0.819 1.00 177.13 ? 10 PHE B O 1 ATOM 1706 C CB . PHE B 1 10 ? 18.989 19.548 2.305 1.00 136.67 ? 10 PHE B CB 1 ATOM 1707 C CG . PHE B 1 10 ? 17.555 19.445 2.835 1.00 134.31 ? 10 PHE B CG 1 ATOM 1708 C CD1 . PHE B 1 10 ? 16.580 18.818 2.136 1.00 137.23 ? 10 PHE B CD1 1 ATOM 1709 C CD2 . PHE B 1 10 ? 17.254 19.818 4.158 1.00 134.72 ? 10 PHE B CD2 1 ATOM 1710 C CE1 . PHE B 1 10 ? 15.314 18.699 2.660 1.00 133.61 ? 10 PHE B CE1 1 ATOM 1711 C CE2 . PHE B 1 10 ? 16.000 19.665 4.693 1.00 134.83 ? 10 PHE B CE2 1 ATOM 1712 C CZ . PHE B 1 10 ? 15.027 19.100 3.941 1.00 132.28 ? 10 PHE B CZ 1 ATOM 1713 N N . ASN B 1 11 ? 19.444 22.602 0.464 1.00 189.43 ? 11 ASN B N 1 ATOM 1714 C CA . ASN B 1 11 ? 19.286 24.047 0.463 1.00 204.61 ? 11 ASN B CA 1 ATOM 1715 C C . ASN B 1 11 ? 17.947 24.592 0.052 1.00 214.48 ? 11 ASN B C 1 ATOM 1716 O O . ASN B 1 11 ? 16.996 24.671 0.824 1.00 217.55 ? 11 ASN B O 1 ATOM 1717 C CB . ASN B 1 11 ? 20.369 24.649 -0.455 1.00 201.05 ? 11 ASN B CB 1 ATOM 1718 C CG . ASN B 1 11 ? 20.416 24.008 -1.824 1.00 188.44 ? 11 ASN B CG 1 ATOM 1719 O OD1 . ASN B 1 11 ? 19.925 22.901 -2.038 1.00 183.18 ? 11 ASN B OD1 1 ATOM 1720 N ND2 . ASN B 1 11 ? 20.928 24.757 -2.783 1.00 189.59 ? 11 ASN B ND2 1 ATOM 1721 N N . ASP B 1 12 ? 17.868 24.947 -1.202 1.00 222.89 ? 12 ASP B N 1 ATOM 1722 C CA . ASP B 1 12 ? 16.598 25.248 -1.744 1.00 224.75 ? 12 ASP B CA 1 ATOM 1723 C C . ASP B 1 12 ? 16.628 24.550 -3.075 1.00 215.44 ? 12 ASP B C 1 ATOM 1724 O O . ASP B 1 12 ? 16.319 25.081 -4.149 1.00 227.85 ? 12 ASP B O 1 ATOM 1725 C CB . ASP B 1 12 ? 16.382 26.750 -1.753 1.00 234.79 ? 12 ASP B CB 1 ATOM 1726 C CG . ASP B 1 12 ? 15.892 27.255 -0.390 1.00 241.42 ? 12 ASP B CG 1 ATOM 1727 O OD1 . ASP B 1 12 ? 15.155 26.501 0.284 1.00 240.91 ? 12 ASP B OD1 1 ATOM 1728 O OD2 . ASP B 1 12 ? 16.233 28.380 0.020 1.00 245.12 ? 12 ASP B OD2 1 ATOM 1729 N N . LEU B 1 13 ? 17.057 23.295 -2.920 1.00 190.16 ? 13 LEU B N 1 ATOM 1730 C CA . LEU B 1 13 ? 16.585 22.217 -3.741 1.00 163.89 ? 13 LEU B CA 1 ATOM 1731 C C . LEU B 1 13 ? 15.126 22.104 -3.334 1.00 154.22 ? 13 LEU B C 1 ATOM 1732 O O . LEU B 1 13 ? 14.328 21.526 -4.053 1.00 164.62 ? 13 LEU B O 1 ATOM 1733 C CB . LEU B 1 13 ? 17.329 20.893 -3.483 1.00 139.85 ? 13 LEU B CB 1 ATOM 1734 C CG . LEU B 1 13 ? 18.810 20.666 -3.790 1.00 125.08 ? 13 LEU B CG 1 ATOM 1735 C CD1 . LEU B 1 13 ? 19.222 19.231 -3.456 1.00 103.53 ? 13 LEU B CD1 1 ATOM 1736 C CD2 . LEU B 1 13 ? 19.096 20.978 -5.259 1.00 136.43 ? 13 LEU B CD2 1 ATOM 1737 N N . PHE B 1 14 ? 14.798 22.699 -2.183 1.00 146.56 ? 14 PHE B N 1 ATOM 1738 C CA . PHE B 1 14 ? 13.507 22.551 -1.530 1.00 131.00 ? 14 PHE B CA 1 ATOM 1739 C C . PHE B 1 14 ? 12.743 23.851 -1.218 1.00 137.24 ? 14 PHE B C 1 ATOM 1740 O O . PHE B 1 14 ? 11.726 23.809 -0.521 1.00 137.51 ? 14 PHE B O 1 ATOM 1741 C CB . PHE B 1 14 ? 13.726 21.741 -0.264 1.00 116.72 ? 14 PHE B CB 1 ATOM 1742 C CG . PHE B 1 14 ? 14.156 20.330 -0.535 1.00 116.07 ? 14 PHE B CG 1 ATOM 1743 C CD1 . PHE B 1 14 ? 15.489 20.034 -0.750 1.00 121.86 ? 14 PHE B CD1 1 ATOM 1744 C CD2 . PHE B 1 14 ? 13.219 19.320 -0.691 1.00 115.92 ? 14 PHE B CD2 1 ATOM 1745 C CE1 . PHE B 1 14 ? 15.894 18.739 -1.041 1.00 122.48 ? 14 PHE B CE1 1 ATOM 1746 C CE2 . PHE B 1 14 ? 13.615 18.017 -0.961 1.00 115.50 ? 14 PHE B CE2 1 ATOM 1747 C CZ . PHE B 1 14 ? 14.956 17.727 -1.142 1.00 117.72 ? 14 PHE B CZ 1 ATOM 1748 N N . GLU B 1 15 ? 13.192 24.990 -1.744 1.00 133.35 ? 15 GLU B N 1 ATOM 1749 C CA . GLU B 1 15 ? 12.355 26.195 -1.722 1.00 142.92 ? 15 GLU B CA 1 ATOM 1750 C C . GLU B 1 15 ? 11.400 26.102 -2.872 1.00 147.48 ? 15 GLU B C 1 ATOM 1751 O O . GLU B 1 15 ? 10.182 26.174 -2.708 1.00 144.79 ? 15 GLU B O 1 ATOM 1752 C CB . GLU B 1 15 ? 13.176 27.466 -1.876 1.00 150.90 ? 15 GLU B CB 1 ATOM 1753 C CG . GLU B 1 15 ? 12.422 28.786 -1.894 1.00 158.13 ? 15 GLU B CG 1 ATOM 1754 C CD . GLU B 1 15 ? 13.374 29.968 -2.045 1.00 162.48 ? 15 GLU B CD 1 ATOM 1755 O OE1 . GLU B 1 15 ? 14.519 29.864 -1.555 1.00 159.11 ? 15 GLU B OE1 1 ATOM 1756 O OE2 . GLU B 1 15 ? 12.991 30.985 -2.669 1.00 168.21 ? 15 GLU B OE2 1 ATOM 1757 N N . ASP B 1 16 ? 11.975 25.865 -4.042 1.00 150.12 ? 16 ASP B N 1 ATOM 1758 C CA . ASP B 1 16 ? 11.176 25.706 -5.229 1.00 154.16 ? 16 ASP B CA 1 ATOM 1759 C C . ASP B 1 16 ? 11.132 24.218 -5.518 1.00 146.81 ? 16 ASP B C 1 ATOM 1760 O O . ASP B 1 16 ? 11.605 23.720 -6.544 1.00 150.54 ? 16 ASP B O 1 ATOM 1761 C CB . ASP B 1 16 ? 11.770 26.510 -6.396 1.00 159.83 ? 16 ASP B CB 1 ATOM 1762 C CG . ASP B 1 16 ? 13.175 26.051 -6.772 1.00 162.86 ? 16 ASP B CG 1 ATOM 1763 O OD1 . ASP B 1 16 ? 14.141 26.401 -6.055 1.00 160.13 ? 16 ASP B OD1 1 ATOM 1764 O OD2 . ASP B 1 16 ? 13.316 25.357 -7.804 1.00 165.43 ? 16 ASP B OD2 1 ATOM 1765 N N . TYR B 1 17 ? 10.517 23.497 -4.593 1.00 140.86 ? 17 TYR B N 1 ATOM 1766 C CA . TYR B 1 17 ? 10.316 22.088 -4.819 1.00 136.93 ? 17 TYR B CA 1 ATOM 1767 C C . TYR B 1 17 ? 8.983 21.714 -4.211 1.00 135.68 ? 17 TYR B C 1 ATOM 1768 O O . TYR B 1 17 ? 8.620 22.187 -3.133 1.00 136.54 ? 17 TYR B O 1 ATOM 1769 C CB . TYR B 1 17 ? 11.451 21.256 -4.225 1.00 133.21 ? 17 TYR B CB 1 ATOM 1770 C CG . TYR B 1 17 ? 11.407 19.791 -4.619 1.00 130.88 ? 17 TYR B CG 1 ATOM 1771 C CD1 . TYR B 1 17 ? 10.669 18.865 -3.897 1.00 128.05 ? 17 TYR B CD1 1 ATOM 1772 C CD2 . TYR B 1 17 ? 12.104 19.343 -5.741 1.00 130.02 ? 17 TYR B CD2 1 ATOM 1773 C CE1 . TYR B 1 17 ? 10.629 17.530 -4.277 1.00 128.01 ? 17 TYR B CE1 1 ATOM 1774 C CE2 . TYR B 1 17 ? 12.069 18.018 -6.129 1.00 127.92 ? 17 TYR B CE2 1 ATOM 1775 C CZ . TYR B 1 17 ? 11.332 17.114 -5.394 1.00 129.12 ? 17 TYR B CZ 1 ATOM 1776 O OH . TYR B 1 17 ? 11.296 15.793 -5.783 1.00 128.46 ? 17 TYR B OH 1 ATOM 1777 N N . SER B 1 18 ? 8.247 20.868 -4.907 1.00 142.74 ? 18 SER B N 1 ATOM 1778 C CA . SER B 1 18 ? 7.149 20.191 -4.262 1.00 144.58 ? 18 SER B CA 1 ATOM 1779 C C . SER B 1 18 ? 7.133 18.793 -4.784 1.00 140.21 ? 18 SER B C 1 ATOM 1780 O O . SER B 1 18 ? 7.585 18.509 -5.892 1.00 138.78 ? 18 SER B O 1 ATOM 1781 C CB . SER B 1 18 ? 5.812 20.857 -4.535 1.00 151.56 ? 18 SER B CB 1 ATOM 1782 O OG . SER B 1 18 ? 5.308 20.409 -5.777 1.00 155.24 ? 18 SER B OG 1 ATOM 1783 N N . ASN B 1 19 ? 6.635 17.903 -3.956 1.00 135.35 ? 19 ASN B N 1 ATOM 1784 C CA . ASN B 1 19 ? 6.748 16.516 -4.285 1.00 128.88 ? 19 ASN B CA 1 ATOM 1785 C C . ASN B 1 19 ? 5.494 16.086 -5.051 1.00 121.69 ? 19 ASN B C 1 ATOM 1786 O O . ASN B 1 19 ? 5.202 14.902 -5.204 1.00 116.97 ? 19 ASN B O 1 ATOM 1787 C CB . ASN B 1 19 ? 7.047 15.678 -3.024 1.00 126.93 ? 19 ASN B CB 1 ATOM 1788 C CG . ASN B 1 19 ? 6.017 15.817 -1.921 1.00 127.09 ? 19 ASN B CG 1 ATOM 1789 O OD1 . ASN B 1 19 ? 4.842 16.087 -2.169 1.00 128.21 ? 19 ASN B OD1 1 ATOM 1790 N ND2 . ASN B 1 19 ? 6.451 15.562 -0.682 1.00 122.44 ? 19 ASN B ND2 1 ATOM 1791 N N . ALA B 1 20 ? 4.734 17.083 -5.495 1.00 115.11 ? 20 ALA B N 1 ATOM 1792 C CA . ALA B 1 20 ? 3.490 16.853 -6.217 1.00 121.91 ? 20 ALA B CA 1 ATOM 1793 C C . ALA B 1 20 ? 3.721 16.649 -7.729 1.00 135.22 ? 20 ALA B C 1 ATOM 1794 O O . ALA B 1 20 ? 3.172 15.718 -8.322 1.00 140.78 ? 20 ALA B O 1 ATOM 1795 C CB . ALA B 1 20 ? 2.522 17.995 -5.976 1.00 124.33 ? 20 ALA B CB 1 ATOM 1796 N N . LEU B 1 21 ? 4.512 17.516 -8.364 1.00 133.80 ? 21 LEU B N 1 ATOM 1797 C CA . LEU B 1 21 ? 4.666 17.421 -9.816 1.00 136.52 ? 21 LEU B CA 1 ATOM 1798 C C . LEU B 1 21 ? 5.980 16.749 -10.206 1.00 132.63 ? 21 LEU B C 1 ATOM 1799 O O . LEU B 1 21 ? 7.052 17.005 -9.658 1.00 127.26 ? 21 LEU B O 1 ATOM 1800 C CB . LEU B 1 21 ? 4.564 18.803 -10.475 1.00 142.39 ? 21 LEU B CB 1 ATOM 1801 C CG . LEU B 1 21 ? 5.140 19.067 -11.876 1.00 149.97 ? 21 LEU B CG 1 ATOM 1802 C CD1 . LEU B 1 21 ? 4.513 18.154 -12.936 1.00 147.83 ? 21 LEU B CD1 1 ATOM 1803 C CD2 . LEU B 1 21 ? 4.947 20.531 -12.268 1.00 152.89 ? 21 LEU B CD2 1 ATOM 1804 N N . ARG B 1 22 ? 5.838 15.893 -11.202 1.00 129.35 ? 22 ARG B N 1 ATOM 1805 C CA . ARG B 1 22 ? 6.845 14.988 -11.700 1.00 117.11 ? 22 ARG B CA 1 ATOM 1806 C C . ARG B 1 22 ? 8.089 15.729 -12.143 1.00 113.76 ? 22 ARG B C 1 ATOM 1807 O O . ARG B 1 22 ? 7.996 16.717 -12.875 1.00 125.65 ? 22 ARG B O 1 ATOM 1808 C CB . ARG B 1 22 ? 6.251 14.224 -12.865 1.00 112.86 ? 22 ARG B CB 1 ATOM 1809 C CG . ARG B 1 22 ? 5.019 13.426 -12.504 1.00 113.77 ? 22 ARG B CG 1 ATOM 1810 C CD . ARG B 1 22 ? 4.340 13.043 -13.777 1.00 123.29 ? 22 ARG B CD 1 ATOM 1811 N NE . ARG B 1 22 ? 5.323 12.494 -14.703 1.00 131.97 ? 22 ARG B NE 1 ATOM 1812 C CZ . ARG B 1 22 ? 5.376 12.776 -16.002 1.00 130.56 ? 22 ARG B CZ 1 ATOM 1813 N NH1 . ARG B 1 22 ? 4.489 13.600 -16.543 1.00 131.25 ? 22 ARG B NH1 1 ATOM 1814 N NH2 . ARG B 1 22 ? 6.317 12.228 -16.759 1.00 126.62 ? 22 ARG B NH2 1 ATOM 1815 N N . PRO B 1 23 ? 9.259 15.256 -11.706 1.00 100.03 ? 23 PRO B N 1 ATOM 1816 C CA . PRO B 1 23 ? 10.557 15.885 -11.970 1.00 100.40 ? 23 PRO B CA 1 ATOM 1817 C C . PRO B 1 23 ? 11.124 15.637 -13.373 1.00 95.39 ? 23 PRO B C 1 ATOM 1818 O O . PRO B 1 23 ? 12.278 15.219 -13.462 1.00 83.48 ? 23 PRO B O 1 ATOM 1819 C CB . PRO B 1 23 ? 11.463 15.234 -10.930 1.00 100.22 ? 23 PRO B CB 1 ATOM 1820 C CG . PRO B 1 23 ? 10.898 13.876 -10.794 1.00 98.30 ? 23 PRO B CG 1 ATOM 1821 C CD . PRO B 1 23 ? 9.399 14.042 -10.890 1.00 93.22 ? 23 PRO B CD 1 ATOM 1822 N N . VAL B 1 24 ? 10.352 15.873 -14.438 1.00 110.36 ? 24 VAL B N 1 ATOM 1823 C CA . VAL B 1 24 ? 10.955 15.864 -15.770 1.00 126.29 ? 24 VAL B CA 1 ATOM 1824 C C . VAL B 1 24 ? 10.988 17.295 -16.300 1.00 128.15 ? 24 VAL B C 1 ATOM 1825 O O . VAL B 1 24 ? 10.170 18.136 -15.899 1.00 123.07 ? 24 VAL B O 1 ATOM 1826 C CB . VAL B 1 24 ? 10.234 14.950 -16.794 1.00 93.81 ? 24 VAL B CB 1 ATOM 1827 C CG1 . VAL B 1 24 ? 11.300 14.252 -17.641 1.00 99.52 ? 24 VAL B CG1 1 ATOM 1828 C CG2 . VAL B 1 24 ? 9.303 13.927 -16.130 1.00 88.58 ? 24 VAL B CG2 1 ATOM 1829 N N . GLU B 1 25 ? 11.956 17.537 -17.194 1.00 136.10 ? 25 GLU B N 1 ATOM 1830 C CA . GLU B 1 25 ? 12.302 18.853 -17.752 1.00 145.03 ? 25 GLU B CA 1 ATOM 1831 C C . GLU B 1 25 ? 11.092 19.525 -18.431 1.00 155.23 ? 25 GLU B C 1 ATOM 1832 O O . GLU B 1 25 ? 10.960 20.740 -18.380 1.00 152.79 ? 25 GLU B O 1 ATOM 1833 C CB . GLU B 1 25 ? 13.541 18.731 -18.663 1.00 147.73 ? 25 GLU B CB 1 ATOM 1834 C CG . GLU B 1 25 ? 14.724 17.985 -17.960 1.00 161.97 ? 25 GLU B CG 1 ATOM 1835 C CD . GLU B 1 25 ? 16.052 18.134 -18.669 1.00 165.28 ? 25 GLU B CD 1 ATOM 1836 O OE1 . GLU B 1 25 ? 16.149 19.023 -19.534 1.00 172.02 ? 25 GLU B OE1 1 ATOM 1837 O OE2 . GLU B 1 25 ? 16.996 17.372 -18.354 1.00 161.09 ? 25 GLU B OE2 1 ATOM 1838 N N . ASP B 1 26 ? 10.177 18.751 -19.007 1.00 151.92 ? 26 ASP B N 1 ATOM 1839 C CA . ASP B 1 26 ? 8.858 19.313 -19.389 1.00 151.05 ? 26 ASP B CA 1 ATOM 1840 C C . ASP B 1 26 ? 7.887 18.150 -19.502 1.00 132.21 ? 26 ASP B C 1 ATOM 1841 O O . ASP B 1 26 ? 8.296 16.994 -19.548 1.00 117.45 ? 26 ASP B O 1 ATOM 1842 C CB . ASP B 1 26 ? 8.878 20.163 -20.678 1.00 159.76 ? 26 ASP B CB 1 ATOM 1843 C CG . ASP B 1 26 ? 9.240 19.355 -21.960 1.00 171.73 ? 26 ASP B CG 1 ATOM 1844 O OD1 . ASP B 1 26 ? 9.274 18.107 -21.873 1.00 168.79 ? 26 ASP B OD1 1 ATOM 1845 O OD2 . ASP B 1 26 ? 9.505 19.938 -23.071 1.00 170.76 ? 26 ASP B OD2 1 ATOM 1846 N N . THR B 1 27 ? 6.601 18.468 -19.558 1.00 131.13 ? 27 THR B N 1 ATOM 1847 C CA . THR B 1 27 ? 5.552 17.552 -19.126 1.00 129.36 ? 27 THR B CA 1 ATOM 1848 C C . THR B 1 27 ? 5.533 16.193 -19.819 1.00 134.30 ? 27 THR B C 1 ATOM 1849 O O . THR B 1 27 ? 5.390 15.178 -19.131 1.00 131.85 ? 27 THR B O 1 ATOM 1850 C CB . THR B 1 27 ? 4.111 18.208 -19.255 1.00 152.50 ? 27 THR B CB 1 ATOM 1851 O OG1 . THR B 1 27 ? 3.129 17.242 -18.877 1.00 153.24 ? 27 THR B OG1 1 ATOM 1852 C CG2 . THR B 1 27 ? 3.773 18.665 -20.652 1.00 149.40 ? 27 THR B CG2 1 ATOM 1853 N N . ASP B 1 28 ? 5.696 16.148 -21.140 1.00 143.23 ? 28 ASP B N 1 ATOM 1854 C CA . ASP B 1 28 ? 5.410 14.903 -21.843 1.00 145.60 ? 28 ASP B CA 1 ATOM 1855 C C . ASP B 1 28 ? 6.617 14.002 -22.069 1.00 139.83 ? 28 ASP B C 1 ATOM 1856 O O . ASP B 1 28 ? 6.615 13.208 -23.001 1.00 126.48 ? 28 ASP B O 1 ATOM 1857 C CB . ASP B 1 28 ? 4.677 15.187 -23.174 1.00 160.21 ? 28 ASP B CB 1 ATOM 1858 C CG . ASP B 1 28 ? 5.187 16.430 -23.882 1.00 169.69 ? 28 ASP B CG 1 ATOM 1859 O OD1 . ASP B 1 28 ? 5.665 17.349 -23.187 1.00 172.19 ? 28 ASP B OD1 1 ATOM 1860 O OD2 . ASP B 1 28 ? 5.080 16.501 -25.127 1.00 170.14 ? 28 ASP B OD2 1 ATOM 1861 N N . LYS B 1 29 ? 7.630 14.080 -21.206 1.00 139.29 ? 29 LYS B N 1 ATOM 1862 C CA . LYS B 1 29 ? 8.542 12.939 -21.137 1.00 126.33 ? 29 LYS B CA 1 ATOM 1863 C C . LYS B 1 29 ? 8.075 12.000 -20.054 1.00 116.58 ? 29 LYS B C 1 ATOM 1864 O O . LYS B 1 29 ? 7.118 12.275 -19.323 1.00 122.85 ? 29 LYS B O 1 ATOM 1865 C CB . LYS B 1 29 ? 10.010 13.287 -20.866 1.00 128.30 ? 29 LYS B CB 1 ATOM 1866 C CG . LYS B 1 29 ? 10.597 14.460 -21.569 1.00 131.10 ? 29 LYS B CG 1 ATOM 1867 C CD . LYS B 1 29 ? 10.692 15.698 -20.760 1.00 135.59 ? 29 LYS B CD 1 ATOM 1868 C CE . LYS B 1 29 ? 11.952 16.405 -21.211 1.00 153.12 ? 29 LYS B CE 1 ATOM 1869 N NZ . LYS B 1 29 ? 11.952 17.915 -21.271 1.00 154.57 ? 29 LYS B NZ 1 ATOM 1870 N N . VAL B 1 30 ? 8.751 10.870 -19.959 1.00 107.63 ? 30 VAL B N 1 ATOM 1871 C CA . VAL B 1 30 ? 8.321 9.864 -19.036 1.00 97.96 ? 30 VAL B CA 1 ATOM 1872 C C . VAL B 1 30 ? 9.429 9.651 -18.025 1.00 105.80 ? 30 VAL B C 1 ATOM 1873 O O . VAL B 1 30 ? 10.608 9.794 -18.324 1.00 111.30 ? 30 VAL B O 1 ATOM 1874 C CB . VAL B 1 30 ? 7.968 8.560 -19.752 1.00 83.29 ? 30 VAL B CB 1 ATOM 1875 C CG1 . VAL B 1 30 ? 8.665 7.346 -19.097 1.00 84.42 ? 30 VAL B CG1 1 ATOM 1876 C CG2 . VAL B 1 30 ? 6.510 8.375 -19.711 1.00 65.88 ? 30 VAL B CG2 1 ATOM 1877 N N . LEU B 1 31 ? 9.022 9.365 -16.804 1.00 101.28 ? 31 LEU B N 1 ATOM 1878 C CA . LEU B 1 31 ? 9.936 9.012 -15.751 1.00 92.59 ? 31 LEU B CA 1 ATOM 1879 C C . LEU B 1 31 ? 9.886 7.494 -15.616 1.00 93.86 ? 31 LEU B C 1 ATOM 1880 O O . LEU B 1 31 ? 8.937 6.954 -15.058 1.00 90.64 ? 31 LEU B O 1 ATOM 1881 C CB . LEU B 1 31 ? 9.525 9.738 -14.469 1.00 87.75 ? 31 LEU B CB 1 ATOM 1882 C CG . LEU B 1 31 ? 10.410 9.858 -13.244 1.00 88.91 ? 31 LEU B CG 1 ATOM 1883 C CD1 . LEU B 1 31 ? 9.820 10.920 -12.349 1.00 90.62 ? 31 LEU B CD1 1 ATOM 1884 C CD2 . LEU B 1 31 ? 10.372 8.536 -12.532 1.00 83.96 ? 31 LEU B CD2 1 ATOM 1885 N N . ASN B 1 32 ? 10.887 6.780 -16.115 1.00 96.27 ? 32 ASN B N 1 ATOM 1886 C CA . ASN B 1 32 ? 10.785 5.347 -15.941 1.00 101.47 ? 32 ASN B CA 1 ATOM 1887 C C . ASN B 1 32 ? 11.328 4.962 -14.562 1.00 102.54 ? 32 ASN B C 1 ATOM 1888 O O . ASN B 1 32 ? 12.032 5.755 -13.934 1.00 105.10 ? 32 ASN B O 1 ATOM 1889 C CB . ASN B 1 32 ? 11.527 4.563 -17.032 1.00 109.79 ? 32 ASN B CB 1 ATOM 1890 C CG . ASN B 1 32 ? 11.306 5.081 -18.463 1.00 130.15 ? 32 ASN B CG 1 ATOM 1891 O OD1 . ASN B 1 32 ? 10.355 4.663 -19.142 1.00 124.52 ? 32 ASN B OD1 1 ATOM 1892 N ND2 . ASN B 1 32 ? 12.239 5.896 -18.972 1.00 143.96 ? 32 ASN B ND2 1 ATOM 1893 N N . VAL B 1 33 ? 10.993 3.762 -14.078 1.00 96.06 ? 33 VAL B N 1 ATOM 1894 C CA . VAL B 1 33 ? 11.296 3.402 -12.697 1.00 86.61 ? 33 VAL B CA 1 ATOM 1895 C C . VAL B 1 33 ? 11.693 1.932 -12.586 1.00 91.90 ? 33 VAL B C 1 ATOM 1896 O O . VAL B 1 33 ? 11.028 1.053 -13.132 1.00 93.82 ? 33 VAL B O 1 ATOM 1897 C CB . VAL B 1 33 ? 10.105 3.672 -11.748 1.00 83.16 ? 33 VAL B CB 1 ATOM 1898 C CG1 . VAL B 1 33 ? 10.372 3.087 -10.363 1.00 69.32 ? 33 VAL B CG1 1 ATOM 1899 C CG2 . VAL B 1 33 ? 9.845 5.159 -11.608 1.00 87.91 ? 33 VAL B CG2 1 ATOM 1900 N N . THR B 1 34 ? 12.771 1.676 -11.850 1.00 89.18 ? 34 THR B N 1 ATOM 1901 C CA . THR B 1 34 ? 13.300 0.345 -11.712 1.00 77.18 ? 34 THR B CA 1 ATOM 1902 C C . THR B 1 34 ? 12.781 -0.187 -10.427 1.00 74.56 ? 34 THR B C 1 ATOM 1903 O O . THR B 1 34 ? 12.777 0.508 -9.421 1.00 80.87 ? 34 THR B O 1 ATOM 1904 C CB . THR B 1 34 ? 14.824 0.335 -11.729 1.00 89.61 ? 34 THR B CB 1 ATOM 1905 O OG1 . THR B 1 34 ? 15.311 1.235 -12.740 1.00 100.77 ? 34 THR B OG1 1 ATOM 1906 C CG2 . THR B 1 34 ? 15.324 -1.061 -11.994 1.00 75.58 ? 34 THR B CG2 1 ATOM 1907 N N . LEU B 1 35 ? 12.298 -1.414 -10.466 1.00 72.41 ? 35 LEU B N 1 ATOM 1908 C CA . LEU B 1 35 ? 11.651 -1.990 -9.303 1.00 70.10 ? 35 LEU B CA 1 ATOM 1909 C C . LEU B 1 35 ? 12.174 -3.354 -8.990 1.00 64.61 ? 35 LEU B C 1 ATOM 1910 O O . LEU B 1 35 ? 12.295 -4.199 -9.885 1.00 60.00 ? 35 LEU B O 1 ATOM 1911 C CB . LEU B 1 35 ? 10.131 -2.047 -9.527 1.00 86.11 ? 35 LEU B CB 1 ATOM 1912 C CG . LEU B 1 35 ? 9.243 -2.453 -8.348 1.00 77.09 ? 35 LEU B CG 1 ATOM 1913 C CD1 . LEU B 1 35 ? 8.160 -1.433 -8.216 1.00 81.27 ? 35 LEU B CD1 1 ATOM 1914 C CD2 . LEU B 1 35 ? 8.646 -3.805 -8.597 1.00 59.63 ? 35 LEU B CD2 1 ATOM 1915 N N . GLN B 1 36 ? 12.458 -3.607 -7.721 1.00 68.57 ? 36 GLN B N 1 ATOM 1916 C CA . GLN B 1 36 ? 12.985 -4.917 -7.400 1.00 86.18 ? 36 GLN B CA 1 ATOM 1917 C C . GLN B 1 36 ? 12.412 -5.324 -6.044 1.00 98.10 ? 36 GLN B C 1 ATOM 1918 O O . GLN B 1 36 ? 12.643 -4.700 -5.007 1.00 116.99 ? 36 GLN B O 1 ATOM 1919 C CB . GLN B 1 36 ? 14.549 -4.792 -7.516 1.00 96.52 ? 36 GLN B CB 1 ATOM 1920 C CG . GLN B 1 36 ? 15.589 -5.964 -7.797 1.00 103.44 ? 36 GLN B CG 1 ATOM 1921 C CD . GLN B 1 36 ? 15.070 -7.349 -8.254 1.00 116.54 ? 36 GLN B CD 1 ATOM 1922 O OE1 . GLN B 1 36 ? 15.686 -8.344 -7.869 1.00 127.20 ? 36 GLN B OE1 1 ATOM 1923 N NE2 . GLN B 1 36 ? 13.806 -7.425 -8.728 1.00 131.41 ? 36 GLN B NE2 1 ATOM 1924 N N . ILE B 1 37 ? 11.606 -6.372 -6.098 1.00 93.88 ? 37 ILE B N 1 ATOM 1925 C CA . ILE B 1 37 ? 11.125 -7.004 -4.902 1.00 78.97 ? 37 ILE B CA 1 ATOM 1926 C C . ILE B 1 37 ? 12.289 -7.825 -4.456 1.00 83.66 ? 37 ILE B C 1 ATOM 1927 O O . ILE B 1 37 ? 12.891 -8.511 -5.269 1.00 92.86 ? 37 ILE B O 1 ATOM 1928 C CB . ILE B 1 37 ? 9.874 -7.890 -5.173 1.00 76.38 ? 37 ILE B CB 1 ATOM 1929 C CG1 . ILE B 1 37 ? 8.622 -7.026 -5.225 1.00 81.08 ? 37 ILE B CG1 1 ATOM 1930 C CG2 . ILE B 1 37 ? 9.727 -9.027 -4.179 1.00 62.29 ? 37 ILE B CG2 1 ATOM 1931 C CD1 . ILE B 1 37 ? 8.612 -5.889 -4.254 1.00 78.87 ? 37 ILE B CD1 1 ATOM 1932 N N . THR B 1 38 ? 12.617 -7.749 -3.172 1.00 90.93 ? 38 THR B N 1 ATOM 1933 C CA . THR B 1 38 ? 13.610 -8.618 -2.571 1.00 89.39 ? 38 THR B CA 1 ATOM 1934 C C . THR B 1 38 ? 12.852 -9.287 -1.455 1.00 91.95 ? 38 THR B C 1 ATOM 1935 O O . THR B 1 38 ? 12.511 -8.655 -0.450 1.00 103.55 ? 38 THR B O 1 ATOM 1936 C CB . THR B 1 38 ? 14.874 -7.903 -2.019 1.00 67.99 ? 38 THR B CB 1 ATOM 1937 O OG1 . THR B 1 38 ? 15.457 -7.010 -2.986 1.00 61.26 ? 38 THR B OG1 1 ATOM 1938 C CG2 . THR B 1 38 ? 15.890 -8.942 -1.671 1.00 81.59 ? 38 THR B CG2 1 ATOM 1939 N N . LEU B 1 39 ? 12.474 -10.532 -1.683 1.00 85.71 ? 39 LEU B N 1 ATOM 1940 C CA . LEU B 1 39 ? 11.763 -11.308 -0.680 1.00 75.35 ? 39 LEU B CA 1 ATOM 1941 C C . LEU B 1 39 ? 12.590 -11.686 0.536 1.00 83.19 ? 39 LEU B C 1 ATOM 1942 O O . LEU B 1 39 ? 13.752 -12.060 0.424 1.00 97.31 ? 39 LEU B O 1 ATOM 1943 C CB . LEU B 1 39 ? 11.167 -12.552 -1.334 1.00 67.41 ? 39 LEU B CB 1 ATOM 1944 C CG . LEU B 1 39 ? 10.693 -13.646 -0.390 1.00 72.45 ? 39 LEU B CG 1 ATOM 1945 C CD1 . LEU B 1 39 ? 9.390 -14.347 -0.804 1.00 64.75 ? 39 LEU B CD1 1 ATOM 1946 C CD2 . LEU B 1 39 ? 11.802 -14.633 -0.477 1.00 69.99 ? 39 LEU B CD2 1 ATOM 1947 N N . SER B 1 40 ? 11.998 -11.552 1.710 1.00 84.98 ? 40 SER B N 1 ATOM 1948 C CA . SER B 1 40 ? 12.675 -12.003 2.924 1.00 92.22 ? 40 SER B CA 1 ATOM 1949 C C . SER B 1 40 ? 11.998 -13.246 3.504 1.00 95.56 ? 40 SER B C 1 ATOM 1950 O O . SER B 1 40 ? 12.669 -14.241 3.792 1.00 84.50 ? 40 SER B O 1 ATOM 1951 C CB . SER B 1 40 ? 12.721 -10.891 3.998 1.00 86.56 ? 40 SER B CB 1 ATOM 1952 O OG . SER B 1 40 ? 13.511 -9.766 3.602 1.00 94.03 ? 40 SER B OG 1 ATOM 1953 N N . GLN B 1 41 ? 10.668 -13.220 3.618 1.00 100.74 ? 41 GLN B N 1 ATOM 1954 C CA . GLN B 1 41 ? 9.957 -14.351 4.215 1.00 87.23 ? 41 GLN B CA 1 ATOM 1955 C C . GLN B 1 41 ? 8.474 -14.472 3.917 1.00 76.51 ? 41 GLN B C 1 ATOM 1956 O O . GLN B 1 41 ? 7.775 -13.474 3.713 1.00 70.75 ? 41 GLN B O 1 ATOM 1957 C CB . GLN B 1 41 ? 10.157 -14.322 5.725 1.00 87.64 ? 41 GLN B CB 1 ATOM 1958 C CG . GLN B 1 41 ? 8.980 -14.845 6.604 1.00 145.37 ? 41 GLN B CG 1 ATOM 1959 C CD . GLN B 1 41 ? 8.794 -16.362 6.602 1.00 139.40 ? 41 GLN B CD 1 ATOM 1960 O OE1 . GLN B 1 41 ? 9.106 -17.047 5.622 1.00 135.01 ? 41 GLN B OE1 1 ATOM 1961 N NE2 . GLN B 1 41 ? 8.239 -16.887 7.695 1.00 134.23 ? 41 GLN B NE2 1 ATOM 1962 N N . ILE B 1 42 ? 8.032 -15.730 3.865 1.00 70.55 ? 42 ILE B N 1 ATOM 1963 C CA . ILE B 1 42 ? 6.627 -16.113 3.968 1.00 72.35 ? 42 ILE B CA 1 ATOM 1964 C C . ILE B 1 42 ? 6.111 -16.228 5.429 1.00 74.75 ? 42 ILE B C 1 ATOM 1965 O O . ILE B 1 42 ? 6.237 -17.302 6.030 1.00 73.70 ? 42 ILE B O 1 ATOM 1966 C CB . ILE B 1 42 ? 6.396 -17.489 3.287 1.00 99.60 ? 42 ILE B CB 1 ATOM 1967 C CG1 . ILE B 1 42 ? 6.935 -17.487 1.859 1.00 97.41 ? 42 ILE B CG1 1 ATOM 1968 C CG2 . ILE B 1 42 ? 4.916 -17.878 3.317 1.00 99.89 ? 42 ILE B CG2 1 ATOM 1969 C CD1 . ILE B 1 42 ? 6.678 -18.778 1.111 1.00 96.81 ? 42 ILE B CD1 1 ATOM 1970 N N . LYS B 1 43 ? 5.555 -15.156 6.007 1.00 82.96 ? 43 LYS B N 1 ATOM 1971 C CA . LYS B 1 43 ? 5.086 -15.191 7.415 1.00 77.52 ? 43 LYS B CA 1 ATOM 1972 C C . LYS B 1 43 ? 3.954 -16.183 7.624 1.00 64.53 ? 43 LYS B C 1 ATOM 1973 O O . LYS B 1 43 ? 3.816 -16.795 8.672 1.00 70.29 ? 43 LYS B O 1 ATOM 1974 C CB . LYS B 1 43 ? 4.607 -13.813 7.901 1.00 76.54 ? 43 LYS B CB 1 ATOM 1975 C CG . LYS B 1 43 ? 3.818 -13.900 9.207 1.00 84.60 ? 43 LYS B CG 1 ATOM 1976 C CD . LYS B 1 43 ? 4.431 -13.101 10.353 1.00 98.01 ? 43 LYS B CD 1 ATOM 1977 C CE . LYS B 1 43 ? 4.346 -13.896 11.669 1.00 105.77 ? 43 LYS B CE 1 ATOM 1978 N NZ . LYS B 1 43 ? 4.533 -13.062 12.894 1.00 112.91 ? 43 LYS B NZ 1 ATOM 1979 N N . ASP B 1 44 ? 3.166 -16.376 6.590 1.00 82.84 ? 44 ASP B N 1 ATOM 1980 C CA . ASP B 1 44 ? 2.027 -17.248 6.701 1.00 93.97 ? 44 ASP B CA 1 ATOM 1981 C C . ASP B 1 44 ? 1.458 -17.467 5.314 1.00 86.24 ? 44 ASP B C 1 ATOM 1982 O O . ASP B 1 44 ? 1.128 -16.515 4.590 1.00 67.37 ? 44 ASP B O 1 ATOM 1983 C CB . ASP B 1 44 ? 0.975 -16.639 7.650 1.00 99.28 ? 44 ASP B CB 1 ATOM 1984 C CG . ASP B 1 44 ? -0.254 -17.507 7.806 1.00 99.47 ? 44 ASP B CG 1 ATOM 1985 O OD1 . ASP B 1 44 ? -1.113 -17.498 6.906 1.00 109.12 ? 44 ASP B OD1 1 ATOM 1986 O OD2 . ASP B 1 44 ? -0.374 -18.194 8.824 1.00 94.37 ? 44 ASP B OD2 1 ATOM 1987 N N . MET B 1 45 ? 1.407 -18.738 4.945 1.00 77.93 ? 45 MET B N 1 ATOM 1988 C CA . MET B 1 45 ? 0.655 -19.145 3.795 1.00 72.04 ? 45 MET B CA 1 ATOM 1989 C C . MET B 1 45 ? -0.670 -19.650 4.347 1.00 81.10 ? 45 MET B C 1 ATOM 1990 O O . MET B 1 45 ? -0.819 -20.841 4.623 1.00 92.39 ? 45 MET B O 1 ATOM 1991 C CB . MET B 1 45 ? 1.382 -20.232 2.997 1.00 75.03 ? 45 MET B CB 1 ATOM 1992 C CG . MET B 1 45 ? 0.741 -20.539 1.638 1.00 75.32 ? 45 MET B CG 1 ATOM 1993 S SD . MET B 1 45 ? 0.727 -19.012 0.632 1.00 102.98 ? 45 MET B SD 1 ATOM 1994 C CE . MET B 1 45 ? -0.935 -18.979 -0.015 1.00 59.95 ? 45 MET B CE 1 ATOM 1995 N N . ASP B 1 46 ? -1.617 -18.738 4.533 1.00 73.33 ? 46 ASP B N 1 ATOM 1996 C CA . ASP B 1 46 ? -2.977 -19.097 4.956 1.00 71.44 ? 46 ASP B CA 1 ATOM 1997 C C . ASP B 1 46 ? -3.565 -20.016 3.890 1.00 79.31 ? 46 ASP B C 1 ATOM 1998 O O . ASP B 1 46 ? -4.064 -19.556 2.851 1.00 76.00 ? 46 ASP B O 1 ATOM 1999 C CB . ASP B 1 46 ? -3.813 -17.818 5.144 1.00 56.03 ? 46 ASP B CB 1 ATOM 2000 C CG . ASP B 1 46 ? -5.155 -18.047 5.825 1.00 61.18 ? 46 ASP B CG 1 ATOM 2001 O OD1 . ASP B 1 46 ? -5.754 -19.161 5.738 1.00 60.83 ? 46 ASP B OD1 1 ATOM 2002 O OD2 . ASP B 1 46 ? -5.648 -17.048 6.409 1.00 63.16 ? 46 ASP B OD2 1 ATOM 2003 N N . GLU B 1 47 ? -3.484 -21.320 4.118 1.00 80.00 ? 47 GLU B N 1 ATOM 2004 C CA . GLU B 1 47 ? -3.974 -22.217 3.090 1.00 89.20 ? 47 GLU B CA 1 ATOM 2005 C C . GLU B 1 47 ? -5.467 -22.105 2.868 1.00 111.77 ? 47 GLU B C 1 ATOM 2006 O O . GLU B 1 47 ? -5.877 -21.907 1.735 1.00 123.65 ? 47 GLU B O 1 ATOM 2007 C CB . GLU B 1 47 ? -3.678 -23.665 3.411 1.00 86.15 ? 47 GLU B CB 1 ATOM 2008 C CG . GLU B 1 47 ? -2.322 -24.109 3.013 1.00 91.26 ? 47 GLU B CG 1 ATOM 2009 C CD . GLU B 1 47 ? -2.300 -25.595 2.706 1.00 98.14 ? 47 GLU B CD 1 ATOM 2010 O OE1 . GLU B 1 47 ? -2.694 -26.410 3.577 1.00 106.93 ? 47 GLU B OE1 1 ATOM 2011 O OE2 . GLU B 1 47 ? -1.878 -25.943 1.583 1.00 96.58 ? 47 GLU B OE2 1 ATOM 2012 N N . ARG B 1 48 ? -6.294 -22.179 3.911 1.00 106.32 ? 48 ARG B N 1 ATOM 2013 C CA . ARG B 1 48 ? -7.710 -22.382 3.629 1.00 98.76 ? 48 ARG B CA 1 ATOM 2014 C C . ARG B 1 48 ? -8.413 -21.053 3.431 1.00 91.59 ? 48 ARG B C 1 ATOM 2015 O O . ARG B 1 48 ? -9.562 -21.014 3.037 1.00 103.57 ? 48 ARG B O 1 ATOM 2016 C CB . ARG B 1 48 ? -8.392 -23.194 4.736 1.00 112.43 ? 48 ARG B CB 1 ATOM 2017 C CG . ARG B 1 48 ? -8.335 -24.727 4.531 1.00 126.04 ? 48 ARG B CG 1 ATOM 2018 C CD . ARG B 1 48 ? -9.264 -25.161 3.374 1.00 134.63 ? 48 ARG B CD 1 ATOM 2019 N NE . ARG B 1 48 ? -9.107 -26.542 2.885 1.00 135.46 ? 48 ARG B NE 1 ATOM 2020 C CZ . ARG B 1 48 ? -7.965 -27.103 2.465 1.00 134.23 ? 48 ARG B CZ 1 ATOM 2021 N NH1 . ARG B 1 48 ? -6.800 -26.429 2.459 1.00 129.12 ? 48 ARG B NH1 1 ATOM 2022 N NH2 . ARG B 1 48 ? -7.991 -28.365 2.035 1.00 136.20 ? 48 ARG B NH2 1 ATOM 2023 N N . ASN B 1 49 ? -7.693 -19.959 3.601 1.00 86.44 ? 49 ASN B N 1 ATOM 2024 C CA . ASN B 1 49 ? -8.191 -18.681 3.127 1.00 87.24 ? 49 ASN B CA 1 ATOM 2025 C C . ASN B 1 49 ? -7.522 -18.278 1.837 1.00 98.97 ? 49 ASN B C 1 ATOM 2026 O O . ASN B 1 49 ? -7.853 -17.250 1.275 1.00 117.84 ? 49 ASN B O 1 ATOM 2027 C CB . ASN B 1 49 ? -7.975 -17.591 4.180 1.00 86.79 ? 49 ASN B CB 1 ATOM 2028 C CG . ASN B 1 49 ? -8.692 -17.884 5.445 1.00 89.97 ? 49 ASN B CG 1 ATOM 2029 O OD1 . ASN B 1 49 ? -9.820 -18.377 5.419 1.00 91.96 ? 49 ASN B OD1 1 ATOM 2030 N ND2 . ASN B 1 49 ? -8.053 -17.603 6.574 1.00 87.74 ? 49 ASN B ND2 1 ATOM 2031 N N . GLN B 1 50 ? -6.551 -19.082 1.405 1.00 105.07 ? 50 GLN B N 1 ATOM 2032 C CA . GLN B 1 50 ? -5.688 -18.798 0.252 1.00 87.55 ? 50 GLN B CA 1 ATOM 2033 C C . GLN B 1 50 ? -5.101 -17.418 0.308 1.00 86.72 ? 50 GLN B C 1 ATOM 2034 O O . GLN B 1 50 ? -5.140 -16.695 -0.681 1.00 92.87 ? 50 GLN B O 1 ATOM 2035 C CB . GLN B 1 50 ? -6.463 -18.917 -1.041 1.00 83.27 ? 50 GLN B CB 1 ATOM 2036 C CG . GLN B 1 50 ? -5.892 -19.879 -1.990 1.00 95.45 ? 50 GLN B CG 1 ATOM 2037 C CD . GLN B 1 50 ? -5.976 -21.276 -1.440 1.00 100.65 ? 50 GLN B CD 1 ATOM 2038 O OE1 . GLN B 1 50 ? -6.951 -21.649 -0.803 1.00 114.05 ? 50 GLN B OE1 1 ATOM 2039 N NE2 . GLN B 1 50 ? -4.990 -22.084 -1.745 1.00 101.06 ? 50 GLN B NE2 1 ATOM 2040 N N . ILE B 1 51 ? -4.566 -17.033 1.454 1.00 74.97 ? 51 ILE B N 1 ATOM 2041 C CA . ILE B 1 51 ? -3.944 -15.732 1.540 1.00 71.47 ? 51 ILE B CA 1 ATOM 2042 C C . ILE B 1 51 ? -2.473 -15.980 1.816 1.00 79.32 ? 51 ILE B C 1 ATOM 2043 O O . ILE B 1 51 ? -2.128 -16.875 2.588 1.00 95.79 ? 51 ILE B O 1 ATOM 2044 C CB . ILE B 1 51 ? -4.598 -14.850 2.628 1.00 64.42 ? 51 ILE B CB 1 ATOM 2045 C CG1 . ILE B 1 51 ? -5.964 -14.406 2.162 1.00 68.08 ? 51 ILE B CG1 1 ATOM 2046 C CG2 . ILE B 1 51 ? -3.801 -13.593 2.842 1.00 68.55 ? 51 ILE B CG2 1 ATOM 2047 C CD1 . ILE B 1 51 ? -5.880 -13.506 0.928 1.00 57.51 ? 51 ILE B CD1 1 ATOM 2048 N N . LEU B 1 52 ? -1.605 -15.230 1.154 1.00 67.99 ? 52 LEU B N 1 ATOM 2049 C CA . LEU B 1 52 ? -0.180 -15.277 1.444 1.00 56.33 ? 52 LEU B CA 1 ATOM 2050 C C . LEU B 1 52 ? 0.206 -14.044 2.233 1.00 61.09 ? 52 LEU B C 1 ATOM 2051 O O . LEU B 1 52 ? -0.170 -12.922 1.899 1.00 70.53 ? 52 LEU B O 1 ATOM 2052 C CB . LEU B 1 52 ? 0.622 -15.339 0.165 1.00 61.03 ? 52 LEU B CB 1 ATOM 2053 C CG . LEU B 1 52 ? 2.100 -15.019 0.337 1.00 69.11 ? 52 LEU B CG 1 ATOM 2054 C CD1 . LEU B 1 52 ? 2.966 -16.270 0.588 1.00 68.41 ? 52 LEU B CD1 1 ATOM 2055 C CD2 . LEU B 1 52 ? 2.605 -14.189 -0.831 1.00 68.68 ? 52 LEU B CD2 1 ATOM 2056 N N . THR B 1 53 ? 0.926 -14.244 3.316 1.00 74.33 ? 53 THR B N 1 ATOM 2057 C CA . THR B 1 53 ? 1.433 -13.108 4.048 1.00 69.34 ? 53 THR B CA 1 ATOM 2058 C C . THR B 1 53 ? 2.951 -13.037 3.890 1.00 61.89 ? 53 THR B C 1 ATOM 2059 O O . THR B 1 53 ? 3.634 -14.059 3.990 1.00 57.27 ? 53 THR B O 1 ATOM 2060 C CB . THR B 1 53 ? 1.039 -13.198 5.514 1.00 71.93 ? 53 THR B CB 1 ATOM 2061 O OG1 . THR B 1 53 ? -0.381 -13.488 5.620 1.00 70.82 ? 53 THR B OG1 1 ATOM 2062 C CG2 . THR B 1 53 ? 1.391 -11.853 6.211 1.00 45.88 ? 53 THR B CG2 1 ATOM 2063 N N . ALA B 1 54 ? 3.485 -11.855 3.603 1.00 53.76 ? 54 ALA B N 1 ATOM 2064 C CA . ALA B 1 54 ? 4.898 -11.777 3.329 1.00 68.88 ? 54 ALA B CA 1 ATOM 2065 C C . ALA B 1 54 ? 5.573 -10.501 3.825 1.00 78.89 ? 54 ALA B C 1 ATOM 2066 O O . ALA B 1 54 ? 4.971 -9.430 3.852 1.00 87.32 ? 54 ALA B O 1 ATOM 2067 C CB . ALA B 1 54 ? 5.121 -11.932 1.839 1.00 82.76 ? 54 ALA B CB 1 ATOM 2068 N N . TYR B 1 55 ? 6.832 -10.655 4.230 1.00 64.22 ? 55 TYR B N 1 ATOM 2069 C CA . TYR B 1 55 ? 7.749 -9.559 4.517 1.00 73.30 ? 55 TYR B CA 1 ATOM 2070 C C . TYR B 1 55 ? 8.638 -9.339 3.277 1.00 73.14 ? 55 TYR B C 1 ATOM 2071 O O . TYR B 1 55 ? 9.167 -10.307 2.705 1.00 76.75 ? 55 TYR B O 1 ATOM 2072 C CB . TYR B 1 55 ? 8.605 -9.887 5.759 1.00 88.86 ? 55 TYR B CB 1 ATOM 2073 C CG . TYR B 1 55 ? 7.834 -9.998 7.087 1.00 92.33 ? 55 TYR B CG 1 ATOM 2074 C CD1 . TYR B 1 55 ? 6.905 -9.040 7.456 1.00 93.21 ? 55 TYR B CD1 1 ATOM 2075 C CD2 . TYR B 1 55 ? 7.990 -11.108 7.918 1.00 87.09 ? 55 TYR B CD2 1 ATOM 2076 C CE1 . TYR B 1 55 ? 6.193 -9.147 8.625 1.00 92.21 ? 55 TYR B CE1 1 ATOM 2077 C CE2 . TYR B 1 55 ? 7.272 -11.228 9.085 1.00 89.74 ? 55 TYR B CE2 1 ATOM 2078 C CZ . TYR B 1 55 ? 6.369 -10.241 9.436 1.00 93.89 ? 55 TYR B CZ 1 ATOM 2079 O OH . TYR B 1 55 ? 5.639 -10.325 10.608 1.00 92.67 ? 55 TYR B OH 1 ATOM 2080 N N . LEU B 1 56 ? 8.777 -8.083 2.846 1.00 59.17 ? 56 LEU B N 1 ATOM 2081 C CA . LEU B 1 56 ? 9.607 -7.759 1.693 1.00 67.43 ? 56 LEU B CA 1 ATOM 2082 C C . LEU B 1 56 ? 10.393 -6.452 1.864 1.00 71.07 ? 56 LEU B C 1 ATOM 2083 O O . LEU B 1 56 ? 10.037 -5.607 2.691 1.00 77.57 ? 56 LEU B O 1 ATOM 2084 C CB . LEU B 1 56 ? 8.752 -7.600 0.429 1.00 72.34 ? 56 LEU B CB 1 ATOM 2085 C CG . LEU B 1 56 ? 7.657 -8.511 -0.087 1.00 60.16 ? 56 LEU B CG 1 ATOM 2086 C CD1 . LEU B 1 56 ? 7.116 -7.777 -1.265 1.00 57.13 ? 56 LEU B CD1 1 ATOM 2087 C CD2 . LEU B 1 56 ? 8.150 -9.897 -0.480 1.00 58.14 ? 56 LEU B CD2 1 ATOM 2088 N N . TRP B 1 57 ? 11.420 -6.279 1.034 1.00 55.18 ? 57 TRP B N 1 ATOM 2089 C CA . TRP B 1 57 ? 12.138 -5.024 0.857 1.00 53.48 ? 57 TRP B CA 1 ATOM 2090 C C . TRP B 1 57 ? 11.923 -4.609 -0.565 1.00 63.24 ? 57 TRP B C 1 ATOM 2091 O O . TRP B 1 57 ? 11.962 -5.462 -1.435 1.00 78.16 ? 57 TRP B O 1 ATOM 2092 C CB . TRP B 1 57 ? 13.634 -5.215 1.176 1.00 76.23 ? 57 TRP B CB 1 ATOM 2093 C CG . TRP B 1 57 ? 13.837 -5.377 2.660 1.00 63.79 ? 57 TRP B CG 1 ATOM 2094 C CD1 . TRP B 1 57 ? 13.875 -6.539 3.360 1.00 65.82 ? 57 TRP B CD1 1 ATOM 2095 C CD2 . TRP B 1 57 ? 13.947 -4.318 3.612 1.00 59.64 ? 57 TRP B CD2 1 ATOM 2096 N NE1 . TRP B 1 57 ? 14.012 -6.263 4.696 1.00 84.18 ? 57 TRP B NE1 1 ATOM 2097 C CE2 . TRP B 1 57 ? 14.056 -4.901 4.867 1.00 81.13 ? 57 TRP B CE2 1 ATOM 2098 C CE3 . TRP B 1 57 ? 13.961 -2.922 3.512 1.00 60.38 ? 57 TRP B CE3 1 ATOM 2099 C CZ2 . TRP B 1 57 ? 14.196 -4.138 6.018 1.00 89.85 ? 57 TRP B CZ2 1 ATOM 2100 C CZ3 . TRP B 1 57 ? 14.088 -2.173 4.639 1.00 64.68 ? 57 TRP B CZ3 1 ATOM 2101 C CH2 . TRP B 1 57 ? 14.209 -2.773 5.877 1.00 81.43 ? 57 TRP B CH2 1 ATOM 2102 N N . ILE B 1 58 ? 11.640 -3.332 -0.812 1.00 53.79 ? 58 ILE B N 1 ATOM 2103 C CA . ILE B 1 58 ? 11.206 -2.906 -2.123 1.00 56.57 ? 58 ILE B CA 1 ATOM 2104 C C . ILE B 1 58 ? 12.008 -1.742 -2.634 1.00 75.62 ? 58 ILE B C 1 ATOM 2105 O O . ILE B 1 58 ? 11.736 -0.579 -2.266 1.00 79.51 ? 58 ILE B O 1 ATOM 2106 C CB . ILE B 1 58 ? 9.718 -2.486 -2.102 1.00 78.72 ? 58 ILE B CB 1 ATOM 2107 C CG1 . ILE B 1 58 ? 8.825 -3.648 -1.631 1.00 83.72 ? 58 ILE B CG1 1 ATOM 2108 C CG2 . ILE B 1 58 ? 9.276 -1.889 -3.445 1.00 76.90 ? 58 ILE B CG2 1 ATOM 2109 C CD1 . ILE B 1 58 ? 7.317 -3.342 -1.666 1.00 88.01 ? 58 ILE B CD1 1 ATOM 2110 N N . ARG B 1 59 ? 12.906 -2.036 -3.575 1.00 75.66 ? 59 ARG B N 1 ATOM 2111 C CA . ARG B 1 59 ? 13.750 -1.026 -4.166 1.00 81.50 ? 59 ARG B CA 1 ATOM 2112 C C . ARG B 1 59 ? 13.111 -0.342 -5.377 1.00 88.95 ? 59 ARG B C 1 ATOM 2113 O O . ARG B 1 59 ? 12.673 -0.990 -6.328 1.00 101.53 ? 59 ARG B O 1 ATOM 2114 C CB . ARG B 1 59 ? 15.096 -1.634 -4.561 1.00 96.40 ? 59 ARG B CB 1 ATOM 2115 C CG . ARG B 1 59 ? 15.812 -0.820 -5.633 1.00 102.93 ? 59 ARG B CG 1 ATOM 2116 C CD . ARG B 1 59 ? 17.096 -1.473 -6.098 1.00 112.52 ? 59 ARG B CD 1 ATOM 2117 N NE . ARG B 1 59 ? 18.011 -1.905 -5.027 1.00 109.05 ? 59 ARG B NE 1 ATOM 2118 C CZ . ARG B 1 59 ? 18.638 -1.111 -4.158 1.00 89.25 ? 59 ARG B CZ 1 ATOM 2119 N NH1 . ARG B 1 59 ? 18.459 0.205 -4.160 1.00 79.42 ? 59 ARG B NH1 1 ATOM 2120 N NH2 . ARG B 1 59 ? 19.445 -1.649 -3.266 1.00 80.00 ? 59 ARG B NH2 1 ATOM 2121 N N . GLN B 1 60 ? 13.065 0.982 -5.328 1.00 78.81 ? 60 GLN B N 1 ATOM 2122 C CA . GLN B 1 60 ? 12.565 1.786 -6.425 1.00 73.83 ? 60 GLN B CA 1 ATOM 2123 C C . GLN B 1 60 ? 13.608 2.833 -6.717 1.00 87.52 ? 60 GLN B C 1 ATOM 2124 O O . GLN B 1 60 ? 14.191 3.406 -5.798 1.00 91.16 ? 60 GLN B O 1 ATOM 2125 C CB . GLN B 1 60 ? 11.221 2.440 -6.083 1.00 76.94 ? 60 GLN B CB 1 ATOM 2126 C CG . GLN B 1 60 ? 10.083 1.486 -5.722 1.00 72.57 ? 60 GLN B CG 1 ATOM 2127 C CD . GLN B 1 60 ? 8.973 2.213 -4.995 1.00 83.88 ? 60 GLN B CD 1 ATOM 2128 O OE1 . GLN B 1 60 ? 8.448 3.215 -5.491 1.00 83.22 ? 60 GLN B OE1 1 ATOM 2129 N NE2 . GLN B 1 60 ? 8.619 1.726 -3.798 1.00 92.84 ? 60 GLN B NE2 1 ATOM 2130 N N . ILE B 1 61 ? 13.922 3.004 -7.999 1.00 92.12 ? 61 ILE B N 1 ATOM 2131 C CA . ILE B 1 61 ? 14.943 3.954 -8.428 1.00 87.35 ? 61 ILE B CA 1 ATOM 2132 C C . ILE B 1 61 ? 14.441 4.730 -9.618 1.00 79.48 ? 61 ILE B C 1 ATOM 2133 O O . ILE B 1 61 ? 13.730 4.178 -10.450 1.00 75.78 ? 61 ILE B O 1 ATOM 2134 C CB . ILE B 1 61 ? 16.265 3.285 -8.786 1.00 90.35 ? 61 ILE B CB 1 ATOM 2135 C CG1 . ILE B 1 61 ? 16.565 2.134 -7.833 1.00 90.01 ? 61 ILE B CG1 1 ATOM 2136 C CG2 . ILE B 1 61 ? 17.379 4.287 -8.668 1.00 91.47 ? 61 ILE B CG2 1 ATOM 2137 C CD1 . ILE B 1 61 ? 17.786 1.377 -8.243 1.00 92.32 ? 61 ILE B CD1 1 ATOM 2138 N N . TRP B 1 62 ? 14.748 6.023 -9.626 1.00 70.05 ? 62 TRP B N 1 ATOM 2139 C CA . TRP B 1 62 ? 14.281 6.969 -10.629 1.00 77.42 ? 62 TRP B CA 1 ATOM 2140 C C . TRP B 1 62 ? 15.037 8.268 -10.489 1.00 88.23 ? 62 TRP B C 1 ATOM 2141 O O . TRP B 1 62 ? 15.676 8.492 -9.485 1.00 98.64 ? 62 TRP B O 1 ATOM 2142 C CB . TRP B 1 62 ? 12.782 7.210 -10.497 1.00 84.49 ? 62 TRP B CB 1 ATOM 2143 C CG . TRP B 1 62 ? 12.489 7.886 -9.259 1.00 94.49 ? 62 TRP B CG 1 ATOM 2144 C CD1 . TRP B 1 62 ? 12.303 9.230 -9.031 1.00 94.86 ? 62 TRP B CD1 1 ATOM 2145 C CD2 . TRP B 1 62 ? 12.359 7.234 -7.986 1.00 106.31 ? 62 TRP B CD2 1 ATOM 2146 N NE1 . TRP B 1 62 ? 12.066 9.424 -7.684 1.00 101.08 ? 62 TRP B NE1 1 ATOM 2147 C CE2 . TRP B 1 62 ? 12.108 8.220 -7.038 1.00 101.91 ? 62 TRP B CE2 1 ATOM 2148 C CE3 . TRP B 1 62 ? 12.442 5.907 -7.572 1.00 107.79 ? 62 TRP B CE3 1 ATOM 2149 C CZ2 . TRP B 1 62 ? 11.966 7.903 -5.683 1.00 97.94 ? 62 TRP B CZ2 1 ATOM 2150 C CZ3 . TRP B 1 62 ? 12.281 5.617 -6.218 1.00 106.96 ? 62 TRP B CZ3 1 ATOM 2151 C CH2 . TRP B 1 62 ? 12.023 6.614 -5.303 1.00 100.45 ? 62 TRP B CH2 1 ATOM 2152 N N . HIS B 1 63 ? 14.929 9.140 -11.483 1.00 103.33 ? 63 HIS B N 1 ATOM 2153 C CA . HIS B 1 63 ? 15.625 10.424 -11.467 1.00 104.70 ? 63 HIS B CA 1 ATOM 2154 C C . HIS B 1 63 ? 14.739 11.627 -11.149 1.00 111.72 ? 63 HIS B C 1 ATOM 2155 O O . HIS B 1 63 ? 13.602 11.718 -11.603 1.00 124.66 ? 63 HIS B O 1 ATOM 2156 C CB . HIS B 1 63 ? 16.301 10.676 -12.817 1.00 109.80 ? 63 HIS B CB 1 ATOM 2157 C CG . HIS B 1 63 ? 17.480 9.795 -13.083 1.00 122.98 ? 63 HIS B CG 1 ATOM 2158 N ND1 . HIS B 1 63 ? 17.352 8.521 -13.586 1.00 129.24 ? 63 HIS B ND1 1 ATOM 2159 C CD2 . HIS B 1 63 ? 18.810 10.018 -12.939 1.00 126.90 ? 63 HIS B CD2 1 ATOM 2160 C CE1 . HIS B 1 63 ? 18.555 7.985 -13.726 1.00 131.31 ? 63 HIS B CE1 1 ATOM 2161 N NE2 . HIS B 1 63 ? 19.454 8.872 -13.342 1.00 128.84 ? 63 HIS B NE2 1 ATOM 2162 N N . ASP B 1 64 ? 15.267 12.551 -10.358 1.00 100.05 ? 64 ASP B N 1 ATOM 2163 C CA . ASP B 1 64 ? 14.602 13.829 -10.122 1.00 108.89 ? 64 ASP B CA 1 ATOM 2164 C C . ASP B 1 64 ? 15.486 14.929 -10.683 1.00 123.92 ? 64 ASP B C 1 ATOM 2165 O O . ASP B 1 64 ? 16.486 15.296 -10.065 1.00 136.21 ? 64 ASP B O 1 ATOM 2166 C CB . ASP B 1 64 ? 14.346 14.072 -8.641 1.00 108.60 ? 64 ASP B CB 1 ATOM 2167 C CG . ASP B 1 64 ? 13.592 15.367 -8.379 1.00 115.40 ? 64 ASP B CG 1 ATOM 2168 O OD1 . ASP B 1 64 ? 14.030 16.443 -8.854 1.00 113.65 ? 64 ASP B OD1 1 ATOM 2169 O OD2 . ASP B 1 64 ? 12.560 15.309 -7.677 1.00 122.01 ? 64 ASP B OD2 1 ATOM 2170 N N . ALA B 1 65 ? 15.109 15.469 -11.840 1.00 119.71 ? 65 ALA B N 1 ATOM 2171 C CA . ALA B 1 65 ? 15.979 16.388 -12.568 1.00 117.47 ? 65 ALA B CA 1 ATOM 2172 C C . ALA B 1 65 ? 16.183 17.707 -11.818 1.00 125.88 ? 65 ALA B C 1 ATOM 2173 O O . ALA B 1 65 ? 17.102 18.473 -12.128 1.00 129.97 ? 65 ALA B O 1 ATOM 2174 C CB . ALA B 1 65 ? 15.417 16.647 -13.949 1.00 111.42 ? 65 ALA B CB 1 ATOM 2175 N N . TYR B 1 66 ? 15.349 17.948 -10.810 1.00 124.41 ? 66 TYR B N 1 ATOM 2176 C CA . TYR B 1 66 ? 15.403 19.191 -10.048 1.00 124.94 ? 66 TYR B CA 1 ATOM 2177 C C . TYR B 1 66 ? 16.331 19.102 -8.826 1.00 125.27 ? 66 TYR B C 1 ATOM 2178 O O . TYR B 1 66 ? 16.731 20.126 -8.263 1.00 134.65 ? 66 TYR B O 1 ATOM 2179 C CB . TYR B 1 66 ? 13.998 19.595 -9.620 1.00 120.41 ? 66 TYR B CB 1 ATOM 2180 C CG . TYR B 1 66 ? 13.066 19.927 -10.768 1.00 117.88 ? 66 TYR B CG 1 ATOM 2181 C CD1 . TYR B 1 66 ? 13.055 21.195 -11.342 1.00 117.52 ? 66 TYR B CD1 1 ATOM 2182 C CD2 . TYR B 1 66 ? 12.178 18.977 -11.261 1.00 119.23 ? 66 TYR B CD2 1 ATOM 2183 C CE1 . TYR B 1 66 ? 12.186 21.503 -12.380 1.00 122.62 ? 66 TYR B CE1 1 ATOM 2184 C CE2 . TYR B 1 66 ? 11.307 19.274 -12.303 1.00 119.76 ? 66 TYR B CE2 1 ATOM 2185 C CZ . TYR B 1 66 ? 11.314 20.535 -12.854 1.00 120.01 ? 66 TYR B CZ 1 ATOM 2186 O OH . TYR B 1 66 ? 10.449 20.822 -13.882 1.00 116.43 ? 66 TYR B OH 1 ATOM 2187 N N . LEU B 1 67 ? 16.701 17.884 -8.441 1.00 115.42 ? 67 LEU B N 1 ATOM 2188 C CA . LEU B 1 67 ? 17.622 17.670 -7.320 1.00 108.33 ? 67 LEU B CA 1 ATOM 2189 C C . LEU B 1 67 ? 19.057 17.521 -7.817 1.00 111.26 ? 67 LEU B C 1 ATOM 2190 O O . LEU B 1 67 ? 19.756 16.563 -7.484 1.00 103.09 ? 67 LEU B O 1 ATOM 2191 C CB . LEU B 1 67 ? 17.219 16.438 -6.528 1.00 100.39 ? 67 LEU B CB 1 ATOM 2192 C CG . LEU B 1 67 ? 15.756 16.471 -6.091 1.00 96.25 ? 67 LEU B CG 1 ATOM 2193 C CD1 . LEU B 1 67 ? 15.372 15.199 -5.341 1.00 89.59 ? 67 LEU B CD1 1 ATOM 2194 C CD2 . LEU B 1 67 ? 15.472 17.708 -5.250 1.00 100.97 ? 67 LEU B CD2 1 ATOM 2195 N N . THR B 1 68 ? 19.471 18.448 -8.667 1.00 119.90 ? 68 THR B N 1 ATOM 2196 C CA . THR B 1 68 ? 20.808 18.407 -9.211 1.00 130.43 ? 68 THR B CA 1 ATOM 2197 C C . THR B 1 68 ? 21.708 19.405 -8.516 1.00 138.10 ? 68 THR B C 1 ATOM 2198 O O . THR B 1 68 ? 21.323 20.539 -8.218 1.00 142.14 ? 68 THR B O 1 ATOM 2199 C CB . THR B 1 68 ? 20.801 18.678 -10.758 1.00 151.85 ? 68 THR B CB 1 ATOM 2200 O OG1 . THR B 1 68 ? 22.118 18.506 -11.303 1.00 154.24 ? 68 THR B OG1 1 ATOM 2201 C CG2 . THR B 1 68 ? 20.283 20.081 -11.089 1.00 155.02 ? 68 THR B CG2 1 ATOM 2202 N N . TRP B 1 69 ? 22.906 18.938 -8.216 1.00 144.42 ? 69 TRP B N 1 ATOM 2203 C CA . TRP B 1 69 ? 23.979 19.807 -7.801 1.00 149.06 ? 69 TRP B CA 1 ATOM 2204 C C . TRP B 1 69 ? 25.244 19.136 -8.286 1.00 158.78 ? 69 TRP B C 1 ATOM 2205 O O . TRP B 1 69 ? 25.363 17.913 -8.213 1.00 161.22 ? 69 TRP B O 1 ATOM 2206 C CB . TRP B 1 69 ? 23.993 20.012 -6.292 1.00 146.37 ? 69 TRP B CB 1 ATOM 2207 C CG . TRP B 1 69 ? 24.620 18.885 -5.542 1.00 145.77 ? 69 TRP B CG 1 ATOM 2208 C CD1 . TRP B 1 69 ? 25.939 18.760 -5.186 1.00 145.90 ? 69 TRP B CD1 1 ATOM 2209 C CD2 . TRP B 1 69 ? 23.959 17.717 -5.052 1.00 143.22 ? 69 TRP B CD2 1 ATOM 2210 N NE1 . TRP B 1 69 ? 26.134 17.581 -4.504 1.00 143.97 ? 69 TRP B NE1 1 ATOM 2211 C CE2 . TRP B 1 69 ? 24.933 16.924 -4.406 1.00 144.38 ? 69 TRP B CE2 1 ATOM 2212 C CE3 . TRP B 1 69 ? 22.638 17.264 -5.091 1.00 140.07 ? 69 TRP B CE3 1 ATOM 2213 C CZ2 . TRP B 1 69 ? 24.624 15.705 -3.805 1.00 144.98 ? 69 TRP B CZ2 1 ATOM 2214 C CZ3 . TRP B 1 69 ? 22.333 16.056 -4.498 1.00 141.02 ? 69 TRP B CZ3 1 ATOM 2215 C CH2 . TRP B 1 69 ? 23.320 15.290 -3.862 1.00 143.72 ? 69 TRP B CH2 1 ATOM 2216 N N . ASP B 1 70 ? 26.180 19.909 -8.814 1.00 163.58 ? 70 ASP B N 1 ATOM 2217 C CA . ASP B 1 70 ? 27.460 19.326 -9.150 1.00 163.81 ? 70 ASP B CA 1 ATOM 2218 C C . ASP B 1 70 ? 28.306 19.233 -7.875 1.00 167.75 ? 70 ASP B C 1 ATOM 2219 O O . ASP B 1 70 ? 28.414 20.193 -7.107 1.00 170.55 ? 70 ASP B O 1 ATOM 2220 C CB . ASP B 1 70 ? 28.163 20.111 -10.242 1.00 163.94 ? 70 ASP B CB 1 ATOM 2221 C CG . ASP B 1 70 ? 29.462 19.476 -10.639 1.00 165.49 ? 70 ASP B CG 1 ATOM 2222 O OD1 . ASP B 1 70 ? 29.534 18.228 -10.597 1.00 161.80 ? 70 ASP B OD1 1 ATOM 2223 O OD2 . ASP B 1 70 ? 30.393 20.214 -11.015 1.00 169.57 ? 70 ASP B OD2 1 ATOM 2224 N N . ARG B 1 71 ? 28.891 18.061 -7.659 1.00 158.44 ? 71 ARG B N 1 ATOM 2225 C CA . ARG B 1 71 ? 29.583 17.711 -6.423 1.00 145.67 ? 71 ARG B CA 1 ATOM 2226 C C . ARG B 1 71 ? 30.830 18.564 -6.243 1.00 151.98 ? 71 ARG B C 1 ATOM 2227 O O . ARG B 1 71 ? 31.098 19.019 -5.132 1.00 149.25 ? 71 ARG B O 1 ATOM 2228 C CB . ARG B 1 71 ? 29.909 16.217 -6.444 1.00 134.33 ? 71 ARG B CB 1 ATOM 2229 C CG . ARG B 1 71 ? 30.286 15.797 -7.847 1.00 137.15 ? 71 ARG B CG 1 ATOM 2230 C CD . ARG B 1 71 ? 30.842 14.409 -7.983 1.00 133.43 ? 71 ARG B CD 1 ATOM 2231 N NE . ARG B 1 71 ? 30.831 14.051 -9.400 1.00 132.15 ? 71 ARG B NE 1 ATOM 2232 C CZ . ARG B 1 71 ? 31.222 12.880 -9.893 1.00 122.41 ? 71 ARG B CZ 1 ATOM 2233 N NH1 . ARG B 1 71 ? 31.703 11.934 -9.085 1.00 107.87 ? 71 ARG B NH1 1 ATOM 2234 N NH2 . ARG B 1 71 ? 31.152 12.669 -11.204 1.00 121.02 ? 71 ARG B NH2 1 ATOM 2235 N N . ASP B 1 72 ? 31.536 18.822 -7.347 1.00 161.87 ? 72 ASP B N 1 ATOM 2236 C CA . ASP B 1 72 ? 32.841 19.490 -7.359 1.00 173.10 ? 72 ASP B CA 1 ATOM 2237 C C . ASP B 1 72 ? 32.974 20.528 -6.270 1.00 177.75 ? 72 ASP B C 1 ATOM 2238 O O . ASP B 1 72 ? 33.886 20.497 -5.449 1.00 180.46 ? 72 ASP B O 1 ATOM 2239 C CB . ASP B 1 72 ? 33.034 20.250 -8.679 1.00 171.29 ? 72 ASP B CB 1 ATOM 2240 C CG . ASP B 1 72 ? 33.894 19.530 -9.682 1.00 168.58 ? 72 ASP B CG 1 ATOM 2241 O OD1 . ASP B 1 72 ? 34.710 18.664 -9.320 1.00 163.55 ? 72 ASP B OD1 1 ATOM 2242 O OD2 . ASP B 1 72 ? 33.768 19.889 -10.868 1.00 173.75 ? 72 ASP B OD2 1 ATOM 2243 N N . GLN B 1 73 ? 31.985 21.411 -6.239 1.00 185.28 ? 73 GLN B N 1 ATOM 2244 C CA . GLN B 1 73 ? 32.140 22.662 -5.534 1.00 188.28 ? 73 GLN B CA 1 ATOM 2245 C C . GLN B 1 73 ? 31.367 22.700 -4.229 1.00 188.24 ? 73 GLN B C 1 ATOM 2246 O O . GLN B 1 73 ? 31.322 23.725 -3.548 1.00 184.82 ? 73 GLN B O 1 ATOM 2247 C CB . GLN B 1 73 ? 31.744 23.830 -6.436 1.00 191.95 ? 73 GLN B CB 1 ATOM 2248 C CG . GLN B 1 73 ? 32.354 25.154 -6.001 1.00 200.58 ? 73 GLN B CG 1 ATOM 2249 C CD . GLN B 1 73 ? 33.825 25.259 -6.325 1.00 205.28 ? 73 GLN B CD 1 ATOM 2250 O OE1 . GLN B 1 73 ? 34.670 24.830 -5.542 1.00 205.43 ? 73 GLN B OE1 1 ATOM 2251 N NE2 . GLN B 1 73 ? 34.142 25.839 -7.477 1.00 204.09 ? 73 GLN B NE2 1 ATOM 2252 N N . TYR B 1 74 ? 30.762 21.599 -3.827 1.00 182.46 ? 74 TYR B N 1 ATOM 2253 C CA . TYR B 1 74 ? 30.453 21.517 -2.415 1.00 182.46 ? 74 TYR B CA 1 ATOM 2254 C C . TYR B 1 74 ? 31.234 20.400 -1.783 1.00 172.49 ? 74 TYR B C 1 ATOM 2255 O O . TYR B 1 74 ? 30.665 19.390 -1.334 1.00 169.51 ? 74 TYR B O 1 ATOM 2256 C CB . TYR B 1 74 ? 28.988 21.362 -2.061 1.00 191.06 ? 74 TYR B CB 1 ATOM 2257 C CG . TYR B 1 74 ? 28.812 21.973 -0.674 1.00 199.94 ? 74 TYR B CG 1 ATOM 2258 C CD1 . TYR B 1 74 ? 29.511 21.464 0.417 1.00 201.57 ? 74 TYR B CD1 1 ATOM 2259 C CD2 . TYR B 1 74 ? 28.025 23.103 -0.464 1.00 205.77 ? 74 TYR B CD2 1 ATOM 2260 C CE1 . TYR B 1 74 ? 29.416 22.023 1.669 1.00 206.91 ? 74 TYR B CE1 1 ATOM 2261 C CE2 . TYR B 1 74 ? 27.921 23.675 0.807 1.00 208.68 ? 74 TYR B CE2 1 ATOM 2262 C CZ . TYR B 1 74 ? 28.620 23.123 1.865 1.00 210.70 ? 74 TYR B CZ 1 ATOM 2263 O OH . TYR B 1 74 ? 28.520 23.672 3.123 1.00 213.92 ? 74 TYR B OH 1 ATOM 2264 N N . ASP B 1 75 ? 32.542 20.608 -1.732 1.00 166.29 ? 75 ASP B N 1 ATOM 2265 C CA . ASP B 1 75 ? 33.439 19.673 -1.097 1.00 158.78 ? 75 ASP B CA 1 ATOM 2266 C C . ASP B 1 75 ? 33.290 18.266 -1.653 1.00 157.82 ? 75 ASP B C 1 ATOM 2267 O O . ASP B 1 75 ? 33.565 17.283 -0.965 1.00 157.79 ? 75 ASP B O 1 ATOM 2268 C CB . ASP B 1 75 ? 33.145 19.699 0.405 1.00 151.31 ? 75 ASP B CB 1 ATOM 2269 C CG . ASP B 1 75 ? 34.329 19.334 1.232 1.00 140.13 ? 75 ASP B CG 1 ATOM 2270 O OD1 . ASP B 1 75 ? 35.133 20.245 1.519 1.00 138.91 ? 75 ASP B OD1 1 ATOM 2271 O OD2 . ASP B 1 75 ? 34.441 18.150 1.601 1.00 128.98 ? 75 ASP B OD2 1 ATOM 2272 N N . GLY B 1 76 ? 32.874 18.201 -2.917 1.00 159.47 ? 76 GLY B N 1 ATOM 2273 C CA . GLY B 1 76 ? 32.749 16.957 -3.652 1.00 153.70 ? 76 GLY B CA 1 ATOM 2274 C C . GLY B 1 76 ? 31.718 15.980 -3.119 1.00 146.37 ? 76 GLY B C 1 ATOM 2275 O O . GLY B 1 76 ? 31.872 14.776 -3.313 1.00 145.92 ? 76 GLY B O 1 ATOM 2276 N N . LEU B 1 77 ? 30.636 16.470 -2.518 1.00 141.34 ? 77 LEU B N 1 ATOM 2277 C CA . LEU B 1 77 ? 29.689 15.565 -1.864 1.00 133.05 ? 77 LEU B CA 1 ATOM 2278 C C . LEU B 1 77 ? 28.787 14.777 -2.815 1.00 135.00 ? 77 LEU B C 1 ATOM 2279 O O . LEU B 1 77 ? 27.888 15.319 -3.459 1.00 140.96 ? 77 LEU B O 1 ATOM 2280 C CB . LEU B 1 77 ? 28.817 16.350 -0.888 1.00 129.35 ? 77 LEU B CB 1 ATOM 2281 C CG . LEU B 1 77 ? 28.670 15.657 0.463 1.00 128.39 ? 77 LEU B CG 1 ATOM 2282 C CD1 . LEU B 1 77 ? 29.981 15.741 1.249 1.00 134.71 ? 77 LEU B CD1 1 ATOM 2283 C CD2 . LEU B 1 77 ? 27.501 16.236 1.250 1.00 125.73 ? 77 LEU B CD2 1 ATOM 2284 N N . ASP B 1 78 ? 29.043 13.474 -2.849 1.00 129.98 ? 78 ASP B N 1 ATOM 2285 C CA . ASP B 1 78 ? 28.391 12.511 -3.739 1.00 130.55 ? 78 ASP B CA 1 ATOM 2286 C C . ASP B 1 78 ? 26.923 12.179 -3.446 1.00 123.60 ? 78 ASP B C 1 ATOM 2287 O O . ASP B 1 78 ? 26.096 12.191 -4.348 1.00 122.83 ? 78 ASP B O 1 ATOM 2288 C CB . ASP B 1 78 ? 29.197 11.220 -3.739 1.00 132.06 ? 78 ASP B CB 1 ATOM 2289 C CG . ASP B 1 78 ? 29.635 10.833 -2.359 1.00 142.80 ? 78 ASP B CG 1 ATOM 2290 O OD1 . ASP B 1 78 ? 29.927 11.755 -1.567 1.00 144.29 ? 78 ASP B OD1 1 ATOM 2291 O OD2 . ASP B 1 78 ? 29.660 9.622 -2.051 1.00 145.84 ? 78 ASP B OD2 1 ATOM 2292 N N . SER B 1 79 ? 26.607 11.872 -2.193 1.00 119.02 ? 79 SER B N 1 ATOM 2293 C CA . SER B 1 79 ? 25.270 11.417 -1.835 1.00 122.18 ? 79 SER B CA 1 ATOM 2294 C C . SER B 1 79 ? 24.778 11.861 -0.477 1.00 130.50 ? 79 SER B C 1 ATOM 2295 O O . SER B 1 79 ? 25.539 11.943 0.492 1.00 133.00 ? 79 SER B O 1 ATOM 2296 C CB . SER B 1 79 ? 25.242 9.886 -1.797 1.00 125.35 ? 79 SER B CB 1 ATOM 2297 O OG . SER B 1 79 ? 25.502 9.438 -0.455 1.00 131.40 ? 79 SER B OG 1 ATOM 2298 N N . ILE B 1 80 ? 23.477 12.112 -0.404 1.00 119.73 ? 80 ILE B N 1 ATOM 2299 C CA . ILE B 1 80 ? 22.868 12.457 0.861 1.00 113.74 ? 80 ILE B CA 1 ATOM 2300 C C . ILE B 1 80 ? 21.644 11.580 1.048 1.00 124.24 ? 80 ILE B C 1 ATOM 2301 O O . ILE B 1 80 ? 20.945 11.245 0.083 1.00 122.50 ? 80 ILE B O 1 ATOM 2302 C CB . ILE B 1 80 ? 22.502 13.945 0.937 1.00 98.67 ? 80 ILE B CB 1 ATOM 2303 C CG1 . ILE B 1 80 ? 21.461 14.329 -0.091 1.00 93.43 ? 80 ILE B CG1 1 ATOM 2304 C CG2 . ILE B 1 80 ? 23.733 14.805 0.692 1.00 102.97 ? 80 ILE B CG2 1 ATOM 2305 C CD1 . ILE B 1 80 ? 21.290 15.832 -0.162 1.00 95.92 ? 80 ILE B CD1 1 ATOM 2306 N N . ARG B 1 81 ? 21.369 11.232 2.296 1.00 126.25 ? 81 ARG B N 1 ATOM 2307 C CA . ARG B 1 81 ? 20.170 10.488 2.621 1.00 128.03 ? 81 ARG B CA 1 ATOM 2308 C C . ARG B 1 81 ? 19.112 11.489 3.080 1.00 119.70 ? 81 ARG B C 1 ATOM 2309 O O . ARG B 1 81 ? 19.398 12.350 3.911 1.00 116.69 ? 81 ARG B O 1 ATOM 2310 C CB . ARG B 1 81 ? 20.485 9.464 3.701 1.00 131.42 ? 81 ARG B CB 1 ATOM 2311 C CG . ARG B 1 81 ? 21.780 8.716 3.421 1.00 138.29 ? 81 ARG B CG 1 ATOM 2312 C CD . ARG B 1 81 ? 21.573 7.240 3.229 1.00 141.21 ? 81 ARG B CD 1 ATOM 2313 N NE . ARG B 1 81 ? 22.856 6.549 3.154 1.00 153.63 ? 81 ARG B NE 1 ATOM 2314 C CZ . ARG B 1 81 ? 23.126 5.410 3.785 1.00 159.88 ? 81 ARG B CZ 1 ATOM 2315 N NH1 . ARG B 1 81 ? 22.195 4.817 4.528 1.00 165.04 ? 81 ARG B NH1 1 ATOM 2316 N NH2 . ARG B 1 81 ? 24.325 4.857 3.667 1.00 159.26 ? 81 ARG B NH2 1 ATOM 2317 N N . ILE B 1 82 ? 17.900 11.390 2.546 1.00 111.34 ? 82 ILE B N 1 ATOM 2318 C CA . ILE B 1 82 ? 16.830 12.295 2.943 1.00 104.19 ? 82 ILE B CA 1 ATOM 2319 C C . ILE B 1 82 ? 15.484 11.571 2.963 1.00 113.90 ? 82 ILE B C 1 ATOM 2320 O O . ILE B 1 82 ? 15.345 10.510 2.357 1.00 114.46 ? 82 ILE B O 1 ATOM 2321 C CB . ILE B 1 82 ? 16.754 13.496 2.017 1.00 99.33 ? 82 ILE B CB 1 ATOM 2322 C CG1 . ILE B 1 82 ? 16.994 13.049 0.589 1.00 108.61 ? 82 ILE B CG1 1 ATOM 2323 C CG2 . ILE B 1 82 ? 17.773 14.535 2.397 1.00 95.78 ? 82 ILE B CG2 1 ATOM 2324 C CD1 . ILE B 1 82 ? 16.938 14.185 -0.391 1.00 116.77 ? 82 ILE B CD1 1 ATOM 2325 N N . PRO B 1 83 ? 14.511 12.103 3.725 1.00 118.96 ? 83 PRO B N 1 ATOM 2326 C CA . PRO B 1 83 ? 13.192 11.476 3.840 1.00 120.61 ? 83 PRO B CA 1 ATOM 2327 C C . PRO B 1 83 ? 12.434 11.268 2.544 1.00 115.86 ? 83 PRO B C 1 ATOM 2328 O O . PRO B 1 83 ? 12.273 12.187 1.750 1.00 110.33 ? 83 PRO B O 1 ATOM 2329 C CB . PRO B 1 83 ? 12.420 12.452 4.728 1.00 126.03 ? 83 PRO B CB 1 ATOM 2330 C CG . PRO B 1 83 ? 13.449 13.044 5.589 1.00 129.25 ? 83 PRO B CG 1 ATOM 2331 C CD . PRO B 1 83 ? 14.680 13.175 4.722 1.00 127.93 ? 83 PRO B CD 1 ATOM 2332 N N . SER B 1 84 ? 11.943 10.050 2.373 1.00 114.25 ? 84 SER B N 1 ATOM 2333 C CA . SER B 1 84 ? 11.042 9.710 1.287 1.00 118.97 ? 84 SER B CA 1 ATOM 2334 C C . SER B 1 84 ? 9.811 10.619 1.319 1.00 123.81 ? 84 SER B C 1 ATOM 2335 O O . SER B 1 84 ? 9.190 10.908 0.291 1.00 135.33 ? 84 SER B O 1 ATOM 2336 C CB . SER B 1 84 ? 10.609 8.260 1.407 1.00 117.18 ? 84 SER B CB 1 ATOM 2337 O OG . SER B 1 84 ? 9.562 8.170 2.355 1.00 115.72 ? 84 SER B OG 1 ATOM 2338 N N . ASP B 1 85 ? 9.468 11.069 2.517 1.00 117.47 ? 85 ASP B N 1 ATOM 2339 C CA . ASP B 1 85 ? 8.299 11.898 2.737 1.00 121.30 ? 85 ASP B CA 1 ATOM 2340 C C . ASP B 1 85 ? 8.479 13.243 2.039 1.00 115.55 ? 85 ASP B C 1 ATOM 2341 O O . ASP B 1 85 ? 7.539 13.996 1.866 1.00 120.85 ? 85 ASP B O 1 ATOM 2342 C CB . ASP B 1 85 ? 8.119 12.091 4.258 1.00 127.85 ? 85 ASP B CB 1 ATOM 2343 C CG . ASP B 1 85 ? 6.813 12.778 4.640 1.00 133.35 ? 85 ASP B CG 1 ATOM 2344 O OD1 . ASP B 1 85 ? 5.961 13.001 3.764 1.00 134.51 ? 85 ASP B OD1 1 ATOM 2345 O OD2 . ASP B 1 85 ? 6.640 13.094 5.842 1.00 135.17 ? 85 ASP B OD2 1 ATOM 2346 N N . LEU B 1 86 ? 9.680 13.534 1.577 1.00 111.81 ? 86 LEU B N 1 ATOM 2347 C CA . LEU B 1 86 ? 9.912 14.880 1.102 1.00 114.05 ? 86 LEU B CA 1 ATOM 2348 C C . LEU B 1 86 ? 10.261 15.004 -0.401 1.00 114.30 ? 86 LEU B C 1 ATOM 2349 O O . LEU B 1 86 ? 10.549 16.106 -0.880 1.00 116.49 ? 86 LEU B O 1 ATOM 2350 C CB . LEU B 1 86 ? 10.968 15.532 1.988 1.00 118.63 ? 86 LEU B CB 1 ATOM 2351 C CG . LEU B 1 86 ? 10.767 17.046 2.105 1.00 122.01 ? 86 LEU B CG 1 ATOM 2352 C CD1 . LEU B 1 86 ? 9.280 17.407 2.264 1.00 121.00 ? 86 LEU B CD1 1 ATOM 2353 C CD2 . LEU B 1 86 ? 11.553 17.576 3.293 1.00 119.66 ? 86 LEU B CD2 1 ATOM 2354 N N . VAL B 1 87 ? 10.278 13.895 -1.142 1.00 109.07 ? 87 VAL B N 1 ATOM 2355 C CA . VAL B 1 87 ? 10.511 13.981 -2.597 1.00 102.54 ? 87 VAL B CA 1 ATOM 2356 C C . VAL B 1 87 ? 9.277 13.571 -3.422 1.00 114.25 ? 87 VAL B C 1 ATOM 2357 O O . VAL B 1 87 ? 8.422 12.853 -2.865 1.00 120.46 ? 87 VAL B O 1 ATOM 2358 C CB . VAL B 1 87 ? 11.726 13.104 -2.969 1.00 87.08 ? 87 VAL B CB 1 ATOM 2359 C CG1 . VAL B 1 87 ? 13.001 13.769 -2.512 1.00 88.01 ? 87 VAL B CG1 1 ATOM 2360 C CG2 . VAL B 1 87 ? 11.602 11.756 -2.329 1.00 76.72 ? 87 VAL B CG2 1 ATOM 2361 N N . TRP B 1 88 ? 9.139 14.067 -4.685 1.00 117.98 ? 88 TRP B N 1 ATOM 2362 C CA . TRP B 1 88 ? 7.995 13.685 -5.600 1.00 121.79 ? 88 TRP B CA 1 ATOM 2363 C C . TRP B 1 88 ? 7.957 12.258 -5.773 1.00 114.03 ? 88 TRP B C 1 ATOM 2364 O O . TRP B 1 88 ? 8.879 11.828 -6.295 1.00 121.85 ? 88 TRP B O 1 ATOM 2365 C CB . TRP B 1 88 ? 8.157 14.257 -7.006 1.00 122.53 ? 88 TRP B CB 1 ATOM 2366 C CG . TRP B 1 88 ? 7.159 13.667 -8.051 1.00 111.12 ? 88 TRP B CG 1 ATOM 2367 C CD1 . TRP B 1 88 ? 5.926 14.157 -8.383 1.00 114.79 ? 88 TRP B CD1 1 ATOM 2368 C CD2 . TRP B 1 88 ? 7.227 12.345 -8.693 1.00 106.95 ? 88 TRP B CD2 1 ATOM 2369 N NE1 . TRP B 1 88 ? 5.329 13.331 -9.308 1.00 122.46 ? 88 TRP B NE1 1 ATOM 2370 C CE2 . TRP B 1 88 ? 6.094 12.208 -9.485 1.00 116.17 ? 88 TRP B CE2 1 ATOM 2371 C CE3 . TRP B 1 88 ? 8.164 11.310 -8.716 1.00 103.94 ? 88 TRP B CE3 1 ATOM 2372 C CZ2 . TRP B 1 88 ? 5.869 11.095 -10.286 1.00 114.08 ? 88 TRP B CZ2 1 ATOM 2373 C CZ3 . TRP B 1 88 ? 7.928 10.203 -9.514 1.00 98.65 ? 88 TRP B CZ3 1 ATOM 2374 C CH2 . TRP B 1 88 ? 6.797 10.106 -10.279 1.00 100.90 ? 88 TRP B CH2 1 ATOM 2375 N N . ARG B 1 89 ? 6.928 11.474 -5.557 1.00 111.64 ? 89 ARG B N 1 ATOM 2376 C CA . ARG B 1 89 ? 7.240 10.052 -5.764 1.00 112.07 ? 89 ARG B CA 1 ATOM 2377 C C . ARG B 1 89 ? 6.238 9.108 -6.377 1.00 118.25 ? 89 ARG B C 1 ATOM 2378 O O . ARG B 1 89 ? 5.034 9.285 -6.249 1.00 122.03 ? 89 ARG B O 1 ATOM 2379 C CB . ARG B 1 89 ? 7.736 9.458 -4.463 1.00 127.57 ? 89 ARG B CB 1 ATOM 2380 C CG . ARG B 1 89 ? 9.067 10.135 -4.002 1.00 142.46 ? 89 ARG B CG 1 ATOM 2381 C CD . ARG B 1 89 ? 10.381 10.115 -4.979 1.00 150.94 ? 89 ARG B CD 1 ATOM 2382 N NE . ARG B 1 89 ? 11.151 11.382 -5.284 1.00 151.57 ? 89 ARG B NE 1 ATOM 2383 C CZ . ARG B 1 89 ? 11.304 12.108 -6.433 1.00 148.14 ? 89 ARG B CZ 1 ATOM 2384 N NH1 . ARG B 1 89 ? 10.833 11.767 -7.637 1.00 152.29 ? 89 ARG B NH1 1 ATOM 2385 N NH2 . ARG B 1 89 ? 11.917 13.272 -6.369 1.00 145.55 ? 89 ARG B NH2 1 ATOM 2386 N N . PRO B 1 90 ? 6.747 8.113 -7.102 1.00 103.80 ? 90 PRO B N 1 ATOM 2387 C CA . PRO B 1 90 ? 5.835 7.218 -7.806 1.00 108.62 ? 90 PRO B CA 1 ATOM 2388 C C . PRO B 1 90 ? 4.984 6.415 -6.821 1.00 104.11 ? 90 PRO B C 1 ATOM 2389 O O . PRO B 1 90 ? 5.470 5.634 -5.994 1.00 116.95 ? 90 PRO B O 1 ATOM 2390 C CB . PRO B 1 90 ? 6.774 6.314 -8.599 1.00 106.56 ? 90 PRO B CB 1 ATOM 2391 C CG . PRO B 1 90 ? 8.004 6.256 -7.782 1.00 98.13 ? 90 PRO B CG 1 ATOM 2392 C CD . PRO B 1 90 ? 8.134 7.609 -7.122 1.00 95.48 ? 90 PRO B CD 1 ATOM 2393 N N . ASP B 1 91 ? 3.686 6.652 -6.900 1.00 81.01 ? 91 ASP B N 1 ATOM 2394 C CA . ASP B 1 91 ? 2.772 6.075 -5.961 1.00 78.92 ? 91 ASP B CA 1 ATOM 2395 C C . ASP B 1 91 ? 2.662 4.589 -6.275 1.00 79.86 ? 91 ASP B C 1 ATOM 2396 O O . ASP B 1 91 ? 1.617 4.128 -6.717 1.00 92.92 ? 91 ASP B O 1 ATOM 2397 C CB . ASP B 1 91 ? 1.406 6.759 -6.042 1.00 89.27 ? 91 ASP B CB 1 ATOM 2398 C CG . ASP B 1 91 ? 1.457 8.213 -5.609 1.00 105.18 ? 91 ASP B CG 1 ATOM 2399 O OD1 . ASP B 1 91 ? 2.041 8.503 -4.555 1.00 120.03 ? 91 ASP B OD1 1 ATOM 2400 O OD2 . ASP B 1 91 ? 0.889 9.072 -6.313 1.00 109.05 ? 91 ASP B OD2 1 ATOM 2401 N N . ILE B 1 92 ? 3.751 3.844 -6.112 1.00 64.67 ? 92 ILE B N 1 ATOM 2402 C CA . ILE B 1 92 ? 3.705 2.424 -6.452 1.00 68.12 ? 92 ILE B CA 1 ATOM 2403 C C . ILE B 1 92 ? 3.142 1.525 -5.367 1.00 70.58 ? 92 ILE B C 1 ATOM 2404 O O . ILE B 1 92 ? 3.783 1.288 -4.325 1.00 76.84 ? 92 ILE B O 1 ATOM 2405 C CB . ILE B 1 92 ? 5.090 1.874 -6.825 1.00 75.26 ? 92 ILE B CB 1 ATOM 2406 C CG1 . ILE B 1 92 ? 5.528 2.486 -8.152 1.00 103.03 ? 92 ILE B CG1 1 ATOM 2407 C CG2 . ILE B 1 92 ? 5.054 0.330 -6.914 1.00 58.42 ? 92 ILE B CG2 1 ATOM 2408 C CD1 . ILE B 1 92 ? 6.705 1.810 -8.795 1.00 121.45 ? 92 ILE B CD1 1 ATOM 2409 N N . VAL B 1 93 ? 1.974 0.952 -5.638 1.00 59.19 ? 93 VAL B N 1 ATOM 2410 C CA . VAL B 1 93 ? 1.338 0.112 -4.634 1.00 60.74 ? 93 VAL B CA 1 ATOM 2411 C C . VAL B 1 93 ? 1.211 -1.357 -5.085 1.00 59.58 ? 93 VAL B C 1 ATOM 2412 O O . VAL B 1 93 ? 1.409 -1.700 -6.275 1.00 69.18 ? 93 VAL B O 1 ATOM 2413 C CB . VAL B 1 93 ? -0.061 0.654 -4.294 1.00 80.68 ? 93 VAL B CB 1 ATOM 2414 C CG1 . VAL B 1 93 ? -0.117 2.151 -4.609 1.00 82.07 ? 93 VAL B CG1 1 ATOM 2415 C CG2 . VAL B 1 93 ? -1.155 -0.072 -5.117 1.00 69.00 ? 93 VAL B CG2 1 ATOM 2416 N N . LEU B 1 94 ? 0.778 -2.208 -4.162 1.00 54.94 ? 94 LEU B N 1 ATOM 2417 C CA . LEU B 1 94 ? 0.450 -3.556 -4.547 1.00 60.85 ? 94 LEU B CA 1 ATOM 2418 C C . LEU B 1 94 ? -0.985 -3.516 -5.023 1.00 74.90 ? 94 LEU B C 1 ATOM 2419 O O . LEU B 1 94 ? -1.886 -3.261 -4.231 1.00 69.93 ? 94 LEU B O 1 ATOM 2420 C CB . LEU B 1 94 ? 0.575 -4.523 -3.407 1.00 58.46 ? 94 LEU B CB 1 ATOM 2421 C CG . LEU B 1 94 ? 0.415 -5.913 -3.986 1.00 75.34 ? 94 LEU B CG 1 ATOM 2422 C CD1 . LEU B 1 94 ? 1.730 -6.390 -4.503 1.00 90.39 ? 94 LEU B CD1 1 ATOM 2423 C CD2 . LEU B 1 94 ? -0.071 -6.849 -2.936 1.00 85.38 ? 94 LEU B CD2 1 ATOM 2424 N N . TYR B 1 95 ? -1.144 -3.755 -6.329 1.00 82.75 ? 95 TYR B N 1 ATOM 2425 C CA . TYR B 1 95 ? -2.413 -3.822 -7.041 1.00 72.67 ? 95 TYR B CA 1 ATOM 2426 C C . TYR B 1 95 ? -3.196 -5.033 -6.591 1.00 62.36 ? 95 TYR B C 1 ATOM 2427 O O . TYR B 1 95 ? -4.424 -4.989 -6.485 1.00 67.57 ? 95 TYR B O 1 ATOM 2428 C CB . TYR B 1 95 ? -2.208 -3.956 -8.583 1.00 113.38 ? 95 TYR B CB 1 ATOM 2429 C CG . TYR B 1 95 ? -1.970 -2.705 -9.444 1.00 87.32 ? 95 TYR B CG 1 ATOM 2430 C CD1 . TYR B 1 95 ? -1.364 -1.556 -8.941 1.00 77.08 ? 95 TYR B CD1 1 ATOM 2431 C CD2 . TYR B 1 95 ? -2.463 -2.652 -10.737 1.00 95.71 ? 95 TYR B CD2 1 ATOM 2432 C CE1 . TYR B 1 95 ? -1.184 -0.422 -9.723 1.00 65.40 ? 95 TYR B CE1 1 ATOM 2433 C CE2 . TYR B 1 95 ? -2.307 -1.522 -11.524 1.00 94.86 ? 95 TYR B CE2 1 ATOM 2434 C CZ . TYR B 1 95 ? -1.666 -0.414 -11.015 1.00 87.59 ? 95 TYR B CZ 1 ATOM 2435 O OH . TYR B 1 95 ? -1.530 0.692 -11.822 1.00 88.19 ? 95 TYR B OH 1 ATOM 2436 N N . ASN B 1 96 ? -2.443 -6.107 -6.342 1.00 61.05 ? 96 ASN B N 1 ATOM 2437 C CA . ASN B 1 96 ? -2.936 -7.446 -6.010 1.00 66.99 ? 96 ASN B CA 1 ATOM 2438 C C . ASN B 1 96 ? -3.401 -7.695 -4.517 1.00 100.26 ? 96 ASN B C 1 ATOM 2439 O O . ASN B 1 96 ? -3.848 -8.809 -4.167 1.00 86.00 ? 96 ASN B O 1 ATOM 2440 C CB . ASN B 1 96 ? -1.832 -8.434 -6.429 1.00 59.20 ? 96 ASN B CB 1 ATOM 2441 C CG . ASN B 1 96 ? -2.284 -9.881 -6.394 1.00 78.12 ? 96 ASN B CG 1 ATOM 2442 O OD1 . ASN B 1 96 ? -3.473 -10.178 -6.421 1.00 95.73 ? 96 ASN B OD1 1 ATOM 2443 N ND2 . ASN B 1 96 ? -1.330 -10.792 -6.345 1.00 68.99 ? 96 ASN B ND2 1 ATOM 2444 N N . LYS B 1 97 ? -3.282 -6.657 -3.669 1.00 103.49 ? 97 LYS B N 1 ATOM 2445 C CA . LYS B 1 97 ? -3.547 -6.674 -2.207 1.00 96.58 ? 97 LYS B CA 1 ATOM 2446 C C . LYS B 1 97 ? -4.765 -7.490 -1.786 1.00 93.92 ? 97 LYS B C 1 ATOM 2447 O O . LYS B 1 97 ? -5.630 -7.791 -2.604 1.00 91.11 ? 97 LYS B O 1 ATOM 2448 C CB . LYS B 1 97 ? -3.732 -5.235 -1.707 1.00 96.30 ? 97 LYS B CB 1 ATOM 2449 C CG . LYS B 1 97 ? -3.290 -4.983 -0.278 1.00 121.11 ? 97 LYS B CG 1 ATOM 2450 C CD . LYS B 1 97 ? -3.171 -3.483 0.029 1.00 124.23 ? 97 LYS B CD 1 ATOM 2451 C CE . LYS B 1 97 ? -2.825 -2.640 -1.203 1.00 119.76 ? 97 LYS B CE 1 ATOM 2452 N NZ . LYS B 1 97 ? -2.908 -1.161 -0.959 1.00 115.51 ? 97 LYS B NZ 1 ATOM 2453 N N . ALA B 1 98 ? -4.893 -7.779 -0.495 1.00 90.42 ? 98 ALA B N 1 ATOM 2454 C CA . ALA B 1 98 ? -6.087 -8.488 -0.008 1.00 86.20 ? 98 ALA B CA 1 ATOM 2455 C C . ALA B 1 98 ? -6.683 -7.843 1.231 1.00 95.53 ? 98 ALA B C 1 ATOM 2456 O O . ALA B 1 98 ? -7.819 -8.121 1.587 1.00 107.18 ? 98 ALA B O 1 ATOM 2457 C CB . ALA B 1 98 ? -5.771 -9.955 0.273 1.00 72.94 ? 98 ALA B CB 1 ATOM 2458 N N . ASP B 1 99 ? -5.909 -7.001 1.898 1.00 99.82 ? 99 ASP B N 1 ATOM 2459 C CA . ASP B 1 99 ? -6.354 -6.347 3.126 1.00 104.39 ? 99 ASP B CA 1 ATOM 2460 C C . ASP B 1 99 ? -5.975 -4.869 3.062 1.00 100.79 ? 99 ASP B C 1 ATOM 2461 O O . ASP B 1 99 ? -6.424 -4.153 2.160 1.00 91.40 ? 99 ASP B O 1 ATOM 2462 N N . PRO B 1 105 ? 4.823 0.737 4.901 1.00 127.21 ? 105 PRO B N 1 ATOM 2463 C CA . PRO B 1 105 ? 4.112 0.659 6.182 1.00 126.63 ? 105 PRO B CA 1 ATOM 2464 C C . PRO B 1 105 ? 5.120 0.800 7.325 1.00 138.94 ? 105 PRO B C 1 ATOM 2465 O O . PRO B 1 105 ? 5.116 0.007 8.279 1.00 128.14 ? 105 PRO B O 1 ATOM 2466 C CB . PRO B 1 105 ? 3.485 -0.743 6.159 1.00 127.73 ? 105 PRO B CB 1 ATOM 2467 C CG . PRO B 1 105 ? 3.571 -1.232 4.733 1.00 129.15 ? 105 PRO B CG 1 ATOM 2468 C CD . PRO B 1 105 ? 4.321 -0.225 3.904 1.00 131.33 ? 105 PRO B CD 1 ATOM 2469 N N . VAL B 1 106 ? 5.967 1.825 7.197 1.00 143.39 ? 106 VAL B N 1 ATOM 2470 C CA . VAL B 1 106 ? 7.100 2.160 8.086 1.00 145.85 ? 106 VAL B CA 1 ATOM 2471 C C . VAL B 1 106 ? 8.059 3.062 7.315 1.00 150.51 ? 106 VAL B C 1 ATOM 2472 O O . VAL B 1 106 ? 8.917 2.579 6.554 1.00 152.73 ? 106 VAL B O 1 ATOM 2473 C CB . VAL B 1 106 ? 7.897 0.923 8.614 1.00 141.08 ? 106 VAL B CB 1 ATOM 2474 C CG1 . VAL B 1 106 ? 8.049 -0.167 7.551 1.00 141.53 ? 106 VAL B CG1 1 ATOM 2475 C CG2 . VAL B 1 106 ? 9.278 1.346 9.131 1.00 139.67 ? 106 VAL B CG2 1 ATOM 2476 N N . ASN B 1 107 ? 7.916 4.375 7.460 1.00 146.47 ? 107 ASN B N 1 ATOM 2477 C CA . ASN B 1 107 ? 8.576 5.225 6.482 1.00 138.28 ? 107 ASN B CA 1 ATOM 2478 C C . ASN B 1 107 ? 10.075 5.271 6.764 1.00 118.44 ? 107 ASN B C 1 ATOM 2479 O O . ASN B 1 107 ? 10.522 5.091 7.892 1.00 119.65 ? 107 ASN B O 1 ATOM 2480 C CB . ASN B 1 107 ? 7.975 6.629 6.439 1.00 142.18 ? 107 ASN B CB 1 ATOM 2481 C CG . ASN B 1 107 ? 8.524 7.461 5.275 1.00 145.11 ? 107 ASN B CG 1 ATOM 2482 O OD1 . ASN B 1 107 ? 9.115 6.924 4.337 1.00 147.83 ? 107 ASN B OD1 1 ATOM 2483 N ND2 . ASN B 1 107 ? 8.325 8.775 5.332 1.00 142.92 ? 107 ASN B ND2 1 ATOM 2484 N N . THR B 1 108 ? 10.827 5.485 5.694 1.00 102.20 ? 108 THR B N 1 ATOM 2485 C CA . THR B 1 108 ? 12.269 5.421 5.666 1.00 86.86 ? 108 THR B CA 1 ATOM 2486 C C . THR B 1 108 ? 12.794 6.561 4.828 1.00 92.01 ? 108 THR B C 1 ATOM 2487 O O . THR B 1 108 ? 12.071 7.502 4.508 1.00 98.45 ? 108 THR B O 1 ATOM 2488 C CB . THR B 1 108 ? 12.761 4.114 5.059 1.00 75.19 ? 108 THR B CB 1 ATOM 2489 O OG1 . THR B 1 108 ? 12.578 4.155 3.630 1.00 72.39 ? 108 THR B OG1 1 ATOM 2490 C CG2 . THR B 1 108 ? 12.008 2.918 5.662 1.00 59.23 ? 108 THR B CG2 1 ATOM 2491 N N . ASN B 1 109 ? 14.055 6.469 4.450 1.00 108.13 ? 109 ASN B N 1 ATOM 2492 C CA . ASN B 1 109 ? 14.660 7.590 3.779 1.00 120.13 ? 109 ASN B CA 1 ATOM 2493 C C . ASN B 1 109 ? 15.294 7.185 2.454 1.00 115.00 ? 109 ASN B C 1 ATOM 2494 O O . ASN B 1 109 ? 15.563 6.010 2.212 1.00 125.85 ? 109 ASN B O 1 ATOM 2495 C CB . ASN B 1 109 ? 15.691 8.221 4.718 1.00 130.73 ? 109 ASN B CB 1 ATOM 2496 C CG . ASN B 1 109 ? 15.051 8.772 5.996 1.00 143.50 ? 109 ASN B CG 1 ATOM 2497 O OD1 . ASN B 1 109 ? 14.447 9.842 5.995 1.00 149.77 ? 109 ASN B OD1 1 ATOM 2498 N ND2 . ASN B 1 109 ? 15.189 8.030 7.095 1.00 141.48 ? 109 ASN B ND2 1 ATOM 2499 N N . VAL B 1 110 ? 15.521 8.168 1.592 1.00 106.03 ? 110 VAL B N 1 ATOM 2500 C CA . VAL B 1 110 ? 15.932 7.874 0.226 1.00 110.34 ? 110 VAL B CA 1 ATOM 2501 C C . VAL B 1 110 ? 17.318 8.480 0.003 1.00 110.80 ? 110 VAL B C 1 ATOM 2502 O O . VAL B 1 110 ? 17.630 9.567 0.495 1.00 112.60 ? 110 VAL B O 1 ATOM 2503 C CB . VAL B 1 110 ? 14.879 8.385 -0.882 1.00 87.92 ? 110 VAL B CB 1 ATOM 2504 C CG1 . VAL B 1 110 ? 13.459 7.810 -0.643 1.00 59.62 ? 110 VAL B CG1 1 ATOM 2505 C CG2 . VAL B 1 110 ? 14.820 9.917 -0.998 1.00 75.07 ? 110 VAL B CG2 1 ATOM 2506 N N . VAL B 1 111 ? 18.158 7.746 -0.714 1.00 106.41 ? 111 VAL B N 1 ATOM 2507 C CA . VAL B 1 111 ? 19.485 8.221 -1.062 1.00 111.92 ? 111 VAL B CA 1 ATOM 2508 C C . VAL B 1 111 ? 19.485 8.985 -2.392 1.00 118.31 ? 111 VAL B C 1 ATOM 2509 O O . VAL B 1 111 ? 19.516 8.385 -3.479 1.00 124.84 ? 111 VAL B O 1 ATOM 2510 C CB . VAL B 1 111 ? 20.493 7.056 -1.151 1.00 110.64 ? 111 VAL B CB 1 ATOM 2511 C CG1 . VAL B 1 111 ? 21.924 7.590 -1.296 1.00 106.64 ? 111 VAL B CG1 1 ATOM 2512 C CG2 . VAL B 1 111 ? 20.387 6.187 0.072 1.00 111.04 ? 111 VAL B CG2 1 ATOM 2513 N N . LEU B 1 112 ? 19.446 10.310 -2.305 1.00 115.52 ? 112 LEU B N 1 ATOM 2514 C CA . LEU B 1 112 ? 19.547 11.156 -3.490 1.00 111.93 ? 112 LEU B CA 1 ATOM 2515 C C . LEU B 1 112 ? 21.016 11.328 -3.879 1.00 105.90 ? 112 LEU B C 1 ATOM 2516 O O . LEU B 1 112 ? 21.859 11.552 -3.016 1.00 96.11 ? 112 LEU B O 1 ATOM 2517 C CB . LEU B 1 112 ? 18.893 12.517 -3.233 1.00 107.22 ? 112 LEU B CB 1 ATOM 2518 C CG . LEU B 1 112 ? 19.227 13.644 -4.214 1.00 104.40 ? 112 LEU B CG 1 ATOM 2519 C CD1 . LEU B 1 112 ? 18.652 13.370 -5.571 1.00 103.63 ? 112 LEU B CD1 1 ATOM 2520 C CD2 . LEU B 1 112 ? 18.737 14.981 -3.685 1.00 107.37 ? 112 LEU B CD2 1 ATOM 2521 N N . ARG B 1 113 ? 21.324 11.191 -5.167 1.00 106.85 ? 113 ARG B N 1 ATOM 2522 C CA . ARG B 1 113 ? 22.699 11.357 -5.638 1.00 111.69 ? 113 ARG B CA 1 ATOM 2523 C C . ARG B 1 113 ? 22.882 12.763 -6.214 1.00 117.09 ? 113 ARG B C 1 ATOM 2524 O O . ARG B 1 113 ? 21.902 13.494 -6.355 1.00 119.98 ? 113 ARG B O 1 ATOM 2525 C CB . ARG B 1 113 ? 23.054 10.278 -6.669 1.00 110.58 ? 113 ARG B CB 1 ATOM 2526 C CG . ARG B 1 113 ? 24.550 9.957 -6.743 1.00 111.24 ? 113 ARG B CG 1 ATOM 2527 C CD . ARG B 1 113 ? 24.819 8.645 -7.467 1.00 106.81 ? 113 ARG B CD 1 ATOM 2528 N NE . ARG B 1 113 ? 24.381 8.675 -8.864 1.00 110.63 ? 113 ARG B NE 1 ATOM 2529 C CZ . ARG B 1 113 ? 24.426 7.617 -9.670 1.00 108.18 ? 113 ARG B CZ 1 ATOM 2530 N NH1 . ARG B 1 113 ? 24.893 6.463 -9.197 1.00 105.71 ? 113 ARG B NH1 1 ATOM 2531 N NH2 . ARG B 1 113 ? 24.010 7.702 -10.936 1.00 102.16 ? 113 ARG B NH2 1 ATOM 2532 N N . TYR B 1 114 ? 24.126 13.145 -6.518 1.00 117.13 ? 114 TYR B N 1 ATOM 2533 C CA . TYR B 1 114 ? 24.424 14.490 -7.025 1.00 121.39 ? 114 TYR B CA 1 ATOM 2534 C C . TYR B 1 114 ? 23.806 14.722 -8.408 1.00 124.77 ? 114 TYR B C 1 ATOM 2535 O O . TYR B 1 114 ? 23.394 15.844 -8.743 1.00 126.50 ? 114 TYR B O 1 ATOM 2536 C CB . TYR B 1 114 ? 25.941 14.728 -7.080 1.00 119.51 ? 114 TYR B CB 1 ATOM 2537 C CG . TYR B 1 114 ? 26.646 13.955 -8.175 1.00 114.14 ? 114 TYR B CG 1 ATOM 2538 C CD1 . TYR B 1 114 ? 27.039 12.634 -7.978 1.00 111.57 ? 114 TYR B CD1 1 ATOM 2539 C CD2 . TYR B 1 114 ? 26.920 14.546 -9.403 1.00 110.34 ? 114 TYR B CD2 1 ATOM 2540 C CE1 . TYR B 1 114 ? 27.673 11.922 -8.976 1.00 107.25 ? 114 TYR B CE1 1 ATOM 2541 C CE2 . TYR B 1 114 ? 27.556 13.841 -10.407 1.00 109.51 ? 114 TYR B CE2 1 ATOM 2542 C CZ . TYR B 1 114 ? 27.926 12.528 -10.184 1.00 109.30 ? 114 TYR B CZ 1 ATOM 2543 O OH . TYR B 1 114 ? 28.552 11.812 -11.172 1.00 114.10 ? 114 TYR B OH 1 ATOM 2544 N N . ASP B 1 115 ? 23.715 13.650 -9.196 1.00 121.86 ? 115 ASP B N 1 ATOM 2545 C CA . ASP B 1 115 ? 23.116 13.730 -10.522 1.00 112.65 ? 115 ASP B CA 1 ATOM 2546 C C . ASP B 1 115 ? 21.611 13.549 -10.418 1.00 115.54 ? 115 ASP B C 1 ATOM 2547 O O . ASP B 1 115 ? 20.926 13.377 -11.435 1.00 125.37 ? 115 ASP B O 1 ATOM 2548 C CB . ASP B 1 115 ? 23.709 12.678 -11.468 1.00 103.45 ? 115 ASP B CB 1 ATOM 2549 C CG . ASP B 1 115 ? 23.441 11.256 -11.004 1.00 100.31 ? 115 ASP B CG 1 ATOM 2550 O OD1 . ASP B 1 115 ? 23.283 11.052 -9.785 1.00 97.83 ? 115 ASP B OD1 1 ATOM 2551 O OD2 . ASP B 1 115 ? 23.376 10.343 -11.857 1.00 98.81 ? 115 ASP B OD2 1 ATOM 2552 N N . GLY B 1 116 ? 21.096 13.588 -9.191 1.00 106.69 ? 116 GLY B N 1 ATOM 2553 C CA . GLY B 1 116 ? 19.659 13.527 -8.985 1.00 107.62 ? 116 GLY B CA 1 ATOM 2554 C C . GLY B 1 116 ? 19.022 12.147 -9.062 1.00 102.48 ? 116 GLY B C 1 ATOM 2555 O O . GLY B 1 116 ? 17.811 12.028 -9.294 1.00 96.29 ? 116 GLY B O 1 ATOM 2556 N N . LEU B 1 117 ? 19.832 11.104 -8.894 1.00 96.50 ? 117 LEU B N 1 ATOM 2557 C CA . LEU B 1 117 ? 19.320 9.738 -8.833 1.00 87.23 ? 117 LEU B CA 1 ATOM 2558 C C . LEU B 1 117 ? 18.794 9.446 -7.441 1.00 105.16 ? 117 LEU B C 1 ATOM 2559 O O . LEU B 1 117 ? 19.474 9.716 -6.440 1.00 120.79 ? 117 LEU B O 1 ATOM 2560 C CB . LEU B 1 117 ? 20.413 8.734 -9.174 1.00 83.10 ? 117 LEU B CB 1 ATOM 2561 C CG . LEU B 1 117 ? 20.049 7.260 -8.970 1.00 74.45 ? 117 LEU B CG 1 ATOM 2562 C CD1 . LEU B 1 117 ? 19.382 6.675 -10.126 1.00 62.21 ? 117 LEU B CD1 1 ATOM 2563 C CD2 . LEU B 1 117 ? 21.260 6.443 -8.625 1.00 88.79 ? 117 LEU B CD2 1 ATOM 2564 N N . ILE B 1 118 ? 17.599 8.873 -7.350 1.00 95.18 ? 118 ILE B N 1 ATOM 2565 C CA . ILE B 1 118 ? 17.045 8.652 -6.026 1.00 81.12 ? 118 ILE B CA 1 ATOM 2566 C C . ILE B 1 118 ? 16.861 7.169 -5.721 1.00 88.60 ? 118 ILE B C 1 ATOM 2567 O O . ILE B 1 118 ? 16.211 6.434 -6.455 1.00 78.84 ? 118 ILE B O 1 ATOM 2568 C CB . ILE B 1 118 ? 15.713 9.374 -5.869 1.00 66.15 ? 118 ILE B CB 1 ATOM 2569 C CG1 . ILE B 1 118 ? 15.938 10.855 -5.586 1.00 71.52 ? 118 ILE B CG1 1 ATOM 2570 C CG2 . ILE B 1 118 ? 14.896 8.762 -4.799 1.00 56.31 ? 118 ILE B CG2 1 ATOM 2571 C CD1 . ILE B 1 118 ? 14.657 11.589 -5.355 1.00 59.40 ? 118 ILE B CD1 1 ATOM 2572 N N . THR B 1 119 ? 17.373 6.743 -4.575 1.00 107.07 ? 119 THR B N 1 ATOM 2573 C CA . THR B 1 119 ? 17.281 5.336 -4.219 1.00 104.08 ? 119 THR B CA 1 ATOM 2574 C C . THR B 1 119 ? 16.463 5.049 -2.973 1.00 96.92 ? 119 THR B C 1 ATOM 2575 O O . THR B 1 119 ? 16.887 5.317 -1.857 1.00 99.27 ? 119 THR B O 1 ATOM 2576 C CB . THR B 1 119 ? 18.653 4.750 -4.002 1.00 89.20 ? 119 THR B CB 1 ATOM 2577 O OG1 . THR B 1 119 ? 19.436 4.936 -5.201 1.00 81.72 ? 119 THR B OG1 1 ATOM 2578 C CG2 . THR B 1 119 ? 18.512 3.272 -3.607 1.00 80.58 ? 119 THR B CG2 1 ATOM 2579 N N . TRP B 1 120 ? 15.298 4.457 -3.197 1.00 84.94 ? 120 TRP B N 1 ATOM 2580 C CA . TRP B 1 120 ? 14.352 4.186 -2.151 1.00 76.40 ? 120 TRP B CA 1 ATOM 2581 C C . TRP B 1 120 ? 14.227 2.697 -1.890 1.00 83.50 ? 120 TRP B C 1 ATOM 2582 O O . TRP B 1 120 ? 13.502 1.996 -2.600 1.00 82.82 ? 120 TRP B O 1 ATOM 2583 C CB . TRP B 1 120 ? 13.001 4.767 -2.515 1.00 71.93 ? 120 TRP B CB 1 ATOM 2584 C CG . TRP B 1 120 ? 12.027 4.737 -1.396 1.00 91.63 ? 120 TRP B CG 1 ATOM 2585 C CD1 . TRP B 1 120 ? 12.310 4.691 -0.061 1.00 92.06 ? 120 TRP B CD1 1 ATOM 2586 C CD2 . TRP B 1 120 ? 10.590 4.748 -1.504 1.00 100.43 ? 120 TRP B CD2 1 ATOM 2587 N NE1 . TRP B 1 120 ? 11.144 4.678 0.665 1.00 96.46 ? 120 TRP B NE1 1 ATOM 2588 C CE2 . TRP B 1 120 ? 10.075 4.715 -0.196 1.00 97.96 ? 120 TRP B CE2 1 ATOM 2589 C CE3 . TRP B 1 120 ? 9.693 4.800 -2.583 1.00 105.67 ? 120 TRP B CE3 1 ATOM 2590 C CZ2 . TRP B 1 120 ? 8.706 4.718 0.065 1.00 100.99 ? 120 TRP B CZ2 1 ATOM 2591 C CZ3 . TRP B 1 120 ? 8.327 4.801 -2.321 1.00 106.57 ? 120 TRP B CZ3 1 ATOM 2592 C CH2 . TRP B 1 120 ? 7.849 4.759 -1.012 1.00 104.15 ? 120 TRP B CH2 1 ATOM 2593 N N . ASP B 1 121 ? 14.919 2.226 -0.851 1.00 89.17 ? 121 ASP B N 1 ATOM 2594 C CA . ASP B 1 121 ? 14.608 0.927 -0.275 1.00 80.06 ? 121 ASP B CA 1 ATOM 2595 C C . ASP B 1 121 ? 13.604 1.134 0.839 1.00 87.52 ? 121 ASP B C 1 ATOM 2596 O O . ASP B 1 121 ? 13.580 2.192 1.474 1.00 97.90 ? 121 ASP B O 1 ATOM 2597 C CB . ASP B 1 121 ? 15.841 0.246 0.295 1.00 71.48 ? 121 ASP B CB 1 ATOM 2598 C CG . ASP B 1 121 ? 16.646 -0.482 -0.731 1.00 82.50 ? 121 ASP B CG 1 ATOM 2599 O OD1 . ASP B 1 121 ? 17.452 0.176 -1.417 1.00 93.46 ? 121 ASP B OD1 1 ATOM 2600 O OD2 . ASP B 1 121 ? 16.481 -1.722 -0.837 1.00 84.45 ? 121 ASP B OD2 1 ATOM 2601 N N . ALA B 1 122 ? 12.745 0.146 1.057 1.00 79.44 ? 122 ALA B N 1 ATOM 2602 C CA . ALA B 1 122 ? 11.708 0.278 2.078 1.00 70.70 ? 122 ALA B CA 1 ATOM 2603 C C . ALA B 1 122 ? 11.086 -1.084 2.408 1.00 74.87 ? 122 ALA B C 1 ATOM 2604 O O . ALA B 1 122 ? 11.173 -2.042 1.611 1.00 68.36 ? 122 ALA B O 1 ATOM 2605 C CB . ALA B 1 122 ? 10.686 1.240 1.648 1.00 69.84 ? 122 ALA B CB 1 ATOM 2606 N N . PRO B 1 123 ? 10.529 -1.218 3.620 1.00 76.39 ? 123 PRO B N 1 ATOM 2607 C CA . PRO B 1 123 ? 10.112 -2.579 3.936 1.00 75.57 ? 123 PRO B CA 1 ATOM 2608 C C . PRO B 1 123 ? 8.606 -2.715 3.810 1.00 72.87 ? 123 PRO B C 1 ATOM 2609 O O . PRO B 1 123 ? 7.895 -1.704 3.828 1.00 77.70 ? 123 PRO B O 1 ATOM 2610 C CB . PRO B 1 123 ? 10.610 -2.762 5.369 1.00 73.41 ? 123 PRO B CB 1 ATOM 2611 C CG . PRO B 1 123 ? 10.583 -1.397 5.916 1.00 76.98 ? 123 PRO B CG 1 ATOM 2612 C CD . PRO B 1 123 ? 10.474 -0.370 4.816 1.00 72.31 ? 123 PRO B CD 1 ATOM 2613 N N . ALA B 1 124 ? 8.125 -3.942 3.649 1.00 66.96 ? 124 ALA B N 1 ATOM 2614 C CA . ALA B 1 124 ? 6.724 -4.097 3.402 1.00 77.84 ? 124 ALA B CA 1 ATOM 2615 C C . ALA B 1 124 ? 6.124 -5.369 4.007 1.00 83.15 ? 124 ALA B C 1 ATOM 2616 O O . ALA B 1 124 ? 6.825 -6.382 4.195 1.00 76.22 ? 124 ALA B O 1 ATOM 2617 C CB . ALA B 1 124 ? 6.488 -4.032 1.878 1.00 67.46 ? 124 ALA B CB 1 ATOM 2618 N N . ILE B 1 125 ? 4.827 -5.299 4.319 1.00 80.33 ? 125 ILE B N 1 ATOM 2619 C CA . ILE B 1 125 ? 4.037 -6.507 4.502 1.00 72.04 ? 125 ILE B CA 1 ATOM 2620 C C . ILE B 1 125 ? 2.863 -6.585 3.445 1.00 71.53 ? 125 ILE B C 1 ATOM 2621 O O . ILE B 1 125 ? 2.273 -5.548 3.008 1.00 53.50 ? 125 ILE B O 1 ATOM 2622 C CB . ILE B 1 125 ? 3.513 -6.599 5.920 1.00 66.26 ? 125 ILE B CB 1 ATOM 2623 C CG1 . ILE B 1 125 ? 4.494 -5.979 6.895 1.00 76.67 ? 125 ILE B CG1 1 ATOM 2624 C CG2 . ILE B 1 125 ? 3.121 -8.057 6.302 1.00 77.01 ? 125 ILE B CG2 1 ATOM 2625 C CD1 . ILE B 1 125 ? 4.083 -6.163 8.389 1.00 56.62 ? 125 ILE B CD1 1 ATOM 2626 N N . THR B 1 126 ? 2.617 -7.798 2.941 1.00 60.23 ? 126 THR B N 1 ATOM 2627 C CA . THR B 1 126 ? 1.589 -7.952 1.928 1.00 73.98 ? 126 THR B CA 1 ATOM 2628 C C . THR B 1 126 ? 0.701 -9.139 2.153 1.00 79.51 ? 126 THR B C 1 ATOM 2629 O O . THR B 1 126 ? 1.174 -10.251 2.457 1.00 78.47 ? 126 THR B O 1 ATOM 2630 C CB . THR B 1 126 ? 2.149 -8.103 0.500 1.00 77.31 ? 126 THR B CB 1 ATOM 2631 O OG1 . THR B 1 126 ? 2.739 -9.402 0.343 1.00 75.96 ? 126 THR B OG1 1 ATOM 2632 C CG2 . THR B 1 126 ? 3.126 -6.989 0.162 1.00 63.31 ? 126 THR B CG2 1 ATOM 2633 N N . LYS B 1 127 ? -0.592 -8.897 1.971 1.00 78.39 ? 127 LYS B N 1 ATOM 2634 C CA . LYS B 1 127 ? -1.530 -9.991 1.930 1.00 87.22 ? 127 LYS B CA 1 ATOM 2635 C C . LYS B 1 127 ? -2.101 -9.983 0.531 1.00 85.54 ? 127 LYS B C 1 ATOM 2636 O O . LYS B 1 127 ? -2.693 -8.993 0.090 1.00 92.60 ? 127 LYS B O 1 ATOM 2637 C CB . LYS B 1 127 ? -2.612 -9.864 3.026 1.00 84.08 ? 127 LYS B CB 1 ATOM 2638 C CG . LYS B 1 127 ? -2.177 -9.038 4.267 1.00 83.10 ? 127 LYS B CG 1 ATOM 2639 C CD . LYS B 1 127 ? -2.698 -9.586 5.620 1.00 73.03 ? 127 LYS B CD 1 ATOM 2640 C CE . LYS B 1 127 ? -2.857 -8.488 6.706 1.00 85.04 ? 127 LYS B CE 1 ATOM 2641 N NZ . LYS B 1 127 ? -4.267 -8.207 7.198 1.00 85.58 ? 127 LYS B NZ 1 ATOM 2642 N N . SER B 1 128 ? -1.856 -11.068 -0.194 1.00 77.48 ? 128 SER B N 1 ATOM 2643 C CA . SER B 1 128 ? -2.293 -11.139 -1.567 1.00 73.28 ? 128 SER B CA 1 ATOM 2644 C C . SER B 1 128 ? -2.991 -12.470 -1.747 1.00 74.00 ? 128 SER B C 1 ATOM 2645 O O . SER B 1 128 ? -2.749 -13.422 -1.000 1.00 64.20 ? 128 SER B O 1 ATOM 2646 C CB . SER B 1 128 ? -1.109 -10.951 -2.540 1.00 74.89 ? 128 SER B CB 1 ATOM 2647 O OG . SER B 1 128 ? -0.216 -12.064 -2.589 1.00 73.16 ? 128 SER B OG 1 ATOM 2648 N N . SER B 1 129 ? -3.886 -12.555 -2.717 1.00 83.03 ? 129 SER B N 1 ATOM 2649 C CA . SER B 1 129 ? -4.588 -13.805 -2.832 1.00 87.55 ? 129 SER B CA 1 ATOM 2650 C C . SER B 1 129 ? -3.787 -14.707 -3.750 1.00 82.66 ? 129 SER B C 1 ATOM 2651 O O . SER B 1 129 ? -3.245 -14.263 -4.742 1.00 83.80 ? 129 SER B O 1 ATOM 2652 C CB . SER B 1 129 ? -6.019 -13.589 -3.329 1.00 98.88 ? 129 SER B CB 1 ATOM 2653 O OG . SER B 1 129 ? -6.677 -14.830 -3.522 1.00 100.74 ? 129 SER B OG 1 ATOM 2654 N N . CYS B 1 130 ? -3.751 -15.982 -3.403 1.00 77.12 ? 130 CYS B N 1 ATOM 2655 C CA . CYS B 1 130 ? -3.019 -16.995 -4.138 1.00 72.85 ? 130 CYS B CA 1 ATOM 2656 C C . CYS B 1 130 ? -3.943 -18.016 -4.779 1.00 83.81 ? 130 CYS B C 1 ATOM 2657 O O . CYS B 1 130 ? -5.137 -18.051 -4.474 1.00 89.86 ? 130 CYS B O 1 ATOM 2658 C CB . CYS B 1 130 ? -2.045 -17.707 -3.205 1.00 55.05 ? 130 CYS B CB 1 ATOM 2659 S SG . CYS B 1 130 ? -0.807 -16.627 -2.593 1.00 146.07 ? 130 CYS B SG 1 ATOM 2660 N N . VAL B 1 131 ? -3.405 -18.836 -5.685 1.00 86.42 ? 131 VAL B N 1 ATOM 2661 C CA . VAL B 1 131 ? -4.219 -19.874 -6.337 1.00 83.32 ? 131 VAL B CA 1 ATOM 2662 C C . VAL B 1 131 ? -3.501 -21.220 -6.289 1.00 87.45 ? 131 VAL B C 1 ATOM 2663 O O . VAL B 1 131 ? -2.270 -21.283 -6.246 1.00 74.33 ? 131 VAL B O 1 ATOM 2664 C CB . VAL B 1 131 ? -4.602 -19.540 -7.832 1.00 79.40 ? 131 VAL B CB 1 ATOM 2665 C CG1 . VAL B 1 131 ? -5.523 -20.599 -8.435 1.00 67.90 ? 131 VAL B CG1 1 ATOM 2666 C CG2 . VAL B 1 131 ? -5.268 -18.175 -7.960 1.00 77.92 ? 131 VAL B CG2 1 ATOM 2667 N N . VAL B 1 132 ? -4.311 -22.279 -6.285 1.00 103.61 ? 132 VAL B N 1 ATOM 2668 C CA . VAL B 1 132 ? -3.880 -23.671 -6.354 1.00 112.12 ? 132 VAL B CA 1 ATOM 2669 C C . VAL B 1 132 ? -3.670 -24.099 -7.808 1.00 130.14 ? 132 VAL B C 1 ATOM 2670 O O . VAL B 1 132 ? -4.213 -23.510 -8.739 1.00 129.63 ? 132 VAL B O 1 ATOM 2671 C CB . VAL B 1 132 ? -4.899 -24.622 -5.727 1.00 114.57 ? 132 VAL B CB 1 ATOM 2672 C CG1 . VAL B 1 132 ? -6.172 -24.657 -6.581 1.00 117.84 ? 132 VAL B CG1 1 ATOM 2673 C CG2 . VAL B 1 132 ? -4.315 -26.022 -5.577 1.00 105.42 ? 132 VAL B CG2 1 ATOM 2674 N N . ASP B 1 133 ? -2.836 -25.115 -7.968 1.00 133.90 ? 133 ASP B N 1 ATOM 2675 C CA . ASP B 1 133 ? -2.425 -25.639 -9.240 1.00 144.27 ? 133 ASP B CA 1 ATOM 2676 C C . ASP B 1 133 ? -2.238 -27.179 -9.174 1.00 137.16 ? 133 ASP B C 1 ATOM 2677 O O . ASP B 1 133 ? -1.477 -27.688 -8.355 1.00 145.99 ? 133 ASP B O 1 ATOM 2678 C CB . ASP B 1 133 ? -1.126 -24.927 -9.611 1.00 151.70 ? 133 ASP B CB 1 ATOM 2679 C CG . ASP B 1 133 ? -0.361 -25.624 -10.656 1.00 165.86 ? 133 ASP B CG 1 ATOM 2680 O OD1 . ASP B 1 133 ? -0.901 -26.560 -11.234 1.00 178.29 ? 133 ASP B OD1 1 ATOM 2681 O OD2 . ASP B 1 133 ? 0.813 -25.272 -10.855 1.00 168.13 ? 133 ASP B OD2 1 ATOM 2682 N N . VAL B 1 134 ? -2.946 -27.924 -10.013 1.00 142.99 ? 134 VAL B N 1 ATOM 2683 C CA . VAL B 1 134 ? -2.686 -29.363 -10.126 1.00 142.72 ? 134 VAL B CA 1 ATOM 2684 C C . VAL B 1 134 ? -2.038 -29.549 -11.521 1.00 154.08 ? 134 VAL B C 1 ATOM 2685 O O . VAL B 1 134 ? -2.562 -30.226 -12.372 1.00 159.64 ? 134 VAL B O 1 ATOM 2686 C CB . VAL B 1 134 ? -3.978 -30.205 -9.931 1.00 140.84 ? 134 VAL B CB 1 ATOM 2687 C CG1 . VAL B 1 134 ? -3.681 -31.699 -9.815 1.00 143.91 ? 134 VAL B CG1 1 ATOM 2688 C CG2 . VAL B 1 134 ? -4.734 -29.741 -8.685 1.00 137.14 ? 134 VAL B CG2 1 ATOM 2689 N N . THR B 1 135 ? -0.917 -28.854 -11.723 1.00 155.68 ? 135 THR B N 1 ATOM 2690 C CA . THR B 1 135 ? -0.068 -28.772 -12.936 1.00 157.76 ? 135 THR B CA 1 ATOM 2691 C C . THR B 1 135 ? 1.316 -28.728 -12.297 1.00 158.69 ? 135 THR B C 1 ATOM 2692 O O . THR B 1 135 ? 1.383 -28.508 -11.091 1.00 166.08 ? 135 THR B O 1 ATOM 2693 C CB . THR B 1 135 ? -0.367 -27.495 -13.818 1.00 136.98 ? 135 THR B CB 1 ATOM 2694 O OG1 . THR B 1 135 ? -1.344 -27.804 -14.823 1.00 144.53 ? 135 THR B OG1 1 ATOM 2695 C CG2 . THR B 1 135 ? 0.892 -26.876 -14.424 1.00 130.48 ? 135 THR B CG2 1 ATOM 2696 N N . TYR B 1 136 ? 2.401 -29.003 -13.018 1.00 162.31 ? 136 TYR B N 1 ATOM 2697 C CA . TYR B 1 136 ? 3.737 -28.651 -12.522 1.00 160.45 ? 136 TYR B CA 1 ATOM 2698 C C . TYR B 1 136 ? 4.088 -29.557 -11.354 1.00 161.97 ? 136 TYR B C 1 ATOM 2699 O O . TYR B 1 136 ? 3.929 -29.166 -10.225 1.00 148.84 ? 136 TYR B O 1 ATOM 2700 C CB . TYR B 1 136 ? 3.834 -27.162 -12.108 1.00 164.15 ? 136 TYR B CB 1 ATOM 2701 C CG . TYR B 1 136 ? 5.187 -26.726 -11.540 1.00 172.88 ? 136 TYR B CG 1 ATOM 2702 C CD1 . TYR B 1 136 ? 6.257 -26.414 -12.378 1.00 176.89 ? 136 TYR B CD1 1 ATOM 2703 C CD2 . TYR B 1 136 ? 5.393 -26.629 -10.164 1.00 177.88 ? 136 TYR B CD2 1 ATOM 2704 C CE1 . TYR B 1 136 ? 7.493 -26.016 -11.855 1.00 179.78 ? 136 TYR B CE1 1 ATOM 2705 C CE2 . TYR B 1 136 ? 6.621 -26.240 -9.637 1.00 180.49 ? 136 TYR B CE2 1 ATOM 2706 C CZ . TYR B 1 136 ? 7.664 -25.933 -10.484 1.00 180.42 ? 136 TYR B CZ 1 ATOM 2707 O OH . TYR B 1 136 ? 8.871 -25.545 -9.948 1.00 176.58 ? 136 TYR B OH 1 ATOM 2708 N N . PHE B 1 137 ? 4.600 -30.747 -11.649 1.00 170.30 ? 137 PHE B N 1 ATOM 2709 C CA . PHE B 1 137 ? 4.959 -31.761 -10.651 1.00 173.06 ? 137 PHE B CA 1 ATOM 2710 C C . PHE B 1 137 ? 5.675 -31.160 -9.430 1.00 172.57 ? 137 PHE B C 1 ATOM 2711 O O . PHE B 1 137 ? 6.578 -30.352 -9.593 1.00 164.81 ? 137 PHE B O 1 ATOM 2712 C CB . PHE B 1 137 ? 5.884 -32.782 -11.336 1.00 183.62 ? 137 PHE B CB 1 ATOM 2713 C CG . PHE B 1 137 ? 7.164 -32.157 -11.906 1.00 190.45 ? 137 PHE B CG 1 ATOM 2714 C CD1 . PHE B 1 137 ? 7.202 -31.614 -13.193 1.00 191.04 ? 137 PHE B CD1 1 ATOM 2715 C CD2 . PHE B 1 137 ? 8.318 -32.092 -11.138 1.00 190.84 ? 137 PHE B CD2 1 ATOM 2716 C CE1 . PHE B 1 137 ? 8.367 -31.029 -13.692 1.00 188.91 ? 137 PHE B CE1 1 ATOM 2717 C CE2 . PHE B 1 137 ? 9.475 -31.508 -11.631 1.00 191.50 ? 137 PHE B CE2 1 ATOM 2718 C CZ . PHE B 1 137 ? 9.500 -30.980 -12.910 1.00 188.67 ? 137 PHE B CZ 1 ATOM 2719 N N . PRO B 1 138 ? 5.255 -31.503 -8.195 1.00 170.40 ? 138 PRO B N 1 ATOM 2720 C CA . PRO B 1 138 ? 4.188 -32.375 -7.684 1.00 171.77 ? 138 PRO B CA 1 ATOM 2721 C C . PRO B 1 138 ? 2.847 -31.700 -7.968 1.00 171.37 ? 138 PRO B C 1 ATOM 2722 O O . PRO B 1 138 ? 2.837 -30.741 -8.720 1.00 173.44 ? 138 PRO B O 1 ATOM 2723 C CB . PRO B 1 138 ? 4.464 -32.462 -6.173 1.00 170.05 ? 138 PRO B CB 1 ATOM 2724 C CG . PRO B 1 138 ? 5.430 -31.381 -5.864 1.00 166.77 ? 138 PRO B CG 1 ATOM 2725 C CD . PRO B 1 138 ? 6.119 -30.987 -7.117 1.00 169.47 ? 138 PRO B CD 1 ATOM 2726 N N . PHE B 1 139 ? 1.724 -32.162 -7.439 1.00 172.60 ? 139 PHE B N 1 ATOM 2727 C CA . PHE B 1 139 ? 0.505 -31.412 -7.738 1.00 173.76 ? 139 PHE B CA 1 ATOM 2728 C C . PHE B 1 139 ? -0.316 -30.896 -6.555 1.00 183.47 ? 139 PHE B C 1 ATOM 2729 O O . PHE B 1 139 ? -1.545 -31.043 -6.496 1.00 184.27 ? 139 PHE B O 1 ATOM 2730 C CB . PHE B 1 139 ? -0.348 -32.236 -8.686 1.00 169.26 ? 139 PHE B CB 1 ATOM 2731 C CG . PHE B 1 139 ? 0.417 -32.698 -9.893 1.00 167.35 ? 139 PHE B CG 1 ATOM 2732 C CD1 . PHE B 1 139 ? 0.787 -31.797 -10.887 1.00 163.40 ? 139 PHE B CD1 1 ATOM 2733 C CD2 . PHE B 1 139 ? 0.845 -34.011 -9.992 1.00 167.77 ? 139 PHE B CD2 1 ATOM 2734 C CE1 . PHE B 1 139 ? 1.522 -32.212 -11.982 1.00 160.61 ? 139 PHE B CE1 1 ATOM 2735 C CE2 . PHE B 1 139 ? 1.576 -34.432 -11.083 1.00 166.52 ? 139 PHE B CE2 1 ATOM 2736 C CZ . PHE B 1 139 ? 1.916 -33.532 -12.079 1.00 162.76 ? 139 PHE B CZ 1 ATOM 2737 N N . ASP B 1 140 ? 0.386 -30.176 -5.692 1.00 179.80 ? 140 ASP B N 1 ATOM 2738 C CA . ASP B 1 140 ? -0.164 -29.562 -4.502 1.00 181.94 ? 140 ASP B CA 1 ATOM 2739 C C . ASP B 1 140 ? 0.154 -28.099 -4.720 1.00 182.94 ? 140 ASP B C 1 ATOM 2740 O O . ASP B 1 140 ? 0.548 -27.358 -3.830 1.00 178.40 ? 140 ASP B O 1 ATOM 2741 C CB . ASP B 1 140 ? 0.525 -30.124 -3.258 1.00 178.39 ? 140 ASP B CB 1 ATOM 2742 C CG . ASP B 1 140 ? 0.365 -29.247 -2.066 1.00 173.17 ? 140 ASP B CG 1 ATOM 2743 O OD1 . ASP B 1 140 ? -0.788 -29.072 -1.636 1.00 172.25 ? 140 ASP B OD1 1 ATOM 2744 O OD2 . ASP B 1 140 ? 1.383 -28.668 -1.621 1.00 170.27 ? 140 ASP B OD2 1 ATOM 2745 N N . ASN B 1 141 ? -0.102 -27.619 -5.918 1.00 197.43 ? 141 ASN B N 1 ATOM 2746 C CA . ASN B 1 141 ? 0.622 -26.408 -6.147 1.00 195.73 ? 141 ASN B CA 1 ATOM 2747 C C . ASN B 1 141 ? -0.174 -25.119 -6.043 1.00 176.99 ? 141 ASN B C 1 ATOM 2748 O O . ASN B 1 141 ? -1.334 -25.028 -6.387 1.00 184.08 ? 141 ASN B O 1 ATOM 2749 C CB . ASN B 1 141 ? 1.405 -26.504 -7.463 1.00 212.73 ? 141 ASN B CB 1 ATOM 2750 C CG . ASN B 1 141 ? 2.442 -27.645 -7.463 1.00 221.42 ? 141 ASN B CG 1 ATOM 2751 O OD1 . ASN B 1 141 ? 3.256 -27.707 -8.359 1.00 222.73 ? 141 ASN B OD1 1 ATOM 2752 N ND2 . ASN B 1 141 ? 2.398 -28.537 -6.489 1.00 225.86 ? 141 ASN B ND2 1 ATOM 2753 N N . GLN B 1 142 ? 0.538 -24.132 -5.519 1.00 132.20 ? 142 GLN B N 1 ATOM 2754 C CA . GLN B 1 142 ? 0.057 -22.827 -5.134 1.00 117.27 ? 142 GLN B CA 1 ATOM 2755 C C . GLN B 1 142 ? 0.846 -21.715 -5.793 1.00 92.57 ? 142 GLN B C 1 ATOM 2756 O O . GLN B 1 142 ? 2.057 -21.620 -5.616 1.00 89.54 ? 142 GLN B O 1 ATOM 2757 C CB . GLN B 1 142 ? 0.214 -22.646 -3.618 1.00 109.93 ? 142 GLN B CB 1 ATOM 2758 C CG . GLN B 1 142 ? -0.978 -22.981 -2.678 1.00 120.46 ? 142 GLN B CG 1 ATOM 2759 C CD . GLN B 1 142 ? -1.788 -21.737 -2.281 1.00 122.32 ? 142 GLN B CD 1 ATOM 2760 O OE1 . GLN B 1 142 ? -1.856 -20.755 -3.028 1.00 126.13 ? 142 GLN B OE1 1 ATOM 2761 N NE2 . GLN B 1 142 ? -2.307 -21.737 -1.057 1.00 122.51 ? 142 GLN B NE2 1 ATOM 2762 N N . GLN B 1 143 ? 0.145 -20.854 -6.519 1.00 91.49 ? 143 GLN B N 1 ATOM 2763 C CA . GLN B 1 143 ? 0.762 -19.748 -7.235 1.00 91.48 ? 143 GLN B CA 1 ATOM 2764 C C . GLN B 1 143 ? 0.367 -18.454 -6.532 1.00 85.84 ? 143 GLN B C 1 ATOM 2765 O O . GLN B 1 143 ? -0.823 -18.235 -6.186 1.00 85.76 ? 143 GLN B O 1 ATOM 2766 C CB . GLN B 1 143 ? 0.346 -19.724 -8.724 1.00 98.44 ? 143 GLN B CB 1 ATOM 2767 C CG . GLN B 1 143 ? 1.197 -18.817 -9.638 1.00 97.75 ? 143 GLN B CG 1 ATOM 2768 C CD . GLN B 1 143 ? 0.503 -18.446 -10.948 1.00 105.92 ? 143 GLN B CD 1 ATOM 2769 O OE1 . GLN B 1 143 ? -0.209 -17.439 -11.031 1.00 109.46 ? 143 GLN B OE1 1 ATOM 2770 N NE2 . GLN B 1 143 ? 0.702 -19.265 -11.975 1.00 114.94 ? 143 GLN B NE2 1 ATOM 2771 N N . CYS B 1 144 ? 1.366 -17.612 -6.292 1.00 75.42 ? 144 CYS B N 1 ATOM 2772 C CA . CYS B 1 144 ? 1.080 -16.314 -5.711 1.00 73.58 ? 144 CYS B CA 1 ATOM 2773 C C . CYS B 1 144 ? 1.637 -15.204 -6.575 1.00 74.23 ? 144 CYS B C 1 ATOM 2774 O O . CYS B 1 144 ? 2.828 -15.089 -6.754 1.00 85.61 ? 144 CYS B O 1 ATOM 2775 C CB . CYS B 1 144 ? 1.631 -16.227 -4.287 1.00 60.87 ? 144 CYS B CB 1 ATOM 2776 S SG . CYS B 1 144 ? 0.953 -17.464 -3.225 1.00 104.11 ? 144 CYS B SG 1 ATOM 2777 N N . ASN B 1 145 ? 0.761 -14.390 -7.129 1.00 89.63 ? 145 ASN B N 1 ATOM 2778 C CA . ASN B 1 145 ? 1.228 -13.279 -7.926 1.00 96.10 ? 145 ASN B CA 1 ATOM 2779 C C . ASN B 1 145 ? 1.339 -12.106 -7.010 1.00 99.54 ? 145 ASN B C 1 ATOM 2780 O O . ASN B 1 145 ? 0.513 -11.939 -6.129 1.00 109.97 ? 145 ASN B O 1 ATOM 2781 C CB . ASN B 1 145 ? 0.262 -12.942 -9.069 1.00 96.86 ? 145 ASN B CB 1 ATOM 2782 C CG . ASN B 1 145 ? 0.437 -13.839 -10.262 1.00 95.18 ? 145 ASN B CG 1 ATOM 2783 O OD1 . ASN B 1 145 ? 1.177 -14.823 -10.202 1.00 82.11 ? 145 ASN B OD1 1 ATOM 2784 N ND2 . ASN B 1 145 ? -0.243 -13.513 -11.360 1.00 102.39 ? 145 ASN B ND2 1 ATOM 2785 N N . LEU B 1 146 ? 2.337 -11.277 -7.223 1.00 93.85 ? 146 LEU B N 1 ATOM 2786 C CA . LEU B 1 146 ? 2.392 -10.014 -6.532 1.00 87.95 ? 146 LEU B CA 1 ATOM 2787 C C . LEU B 1 146 ? 2.552 -8.909 -7.558 1.00 81.52 ? 146 LEU B C 1 ATOM 2788 O O . LEU B 1 146 ? 3.663 -8.692 -8.054 1.00 88.69 ? 146 LEU B O 1 ATOM 2789 C CB . LEU B 1 146 ? 3.541 -9.997 -5.536 1.00 87.66 ? 146 LEU B CB 1 ATOM 2790 C CG . LEU B 1 146 ? 3.529 -10.858 -4.286 1.00 74.76 ? 146 LEU B CG 1 ATOM 2791 C CD1 . LEU B 1 146 ? 4.953 -11.104 -3.841 1.00 65.58 ? 146 LEU B CD1 1 ATOM 2792 C CD2 . LEU B 1 146 ? 2.818 -10.033 -3.254 1.00 70.84 ? 146 LEU B CD2 1 ATOM 2793 N N . THR B 1 147 ? 1.472 -8.175 -7.822 1.00 58.70 ? 147 THR B N 1 ATOM 2794 C CA . THR B 1 147 ? 1.511 -7.157 -8.857 1.00 56.40 ? 147 THR B CA 1 ATOM 2795 C C . THR B 1 147 ? 1.647 -5.714 -8.312 1.00 64.99 ? 147 THR B C 1 ATOM 2796 O O . THR B 1 147 ? 0.872 -5.257 -7.479 1.00 70.70 ? 147 THR B O 1 ATOM 2797 C CB . THR B 1 147 ? 0.284 -7.269 -9.728 1.00 61.11 ? 147 THR B CB 1 ATOM 2798 O OG1 . THR B 1 147 ? 0.282 -8.584 -10.297 1.00 69.22 ? 147 THR B OG1 1 ATOM 2799 C CG2 . THR B 1 147 ? 0.301 -6.194 -10.825 1.00 53.02 ? 147 THR B CG2 1 ATOM 2800 N N . PHE B 1 148 ? 2.710 -5.045 -8.748 1.00 71.19 ? 148 PHE B N 1 ATOM 2801 C CA . PHE B 1 148 ? 3.056 -3.693 -8.322 1.00 67.15 ? 148 PHE B CA 1 ATOM 2802 C C . PHE B 1 148 ? 2.892 -2.777 -9.510 1.00 71.59 ? 148 PHE B C 1 ATOM 2803 O O . PHE B 1 148 ? 3.320 -3.111 -10.623 1.00 72.92 ? 148 PHE B O 1 ATOM 2804 C CB . PHE B 1 148 ? 4.511 -3.619 -7.800 1.00 50.71 ? 148 PHE B CB 1 ATOM 2805 C CG . PHE B 1 148 ? 4.810 -4.619 -6.713 1.00 51.46 ? 148 PHE B CG 1 ATOM 2806 C CD1 . PHE B 1 148 ? 4.987 -5.971 -7.024 1.00 52.57 ? 148 PHE B CD1 1 ATOM 2807 C CD2 . PHE B 1 148 ? 4.855 -4.221 -5.361 1.00 49.22 ? 148 PHE B CD2 1 ATOM 2808 C CE1 . PHE B 1 148 ? 5.252 -6.900 -6.019 1.00 58.43 ? 148 PHE B CE1 1 ATOM 2809 C CE2 . PHE B 1 148 ? 5.069 -5.135 -4.347 1.00 48.52 ? 148 PHE B CE2 1 ATOM 2810 C CZ . PHE B 1 148 ? 5.280 -6.489 -4.656 1.00 61.01 ? 148 PHE B CZ 1 ATOM 2811 N N . GLY B 1 149 ? 2.313 -1.609 -9.295 1.00 63.29 ? 149 GLY B N 1 ATOM 2812 C CA . GLY B 1 149 ? 2.270 -0.606 -10.354 1.00 68.76 ? 149 GLY B CA 1 ATOM 2813 C C . GLY B 1 149 ? 1.989 0.712 -9.673 1.00 74.33 ? 149 GLY B C 1 ATOM 2814 O O . GLY B 1 149 ? 1.800 0.732 -8.458 1.00 88.38 ? 149 GLY B O 1 ATOM 2815 N N . SER B 1 150 ? 2.001 1.809 -10.414 1.00 68.83 ? 150 SER B N 1 ATOM 2816 C CA . SER B 1 150 ? 1.665 3.101 -9.835 1.00 79.69 ? 150 SER B CA 1 ATOM 2817 C C . SER B 1 150 ? 0.154 3.206 -9.509 1.00 89.36 ? 150 SER B C 1 ATOM 2818 O O . SER B 1 150 ? -0.683 2.533 -10.106 1.00 84.86 ? 150 SER B O 1 ATOM 2819 C CB . SER B 1 150 ? 2.093 4.223 -10.782 1.00 82.85 ? 150 SER B CB 1 ATOM 2820 O OG . SER B 1 150 ? 1.651 5.491 -10.332 1.00 88.63 ? 150 SER B OG 1 ATOM 2821 N N . TRP B 1 151 ? -0.193 4.045 -8.541 1.00 102.89 ? 151 TRP B N 1 ATOM 2822 C CA . TRP B 1 151 ? -1.592 4.203 -8.169 1.00 100.81 ? 151 TRP B CA 1 ATOM 2823 C C . TRP B 1 151 ? -2.177 5.371 -8.912 1.00 88.57 ? 151 TRP B C 1 ATOM 2824 O O . TRP B 1 151 ? -3.388 5.446 -9.057 1.00 113.65 ? 151 TRP B O 1 ATOM 2825 C CB . TRP B 1 151 ? -1.781 4.409 -6.652 1.00 110.33 ? 151 TRP B CB 1 ATOM 2826 C CG . TRP B 1 151 ? -3.217 4.773 -6.307 1.00 123.01 ? 151 TRP B CG 1 ATOM 2827 C CD1 . TRP B 1 151 ? -3.727 6.034 -6.174 1.00 132.29 ? 151 TRP B CD1 1 ATOM 2828 C CD2 . TRP B 1 151 ? -4.319 3.879 -6.096 1.00 131.31 ? 151 TRP B CD2 1 ATOM 2829 N NE1 . TRP B 1 151 ? -5.070 5.983 -5.899 1.00 137.62 ? 151 TRP B NE1 1 ATOM 2830 C CE2 . TRP B 1 151 ? -5.460 4.672 -5.839 1.00 134.32 ? 151 TRP B CE2 1 ATOM 2831 C CE3 . TRP B 1 151 ? -4.454 2.489 -6.090 1.00 132.20 ? 151 TRP B CE3 1 ATOM 2832 C CZ2 . TRP B 1 151 ? -6.716 4.120 -5.580 1.00 132.89 ? 151 TRP B CZ2 1 ATOM 2833 C CZ3 . TRP B 1 151 ? -5.707 1.943 -5.828 1.00 132.98 ? 151 TRP B CZ3 1 ATOM 2834 C CH2 . TRP B 1 151 ? -6.819 2.759 -5.582 1.00 132.56 ? 151 TRP B CH2 1 ATOM 2835 N N . THR B 1 152 ? -1.335 6.295 -9.370 1.00 73.47 ? 152 THR B N 1 ATOM 2836 C CA . THR B 1 152 ? -1.848 7.539 -9.969 1.00 82.33 ? 152 THR B CA 1 ATOM 2837 C C . THR B 1 152 ? -1.200 7.938 -11.300 1.00 90.40 ? 152 THR B C 1 ATOM 2838 O O . THR B 1 152 ? -1.442 9.041 -11.797 1.00 97.07 ? 152 THR B O 1 ATOM 2839 C CB . THR B 1 152 ? -1.706 8.771 -9.016 1.00 91.90 ? 152 THR B CB 1 ATOM 2840 O OG1 . THR B 1 152 ? -0.359 9.247 -9.016 1.00 97.45 ? 152 THR B OG1 1 ATOM 2841 C CG2 . THR B 1 152 ? -2.141 8.441 -7.604 1.00 89.60 ? 152 THR B CG2 1 ATOM 2842 N N . TYR B 1 153 ? -0.333 7.094 -11.853 1.00 93.49 ? 153 TYR B N 1 ATOM 2843 C CA . TYR B 1 153 ? 0.443 7.506 -13.031 1.00 101.38 ? 153 TYR B CA 1 ATOM 2844 C C . TYR B 1 153 ? 0.440 6.453 -14.153 1.00 113.90 ? 153 TYR B C 1 ATOM 2845 O O . TYR B 1 153 ? 0.979 5.341 -13.970 1.00 123.20 ? 153 TYR B O 1 ATOM 2846 C CB . TYR B 1 153 ? 1.906 7.812 -12.628 1.00 97.16 ? 153 TYR B CB 1 ATOM 2847 C CG . TYR B 1 153 ? 2.110 9.091 -11.814 1.00 87.28 ? 153 TYR B CG 1 ATOM 2848 C CD1 . TYR B 1 153 ? 2.025 10.349 -12.426 1.00 89.89 ? 153 TYR B CD1 1 ATOM 2849 C CD2 . TYR B 1 153 ? 2.420 9.048 -10.449 1.00 68.68 ? 153 TYR B CD2 1 ATOM 2850 C CE1 . TYR B 1 153 ? 2.207 11.532 -11.696 1.00 93.32 ? 153 TYR B CE1 1 ATOM 2851 C CE2 . TYR B 1 153 ? 2.603 10.234 -9.710 1.00 72.23 ? 153 TYR B CE2 1 ATOM 2852 C CZ . TYR B 1 153 ? 2.502 11.471 -10.337 1.00 84.06 ? 153 TYR B CZ 1 ATOM 2853 O OH . TYR B 1 153 ? 2.677 12.656 -9.632 1.00 78.46 ? 153 TYR B OH 1 ATOM 2854 N N . ASN B 1 154 ? -0.135 6.833 -15.305 1.00 107.87 ? 154 ASN B N 1 ATOM 2855 C CA . ASN B 1 154 ? -0.132 6.041 -16.544 1.00 107.78 ? 154 ASN B CA 1 ATOM 2856 C C . ASN B 1 154 ? 1.273 5.754 -17.075 1.00 108.64 ? 154 ASN B C 1 ATOM 2857 O O . ASN B 1 154 ? 2.189 6.534 -16.821 1.00 103.19 ? 154 ASN B O 1 ATOM 2858 C CB . ASN B 1 154 ? -0.938 6.765 -17.617 1.00 105.42 ? 154 ASN B CB 1 ATOM 2859 C CG . ASN B 1 154 ? -0.614 8.207 -17.675 1.00 111.92 ? 154 ASN B CG 1 ATOM 2860 O OD1 . ASN B 1 154 ? 0.491 8.564 -18.060 1.00 126.70 ? 154 ASN B OD1 1 ATOM 2861 N ND2 . ASN B 1 154 ? -1.523 9.049 -17.209 1.00 96.37 ? 154 ASN B ND2 1 ATOM 2862 N N . GLY B 1 155 ? 1.417 4.731 -17.922 1.00 111.61 ? 155 GLY B N 1 ATOM 2863 C CA . GLY B 1 155 ? 2.678 4.451 -18.610 1.00 110.97 ? 155 GLY B CA 1 ATOM 2864 C C . GLY B 1 155 ? 3.228 5.593 -19.445 1.00 103.99 ? 155 GLY B C 1 ATOM 2865 O O . GLY B 1 155 ? 4.336 5.507 -19.995 1.00 99.65 ? 155 GLY B O 1 ATOM 2866 N N . ASN B 1 156 ? 2.442 6.657 -19.557 1.00 101.58 ? 156 ASN B N 1 ATOM 2867 C CA . ASN B 1 156 ? 2.862 7.834 -20.304 1.00 115.06 ? 156 ASN B CA 1 ATOM 2868 C C . ASN B 1 156 ? 3.377 8.969 -19.409 1.00 113.14 ? 156 ASN B C 1 ATOM 2869 O O . ASN B 1 156 ? 3.949 9.937 -19.879 1.00 110.86 ? 156 ASN B O 1 ATOM 2870 C CB . ASN B 1 156 ? 1.713 8.330 -21.178 1.00 123.90 ? 156 ASN B CB 1 ATOM 2871 C CG . ASN B 1 156 ? 2.177 9.255 -22.268 1.00 131.82 ? 156 ASN B CG 1 ATOM 2872 O OD1 . ASN B 1 156 ? 2.311 10.462 -22.065 1.00 134.74 ? 156 ASN B OD1 1 ATOM 2873 N ND2 . ASN B 1 156 ? 2.458 8.692 -23.429 1.00 140.48 ? 156 ASN B ND2 1 ATOM 2874 N N . GLN B 1 157 ? 3.166 8.868 -18.113 1.00 113.84 ? 157 GLN B N 1 ATOM 2875 C CA . GLN B 1 157 ? 3.942 9.703 -17.236 1.00 107.56 ? 157 GLN B CA 1 ATOM 2876 C C . GLN B 1 157 ? 5.005 8.852 -16.504 1.00 106.82 ? 157 GLN B C 1 ATOM 2877 O O . GLN B 1 157 ? 6.116 9.329 -16.255 1.00 110.19 ? 157 GLN B O 1 ATOM 2878 C CB . GLN B 1 157 ? 3.055 10.507 -16.288 1.00 105.32 ? 157 GLN B CB 1 ATOM 2879 C CG . GLN B 1 157 ? 1.667 10.028 -15.961 1.00 113.11 ? 157 GLN B CG 1 ATOM 2880 C CD . GLN B 1 157 ? 0.757 11.169 -15.536 1.00 118.66 ? 157 GLN B CD 1 ATOM 2881 O OE1 . GLN B 1 157 ? 1.132 12.327 -15.654 1.00 127.02 ? 157 GLN B OE1 1 ATOM 2882 N NE2 . GLN B 1 157 ? -0.384 10.846 -14.914 1.00 120.44 ? 157 GLN B NE2 1 ATOM 2883 N N . VAL B 1 158 ? 4.668 7.634 -16.083 1.00 86.34 ? 158 VAL B N 1 ATOM 2884 C CA . VAL B 1 158 ? 5.706 6.770 -15.502 1.00 73.27 ? 158 VAL B CA 1 ATOM 2885 C C . VAL B 1 158 ? 5.649 5.278 -15.940 1.00 84.29 ? 158 VAL B C 1 ATOM 2886 O O . VAL B 1 158 ? 4.599 4.627 -15.911 1.00 85.60 ? 158 VAL B O 1 ATOM 2887 C CB . VAL B 1 158 ? 5.747 6.889 -13.952 1.00 93.66 ? 158 VAL B CB 1 ATOM 2888 C CG1 . VAL B 1 158 ? 5.144 8.221 -13.493 1.00 85.76 ? 158 VAL B CG1 1 ATOM 2889 C CG2 . VAL B 1 158 ? 5.086 5.718 -13.266 1.00 99.75 ? 158 VAL B CG2 1 ATOM 2890 N N . ASP B 1 159 ? 6.768 4.783 -16.467 1.00 81.95 ? 159 ASP B N 1 ATOM 2891 C CA . ASP B 1 159 ? 6.869 3.376 -16.845 1.00 92.35 ? 159 ASP B CA 1 ATOM 2892 C C . ASP B 1 159 ? 7.702 2.683 -15.775 1.00 97.13 ? 159 ASP B C 1 ATOM 2893 O O . ASP B 1 159 ? 8.690 3.225 -15.300 1.00 95.02 ? 159 ASP B O 1 ATOM 2894 C CB . ASP B 1 159 ? 7.519 3.231 -18.233 1.00 100.97 ? 159 ASP B CB 1 ATOM 2895 C CG . ASP B 1 159 ? 7.261 1.868 -18.884 1.00 101.32 ? 159 ASP B CG 1 ATOM 2896 O OD1 . ASP B 1 159 ? 6.837 0.918 -18.175 1.00 90.83 ? 159 ASP B OD1 1 ATOM 2897 O OD2 . ASP B 1 159 ? 7.493 1.761 -20.119 1.00 104.22 ? 159 ASP B OD2 1 ATOM 2898 N N . ILE B 1 160 ? 7.342 1.467 -15.416 1.00 96.03 ? 160 ILE B N 1 ATOM 2899 C CA . ILE B 1 160 ? 8.024 0.837 -14.318 1.00 92.66 ? 160 ILE B CA 1 ATOM 2900 C C . ILE B 1 160 ? 8.519 -0.508 -14.818 1.00 96.07 ? 160 ILE B C 1 ATOM 2901 O O . ILE B 1 160 ? 7.739 -1.341 -15.277 1.00 94.37 ? 160 ILE B O 1 ATOM 2902 C CB . ILE B 1 160 ? 7.089 0.739 -13.062 1.00 102.73 ? 160 ILE B CB 1 ATOM 2903 C CG1 . ILE B 1 160 ? 5.868 -0.130 -13.305 1.00 96.53 ? 160 ILE B CG1 1 ATOM 2904 C CG2 . ILE B 1 160 ? 6.541 2.110 -12.690 1.00 105.19 ? 160 ILE B CG2 1 ATOM 2905 C CD1 . ILE B 1 160 ? 5.914 -1.423 -12.574 1.00 98.60 ? 160 ILE B CD1 1 ATOM 2906 N N . PHE B 1 161 ? 9.837 -0.688 -14.770 1.00 95.92 ? 161 PHE B N 1 ATOM 2907 C CA . PHE B 1 161 ? 10.482 -1.899 -15.266 1.00 90.06 ? 161 PHE B CA 1 ATOM 2908 C C . PHE B 1 161 ? 11.026 -2.712 -14.124 1.00 77.91 ? 161 PHE B C 1 ATOM 2909 O O . PHE B 1 161 ? 11.602 -2.148 -13.193 1.00 91.00 ? 161 PHE B O 1 ATOM 2910 C CB . PHE B 1 161 ? 11.632 -1.570 -16.238 1.00 94.31 ? 161 PHE B CB 1 ATOM 2911 C CG . PHE B 1 161 ? 11.231 -0.682 -17.372 1.00 87.90 ? 161 PHE B CG 1 ATOM 2912 C CD1 . PHE B 1 161 ? 10.547 -1.192 -18.452 1.00 93.23 ? 161 PHE B CD1 1 ATOM 2913 C CD2 . PHE B 1 161 ? 11.529 0.668 -17.351 1.00 87.81 ? 161 PHE B CD2 1 ATOM 2914 C CE1 . PHE B 1 161 ? 10.133 -0.358 -19.486 1.00 105.34 ? 161 PHE B CE1 1 ATOM 2915 C CE2 . PHE B 1 161 ? 11.147 1.500 -18.384 1.00 90.35 ? 161 PHE B CE2 1 ATOM 2916 C CZ . PHE B 1 161 ? 10.437 0.993 -19.452 1.00 99.81 ? 161 PHE B CZ 1 ATOM 2917 N N . ASN B 1 162 ? 10.898 -4.034 -14.213 1.00 63.60 ? 162 ASN B N 1 ATOM 2918 C CA . ASN B 1 162 ? 11.601 -4.893 -13.267 1.00 76.83 ? 162 ASN B CA 1 ATOM 2919 C C . ASN B 1 162 ? 13.108 -4.766 -13.476 1.00 90.06 ? 162 ASN B C 1 ATOM 2920 O O . ASN B 1 162 ? 13.584 -4.699 -14.620 1.00 101.23 ? 162 ASN B O 1 ATOM 2921 C CB . ASN B 1 162 ? 11.154 -6.358 -13.407 1.00 82.30 ? 162 ASN B CB 1 ATOM 2922 C CG . ASN B 1 162 ? 11.095 -6.824 -14.839 1.00 93.65 ? 162 ASN B CG 1 ATOM 2923 O OD1 . ASN B 1 162 ? 10.792 -6.049 -15.742 1.00 108.47 ? 162 ASN B OD1 1 ATOM 2924 N ND2 . ASN B 1 162 ? 11.349 -8.111 -15.054 1.00 96.10 ? 162 ASN B ND2 1 ATOM 2925 N N . ALA B 1 163 ? 13.857 -4.686 -12.380 1.00 75.62 ? 163 ALA B N 1 ATOM 2926 C CA . ALA B 1 163 ? 15.320 -4.596 -12.508 1.00 74.67 ? 163 ALA B CA 1 ATOM 2927 C C . ALA B 1 163 ? 15.916 -5.889 -13.027 1.00 73.35 ? 163 ALA B C 1 ATOM 2928 O O . ALA B 1 163 ? 16.938 -5.837 -13.690 1.00 88.85 ? 163 ALA B O 1 ATOM 2929 C CB . ALA B 1 163 ? 15.971 -4.240 -11.196 1.00 92.76 ? 163 ALA B CB 1 ATOM 2930 N N . LEU B 1 164 ? 15.318 -7.042 -12.700 1.00 71.67 ? 164 LEU B N 1 ATOM 2931 C CA . LEU B 1 164 ? 15.670 -8.290 -13.393 1.00 89.17 ? 164 LEU B CA 1 ATOM 2932 C C . LEU B 1 164 ? 14.600 -9.379 -13.247 1.00 105.50 ? 164 LEU B C 1 ATOM 2933 O O . LEU B 1 164 ? 13.656 -9.254 -12.456 1.00 109.80 ? 164 LEU B O 1 ATOM 2934 C CB . LEU B 1 164 ? 17.044 -8.835 -12.963 1.00 88.50 ? 164 LEU B CB 1 ATOM 2935 C CG . LEU B 1 164 ? 17.596 -9.553 -11.733 1.00 98.59 ? 164 LEU B CG 1 ATOM 2936 C CD1 . LEU B 1 164 ? 17.321 -11.073 -11.797 1.00 104.69 ? 164 LEU B CD1 1 ATOM 2937 C CD2 . LEU B 1 164 ? 19.087 -9.257 -11.675 1.00 86.30 ? 164 LEU B CD2 1 ATOM 2938 N N . ASP B 1 165 ? 14.756 -10.435 -14.047 1.00 115.42 ? 165 ASP B N 1 ATOM 2939 C CA . ASP B 1 165 ? 13.702 -11.417 -14.292 1.00 122.41 ? 165 ASP B CA 1 ATOM 2940 C C . ASP B 1 165 ? 13.541 -12.429 -13.181 1.00 116.17 ? 165 ASP B C 1 ATOM 2941 O O . ASP B 1 165 ? 13.128 -13.569 -13.410 1.00 105.80 ? 165 ASP B O 1 ATOM 2942 C CB . ASP B 1 165 ? 13.959 -12.169 -15.609 1.00 136.14 ? 165 ASP B CB 1 ATOM 2943 C CG . ASP B 1 165 ? 13.744 -11.301 -16.839 1.00 143.94 ? 165 ASP B CG 1 ATOM 2944 O OD1 . ASP B 1 165 ? 14.044 -10.089 -16.764 1.00 144.33 ? 165 ASP B OD1 1 ATOM 2945 O OD2 . ASP B 1 165 ? 13.262 -11.830 -17.871 1.00 145.05 ? 165 ASP B OD2 1 ATOM 2946 N N . SER B 1 166 ? 13.841 -11.995 -11.971 1.00 119.49 ? 166 SER B N 1 ATOM 2947 C CA . SER B 1 166 ? 13.453 -12.732 -10.788 1.00 133.07 ? 166 SER B CA 1 ATOM 2948 C C . SER B 1 166 ? 13.248 -11.728 -9.691 1.00 133.76 ? 166 SER B C 1 ATOM 2949 O O . SER B 1 166 ? 13.603 -10.561 -9.836 1.00 132.42 ? 166 SER B O 1 ATOM 2950 C CB . SER B 1 166 ? 14.503 -13.771 -10.387 1.00 142.11 ? 166 SER B CB 1 ATOM 2951 O OG . SER B 1 166 ? 14.591 -14.811 -11.346 1.00 149.91 ? 166 SER B OG 1 ATOM 2952 N N . GLY B 1 167 ? 12.592 -12.158 -8.629 1.00 137.64 ? 167 GLY B N 1 ATOM 2953 C CA . GLY B 1 167 ? 12.611 -11.397 -7.400 1.00 141.14 ? 167 GLY B CA 1 ATOM 2954 C C . GLY B 1 167 ? 13.790 -11.966 -6.645 1.00 138.34 ? 167 GLY B C 1 ATOM 2955 O O . GLY B 1 167 ? 13.907 -13.188 -6.539 1.00 139.60 ? 167 GLY B O 1 ATOM 2956 N N . ASP B 1 168 ? 14.656 -11.093 -6.133 1.00 137.49 ? 168 ASP B N 1 ATOM 2957 C CA . ASP B 1 168 ? 15.873 -11.513 -5.432 1.00 130.50 ? 168 ASP B CA 1 ATOM 2958 C C . ASP B 1 168 ? 15.648 -12.506 -4.295 1.00 117.16 ? 168 ASP B C 1 ATOM 2959 O O . ASP B 1 168 ? 15.101 -12.161 -3.243 1.00 103.17 ? 168 ASP B O 1 ATOM 2960 C CB . ASP B 1 168 ? 16.618 -10.313 -4.872 1.00 135.43 ? 168 ASP B CB 1 ATOM 2961 C CG . ASP B 1 168 ? 17.924 -10.716 -4.242 1.00 148.00 ? 168 ASP B CG 1 ATOM 2962 O OD1 . ASP B 1 168 ? 18.543 -11.678 -4.751 1.00 146.72 ? 168 ASP B OD1 1 ATOM 2963 O OD2 . ASP B 1 168 ? 18.319 -10.101 -3.231 1.00 154.09 ? 168 ASP B OD2 1 ATOM 2964 N N . LEU B 1 169 ? 16.108 -13.734 -4.522 1.00 113.40 ? 169 LEU B N 1 ATOM 2965 C CA . LEU B 1 169 ? 16.069 -14.767 -3.508 1.00 106.77 ? 169 LEU B CA 1 ATOM 2966 C C . LEU B 1 169 ? 17.072 -14.406 -2.428 1.00 114.32 ? 169 LEU B C 1 ATOM 2967 O O . LEU B 1 169 ? 16.651 -14.146 -1.308 1.00 107.51 ? 169 LEU B O 1 ATOM 2968 C CB . LEU B 1 169 ? 16.338 -16.176 -4.115 1.00 109.33 ? 169 LEU B CB 1 ATOM 2969 C CG . LEU B 1 169 ? 17.295 -16.527 -5.308 1.00 103.56 ? 169 LEU B CG 1 ATOM 2970 C CD1 . LEU B 1 169 ? 18.820 -16.496 -5.051 1.00 99.54 ? 169 LEU B CD1 1 ATOM 2971 C CD2 . LEU B 1 169 ? 16.920 -17.872 -5.990 1.00 88.77 ? 169 LEU B CD2 1 ATOM 2972 N N . SER B 1 170 ? 18.354 -14.283 -2.807 1.00 121.35 ? 170 SER B N 1 ATOM 2973 C CA . SER B 1 170 ? 19.557 -14.111 -1.933 1.00 129.99 ? 170 SER B CA 1 ATOM 2974 C C . SER B 1 170 ? 19.330 -14.018 -0.411 1.00 132.46 ? 170 SER B C 1 ATOM 2975 O O . SER B 1 170 ? 19.868 -14.836 0.339 1.00 125.00 ? 170 SER B O 1 ATOM 2976 C CB . SER B 1 170 ? 20.369 -12.881 -2.387 1.00 122.95 ? 170 SER B CB 1 ATOM 2977 O OG . SER B 1 170 ? 20.090 -11.722 -1.617 1.00 123.57 ? 170 SER B OG 1 ATOM 2978 N N . ASP B 1 171 ? 18.554 -13.022 0.030 1.00 138.09 ? 171 ASP B N 1 ATOM 2979 C CA . ASP B 1 171 ? 18.148 -12.881 1.435 1.00 129.48 ? 171 ASP B CA 1 ATOM 2980 C C . ASP B 1 171 ? 16.780 -13.524 1.679 1.00 135.45 ? 171 ASP B C 1 ATOM 2981 O O . ASP B 1 171 ? 15.983 -13.032 2.477 1.00 146.30 ? 171 ASP B O 1 ATOM 2982 C CB . ASP B 1 171 ? 18.087 -11.405 1.818 1.00 126.62 ? 171 ASP B CB 1 ATOM 2983 C CG . ASP B 1 171 ? 19.186 -10.595 1.174 1.00 137.35 ? 171 ASP B CG 1 ATOM 2984 O OD1 . ASP B 1 171 ? 20.362 -11.015 1.261 1.00 141.74 ? 171 ASP B OD1 1 ATOM 2985 O OD2 . ASP B 1 171 ? 18.867 -9.562 0.540 1.00 130.64 ? 171 ASP B OD2 1 ATOM 2986 N N . PHE B 1 172 ? 16.518 -14.619 0.971 1.00 131.79 ? 172 PHE B N 1 ATOM 2987 C CA . PHE B 1 172 ? 15.380 -15.492 1.233 1.00 114.22 ? 172 PHE B CA 1 ATOM 2988 C C . PHE B 1 172 ? 15.784 -16.406 2.393 1.00 128.29 ? 172 PHE B C 1 ATOM 2989 O O . PHE B 1 172 ? 16.976 -16.631 2.596 1.00 131.10 ? 172 PHE B O 1 ATOM 2990 C CB . PHE B 1 172 ? 14.988 -16.267 -0.030 1.00 95.75 ? 172 PHE B CB 1 ATOM 2991 C CG . PHE B 1 172 ? 14.101 -17.456 0.222 1.00 91.96 ? 172 PHE B CG 1 ATOM 2992 C CD1 . PHE B 1 172 ? 12.809 -17.299 0.740 1.00 87.50 ? 172 PHE B CD1 1 ATOM 2993 C CD2 . PHE B 1 172 ? 14.545 -18.734 -0.091 1.00 94.77 ? 172 PHE B CD2 1 ATOM 2994 C CE1 . PHE B 1 172 ? 11.975 -18.386 0.956 1.00 86.83 ? 172 PHE B CE1 1 ATOM 2995 C CE2 . PHE B 1 172 ? 13.725 -19.835 0.126 1.00 97.05 ? 172 PHE B CE2 1 ATOM 2996 C CZ . PHE B 1 172 ? 12.432 -19.659 0.651 1.00 94.00 ? 172 PHE B CZ 1 ATOM 2997 N N . ILE B 1 173 ? 14.811 -16.931 3.141 1.00 130.74 ? 173 ILE B N 1 ATOM 2998 C CA . ILE B 1 173 ? 15.083 -17.540 4.443 1.00 133.80 ? 173 ILE B CA 1 ATOM 2999 C C . ILE B 1 173 ? 14.707 -19.048 4.513 1.00 137.52 ? 173 ILE B C 1 ATOM 3000 O O . ILE B 1 173 ? 15.226 -19.773 5.373 1.00 156.42 ? 173 ILE B O 1 ATOM 3001 C CB . ILE B 1 173 ? 14.339 -16.713 5.580 1.00 96.24 ? 173 ILE B CB 1 ATOM 3002 C CG1 . ILE B 1 173 ? 14.859 -15.259 5.622 1.00 97.51 ? 173 ILE B CG1 1 ATOM 3003 C CG2 . ILE B 1 173 ? 14.575 -17.316 6.965 1.00 81.54 ? 173 ILE B CG2 1 ATOM 3004 C CD1 . ILE B 1 173 ? 14.280 -14.417 6.750 1.00 94.38 ? 173 ILE B CD1 1 ATOM 3005 N N . GLU B 1 174 ? 13.926 -19.546 3.556 1.00 123.67 ? 174 GLU B N 1 ATOM 3006 C CA . GLU B 1 174 ? 13.493 -20.938 3.577 1.00 117.09 ? 174 GLU B CA 1 ATOM 3007 C C . GLU B 1 174 ? 12.713 -21.246 4.869 1.00 130.27 ? 174 GLU B C 1 ATOM 3008 O O . GLU B 1 174 ? 13.288 -21.736 5.824 1.00 129.65 ? 174 GLU B O 1 ATOM 3009 C CB . GLU B 1 174 ? 14.716 -21.906 3.422 1.00 127.13 ? 174 GLU B CB 1 ATOM 3010 C CG . GLU B 1 174 ? 15.264 -22.130 2.020 1.00 137.59 ? 174 GLU B CG 1 ATOM 3011 C CD . GLU B 1 174 ? 16.367 -21.165 1.593 1.00 155.16 ? 174 GLU B CD 1 ATOM 3012 O OE1 . GLU B 1 174 ? 16.588 -20.144 2.276 1.00 158.38 ? 174 GLU B OE1 1 ATOM 3013 O OE2 . GLU B 1 174 ? 17.005 -21.434 0.545 1.00 162.39 ? 174 GLU B OE2 1 ATOM 3014 N N . ASP B 1 175 ? 11.409 -20.981 4.925 1.00 132.80 ? 175 ASP B N 1 ATOM 3015 C CA . ASP B 1 175 ? 10.699 -21.409 6.148 1.00 142.20 ? 175 ASP B CA 1 ATOM 3016 C C . ASP B 1 175 ? 10.654 -22.986 6.251 1.00 143.93 ? 175 ASP B C 1 ATOM 3017 O O . ASP B 1 175 ? 11.399 -23.639 5.560 1.00 136.22 ? 175 ASP B O 1 ATOM 3018 C CB . ASP B 1 175 ? 9.333 -20.620 6.266 1.00 157.49 ? 175 ASP B CB 1 ATOM 3019 C CG . ASP B 1 175 ? 8.180 -21.130 5.444 1.00 161.22 ? 175 ASP B CG 1 ATOM 3020 O OD1 . ASP B 1 175 ? 8.104 -22.286 5.039 1.00 163.40 ? 175 ASP B OD1 1 ATOM 3021 O OD2 . ASP B 1 175 ? 7.302 -20.270 5.199 1.00 162.60 ? 175 ASP B OD2 1 ATOM 3022 N N . VAL B 1 176 ? 9.887 -23.645 7.110 1.00 152.70 ? 176 VAL B N 1 ATOM 3023 C CA . VAL B 1 176 ? 10.216 -25.089 7.274 1.00 144.53 ? 176 VAL B CA 1 ATOM 3024 C C . VAL B 1 176 ? 9.509 -26.020 6.246 1.00 151.09 ? 176 VAL B C 1 ATOM 3025 O O . VAL B 1 176 ? 9.955 -27.128 5.994 1.00 154.47 ? 176 VAL B O 1 ATOM 3026 C CB . VAL B 1 176 ? 10.033 -25.563 8.772 1.00 160.62 ? 176 VAL B CB 1 ATOM 3027 C CG1 . VAL B 1 176 ? 10.191 -27.078 8.896 1.00 160.20 ? 176 VAL B CG1 1 ATOM 3028 C CG2 . VAL B 1 176 ? 11.135 -24.904 9.616 1.00 157.93 ? 176 VAL B CG2 1 ATOM 3029 N N . GLU B 1 177 ? 8.328 -25.626 5.799 1.00 145.60 ? 177 GLU B N 1 ATOM 3030 C CA . GLU B 1 177 ? 8.224 -25.023 4.460 1.00 163.30 ? 177 GLU B CA 1 ATOM 3031 C C . GLU B 1 177 ? 7.149 -25.080 3.424 1.00 144.59 ? 177 GLU B C 1 ATOM 3032 O O . GLU B 1 177 ? 6.542 -26.114 3.084 1.00 149.73 ? 177 GLU B O 1 ATOM 3033 C CB . GLU B 1 177 ? 9.452 -25.334 3.582 1.00 177.69 ? 177 GLU B CB 1 ATOM 3034 C CG . GLU B 1 177 ? 10.071 -23.958 3.200 1.00 187.90 ? 177 GLU B CG 1 ATOM 3035 C CD . GLU B 1 177 ? 11.353 -23.933 2.430 1.00 185.76 ? 177 GLU B CD 1 ATOM 3036 O OE1 . GLU B 1 177 ? 11.319 -24.108 1.236 1.00 181.51 ? 177 GLU B OE1 1 ATOM 3037 O OE2 . GLU B 1 177 ? 12.418 -23.827 3.027 1.00 185.26 ? 177 GLU B OE2 1 ATOM 3038 N N . TRP B 1 178 ? 7.058 -23.843 2.911 1.00 135.58 ? 178 TRP B N 1 ATOM 3039 C CA . TRP B 1 178 ? 6.682 -23.463 1.563 1.00 142.18 ? 178 TRP B CA 1 ATOM 3040 C C . TRP B 1 178 ? 7.952 -22.861 0.925 1.00 143.83 ? 178 TRP B C 1 ATOM 3041 O O . TRP B 1 178 ? 8.585 -21.942 1.477 1.00 148.89 ? 178 TRP B O 1 ATOM 3042 C CB . TRP B 1 178 ? 5.525 -22.460 1.530 1.00 128.41 ? 178 TRP B CB 1 ATOM 3043 C CG . TRP B 1 178 ? 4.216 -23.063 1.824 1.00 124.37 ? 178 TRP B CG 1 ATOM 3044 C CD1 . TRP B 1 178 ? 3.495 -22.906 2.950 1.00 126.17 ? 178 TRP B CD1 1 ATOM 3045 C CD2 . TRP B 1 178 ? 3.480 -23.959 0.989 1.00 127.54 ? 178 TRP B CD2 1 ATOM 3046 N NE1 . TRP B 1 178 ? 2.334 -23.620 2.868 1.00 125.72 ? 178 TRP B NE1 1 ATOM 3047 C CE2 . TRP B 1 178 ? 2.304 -24.285 1.674 1.00 126.66 ? 178 TRP B CE2 1 ATOM 3048 C CE3 . TRP B 1 178 ? 3.697 -24.507 -0.277 1.00 138.11 ? 178 TRP B CE3 1 ATOM 3049 C CZ2 . TRP B 1 178 ? 1.344 -25.140 1.144 1.00 135.37 ? 178 TRP B CZ2 1 ATOM 3050 C CZ3 . TRP B 1 178 ? 2.742 -25.356 -0.805 1.00 143.44 ? 178 TRP B CZ3 1 ATOM 3051 C CH2 . TRP B 1 178 ? 1.579 -25.663 -0.094 1.00 143.08 ? 178 TRP B CH2 1 ATOM 3052 N N . GLU B 1 179 ? 8.228 -23.372 -0.278 1.00 149.02 ? 179 GLU B N 1 ATOM 3053 C CA . GLU B 1 179 ? 9.545 -23.431 -0.922 1.00 141.28 ? 179 GLU B CA 1 ATOM 3054 C C . GLU B 1 179 ? 9.683 -22.797 -2.274 1.00 123.16 ? 179 GLU B C 1 ATOM 3055 O O . GLU B 1 179 ? 9.282 -23.406 -3.267 1.00 125.10 ? 179 GLU B O 1 ATOM 3056 C CB . GLU B 1 179 ? 10.001 -24.914 -1.019 1.00 155.48 ? 179 GLU B CB 1 ATOM 3057 C CG . GLU B 1 179 ? 8.904 -25.833 -1.398 1.00 163.84 ? 179 GLU B CG 1 ATOM 3058 C CD . GLU B 1 179 ? 7.900 -25.971 -0.287 1.00 178.49 ? 179 GLU B CD 1 ATOM 3059 O OE1 . GLU B 1 179 ? 8.228 -26.315 0.866 1.00 178.95 ? 179 GLU B OE1 1 ATOM 3060 O OE2 . GLU B 1 179 ? 6.783 -25.476 -0.522 1.00 182.21 ? 179 GLU B OE2 1 ATOM 3061 N N . VAL B 1 180 ? 10.332 -21.642 -2.324 1.00 94.47 ? 180 VAL B N 1 ATOM 3062 C CA . VAL B 1 180 ? 10.511 -20.953 -3.575 1.00 106.41 ? 180 VAL B CA 1 ATOM 3063 C C . VAL B 1 180 ? 11.264 -21.790 -4.583 1.00 135.83 ? 180 VAL B C 1 ATOM 3064 O O . VAL B 1 180 ? 12.453 -22.073 -4.429 1.00 140.28 ? 180 VAL B O 1 ATOM 3065 C CB . VAL B 1 180 ? 11.254 -19.653 -3.323 1.00 99.50 ? 180 VAL B CB 1 ATOM 3066 C CG1 . VAL B 1 180 ? 11.990 -19.047 -4.652 1.00 69.35 ? 180 VAL B CG1 1 ATOM 3067 C CG2 . VAL B 1 180 ? 10.334 -18.687 -2.556 1.00 80.67 ? 180 VAL B CG2 1 ATOM 3068 N N . HIS B 1 181 ? 10.526 -22.176 -5.619 1.00 169.60 ? 181 HIS B N 1 ATOM 3069 C CA . HIS B 1 181 ? 11.063 -22.914 -6.733 1.00 175.04 ? 181 HIS B CA 1 ATOM 3070 C C . HIS B 1 181 ? 11.419 -21.930 -7.810 1.00 166.77 ? 181 HIS B C 1 ATOM 3071 O O . HIS B 1 181 ? 12.449 -22.040 -8.473 1.00 172.96 ? 181 HIS B O 1 ATOM 3072 C CB . HIS B 1 181 ? 10.043 -23.932 -7.221 1.00 186.46 ? 181 HIS B CB 1 ATOM 3073 C CG . HIS B 1 181 ? 9.981 -25.151 -6.368 1.00 199.93 ? 181 HIS B CG 1 ATOM 3074 N ND1 . HIS B 1 181 ? 9.802 -25.089 -4.997 1.00 208.36 ? 181 HIS B ND1 1 ATOM 3075 C CD2 . HIS B 1 181 ? 10.130 -26.463 -6.663 1.00 205.51 ? 181 HIS B CD2 1 ATOM 3076 C CE1 . HIS B 1 181 ? 9.816 -26.308 -4.500 1.00 210.66 ? 181 HIS B CE1 1 ATOM 3077 N NE2 . HIS B 1 181 ? 10.016 -27.164 -5.489 1.00 211.15 ? 181 HIS B NE2 1 ATOM 3078 N N . GLY B 1 182 ? 10.549 -20.946 -7.962 1.00 142.70 ? 182 GLY B N 1 ATOM 3079 C CA . GLY B 1 182 ? 10.803 -19.868 -8.881 1.00 127.22 ? 182 GLY B CA 1 ATOM 3080 C C . GLY B 1 182 ? 10.123 -18.609 -8.418 1.00 112.85 ? 182 GLY B C 1 ATOM 3081 O O . GLY B 1 182 ? 9.109 -18.684 -7.752 1.00 98.78 ? 182 GLY B O 1 ATOM 3082 N N . MET B 1 183 ? 10.680 -17.460 -8.788 1.00 120.59 ? 183 MET B N 1 ATOM 3083 C CA . MET B 1 183 ? 9.996 -16.176 -8.659 1.00 118.44 ? 183 MET B CA 1 ATOM 3084 C C . MET B 1 183 ? 10.178 -15.306 -9.918 1.00 106.20 ? 183 MET B C 1 ATOM 3085 O O . MET B 1 183 ? 10.656 -14.170 -9.836 1.00 101.50 ? 183 MET B O 1 ATOM 3086 C CB . MET B 1 183 ? 10.503 -15.435 -7.409 1.00 123.53 ? 183 MET B CB 1 ATOM 3087 C CG . MET B 1 183 ? 9.543 -14.355 -6.901 1.00 126.78 ? 183 MET B CG 1 ATOM 3088 S SD . MET B 1 183 ? 10.245 -13.145 -5.749 1.00 93.38 ? 183 MET B SD 1 ATOM 3089 C CE . MET B 1 183 ? 8.793 -12.191 -5.355 1.00 86.46 ? 183 MET B CE 1 ATOM 3090 N N . PRO B 1 184 ? 9.741 -15.815 -11.084 1.00 106.34 ? 184 PRO B N 1 ATOM 3091 C CA . PRO B 1 184 ? 10.011 -15.040 -12.305 1.00 101.27 ? 184 PRO B CA 1 ATOM 3092 C C . PRO B 1 184 ? 9.271 -13.712 -12.301 1.00 91.17 ? 184 PRO B C 1 ATOM 3093 O O . PRO B 1 184 ? 8.150 -13.622 -11.787 1.00 103.27 ? 184 PRO B O 1 ATOM 3094 C CB . PRO B 1 184 ? 9.484 -15.945 -13.424 1.00 104.91 ? 184 PRO B CB 1 ATOM 3095 C CG . PRO B 1 184 ? 8.421 -16.793 -12.750 1.00 104.74 ? 184 PRO B CG 1 ATOM 3096 C CD . PRO B 1 184 ? 8.927 -17.019 -11.351 1.00 103.26 ? 184 PRO B CD 1 ATOM 3097 N N . ALA B 1 185 ? 9.873 -12.702 -12.907 1.00 75.74 ? 185 ALA B N 1 ATOM 3098 C CA . ALA B 1 185 ? 9.253 -11.392 -12.943 1.00 67.30 ? 185 ALA B CA 1 ATOM 3099 C C . ALA B 1 185 ? 8.840 -11.111 -14.344 1.00 82.16 ? 185 ALA B C 1 ATOM 3100 O O . ALA B 1 185 ? 9.511 -11.501 -15.298 1.00 87.85 ? 185 ALA B O 1 ATOM 3101 C CB . ALA B 1 185 ? 10.196 -10.327 -12.456 1.00 75.01 ? 185 ALA B CB 1 ATOM 3102 N N . VAL B 1 186 ? 7.723 -10.406 -14.450 1.00 84.13 ? 186 VAL B N 1 ATOM 3103 C CA . VAL B 1 186 ? 7.035 -10.182 -15.702 1.00 59.86 ? 186 VAL B CA 1 ATOM 3104 C C . VAL B 1 186 ? 6.426 -8.784 -15.726 1.00 67.18 ? 186 VAL B C 1 ATOM 3105 O O . VAL B 1 186 ? 5.895 -8.337 -14.727 1.00 88.78 ? 186 VAL B O 1 ATOM 3106 C CB . VAL B 1 186 ? 5.936 -11.243 -15.889 1.00 58.40 ? 186 VAL B CB 1 ATOM 3107 C CG1 . VAL B 1 186 ? 5.037 -10.916 -17.141 1.00 64.26 ? 186 VAL B CG1 1 ATOM 3108 C CG2 . VAL B 1 186 ? 6.560 -12.654 -15.973 1.00 55.90 ? 186 VAL B CG2 1 ATOM 3109 N N . LYS B 1 187 ? 6.508 -8.097 -16.855 1.00 66.73 ? 187 LYS B N 1 ATOM 3110 C CA . LYS B 1 187 ? 5.958 -6.767 -16.990 1.00 67.77 ? 187 LYS B CA 1 ATOM 3111 C C . LYS B 1 187 ? 4.787 -6.794 -17.983 1.00 78.65 ? 187 LYS B C 1 ATOM 3112 O O . LYS B 1 187 ? 4.949 -7.242 -19.114 1.00 88.82 ? 187 LYS B O 1 ATOM 3113 C CB . LYS B 1 187 ? 7.029 -5.795 -17.456 1.00 71.26 ? 187 LYS B CB 1 ATOM 3114 C CG . LYS B 1 187 ? 6.542 -4.378 -17.712 1.00 79.56 ? 187 LYS B CG 1 ATOM 3115 C CD . LYS B 1 187 ? 7.647 -3.555 -18.379 1.00 91.88 ? 187 LYS B CD 1 ATOM 3116 C CE . LYS B 1 187 ? 7.207 -2.143 -18.676 1.00 94.68 ? 187 LYS B CE 1 ATOM 3117 N NZ . LYS B 1 187 ? 5.979 -2.174 -19.462 1.00 99.55 ? 187 LYS B NZ 1 ATOM 3118 N N . ASN B 1 188 ? 3.614 -6.331 -17.554 1.00 61.78 ? 188 ASN B N 1 ATOM 3119 C CA . ASN B 1 188 ? 2.439 -6.317 -18.394 1.00 71.61 ? 188 ASN B CA 1 ATOM 3120 C C . ASN B 1 188 ? 1.885 -4.909 -18.440 1.00 75.40 ? 188 ASN B C 1 ATOM 3121 O O . ASN B 1 188 ? 2.409 -4.015 -17.768 1.00 69.96 ? 188 ASN B O 1 ATOM 3122 C CB . ASN B 1 188 ? 1.390 -7.296 -17.877 1.00 81.92 ? 188 ASN B CB 1 ATOM 3123 C CG . ASN B 1 188 ? 1.910 -8.716 -17.824 1.00 97.86 ? 188 ASN B CG 1 ATOM 3124 O OD1 . ASN B 1 188 ? 2.897 -9.045 -18.485 1.00 105.44 ? 188 ASN B OD1 1 ATOM 3125 N ND2 . ASN B 1 188 ? 1.271 -9.560 -17.015 1.00 95.12 ? 188 ASN B ND2 1 ATOM 3126 N N . VAL B 1 189 ? 0.896 -4.686 -19.295 1.00 85.59 ? 189 VAL B N 1 ATOM 3127 C CA . VAL B 1 189 ? 0.139 -3.451 -19.219 1.00 91.02 ? 189 VAL B CA 1 ATOM 3128 C C . VAL B 1 189 ? -1.313 -3.761 -18.987 1.00 93.03 ? 189 VAL B C 1 ATOM 3129 O O . VAL B 1 189 ? -1.771 -4.842 -19.332 1.00 103.21 ? 189 VAL B O 1 ATOM 3130 C CB . VAL B 1 189 ? 0.264 -2.609 -20.455 1.00 92.16 ? 189 VAL B CB 1 ATOM 3131 C CG1 . VAL B 1 189 ? 1.694 -2.103 -20.556 1.00 83.80 ? 189 VAL B CG1 1 ATOM 3132 C CG2 . VAL B 1 189 ? -0.150 -3.424 -21.655 1.00 98.55 ? 189 VAL B CG2 1 ATOM 3133 N N . ILE B 1 190 ? -1.996 -2.830 -18.324 1.00 82.26 ? 190 ILE B N 1 ATOM 3134 C CA . ILE B 1 190 ? -3.427 -2.879 -18.081 1.00 65.78 ? 190 ILE B CA 1 ATOM 3135 C C . ILE B 1 190 ? -4.085 -1.664 -18.726 1.00 77.14 ? 190 ILE B C 1 ATOM 3136 O O . ILE B 1 190 ? -3.553 -0.554 -18.656 1.00 83.89 ? 190 ILE B O 1 ATOM 3137 C CB . ILE B 1 190 ? -3.738 -2.886 -16.627 1.00 76.07 ? 190 ILE B CB 1 ATOM 3138 C CG1 . ILE B 1 190 ? -2.795 -3.803 -15.860 1.00 74.74 ? 190 ILE B CG1 1 ATOM 3139 C CG2 . ILE B 1 190 ? -5.132 -3.408 -16.421 1.00 94.25 ? 190 ILE B CG2 1 ATOM 3140 C CD1 . ILE B 1 190 ? -3.067 -5.285 -16.094 1.00 74.72 ? 190 ILE B CD1 1 ATOM 3141 N N . SER B 1 191 ? -5.190 -1.895 -19.423 1.00 79.79 ? 191 SER B N 1 ATOM 3142 C CA . SER B 1 191 ? -5.844 -0.873 -20.260 1.00 94.23 ? 191 SER B CA 1 ATOM 3143 C C . SER B 1 191 ? -6.697 0.208 -19.557 1.00 86.97 ? 191 SER B C 1 ATOM 3144 O O . SER B 1 191 ? -6.516 1.387 -19.803 1.00 86.38 ? 191 SER B O 1 ATOM 3145 C CB . SER B 1 191 ? -6.656 -1.593 -21.315 1.00 101.35 ? 191 SER B CB 1 ATOM 3146 O OG . SER B 1 191 ? -7.185 -2.746 -20.699 1.00 108.00 ? 191 SER B OG 1 ATOM 3147 N N . TYR B 1 192 ? -7.698 -0.206 -18.790 1.00 71.38 ? 192 TYR B N 1 ATOM 3148 C CA . TYR B 1 192 ? -8.587 0.723 -18.071 1.00 79.40 ? 192 TYR B CA 1 ATOM 3149 C C . TYR B 1 192 ? -9.423 1.640 -18.948 1.00 93.98 ? 192 TYR B C 1 ATOM 3150 O O . TYR B 1 192 ? -8.892 2.515 -19.650 1.00 108.95 ? 192 TYR B O 1 ATOM 3151 C CB . TYR B 1 192 ? -7.761 1.544 -17.099 1.00 92.09 ? 192 TYR B CB 1 ATOM 3152 C CG . TYR B 1 192 ? -7.304 0.726 -15.926 1.00 78.42 ? 192 TYR B CG 1 ATOM 3153 C CD1 . TYR B 1 192 ? -8.210 0.266 -14.989 1.00 67.57 ? 192 TYR B CD1 1 ATOM 3154 C CD2 . TYR B 1 192 ? -5.977 0.393 -15.777 1.00 67.39 ? 192 TYR B CD2 1 ATOM 3155 C CE1 . TYR B 1 192 ? -7.802 -0.513 -13.957 1.00 76.11 ? 192 TYR B CE1 1 ATOM 3156 C CE2 . TYR B 1 192 ? -5.567 -0.381 -14.723 1.00 63.65 ? 192 TYR B CE2 1 ATOM 3157 C CZ . TYR B 1 192 ? -6.475 -0.834 -13.824 1.00 73.30 ? 192 TYR B CZ 1 ATOM 3158 O OH . TYR B 1 192 ? -6.013 -1.604 -12.786 1.00 86.90 ? 192 TYR B OH 1 ATOM 3159 N N . GLY B 1 193 ? -10.746 1.446 -18.888 1.00 91.37 ? 193 GLY B N 1 ATOM 3160 C CA . GLY B 1 193 ? -11.657 2.118 -19.796 1.00 85.24 ? 193 GLY B CA 1 ATOM 3161 C C . GLY B 1 193 ? -11.713 3.620 -19.595 1.00 94.56 ? 193 GLY B C 1 ATOM 3162 O O . GLY B 1 193 ? -12.351 4.361 -20.361 1.00 106.57 ? 193 GLY B O 1 ATOM 3163 N N . CYS B 1 194 ? -11.007 4.067 -18.569 1.00 96.86 ? 194 CYS B N 1 ATOM 3164 C CA . CYS B 1 194 ? -11.032 5.445 -18.110 1.00 106.41 ? 194 CYS B CA 1 ATOM 3165 C C . CYS B 1 194 ? -10.433 6.385 -19.114 1.00 101.14 ? 194 CYS B C 1 ATOM 3166 O O . CYS B 1 194 ? -10.847 7.537 -19.208 1.00 97.23 ? 194 CYS B O 1 ATOM 3167 C CB . CYS B 1 194 ? -10.253 5.572 -16.812 1.00 111.76 ? 194 CYS B CB 1 ATOM 3168 S SG . CYS B 1 194 ? -8.632 4.870 -16.997 1.00 206.31 ? 194 CYS B SG 1 ATOM 3169 N N . CYS B 1 195 ? -9.409 5.911 -19.816 1.00 110.71 ? 195 CYS B N 1 ATOM 3170 C CA . CYS B 1 195 ? -8.656 6.779 -20.700 1.00 113.06 ? 195 CYS B CA 1 ATOM 3171 C C . CYS B 1 195 ? -7.636 6.055 -21.540 1.00 108.66 ? 195 CYS B C 1 ATOM 3172 O O . CYS B 1 195 ? -7.153 4.978 -21.171 1.00 108.79 ? 195 CYS B O 1 ATOM 3173 C CB . CYS B 1 195 ? -7.940 7.867 -19.901 1.00 117.37 ? 195 CYS B CB 1 ATOM 3174 S SG . CYS B 1 195 ? -6.861 7.290 -18.551 1.00 124.15 ? 195 CYS B SG 1 ATOM 3175 N N . SER B 1 196 ? -7.358 6.663 -22.693 1.00 109.80 ? 196 SER B N 1 ATOM 3176 C CA . SER B 1 196 ? -6.068 6.599 -23.369 1.00 110.69 ? 196 SER B CA 1 ATOM 3177 C C . SER B 1 196 ? -4.928 6.562 -22.354 1.00 121.30 ? 196 SER B C 1 ATOM 3178 O O . SER B 1 196 ? -5.119 6.995 -21.221 1.00 143.97 ? 196 SER B O 1 ATOM 3179 C CB . SER B 1 196 ? -5.945 7.808 -24.287 1.00 105.71 ? 196 SER B CB 1 ATOM 3180 O OG . SER B 1 196 ? -6.225 8.982 -23.531 1.00 107.80 ? 196 SER B OG 1 ATOM 3181 N N . GLU B 1 197 ? -3.750 6.095 -22.768 1.00 106.33 ? 197 GLU B N 1 ATOM 3182 C CA . GLU B 1 197 ? -2.600 5.832 -21.881 1.00 92.64 ? 197 GLU B CA 1 ATOM 3183 C C . GLU B 1 197 ? -2.894 4.524 -21.170 1.00 102.68 ? 197 GLU B C 1 ATOM 3184 O O . GLU B 1 197 ? -3.659 4.520 -20.209 1.00 122.41 ? 197 GLU B O 1 ATOM 3185 C CB . GLU B 1 197 ? -2.338 6.901 -20.787 1.00 130.54 ? 197 GLU B CB 1 ATOM 3186 C CG . GLU B 1 197 ? -2.485 8.417 -21.023 1.00 140.64 ? 197 GLU B CG 1 ATOM 3187 C CD . GLU B 1 197 ? -1.946 8.938 -22.321 1.00 157.27 ? 197 GLU B CD 1 ATOM 3188 O OE1 . GLU B 1 197 ? -1.094 8.267 -22.943 1.00 157.78 ? 197 GLU B OE1 1 ATOM 3189 O OE2 . GLU B 1 197 ? -2.386 10.039 -22.715 1.00 165.03 ? 197 GLU B OE2 1 ATOM 3190 N N . PRO B 1 198 ? -2.265 3.415 -21.572 1.00 93.89 ? 198 PRO B N 1 ATOM 3191 C CA . PRO B 1 198 ? -2.514 2.192 -20.794 1.00 93.07 ? 198 PRO B CA 1 ATOM 3192 C C . PRO B 1 198 ? -1.656 2.155 -19.522 1.00 101.92 ? 198 PRO B C 1 ATOM 3193 O O . PRO B 1 198 ? -0.750 2.978 -19.396 1.00 102.74 ? 198 PRO B O 1 ATOM 3194 C CB . PRO B 1 198 ? -2.143 1.071 -21.774 1.00 87.60 ? 198 PRO B CB 1 ATOM 3195 C CG . PRO B 1 198 ? -1.144 1.671 -22.660 1.00 100.29 ? 198 PRO B CG 1 ATOM 3196 C CD . PRO B 1 198 ? -1.423 3.161 -22.751 1.00 102.73 ? 198 PRO B CD 1 ATOM 3197 N N . TYR B 1 199 ? -1.949 1.250 -18.587 1.00 103.25 ? 199 TYR B N 1 ATOM 3198 C CA . TYR B 1 199 ? -1.277 1.252 -17.264 1.00 97.27 ? 199 TYR B CA 1 ATOM 3199 C C . TYR B 1 199 ? -0.348 0.085 -16.996 1.00 83.23 ? 199 TYR B C 1 ATOM 3200 O O . TYR B 1 199 ? -0.816 -1.042 -16.880 1.00 93.93 ? 199 TYR B O 1 ATOM 3201 C CB . TYR B 1 199 ? -2.311 1.289 -16.122 1.00 92.34 ? 199 TYR B CB 1 ATOM 3202 C CG . TYR B 1 199 ? -2.870 2.669 -15.824 1.00 114.06 ? 199 TYR B CG 1 ATOM 3203 C CD1 . TYR B 1 199 ? -2.955 3.654 -16.805 1.00 121.38 ? 199 TYR B CD1 1 ATOM 3204 C CD2 . TYR B 1 199 ? -3.316 2.991 -14.564 1.00 121.87 ? 199 TYR B CD2 1 ATOM 3205 C CE1 . TYR B 1 199 ? -3.478 4.917 -16.516 1.00 122.40 ? 199 TYR B CE1 1 ATOM 3206 C CE2 . TYR B 1 199 ? -3.837 4.248 -14.277 1.00 122.72 ? 199 TYR B CE2 1 ATOM 3207 C CZ . TYR B 1 199 ? -3.920 5.202 -15.246 1.00 118.24 ? 199 TYR B CZ 1 ATOM 3208 O OH . TYR B 1 199 ? -4.439 6.438 -14.919 1.00 109.12 ? 199 TYR B OH 1 ATOM 3209 N N . PRO B 1 200 ? 0.954 0.366 -16.822 1.00 72.20 ? 200 PRO B N 1 ATOM 3210 C CA . PRO B 1 200 ? 2.085 -0.549 -16.539 1.00 57.95 ? 200 PRO B CA 1 ATOM 3211 C C . PRO B 1 200 ? 2.042 -1.199 -15.162 1.00 65.11 ? 200 PRO B C 1 ATOM 3212 O O . PRO B 1 200 ? 1.625 -0.552 -14.197 1.00 56.38 ? 200 PRO B O 1 ATOM 3213 C CB . PRO B 1 200 ? 3.299 0.366 -16.602 1.00 59.70 ? 200 PRO B CB 1 ATOM 3214 C CG . PRO B 1 200 ? 2.750 1.694 -16.129 1.00 75.88 ? 200 PRO B CG 1 ATOM 3215 C CD . PRO B 1 200 ? 1.369 1.777 -16.777 1.00 77.36 ? 200 PRO B CD 1 ATOM 3216 N N . ASP B 1 201 ? 2.455 -2.469 -15.095 1.00 61.94 ? 201 ASP B N 1 ATOM 3217 C CA . ASP B 1 201 ? 2.498 -3.200 -13.858 1.00 64.80 ? 201 ASP B CA 1 ATOM 3218 C C . ASP B 1 201 ? 3.569 -4.288 -13.960 1.00 95.11 ? 201 ASP B C 1 ATOM 3219 O O . ASP B 1 201 ? 3.802 -4.785 -15.049 1.00 122.27 ? 201 ASP B O 1 ATOM 3220 C CB . ASP B 1 201 ? 1.124 -3.769 -13.523 1.00 62.76 ? 201 ASP B CB 1 ATOM 3221 C CG . ASP B 1 201 ? 0.718 -5.003 -14.343 1.00 74.24 ? 201 ASP B CG 1 ATOM 3222 O OD1 . ASP B 1 201 ? 1.555 -5.708 -14.918 1.00 73.79 ? 201 ASP B OD1 1 ATOM 3223 O OD2 . ASP B 1 201 ? -0.504 -5.307 -14.373 1.00 86.46 ? 201 ASP B OD2 1 ATOM 3224 N N . VAL B 1 202 ? 4.321 -4.570 -12.901 1.00 86.87 ? 202 VAL B N 1 ATOM 3225 C CA . VAL B 1 202 ? 5.152 -5.763 -12.948 1.00 80.27 ? 202 VAL B CA 1 ATOM 3226 C C . VAL B 1 202 ? 4.724 -6.837 -11.943 1.00 69.83 ? 202 VAL B C 1 ATOM 3227 O O . VAL B 1 202 ? 4.268 -6.526 -10.850 1.00 73.30 ? 202 VAL B O 1 ATOM 3228 C CB . VAL B 1 202 ? 6.633 -5.407 -12.791 1.00 97.74 ? 202 VAL B CB 1 ATOM 3229 C CG1 . VAL B 1 202 ? 7.029 -4.414 -13.889 1.00 113.79 ? 202 VAL B CG1 1 ATOM 3230 C CG2 . VAL B 1 202 ? 6.923 -4.849 -11.453 1.00 91.21 ? 202 VAL B CG2 1 ATOM 3231 N N . THR B 1 203 ? 4.899 -8.102 -12.314 1.00 61.97 ? 203 THR B N 1 ATOM 3232 C CA . THR B 1 203 ? 4.388 -9.208 -11.535 1.00 52.36 ? 203 THR B CA 1 ATOM 3233 C C . THR B 1 203 ? 5.371 -10.265 -11.133 1.00 79.27 ? 203 THR B C 1 ATOM 3234 O O . THR B 1 203 ? 5.795 -11.112 -11.923 1.00 81.46 ? 203 THR B O 1 ATOM 3235 C CB . THR B 1 203 ? 3.260 -9.815 -12.288 1.00 56.52 ? 203 THR B CB 1 ATOM 3236 O OG1 . THR B 1 203 ? 2.134 -8.962 -12.080 1.00 80.94 ? 203 THR B OG1 1 ATOM 3237 C CG2 . THR B 1 203 ? 2.909 -11.190 -11.795 1.00 55.66 ? 203 THR B CG2 1 ATOM 3238 N N . PHE B 1 204 ? 5.733 -10.185 -9.860 1.00 75.92 ? 204 PHE B N 1 ATOM 3239 C CA . PHE B 1 204 ? 6.546 -11.192 -9.212 1.00 64.67 ? 204 PHE B CA 1 ATOM 3240 C C . PHE B 1 204 ? 5.678 -12.348 -8.907 1.00 69.01 ? 204 PHE B C 1 ATOM 3241 O O . PHE B 1 204 ? 4.569 -12.186 -8.388 1.00 75.77 ? 204 PHE B O 1 ATOM 3242 C CB . PHE B 1 204 ? 7.183 -10.604 -8.002 1.00 50.09 ? 204 PHE B CB 1 ATOM 3243 C CG . PHE B 1 204 ? 7.990 -9.410 -8.336 1.00 59.03 ? 204 PHE B CG 1 ATOM 3244 C CD1 . PHE B 1 204 ? 9.311 -9.550 -8.784 1.00 50.32 ? 204 PHE B CD1 1 ATOM 3245 C CD2 . PHE B 1 204 ? 7.410 -8.149 -8.299 1.00 52.32 ? 204 PHE B CD2 1 ATOM 3246 C CE1 . PHE B 1 204 ? 10.036 -8.462 -9.137 1.00 59.03 ? 204 PHE B CE1 1 ATOM 3247 C CE2 . PHE B 1 204 ? 8.153 -7.038 -8.660 1.00 54.42 ? 204 PHE B CE2 1 ATOM 3248 C CZ . PHE B 1 204 ? 9.457 -7.194 -9.092 1.00 60.47 ? 204 PHE B CZ 1 ATOM 3249 N N . THR B 1 205 ? 6.118 -13.503 -9.366 1.00 64.42 ? 205 THR B N 1 ATOM 3250 C CA . THR B 1 205 ? 5.223 -14.642 -9.373 1.00 65.57 ? 205 THR B CA 1 ATOM 3251 C C . THR B 1 205 ? 5.904 -15.696 -8.605 1.00 69.19 ? 205 THR B C 1 ATOM 3252 O O . THR B 1 205 ? 6.909 -16.228 -9.035 1.00 87.74 ? 205 THR B O 1 ATOM 3253 C CB . THR B 1 205 ? 4.891 -15.118 -10.823 1.00 97.07 ? 205 THR B CB 1 ATOM 3254 O OG1 . THR B 1 205 ? 4.143 -14.107 -11.522 1.00 97.85 ? 205 THR B OG1 1 ATOM 3255 C CG2 . THR B 1 205 ? 4.104 -16.436 -10.820 1.00 83.05 ? 205 THR B CG2 1 ATOM 3256 N N . LEU B 1 206 ? 5.341 -16.009 -7.469 1.00 86.29 ? 206 LEU B N 1 ATOM 3257 C CA . LEU B 1 206 ? 6.019 -16.786 -6.469 1.00 89.03 ? 206 LEU B CA 1 ATOM 3258 C C . LEU B 1 206 ? 5.445 -18.164 -6.441 1.00 92.76 ? 206 LEU B C 1 ATOM 3259 O O . LEU B 1 206 ? 4.239 -18.339 -6.419 1.00 104.23 ? 206 LEU B O 1 ATOM 3260 C CB . LEU B 1 206 ? 5.879 -16.082 -5.129 1.00 86.03 ? 206 LEU B CB 1 ATOM 3261 C CG . LEU B 1 206 ? 6.760 -16.505 -3.993 1.00 83.93 ? 206 LEU B CG 1 ATOM 3262 C CD1 . LEU B 1 206 ? 8.109 -16.741 -4.517 1.00 94.19 ? 206 LEU B CD1 1 ATOM 3263 C CD2 . LEU B 1 206 ? 6.804 -15.272 -3.171 1.00 80.09 ? 206 LEU B CD2 1 ATOM 3264 N N . LEU B 1 207 ? 6.299 -19.157 -6.482 1.00 88.49 ? 207 LEU B N 1 ATOM 3265 C CA . LEU B 1 207 ? 5.785 -20.503 -6.523 1.00 100.53 ? 207 LEU B CA 1 ATOM 3266 C C . LEU B 1 207 ? 6.428 -21.348 -5.435 1.00 109.51 ? 207 LEU B C 1 ATOM 3267 O O . LEU B 1 207 ? 7.650 -21.404 -5.343 1.00 114.51 ? 207 LEU B O 1 ATOM 3268 C CB . LEU B 1 207 ? 6.012 -21.102 -7.901 1.00 110.31 ? 207 LEU B CB 1 ATOM 3269 C CG . LEU B 1 207 ? 5.392 -22.468 -8.187 1.00 119.03 ? 207 LEU B CG 1 ATOM 3270 C CD1 . LEU B 1 207 ? 3.961 -22.526 -7.745 1.00 110.37 ? 207 LEU B CD1 1 ATOM 3271 C CD2 . LEU B 1 207 ? 5.444 -22.713 -9.676 1.00 129.98 ? 207 LEU B CD2 1 ATOM 3272 N N . LEU B 1 208 ? 5.620 -22.035 -4.633 1.00 107.68 ? 208 LEU B N 1 ATOM 3273 C CA . LEU B 1 208 ? 6.112 -22.696 -3.413 1.00 107.08 ? 208 LEU B CA 1 ATOM 3274 C C . LEU B 1 208 ? 6.030 -24.199 -3.692 1.00 120.50 ? 208 LEU B C 1 ATOM 3275 O O . LEU B 1 208 ? 6.054 -24.468 -4.839 1.00 138.51 ? 208 LEU B O 1 ATOM 3276 C CB . LEU B 1 208 ? 5.264 -22.244 -2.214 1.00 92.75 ? 208 LEU B CB 1 ATOM 3277 C CG . LEU B 1 208 ? 4.739 -20.793 -2.266 1.00 76.06 ? 208 LEU B CG 1 ATOM 3278 C CD1 . LEU B 1 208 ? 3.918 -20.421 -1.048 1.00 74.06 ? 208 LEU B CD1 1 ATOM 3279 C CD2 . LEU B 1 208 ? 5.866 -19.803 -2.406 1.00 74.52 ? 208 LEU B CD2 1 ATOM 3280 N N . LYS B 1 209 ? 6.036 -25.145 -2.727 1.00 117.98 ? 209 LYS B N 1 ATOM 3281 C CA . LYS B 1 209 ? 5.447 -26.548 -2.813 1.00 128.60 ? 209 LYS B CA 1 ATOM 3282 C C . LYS B 1 209 ? 5.839 -27.609 -1.791 1.00 123.18 ? 209 LYS B C 1 ATOM 3283 O O . LYS B 1 209 ? 6.425 -28.596 -2.167 1.00 125.82 ? 209 LYS B O 1 ATOM 3284 C CB . LYS B 1 209 ? 5.638 -27.248 -4.177 1.00 139.40 ? 209 LYS B CB 1 ATOM 3285 C CG . LYS B 1 209 ? 4.670 -26.695 -5.170 1.00 148.27 ? 209 LYS B CG 1 ATOM 3286 C CD . LYS B 1 209 ? 3.493 -26.323 -4.348 1.00 148.44 ? 209 LYS B CD 1 ATOM 3287 C CE . LYS B 1 209 ? 3.026 -24.965 -4.786 1.00 144.98 ? 209 LYS B CE 1 ATOM 3288 N NZ . LYS B 1 209 ? 3.257 -23.710 -4.072 1.00 139.65 ? 209 LYS B NZ 1 ATOM 3289 N N . ARG B 1 210 ? 5.438 -27.399 -0.537 1.00 130.92 ? 210 ARG B N 1 ATOM 3290 C CA . ARG B 1 210 ? 5.588 -28.286 0.637 1.00 130.52 ? 210 ARG B CA 1 ATOM 3291 C C . ARG B 1 210 ? 6.475 -29.527 0.651 1.00 128.72 ? 210 ARG B C 1 ATOM 3292 O O . ARG B 1 210 ? 6.458 -30.368 -0.241 1.00 130.89 ? 210 ARG B O 1 ATOM 3293 C CB . ARG B 1 210 ? 4.193 -28.795 1.080 1.00 134.84 ? 210 ARG B CB 1 ATOM 3294 C CG . ARG B 1 210 ? 3.495 -29.882 0.212 1.00 140.84 ? 210 ARG B CG 1 ATOM 3295 C CD . ARG B 1 210 ? 2.094 -30.190 0.785 1.00 141.65 ? 210 ARG B CD 1 ATOM 3296 N NE . ARG B 1 210 ? 1.253 -28.996 0.683 1.00 137.66 ? 210 ARG B NE 1 ATOM 3297 C CZ . ARG B 1 210 ? -0.044 -28.935 0.967 1.00 138.31 ? 210 ARG B CZ 1 ATOM 3298 N NH1 . ARG B 1 210 ? -0.713 -30.022 1.330 1.00 146.33 ? 210 ARG B NH1 1 ATOM 3299 N NH2 . ARG B 1 210 ? -0.687 -27.784 0.812 1.00 134.20 ? 210 ARG B NH2 1 ATOM 3300 N N . ARG B 1 211 ? 7.202 -29.650 1.746 1.00 135.25 ? 211 ARG B N 1 ATOM 3301 C CA . ARG B 1 211 ? 7.908 -30.865 2.038 1.00 134.31 ? 211 ARG B CA 1 ATOM 3302 C C . ARG B 1 211 ? 6.908 -31.496 2.979 1.00 148.51 ? 211 ARG B C 1 ATOM 3303 O O . ARG B 1 211 ? 6.436 -30.825 3.897 1.00 139.72 ? 211 ARG B O 1 ATOM 3304 C CB . ARG B 1 211 ? 9.262 -30.599 2.655 1.00 153.87 ? 211 ARG B CB 1 ATOM 3305 C CG . ARG B 1 211 ? 9.778 -29.212 2.358 1.00 147.04 ? 211 ARG B CG 1 ATOM 3306 C CD . ARG B 1 211 ? 11.014 -29.025 3.188 1.00 140.76 ? 211 ARG B CD 1 ATOM 3307 N NE . ARG B 1 211 ? 11.545 -27.676 3.157 1.00 132.32 ? 211 ARG B NE 1 ATOM 3308 C CZ . ARG B 1 211 ? 12.515 -27.307 2.336 1.00 131.22 ? 211 ARG B CZ 1 ATOM 3309 N NH1 . ARG B 1 211 ? 13.017 -28.181 1.476 1.00 137.48 ? 211 ARG B NH1 1 ATOM 3310 N NH2 . ARG B 1 211 ? 12.982 -26.077 2.369 1.00 131.53 ? 211 ARG B NH2 1 ATOM 3311 N N . SER B 1 212 ? 6.529 -32.737 2.683 1.00 144.72 ? 212 SER B N 1 ATOM 3312 C CA . SER B 1 212 ? 5.504 -33.493 3.411 1.00 149.21 ? 212 SER B CA 1 ATOM 3313 C C . SER B 1 212 ? 5.346 -33.361 4.937 1.00 147.19 ? 212 SER B C 1 ATOM 3314 O O . SER B 1 212 ? 5.627 -32.349 5.567 1.00 144.15 ? 212 SER B O 1 ATOM 3315 C CB . SER B 1 212 ? 5.715 -34.971 3.122 1.00 151.98 ? 212 SER B CB 1 ATOM 3316 O OG . SER B 1 212 ? 5.384 -35.722 4.274 1.00 151.30 ? 212 SER B OG 1 ATOM 3317 N N . ILE C 2 1 ? 34.658 -10.771 55.871 1.00 85.34 ? 1 ILE C N 1 ATOM 3318 C CA . ILE C 2 1 ? 35.386 -9.673 55.260 1.00 79.00 ? 1 ILE C CA 1 ATOM 3319 C C . ILE C 2 1 ? 34.394 -8.825 54.505 1.00 69.89 ? 1 ILE C C 1 ATOM 3320 O O . ILE C 2 1 ? 33.430 -9.358 54.011 1.00 80.86 ? 1 ILE C O 1 ATOM 3321 C CB . ILE C 2 1 ? 36.541 -10.242 54.378 1.00 88.05 ? 1 ILE C CB 1 ATOM 3322 C CG1 . ILE C 2 1 ? 37.156 -9.210 53.427 1.00 71.76 ? 1 ILE C CG1 1 ATOM 3323 C CG2 . ILE C 2 1 ? 36.027 -11.310 53.473 1.00 102.14 ? 1 ILE C CG2 1 ATOM 3324 C CD1 . ILE C 2 1 ? 37.475 -7.844 53.965 1.00 67.02 ? 1 ILE C CD1 1 ATOM 3325 N N . VAL C 2 2 ? 34.604 -7.507 54.480 1.00 70.46 ? 2 VAL C N 1 ATOM 3326 C CA . VAL C 2 2 ? 33.853 -6.568 53.629 1.00 73.34 ? 2 VAL C CA 1 ATOM 3327 C C . VAL C 2 2 ? 34.649 -6.088 52.392 1.00 95.89 ? 2 VAL C C 1 ATOM 3328 O O . VAL C 2 2 ? 35.629 -5.353 52.535 1.00 114.47 ? 2 VAL C O 1 ATOM 3329 C CB . VAL C 2 2 ? 33.458 -5.328 54.443 1.00 73.56 ? 2 VAL C CB 1 ATOM 3330 C CG1 . VAL C 2 2 ? 32.832 -4.310 53.556 1.00 87.98 ? 2 VAL C CG1 1 ATOM 3331 C CG2 . VAL C 2 2 ? 32.527 -5.692 55.557 1.00 69.33 ? 2 VAL C CG2 1 ATOM 3332 N N . CYS C 2 3 ? 34.206 -6.456 51.188 1.00 92.99 ? 3 CYS C N 1 ATOM 3333 C CA . CYS C 2 3 ? 34.892 -6.146 49.911 1.00 73.82 ? 3 CYS C CA 1 ATOM 3334 C C . CYS C 2 3 ? 34.019 -5.236 49.042 1.00 70.68 ? 3 CYS C C 1 ATOM 3335 O O . CYS C 2 3 ? 32.826 -5.221 49.296 1.00 69.87 ? 3 CYS C O 1 ATOM 3336 C CB . CYS C 2 3 ? 35.175 -7.432 49.146 1.00 66.53 ? 3 CYS C CB 1 ATOM 3337 S SG . CYS C 2 3 ? 35.643 -8.789 50.214 1.00 170.39 ? 3 CYS C SG 1 ATOM 3338 N N . HIS C 2 4 ? 34.557 -4.461 48.082 1.00 60.56 ? 4 HIS C N 1 ATOM 3339 C CA . HIS C 2 4 ? 33.674 -3.855 47.039 1.00 90.99 ? 4 HIS C CA 1 ATOM 3340 C C . HIS C 2 4 ? 33.338 -4.909 45.940 1.00 75.41 ? 4 HIS C C 1 ATOM 3341 O O . HIS C 2 4 ? 34.192 -5.652 45.474 1.00 74.84 ? 4 HIS C O 1 ATOM 3342 C CB . HIS C 2 4 ? 34.307 -2.651 46.342 1.00 87.86 ? 4 HIS C CB 1 ATOM 3343 C CG . HIS C 2 4 ? 34.797 -1.568 47.266 1.00 96.57 ? 4 HIS C CG 1 ATOM 3344 N ND1 . HIS C 2 4 ? 34.063 -0.439 47.564 1.00 95.15 ? 4 HIS C ND1 1 ATOM 3345 C CD2 . HIS C 2 4 ? 36.002 -1.406 47.879 1.00 88.94 ? 4 HIS C CD2 1 ATOM 3346 C CE1 . HIS C 2 4 ? 34.781 0.352 48.348 1.00 98.55 ? 4 HIS C CE1 1 ATOM 3347 N NE2 . HIS C 2 4 ? 35.964 -0.208 48.551 1.00 85.71 ? 4 HIS C NE2 1 ATOM 3348 N N . THR C 2 5 ? 32.114 -4.943 45.468 1.00 91.76 ? 5 THR C N 1 ATOM 3349 C CA . THR C 2 5 ? 31.781 -5.883 44.422 1.00 89.16 ? 5 THR C CA 1 ATOM 3350 C C . THR C 2 5 ? 31.192 -5.021 43.367 1.00 77.84 ? 5 THR C C 1 ATOM 3351 O O . THR C 2 5 ? 30.493 -4.089 43.715 1.00 76.64 ? 5 THR C O 1 ATOM 3352 C CB . THR C 2 5 ? 30.790 -6.956 44.900 1.00 89.96 ? 5 THR C CB 1 ATOM 3353 O OG1 . THR C 2 5 ? 30.334 -7.703 43.770 1.00 90.49 ? 5 THR C OG1 1 ATOM 3354 C CG2 . THR C 2 5 ? 29.593 -6.301 45.498 1.00 86.59 ? 5 THR C CG2 1 ATOM 3355 N N . THR C 2 6 ? 31.427 -5.371 42.102 1.00 84.96 ? 6 THR C N 1 ATOM 3356 C CA . THR C 2 6 ? 31.024 -4.576 40.929 1.00 80.44 ? 6 THR C CA 1 ATOM 3357 C C . THR C 2 6 ? 29.753 -5.102 40.315 1.00 89.00 ? 6 THR C C 1 ATOM 3358 O O . THR C 2 6 ? 29.228 -4.517 39.357 1.00 98.85 ? 6 THR C O 1 ATOM 3359 C CB . THR C 2 6 ? 32.128 -4.531 39.819 1.00 72.26 ? 6 THR C CB 1 ATOM 3360 O OG1 . THR C 2 6 ? 32.916 -5.735 39.835 1.00 66.22 ? 6 THR C OG1 1 ATOM 3361 C CG2 . THR C 2 6 ? 33.005 -3.237 39.825 1.00 55.42 ? 6 THR C CG2 1 ATOM 3362 N N . ALA C 2 7 ? 29.274 -6.214 40.878 1.00 90.64 ? 7 ALA C N 1 ATOM 3363 C CA . ALA C 2 7 ? 27.983 -6.815 40.543 1.00 90.96 ? 7 ALA C CA 1 ATOM 3364 C C . ALA C 2 7 ? 26.796 -5.878 40.810 1.00 88.35 ? 7 ALA C C 1 ATOM 3365 O O . ALA C 2 7 ? 25.651 -6.148 40.414 1.00 79.76 ? 7 ALA C O 1 ATOM 3366 C CB . ALA C 2 7 ? 27.813 -8.117 41.351 1.00 83.17 ? 7 ALA C CB 1 ATOM 3367 N N . THR C 2 8 ? 27.103 -4.716 41.363 1.00 87.16 ? 8 THR C N 1 ATOM 3368 C CA . THR C 2 8 ? 26.091 -3.896 41.978 1.00 96.95 ? 8 THR C CA 1 ATOM 3369 C C . THR C 2 8 ? 26.076 -2.543 41.316 1.00 89.23 ? 8 THR C C 1 ATOM 3370 O O . THR C 2 8 ? 27.104 -2.021 40.911 1.00 92.13 ? 8 THR C O 1 ATOM 3371 C CB . THR C 2 8 ? 26.376 -3.741 43.530 1.00 69.77 ? 8 THR C CB 1 ATOM 3372 O OG1 . THR C 2 8 ? 25.214 -3.281 44.207 1.00 71.96 ? 8 THR C OG1 1 ATOM 3373 C CG2 . THR C 2 8 ? 27.454 -2.737 43.784 1.00 61.35 ? 8 THR C CG2 1 ATOM 3374 N N . SER C 2 9 ? 24.896 -1.965 41.208 1.00 83.26 ? 9 SER C N 1 ATOM 3375 C CA . SER C 2 9 ? 24.757 -0.706 40.505 1.00 78.10 ? 9 SER C CA 1 ATOM 3376 C C . SER C 2 9 ? 23.961 0.249 41.402 1.00 91.76 ? 9 SER C C 1 ATOM 3377 O O . SER C 2 9 ? 22.830 -0.077 41.777 1.00 97.60 ? 9 SER C O 1 ATOM 3378 C CB . SER C 2 9 ? 24.088 -0.951 39.159 1.00 67.25 ? 9 SER C CB 1 ATOM 3379 O OG . SER C 2 9 ? 23.736 0.266 38.530 1.00 79.34 ? 9 SER C OG 1 ATOM 3380 N N . PRO C 2 10 ? 24.576 1.361 41.860 1.00 91.33 ? 10 PRO C N 1 ATOM 3381 C CA . PRO C 2 10 ? 25.992 1.707 41.749 1.00 96.50 ? 10 PRO C CA 1 ATOM 3382 C C . PRO C 2 10 ? 26.884 0.828 42.590 1.00 87.50 ? 10 PRO C C 1 ATOM 3383 O O . PRO C 2 10 ? 26.384 -0.016 43.373 1.00 70.89 ? 10 PRO C O 1 ATOM 3384 C CB . PRO C 2 10 ? 26.057 3.124 42.330 1.00 97.71 ? 10 PRO C CB 1 ATOM 3385 C CG . PRO C 2 10 ? 25.014 3.144 43.328 1.00 91.43 ? 10 PRO C CG 1 ATOM 3386 C CD . PRO C 2 10 ? 23.885 2.311 42.752 1.00 92.81 ? 10 PRO C CD 1 ATOM 3387 N N . ILE C 2 11 ? 28.176 1.147 42.550 1.00 96.60 ? 11 ILE C N 1 ATOM 3388 C CA . ILE C 2 11 ? 29.167 0.325 43.223 1.00 94.54 ? 11 ILE C CA 1 ATOM 3389 C C . ILE C 2 11 ? 29.168 0.678 44.690 1.00 84.50 ? 11 ILE C C 1 ATOM 3390 O O . ILE C 2 11 ? 29.042 1.854 45.074 1.00 81.42 ? 11 ILE C O 1 ATOM 3391 C CB . ILE C 2 11 ? 30.604 0.550 42.657 1.00 124.22 ? 11 ILE C CB 1 ATOM 3392 C CG1 . ILE C 2 11 ? 31.570 -0.501 43.167 1.00 102.68 ? 11 ILE C CG1 1 ATOM 3393 C CG2 . ILE C 2 11 ? 31.157 1.942 43.001 1.00 126.41 ? 11 ILE C CG2 1 ATOM 3394 C CD1 . ILE C 2 11 ? 31.336 -1.723 42.490 1.00 100.21 ? 11 ILE C CD1 1 ATOM 3395 N N . SER C 2 12 ? 29.360 -0.358 45.500 1.00 79.42 ? 12 SER C N 1 ATOM 3396 C CA . SER C 2 12 ? 29.028 -0.320 46.900 1.00 71.23 ? 12 SER C CA 1 ATOM 3397 C C . SER C 2 12 ? 29.770 -1.444 47.601 1.00 77.67 ? 12 SER C C 1 ATOM 3398 O O . SER C 2 12 ? 30.488 -2.197 46.959 1.00 79.85 ? 12 SER C O 1 ATOM 3399 C CB . SER C 2 12 ? 27.501 -0.457 47.113 1.00 73.45 ? 12 SER C CB 1 ATOM 3400 O OG . SER C 2 12 ? 26.974 -1.732 46.701 1.00 64.71 ? 12 SER C OG 1 ATOM 3401 N N . ALA C 2 13 ? 29.509 -1.607 48.901 1.00 81.99 ? 13 ALA C N 1 ATOM 3402 C CA . ALA C 2 13 ? 30.236 -2.538 49.726 1.00 68.00 ? 13 ALA C CA 1 ATOM 3403 C C . ALA C 2 13 ? 29.421 -3.725 50.145 1.00 58.58 ? 13 ALA C C 1 ATOM 3404 O O . ALA C 2 13 ? 28.294 -3.591 50.576 1.00 59.26 ? 13 ALA C O 1 ATOM 3405 C CB . ALA C 2 13 ? 30.744 -1.840 50.947 1.00 74.06 ? 13 ALA C CB 1 ATOM 3406 N N . VAL C 2 14 ? 30.022 -4.900 50.078 1.00 65.39 ? 14 VAL C N 1 ATOM 3407 C CA . VAL C 2 14 ? 29.334 -6.091 50.520 1.00 67.79 ? 14 VAL C CA 1 ATOM 3408 C C . VAL C 2 14 ? 30.216 -6.848 51.496 1.00 79.11 ? 14 VAL C C 1 ATOM 3409 O O . VAL C 2 14 ? 31.426 -6.698 51.509 1.00 81.47 ? 14 VAL C O 1 ATOM 3410 C CB . VAL C 2 14 ? 28.984 -6.988 49.345 1.00 68.53 ? 14 VAL C CB 1 ATOM 3411 C CG1 . VAL C 2 14 ? 28.524 -8.388 49.786 1.00 58.80 ? 14 VAL C CG1 1 ATOM 3412 C CG2 . VAL C 2 14 ? 27.913 -6.339 48.592 1.00 97.92 ? 14 VAL C CG2 1 ATOM 3413 N N . THR C 2 15 ? 29.579 -7.611 52.358 1.00 66.58 ? 15 THR C N 1 ATOM 3414 C CA . THR C 2 15 ? 30.263 -8.518 53.215 1.00 61.07 ? 15 THR C CA 1 ATOM 3415 C C . THR C 2 15 ? 30.408 -9.827 52.478 1.00 66.72 ? 15 THR C C 1 ATOM 3416 O O . THR C 2 15 ? 29.430 -10.489 52.211 1.00 86.49 ? 15 THR C O 1 ATOM 3417 C CB . THR C 2 15 ? 29.457 -8.696 54.473 1.00 64.95 ? 15 THR C CB 1 ATOM 3418 O OG1 . THR C 2 15 ? 28.945 -7.403 54.828 1.00 78.91 ? 15 THR C OG1 1 ATOM 3419 C CG2 . THR C 2 15 ? 30.290 -9.275 55.572 1.00 64.21 ? 15 THR C CG2 1 ATOM 3420 N N . CYS C 2 16 ? 31.618 -10.229 52.171 1.00 79.90 ? 16 CYS C N 1 ATOM 3421 C CA . CYS C 2 16 ? 31.830 -11.481 51.449 1.00 98.66 ? 16 CYS C CA 1 ATOM 3422 C C . CYS C 2 16 ? 31.175 -12.687 52.193 1.00 63.31 ? 16 CYS C C 1 ATOM 3423 O O . CYS C 2 16 ? 30.811 -12.562 53.335 1.00 63.76 ? 16 CYS C O 1 ATOM 3424 C CB . CYS C 2 16 ? 33.347 -11.690 51.253 1.00 98.52 ? 16 CYS C CB 1 ATOM 3425 S SG . CYS C 2 16 ? 34.234 -10.198 50.657 1.00 176.35 ? 16 CYS C SG 1 ATOM 3426 N N . PRO C 2 17 ? 30.938 -13.813 51.490 1.00 73.38 ? 17 PRO C N 1 ATOM 3427 C CA . PRO C 2 17 ? 30.533 -15.119 52.035 1.00 73.83 ? 17 PRO C CA 1 ATOM 3428 C C . PRO C 2 17 ? 31.471 -15.647 53.076 1.00 82.00 ? 17 PRO C C 1 ATOM 3429 O O . PRO C 2 17 ? 32.499 -15.036 53.316 1.00 94.34 ? 17 PRO C O 1 ATOM 3430 C CB . PRO C 2 17 ? 30.573 -16.046 50.810 1.00 63.76 ? 17 PRO C CB 1 ATOM 3431 C CG . PRO C 2 17 ? 30.287 -15.134 49.650 1.00 79.73 ? 17 PRO C CG 1 ATOM 3432 C CD . PRO C 2 17 ? 30.802 -13.768 50.018 1.00 78.04 ? 17 PRO C CD 1 ATOM 3433 N N . PRO C 2 18 ? 31.098 -16.752 53.730 1.00 99.73 ? 18 PRO C N 1 ATOM 3434 C CA . PRO C 2 18 ? 32.033 -17.500 54.587 1.00 115.04 ? 18 PRO C CA 1 ATOM 3435 C C . PRO C 2 18 ? 33.069 -18.275 53.776 1.00 123.09 ? 18 PRO C C 1 ATOM 3436 O O . PRO C 2 18 ? 32.692 -18.966 52.833 1.00 120.90 ? 18 PRO C O 1 ATOM 3437 C CB . PRO C 2 18 ? 31.122 -18.464 55.354 1.00 113.41 ? 18 PRO C CB 1 ATOM 3438 C CG . PRO C 2 18 ? 29.734 -17.888 55.226 1.00 106.22 ? 18 PRO C CG 1 ATOM 3439 C CD . PRO C 2 18 ? 29.709 -17.222 53.883 1.00 101.51 ? 18 PRO C CD 1 ATOM 3440 N N . GLY C 2 19 ? 34.343 -18.177 54.134 1.00 130.10 ? 19 GLY C N 1 ATOM 3441 C CA . GLY C 2 19 ? 35.361 -18.943 53.442 1.00 133.41 ? 19 GLY C CA 1 ATOM 3442 C C . GLY C 2 19 ? 35.969 -18.121 52.327 1.00 127.96 ? 19 GLY C C 1 ATOM 3443 O O . GLY C 2 19 ? 37.084 -18.385 51.881 1.00 134.30 ? 19 GLY C O 1 ATOM 3444 N N . GLU C 2 20 ? 35.213 -17.150 51.829 1.00 119.33 ? 20 GLU C N 1 ATOM 3445 C CA . GLU C 2 20 ? 35.781 -16.243 50.853 1.00 114.44 ? 20 GLU C CA 1 ATOM 3446 C C . GLU C 2 20 ? 36.322 -15.013 51.582 1.00 113.37 ? 20 GLU C C 1 ATOM 3447 O O . GLU C 2 20 ? 35.630 -13.993 51.660 1.00 102.44 ? 20 GLU C O 1 ATOM 3448 C CB . GLU C 2 20 ? 34.759 -15.840 49.781 1.00 112.45 ? 20 GLU C CB 1 ATOM 3449 C CG . GLU C 2 20 ? 34.312 -16.992 48.882 1.00 111.26 ? 20 GLU C CG 1 ATOM 3450 C CD . GLU C 2 20 ? 33.414 -16.548 47.736 1.00 115.80 ? 20 GLU C CD 1 ATOM 3451 O OE1 . GLU C 2 20 ? 33.111 -15.338 47.632 1.00 112.99 ? 20 GLU C OE1 1 ATOM 3452 O OE2 . GLU C 2 20 ? 33.012 -17.413 46.925 1.00 121.89 -1 20 GLU C OE2 1 ATOM 3453 N N . ASN C 2 21 ? 37.583 -15.113 52.039 1.00 117.76 ? 21 ASN C N 1 ATOM 3454 C CA . ASN C 2 21 ? 38.234 -14.154 52.958 1.00 105.15 ? 21 ASN C CA 1 ATOM 3455 C C . ASN C 2 21 ? 38.948 -12.980 52.304 1.00 97.39 ? 21 ASN C C 1 ATOM 3456 O O . ASN C 2 21 ? 39.161 -11.934 52.926 1.00 98.39 ? 21 ASN C O 1 ATOM 3457 C CB . ASN C 2 21 ? 39.240 -14.880 53.861 1.00 91.43 ? 21 ASN C CB 1 ATOM 3458 C CG . ASN C 2 21 ? 38.610 -16.011 54.630 1.00 91.26 ? 21 ASN C CG 1 ATOM 3459 O OD1 . ASN C 2 21 ? 37.464 -15.900 55.055 1.00 100.42 ? 21 ASN C OD1 1 ATOM 3460 N ND2 . ASN C 2 21 ? 39.359 -17.086 54.854 1.00 90.24 ? 21 ASN C ND2 1 ATOM 3461 N N . LEU C 2 22 ? 39.306 -13.154 51.048 1.00 90.63 ? 22 LEU C N 1 ATOM 3462 C CA . LEU C 2 22 ? 40.054 -12.157 50.326 1.00 85.21 ? 22 LEU C CA 1 ATOM 3463 C C . LEU C 2 22 ? 39.187 -11.246 49.511 1.00 74.96 ? 22 LEU C C 1 ATOM 3464 O O . LEU C 2 22 ? 38.169 -11.664 48.961 1.00 76.43 ? 22 LEU C O 1 ATOM 3465 C CB . LEU C 2 22 ? 41.021 -12.813 49.356 1.00 97.30 ? 22 LEU C CB 1 ATOM 3466 C CG . LEU C 2 22 ? 42.083 -13.647 50.013 1.00 109.58 ? 22 LEU C CG 1 ATOM 3467 C CD1 . LEU C 2 22 ? 42.890 -14.290 48.911 1.00 123.07 ? 22 LEU C CD1 1 ATOM 3468 C CD2 . LEU C 2 22 ? 42.920 -12.704 50.873 1.00 108.75 ? 22 LEU C CD2 1 ATOM 3469 N N . CYS C 2 23 ? 39.631 -10.008 49.377 1.00 70.39 ? 23 CYS C N 1 ATOM 3470 C CA . CYS C 2 23 ? 39.092 -9.131 48.354 1.00 75.15 ? 23 CYS C CA 1 ATOM 3471 C C . CYS C 2 23 ? 40.088 -9.104 47.189 1.00 86.19 ? 23 CYS C C 1 ATOM 3472 O O . CYS C 2 23 ? 41.311 -9.217 47.402 1.00 88.67 ? 23 CYS C O 1 ATOM 3473 C CB . CYS C 2 23 ? 38.809 -7.734 48.925 1.00 71.98 ? 23 CYS C CB 1 ATOM 3474 S SG . CYS C 2 23 ? 37.347 -7.663 50.094 1.00 89.44 ? 23 CYS C SG 1 ATOM 3475 N N . TYR C 2 24 ? 39.555 -9.031 45.967 1.00 91.64 ? 24 TYR C N 1 ATOM 3476 C CA . TYR C 2 24 ? 40.372 -9.035 44.751 1.00 90.00 ? 24 TYR C CA 1 ATOM 3477 C C . TYR C 2 24 ? 40.052 -7.867 43.821 1.00 85.71 ? 24 TYR C C 1 ATOM 3478 O O . TYR C 2 24 ? 39.040 -7.197 43.996 1.00 86.15 ? 24 TYR C O 1 ATOM 3479 C CB . TYR C 2 24 ? 40.207 -10.354 43.958 1.00 93.81 ? 24 TYR C CB 1 ATOM 3480 C CG . TYR C 2 24 ? 38.922 -10.489 43.156 1.00 96.15 ? 24 TYR C CG 1 ATOM 3481 C CD1 . TYR C 2 24 ? 38.761 -9.867 41.924 1.00 111.77 ? 24 TYR C CD1 1 ATOM 3482 C CD2 . TYR C 2 24 ? 37.888 -11.283 43.612 1.00 102.74 ? 24 TYR C CD2 1 ATOM 3483 C CE1 . TYR C 2 24 ? 37.578 -9.995 41.201 1.00 110.89 ? 24 TYR C CE1 1 ATOM 3484 C CE2 . TYR C 2 24 ? 36.714 -11.424 42.894 1.00 100.73 ? 24 TYR C CE2 1 ATOM 3485 C CZ . TYR C 2 24 ? 36.566 -10.782 41.703 1.00 101.80 ? 24 TYR C CZ 1 ATOM 3486 O OH . TYR C 2 24 ? 35.401 -10.946 41.017 1.00 100.83 ? 24 TYR C OH 1 ATOM 3487 N N . ARG C 2 25 ? 40.919 -7.645 42.829 1.00 80.25 ? 25 ARG C N 1 ATOM 3488 C CA . ARG C 2 25 ? 40.626 -6.710 41.739 1.00 78.94 ? 25 ARG C CA 1 ATOM 3489 C C . ARG C 2 25 ? 41.056 -7.367 40.434 1.00 88.71 ? 25 ARG C C 1 ATOM 3490 O O . ARG C 2 25 ? 42.149 -7.905 40.376 1.00 91.72 ? 25 ARG C O 1 ATOM 3491 C CB . ARG C 2 25 ? 41.341 -5.371 41.906 1.00 77.15 ? 25 ARG C CB 1 ATOM 3492 C CG . ARG C 2 25 ? 40.875 -4.404 40.887 1.00 62.75 ? 25 ARG C CG 1 ATOM 3493 C CD . ARG C 2 25 ? 41.273 -3.012 41.179 1.00 73.65 ? 25 ARG C CD 1 ATOM 3494 N NE . ARG C 2 25 ? 42.698 -2.850 41.020 1.00 97.39 ? 25 ARG C NE 1 ATOM 3495 C CZ . ARG C 2 25 ? 43.271 -1.664 40.895 1.00 102.94 ? 25 ARG C CZ 1 ATOM 3496 N NH1 . ARG C 2 25 ? 42.510 -0.573 40.893 1.00 100.42 ? 25 ARG C NH1 1 ATOM 3497 N NH2 . ARG C 2 25 ? 44.586 -1.568 40.730 1.00 105.75 ? 25 ARG C NH2 1 ATOM 3498 N N . LYS C 2 26 ? 40.190 -7.374 39.423 1.00 86.30 ? 26 LYS C N 1 ATOM 3499 C CA . LYS C 2 26 ? 40.536 -7.910 38.098 1.00 87.74 ? 26 LYS C CA 1 ATOM 3500 C C . LYS C 2 26 ? 40.430 -6.831 37.067 1.00 83.19 ? 26 LYS C C 1 ATOM 3501 O O . LYS C 2 26 ? 39.418 -6.140 37.031 1.00 81.29 ? 26 LYS C O 1 ATOM 3502 C CB . LYS C 2 26 ? 39.597 -9.038 37.681 1.00 87.19 ? 26 LYS C CB 1 ATOM 3503 C CG . LYS C 2 26 ? 40.271 -10.265 37.127 1.00 100.52 ? 26 LYS C CG 1 ATOM 3504 C CD . LYS C 2 26 ? 39.299 -11.441 37.114 1.00 113.72 ? 26 LYS C CD 1 ATOM 3505 C CE . LYS C 2 26 ? 39.833 -12.615 36.302 1.00 120.15 ? 26 LYS C CE 1 ATOM 3506 N NZ . LYS C 2 26 ? 39.279 -13.916 36.805 1.00 122.19 ? 26 LYS C NZ 1 ATOM 3507 N N . MET C 2 27 ? 41.440 -6.673 36.218 1.00 90.05 ? 27 MET C N 1 ATOM 3508 C CA . MET C 2 27 ? 41.264 -5.810 35.050 1.00 96.81 ? 27 MET C CA 1 ATOM 3509 C C . MET C 2 27 ? 41.819 -6.399 33.734 1.00 111.91 ? 27 MET C C 1 ATOM 3510 O O . MET C 2 27 ? 43.031 -6.535 33.585 1.00 115.97 ? 27 MET C O 1 ATOM 3511 C CB . MET C 2 27 ? 41.896 -4.448 35.299 1.00 87.46 ? 27 MET C CB 1 ATOM 3512 C CG . MET C 2 27 ? 41.367 -3.719 36.492 1.00 77.23 ? 27 MET C CG 1 ATOM 3513 S SD . MET C 2 27 ? 42.466 -2.353 36.884 1.00 89.42 ? 27 MET C SD 1 ATOM 3514 C CE . MET C 2 27 ? 41.705 -1.056 35.913 1.00 62.33 ? 27 MET C CE 1 ATOM 3515 N N . TRP C 2 28 ? 40.938 -6.783 32.808 1.00 112.02 ? 28 TRP C N 1 ATOM 3516 C CA . TRP C 2 28 ? 41.347 -7.137 31.445 1.00 91.15 ? 28 TRP C CA 1 ATOM 3517 C C . TRP C 2 28 ? 40.887 -6.067 30.484 1.00 90.74 ? 28 TRP C C 1 ATOM 3518 O O . TRP C 2 28 ? 40.525 -4.949 30.889 1.00 76.23 ? 28 TRP C O 1 ATOM 3519 C CB . TRP C 2 28 ? 40.767 -8.482 30.996 1.00 98.61 ? 28 TRP C CB 1 ATOM 3520 C CG . TRP C 2 28 ? 39.244 -8.506 30.926 1.00 101.97 ? 28 TRP C CG 1 ATOM 3521 C CD1 . TRP C 2 28 ? 38.466 -8.224 29.830 1.00 84.55 ? 28 TRP C CD1 1 ATOM 3522 C CD2 . TRP C 2 28 ? 38.326 -8.807 31.995 1.00 104.15 ? 28 TRP C CD2 1 ATOM 3523 N NE1 . TRP C 2 28 ? 37.134 -8.347 30.145 1.00 79.94 ? 28 TRP C NE1 1 ATOM 3524 C CE2 . TRP C 2 28 ? 37.016 -8.697 31.466 1.00 96.80 ? 28 TRP C CE2 1 ATOM 3525 C CE3 . TRP C 2 28 ? 38.481 -9.165 33.328 1.00 92.96 ? 28 TRP C CE3 1 ATOM 3526 C CZ2 . TRP C 2 28 ? 35.877 -8.924 32.237 1.00 97.26 ? 28 TRP C CZ2 1 ATOM 3527 C CZ3 . TRP C 2 28 ? 37.345 -9.400 34.085 1.00 106.44 ? 28 TRP C CZ3 1 ATOM 3528 C CH2 . TRP C 2 28 ? 36.063 -9.284 33.536 1.00 103.16 ? 28 TRP C CH2 1 ATOM 3529 N N . CYS C 2 29 ? 40.873 -6.430 29.204 1.00 99.59 ? 29 CYS C N 1 ATOM 3530 C CA . CYS C 2 29 ? 40.542 -5.482 28.138 1.00 104.80 ? 29 CYS C CA 1 ATOM 3531 C C . CYS C 2 29 ? 39.493 -6.013 27.133 1.00 107.87 ? 29 CYS C C 1 ATOM 3532 O O . CYS C 2 29 ? 39.706 -7.013 26.429 1.00 107.28 ? 29 CYS C O 1 ATOM 3533 C CB . CYS C 2 29 ? 41.807 -5.070 27.355 1.00 102.00 ? 29 CYS C CB 1 ATOM 3534 S SG . CYS C 2 29 ? 42.628 -3.478 27.814 1.00 96.85 ? 29 CYS C SG 1 ATOM 3535 N N . ASP C 2 30 ? 38.330 -5.364 27.186 1.00 102.95 ? 30 ASP C N 1 ATOM 3536 C CA . ASP C 2 30 ? 37.548 -4.880 26.066 1.00 124.40 ? 30 ASP C CA 1 ATOM 3537 C C . ASP C 2 30 ? 38.421 -4.440 24.863 1.00 144.74 ? 30 ASP C C 1 ATOM 3538 O O . ASP C 2 30 ? 39.650 -4.540 24.914 1.00 150.21 ? 30 ASP C O 1 ATOM 3539 C CB . ASP C 2 30 ? 36.718 -3.734 26.629 1.00 126.51 ? 30 ASP C CB 1 ATOM 3540 C CG . ASP C 2 30 ? 37.570 -2.533 26.985 1.00 127.55 ? 30 ASP C CG 1 ATOM 3541 O OD1 . ASP C 2 30 ? 38.687 -2.358 26.473 1.00 134.79 ? 30 ASP C OD1 1 ATOM 3542 O OD2 . ASP C 2 30 ? 37.156 -1.827 27.916 1.00 132.14 -1 30 ASP C OD2 1 ATOM 3543 N N . VAL C 2 31 ? 37.846 -3.943 23.778 1.00 152.00 ? 31 VAL C N 1 ATOM 3544 C CA . VAL C 2 31 ? 38.669 -2.990 23.026 1.00 161.69 ? 31 VAL C CA 1 ATOM 3545 C C . VAL C 2 31 ? 38.029 -1.596 23.113 1.00 154.83 ? 31 VAL C C 1 ATOM 3546 O O . VAL C 2 31 ? 38.377 -0.689 22.337 1.00 162.41 ? 31 VAL C O 1 ATOM 3547 C CB . VAL C 2 31 ? 38.933 -3.419 21.550 1.00 149.98 ? 31 VAL C CB 1 ATOM 3548 C CG1 . VAL C 2 31 ? 40.107 -2.628 20.967 1.00 142.65 ? 31 VAL C CG1 1 ATOM 3549 C CG2 . VAL C 2 31 ? 39.288 -4.899 21.467 1.00 157.29 ? 31 VAL C CG2 1 ATOM 3550 N N . PHE C 2 32 ? 37.175 -1.401 24.122 1.00 123.88 ? 32 PHE C N 1 ATOM 3551 C CA . PHE C 2 32 ? 36.775 -0.045 24.499 1.00 107.22 ? 32 PHE C CA 1 ATOM 3552 C C . PHE C 2 32 ? 37.932 0.638 25.261 1.00 109.87 ? 32 PHE C C 1 ATOM 3553 O O . PHE C 2 32 ? 37.902 1.834 25.519 1.00 104.83 ? 32 PHE C O 1 ATOM 3554 C CB . PHE C 2 32 ? 35.524 -0.044 25.398 1.00 106.30 ? 32 PHE C CB 1 ATOM 3555 C CG . PHE C 2 32 ? 34.205 0.149 24.672 1.00 98.51 ? 32 PHE C CG 1 ATOM 3556 C CD1 . PHE C 2 32 ? 33.819 1.424 24.247 1.00 92.21 ? 32 PHE C CD1 1 ATOM 3557 C CD2 . PHE C 2 32 ? 33.304 -0.912 24.501 1.00 89.24 ? 32 PHE C CD2 1 ATOM 3558 C CE1 . PHE C 2 32 ? 32.597 1.632 23.584 1.00 72.43 ? 32 PHE C CE1 1 ATOM 3559 C CE2 . PHE C 2 32 ? 32.072 -0.707 23.832 1.00 68.25 ? 32 PHE C CE2 1 ATOM 3560 C CZ . PHE C 2 32 ? 31.727 0.565 23.393 1.00 61.86 ? 32 PHE C CZ 1 ATOM 3561 N N . CYS C 2 33 ? 38.944 -0.161 25.605 1.00 126.20 ? 33 CYS C N 1 ATOM 3562 C CA . CYS C 2 33 ? 40.133 0.185 26.433 1.00 137.03 ? 33 CYS C CA 1 ATOM 3563 C C . CYS C 2 33 ? 40.744 1.547 26.145 1.00 128.50 ? 33 CYS C C 1 ATOM 3564 O O . CYS C 2 33 ? 40.984 2.347 27.059 1.00 124.28 ? 33 CYS C O 1 ATOM 3565 C CB . CYS C 2 33 ? 41.209 -0.903 26.222 1.00 146.89 ? 33 CYS C CB 1 ATOM 3566 S SG . CYS C 2 33 ? 42.203 -1.469 27.627 1.00 85.45 ? 33 CYS C SG 1 ATOM 3567 N N . SER C 2 34 ? 41.055 1.751 24.867 1.00 114.66 ? 34 SER C N 1 ATOM 3568 C CA . SER C 2 34 ? 41.491 3.027 24.346 1.00 116.46 ? 34 SER C CA 1 ATOM 3569 C C . SER C 2 34 ? 40.512 4.146 24.742 1.00 117.56 ? 34 SER C C 1 ATOM 3570 O O . SER C 2 34 ? 40.919 5.156 25.323 1.00 116.42 ? 34 SER C O 1 ATOM 3571 C CB . SER C 2 34 ? 41.629 2.903 22.835 1.00 120.41 ? 34 SER C CB 1 ATOM 3572 O OG . SER C 2 34 ? 40.473 2.256 22.324 1.00 126.62 ? 34 SER C OG 1 ATOM 3573 N N . SER C 2 35 ? 39.218 3.916 24.487 1.00 119.65 ? 35 SER C N 1 ATOM 3574 C CA . SER C 2 35 ? 38.121 4.894 24.685 1.00 114.43 ? 35 SER C CA 1 ATOM 3575 C C . SER C 2 35 ? 37.702 5.094 26.159 1.00 109.12 ? 35 SER C C 1 ATOM 3576 O O . SER C 2 35 ? 37.459 6.212 26.626 1.00 108.45 ? 35 SER C O 1 ATOM 3577 C CB . SER C 2 35 ? 36.895 4.455 23.895 1.00 111.05 ? 35 SER C CB 1 ATOM 3578 O OG . SER C 2 35 ? 36.611 3.084 24.137 1.00 108.90 ? 35 SER C OG 1 ATOM 3579 N N . ARG C 2 36 ? 37.533 3.989 26.864 1.00 100.85 ? 36 ARG C N 1 ATOM 3580 C CA . ARG C 2 36 ? 37.190 4.045 28.271 1.00 112.53 ? 36 ARG C CA 1 ATOM 3581 C C . ARG C 2 36 ? 38.004 2.957 28.976 1.00 119.92 ? 36 ARG C C 1 ATOM 3582 O O . ARG C 2 36 ? 37.670 1.778 28.967 1.00 120.52 ? 36 ARG C O 1 ATOM 3583 C CB . ARG C 2 36 ? 35.671 3.908 28.497 1.00 113.78 ? 36 ARG C CB 1 ATOM 3584 C CG . ARG C 2 36 ? 34.876 2.866 27.707 1.00 109.43 ? 36 ARG C CG 1 ATOM 3585 C CD . ARG C 2 36 ? 33.422 3.329 27.756 1.00 108.06 ? 36 ARG C CD 1 ATOM 3586 N NE . ARG C 2 36 ? 32.419 2.439 27.178 1.00 105.01 ? 36 ARG C NE 1 ATOM 3587 C CZ . ARG C 2 36 ? 31.179 2.841 26.919 1.00 105.54 ? 36 ARG C CZ 1 ATOM 3588 N NH1 . ARG C 2 36 ? 30.831 4.091 27.190 1.00 110.37 ? 36 ARG C NH1 1 ATOM 3589 N NH2 . ARG C 2 36 ? 30.285 2.019 26.392 1.00 98.68 ? 36 ARG C NH2 1 ATOM 3590 N N . GLY C 2 37 ? 39.098 3.386 29.576 1.00 111.37 ? 37 GLY C N 1 ATOM 3591 C CA . GLY C 2 37 ? 40.115 2.480 30.052 1.00 116.50 ? 37 GLY C CA 1 ATOM 3592 C C . GLY C 2 37 ? 39.736 1.269 30.861 1.00 119.92 ? 37 GLY C C 1 ATOM 3593 O O . GLY C 2 37 ? 39.113 1.398 31.907 1.00 134.15 ? 37 GLY C O 1 ATOM 3594 N N . LYS C 2 38 ? 40.045 0.093 30.324 1.00 112.16 ? 38 LYS C N 1 ATOM 3595 C CA . LYS C 2 38 ? 40.188 -1.090 31.146 1.00 97.27 ? 38 LYS C CA 1 ATOM 3596 C C . LYS C 2 38 ? 38.912 -1.577 31.881 1.00 90.88 ? 38 LYS C C 1 ATOM 3597 O O . LYS C 2 38 ? 38.257 -0.818 32.604 1.00 87.83 ? 38 LYS C O 1 ATOM 3598 C CB . LYS C 2 38 ? 41.267 -0.741 32.154 1.00 112.86 ? 38 LYS C CB 1 ATOM 3599 C CG . LYS C 2 38 ? 41.978 -1.877 32.731 1.00 133.03 ? 38 LYS C CG 1 ATOM 3600 C CD . LYS C 2 38 ? 42.786 -2.451 31.660 1.00 141.76 ? 38 LYS C CD 1 ATOM 3601 C CE . LYS C 2 38 ? 43.241 -3.799 32.038 1.00 146.63 ? 38 LYS C CE 1 ATOM 3602 N NZ . LYS C 2 38 ? 43.229 -4.501 30.770 1.00 153.90 ? 38 LYS C NZ 1 ATOM 3603 N N . VAL C 2 39 ? 38.554 -2.844 31.781 1.00 87.50 ? 39 VAL C N 1 ATOM 3604 C CA . VAL C 2 39 ? 37.318 -3.199 32.461 1.00 81.30 ? 39 VAL C CA 1 ATOM 3605 C C . VAL C 2 39 ? 37.653 -3.878 33.726 1.00 87.28 ? 39 VAL C C 1 ATOM 3606 O O . VAL C 2 39 ? 38.469 -4.807 33.725 1.00 88.18 ? 39 VAL C O 1 ATOM 3607 C CB . VAL C 2 39 ? 36.409 -4.119 31.612 1.00 96.96 ? 39 VAL C CB 1 ATOM 3608 C CG1 . VAL C 2 39 ? 37.245 -5.082 30.824 1.00 96.19 ? 39 VAL C CG1 1 ATOM 3609 C CG2 . VAL C 2 39 ? 35.486 -4.965 32.534 1.00 54.87 ? 39 VAL C CG2 1 ATOM 3610 N N . VAL C 2 40 ? 36.923 -3.462 34.774 1.00 92.72 ? 40 VAL C N 1 ATOM 3611 C CA . VAL C 2 40 ? 37.169 -3.805 36.183 1.00 73.06 ? 40 VAL C CA 1 ATOM 3612 C C . VAL C 2 40 ? 36.144 -4.690 36.835 1.00 72.16 ? 40 VAL C C 1 ATOM 3613 O O . VAL C 2 40 ? 34.978 -4.358 36.866 1.00 89.99 ? 40 VAL C O 1 ATOM 3614 C CB . VAL C 2 40 ? 37.206 -2.552 37.065 1.00 72.41 ? 40 VAL C CB 1 ATOM 3615 C CG1 . VAL C 2 40 ? 37.629 -2.940 38.428 1.00 79.24 ? 40 VAL C CG1 1 ATOM 3616 C CG2 . VAL C 2 40 ? 38.146 -1.532 36.514 1.00 85.82 ? 40 VAL C CG2 1 ATOM 3617 N N . GLU C 2 41 ? 36.572 -5.806 37.378 1.00 70.46 ? 41 GLU C N 1 ATOM 3618 C CA . GLU C 2 41 ? 35.683 -6.634 38.135 1.00 65.55 ? 41 GLU C CA 1 ATOM 3619 C C . GLU C 2 41 ? 36.220 -6.689 39.567 1.00 90.46 ? 41 GLU C C 1 ATOM 3620 O O . GLU C 2 41 ? 37.329 -7.185 39.818 1.00 96.53 ? 41 GLU C O 1 ATOM 3621 C CB . GLU C 2 41 ? 35.605 -8.009 37.490 1.00 63.15 ? 41 GLU C CB 1 ATOM 3622 C CG . GLU C 2 41 ? 35.126 -9.107 38.411 1.00 69.36 ? 41 GLU C CG 1 ATOM 3623 C CD . GLU C 2 41 ? 34.983 -10.409 37.666 1.00 87.35 ? 41 GLU C CD 1 ATOM 3624 O OE1 . GLU C 2 41 ? 34.635 -10.348 36.459 1.00 91.10 ? 41 GLU C OE1 1 ATOM 3625 O OE2 . GLU C 2 41 ? 35.209 -11.477 38.286 1.00 85.09 -1 41 GLU C OE2 1 ATOM 3626 N N . LEU C 2 42 ? 35.440 -6.175 40.517 1.00 95.87 ? 42 LEU C N 1 ATOM 3627 C CA . LEU C 2 42 ? 35.809 -6.177 41.940 1.00 72.05 ? 42 LEU C CA 1 ATOM 3628 C C . LEU C 2 42 ? 34.920 -7.174 42.653 1.00 69.10 ? 42 LEU C C 1 ATOM 3629 O O . LEU C 2 42 ? 33.721 -7.266 42.348 1.00 83.82 ? 42 LEU C O 1 ATOM 3630 C CB . LEU C 2 42 ? 35.639 -4.788 42.561 1.00 66.01 ? 42 LEU C CB 1 ATOM 3631 C CG . LEU C 2 42 ? 36.206 -3.569 41.830 1.00 81.04 ? 42 LEU C CG 1 ATOM 3632 C CD1 . LEU C 2 42 ? 35.841 -2.251 42.455 1.00 58.96 ? 42 LEU C CD1 1 ATOM 3633 C CD2 . LEU C 2 42 ? 37.688 -3.693 41.769 1.00 91.59 ? 42 LEU C CD2 1 ATOM 3634 N N . GLY C 2 43 ? 35.476 -7.943 43.584 1.00 74.05 ? 43 GLY C N 1 ATOM 3635 C CA . GLY C 2 43 ? 34.648 -8.826 44.393 1.00 64.60 ? 43 GLY C CA 1 ATOM 3636 C C . GLY C 2 43 ? 35.341 -9.552 45.520 1.00 68.38 ? 43 GLY C C 1 ATOM 3637 O O . GLY C 2 43 ? 36.279 -9.056 46.142 1.00 70.94 ? 43 GLY C O 1 ATOM 3638 N N . CYS C 2 44 ? 34.802 -10.720 45.834 1.00 75.33 ? 44 CYS C N 1 ATOM 3639 C CA . CYS C 2 44 ? 35.280 -11.572 46.918 1.00 79.80 ? 44 CYS C CA 1 ATOM 3640 C C . CYS C 2 44 ? 35.879 -12.809 46.312 1.00 81.16 ? 44 CYS C C 1 ATOM 3641 O O . CYS C 2 44 ? 35.568 -13.136 45.165 1.00 80.75 ? 44 CYS C O 1 ATOM 3642 C CB . CYS C 2 44 ? 34.131 -11.959 47.867 1.00 96.45 ? 44 CYS C CB 1 ATOM 3643 S SG . CYS C 2 44 ? 33.425 -10.595 48.846 1.00 120.35 ? 44 CYS C SG 1 ATOM 3644 N N . ALA C 2 45 ? 36.701 -13.527 47.067 1.00 84.40 ? 45 ALA C N 1 ATOM 3645 C CA . ALA C 2 45 ? 37.221 -14.797 46.564 1.00 77.39 ? 45 ALA C CA 1 ATOM 3646 C C . ALA C 2 45 ? 37.714 -15.581 47.728 1.00 84.70 ? 45 ALA C C 1 ATOM 3647 O O . ALA C 2 45 ? 38.060 -14.990 48.734 1.00 87.22 ? 45 ALA C O 1 ATOM 3648 C CB . ALA C 2 45 ? 38.339 -14.575 45.546 1.00 68.51 ? 45 ALA C CB 1 ATOM 3649 N N . ALA C 2 46 ? 37.710 -16.904 47.629 1.00 87.30 ? 46 ALA C N 1 ATOM 3650 C CA . ALA C 2 46 ? 38.282 -17.717 48.697 1.00 104.70 ? 46 ALA C CA 1 ATOM 3651 C C . ALA C 2 46 ? 39.826 -17.714 48.609 1.00 114.95 ? 46 ALA C C 1 ATOM 3652 O O . ALA C 2 46 ? 40.515 -17.394 49.575 1.00 120.23 ? 46 ALA C O 1 ATOM 3653 C CB . ALA C 2 46 ? 37.732 -19.132 48.640 1.00 106.41 ? 46 ALA C CB 1 ATOM 3654 N N . THR C 2 47 ? 40.351 -18.051 47.436 1.00 119.56 ? 47 THR C N 1 ATOM 3655 C CA . THR C 2 47 ? 41.781 -18.012 47.164 1.00 118.58 ? 47 THR C CA 1 ATOM 3656 C C . THR C 2 47 ? 42.014 -16.994 46.047 1.00 124.31 ? 47 THR C C 1 ATOM 3657 O O . THR C 2 47 ? 41.173 -16.892 45.148 1.00 121.80 ? 47 THR C O 1 ATOM 3658 C CB . THR C 2 47 ? 42.282 -19.401 46.747 1.00 119.80 ? 47 THR C CB 1 ATOM 3659 O OG1 . THR C 2 47 ? 41.762 -19.731 45.458 1.00 129.85 ? 47 THR C OG1 1 ATOM 3660 C CG2 . THR C 2 47 ? 41.795 -20.444 47.737 1.00 118.89 ? 47 THR C CG2 1 ATOM 3661 N N . CYS C 2 48 ? 43.120 -16.244 46.074 1.00 119.97 ? 48 CYS C N 1 ATOM 3662 C CA . CYS C 2 48 ? 43.299 -15.207 45.048 1.00 129.87 ? 48 CYS C CA 1 ATOM 3663 C C . CYS C 2 48 ? 43.297 -15.847 43.654 1.00 130.47 ? 48 CYS C C 1 ATOM 3664 O O . CYS C 2 48 ? 44.138 -16.706 43.372 1.00 126.25 ? 48 CYS C O 1 ATOM 3665 C CB . CYS C 2 48 ? 44.581 -14.385 45.263 1.00 132.25 ? 48 CYS C CB 1 ATOM 3666 S SG . CYS C 2 48 ? 44.594 -12.771 44.330 1.00 118.94 ? 48 CYS C SG 1 ATOM 3667 N N . PRO C 2 49 ? 42.364 -15.415 42.776 1.00 124.15 ? 49 PRO C N 1 ATOM 3668 C CA . PRO C 2 49 ? 42.198 -15.991 41.420 1.00 120.69 ? 49 PRO C CA 1 ATOM 3669 C C . PRO C 2 49 ? 43.490 -15.925 40.596 1.00 125.57 ? 49 PRO C C 1 ATOM 3670 O O . PRO C 2 49 ? 43.984 -14.834 40.408 1.00 119.02 ? 49 PRO C O 1 ATOM 3671 C CB . PRO C 2 49 ? 41.105 -15.112 40.796 1.00 106.99 ? 49 PRO C CB 1 ATOM 3672 C CG . PRO C 2 49 ? 41.162 -13.799 41.581 1.00 111.67 ? 49 PRO C CG 1 ATOM 3673 C CD . PRO C 2 49 ? 41.497 -14.239 42.994 1.00 115.86 ? 49 PRO C CD 1 ATOM 3674 N N . SER C 2 50 ? 43.982 -17.063 40.105 1.00 141.70 ? 50 SER C N 1 ATOM 3675 C CA . SER C 2 50 ? 45.190 -17.164 39.288 1.00 158.65 ? 50 SER C CA 1 ATOM 3676 C C . SER C 2 50 ? 45.164 -16.625 37.866 1.00 174.95 ? 50 SER C C 1 ATOM 3677 O O . SER C 2 50 ? 46.148 -16.046 37.436 1.00 172.47 ? 50 SER C O 1 ATOM 3678 C CB . SER C 2 50 ? 45.601 -18.622 39.223 1.00 161.54 ? 50 SER C CB 1 ATOM 3679 O OG . SER C 2 50 ? 46.935 -18.772 38.762 1.00 168.18 ? 50 SER C OG 1 ATOM 3680 N N . LYS C 2 51 ? 44.128 -16.926 37.100 1.00 197.62 ? 51 LYS C N 1 ATOM 3681 C CA . LYS C 2 51 ? 43.866 -16.181 35.887 1.00 198.32 ? 51 LYS C CA 1 ATOM 3682 C C . LYS C 2 51 ? 44.847 -15.990 34.734 1.00 198.25 ? 51 LYS C C 1 ATOM 3683 O O . LYS C 2 51 ? 46.067 -16.086 34.847 1.00 199.72 ? 51 LYS C O 1 ATOM 3684 C CB . LYS C 2 51 ? 43.517 -14.811 36.393 1.00 193.15 ? 51 LYS C CB 1 ATOM 3685 C CG . LYS C 2 51 ? 44.386 -13.721 35.873 1.00 190.90 ? 51 LYS C CG 1 ATOM 3686 C CD . LYS C 2 51 ? 44.383 -12.822 36.851 1.00 184.86 ? 51 LYS C CD 1 ATOM 3687 C CE . LYS C 2 51 ? 45.189 -13.384 37.907 1.00 183.57 ? 51 LYS C CE 1 ATOM 3688 N NZ . LYS C 2 51 ? 44.565 -13.248 39.213 1.00 182.64 ? 51 LYS C NZ 1 ATOM 3689 N N . LYS C 2 52 ? 44.183 -15.739 33.612 1.00 189.98 ? 52 LYS C N 1 ATOM 3690 C CA . LYS C 2 52 ? 44.581 -14.946 32.457 1.00 174.87 ? 52 LYS C CA 1 ATOM 3691 C C . LYS C 2 52 ? 46.058 -14.664 32.098 1.00 173.97 ? 52 LYS C C 1 ATOM 3692 O O . LYS C 2 52 ? 46.977 -14.959 32.860 1.00 186.42 ? 52 LYS C O 1 ATOM 3693 C CB . LYS C 2 52 ? 43.922 -13.581 32.594 1.00 168.04 ? 52 LYS C CB 1 ATOM 3694 C CG . LYS C 2 52 ? 42.548 -13.501 33.179 1.00 154.89 ? 52 LYS C CG 1 ATOM 3695 C CD . LYS C 2 52 ? 41.588 -14.406 32.545 1.00 154.23 ? 52 LYS C CD 1 ATOM 3696 C CE . LYS C 2 52 ? 40.322 -14.318 33.313 1.00 150.08 ? 52 LYS C CE 1 ATOM 3697 N NZ . LYS C 2 52 ? 39.277 -15.038 32.577 1.00 144.62 ? 52 LYS C NZ 1 ATOM 3698 N N . PRO C 2 53 ? 46.288 -14.109 30.882 1.00 154.46 ? 53 PRO C N 1 ATOM 3699 C CA . PRO C 2 53 ? 47.615 -13.734 30.375 1.00 154.23 ? 53 PRO C CA 1 ATOM 3700 C C . PRO C 2 53 ? 47.934 -12.217 30.484 1.00 175.05 ? 53 PRO C C 1 ATOM 3701 O O . PRO C 2 53 ? 49.093 -11.794 30.371 1.00 166.10 ? 53 PRO C O 1 ATOM 3702 C CB . PRO C 2 53 ? 47.546 -14.198 28.914 1.00 149.39 ? 53 PRO C CB 1 ATOM 3703 C CG . PRO C 2 53 ? 46.026 -14.269 28.585 1.00 141.61 ? 53 PRO C CG 1 ATOM 3704 C CD . PRO C 2 53 ? 45.297 -13.850 29.816 1.00 146.49 ? 53 PRO C CD 1 ATOM 3705 N N . TYR C 2 54 ? 46.880 -11.426 30.677 1.00 182.13 ? 54 TYR C N 1 ATOM 3706 C CA . TYR C 2 54 ? 46.890 -9.966 30.577 1.00 186.78 ? 54 TYR C CA 1 ATOM 3707 C C . TYR C 2 54 ? 46.232 -9.176 31.759 1.00 147.37 ? 54 TYR C C 1 ATOM 3708 O O . TYR C 2 54 ? 45.227 -8.494 31.579 1.00 131.31 ? 54 TYR C O 1 ATOM 3709 C CB . TYR C 2 54 ? 46.198 -9.632 29.255 1.00 191.91 ? 54 TYR C CB 1 ATOM 3710 C CG . TYR C 2 54 ? 45.899 -8.193 29.083 1.00 198.42 ? 54 TYR C CG 1 ATOM 3711 C CD1 . TYR C 2 54 ? 46.890 -7.231 29.150 1.00 202.77 ? 54 TYR C CD1 1 ATOM 3712 C CD2 . TYR C 2 54 ? 44.581 -7.789 28.966 1.00 201.39 ? 54 TYR C CD2 1 ATOM 3713 C CE1 . TYR C 2 54 ? 46.574 -5.905 29.038 1.00 208.00 ? 54 TYR C CE1 1 ATOM 3714 C CE2 . TYR C 2 54 ? 44.262 -6.499 28.869 1.00 207.55 ? 54 TYR C CE2 1 ATOM 3715 C CZ . TYR C 2 54 ? 45.251 -5.548 28.897 1.00 213.70 ? 54 TYR C CZ 1 ATOM 3716 O OH . TYR C 2 54 ? 44.897 -4.229 28.787 1.00 219.35 ? 54 TYR C OH 1 ATOM 3717 N N . GLU C 2 55 ? 46.790 -9.205 32.970 1.00 152.81 ? 55 GLU C N 1 ATOM 3718 C CA . GLU C 2 55 ? 46.025 -8.621 34.088 1.00 137.32 ? 55 GLU C CA 1 ATOM 3719 C C . GLU C 2 55 ? 46.625 -7.577 35.018 1.00 130.47 ? 55 GLU C C 1 ATOM 3720 O O . GLU C 2 55 ? 47.846 -7.411 35.137 1.00 130.10 ? 55 GLU C O 1 ATOM 3721 C CB . GLU C 2 55 ? 45.560 -9.764 34.964 1.00 135.02 ? 55 GLU C CB 1 ATOM 3722 C CG . GLU C 2 55 ? 44.994 -10.879 34.175 1.00 143.51 ? 55 GLU C CG 1 ATOM 3723 C CD . GLU C 2 55 ? 44.008 -10.433 33.120 1.00 152.05 ? 55 GLU C CD 1 ATOM 3724 O OE1 . GLU C 2 55 ? 43.082 -9.654 33.439 1.00 150.84 ? 55 GLU C OE1 1 ATOM 3725 O OE2 . GLU C 2 55 ? 44.205 -10.832 31.946 1.00 157.63 -1 55 GLU C OE2 1 ATOM 3726 N N . GLU C 2 56 ? 45.721 -6.906 35.725 1.00 122.12 ? 56 GLU C N 1 ATOM 3727 C CA . GLU C 2 56 ? 46.120 -5.924 36.707 1.00 127.30 ? 56 GLU C CA 1 ATOM 3728 C C . GLU C 2 56 ? 45.338 -6.272 37.967 1.00 125.40 ? 56 GLU C C 1 ATOM 3729 O O . GLU C 2 56 ? 44.831 -5.412 38.707 1.00 130.93 ? 56 GLU C O 1 ATOM 3730 C CB . GLU C 2 56 ? 45.849 -4.522 36.234 1.00 112.99 ? 56 GLU C CB 1 ATOM 3731 C CG . GLU C 2 56 ? 46.336 -4.380 34.868 1.00 101.09 ? 56 GLU C CG 1 ATOM 3732 C CD . GLU C 2 56 ? 47.042 -3.115 34.657 1.00 109.32 ? 56 GLU C CD 1 ATOM 3733 O OE1 . GLU C 2 56 ? 47.003 -2.230 35.527 1.00 98.68 ? 56 GLU C OE1 1 ATOM 3734 O OE2 . GLU C 2 56 ? 47.611 -2.983 33.571 1.00 128.12 -1 56 GLU C OE2 1 ATOM 3735 N N . VAL C 2 57 ? 45.265 -7.589 38.133 1.00 105.99 ? 57 VAL C N 1 ATOM 3736 C CA . VAL C 2 57 ? 44.882 -8.334 39.324 1.00 84.84 ? 57 VAL C CA 1 ATOM 3737 C C . VAL C 2 57 ? 45.603 -8.094 40.585 1.00 79.99 ? 57 VAL C C 1 ATOM 3738 O O . VAL C 2 57 ? 46.797 -8.078 40.594 1.00 89.95 ? 57 VAL C O 1 ATOM 3739 C CB . VAL C 2 57 ? 44.991 -9.732 39.023 1.00 73.10 ? 57 VAL C CB 1 ATOM 3740 C CG1 . VAL C 2 57 ? 44.944 -10.610 40.410 1.00 67.71 ? 57 VAL C CG1 1 ATOM 3741 C CG2 . VAL C 2 57 ? 43.908 -9.906 37.829 1.00 91.87 ? 57 VAL C CG2 1 ATOM 3742 N N . THR C 2 58 ? 44.835 -7.914 41.647 1.00 79.29 ? 58 THR C N 1 ATOM 3743 C CA . THR C 2 58 ? 45.296 -7.512 42.972 1.00 75.44 ? 58 THR C CA 1 ATOM 3744 C C . THR C 2 58 ? 44.416 -8.193 44.062 1.00 96.58 ? 58 THR C C 1 ATOM 3745 O O . THR C 2 58 ? 43.206 -8.213 43.919 1.00 103.48 ? 58 THR C O 1 ATOM 3746 C CB . THR C 2 58 ? 45.209 -5.926 43.114 1.00 84.88 ? 58 THR C CB 1 ATOM 3747 O OG1 . THR C 2 58 ? 45.430 -5.292 41.841 1.00 83.43 ? 58 THR C OG1 1 ATOM 3748 C CG2 . THR C 2 58 ? 46.174 -5.338 44.107 1.00 70.08 ? 58 THR C CG2 1 ATOM 3749 N N . CYS C 2 59 ? 45.027 -8.796 45.081 1.00 88.44 ? 59 CYS C N 1 ATOM 3750 C CA . CYS C 2 59 ? 44.394 -9.382 46.270 1.00 86.43 ? 59 CYS C CA 1 ATOM 3751 C C . CYS C 2 59 ? 44.599 -8.442 47.455 1.00 94.11 ? 59 CYS C C 1 ATOM 3752 O O . CYS C 2 59 ? 45.515 -7.611 47.458 1.00 87.52 ? 59 CYS C O 1 ATOM 3753 C CB . CYS C 2 59 ? 45.056 -10.720 46.702 1.00 87.40 ? 59 CYS C CB 1 ATOM 3754 S SG . CYS C 2 59 ? 44.351 -12.375 46.318 1.00 115.59 ? 59 CYS C SG 1 ATOM 3755 N N . CYS C 2 60 ? 43.779 -8.616 48.486 1.00 100.13 ? 60 CYS C N 1 ATOM 3756 C CA . CYS C 2 60 ? 43.997 -7.929 49.735 1.00 88.61 ? 60 CYS C CA 1 ATOM 3757 C C . CYS C 2 60 ? 43.169 -8.632 50.780 1.00 87.16 ? 60 CYS C C 1 ATOM 3758 O O . CYS C 2 60 ? 42.242 -9.340 50.446 1.00 88.43 ? 60 CYS C O 1 ATOM 3759 C CB . CYS C 2 60 ? 43.636 -6.449 49.638 1.00 90.74 ? 60 CYS C CB 1 ATOM 3760 S SG . CYS C 2 60 ? 42.070 -6.049 48.849 1.00 112.98 ? 60 CYS C SG 1 ATOM 3761 N N . SER C 2 61 ? 43.500 -8.407 52.047 1.00 95.30 ? 61 SER C N 1 ATOM 3762 C CA . SER C 2 61 ? 42.958 -9.193 53.148 1.00 87.55 ? 61 SER C CA 1 ATOM 3763 C C . SER C 2 61 ? 42.384 -8.287 54.201 1.00 94.24 ? 61 SER C C 1 ATOM 3764 O O . SER C 2 61 ? 41.835 -8.735 55.197 1.00 87.60 ? 61 SER C O 1 ATOM 3765 C CB . SER C 2 61 ? 43.992 -10.107 53.734 1.00 87.34 ? 61 SER C CB 1 ATOM 3766 O OG . SER C 2 61 ? 44.672 -10.744 52.686 1.00 113.21 ? 61 SER C OG 1 ATOM 3767 N N . THR C 2 62 ? 42.496 -7.000 53.921 1.00 97.51 ? 62 THR C N 1 ATOM 3768 C CA . THR C 2 62 ? 42.002 -5.932 54.759 1.00 90.31 ? 62 THR C CA 1 ATOM 3769 C C . THR C 2 62 ? 40.500 -5.748 54.408 1.00 109.86 ? 62 THR C C 1 ATOM 3770 O O . THR C 2 62 ? 40.049 -6.187 53.349 1.00 112.89 ? 62 THR C O 1 ATOM 3771 C CB . THR C 2 62 ? 42.837 -4.637 54.452 1.00 109.15 ? 62 THR C CB 1 ATOM 3772 O OG1 . THR C 2 62 ? 44.228 -4.904 54.623 1.00 131.83 ? 62 THR C OG1 1 ATOM 3773 C CG2 . THR C 2 62 ? 42.433 -3.409 55.237 1.00 90.10 ? 62 THR C CG2 1 ATOM 3774 N N . ASP C 2 63 ? 39.709 -5.153 55.299 1.00 104.59 ? 63 ASP C N 1 ATOM 3775 C CA . ASP C 2 63 ? 38.408 -4.610 54.909 1.00 95.85 ? 63 ASP C CA 1 ATOM 3776 C C . ASP C 2 63 ? 38.741 -3.548 53.867 1.00 102.57 ? 63 ASP C C 1 ATOM 3777 O O . ASP C 2 63 ? 39.911 -3.331 53.600 1.00 94.67 ? 63 ASP C O 1 ATOM 3778 C CB . ASP C 2 63 ? 37.635 -4.019 56.114 1.00 85.62 ? 63 ASP C CB 1 ATOM 3779 C CG . ASP C 2 63 ? 36.755 -5.052 56.818 1.00 93.82 ? 63 ASP C CG 1 ATOM 3780 O OD1 . ASP C 2 63 ? 36.612 -6.160 56.259 1.00 98.29 -1 63 ASP C OD1 1 ATOM 3781 O OD2 . ASP C 2 63 ? 36.216 -4.774 57.932 1.00 101.28 ? 63 ASP C OD2 1 ATOM 3782 N N . LYS C 2 64 ? 37.752 -2.903 53.249 1.00 122.35 ? 64 LYS C N 1 ATOM 3783 C CA . LYS C 2 64 ? 38.063 -1.668 52.523 1.00 129.22 ? 64 LYS C CA 1 ATOM 3784 C C . LYS C 2 64 ? 38.876 -1.803 51.223 1.00 116.03 ? 64 LYS C C 1 ATOM 3785 O O . LYS C 2 64 ? 38.840 -0.911 50.382 1.00 108.53 ? 64 LYS C O 1 ATOM 3786 C CB . LYS C 2 64 ? 38.901 -0.763 53.456 1.00 149.42 ? 64 LYS C CB 1 ATOM 3787 C CG . LYS C 2 64 ? 38.217 -0.020 54.576 1.00 164.87 ? 64 LYS C CG 1 ATOM 3788 C CD . LYS C 2 64 ? 39.197 1.003 55.152 1.00 165.47 ? 64 LYS C CD 1 ATOM 3789 C CE . LYS C 2 64 ? 39.593 1.981 54.089 1.00 168.28 ? 64 LYS C CE 1 ATOM 3790 N NZ . LYS C 2 64 ? 38.347 2.417 53.416 1.00 165.37 ? 64 LYS C NZ 1 ATOM 3791 N N . CYS C 2 65 ? 39.615 -2.897 51.051 1.00 113.77 ? 65 CYS C N 1 ATOM 3792 C CA . CYS C 2 65 ? 40.897 -2.790 50.341 1.00 108.85 ? 65 CYS C CA 1 ATOM 3793 C C . CYS C 2 65 ? 40.902 -2.982 48.840 1.00 111.95 ? 65 CYS C C 1 ATOM 3794 O O . CYS C 2 65 ? 41.942 -2.809 48.245 1.00 112.86 ? 65 CYS C O 1 ATOM 3795 C CB . CYS C 2 65 ? 41.927 -3.760 50.934 1.00 104.24 ? 65 CYS C CB 1 ATOM 3796 S SG . CYS C 2 65 ? 41.625 -5.544 50.766 1.00 94.13 ? 65 CYS C SG 1 ATOM 3797 N N . ASN C 2 66 ? 39.787 -3.351 48.211 1.00 112.57 ? 66 ASN C N 1 ATOM 3798 C CA . ASN C 2 66 ? 39.793 -3.433 46.742 1.00 104.59 ? 66 ASN C CA 1 ATOM 3799 C C . ASN C 2 66 ? 38.880 -2.380 46.094 1.00 84.72 ? 66 ASN C C 1 ATOM 3800 O O . ASN C 2 66 ? 37.879 -2.719 45.496 1.00 74.77 ? 66 ASN C O 1 ATOM 3801 C CB . ASN C 2 66 ? 39.397 -4.856 46.259 1.00 98.06 ? 66 ASN C CB 1 ATOM 3802 C CG . ASN C 2 66 ? 37.912 -5.188 46.449 1.00 86.20 ? 66 ASN C CG 1 ATOM 3803 O OD1 . ASN C 2 66 ? 37.300 -4.836 47.446 1.00 91.81 ? 66 ASN C OD1 1 ATOM 3804 N ND2 . ASN C 2 66 ? 37.340 -5.896 45.477 1.00 79.78 ? 66 ASN C ND2 1 ATOM 3805 N N . PRO C 2 67 ? 39.233 -1.085 46.205 1.00 89.90 ? 67 PRO C N 1 ATOM 3806 C CA . PRO C 2 67 ? 38.363 -0.130 45.521 1.00 91.82 ? 67 PRO C CA 1 ATOM 3807 C C . PRO C 2 67 ? 38.692 -0.010 44.050 1.00 106.55 ? 67 PRO C C 1 ATOM 3808 O O . PRO C 2 67 ? 39.863 -0.179 43.669 1.00 118.47 ? 67 PRO C O 1 ATOM 3809 C CB . PRO C 2 67 ? 38.650 1.192 46.239 1.00 86.99 ? 67 PRO C CB 1 ATOM 3810 C CG . PRO C 2 67 ? 40.059 1.074 46.663 1.00 87.84 ? 67 PRO C CG 1 ATOM 3811 C CD . PRO C 2 67 ? 40.303 -0.405 46.960 1.00 90.64 ? 67 PRO C CD 1 ATOM 3812 N N . HIS C 2 68 ? 37.669 0.305 43.251 1.00 108.00 ? 68 HIS C N 1 ATOM 3813 C CA . HIS C 2 68 ? 37.839 0.668 41.855 1.00 111.15 ? 68 HIS C CA 1 ATOM 3814 C C . HIS C 2 68 ? 38.811 1.857 41.835 1.00 123.72 ? 68 HIS C C 1 ATOM 3815 O O . HIS C 2 68 ? 38.987 2.520 42.864 1.00 135.97 ? 68 HIS C O 1 ATOM 3816 C CB . HIS C 2 68 ? 36.465 0.975 41.233 1.00 103.62 ? 68 HIS C CB 1 ATOM 3817 C CG . HIS C 2 68 ? 36.489 1.283 39.767 1.00 109.54 ? 68 HIS C CG 1 ATOM 3818 N ND1 . HIS C 2 68 ? 36.678 2.555 39.264 1.00 110.77 ? 68 HIS C ND1 1 ATOM 3819 C CD2 . HIS C 2 68 ? 36.375 0.469 38.691 1.00 112.82 ? 68 HIS C CD2 1 ATOM 3820 C CE1 . HIS C 2 68 ? 36.659 2.509 37.947 1.00 116.70 ? 68 HIS C CE1 1 ATOM 3821 N NE2 . HIS C 2 68 ? 36.482 1.252 37.571 1.00 118.38 ? 68 HIS C NE2 1 ATOM 3822 N N . PRO C 2 69 ? 39.463 2.138 40.686 1.00 108.97 ? 69 PRO C N 1 ATOM 3823 C CA . PRO C 2 69 ? 40.280 3.357 40.651 1.00 102.08 ? 69 PRO C CA 1 ATOM 3824 C C . PRO C 2 69 ? 39.476 4.647 40.901 1.00 106.92 ? 69 PRO C C 1 ATOM 3825 O O . PRO C 2 69 ? 39.994 5.749 40.766 1.00 94.25 ? 69 PRO C O 1 ATOM 3826 C CB . PRO C 2 69 ? 40.865 3.313 39.257 1.00 106.26 ? 69 PRO C CB 1 ATOM 3827 C CG . PRO C 2 69 ? 41.045 1.845 39.015 1.00 100.89 ? 69 PRO C CG 1 ATOM 3828 C CD . PRO C 2 69 ? 39.820 1.218 39.590 1.00 92.16 ? 69 PRO C CD 1 ATOM 3829 N N . LYS C 2 70 ? 38.212 4.474 41.286 1.00 131.45 ? 70 LYS C N 1 ATOM 3830 C CA . LYS C 2 70 ? 37.341 5.526 41.808 1.00 144.36 ? 70 LYS C CA 1 ATOM 3831 C C . LYS C 2 70 ? 38.051 6.582 42.674 1.00 162.72 ? 70 LYS C C 1 ATOM 3832 O O . LYS C 2 70 ? 38.261 7.701 42.202 1.00 165.90 ? 70 LYS C O 1 ATOM 3833 C CB . LYS C 2 70 ? 36.180 4.857 42.578 1.00 144.04 ? 70 LYS C CB 1 ATOM 3834 C CG . LYS C 2 70 ? 36.548 4.056 43.841 1.00 141.24 ? 70 LYS C CG 1 ATOM 3835 C CD . LYS C 2 70 ? 35.661 2.825 44.015 1.00 130.86 ? 70 LYS C CD 1 ATOM 3836 C CE . LYS C 2 70 ? 34.772 2.897 45.237 1.00 121.53 ? 70 LYS C CE 1 ATOM 3837 N NZ . LYS C 2 70 ? 34.027 1.623 45.432 1.00 117.78 ? 70 LYS C NZ 1 ATOM 3838 N N . GLN C 2 71 ? 38.424 6.248 43.912 1.00 170.17 ? 71 GLN C N 1 ATOM 3839 C CA . GLN C 2 71 ? 39.229 7.152 44.740 1.00 172.66 ? 71 GLN C CA 1 ATOM 3840 C C . GLN C 2 71 ? 40.446 6.503 45.440 1.00 172.78 ? 71 GLN C C 1 ATOM 3841 O O . GLN C 2 71 ? 41.438 6.154 44.794 1.00 167.85 ? 71 GLN C O 1 ATOM 3842 C CB . GLN C 2 71 ? 38.338 7.834 45.795 1.00 171.50 ? 71 GLN C CB 1 ATOM 3843 C CG . GLN C 2 71 ? 37.088 8.529 45.242 1.00 173.64 ? 71 GLN C CG 1 ATOM 3844 C CD . GLN C 2 71 ? 36.888 9.917 45.842 1.00 178.49 ? 71 GLN C CD 1 ATOM 3845 O OE1 . GLN C 2 71 ? 37.176 10.141 47.016 1.00 184.76 ? 71 GLN C OE1 1 ATOM 3846 N NE2 . GLN C 2 71 ? 36.419 10.859 45.029 1.00 174.70 ? 71 GLN C NE2 1 ATOM 3847 N N . ARG C 2 72 ? 40.356 6.363 46.763 1.00 175.69 ? 72 ARG C N 1 ATOM 3848 C CA . ARG C 2 72 ? 41.408 5.768 47.597 1.00 185.74 ? 72 ARG C CA 1 ATOM 3849 C C . ARG C 2 72 ? 40.689 4.927 48.678 1.00 192.36 ? 72 ARG C C 1 ATOM 3850 O O . ARG C 2 72 ? 39.510 5.196 48.936 1.00 189.92 ? 72 ARG C O 1 ATOM 3851 C CB . ARG C 2 72 ? 42.327 6.893 48.160 1.00 166.05 ? 72 ARG C CB 1 ATOM 3852 C CG . ARG C 2 72 ? 42.764 6.786 49.628 1.00 170.21 ? 72 ARG C CG 1 ATOM 3853 C CD . ARG C 2 72 ? 44.171 7.335 49.892 1.00 174.46 ? 72 ARG C CD 1 ATOM 3854 N NE . ARG C 2 72 ? 44.673 6.962 51.221 1.00 179.32 ? 72 ARG C NE 1 ATOM 3855 C CZ . ARG C 2 72 ? 45.549 5.987 51.472 1.00 173.17 ? 72 ARG C CZ 1 ATOM 3856 N NH1 . ARG C 2 72 ? 46.083 5.270 50.490 1.00 167.98 ? 72 ARG C NH1 1 ATOM 3857 N NH2 . ARG C 2 72 ? 45.914 5.745 52.723 1.00 172.49 ? 72 ARG C NH2 1 ATOM 3858 N N . PRO C 2 73 ? 41.362 3.892 49.271 1.00 190.28 ? 73 PRO C N 1 ATOM 3859 C CA . PRO C 2 73 ? 40.608 2.888 50.046 1.00 190.85 ? 73 PRO C CA 1 ATOM 3860 C C . PRO C 2 73 ? 39.529 3.431 50.986 1.00 193.89 ? 73 PRO C C 1 ATOM 3861 O O . PRO C 2 73 ? 39.688 4.409 51.725 1.00 196.48 ? 73 PRO C O 1 ATOM 3862 C CB . PRO C 2 73 ? 41.691 2.146 50.849 1.00 189.61 ? 73 PRO C CB 1 ATOM 3863 C CG . PRO C 2 73 ? 42.940 2.876 50.678 1.00 192.50 ? 73 PRO C CG 1 ATOM 3864 C CD . PRO C 2 73 ? 42.816 3.700 49.433 1.00 193.09 ? 73 PRO C CD 1 ATOM 3865 N N . ILE D 2 1 ? -8.162 -10.414 -40.541 1.00 85.66 ? 1 ILE D N 1 ATOM 3866 C CA . ILE D 2 1 ? -8.857 -9.242 -40.046 1.00 83.26 ? 1 ILE D CA 1 ATOM 3867 C C . ILE D 2 1 ? -7.860 -8.418 -39.254 1.00 101.36 ? 1 ILE D C 1 ATOM 3868 O O . ILE D 2 1 ? -6.937 -8.957 -38.645 1.00 99.32 ? 1 ILE D O 1 ATOM 3869 C CB . ILE D 2 1 ? -10.071 -9.668 -39.190 1.00 85.82 ? 1 ILE D CB 1 ATOM 3870 C CG1 . ILE D 2 1 ? -10.900 -8.495 -38.665 1.00 88.17 ? 1 ILE D CG1 1 ATOM 3871 C CG2 . ILE D 2 1 ? -9.660 -10.542 -38.086 1.00 81.46 ? 1 ILE D CG2 1 ATOM 3872 C CD1 . ILE D 2 1 ? -11.229 -7.466 -39.668 1.00 111.69 ? 1 ILE D CD1 1 ATOM 3873 N N . VAL D 2 2 ? -8.019 -7.104 -39.285 1.00 113.91 ? 2 VAL D N 1 ATOM 3874 C CA . VAL D 2 2 ? -7.260 -6.237 -38.385 1.00 108.99 ? 2 VAL D CA 1 ATOM 3875 C C . VAL D 2 2 ? -8.093 -5.890 -37.174 1.00 108.98 ? 2 VAL D C 1 ATOM 3876 O O . VAL D 2 2 ? -9.198 -5.345 -37.296 1.00 111.18 ? 2 VAL D O 1 ATOM 3877 C CB . VAL D 2 2 ? -6.852 -4.906 -38.996 1.00 110.00 ? 2 VAL D CB 1 ATOM 3878 C CG1 . VAL D 2 2 ? -6.444 -3.939 -37.846 1.00 80.25 ? 2 VAL D CG1 1 ATOM 3879 C CG2 . VAL D 2 2 ? -5.812 -5.073 -40.115 1.00 82.30 ? 2 VAL D CG2 1 ATOM 3880 N N . CYS D 2 3 ? -7.569 -6.262 -36.009 1.00 113.84 ? 3 CYS D N 1 ATOM 3881 C CA . CYS D 2 3 ? -8.218 -6.039 -34.719 1.00 93.85 ? 3 CYS D CA 1 ATOM 3882 C C . CYS D 2 3 ? -7.387 -5.082 -33.892 1.00 76.00 ? 3 CYS D C 1 ATOM 3883 O O . CYS D 2 3 ? -6.194 -5.107 -33.982 1.00 75.45 ? 3 CYS D O 1 ATOM 3884 C CB . CYS D 2 3 ? -8.345 -7.369 -33.980 1.00 84.68 ? 3 CYS D CB 1 ATOM 3885 S SG . CYS D 2 3 ? -8.751 -8.818 -35.027 1.00 143.81 ? 3 CYS D SG 1 ATOM 3886 N N . HIS D 2 4 ? -7.989 -4.298 -33.025 1.00 76.78 ? 4 HIS D N 1 ATOM 3887 C CA . HIS D 2 4 ? -7.170 -3.690 -31.981 1.00 84.39 ? 4 HIS D CA 1 ATOM 3888 C C . HIS D 2 4 ? -6.801 -4.671 -30.883 1.00 92.05 ? 4 HIS D C 1 ATOM 3889 O O . HIS D 2 4 ? -7.595 -5.528 -30.500 1.00 102.77 ? 4 HIS D O 1 ATOM 3890 C CB . HIS D 2 4 ? -7.876 -2.527 -31.333 1.00 89.06 ? 4 HIS D CB 1 ATOM 3891 C CG . HIS D 2 4 ? -8.008 -1.351 -32.213 1.00 83.20 ? 4 HIS D CG 1 ATOM 3892 N ND1 . HIS D 2 4 ? -9.238 -0.825 -32.579 1.00 94.34 ? 4 HIS D ND1 1 ATOM 3893 C CD2 . HIS D 2 4 ? -7.083 -0.547 -32.772 1.00 76.30 ? 4 HIS D CD2 1 ATOM 3894 C CE1 . HIS D 2 4 ? -9.055 0.217 -33.353 1.00 87.26 ? 4 HIS D CE1 1 ATOM 3895 N NE2 . HIS D 2 4 ? -7.748 0.424 -33.474 1.00 90.25 ? 4 HIS D NE2 1 ATOM 3896 N N . THR D 2 5 ? -5.586 -4.540 -30.374 1.00 91.59 ? 5 THR D N 1 ATOM 3897 C CA . THR D 2 5 ? -5.159 -5.328 -29.226 1.00 81.20 ? 5 THR D CA 1 ATOM 3898 C C . THR D 2 5 ? -4.547 -4.515 -28.107 1.00 72.40 ? 5 THR D C 1 ATOM 3899 O O . THR D 2 5 ? -3.979 -3.450 -28.305 1.00 69.03 ? 5 THR D O 1 ATOM 3900 C CB . THR D 2 5 ? -4.179 -6.437 -29.628 1.00 89.38 ? 5 THR D CB 1 ATOM 3901 O OG1 . THR D 2 5 ? -3.663 -7.049 -28.421 1.00 68.21 ? 5 THR D OG1 1 ATOM 3902 C CG2 . THR D 2 5 ? -3.025 -5.861 -30.527 1.00 70.21 ? 5 THR D CG2 1 ATOM 3903 N N . THR D 2 6 ? -4.712 -5.050 -26.914 1.00 72.83 ? 6 THR D N 1 ATOM 3904 C CA . THR D 2 6 ? -4.250 -4.391 -25.705 1.00 89.68 ? 6 THR D CA 1 ATOM 3905 C C . THR D 2 6 ? -2.981 -4.986 -25.140 1.00 87.23 ? 6 THR D C 1 ATOM 3906 O O . THR D 2 6 ? -2.318 -4.330 -24.342 1.00 92.66 ? 6 THR D O 1 ATOM 3907 C CB . THR D 2 6 ? -5.334 -4.430 -24.573 1.00 68.84 ? 6 THR D CB 1 ATOM 3908 O OG1 . THR D 2 6 ? -5.923 -5.732 -24.540 1.00 65.89 ? 6 THR D OG1 1 ATOM 3909 C CG2 . THR D 2 6 ? -6.388 -3.400 -24.792 1.00 66.93 ? 6 THR D CG2 1 ATOM 3910 N N . ALA D 2 7 ? -2.592 -6.163 -25.636 1.00 93.00 ? 7 ALA D N 1 ATOM 3911 C CA . ALA D 2 7 ? -1.307 -6.831 -25.296 1.00 94.07 ? 7 ALA D CA 1 ATOM 3912 C C . ALA D 2 7 ? -0.058 -6.002 -25.622 1.00 67.05 ? 7 ALA D C 1 ATOM 3913 O O . ALA D 2 7 ? 1.048 -6.422 -25.399 1.00 87.58 ? 7 ALA D O 1 ATOM 3914 C CB . ALA D 2 7 ? -1.218 -8.191 -26.001 1.00 100.70 ? 7 ALA D CB 1 ATOM 3915 N N . THR D 2 8 ? -0.306 -4.800 -26.095 1.00 65.15 ? 8 THR D N 1 ATOM 3916 C CA . THR D 2 8 ? 0.594 -3.881 -26.747 1.00 65.73 ? 8 THR D CA 1 ATOM 3917 C C . THR D 2 8 ? 0.527 -2.506 -26.070 1.00 75.90 ? 8 THR D C 1 ATOM 3918 O O . THR D 2 8 ? -0.490 -2.120 -25.509 1.00 86.33 ? 8 THR D O 1 ATOM 3919 C CB . THR D 2 8 ? 0.192 -3.780 -28.255 1.00 83.99 ? 8 THR D CB 1 ATOM 3920 O OG1 . THR D 2 8 ? 1.106 -4.487 -29.121 1.00 73.22 ? 8 THR D OG1 1 ATOM 3921 C CG2 . THR D 2 8 ? 0.074 -2.412 -28.673 1.00 83.98 ? 8 THR D CG2 1 ATOM 3922 N N . SER D 2 9 ? 1.650 -1.818 -26.043 1.00 93.77 ? 9 SER D N 1 ATOM 3923 C CA . SER D 2 9 ? 1.798 -0.551 -25.347 1.00 100.36 ? 9 SER D CA 1 ATOM 3924 C C . SER D 2 9 ? 2.558 0.414 -26.264 1.00 103.59 ? 9 SER D C 1 ATOM 3925 O O . SER D 2 9 ? 3.728 0.147 -26.601 1.00 98.98 ? 9 SER D O 1 ATOM 3926 C CB . SER D 2 9 ? 2.525 -0.752 -24.017 1.00 103.68 ? 9 SER D CB 1 ATOM 3927 O OG . SER D 2 9 ? 2.826 0.489 -23.409 1.00 107.37 ? 9 SER D OG 1 ATOM 3928 N N . PRO D 2 10 ? 1.920 1.526 -26.689 1.00 100.89 ? 10 PRO D N 1 ATOM 3929 C CA . PRO D 2 10 ? 0.536 1.975 -26.534 1.00 98.14 ? 10 PRO D CA 1 ATOM 3930 C C . PRO D 2 10 ? -0.350 1.075 -27.335 1.00 96.58 ? 10 PRO D C 1 ATOM 3931 O O . PRO D 2 10 ? 0.189 0.102 -27.802 1.00 93.44 ? 10 PRO D O 1 ATOM 3932 C CB . PRO D 2 10 ? 0.545 3.386 -27.118 1.00 87.85 ? 10 PRO D CB 1 ATOM 3933 C CG . PRO D 2 10 ? 1.572 3.322 -28.148 1.00 87.32 ? 10 PRO D CG 1 ATOM 3934 C CD . PRO D 2 10 ? 2.652 2.419 -27.608 1.00 91.50 ? 10 PRO D CD 1 ATOM 3935 N N . ILE D 2 11 ? -1.635 1.402 -27.498 1.00 94.66 ? 11 ILE D N 1 ATOM 3936 C CA . ILE D 2 11 ? -2.621 0.512 -28.093 1.00 69.94 ? 11 ILE D CA 1 ATOM 3937 C C . ILE D 2 11 ? -2.618 0.578 -29.607 1.00 114.29 ? 11 ILE D C 1 ATOM 3938 O O . ILE D 2 11 ? -2.347 1.634 -30.205 1.00 97.62 ? 11 ILE D O 1 ATOM 3939 C CB . ILE D 2 11 ? -4.013 0.869 -27.580 1.00 90.64 ? 11 ILE D CB 1 ATOM 3940 C CG1 . ILE D 2 11 ? -4.972 -0.282 -27.781 1.00 70.26 ? 11 ILE D CG1 1 ATOM 3941 C CG2 . ILE D 2 11 ? -4.498 2.212 -28.129 1.00 100.87 ? 11 ILE D CG2 1 ATOM 3942 C CD1 . ILE D 2 11 ? -4.786 -1.226 -26.749 1.00 68.74 ? 11 ILE D CD1 1 ATOM 3943 N N . SER D 2 12 ? -2.967 -0.538 -30.242 1.00 111.09 ? 12 SER D N 1 ATOM 3944 C CA . SER D 2 12 ? -2.578 -0.707 -31.632 1.00 114.05 ? 12 SER D CA 1 ATOM 3945 C C . SER D 2 12 ? -3.404 -1.686 -32.401 1.00 119.95 ? 12 SER D C 1 ATOM 3946 O O . SER D 2 12 ? -4.272 -2.355 -31.834 1.00 130.21 ? 12 SER D O 1 ATOM 3947 C CB . SER D 2 12 ? -1.194 -1.248 -31.703 1.00 108.37 ? 12 SER D CB 1 ATOM 3948 O OG . SER D 2 12 ? -1.307 -2.576 -31.216 1.00 108.86 ? 12 SER D OG 1 ATOM 3949 N N . ALA D 2 13 ? -3.043 -1.817 -33.684 1.00 109.32 ? 13 ALA D N 1 ATOM 3950 C CA . ALA D 2 13 ? -3.769 -2.646 -34.639 1.00 90.00 ? 13 ALA D CA 1 ATOM 3951 C C . ALA D 2 13 ? -2.966 -3.787 -35.178 1.00 75.66 ? 13 ALA D C 1 ATOM 3952 O O . ALA D 2 13 ? -1.855 -3.571 -35.673 1.00 75.86 ? 13 ALA D O 1 ATOM 3953 C CB . ALA D 2 13 ? -4.203 -1.828 -35.733 1.00 77.54 ? 13 ALA D CB 1 ATOM 3954 N N . VAL D 2 14 ? -3.484 -5.010 -35.117 1.00 75.46 ? 14 VAL D N 1 ATOM 3955 C CA . VAL D 2 14 ? -2.722 -6.104 -35.734 1.00 92.41 ? 14 VAL D CA 1 ATOM 3956 C C . VAL D 2 14 ? -3.606 -7.016 -36.523 1.00 90.29 ? 14 VAL D C 1 ATOM 3957 O O . VAL D 2 14 ? -4.821 -7.031 -36.347 1.00 98.57 ? 14 VAL D O 1 ATOM 3958 C CB . VAL D 2 14 ? -1.940 -6.970 -34.762 1.00 89.46 ? 14 VAL D CB 1 ATOM 3959 C CG1 . VAL D 2 14 ? -1.391 -6.131 -33.659 1.00 110.52 ? 14 VAL D CG1 1 ATOM 3960 C CG2 . VAL D 2 14 ? -2.822 -8.058 -34.225 1.00 97.75 ? 14 VAL D CG2 1 ATOM 3961 N N . THR D 2 15 ? -2.963 -7.769 -37.407 1.00 82.88 ? 15 THR D N 1 ATOM 3962 C CA . THR D 2 15 ? -3.629 -8.757 -38.222 1.00 86.11 ? 15 THR D CA 1 ATOM 3963 C C . THR D 2 15 ? -3.750 -10.070 -37.463 1.00 77.63 ? 15 THR D C 1 ATOM 3964 O O . THR D 2 15 ? -2.776 -10.692 -37.128 1.00 85.38 ? 15 THR D O 1 ATOM 3965 C CB . THR D 2 15 ? -2.890 -8.972 -39.581 1.00 92.24 ? 15 THR D CB 1 ATOM 3966 O OG1 . THR D 2 15 ? -2.561 -7.699 -40.208 1.00 80.49 ? 15 THR D OG1 1 ATOM 3967 C CG2 . THR D 2 15 ? -3.789 -9.781 -40.485 1.00 81.19 ? 15 THR D CG2 1 ATOM 3968 N N . CYS D 2 16 ? -4.974 -10.482 -37.180 1.00 90.01 ? 16 CYS D N 1 ATOM 3969 C CA . CYS D 2 16 ? -5.196 -11.706 -36.425 1.00 96.02 ? 16 CYS D CA 1 ATOM 3970 C C . CYS D 2 16 ? -4.530 -12.910 -37.128 1.00 89.38 ? 16 CYS D C 1 ATOM 3971 O O . CYS D 2 16 ? -4.174 -12.824 -38.289 1.00 84.50 ? 16 CYS D O 1 ATOM 3972 C CB . CYS D 2 16 ? -6.705 -11.885 -36.219 1.00 107.78 ? 16 CYS D CB 1 ATOM 3973 S SG . CYS D 2 16 ? -7.519 -10.359 -35.578 1.00 188.73 ? 16 CYS D SG 1 ATOM 3974 N N . PRO D 2 17 ? -4.278 -14.003 -36.393 1.00 97.33 ? 17 PRO D N 1 ATOM 3975 C CA . PRO D 2 17 ? -3.767 -15.255 -36.963 1.00 98.23 ? 17 PRO D CA 1 ATOM 3976 C C . PRO D 2 17 ? -4.688 -15.805 -38.020 1.00 103.34 ? 17 PRO D C 1 ATOM 3977 O O . PRO D 2 17 ? -5.777 -15.282 -38.207 1.00 122.18 ? 17 PRO D O 1 ATOM 3978 C CB . PRO D 2 17 ? -3.731 -16.212 -35.775 1.00 103.81 ? 17 PRO D CB 1 ATOM 3979 C CG . PRO D 2 17 ? -3.672 -15.362 -34.590 1.00 105.72 ? 17 PRO D CG 1 ATOM 3980 C CD . PRO D 2 17 ? -4.366 -14.066 -34.929 1.00 109.79 ? 17 PRO D CD 1 ATOM 3981 N N . PRO D 2 18 ? -4.262 -16.869 -38.702 1.00 105.15 ? 18 PRO D N 1 ATOM 3982 C CA . PRO D 2 18 ? -5.176 -17.584 -39.596 1.00 111.97 ? 18 PRO D CA 1 ATOM 3983 C C . PRO D 2 18 ? -6.325 -18.300 -38.887 1.00 118.46 ? 18 PRO D C 1 ATOM 3984 O O . PRO D 2 18 ? -6.112 -19.008 -37.902 1.00 128.79 ? 18 PRO D O 1 ATOM 3985 C CB . PRO D 2 18 ? -4.250 -18.606 -40.285 1.00 105.77 ? 18 PRO D CB 1 ATOM 3986 C CG . PRO D 2 18 ? -2.917 -18.502 -39.604 1.00 94.69 ? 18 PRO D CG 1 ATOM 3987 C CD . PRO D 2 18 ? -2.860 -17.121 -39.063 1.00 96.53 ? 18 PRO D CD 1 ATOM 3988 N N . GLY D 2 19 ? -7.540 -18.108 -39.391 1.00 117.40 ? 19 GLY D N 1 ATOM 3989 C CA . GLY D 2 19 ? -8.696 -18.803 -38.859 1.00 116.30 ? 19 GLY D CA 1 ATOM 3990 C C . GLY D 2 19 ? -9.437 -17.972 -37.838 1.00 130.18 ? 19 GLY D C 1 ATOM 3991 O O . GLY D 2 19 ? -10.656 -18.146 -37.637 1.00 134.59 ? 19 GLY D O 1 ATOM 3992 N N . GLU D 2 20 ? -8.701 -17.041 -37.226 1.00 130.08 ? 20 GLU D N 1 ATOM 3993 C CA . GLU D 2 20 ? -9.251 -16.099 -36.246 1.00 122.37 ? 20 GLU D CA 1 ATOM 3994 C C . GLU D 2 20 ? -9.782 -14.857 -36.966 1.00 124.77 ? 20 GLU D C 1 ATOM 3995 O O . GLU D 2 20 ? -9.082 -13.848 -37.158 1.00 123.65 ? 20 GLU D O 1 ATOM 3996 C CB . GLU D 2 20 ? -8.221 -15.707 -35.194 1.00 111.12 ? 20 GLU D CB 1 ATOM 3997 C CG . GLU D 2 20 ? -7.807 -16.828 -34.257 1.00 109.40 ? 20 GLU D CG 1 ATOM 3998 C CD . GLU D 2 20 ? -6.893 -16.316 -33.151 1.00 115.81 ? 20 GLU D CD 1 ATOM 3999 O OE1 . GLU D 2 20 ? -6.633 -15.094 -33.128 1.00 116.56 ? 20 GLU D OE1 1 ATOM 4000 O OE2 . GLU D 2 20 ? -6.457 -17.109 -32.284 1.00 117.68 -1 20 GLU D OE2 1 ATOM 4001 N N . ASN D 2 21 ? -11.075 -14.972 -37.266 1.00 114.55 ? 21 ASN D N 1 ATOM 4002 C CA . ASN D 2 21 ? -11.890 -14.159 -38.137 1.00 105.63 ? 21 ASN D CA 1 ATOM 4003 C C . ASN D 2 21 ? -12.464 -12.886 -37.525 1.00 101.34 ? 21 ASN D C 1 ATOM 4004 O O . ASN D 2 21 ? -12.571 -11.828 -38.161 1.00 91.71 ? 21 ASN D O 1 ATOM 4005 C CB . ASN D 2 21 ? -13.027 -15.114 -38.529 1.00 132.73 ? 21 ASN D CB 1 ATOM 4006 C CG . ASN D 2 21 ? -12.613 -16.124 -39.570 1.00 140.34 ? 21 ASN D CG 1 ATOM 4007 O OD1 . ASN D 2 21 ? -13.463 -16.828 -40.125 1.00 148.45 ? 21 ASN D OD1 1 ATOM 4008 N ND2 . ASN D 2 21 ? -11.414 -15.906 -40.092 1.00 148.66 ? 21 ASN D ND2 1 ATOM 4009 N N . LEU D 2 22 ? -12.717 -12.991 -36.231 1.00 104.02 ? 22 LEU D N 1 ATOM 4010 C CA . LEU D 2 22 ? -13.411 -11.992 -35.448 1.00 92.46 ? 22 LEU D CA 1 ATOM 4011 C C . LEU D 2 22 ? -12.514 -11.104 -34.596 1.00 87.63 ? 22 LEU D C 1 ATOM 4012 O O . LEU D 2 22 ? -11.468 -11.538 -34.149 1.00 78.38 ? 22 LEU D O 1 ATOM 4013 C CB . LEU D 2 22 ? -14.378 -12.713 -34.528 1.00 97.61 ? 22 LEU D CB 1 ATOM 4014 C CG . LEU D 2 22 ? -15.291 -13.639 -35.305 1.00 102.92 ? 22 LEU D CG 1 ATOM 4015 C CD1 . LEU D 2 22 ? -16.155 -14.412 -34.330 1.00 100.60 ? 22 LEU D CD1 1 ATOM 4016 C CD2 . LEU D 2 22 ? -16.089 -12.872 -36.363 1.00 105.81 ? 22 LEU D CD2 1 ATOM 4017 N N . CYS D 2 23 ? -12.923 -9.863 -34.384 1.00 85.14 ? 23 CYS D N 1 ATOM 4018 C CA . CYS D 2 23 ? -12.359 -9.052 -33.326 1.00 78.04 ? 23 CYS D CA 1 ATOM 4019 C C . CYS D 2 23 ? -13.367 -8.931 -32.160 1.00 108.03 ? 23 CYS D C 1 ATOM 4020 O O . CYS D 2 23 ? -14.576 -8.841 -32.390 1.00 109.03 ? 23 CYS D O 1 ATOM 4021 C CB . CYS D 2 23 ? -11.980 -7.708 -33.905 1.00 78.96 ? 23 CYS D CB 1 ATOM 4022 S SG . CYS D 2 23 ? -10.570 -7.873 -35.087 1.00 78.76 ? 23 CYS D SG 1 ATOM 4023 N N . TYR D 2 24 ? -12.873 -8.963 -30.918 1.00 117.58 ? 24 TYR D N 1 ATOM 4024 C CA . TYR D 2 24 ? -13.707 -8.863 -29.697 1.00 102.63 ? 24 TYR D CA 1 ATOM 4025 C C . TYR D 2 24 ? -13.171 -7.826 -28.710 1.00 92.16 ? 24 TYR D C 1 ATOM 4026 O O . TYR D 2 24 ? -12.019 -7.379 -28.835 1.00 88.77 ? 24 TYR D O 1 ATOM 4027 C CB . TYR D 2 24 ? -13.793 -10.198 -28.951 1.00 95.47 ? 24 TYR D CB 1 ATOM 4028 C CG . TYR D 2 24 ? -12.534 -10.461 -28.194 1.00 92.25 ? 24 TYR D CG 1 ATOM 4029 C CD1 . TYR D 2 24 ? -11.385 -10.828 -28.860 1.00 93.53 ? 24 TYR D CD1 1 ATOM 4030 C CD2 . TYR D 2 24 ? -12.469 -10.297 -26.821 1.00 98.93 ? 24 TYR D CD2 1 ATOM 4031 C CE1 . TYR D 2 24 ? -10.203 -11.058 -28.169 1.00 117.82 ? 24 TYR D CE1 1 ATOM 4032 C CE2 . TYR D 2 24 ? -11.268 -10.524 -26.114 1.00 90.19 ? 24 TYR D CE2 1 ATOM 4033 C CZ . TYR D 2 24 ? -10.144 -10.904 -26.798 1.00 95.07 ? 24 TYR D CZ 1 ATOM 4034 O OH . TYR D 2 24 ? -8.940 -11.133 -26.171 1.00 82.74 ? 24 TYR D OH 1 ATOM 4035 N N . ARG D 2 25 ? -14.014 -7.508 -27.721 1.00 82.13 ? 25 ARG D N 1 ATOM 4036 C CA . ARG D 2 25 ? -13.734 -6.652 -26.565 1.00 74.83 ? 25 ARG D CA 1 ATOM 4037 C C . ARG D 2 25 ? -14.341 -7.217 -25.306 1.00 88.05 ? 25 ARG D C 1 ATOM 4038 O O . ARG D 2 25 ? -15.524 -7.499 -25.296 1.00 107.57 ? 25 ARG D O 1 ATOM 4039 C CB . ARG D 2 25 ? -14.290 -5.243 -26.778 1.00 73.51 ? 25 ARG D CB 1 ATOM 4040 C CG . ARG D 2 25 ? -14.016 -4.309 -25.630 1.00 72.47 ? 25 ARG D CG 1 ATOM 4041 C CD . ARG D 2 25 ? -14.237 -2.884 -26.017 1.00 86.85 ? 25 ARG D CD 1 ATOM 4042 N NE . ARG D 2 25 ? -15.637 -2.625 -26.297 1.00 119.62 ? 25 ARG D NE 1 ATOM 4043 C CZ . ARG D 2 25 ? -16.157 -1.411 -26.443 1.00 132.26 ? 25 ARG D CZ 1 ATOM 4044 N NH1 . ARG D 2 25 ? -15.374 -0.340 -26.347 1.00 142.73 ? 25 ARG D NH1 1 ATOM 4045 N NH2 . ARG D 2 25 ? -17.454 -1.269 -26.699 1.00 124.13 ? 25 ARG D NH2 1 ATOM 4046 N N . LYS D 2 26 ? -13.544 -7.344 -24.250 1.00 82.37 ? 26 LYS D N 1 ATOM 4047 C CA . LYS D 2 26 ? -13.985 -7.811 -22.923 1.00 82.19 ? 26 LYS D CA 1 ATOM 4048 C C . LYS D 2 26 ? -13.732 -6.762 -21.857 1.00 84.75 ? 26 LYS D C 1 ATOM 4049 O O . LYS D 2 26 ? -12.669 -6.159 -21.836 1.00 79.76 ? 26 LYS D O 1 ATOM 4050 C CB . LYS D 2 26 ? -13.257 -9.086 -22.498 1.00 80.58 ? 26 LYS D CB 1 ATOM 4051 C CG . LYS D 2 26 ? -13.734 -10.364 -23.148 1.00 86.69 ? 26 LYS D CG 1 ATOM 4052 C CD . LYS D 2 26 ? -12.979 -11.536 -22.514 1.00 104.84 ? 26 LYS D CD 1 ATOM 4053 C CE . LYS D 2 26 ? -13.357 -12.895 -23.121 1.00 114.84 ? 26 LYS D CE 1 ATOM 4054 N NZ . LYS D 2 26 ? -12.249 -13.922 -23.033 1.00 107.78 ? 26 LYS D NZ 1 ATOM 4055 N N . MET D 2 27 ? -14.688 -6.549 -20.968 1.00 95.36 ? 27 MET D N 1 ATOM 4056 C CA . MET D 2 27 ? -14.456 -5.728 -19.778 1.00 96.11 ? 27 MET D CA 1 ATOM 4057 C C . MET D 2 27 ? -14.985 -6.430 -18.512 1.00 108.84 ? 27 MET D C 1 ATOM 4058 O O . MET D 2 27 ? -16.184 -6.600 -18.382 1.00 116.38 ? 27 MET D O 1 ATOM 4059 C CB . MET D 2 27 ? -15.117 -4.350 -19.944 1.00 84.24 ? 27 MET D CB 1 ATOM 4060 C CG . MET D 2 27 ? -14.616 -3.567 -21.150 1.00 87.67 ? 27 MET D CG 1 ATOM 4061 S SD . MET D 2 27 ? -15.691 -2.201 -21.633 1.00 104.35 ? 27 MET D SD 1 ATOM 4062 C CE . MET D 2 27 ? -16.824 -3.039 -22.751 1.00 84.60 ? 27 MET D CE 1 ATOM 4063 N N . TRP D 2 28 ? -14.114 -6.885 -17.606 1.00 117.53 ? 28 TRP D N 1 ATOM 4064 C CA . TRP D 2 28 ? -14.559 -7.320 -16.270 1.00 118.79 ? 28 TRP D CA 1 ATOM 4065 C C . TRP D 2 28 ? -14.126 -6.235 -15.286 1.00 112.95 ? 28 TRP D C 1 ATOM 4066 O O . TRP D 2 28 ? -13.604 -5.218 -15.742 1.00 106.15 ? 28 TRP D O 1 ATOM 4067 C CB . TRP D 2 28 ? -13.939 -8.684 -15.916 1.00 120.24 ? 28 TRP D CB 1 ATOM 4068 C CG . TRP D 2 28 ? -12.444 -8.697 -15.949 1.00 138.05 ? 28 TRP D CG 1 ATOM 4069 C CD1 . TRP D 2 28 ? -11.609 -8.397 -14.919 1.00 138.26 ? 28 TRP D CD1 1 ATOM 4070 C CD2 . TRP D 2 28 ? -11.601 -9.106 -17.043 1.00 149.83 ? 28 TRP D CD2 1 ATOM 4071 N NE1 . TRP D 2 28 ? -10.306 -8.541 -15.306 1.00 143.86 ? 28 TRP D NE1 1 ATOM 4072 C CE2 . TRP D 2 28 ? -10.271 -8.985 -16.603 1.00 155.56 ? 28 TRP D CE2 1 ATOM 4073 C CE3 . TRP D 2 28 ? -11.841 -9.552 -18.349 1.00 150.18 ? 28 TRP D CE3 1 ATOM 4074 C CZ2 . TRP D 2 28 ? -9.184 -9.292 -17.419 1.00 153.60 ? 28 TRP D CZ2 1 ATOM 4075 C CZ3 . TRP D 2 28 ? -10.759 -9.858 -19.157 1.00 148.75 ? 28 TRP D CZ3 1 ATOM 4076 C CH2 . TRP D 2 28 ? -9.449 -9.724 -18.688 1.00 155.02 ? 28 TRP D CH2 1 ATOM 4077 N N . CYS D 2 29 ? -14.253 -6.466 -13.964 1.00 122.15 ? 29 CYS D N 1 ATOM 4078 C CA . CYS D 2 29 ? -13.749 -5.497 -12.948 1.00 119.14 ? 29 CYS D CA 1 ATOM 4079 C C . CYS D 2 29 ? -12.596 -5.853 -12.082 1.00 116.97 ? 29 CYS D C 1 ATOM 4080 O O . CYS D 2 29 ? -12.663 -6.829 -11.375 1.00 117.23 ? 29 CYS D O 1 ATOM 4081 C CB . CYS D 2 29 ? -14.828 -5.050 -11.945 1.00 112.25 ? 29 CYS D CB 1 ATOM 4082 S SG . CYS D 2 29 ? -15.759 -3.584 -12.412 1.00 152.45 ? 29 CYS D SG 1 ATOM 4083 N N . ASP D 2 30 ? -11.531 -5.053 -12.149 1.00 104.69 ? 30 ASP D N 1 ATOM 4084 C CA . ASP D 2 30 ? -10.548 -5.108 -11.076 1.00 93.08 ? 30 ASP D CA 1 ATOM 4085 C C . ASP D 2 30 ? -10.808 -3.938 -10.143 1.00 98.06 ? 30 ASP D C 1 ATOM 4086 O O . ASP D 2 30 ? -11.583 -3.028 -10.465 1.00 103.59 ? 30 ASP D O 1 ATOM 4087 C CB . ASP D 2 30 ? -9.091 -5.119 -11.575 1.00 80.84 ? 30 ASP D CB 1 ATOM 4088 C CG . ASP D 2 30 ? -8.534 -3.727 -11.936 1.00 80.02 ? 30 ASP D CG 1 ATOM 4089 O OD1 . ASP D 2 30 ? -9.123 -2.677 -11.552 1.00 62.68 -1 30 ASP D OD1 1 ATOM 4090 O OD2 . ASP D 2 30 ? -7.440 -3.709 -12.576 1.00 58.04 ? 30 ASP D OD2 1 ATOM 4091 N N . VAL D 2 31 ? -10.077 -3.931 -9.034 1.00 95.66 ? 31 VAL D N 1 ATOM 4092 C CA . VAL D 2 31 ? -10.255 -2.993 -7.931 1.00 90.58 ? 31 VAL D CA 1 ATOM 4093 C C . VAL D 2 31 ? -10.001 -1.517 -8.269 1.00 84.40 ? 31 VAL D C 1 ATOM 4094 O O . VAL D 2 31 ? -9.756 -0.683 -7.405 1.00 100.93 ? 31 VAL D O 1 ATOM 4095 C CB . VAL D 2 31 ? -9.327 -3.430 -6.796 1.00 92.56 ? 31 VAL D CB 1 ATOM 4096 C CG1 . VAL D 2 31 ? -9.648 -4.871 -6.418 1.00 91.68 ? 31 VAL D CG1 1 ATOM 4097 C CG2 . VAL D 2 31 ? -7.881 -3.332 -7.230 1.00 96.96 ? 31 VAL D CG2 1 ATOM 4098 N N . PHE D 2 32 ? -10.087 -1.181 -9.533 1.00 65.92 ? 32 PHE D N 1 ATOM 4099 C CA . PHE D 2 32 ? -9.961 0.195 -9.896 1.00 66.66 ? 32 PHE D CA 1 ATOM 4100 C C . PHE D 2 32 ? -11.263 0.721 -10.489 1.00 85.91 ? 32 PHE D C 1 ATOM 4101 O O . PHE D 2 32 ? -11.336 1.895 -10.881 1.00 96.50 ? 32 PHE D O 1 ATOM 4102 C CB . PHE D 2 32 ? -8.790 0.327 -10.863 1.00 72.20 ? 32 PHE D CB 1 ATOM 4103 C CG . PHE D 2 32 ? -7.446 0.464 -10.173 1.00 96.00 ? 32 PHE D CG 1 ATOM 4104 C CD1 . PHE D 2 32 ? -6.999 1.685 -9.696 1.00 96.57 ? 32 PHE D CD1 1 ATOM 4105 C CD2 . PHE D 2 32 ? -6.662 -0.666 -9.935 1.00 99.40 ? 32 PHE D CD2 1 ATOM 4106 C CE1 . PHE D 2 32 ? -5.781 1.785 -9.067 1.00 84.66 ? 32 PHE D CE1 1 ATOM 4107 C CE2 . PHE D 2 32 ? -5.446 -0.572 -9.300 1.00 84.48 ? 32 PHE D CE2 1 ATOM 4108 C CZ . PHE D 2 32 ? -5.006 0.648 -8.865 1.00 86.36 ? 32 PHE D CZ 1 ATOM 4109 N N . CYS D 2 33 ? -12.256 -0.152 -10.649 1.00 87.73 ? 33 CYS D N 1 ATOM 4110 C CA . CYS D 2 33 ? -13.501 0.252 -11.299 1.00 91.93 ? 33 CYS D CA 1 ATOM 4111 C C . CYS D 2 33 ? -13.952 1.636 -10.894 1.00 89.10 ? 33 CYS D C 1 ATOM 4112 O O . CYS D 2 33 ? -14.145 2.509 -11.726 1.00 92.75 ? 33 CYS D O 1 ATOM 4113 C CB . CYS D 2 33 ? -14.614 -0.801 -11.020 1.00 80.82 ? 33 CYS D CB 1 ATOM 4114 S SG . CYS D 2 33 ? -14.272 -2.403 -11.694 1.00 144.54 ? 33 CYS D SG 1 ATOM 4115 N N . SER D 2 34 ? -14.081 1.817 -9.596 1.00 91.45 ? 34 SER D N 1 ATOM 4116 C CA . SER D 2 34 ? -14.409 3.109 -9.029 1.00 91.29 ? 34 SER D CA 1 ATOM 4117 C C . SER D 2 34 ? -13.487 4.199 -9.547 1.00 97.77 ? 34 SER D C 1 ATOM 4118 O O . SER D 2 34 ? -13.924 5.226 -10.049 1.00 84.90 ? 34 SER D O 1 ATOM 4119 C CB . SER D 2 34 ? -14.311 3.066 -7.491 1.00 72.53 ? 34 SER D CB 1 ATOM 4120 O OG . SER D 2 34 ? -14.514 1.744 -7.024 1.00 66.26 ? 34 SER D OG 1 ATOM 4121 N N . SER D 2 35 ? -12.195 3.929 -9.489 1.00 119.27 ? 35 SER D N 1 ATOM 4122 C CA . SER D 2 35 ? -11.223 4.987 -9.668 1.00 119.93 ? 35 SER D CA 1 ATOM 4123 C C . SER D 2 35 ? -11.032 5.431 -11.081 1.00 112.10 ? 35 SER D C 1 ATOM 4124 O O . SER D 2 35 ? -11.070 6.626 -11.355 1.00 110.42 ? 35 SER D O 1 ATOM 4125 C CB . SER D 2 35 ? -9.874 4.551 -9.088 1.00 115.79 ? 35 SER D CB 1 ATOM 4126 O OG . SER D 2 35 ? -9.539 3.244 -9.509 1.00 109.27 ? 35 SER D OG 1 ATOM 4127 N N . ARG D 2 36 ? -10.808 4.483 -11.979 1.00 113.57 ? 36 ARG D N 1 ATOM 4128 C CA . ARG D 2 36 ? -10.544 4.863 -13.358 1.00 119.62 ? 36 ARG D CA 1 ATOM 4129 C C . ARG D 2 36 ? -11.167 3.893 -14.350 1.00 120.65 ? 36 ARG D C 1 ATOM 4130 O O . ARG D 2 36 ? -10.574 2.878 -14.693 1.00 133.30 ? 36 ARG D O 1 ATOM 4131 C CB . ARG D 2 36 ? -9.040 4.922 -13.585 1.00 116.53 ? 36 ARG D CB 1 ATOM 4132 C CG . ARG D 2 36 ? -8.329 3.653 -13.180 1.00 110.56 ? 36 ARG D CG 1 ATOM 4133 C CD . ARG D 2 36 ? -6.925 3.921 -12.840 1.00 112.25 ? 36 ARG D CD 1 ATOM 4134 N NE . ARG D 2 36 ? -6.188 2.690 -12.622 1.00 105.58 ? 36 ARG D NE 1 ATOM 4135 C CZ . ARG D 2 36 ? -5.050 2.655 -11.957 1.00 89.92 ? 36 ARG D CZ 1 ATOM 4136 N NH1 . ARG D 2 36 ? -4.623 3.783 -11.406 1.00 87.24 ? 36 ARG D NH1 1 ATOM 4137 N NH2 . ARG D 2 36 ? -4.388 1.511 -11.799 1.00 79.12 ? 36 ARG D NH2 1 ATOM 4138 N N . GLY D 2 37 ? -12.326 4.228 -14.879 1.00 106.93 ? 37 GLY D N 1 ATOM 4139 C CA . GLY D 2 37 ? -13.059 3.260 -15.666 1.00 98.68 ? 37 GLY D CA 1 ATOM 4140 C C . GLY D 2 37 ? -12.964 1.779 -15.262 1.00 95.04 ? 37 GLY D C 1 ATOM 4141 O O . GLY D 2 37 ? -12.594 1.376 -14.139 1.00 87.91 ? 37 GLY D O 1 ATOM 4142 N N . LYS D 2 38 ? -13.229 0.947 -16.247 1.00 102.17 ? 38 LYS D N 1 ATOM 4143 C CA . LYS D 2 38 ? -13.148 -0.494 -16.129 1.00 102.14 ? 38 LYS D CA 1 ATOM 4144 C C . LYS D 2 38 ? -12.093 -1.027 -17.111 1.00 106.53 ? 38 LYS D C 1 ATOM 4145 O O . LYS D 2 38 ? -11.568 -0.277 -17.960 1.00 86.19 ? 38 LYS D O 1 ATOM 4146 C CB . LYS D 2 38 ? -14.535 -1.052 -16.397 1.00 111.77 ? 38 LYS D CB 1 ATOM 4147 C CG . LYS D 2 38 ? -14.752 -2.442 -16.164 1.00 113.35 ? 38 LYS D CG 1 ATOM 4148 C CD . LYS D 2 38 ? -16.109 -2.596 -15.651 1.00 137.23 ? 38 LYS D CD 1 ATOM 4149 C CE . LYS D 2 38 ? -16.285 -4.003 -15.448 1.00 141.25 ? 38 LYS D CE 1 ATOM 4150 N NZ . LYS D 2 38 ? -16.205 -4.564 -16.869 1.00 152.58 ? 38 LYS D NZ 1 ATOM 4151 N N . VAL D 2 39 ? -11.723 -2.294 -16.979 1.00 112.99 ? 39 VAL D N 1 ATOM 4152 C CA . VAL D 2 39 ? -10.630 -2.706 -17.829 1.00 111.50 ? 39 VAL D CA 1 ATOM 4153 C C . VAL D 2 39 ? -11.117 -3.537 -18.964 1.00 107.03 ? 39 VAL D C 1 ATOM 4154 O O . VAL D 2 39 ? -11.891 -4.460 -18.767 1.00 90.06 ? 39 VAL D O 1 ATOM 4155 C CB . VAL D 2 39 ? -9.567 -3.529 -17.100 1.00 114.15 ? 39 VAL D CB 1 ATOM 4156 C CG1 . VAL D 2 39 ? -8.327 -3.505 -17.999 1.00 122.41 ? 39 VAL D CG1 1 ATOM 4157 C CG2 . VAL D 2 39 ? -9.345 -3.020 -15.690 1.00 111.04 ? 39 VAL D CG2 1 ATOM 4158 N N . VAL D 2 40 ? -10.528 -3.198 -20.109 1.00 116.86 ? 40 VAL D N 1 ATOM 4159 C CA . VAL D 2 40 ? -10.830 -3.592 -21.460 1.00 105.29 ? 40 VAL D CA 1 ATOM 4160 C C . VAL D 2 40 ? -9.727 -4.437 -22.030 1.00 83.60 ? 40 VAL D C 1 ATOM 4161 O O . VAL D 2 40 ? -8.610 -3.993 -22.155 1.00 79.98 ? 40 VAL D O 1 ATOM 4162 C CB . VAL D 2 40 ? -10.951 -2.344 -22.329 1.00 111.08 ? 40 VAL D CB 1 ATOM 4163 C CG1 . VAL D 2 40 ? -11.493 -2.709 -23.675 1.00 124.44 ? 40 VAL D CG1 1 ATOM 4164 C CG2 . VAL D 2 40 ? -11.852 -1.326 -21.652 1.00 111.87 ? 40 VAL D CG2 1 ATOM 4165 N N . GLU D 2 41 ? -10.080 -5.617 -22.462 1.00 81.81 ? 41 GLU D N 1 ATOM 4166 C CA . GLU D 2 41 ? -9.165 -6.491 -23.109 1.00 66.38 ? 41 GLU D CA 1 ATOM 4167 C C . GLU D 2 41 ? -9.600 -6.555 -24.586 1.00 83.55 ? 41 GLU D C 1 ATOM 4168 O O . GLU D 2 41 ? -10.751 -6.844 -24.895 1.00 76.13 ? 41 GLU D O 1 ATOM 4169 C CB . GLU D 2 41 ? -9.196 -7.828 -22.414 1.00 65.68 ? 41 GLU D CB 1 ATOM 4170 C CG . GLU D 2 41 ? -8.800 -8.971 -23.291 1.00 72.03 ? 41 GLU D CG 1 ATOM 4171 C CD . GLU D 2 41 ? -8.672 -10.231 -22.474 1.00 85.80 ? 41 GLU D CD 1 ATOM 4172 O OE1 . GLU D 2 41 ? -8.182 -10.129 -21.316 1.00 85.09 ? 41 GLU D OE1 1 ATOM 4173 O OE2 . GLU D 2 41 ? -9.103 -11.305 -22.957 1.00 85.09 -1 41 GLU D OE2 1 ATOM 4174 N N . LEU D 2 42 ? -8.718 -6.143 -25.486 1.00 82.93 ? 42 LEU D N 1 ATOM 4175 C CA . LEU D 2 42 ? -8.991 -6.168 -26.924 1.00 74.55 ? 42 LEU D CA 1 ATOM 4176 C C . LEU D 2 42 ? -8.145 -7.194 -27.654 1.00 81.25 ? 42 LEU D C 1 ATOM 4177 O O . LEU D 2 42 ? -6.928 -7.210 -27.514 1.00 96.07 ? 42 LEU D O 1 ATOM 4178 C CB . LEU D 2 42 ? -8.698 -4.797 -27.534 1.00 70.39 ? 42 LEU D CB 1 ATOM 4179 C CG . LEU D 2 42 ? -9.266 -3.487 -26.988 1.00 76.45 ? 42 LEU D CG 1 ATOM 4180 C CD1 . LEU D 2 42 ? -8.526 -2.315 -27.592 1.00 71.11 ? 42 LEU D CD1 1 ATOM 4181 C CD2 . LEU D 2 42 ? -10.743 -3.349 -27.371 1.00 80.15 ? 42 LEU D CD2 1 ATOM 4182 N N . GLY D 2 43 ? -8.742 -7.969 -28.532 1.00 82.44 ? 43 GLY D N 1 ATOM 4183 C CA . GLY D 2 43 ? -7.936 -8.829 -29.373 1.00 80.81 ? 43 GLY D CA 1 ATOM 4184 C C . GLY D 2 43 ? -8.701 -9.493 -30.514 1.00 85.74 ? 43 GLY D C 1 ATOM 4185 O O . GLY D 2 43 ? -9.759 -9.041 -30.954 1.00 76.38 ? 43 GLY D O 1 ATOM 4186 N N . CYS D 2 44 ? -8.151 -10.626 -30.918 1.00 97.63 ? 44 CYS D N 1 ATOM 4187 C CA . CYS D 2 44 ? -8.598 -11.452 -32.005 1.00 74.29 ? 44 CYS D CA 1 ATOM 4188 C C . CYS D 2 44 ? -9.245 -12.691 -31.424 1.00 86.21 ? 44 CYS D C 1 ATOM 4189 O O . CYS D 2 44 ? -8.978 -13.053 -30.287 1.00 117.35 ? 44 CYS D O 1 ATOM 4190 C CB . CYS D 2 44 ? -7.391 -11.878 -32.866 1.00 80.00 ? 44 CYS D CB 1 ATOM 4191 S SG . CYS D 2 44 ? -6.469 -10.630 -33.874 1.00 87.77 ? 44 CYS D SG 1 ATOM 4192 N N . ALA D 2 45 ? -10.080 -13.349 -32.201 1.00 85.52 ? 45 ALA D N 1 ATOM 4193 C CA . ALA D 2 45 ? -10.607 -14.654 -31.828 1.00 95.29 ? 45 ALA D CA 1 ATOM 4194 C C . ALA D 2 45 ? -11.231 -15.351 -33.040 1.00 111.53 ? 45 ALA D C 1 ATOM 4195 O O . ALA D 2 45 ? -11.761 -14.694 -33.944 1.00 105.03 ? 45 ALA D O 1 ATOM 4196 C CB . ALA D 2 45 ? -11.605 -14.514 -30.735 1.00 99.78 ? 45 ALA D CB 1 ATOM 4197 N N . ALA D 2 46 ? -11.187 -16.677 -33.059 1.00 121.45 ? 46 ALA D N 1 ATOM 4198 C CA . ALA D 2 46 ? -11.833 -17.410 -34.142 1.00 133.00 ? 46 ALA D CA 1 ATOM 4199 C C . ALA D 2 46 ? -13.345 -17.457 -33.900 1.00 128.75 ? 46 ALA D C 1 ATOM 4200 O O . ALA D 2 46 ? -14.135 -17.139 -34.787 1.00 113.83 ? 46 ALA D O 1 ATOM 4201 C CB . ALA D 2 46 ? -11.243 -18.809 -34.290 1.00 134.07 ? 46 ALA D CB 1 ATOM 4202 N N . THR D 2 47 ? -13.752 -17.865 -32.701 1.00 139.38 ? 47 THR D N 1 ATOM 4203 C CA . THR D 2 47 ? -15.172 -17.824 -32.350 1.00 142.02 ? 47 THR D CA 1 ATOM 4204 C C . THR D 2 47 ? -15.436 -16.881 -31.178 1.00 125.61 ? 47 THR D C 1 ATOM 4205 O O . THR D 2 47 ? -14.610 -16.748 -30.271 1.00 101.74 ? 47 THR D O 1 ATOM 4206 C CB . THR D 2 47 ? -15.726 -19.231 -32.037 1.00 153.54 ? 47 THR D CB 1 ATOM 4207 O OG1 . THR D 2 47 ? -15.073 -19.751 -30.875 1.00 152.38 ? 47 THR D OG1 1 ATOM 4208 C CG2 . THR D 2 47 ? -15.455 -20.171 -33.198 1.00 155.76 ? 47 THR D CG2 1 ATOM 4209 N N . CYS D 2 48 ? -16.596 -16.228 -31.204 1.00 133.12 ? 48 CYS D N 1 ATOM 4210 C CA . CYS D 2 48 ? -16.891 -15.225 -30.193 1.00 136.72 ? 48 CYS D CA 1 ATOM 4211 C C . CYS D 2 48 ? -16.791 -15.825 -28.812 1.00 135.67 ? 48 CYS D C 1 ATOM 4212 O O . CYS D 2 48 ? -17.506 -16.772 -28.489 1.00 136.37 ? 48 CYS D O 1 ATOM 4213 C CB . CYS D 2 48 ? -18.277 -14.615 -30.388 1.00 135.59 ? 48 CYS D CB 1 ATOM 4214 S SG . CYS D 2 48 ? -18.249 -13.071 -31.309 1.00 202.93 ? 48 CYS D SG 1 ATOM 4215 N N . PRO D 2 49 ? -15.890 -15.267 -27.992 1.00 117.39 ? 49 PRO D N 1 ATOM 4216 C CA . PRO D 2 49 ? -15.706 -15.740 -26.620 1.00 109.53 ? 49 PRO D CA 1 ATOM 4217 C C . PRO D 2 49 ? -16.997 -15.704 -25.848 1.00 107.42 ? 49 PRO D C 1 ATOM 4218 O O . PRO D 2 49 ? -17.708 -14.723 -26.006 1.00 107.91 ? 49 PRO D O 1 ATOM 4219 C CB . PRO D 2 49 ? -14.712 -14.744 -26.032 1.00 101.44 ? 49 PRO D CB 1 ATOM 4220 C CG . PRO D 2 49 ? -14.809 -13.520 -26.925 1.00 100.99 ? 49 PRO D CG 1 ATOM 4221 C CD . PRO D 2 49 ? -15.039 -14.098 -28.287 1.00 100.48 ? 49 PRO D CD 1 ATOM 4222 N N . SER D 2 50 ? -17.344 -16.788 -25.148 1.00 108.85 ? 50 SER D N 1 ATOM 4223 C CA . SER D 2 50 ? -18.453 -16.805 -24.193 1.00 104.76 ? 50 SER D CA 1 ATOM 4224 C C . SER D 2 50 ? -18.263 -15.823 -23.053 1.00 118.43 ? 50 SER D C 1 ATOM 4225 O O . SER D 2 50 ? -17.341 -15.016 -23.083 1.00 115.68 ? 50 SER D O 1 ATOM 4226 C CB . SER D 2 50 ? -18.620 -18.192 -23.619 1.00 106.38 ? 50 SER D CB 1 ATOM 4227 O OG . SER D 2 50 ? -19.805 -18.248 -22.843 1.00 113.71 ? 50 SER D OG 1 ATOM 4228 N N . LYS D 2 51 ? -19.061 -15.936 -21.994 1.00 139.99 ? 51 LYS D N 1 ATOM 4229 C CA . LYS D 2 51 ? -18.798 -15.104 -20.849 1.00 155.83 ? 51 LYS D CA 1 ATOM 4230 C C . LYS D 2 51 ? -19.477 -15.579 -19.565 1.00 165.09 ? 51 LYS D C 1 ATOM 4231 O O . LYS D 2 51 ? -20.412 -16.379 -19.616 1.00 168.99 ? 51 LYS D O 1 ATOM 4232 C CB . LYS D 2 51 ? -19.286 -13.696 -21.135 1.00 163.02 ? 51 LYS D CB 1 ATOM 4233 C CG . LYS D 2 51 ? -19.379 -13.172 -22.565 1.00 169.46 ? 51 LYS D CG 1 ATOM 4234 C CD . LYS D 2 51 ? -19.599 -11.780 -22.364 1.00 180.87 ? 51 LYS D CD 1 ATOM 4235 C CE . LYS D 2 51 ? -18.270 -11.498 -21.704 1.00 181.15 ? 51 LYS D CE 1 ATOM 4236 N NZ . LYS D 2 51 ? -17.054 -10.729 -22.051 1.00 184.67 ? 51 LYS D NZ 1 ATOM 4237 N N . LYS D 2 52 ? -19.001 -15.074 -18.421 1.00 171.21 ? 52 LYS D N 1 ATOM 4238 C CA . LYS D 2 52 ? -19.516 -15.454 -17.098 1.00 173.79 ? 52 LYS D CA 1 ATOM 4239 C C . LYS D 2 52 ? -19.713 -14.146 -16.299 1.00 181.58 ? 52 LYS D C 1 ATOM 4240 O O . LYS D 2 52 ? -20.286 -13.230 -16.871 1.00 181.04 ? 52 LYS D O 1 ATOM 4241 C CB . LYS D 2 52 ? -18.603 -16.491 -16.393 1.00 172.61 ? 52 LYS D CB 1 ATOM 4242 C CG . LYS D 2 52 ? -19.034 -16.842 -14.943 1.00 166.18 ? 52 LYS D CG 1 ATOM 4243 C CD . LYS D 2 52 ? -19.126 -18.320 -14.720 1.00 164.28 ? 52 LYS D CD 1 ATOM 4244 C CE . LYS D 2 52 ? -20.002 -18.632 -13.508 1.00 159.29 ? 52 LYS D CE 1 ATOM 4245 N NZ . LYS D 2 52 ? -20.590 -20.015 -13.505 1.00 158.93 ? 52 LYS D NZ 1 ATOM 4246 N N . PRO D 2 53 ? -19.131 -13.987 -15.094 1.00 192.51 ? 53 PRO D N 1 ATOM 4247 C CA . PRO D 2 53 ? -19.832 -13.270 -14.027 1.00 196.03 ? 53 PRO D CA 1 ATOM 4248 C C . PRO D 2 53 ? -20.273 -11.902 -14.457 1.00 195.40 ? 53 PRO D C 1 ATOM 4249 O O . PRO D 2 53 ? -21.458 -11.603 -14.556 1.00 204.12 ? 53 PRO D O 1 ATOM 4250 C CB . PRO D 2 53 ? -18.784 -13.222 -12.922 1.00 194.19 ? 53 PRO D CB 1 ATOM 4251 C CG . PRO D 2 53 ? -17.421 -13.425 -13.637 1.00 193.84 ? 53 PRO D CG 1 ATOM 4252 C CD . PRO D 2 53 ? -17.691 -13.645 -15.080 1.00 197.60 ? 53 PRO D CD 1 ATOM 4253 N N . TYR D 2 54 ? -19.282 -11.092 -14.711 1.00 154.33 ? 54 TYR D N 1 ATOM 4254 C CA . TYR D 2 54 ? -19.457 -9.736 -15.028 1.00 128.71 ? 54 TYR D CA 1 ATOM 4255 C C . TYR D 2 54 ? -18.650 -9.559 -16.278 1.00 120.33 ? 54 TYR D C 1 ATOM 4256 O O . TYR D 2 54 ? -17.495 -9.174 -16.234 1.00 116.57 ? 54 TYR D O 1 ATOM 4257 C CB . TYR D 2 54 ? -18.991 -8.823 -13.930 1.00 120.49 ? 54 TYR D CB 1 ATOM 4258 C CG . TYR D 2 54 ? -19.207 -7.376 -14.276 1.00 130.10 ? 54 TYR D CG 1 ATOM 4259 C CD1 . TYR D 2 54 ? -18.628 -6.824 -15.412 1.00 134.76 ? 54 TYR D CD1 1 ATOM 4260 C CD2 . TYR D 2 54 ? -19.993 -6.561 -13.489 1.00 136.80 ? 54 TYR D CD2 1 ATOM 4261 C CE1 . TYR D 2 54 ? -18.840 -5.568 -15.778 1.00 141.63 ? 54 TYR D CE1 1 ATOM 4262 C CE2 . TYR D 2 54 ? -20.170 -5.244 -13.821 1.00 144.94 ? 54 TYR D CE2 1 ATOM 4263 C CZ . TYR D 2 54 ? -19.569 -4.739 -14.973 1.00 151.88 ? 54 TYR D CZ 1 ATOM 4264 O OH . TYR D 2 54 ? -19.725 -3.412 -15.354 1.00 160.22 ? 54 TYR D OH 1 ATOM 4265 N N . GLU D 2 55 ? -19.147 -9.957 -17.414 1.00 131.10 ? 55 GLU D N 1 ATOM 4266 C CA . GLU D 2 55 ? -18.271 -9.681 -18.507 1.00 141.85 ? 55 GLU D CA 1 ATOM 4267 C C . GLU D 2 55 ? -18.997 -8.949 -19.680 1.00 115.31 ? 55 GLU D C 1 ATOM 4268 O O . GLU D 2 55 ? -20.221 -8.916 -19.783 1.00 117.84 ? 55 GLU D O 1 ATOM 4269 C CB . GLU D 2 55 ? -17.586 -10.966 -18.933 1.00 146.60 ? 55 GLU D CB 1 ATOM 4270 C CG . GLU D 2 55 ? -16.960 -11.945 -17.948 1.00 138.67 ? 55 GLU D CG 1 ATOM 4271 C CD . GLU D 2 55 ? -16.168 -13.029 -18.691 1.00 136.98 ? 55 GLU D CD 1 ATOM 4272 O OE1 . GLU D 2 55 ? -15.492 -12.674 -19.672 1.00 126.65 ? 55 GLU D OE1 1 ATOM 4273 O OE2 . GLU D 2 55 ? -16.291 -14.234 -18.368 1.00 140.97 -1 55 GLU D OE2 1 ATOM 4274 N N . GLU D 2 56 ? -18.206 -8.363 -20.566 1.00 112.71 ? 56 GLU D N 1 ATOM 4275 C CA . GLU D 2 56 ? -18.716 -7.505 -21.640 1.00 109.30 ? 56 GLU D CA 1 ATOM 4276 C C . GLU D 2 56 ? -18.221 -7.707 -23.095 1.00 101.69 ? 56 GLU D C 1 ATOM 4277 O O . GLU D 2 56 ? -17.859 -6.750 -23.790 1.00 96.48 ? 56 GLU D O 1 ATOM 4278 C CB . GLU D 2 56 ? -18.463 -6.054 -21.219 1.00 107.18 ? 56 GLU D CB 1 ATOM 4279 C CG . GLU D 2 56 ? -19.256 -5.684 -19.932 1.00 108.47 ? 56 GLU D CG 1 ATOM 4280 C CD . GLU D 2 56 ? -19.747 -4.217 -19.867 1.00 111.48 ? 56 GLU D CD 1 ATOM 4281 O OE1 . GLU D 2 56 ? -19.203 -3.329 -20.555 1.00 118.76 ? 56 GLU D OE1 1 ATOM 4282 O OE2 . GLU D 2 56 ? -20.749 -3.966 -19.189 1.00 96.91 -1 56 GLU D OE2 1 ATOM 4283 N N . VAL D 2 57 ? -18.199 -8.961 -23.502 1.00 95.16 ? 57 VAL D N 1 ATOM 4284 C CA . VAL D 2 57 ? -18.028 -9.291 -24.892 1.00 100.83 ? 57 VAL D CA 1 ATOM 4285 C C . VAL D 2 57 ? -18.857 -8.541 -25.862 1.00 94.03 ? 57 VAL D C 1 ATOM 4286 O O . VAL D 2 57 ? -20.067 -8.393 -25.721 1.00 82.56 ? 57 VAL D O 1 ATOM 4287 C CB . VAL D 2 57 ? -18.318 -10.798 -25.199 1.00 123.85 ? 57 VAL D CB 1 ATOM 4288 C CG1 . VAL D 2 57 ? -18.609 -10.960 -26.625 1.00 115.44 ? 57 VAL D CG1 1 ATOM 4289 C CG2 . VAL D 2 57 ? -17.141 -11.655 -24.821 1.00 107.65 ? 57 VAL D CG2 1 ATOM 4290 N N . THR D 2 58 ? -18.133 -8.019 -26.833 1.00 83.71 ? 58 THR D N 1 ATOM 4291 C CA . THR D 2 58 ? -18.709 -7.350 -27.958 1.00 88.73 ? 58 THR D CA 1 ATOM 4292 C C . THR D 2 58 ? -17.781 -7.900 -29.043 1.00 104.70 ? 58 THR D C 1 ATOM 4293 O O . THR D 2 58 ? -16.581 -7.758 -28.948 1.00 110.11 ? 58 THR D O 1 ATOM 4294 C CB . THR D 2 58 ? -18.702 -5.830 -27.808 1.00 80.78 ? 58 THR D CB 1 ATOM 4295 O OG1 . THR D 2 58 ? -17.441 -5.472 -27.246 1.00 88.54 ? 58 THR D OG1 1 ATOM 4296 C CG2 . THR D 2 58 ? -19.790 -5.420 -26.861 1.00 91.33 ? 58 THR D CG2 1 ATOM 4297 N N . CYS D 2 59 ? -18.344 -8.613 -30.020 1.00 105.33 ? 59 CYS D N 1 ATOM 4298 C CA . CYS D 2 59 ? -17.584 -9.172 -31.147 1.00 103.90 ? 59 CYS D CA 1 ATOM 4299 C C . CYS D 2 59 ? -17.921 -8.423 -32.453 1.00 111.43 ? 59 CYS D C 1 ATOM 4300 O O . CYS D 2 59 ? -18.988 -7.842 -32.575 1.00 105.83 ? 59 CYS D O 1 ATOM 4301 C CB . CYS D 2 59 ? -17.906 -10.660 -31.325 1.00 99.06 ? 59 CYS D CB 1 ATOM 4302 S SG . CYS D 2 59 ? -17.676 -11.749 -29.877 1.00 118.32 ? 59 CYS D SG 1 ATOM 4303 N N . CYS D 2 60 ? -17.064 -8.503 -33.461 1.00 114.68 ? 60 CYS D N 1 ATOM 4304 C CA . CYS D 2 60 ? -17.395 -7.885 -34.742 1.00 104.90 ? 60 CYS D CA 1 ATOM 4305 C C . CYS D 2 60 ? -16.538 -8.474 -35.853 1.00 100.83 ? 60 CYS D C 1 ATOM 4306 O O . CYS D 2 60 ? -15.722 -9.336 -35.594 1.00 99.95 ? 60 CYS D O 1 ATOM 4307 C CB . CYS D 2 60 ? -17.302 -6.358 -34.655 1.00 103.09 ? 60 CYS D CB 1 ATOM 4308 S SG . CYS D 2 60 ? -15.899 -5.702 -33.794 1.00 115.95 ? 60 CYS D SG 1 ATOM 4309 N N . SER D 2 61 ? -16.806 -8.089 -37.096 1.00 112.19 ? 61 SER D N 1 ATOM 4310 C CA . SER D 2 61 ? -16.289 -8.811 -38.258 1.00 121.57 ? 61 SER D CA 1 ATOM 4311 C C . SER D 2 61 ? -15.503 -7.917 -39.190 1.00 114.86 ? 61 SER D C 1 ATOM 4312 O O . SER D 2 61 ? -15.004 -8.362 -40.221 1.00 124.54 ? 61 SER D O 1 ATOM 4313 C CB . SER D 2 61 ? -17.453 -9.392 -39.067 1.00 127.16 ? 61 SER D CB 1 ATOM 4314 O OG . SER D 2 61 ? -18.470 -9.903 -38.233 1.00 124.54 ? 61 SER D OG 1 ATOM 4315 N N . THR D 2 62 ? -15.523 -6.636 -38.859 1.00 103.64 ? 62 THR D N 1 ATOM 4316 C CA . THR D 2 62 ? -14.897 -5.560 -39.607 1.00 100.63 ? 62 THR D CA 1 ATOM 4317 C C . THR D 2 62 ? -13.482 -5.146 -39.143 1.00 110.83 ? 62 THR D C 1 ATOM 4318 O O . THR D 2 62 ? -13.131 -5.385 -37.989 1.00 107.40 ? 62 THR D O 1 ATOM 4319 C CB . THR D 2 62 ? -15.886 -4.392 -39.582 1.00 99.45 ? 62 THR D CB 1 ATOM 4320 O OG1 . THR D 2 62 ? -16.701 -4.479 -40.765 1.00 102.02 ? 62 THR D OG1 1 ATOM 4321 C CG2 . THR D 2 62 ? -15.222 -3.046 -39.545 1.00 99.58 ? 62 THR D CG2 1 ATOM 4322 N N . ASP D 2 63 ? -12.681 -4.536 -40.039 1.00 115.77 ? 63 ASP D N 1 ATOM 4323 C CA . ASP D 2 63 ? -11.418 -3.894 -39.639 1.00 110.73 ? 63 ASP D CA 1 ATOM 4324 C C . ASP D 2 63 ? -11.583 -2.784 -38.599 1.00 103.70 ? 63 ASP D C 1 ATOM 4325 O O . ASP D 2 63 ? -12.273 -1.797 -38.862 1.00 110.13 ? 63 ASP D O 1 ATOM 4326 C CB . ASP D 2 63 ? -10.663 -3.306 -40.852 1.00 86.55 ? 63 ASP D CB 1 ATOM 4327 C CG . ASP D 2 63 ? -9.701 -4.301 -41.479 1.00 93.23 ? 63 ASP D CG 1 ATOM 4328 O OD1 . ASP D 2 63 ? -9.504 -5.386 -40.909 1.00 85.24 ? 63 ASP D OD1 1 ATOM 4329 O OD2 . ASP D 2 63 ? -9.103 -3.997 -42.543 1.00 116.29 -1 63 ASP D OD2 1 ATOM 4330 N N . LYS D 2 64 ? -10.901 -2.934 -37.450 1.00 87.44 ? 64 LYS D N 1 ATOM 4331 C CA . LYS D 2 64 ? -10.748 -1.852 -36.462 1.00 81.99 ? 64 LYS D CA 1 ATOM 4332 C C . LYS D 2 64 ? -12.128 -1.576 -35.889 1.00 99.29 ? 64 LYS D C 1 ATOM 4333 O O . LYS D 2 64 ? -12.542 -0.417 -35.807 1.00 97.95 ? 64 LYS D O 1 ATOM 4334 C CB . LYS D 2 64 ? -10.158 -0.567 -37.099 1.00 111.75 ? 64 LYS D CB 1 ATOM 4335 C CG . LYS D 2 64 ? -8.593 -0.488 -37.317 1.00 100.46 ? 64 LYS D CG 1 ATOM 4336 C CD . LYS D 2 64 ? -8.104 1.004 -37.457 1.00 129.28 ? 64 LYS D CD 1 ATOM 4337 C CE . LYS D 2 64 ? -8.365 1.781 -36.127 1.00 140.96 ? 64 LYS D CE 1 ATOM 4338 N NZ . LYS D 2 64 ? -7.643 3.066 -35.809 1.00 130.64 ? 64 LYS D NZ 1 ATOM 4339 N N . CYS D 2 65 ? -12.876 -2.648 -35.615 1.00 103.97 ? 65 CYS D N 1 ATOM 4340 C CA . CYS D 2 65 ? -14.276 -2.525 -35.180 1.00 115.79 ? 65 CYS D CA 1 ATOM 4341 C C . CYS D 2 65 ? -14.452 -2.602 -33.665 1.00 116.53 ? 65 CYS D C 1 ATOM 4342 O O . CYS D 2 65 ? -15.553 -2.344 -33.157 1.00 111.60 ? 65 CYS D O 1 ATOM 4343 C CB . CYS D 2 65 ? -15.167 -3.580 -35.867 1.00 116.39 ? 65 CYS D CB 1 ATOM 4344 S SG . CYS D 2 65 ? -14.913 -5.349 -35.534 1.00 116.87 ? 65 CYS D SG 1 ATOM 4345 N N . ASN D 2 66 ? -13.371 -2.975 -32.966 1.00 110.03 ? 66 ASN D N 1 ATOM 4346 C CA . ASN D 2 66 ? -13.302 -3.020 -31.503 1.00 87.76 ? 66 ASN D CA 1 ATOM 4347 C C . ASN D 2 66 ? -12.299 -2.040 -30.904 1.00 87.71 ? 66 ASN D C 1 ATOM 4348 O O . ASN D 2 66 ? -11.271 -2.447 -30.349 1.00 88.19 ? 66 ASN D O 1 ATOM 4349 C CB . ASN D 2 66 ? -12.978 -4.448 -31.028 1.00 85.65 ? 66 ASN D CB 1 ATOM 4350 C CG . ASN D 2 66 ? -11.685 -4.988 -31.634 1.00 86.55 ? 66 ASN D CG 1 ATOM 4351 O OD1 . ASN D 2 66 ? -11.493 -4.879 -32.835 1.00 95.73 ? 66 ASN D OD1 1 ATOM 4352 N ND2 . ASN D 2 66 ? -10.775 -5.508 -30.799 1.00 75.56 ? 66 ASN D ND2 1 ATOM 4353 N N . PRO D 2 67 ? -12.574 -0.736 -31.014 1.00 87.66 ? 67 PRO D N 1 ATOM 4354 C CA . PRO D 2 67 ? -11.588 0.102 -30.343 1.00 92.12 ? 67 PRO D CA 1 ATOM 4355 C C . PRO D 2 67 ? -11.831 0.183 -28.873 1.00 114.88 ? 67 PRO D C 1 ATOM 4356 O O . PRO D 2 67 ? -12.937 -0.002 -28.382 1.00 126.36 ? 67 PRO D O 1 ATOM 4357 C CB . PRO D 2 67 ? -11.765 1.464 -31.005 1.00 98.35 ? 67 PRO D CB 1 ATOM 4358 C CG . PRO D 2 67 ? -13.166 1.477 -31.473 1.00 95.70 ? 67 PRO D CG 1 ATOM 4359 C CD . PRO D 2 67 ? -13.523 0.053 -31.815 1.00 92.24 ? 67 PRO D CD 1 ATOM 4360 N N . HIS D 2 68 ? -10.748 0.432 -28.164 1.00 117.15 ? 68 HIS D N 1 ATOM 4361 C CA . HIS D 2 68 ? -10.807 0.814 -26.780 1.00 105.29 ? 68 HIS D CA 1 ATOM 4362 C C . HIS D 2 68 ? -11.754 1.994 -26.701 1.00 115.07 ? 68 HIS D C 1 ATOM 4363 O O . HIS D 2 68 ? -11.998 2.681 -27.716 1.00 122.65 ? 68 HIS D O 1 ATOM 4364 C CB . HIS D 2 68 ? -9.383 1.166 -26.312 1.00 107.16 ? 68 HIS D CB 1 ATOM 4365 C CG . HIS D 2 68 ? -9.277 1.692 -24.911 1.00 111.09 ? 68 HIS D CG 1 ATOM 4366 N ND1 . HIS D 2 68 ? -9.363 3.040 -24.615 1.00 114.92 ? 68 HIS D ND1 1 ATOM 4367 C CD2 . HIS D 2 68 ? -9.072 1.066 -23.729 1.00 93.83 ? 68 HIS D CD2 1 ATOM 4368 C CE1 . HIS D 2 68 ? -9.224 3.215 -23.317 1.00 102.55 ? 68 HIS D CE1 1 ATOM 4369 N NE2 . HIS D 2 68 ? -9.051 2.031 -22.754 1.00 98.28 ? 68 HIS D NE2 1 ATOM 4370 N N . PRO D 2 69 ? -12.348 2.230 -25.523 1.00 103.59 ? 69 PRO D N 1 ATOM 4371 C CA . PRO D 2 69 ? -13.023 3.530 -25.558 1.00 101.28 ? 69 PRO D CA 1 ATOM 4372 C C . PRO D 2 69 ? -12.042 4.743 -25.757 1.00 124.35 ? 69 PRO D C 1 ATOM 4373 O O . PRO D 2 69 ? -12.301 5.829 -25.234 1.00 122.43 ? 69 PRO D O 1 ATOM 4374 C CB . PRO D 2 69 ? -13.756 3.542 -24.227 1.00 89.00 ? 69 PRO D CB 1 ATOM 4375 C CG . PRO D 2 69 ? -14.158 2.071 -24.055 1.00 82.36 ? 69 PRO D CG 1 ATOM 4376 C CD . PRO D 2 69 ? -12.943 1.313 -24.523 1.00 76.92 ? 69 PRO D CD 1 ATOM 4377 N N . LYS D 2 70 ? -10.948 4.522 -26.499 1.00 128.35 ? 70 LYS D N 1 ATOM 4378 C CA . LYS D 2 70 ? -10.039 5.550 -27.020 1.00 129.10 ? 70 LYS D CA 1 ATOM 4379 C C . LYS D 2 70 ? -10.662 6.821 -27.644 1.00 133.24 ? 70 LYS D C 1 ATOM 4380 O O . LYS D 2 70 ? -10.764 7.846 -26.966 1.00 97.20 ? 70 LYS D O 1 ATOM 4381 C CB . LYS D 2 70 ? -9.056 4.877 -28.025 1.00 145.39 ? 70 LYS D CB 1 ATOM 4382 C CG . LYS D 2 70 ? -9.663 4.235 -29.292 1.00 139.92 ? 70 LYS D CG 1 ATOM 4383 C CD . LYS D 2 70 ? -8.799 4.452 -30.515 1.00 134.36 ? 70 LYS D CD 1 ATOM 4384 C CE . LYS D 2 70 ? -9.648 4.591 -31.764 1.00 135.53 ? 70 LYS D CE 1 ATOM 4385 N NZ . LYS D 2 70 ? -8.776 4.712 -32.962 1.00 132.88 ? 70 LYS D NZ 1 ATOM 4386 N N . GLN D 2 71 ? -11.139 6.725 -28.892 1.00 167.85 ? 71 GLN D N 1 ATOM 4387 C CA . GLN D 2 71 ? -11.784 7.825 -29.629 1.00 188.63 ? 71 GLN D CA 1 ATOM 4388 C C . GLN D 2 71 ? -13.131 7.371 -30.138 1.00 199.89 ? 71 GLN D C 1 ATOM 4389 O O . GLN D 2 71 ? -14.108 8.011 -29.835 1.00 206.21 ? 71 GLN D O 1 ATOM 4390 C CB . GLN D 2 71 ? -11.014 8.307 -30.895 1.00 177.25 ? 71 GLN D CB 1 ATOM 4391 C CG . GLN D 2 71 ? -9.484 8.613 -30.971 1.00 171.20 ? 71 GLN D CG 1 ATOM 4392 C CD . GLN D 2 71 ? -8.815 9.069 -29.699 1.00 176.84 ? 71 GLN D CD 1 ATOM 4393 O OE1 . GLN D 2 71 ? -9.460 9.474 -28.731 1.00 181.55 ? 71 GLN D OE1 1 ATOM 4394 N NE2 . GLN D 2 71 ? -7.490 9.091 -29.729 1.00 172.63 ? 71 GLN D NE2 1 ATOM 4395 N N . ARG D 2 72 ? -13.097 6.297 -30.945 1.00 204.16 ? 72 ARG D N 1 ATOM 4396 C CA . ARG D 2 72 ? -14.144 5.534 -31.688 1.00 206.46 ? 72 ARG D CA 1 ATOM 4397 C C . ARG D 2 72 ? -13.506 5.488 -33.117 1.00 196.16 ? 72 ARG D C 1 ATOM 4398 O O . ARG D 2 72 ? -12.691 6.359 -33.435 1.00 201.23 ? 72 ARG D O 1 ATOM 4399 C CB . ARG D 2 72 ? -15.609 6.093 -31.666 1.00 201.18 ? 72 ARG D CB 1 ATOM 4400 C CG . ARG D 2 72 ? -16.305 6.427 -30.324 1.00 205.80 ? 72 ARG D CG 1 ATOM 4401 C CD . ARG D 2 72 ? -15.836 5.469 -29.199 1.00 189.64 ? 72 ARG D CD 1 ATOM 4402 N NE . ARG D 2 72 ? -16.036 6.074 -27.889 1.00 190.81 ? 72 ARG D NE 1 ATOM 4403 C CZ . ARG D 2 72 ? -15.054 6.143 -27.019 1.00 191.80 ? 72 ARG D CZ 1 ATOM 4404 N NH1 . ARG D 2 72 ? -13.881 5.803 -27.452 1.00 188.81 ? 72 ARG D NH1 1 ATOM 4405 N NH2 . ARG D 2 72 ? -15.205 6.657 -25.819 1.00 196.55 ? 72 ARG D NH2 1 ATOM 4406 N N . PRO D 2 73 ? -13.944 4.559 -34.003 1.00 185.43 ? 73 PRO D N 1 ATOM 4407 C CA . PRO D 2 73 ? -13.032 3.846 -34.933 1.00 171.19 ? 73 PRO D CA 1 ATOM 4408 C C . PRO D 2 73 ? -11.855 4.637 -35.543 1.00 153.18 ? 73 PRO D C 1 ATOM 4409 O O . PRO D 2 73 ? -11.949 5.463 -36.444 1.00 148.38 ? 73 PRO D O 1 ATOM 4410 C CB . PRO D 2 73 ? -13.964 3.349 -36.046 1.00 178.80 ? 73 PRO D CB 1 ATOM 4411 C CG . PRO D 2 73 ? -15.288 4.032 -35.847 1.00 182.10 ? 73 PRO D CG 1 ATOM 4412 C CD . PRO D 2 73 ? -15.357 4.492 -34.434 1.00 182.80 ? 73 PRO D CD 1 HETATM 4413 C C1 . NAG E 3 . ? 14.130 5.351 35.388 1.00 105.95 ? 1214 NAG A C1 1 HETATM 4414 C C2 . NAG E 3 . ? 13.219 6.512 35.842 1.00 99.44 ? 1214 NAG A C2 1 HETATM 4415 C C3 . NAG E 3 . ? 12.669 6.253 37.233 1.00 103.38 ? 1214 NAG A C3 1 HETATM 4416 C C4 . NAG E 3 . ? 11.959 4.914 37.269 1.00 106.43 ? 1214 NAG A C4 1 HETATM 4417 C C5 . NAG E 3 . ? 12.955 3.828 36.898 1.00 94.10 ? 1214 NAG A C5 1 HETATM 4418 C C6 . NAG E 3 . ? 12.342 2.447 36.824 1.00 84.81 ? 1214 NAG A C6 1 HETATM 4419 C C7 . NAG E 3 . ? 13.364 8.971 36.001 1.00 113.83 ? 1214 NAG A C7 1 HETATM 4420 C C8 . NAG E 3 . ? 14.275 10.164 36.014 1.00 109.11 ? 1214 NAG A C8 1 HETATM 4421 N N2 . NAG E 3 . ? 13.951 7.778 35.825 1.00 106.20 ? 1214 NAG A N2 1 HETATM 4422 O O3 . NAG E 3 . ? 11.772 7.284 37.634 1.00 108.59 ? 1214 NAG A O3 1 HETATM 4423 O O4 . NAG E 3 . ? 11.445 4.679 38.575 1.00 115.60 ? 1214 NAG A O4 1 HETATM 4424 O O5 . NAG E 3 . ? 13.452 4.102 35.595 1.00 90.51 ? 1214 NAG A O5 1 HETATM 4425 O O6 . NAG E 3 . ? 13.182 1.509 36.160 1.00 75.71 ? 1214 NAG A O6 1 HETATM 4426 O O7 . NAG E 3 . ? 12.156 9.087 36.147 1.00 123.30 ? 1214 NAG A O7 1 HETATM 4427 C C1 . NAG F 3 . ? 26.417 -14.588 27.503 1.00 113.70 ? 1215 NAG A C1 1 HETATM 4428 C C2 . NAG F 3 . ? 27.734 -15.097 28.041 1.00 118.37 ? 1215 NAG A C2 1 HETATM 4429 C C3 . NAG F 3 . ? 27.515 -15.852 29.344 1.00 120.49 ? 1215 NAG A C3 1 HETATM 4430 C C4 . NAG F 3 . ? 26.692 -15.017 30.330 1.00 129.79 ? 1215 NAG A C4 1 HETATM 4431 C C5 . NAG F 3 . ? 25.496 -14.323 29.664 1.00 120.22 ? 1215 NAG A C5 1 HETATM 4432 C C6 . NAG F 3 . ? 24.929 -13.196 30.495 1.00 113.68 ? 1215 NAG A C6 1 HETATM 4433 C C7 . NAG F 3 . ? 29.557 -15.615 26.514 1.00 112.21 ? 1215 NAG A C7 1 HETATM 4434 C C8 . NAG F 3 . ? 30.127 -16.586 25.541 1.00 114.44 ? 1215 NAG A C8 1 HETATM 4435 N N2 . NAG F 3 . ? 28.395 -15.946 27.066 1.00 114.69 ? 1215 NAG A N2 1 HETATM 4436 O O3 . NAG F 3 . ? 28.791 -16.181 29.895 1.00 105.23 ? 1215 NAG A O3 1 HETATM 4437 O O4 . NAG F 3 . ? 26.178 -15.869 31.341 1.00 149.49 ? 1215 NAG A O4 1 HETATM 4438 O O5 . NAG F 3 . ? 25.878 -13.719 28.430 1.00 116.50 ? 1215 NAG A O5 1 HETATM 4439 O O6 . NAG F 3 . ? 25.023 -11.958 29.796 1.00 104.18 ? 1215 NAG A O6 1 HETATM 4440 O O7 . NAG F 3 . ? 30.123 -14.555 26.787 1.00 109.59 ? 1215 NAG A O7 1 HETATM 4441 C C1 . NAG G 3 . ? 12.053 6.303 -20.357 1.00 142.04 ? 1214 NAG B C1 1 HETATM 4442 C C2 . NAG G 3 . ? 13.009 7.365 -20.897 1.00 137.03 ? 1214 NAG B C2 1 HETATM 4443 C C3 . NAG G 3 . ? 13.154 7.231 -22.407 1.00 127.83 ? 1214 NAG B C3 1 HETATM 4444 C C4 . NAG G 3 . ? 13.896 5.936 -22.731 1.00 121.56 ? 1214 NAG B C4 1 HETATM 4445 C C5 . NAG G 3 . ? 13.469 4.824 -21.764 1.00 113.76 ? 1214 NAG B C5 1 HETATM 4446 C C6 . NAG G 3 . ? 14.465 4.567 -20.639 1.00 106.49 ? 1214 NAG B C6 1 HETATM 4447 C C7 . NAG G 3 . ? 13.460 9.616 -20.137 1.00 150.22 ? 1214 NAG B C7 1 HETATM 4448 C C8 . NAG G 3 . ? 12.905 10.970 -19.808 1.00 151.10 ? 1214 NAG B C8 1 HETATM 4449 N N2 . NAG G 3 . ? 12.580 8.715 -20.539 1.00 146.41 ? 1214 NAG B N2 1 HETATM 4450 O O3 . NAG G 3 . ? 13.808 8.348 -22.996 1.00 120.09 ? 1214 NAG B O3 1 HETATM 4451 O O4 . NAG G 3 . ? 13.641 5.565 -24.085 1.00 118.34 ? 1214 NAG B O4 1 HETATM 4452 O O5 . NAG G 3 . ? 12.168 5.094 -21.204 1.00 123.14 ? 1214 NAG B O5 1 HETATM 4453 O O6 . NAG G 3 . ? 14.153 3.458 -19.803 1.00 109.76 ? 1214 NAG B O6 1 HETATM 4454 O O7 . NAG G 3 . ? 14.664 9.369 -20.053 1.00 143.81 ? 1214 NAG B O7 1 HETATM 4455 C C1 . NAG H 3 . ? -0.069 -14.288 -12.547 1.00 114.51 ? 1215 NAG B C1 1 HETATM 4456 C C2 . NAG H 3 . ? -1.303 -14.955 -13.134 1.00 114.88 ? 1215 NAG B C2 1 HETATM 4457 C C3 . NAG H 3 . ? -0.933 -15.832 -14.313 1.00 116.50 ? 1215 NAG B C3 1 HETATM 4458 C C4 . NAG H 3 . ? -0.060 -15.063 -15.317 1.00 124.33 ? 1215 NAG B C4 1 HETATM 4459 C C5 . NAG H 3 . ? 1.016 -14.195 -14.651 1.00 123.32 ? 1215 NAG B C5 1 HETATM 4460 C C6 . NAG H 3 . ? 1.613 -13.170 -15.596 1.00 116.90 ? 1215 NAG B C6 1 HETATM 4461 C C7 . NAG H 3 . ? -2.872 -15.204 -11.288 1.00 105.58 ? 1215 NAG B C7 1 HETATM 4462 C C8 . NAG H 3 . ? -3.512 -16.138 -10.297 1.00 108.27 ? 1215 NAG B C8 1 HETATM 4463 N N2 . NAG H 3 . ? -1.987 -15.749 -12.113 1.00 104.45 ? 1215 NAG B N2 1 HETATM 4464 O O3 . NAG H 3 . ? -2.142 -16.253 -14.930 1.00 99.93 ? 1215 NAG B O3 1 HETATM 4465 O O4 . NAG H 3 . ? 0.606 -15.995 -16.157 1.00 133.01 ? 1215 NAG B O4 1 HETATM 4466 O O5 . NAG H 3 . ? 0.492 -13.467 -13.539 1.00 122.80 ? 1215 NAG B O5 1 HETATM 4467 O O6 . NAG H 3 . ? 1.084 -11.865 -15.388 1.00 109.50 ? 1215 NAG B O6 1 HETATM 4468 O O7 . NAG H 3 . ? -3.143 -14.000 -11.326 1.00 102.11 ? 1215 NAG B 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 . TYR A 5 ? 1.8568 1.3309 1.7757 0.2208 -0.1170 0.3354 5 TYR A N 2 C CA . TYR A 5 ? 1.8293 1.3331 1.7552 0.2043 -0.1066 0.3351 5 TYR A CA 3 C C . TYR A 5 ? 1.7704 1.2543 1.6763 0.1971 -0.0903 0.3289 5 TYR A C 4 O O . TYR A 5 ? 1.7771 1.2288 1.6777 0.1948 -0.0928 0.3288 5 TYR A O 5 C CB . TYR A 5 ? 1.8968 1.4057 1.7986 0.2042 -0.0884 0.3437 5 TYR A CB 6 C CG . TYR A 5 ? 2.0022 1.4932 1.8715 0.1933 -0.1417 0.3232 5 TYR A CG 7 C CD1 . TYR A 5 ? 2.0609 1.5744 1.9618 0.2067 -0.1447 0.3381 5 TYR A CD1 8 C CD2 . TYR A 5 ? 1.9648 1.4754 1.8214 0.1947 -0.1264 0.3199 5 TYR A CD2 9 C CE1 . TYR A 5 ? 2.0570 1.5885 1.9450 0.2201 -0.1456 0.3368 5 TYR A CE1 10 C CE2 . TYR A 5 ? 1.9965 1.5411 1.8686 0.2021 -0.1275 0.3262 5 TYR A CE2 11 C CZ . TYR A 5 ? 2.0774 1.6288 1.9573 0.2165 -0.1368 0.3324 5 TYR A CZ 12 O OH . TYR A 5 ? 2.1289 1.7190 2.0179 0.2266 -0.1315 0.3354 5 TYR A OH 13 N N . ALA A 6 ? 1.7824 1.2681 1.6572 0.1924 -0.0827 0.3171 6 ALA A N 14 C CA . ALA A 6 ? 1.8428 1.3159 1.7129 0.1761 -0.0807 0.3120 6 ALA A CA 15 C C . ALA A 6 ? 1.9262 1.3773 1.7870 0.1599 -0.0769 0.3200 6 ALA A C 16 O O . ALA A 6 ? 1.9309 1.3732 1.7925 0.1459 -0.0745 0.3183 6 ALA A O 17 C CB . ALA A 6 ? 1.7867 1.2761 1.6512 0.1652 -0.0858 0.3034 6 ALA A CB 18 N N . GLN A 7 ? 1.9601 1.4035 1.8115 0.1610 -0.0767 0.3289 7 GLN A N 19 C CA . GLN A 7 ? 2.0419 1.4632 1.8855 0.1458 -0.0739 0.3376 7 GLN A CA 20 C C . GLN A 7 ? 1.9932 1.3861 1.8452 0.1462 -0.0758 0.3406 7 GLN A C 21 O O . GLN A 7 ? 2.0960 1.4703 1.9419 0.1304 -0.0750 0.3433 7 GLN A O 22 C CB . GLN A 7 ? 2.2821 1.7011 2.1126 0.1471 -0.0743 0.3471 7 GLN A CB 23 C CG . GLN A 7 ? 2.5016 1.8940 2.3245 0.1364 -0.0725 0.3596 7 GLN A CG 24 C CD . GLN A 7 ? 2.5609 1.9448 2.3824 0.1123 -0.0701 0.3596 7 GLN A CD 25 O OE1 . GLN A 7 ? 2.5208 1.8824 2.3457 0.1053 -0.0713 0.3598 7 GLN A OE1 26 N NE2 . GLN A 7 ? 2.4830 1.8887 2.3024 0.0983 -0.0687 0.3582 7 GLN A NE2 27 N N . LYS A 8 ? 1.8000 1.1900 1.6660 0.1615 -0.0819 0.3372 8 LYS A N 28 C CA . LYS A 8 ? 1.6832 1.0394 1.5492 0.1603 -0.0890 0.3339 8 LYS A CA 29 C C . LYS A 8 ? 1.8215 1.1810 1.6927 0.1562 -0.0902 0.3210 8 LYS A C 30 O O . LYS A 8 ? 1.9499 1.2826 1.8173 0.1538 -0.0959 0.3138 8 LYS A O 31 C CB . LYS A 8 ? 1.5504 0.8921 1.4199 0.1796 -0.0989 0.3345 8 LYS A CB 32 C CG . LYS A 8 ? 1.5881 0.8898 1.4490 0.1827 -0.1076 0.3251 8 LYS A CG 33 C CD . LYS A 8 ? 1.6701 0.9414 1.5184 0.1621 -0.1049 0.3285 8 LYS A CD 34 C CE . LYS A 8 ? 1.7765 1.0032 1.6129 0.1632 -0.1132 0.3203 8 LYS A CE 35 N NZ . LYS A 8 ? 1.8148 1.0268 1.6481 0.1871 -0.1217 0.3163 8 LYS A NZ 36 N N . LEU A 9 ? 1.8243 1.2141 1.7004 0.1538 -0.0845 0.3179 9 LEU A N 37 C CA . LEU A 9 ? 1.7904 1.1844 1.6691 0.1440 -0.0836 0.3087 9 LEU A CA 38 C C . LEU A 9 ? 1.8384 1.2291 1.7083 0.1217 -0.0783 0.3122 9 LEU A C 39 O O . LEU A 9 ? 1.8717 1.2485 1.7407 0.1089 -0.0798 0.3087 9 LEU A O 40 C CB . LEU A 9 ? 1.7742 1.2000 1.6606 0.1513 -0.0813 0.3033 9 LEU A CB 41 C CG . LEU A 9 ? 1.8797 1.3173 1.7661 0.1368 -0.0778 0.2971 9 LEU A CG 42 C CD1 . LEU A 9 ? 1.9230 1.3434 1.8141 0.1350 -0.0830 0.2900 9 LEU A CD1 43 C CD2 . LEU A 9 ? 1.9045 1.3700 1.7944 0.1438 -0.0772 0.2924 9 LEU A CD2 44 N N . PHE A 10 ? 1.8029 1.2075 1.6661 0.1172 -0.0736 0.3187 10 PHE A N 45 C CA . PHE A 10 ? 1.7932 1.1977 1.6497 0.0970 -0.0704 0.3234 10 PHE A CA 46 C C . PHE A 10 ? 1.9373 1.3106 1.7869 0.0920 -0.0728 0.3310 10 PHE A C 47 O O . PHE A 10 ? 2.0177 1.3895 1.8608 0.0775 -0.0709 0.3375 10 PHE A O 48 C CB . PHE A 10 ? 1.6402 1.0694 1.4921 0.0938 -0.0676 0.3264 10 PHE A CB 49 C CG . PHE A 10 ? 1.5582 0.9918 1.4069 0.0732 -0.0653 0.3323 10 PHE A CG 50 C CD1 . PHE A 10 ? 1.6277 1.0475 1.4670 0.0696 -0.0655 0.3423 10 PHE A CD1 51 C CD2 . PHE A 10 ? 1.3072 0.7611 1.1635 0.0581 -0.0630 0.3286 10 PHE A CD2 52 C CE1 . PHE A 10 ? 1.5603 0.9860 1.3981 0.0506 -0.0641 0.3480 10 PHE A CE1 53 C CE2 . PHE A 10 ? 1.2621 0.7236 1.1179 0.0402 -0.0613 0.3343 10 PHE A CE2 54 C CZ . PHE A 10 ? 1.3828 0.8306 1.2294 0.0361 -0.0620 0.3439 10 PHE A CZ 55 N N . ASN A 11 ? 2.0698 1.4185 1.9201 0.1042 -0.0782 0.3308 11 ASN A N 56 C CA . ASN A 11 ? 2.2950 1.6109 2.1360 0.0978 -0.0815 0.3381 11 ASN A CA 57 C C . ASN A 11 ? 2.5607 1.8671 2.3967 0.0735 -0.0807 0.3387 11 ASN A C 58 O O . ASN A 11 ? 2.5165 1.8254 2.3462 0.0605 -0.0778 0.3472 11 ASN A O 59 C CB . ASN A 11 ? 2.2176 1.5033 2.0586 0.1110 -0.0898 0.3336 11 ASN A CB 60 C CG . ASN A 11 ? 2.0414 1.3247 1.8878 0.1132 -0.0939 0.3199 11 ASN A CG 61 O OD1 . ASN A 11 ? 1.8572 1.1682 1.7117 0.1109 -0.0900 0.3150 11 ASN A OD1 62 N ND2 . ASN A 11 ? 2.0692 1.3172 1.9086 0.1164 -0.1018 0.3135 11 ASN A ND2 63 N N . ASP A 12 ? 2.8270 2.1211 2.6655 0.0684 -0.0845 0.3297 12 ASP A N 64 C CA . ASP A 12 ? 2.8690 2.1881 2.7161 0.0626 -0.0819 0.3220 12 ASP A CA 65 C C . ASP A 12 ? 2.7724 2.0847 2.6216 0.0511 -0.0848 0.3139 12 ASP A C 66 O O . ASP A 12 ? 2.8394 2.1209 2.6821 0.0458 -0.0908 0.3103 12 ASP A O 67 C CB . ASP A 12 ? 3.0148 2.3661 2.8636 0.0520 -0.0749 0.3271 12 ASP A CB 68 C CG . ASP A 12 ? 3.1583 2.5037 3.0001 0.0331 -0.0739 0.3355 12 ASP A CG 69 O OD1 . ASP A 12 ? 3.2158 2.5352 3.0518 0.0216 -0.0777 0.3372 12 ASP A OD1 70 O OD2 . ASP A 12 ? 3.2018 2.5695 3.0430 0.0300 -0.0699 0.3408 12 ASP A OD2 71 N N . LEU A 13 ? 2.2266 1.5693 2.0851 0.0530 -0.0810 0.3096 13 LEU A N 72 C CA . LEU A 13 ? 1.9698 1.3243 1.8341 0.0434 -0.0809 0.3035 13 LEU A CA 73 C C . LEU A 13 ? 2.0395 1.3982 1.9012 0.0202 -0.0788 0.3091 13 LEU A C 74 O O . LEU A 13 ? 2.1512 1.5180 2.0170 0.0083 -0.0791 0.3059 13 LEU A O 75 C CB . LEU A 13 ? 1.6741 1.0623 1.5480 0.0527 -0.0764 0.3003 13 LEU A CB 76 C CG . LEU A 13 ? 1.4663 0.8515 1.3425 0.0759 -0.0792 0.2961 13 LEU A CG 77 C CD1 . LEU A 13 ? 1.0741 0.4912 0.9588 0.0848 -0.0758 0.2923 13 LEU A CD1 78 C CD2 . LEU A 13 ? 1.4575 0.8139 1.3317 0.0838 -0.0875 0.2885 13 LEU A CD2 79 N N . PHE A 14 ? 2.0084 1.3617 1.8634 0.0142 -0.0773 0.3179 14 PHE A N 80 C CA . PHE A 14 ? 2.0519 1.4161 1.9054 -0.0063 -0.0750 0.3245 14 PHE A CA 81 C C . PHE A 14 ? 2.4241 1.7558 2.2665 -0.0202 -0.0796 0.3300 14 PHE A C 82 O O . PHE A 14 ? 2.4145 1.7564 2.2554 -0.0371 -0.0782 0.3365 14 PHE A O 83 C CB . PHE A 14 ? 1.6172 1.0085 1.4720 -0.0041 -0.0696 0.3308 14 PHE A CB 84 C CG . PHE A 14 ? 1.4270 0.8483 1.2904 0.0075 -0.0657 0.3255 14 PHE A CG 85 C CD1 . PHE A 14 ? 1.4948 0.9445 1.3669 -0.0015 -0.0628 0.3231 14 PHE A CD1 86 C CD2 . PHE A 14 ? 1.2951 0.7158 1.1580 0.0274 -0.0656 0.3230 14 PHE A CD2 87 C CE1 . PHE A 14 ? 1.4028 0.8774 1.2823 0.0081 -0.0599 0.3181 14 PHE A CE1 88 C CE2 . PHE A 14 ? 1.3131 0.7596 1.1830 0.0360 -0.0632 0.3178 14 PHE A CE2 89 C CZ . PHE A 14 ? 1.2437 0.7161 1.1218 0.0259 -0.0603 0.3152 14 PHE A CZ 90 N N . GLU A 15 ? 2.3884 1.6823 2.2227 -0.0150 -0.0855 0.3274 15 GLU A N 91 C CA . GLU A 15 ? 2.5783 1.8414 2.4013 -0.0332 -0.0903 0.3311 15 GLU A CA 92 C C . GLU A 15 ? 2.6929 1.9521 2.5167 -0.0476 -0.0939 0.3239 15 GLU A C 93 O O . GLU A 15 ? 2.7358 1.9941 2.5558 -0.0694 -0.0952 0.3274 15 GLU A O 94 C CB . GLU A 15 ? 2.4813 1.7004 2.2924 -0.0244 -0.0959 0.3315 15 GLU A CB 95 C CG . GLU A 15 ? 2.5867 1.7916 2.3994 -0.0010 -0.0995 0.3221 15 GLU A CG 96 C CD . GLU A 15 ? 2.6711 1.8971 2.4907 0.0202 -0.0953 0.3251 15 GLU A CD 97 O OE1 . GLU A 15 ? 2.6713 1.9315 2.4976 0.0175 -0.0887 0.3302 15 GLU A OE1 98 O OE2 . GLU A 15 ? 2.7021 1.9109 2.5198 0.0397 -0.0990 0.3220 15 GLU A OE2 99 N N . ASP A 16 ? 2.6321 1.8887 2.4603 -0.0353 -0.0963 0.3137 16 ASP A N 100 C CA . ASP A 16 ? 2.6334 1.8889 2.4627 -0.0471 -0.0997 0.3066 16 ASP A CA 101 C C . ASP A 16 ? 2.5864 1.8855 2.4302 -0.0445 -0.0940 0.3058 16 ASP A C 102 O O . ASP A 16 ? 2.5687 1.8744 2.4186 -0.0322 -0.0946 0.2983 16 ASP A O 103 C CB . ASP A 16 ? 2.6624 1.8832 2.4848 -0.0363 -0.1074 0.2951 16 ASP A CB 104 C CG . ASP A 16 ? 2.6732 1.8944 2.4964 -0.0470 -0.1112 0.2871 16 ASP A CG 105 O OD1 . ASP A 16 ? 2.6561 1.8844 2.4780 -0.0692 -0.1110 0.2910 16 ASP A OD1 106 O OD2 . ASP A 16 ? 2.6614 1.8752 2.4856 -0.0337 -0.1150 0.2769 16 ASP A OD2 107 N N . TYR A 17 ? 2.5091 1.8367 2.3574 -0.0562 -0.0886 0.3140 17 TYR A N 108 C CA . TYR A 17 ? 2.2745 1.6444 2.1351 -0.0582 -0.0828 0.3149 17 TYR A CA 109 C C . TYR A 17 ? 2.1621 1.5547 2.0237 -0.0682 -0.0782 0.3243 17 TYR A C 110 O O . TYR A 17 ? 2.1640 1.5519 2.0214 -0.0617 -0.0766 0.3291 17 TYR A O 111 C CB . TYR A 17 ? 2.1397 1.5271 2.0089 -0.0371 -0.0791 0.3100 17 TYR A CB 112 C CG . TYR A 17 ? 2.0396 1.4682 1.9203 -0.0388 -0.0731 0.3107 17 TYR A CG 113 C CD1 . TYR A 17 ? 2.0529 1.4993 1.9382 -0.0554 -0.0727 0.3127 17 TYR A CD1 114 C CD2 . TYR A 17 ? 1.9936 1.4430 1.8800 -0.0242 -0.0683 0.3094 17 TYR A CD2 115 C CE1 . TYR A 17 ? 2.0543 1.5371 1.9499 -0.0557 -0.0674 0.3135 17 TYR A CE1 116 C CE2 . TYR A 17 ? 2.0000 1.4838 1.8958 -0.0258 -0.0633 0.3093 17 TYR A CE2 117 C CZ . TYR A 17 ? 2.0495 1.5494 1.9502 -0.0408 -0.0628 0.3114 17 TYR A CZ 118 O OH . TYR A 17 ? 2.0675 1.6006 1.9777 -0.0410 -0.0580 0.3115 17 TYR A OH 119 N N . SER A 18 ? 2.0586 1.4773 1.9261 -0.0833 -0.0766 0.3270 18 SER A N 120 C CA . SER A 18 ? 1.9306 1.3813 1.8029 -0.0894 -0.0720 0.3341 18 SER A CA 121 C C . SER A 18 ? 1.7410 1.2249 1.6247 -0.0936 -0.0693 0.3322 18 SER A C 122 O O . SER A 18 ? 1.5543 1.0335 1.4391 -0.1001 -0.0723 0.3288 18 SER A O 123 C CB . SER A 18 ? 1.9116 1.3546 1.7759 -0.1083 -0.0745 0.3427 18 SER A CB 124 O OG . SER A 18 ? 1.8350 1.2614 1.6916 -0.1016 -0.0742 0.3472 18 SER A OG 125 N N . ASN A 19 ? 1.8263 1.3428 1.7178 -0.0898 -0.0642 0.3345 19 ASN A N 126 C CA . ASN A 19 ? 1.9309 1.4800 1.8339 -0.0881 -0.0606 0.3324 19 ASN A CA 127 C C . ASN A 19 ? 2.0382 1.6002 1.9449 -0.1036 -0.0624 0.3345 19 ASN A C 128 O O . ASN A 19 ? 2.1448 1.7348 2.0611 -0.1017 -0.0591 0.3339 19 ASN A O 129 C CB . ASN A 19 ? 1.9661 1.5451 1.8746 -0.0864 -0.0563 0.3365 19 ASN A CB 130 C CG . ASN A 19 ? 2.0828 1.6692 1.9879 -0.1035 -0.0580 0.3455 19 ASN A CG 131 O OD1 . ASN A 19 ? 2.1669 1.7287 2.0622 -0.1110 -0.0616 0.3491 19 ASN A OD1 132 N ND2 . ASN A 19 ? 2.0813 1.7017 1.9946 -0.1100 -0.0559 0.3495 19 ASN A ND2 133 N N . ALA A 20 ? 1.8361 1.3776 1.7348 -0.1189 -0.0677 0.3368 20 ALA A N 134 C CA . ALA A 20 ? 1.6683 1.2272 1.5697 -0.1364 -0.0695 0.3404 20 ALA A CA 135 C C . ALA A 20 ? 1.6190 1.1772 1.5243 -0.1346 -0.0710 0.3352 20 ALA A C 136 O O . ALA A 20 ? 1.6058 1.1944 1.5203 -0.1352 -0.0681 0.3368 20 ALA A O 137 C CB . ALA A 20 ? 1.6394 1.1792 1.5297 -0.1568 -0.0749 0.3451 20 ALA A CB 138 N N . LEU A 21 ? 1.5084 1.0324 1.4070 -0.1305 -0.0753 0.3290 21 LEU A N 139 C CA . LEU A 21 ? 1.4852 1.0070 1.3861 -0.1321 -0.0782 0.3248 21 LEU A CA 140 C C . LEU A 21 ? 1.4073 0.9321 1.3155 -0.1111 -0.0754 0.3184 21 LEU A C 141 O O . LEU A 21 ? 1.4007 0.9109 1.3071 -0.0958 -0.0743 0.3144 21 LEU A O 142 C CB . LEU A 21 ? 1.5750 1.0574 1.4628 -0.1441 -0.0864 0.3212 21 LEU A CB 143 C CG . LEU A 21 ? 1.5778 1.0159 1.4549 -0.1348 -0.0908 0.3148 21 LEU A CG 144 C CD1 . LEU A 21 ? 1.6359 1.0548 1.5119 -0.1258 -0.0955 0.3057 21 LEU A CD1 145 C CD2 . LEU A 21 ? 1.4898 0.8992 1.3526 -0.1534 -0.0962 0.3168 21 LEU A CD2 146 N N . ARG A 22 ? 1.4475 0.9942 1.3641 -0.1114 -0.0741 0.3184 22 ARG A N 147 C CA . ARG A 22 ? 1.4649 1.0216 1.3900 -0.0939 -0.0708 0.3137 22 ARG A CA 148 C C . ARG A 22 ? 1.5959 1.1182 1.5150 -0.0835 -0.0761 0.3059 22 ARG A C 149 O O . ARG A 22 ? 1.5556 1.0517 1.4668 -0.0921 -0.0836 0.3032 22 ARG A O 150 C CB . ARG A 22 ? 1.4821 1.0643 1.4156 -0.0984 -0.0697 0.3163 22 ARG A CB 151 C CG . ARG A 22 ? 1.5152 1.1346 1.4556 -0.1051 -0.0643 0.3237 22 ARG A CG 152 C CD . ARG A 22 ? 1.4963 1.1357 1.4421 -0.1123 -0.0648 0.3275 22 ARG A CD 153 N NE . ARG A 22 ? 1.4920 1.1280 1.4427 -0.0995 -0.0645 0.3228 22 ARG A NE 154 C CZ . ARG A 22 ? 1.4722 1.1029 1.4225 -0.1054 -0.0694 0.3231 22 ARG A CZ 155 N NH1 . ARG A 22 ? 1.5128 1.1455 1.4567 -0.1222 -0.0727 0.3216 22 ARG A NH1 156 N NH2 . ARG A 22 ? 1.3452 0.9792 1.3001 -0.0912 -0.0671 0.3142 22 ARG A NH2 157 N N . PRO A 23 ? 1.7515 1.2742 1.6738 -0.0651 -0.0727 0.3018 23 PRO A N 158 C CA . PRO A 23 ? 1.7863 1.2803 1.7038 -0.0514 -0.0772 0.2946 23 PRO A CA 159 C C . PRO A 23 ? 1.7620 1.2550 1.6842 -0.0460 -0.0809 0.2899 23 PRO A C 160 O O . PRO A 23 ? 1.8167 1.3129 1.7437 -0.0302 -0.0800 0.2856 23 PRO A O 161 C CB . PRO A 23 ? 1.7705 1.2764 1.6914 -0.0361 -0.0712 0.2939 23 PRO A CB 162 C CG . PRO A 23 ? 1.7414 1.2847 1.6721 -0.0382 -0.0639 0.2975 23 PRO A CG 163 C CD . PRO A 23 ? 1.7548 1.3072 1.6849 -0.0567 -0.0645 0.3037 23 PRO A CD 164 N N . VAL A 24 ? 1.6565 1.1467 1.5770 -0.0601 -0.0855 0.2912 24 VAL A N 165 C CA . VAL A 24 ? 1.6654 1.1507 1.5873 -0.0556 -0.0901 0.2841 24 VAL A CA 166 C C . VAL A 24 ? 1.9066 1.3539 1.8136 -0.0605 -0.0982 0.2742 24 VAL A C 167 O O . VAL A 24 ? 1.7744 1.1966 1.6710 -0.0744 -0.1029 0.2805 24 VAL A O 168 C CB . VAL A 24 ? 1.4562 0.9804 1.3872 -0.0636 -0.0843 0.2840 24 VAL A CB 169 C CG1 . VAL A 24 ? 1.2836 0.8415 1.2284 -0.0544 -0.0763 0.2907 24 VAL A CG1 170 C CG2 . VAL A 24 ? 1.4793 1.0078 1.4062 -0.0851 -0.0855 0.2922 24 VAL A CG2 171 N N . GLU A 25 ? 2.5608 2.0031 2.4664 -0.0485 -0.0999 0.2585 25 GLU A N 172 C CA . GLU A 25 ? 2.6588 2.0644 2.5502 -0.0489 -0.1076 0.2456 25 GLU A CA 173 C C . GLU A 25 ? 2.6817 2.0809 2.5654 -0.0716 -0.1103 0.2445 25 GLU A C 174 O O . GLU A 25 ? 2.8704 2.2294 2.7390 -0.0791 -0.1173 0.2411 25 GLU A O 175 C CB . GLU A 25 ? 2.7173 2.1330 2.6121 -0.0317 -0.1072 0.2284 25 GLU A CB 176 C CG . GLU A 25 ? 2.7577 2.2111 2.6610 -0.0384 -0.1025 0.2221 25 GLU A CG 177 C CD . GLU A 25 ? 2.7432 2.2377 2.6603 -0.0443 -0.0942 0.2357 25 GLU A CD 178 O OE1 . GLU A 25 ? 2.7187 2.2183 2.6416 -0.0384 -0.0910 0.2470 25 GLU A OE1 179 O OE2 . GLU A 25 ? 2.7452 2.2660 2.6665 -0.0554 -0.0912 0.2356 25 GLU A OE2 180 N N . ASP A 26 ? 2.4293 1.8678 2.3225 -0.0825 -0.1048 0.2475 26 ASP A N 181 C CA . ASP A 26 ? 2.3832 1.8248 2.2710 -0.1058 -0.1063 0.2492 26 ASP A CA 182 C C . ASP A 26 ? 2.1949 1.6851 2.0959 -0.1135 -0.0989 0.2599 26 ASP A C 183 O O . ASP A 26 ? 2.2010 1.7207 2.1144 -0.1004 -0.0928 0.2618 26 ASP A O 184 C CB . ASP A 26 ? 2.3829 1.8164 2.2635 -0.1098 -0.1101 0.2312 26 ASP A CB 185 C CG . ASP A 26 ? 2.3304 1.8019 2.2226 -0.0982 -0.1052 0.2209 26 ASP A CG 186 O OD1 . ASP A 26 ? 2.2546 1.7669 2.1602 -0.0957 -0.0980 0.2292 26 ASP A OD1 187 O OD2 . ASP A 26 ? 2.3647 1.8245 2.2516 -0.0914 -0.1086 0.2041 26 ASP A OD2 188 N N . THR A 27 ? 2.2799 1.7783 2.1774 -0.1348 -0.0994 0.2665 27 THR A N 189 C CA . THR A 27 ? 2.2799 1.8179 2.1877 -0.1415 -0.0933 0.2807 27 THR A CA 190 C C . THR A 27 ? 2.3980 1.9829 2.3197 -0.1335 -0.0860 0.2800 27 THR A C 191 O O . THR A 27 ? 2.3968 2.0036 2.3285 -0.1249 -0.0804 0.2900 27 THR A O 192 C CB . THR A 27 ? 2.4325 1.9741 2.3332 -0.1670 -0.0956 0.2868 27 THR A CB 193 O OG1 . THR A 27 ? 2.4279 2.0103 2.3386 -0.1717 -0.0898 0.3004 27 THR A OG1 194 C CG2 . THR A 27 ? 2.4115 1.9573 2.3066 -0.1790 -0.0981 0.2734 27 THR A CG2 195 N N . ASP A 28 ? 2.4371 2.0367 2.3590 -0.1354 -0.0859 0.2682 28 ASP A N 196 C CA . ASP A 28 ? 2.3198 1.9664 2.2533 -0.1321 -0.0791 0.2712 28 ASP A CA 197 C C . ASP A 28 ? 2.1668 1.8259 2.1090 -0.1118 -0.0747 0.2661 28 ASP A C 198 O O . ASP A 28 ? 2.1927 1.8851 2.1415 -0.1089 -0.0703 0.2642 28 ASP A O 199 C CB . ASP A 28 ? 2.3384 2.0049 2.2688 -0.1469 -0.0802 0.2640 28 ASP A CB 200 C CG . ASP A 28 ? 2.3377 1.9737 2.2572 -0.1508 -0.0868 0.2470 28 ASP A CG 201 O OD1 . ASP A 28 ? 2.3036 1.8964 2.2144 -0.1478 -0.0920 0.2435 28 ASP A OD1 202 O OD2 . ASP A 28 ? 2.3315 1.9868 2.2505 -0.1567 -0.0869 0.2371 28 ASP A OD2 203 N N . LYS A 29 ? 1.9364 1.5704 1.8781 -0.0982 -0.0758 0.2647 29 LYS A N 204 C CA . LYS A 29 ? 1.7950 1.4445 1.7462 -0.0805 -0.0705 0.2646 29 LYS A CA 205 C C . LYS A 29 ? 1.6913 1.3490 1.6488 -0.0782 -0.0660 0.2803 29 LYS A C 206 O O . LYS A 29 ? 1.4853 1.1378 1.4397 -0.0896 -0.0676 0.2897 29 LYS A O 207 C CB . LYS A 29 ? 1.8025 1.4261 1.7499 -0.0664 -0.0740 0.2521 29 LYS A CB 208 C CG . LYS A 29 ? 1.8597 1.4583 1.7959 -0.0721 -0.0813 0.2377 29 LYS A CG 209 C CD . LYS A 29 ? 1.8496 1.4449 1.7854 -0.0566 -0.0826 0.2217 29 LYS A CD 210 C CE . LYS A 29 ? 1.9217 1.4857 1.8447 -0.0607 -0.0905 0.2069 29 LYS A CE 211 N NZ . LYS A 29 ? 1.8665 1.4148 1.7867 -0.0424 -0.0935 0.1926 29 LYS A NZ 212 N N . VAL A 30 ? 1.7269 1.3990 1.6929 -0.0645 -0.0604 0.2831 30 VAL A N 213 C CA . VAL A 30 ? 1.6855 1.3694 1.6579 -0.0626 -0.0555 0.2972 30 VAL A CA 214 C C . VAL A 30 ? 1.7272 1.3947 1.7017 -0.0504 -0.0548 0.2993 30 VAL A C 215 O O . VAL A 30 ? 1.8750 1.5357 1.8503 -0.0388 -0.0548 0.2906 30 VAL A O 216 C CB . VAL A 30 ? 1.3782 1.0991 1.3590 -0.0596 -0.0482 0.3021 30 VAL A CB 217 C CG1 . VAL A 30 ? 1.3909 1.1188 1.3790 -0.0459 -0.0422 0.3057 30 VAL A CG1 218 C CG2 . VAL A 30 ? 1.3762 1.1170 1.3577 -0.0711 -0.0468 0.3130 30 VAL A CG2 219 N N . LEU A 31 ? 1.5172 1.1814 1.4926 -0.0533 -0.0540 0.3108 31 LEU A N 220 C CA . LEU A 31 ? 1.2431 0.9010 1.2189 -0.0414 -0.0508 0.3070 31 LEU A CA 221 C C . LEU A 31 ? 1.2807 0.9671 1.2633 -0.0344 -0.0417 0.3077 31 LEU A C 222 O O . LEU A 31 ? 1.4760 1.1791 1.4589 -0.0387 -0.0379 0.3110 31 LEU A O 223 C CB . LEU A 31 ? 1.1426 0.7863 1.1102 -0.0460 -0.0522 0.3063 31 LEU A CB 224 C CG . LEU A 31 ? 0.9957 0.6280 0.9603 -0.0342 -0.0505 0.3006 31 LEU A CG 225 C CD1 . LEU A 31 ? 0.9935 0.6058 0.9486 -0.0401 -0.0540 0.3012 31 LEU A CD1 226 C CD2 . LEU A 31 ? 0.8788 0.5346 0.8487 -0.0262 -0.0427 0.2995 31 LEU A CD2 227 N N . ASN A 32 ? 1.2325 0.9243 1.2203 -0.0239 -0.0387 0.3046 32 ASN A N 228 C CA . ASN A 32 ? 1.2772 0.9916 1.2692 -0.0186 -0.0306 0.3042 32 ASN A CA 229 C C . ASN A 32 ? 1.3263 1.0372 1.3159 -0.0127 -0.0281 0.2991 32 ASN A C 230 O O . ASN A 32 ? 1.3865 1.0788 1.3717 -0.0100 -0.0318 0.2958 32 ASN A O 231 C CB . ASN A 32 ? 1.3985 1.1240 1.3969 -0.0118 -0.0269 0.3040 32 ASN A CB 232 C CG . ASN A 32 ? 1.6512 1.3825 1.6526 -0.0165 -0.0294 0.3099 32 ASN A CG 233 O OD1 . ASN A 32 ? 1.7981 1.5419 1.7993 -0.0244 -0.0292 0.3159 32 ASN A OD1 234 N ND2 . ASN A 32 ? 1.6600 1.3887 1.6613 -0.0110 -0.0306 0.3004 32 ASN A ND2 235 N N . VAL A 33 ? 1.1834 0.9124 1.1756 -0.0105 -0.0220 0.2991 33 VAL A N 236 C CA . VAL A 33 ? 1.0707 0.8002 1.0614 -0.0065 -0.0197 0.2954 33 VAL A CA 237 C C . VAL A 33 ? 1.0702 0.8144 1.0655 -0.0011 -0.0136 0.2935 33 VAL A C 238 O O . VAL A 33 ? 0.9114 0.6698 0.9094 -0.0022 -0.0101 0.2965 33 VAL A O 239 C CB . VAL A 33 ? 1.1090 0.8431 1.0968 -0.0128 -0.0201 0.2987 33 VAL A CB 240 C CG1 . VAL A 33 ? 0.9975 0.7400 0.9864 -0.0084 -0.0164 0.2962 33 VAL A CG1 241 C CG2 . VAL A 33 ? 0.8433 0.5584 0.8247 -0.0189 -0.0262 0.3001 33 VAL A CG2 242 N N . THR A 34 ? 1.2926 1.0327 1.2885 0.0047 -0.0124 0.2890 34 THR A N 243 C CA . THR A 34 ? 1.2282 0.9796 1.2279 0.0084 -0.0067 0.2872 34 THR A CA 244 C C . THR A 34 ? 1.1316 0.8889 1.1304 0.0080 -0.0048 0.2867 34 THR A C 245 O O . THR A 34 ? 1.0560 0.8068 1.0523 0.0077 -0.0075 0.2858 34 THR A O 246 C CB . THR A 34 ? 1.1071 0.8535 1.1096 0.0141 -0.0060 0.2838 34 THR A CB 247 O OG1 . THR A 34 ? 1.0788 0.8169 1.0821 0.0154 -0.0097 0.2848 34 THR A OG1 248 C CG2 . THR A 34 ? 0.8465 0.6038 0.8527 0.0158 0.0004 0.2833 34 THR A CG2 249 N N . LEU A 35 ? 0.9047 0.6742 0.9053 0.0082 -0.0004 0.2881 35 LEU A N 250 C CA . LEU A 35 ? 0.9079 0.6837 0.9088 0.0088 0.0014 0.2882 35 LEU A CA 251 C C . LEU A 35 ? 0.9489 0.7299 0.9521 0.0126 0.0067 0.2864 35 LEU A C 252 O O . LEU A 35 ? 0.8437 0.6297 0.8472 0.0137 0.0100 0.2878 35 LEU A O 253 C CB . LEU A 35 ? 0.9898 0.7754 0.9902 0.0050 0.0006 0.2937 35 LEU A CB 254 C CG . LEU A 35 ? 0.7884 0.5814 0.7900 0.0061 0.0020 0.2947 35 LEU A CG 255 C CD1 . LEU A 35 ? 0.6604 0.4556 0.6606 0.0009 -0.0017 0.2989 35 LEU A CD1 256 C CD2 . LEU A 35 ? 0.6872 0.4927 0.6911 0.0092 0.0062 0.2975 35 LEU A CD2 257 N N . GLN A 36 ? 0.8361 0.6154 0.8403 0.0146 0.0074 0.2839 36 GLN A N 258 C CA . GLN A 36 ? 0.9563 0.7400 0.9623 0.0174 0.0123 0.2832 36 GLN A CA 259 C C . GLN A 36 ? 0.9540 0.7406 0.9617 0.0186 0.0126 0.2832 36 GLN A C 260 O O . GLN A 36 ? 0.7453 0.5289 0.7535 0.0183 0.0100 0.2822 36 GLN A O 261 C CB . GLN A 36 ? 0.9994 0.7785 1.0063 0.0188 0.0159 0.2805 36 GLN A CB 262 C CG . GLN A 36 ? 1.2357 1.0153 1.2437 0.0208 0.0207 0.2796 36 GLN A CG 263 C CD . GLN A 36 ? 1.2997 1.0749 1.3075 0.0206 0.0251 0.2785 36 GLN A CD 264 O OE1 . GLN A 36 ? 1.4621 1.2374 1.4681 0.0198 0.0259 0.2799 36 GLN A OE1 265 N NE2 . GLN A 36 ? 1.5592 1.3312 1.5696 0.0206 0.0275 0.2766 36 GLN A NE2 266 N N . ILE A 37 ? 0.9952 0.7883 1.0036 0.0206 0.0157 0.2854 37 ILE A N 267 C CA . ILE A 37 ? 1.2118 1.0094 1.2226 0.0228 0.0175 0.2863 37 ILE A CA 268 C C . ILE A 37 ? 1.3693 1.1611 1.3819 0.0250 0.0216 0.2831 37 ILE A C 269 O O . ILE A 37 ? 1.3636 1.1492 1.3748 0.0250 0.0245 0.2810 37 ILE A O 270 C CB . ILE A 37 ? 1.1218 0.9283 1.1328 0.0255 0.0195 0.2909 37 ILE A CB 271 C CG1 . ILE A 37 ? 1.0951 0.8966 1.1041 0.0288 0.0240 0.2899 37 ILE A CG1 272 C CG2 . ILE A 37 ? 0.9562 0.7705 0.9662 0.0226 0.0162 0.2954 37 ILE A CG2 273 C CD1 . ILE A 37 ? 1.0026 0.8116 1.0112 0.0331 0.0259 0.2949 37 ILE A CD1 274 N N . THR A 38 ? 1.6745 1.4689 1.6902 0.0260 0.0219 0.2833 38 THR A N 275 C CA . THR A 38 ? 1.7827 1.5730 1.8006 0.0277 0.0265 0.2816 38 THR A CA 276 C C . THR A 38 ? 1.7782 1.5745 1.7982 0.0310 0.0289 0.2848 38 THR A C 277 O O . THR A 38 ? 1.8375 1.6416 1.8607 0.0314 0.0270 0.2872 38 THR A O 278 C CB . THR A 38 ? 1.2315 1.0199 1.2527 0.0268 0.0257 0.2798 38 THR A CB 279 O OG1 . THR A 38 ? 1.4528 1.2484 1.4773 0.0280 0.0243 0.2823 38 THR A OG1 280 C CG2 . THR A 38 ? 1.0560 0.8412 1.0754 0.0251 0.0211 0.2784 38 THR A CG2 281 N N . LEU A 39 ? 1.5322 1.3249 1.5500 0.0339 0.0329 0.2856 39 LEU A N 282 C CA . LEU A 39 ? 1.2099 1.0070 1.2294 0.0387 0.0356 0.2892 39 LEU A CA 283 C C . LEU A 39 ? 1.0874 0.8823 1.1109 0.0392 0.0387 0.2884 39 LEU A C 284 O O . LEU A 39 ? 1.0469 0.8315 1.0699 0.0373 0.0422 0.2852 39 LEU A O 285 C CB . LEU A 39 ? 1.0463 0.8362 1.0615 0.0430 0.0394 0.2902 39 LEU A CB 286 C CG . LEU A 39 ? 1.0946 0.8848 1.1103 0.0503 0.0433 0.2939 39 LEU A CG 287 C CD1 . LEU A 39 ? 1.0408 0.8484 1.0593 0.0540 0.0406 0.2999 39 LEU A CD1 288 C CD2 . LEU A 39 ? 1.0801 0.8558 1.0897 0.0546 0.0478 0.2937 39 LEU A CD2 289 N N . SER A 40 ? 1.1127 0.9188 1.1406 0.0416 0.0380 0.2923 40 SER A N 290 C CA . SER A 40 ? 1.1255 0.9331 1.1582 0.0427 0.0409 0.2932 40 SER A CA 291 C C . SER A 40 ? 1.3251 1.1328 1.3588 0.0492 0.0460 0.2968 40 SER A C 292 O O . SER A 40 ? 1.2943 1.0926 1.3287 0.0505 0.0516 0.2958 40 SER A O 293 C CB . SER A 40 ? 0.9686 0.7898 1.0055 0.0408 0.0362 0.2961 40 SER A CB 294 O OG . SER A 40 ? 1.1315 0.9496 1.1669 0.0363 0.0318 0.2929 40 SER A OG 295 N N . GLN A 41 ? 1.3291 1.1471 1.3626 0.0536 0.0445 0.3014 41 GLN A N 296 C CA . GLN A 41 ? 1.2097 1.0288 1.2440 0.0619 0.0493 0.3057 41 GLN A CA 297 C C . GLN A 41 ? 0.8800 0.7083 0.9125 0.0680 0.0483 0.3106 41 GLN A C 298 O O . GLN A 41 ? 0.6775 0.5224 0.7119 0.0653 0.0433 0.3142 41 GLN A O 299 C CB . GLN A 41 ? 1.5157 1.3487 1.5567 0.0634 0.0498 0.3102 41 GLN A CB 300 C CG . GLN A 41 ? 2.2084 2.0560 2.2518 0.0726 0.0518 0.3179 41 GLN A CG 301 C CD . GLN A 41 ? 2.1709 2.0039 2.2116 0.0825 0.0595 0.3181 41 GLN A CD 302 O OE1 . GLN A 41 ? 2.2090 2.0195 2.2440 0.0826 0.0629 0.3127 41 GLN A OE1 303 N NE2 . GLN A 41 ? 2.0199 1.8653 2.0637 0.0913 0.0623 0.3246 41 GLN A NE2 304 N N . ILE A 42 ? 0.7674 0.5851 0.7963 0.0767 0.0534 0.3115 42 ILE A N 305 C CA . ILE A 42 ? 1.0010 0.8286 1.0286 0.0871 0.0543 0.3178 42 ILE A CA 306 C C . ILE A 42 ? 1.1060 0.9515 1.1389 0.0944 0.0557 0.3247 42 ILE A C 307 O O . ILE A 42 ? 1.2086 1.0451 1.2404 0.1035 0.0614 0.3254 42 ILE A O 308 C CB . ILE A 42 ? 1.1215 0.9278 1.1416 0.0956 0.0595 0.3160 42 ILE A CB 309 C CG1 . ILE A 42 ? 1.1408 0.9332 1.1554 0.0888 0.0578 0.3110 42 ILE A CG1 310 C CG2 . ILE A 42 ? 1.2716 1.0895 1.2900 0.1089 0.0604 0.3230 42 ILE A CG2 311 C CD1 . ILE A 42 ? 1.2014 0.9724 1.2072 0.0963 0.0621 0.3100 42 ILE A CD1 312 N N . LYS A 43 ? 1.0036 0.8742 1.0413 0.0906 0.0507 0.3302 43 LYS A N 313 C CA . LYS A 43 ? 0.8460 0.7388 0.8891 0.0951 0.0510 0.3376 43 LYS A CA 314 C C . LYS A 43 ? 0.8602 0.7617 0.9015 0.1111 0.0550 0.3439 43 LYS A C 315 O O . LYS A 43 ? 0.7230 0.6356 0.7669 0.1186 0.0576 0.3481 43 LYS A O 316 C CB . LYS A 43 ? 0.6633 0.5809 0.7103 0.0861 0.0443 0.3426 43 LYS A CB 317 C CG . LYS A 43 ? 0.8187 0.7640 0.8703 0.0902 0.0438 0.3517 43 LYS A CG 318 C CD . LYS A 43 ? 1.0021 0.9436 1.0569 0.0898 0.0462 0.3505 43 LYS A CD 319 C CE . LYS A 43 ? 1.1775 1.1476 1.2353 0.0962 0.0467 0.3549 43 LYS A CE 320 N NZ . LYS A 43 ? 1.1793 1.1537 1.2407 0.0904 0.0464 0.3495 43 LYS A NZ 321 N N . ASP A 44 ? 0.9474 0.8459 0.9839 0.1172 0.0553 0.3445 44 ASP A N 322 C CA . ASP A 44 ? 0.9599 0.8674 0.9932 0.1346 0.0586 0.3502 44 ASP A CA 323 C C . ASP A 44 ? 0.9021 0.8023 0.9297 0.1381 0.0581 0.3493 44 ASP A C 324 O O . ASP A 44 ? 0.8862 0.8006 0.9154 0.1296 0.0534 0.3515 44 ASP A O 325 C CB . ASP A 44 ? 1.0748 1.0218 1.1131 0.1381 0.0555 0.3603 44 ASP A CB 326 C CG . ASP A 44 ? 1.3177 1.2811 1.3522 0.1564 0.0577 0.3604 44 ASP A CG 327 O OD1 . ASP A 44 ? 1.5368 1.4771 1.5647 0.1691 0.0625 0.3544 44 ASP A OD1 328 O OD2 . ASP A 44 ? 1.3933 1.3937 1.4307 0.1576 0.0543 0.3657 44 ASP A OD2 329 N N . MET A 45 ? 0.6844 0.5627 0.7046 0.1508 0.0630 0.3465 45 MET A N 330 C CA . MET A 45 ? 0.7179 0.5950 0.7324 0.1572 0.0626 0.3478 45 MET A CA 331 C C . MET A 45 ? 0.9596 0.8612 0.9729 0.1757 0.0636 0.3556 45 MET A C 332 O O . MET A 45 ? 1.1000 0.9878 1.1067 0.1929 0.0682 0.3543 45 MET A O 333 C CB . MET A 45 ? 0.9528 0.7923 0.9583 0.1598 0.0664 0.3406 45 MET A CB 334 C CG . MET A 45 ? 1.1041 0.9430 1.1035 0.1646 0.0652 0.3426 45 MET A CG 335 S SD . MET A 45 ? 1.1021 0.9611 1.1075 0.1468 0.0587 0.3440 45 MET A SD 336 C CE . MET A 45 ? 0.8456 0.7357 0.8503 0.1594 0.0573 0.3540 45 MET A CE 337 N N . ASP A 46 ? 1.0413 0.9797 1.0602 0.1723 0.0591 0.3633 46 ASP A N 338 C CA . ASP A 46 ? 0.9991 0.9703 1.0170 0.1890 0.0589 0.3715 46 ASP A CA 339 C C . ASP A 46 ? 0.9280 0.8899 0.9379 0.2021 0.0607 0.3710 46 ASP A C 340 O O . ASP A 46 ? 0.8391 0.8128 0.8493 0.1965 0.0579 0.3740 46 ASP A O 341 C CB . ASP A 46 ? 0.9630 0.9748 0.9880 0.1775 0.0532 0.3795 46 ASP A CB 342 C CG . ASP A 46 ? 0.8915 0.9453 0.9168 0.1919 0.0523 0.3872 46 ASP A CG 343 O OD1 . ASP A 46 ? 0.9262 0.9807 0.9454 0.2122 0.0552 0.3844 46 ASP A OD1 344 O OD2 . ASP A 46 ? 0.7112 0.7979 0.7427 0.1803 0.0481 0.3906 46 ASP A OD2 345 N N . GLU A 47 ? 0.9174 0.8574 0.9194 0.2202 0.0655 0.3671 47 GLU A N 346 C CA . GLU A 47 ? 0.8835 0.8087 0.8761 0.2331 0.0674 0.3658 47 GLU A CA 347 C C . GLU A 47 ? 1.1615 1.1275 1.1540 0.2461 0.0651 0.3737 47 GLU A C 348 O O . GLU A 47 ? 1.2565 1.2238 1.2457 0.2466 0.0642 0.3755 47 GLU A O 349 C CB . GLU A 47 ? 1.0598 0.9505 1.0426 0.2502 0.0729 0.3593 47 GLU A CB 350 C CG . GLU A 47 ? 1.2357 1.0801 1.2147 0.2376 0.0757 0.3509 47 GLU A CG 351 C CD . GLU A 47 ? 1.4394 1.2461 1.4052 0.2532 0.0805 0.3451 47 GLU A CD 352 O OE1 . GLU A 47 ? 1.6105 1.4146 1.5720 0.2719 0.0836 0.3433 47 GLU A OE1 353 O OE2 . GLU A 47 ? 1.4608 1.2404 1.4200 0.2469 0.0808 0.3421 47 GLU A OE2 354 N N . ARG A 48 ? 1.2009 1.2027 1.1968 0.2572 0.0640 0.3784 48 ARG A N 355 C CA . ARG A 48 ? 1.1642 1.2040 1.1573 0.2752 0.0626 0.3838 48 ARG A CA 356 C C . ARG A 48 ? 0.9990 1.0837 0.9995 0.2616 0.0574 0.3925 48 ARG A C 357 O O . ARG A 48 ? 1.1357 1.2530 1.1341 0.2730 0.0561 0.3970 48 ARG A O 358 C CB . ARG A 48 ? 1.3600 1.4215 1.3522 0.2937 0.0635 0.3786 48 ARG A CB 359 C CG . ARG A 48 ? 1.3073 1.4299 1.3079 0.2888 0.0590 0.3810 48 ARG A CG 360 C CD . ARG A 48 ? 1.3020 1.4533 1.2990 0.3129 0.0598 0.3743 48 ARG A CD 361 N NE . ARG A 48 ? 1.3812 1.5955 1.3837 0.3118 0.0555 0.3803 48 ARG A NE 362 C CZ . ARG A 48 ? 1.2888 1.5423 1.2887 0.3327 0.0551 0.3774 48 ARG A CZ 363 N NH1 . ARG A 48 ? 1.4045 1.6392 1.3959 0.3585 0.0587 0.3680 48 ARG A NH1 364 N NH2 . ARG A 48 ? 1.0428 1.3550 1.0481 0.3276 0.0511 0.3837 48 ARG A NH2 365 N N . ASN A 49 ? 0.8284 0.9124 0.8366 0.2369 0.0546 0.3940 49 ASN A N 366 C CA . ASN A 49 ? 0.9208 1.0321 0.9341 0.2205 0.0502 0.4002 49 ASN A CA 367 C C . ASN A 49 ? 1.1814 1.2613 1.1941 0.2054 0.0500 0.3963 49 ASN A C 368 O O . ASN A 49 ? 1.3326 1.4307 1.3487 0.1924 0.0465 0.4004 49 ASN A O 369 C CB . ASN A 49 ? 0.9575 1.0955 0.9790 0.2030 0.0461 0.4048 49 ASN A CB 370 C CG . ASN A 49 ? 1.0014 1.1837 1.0242 0.2146 0.0449 0.4082 49 ASN A CG 371 O OD1 . ASN A 49 ? 0.9684 1.1532 0.9866 0.2363 0.0479 0.4023 49 ASN A OD1 372 N ND2 . ASN A 49 ? 0.7738 0.9914 0.8029 0.1974 0.0405 0.4126 49 ASN A ND2 373 N N . GLN A 50 ? 1.2143 1.2487 1.2224 0.2069 0.0534 0.3880 50 GLN A N 374 C CA . GLN A 50 ? 1.0331 1.0356 1.0403 0.1918 0.0531 0.3822 50 GLN A CA 375 C C . GLN A 50 ? 1.0582 1.0651 1.0731 0.1682 0.0488 0.3815 50 GLN A C 376 O O . GLN A 50 ? 1.1151 1.1226 1.1309 0.1569 0.0462 0.3815 50 GLN A O 377 C CB . GLN A 50 ? 0.9682 0.9744 0.9706 0.1971 0.0530 0.3848 50 GLN A CB 378 C CG . GLN A 50 ? 1.1892 1.1576 1.1821 0.2074 0.0570 0.3790 50 GLN A CG 379 C CD . GLN A 50 ? 1.3948 1.3586 1.3811 0.2302 0.0607 0.3786 50 GLN A CD 380 O OE1 . GLN A 50 ? 1.5822 1.5798 1.5701 0.2427 0.0602 0.3840 50 GLN A OE1 381 N NE2 . GLN A 50 ? 1.5245 1.4476 1.5026 0.2360 0.0643 0.3720 50 GLN A NE2 382 N N . ILE A 51 ? 0.9681 0.9773 0.9879 0.1617 0.0480 0.3806 51 ILE A N 383 C CA . ILE A 51 ? 0.9582 0.9673 0.9839 0.1407 0.0439 0.3788 51 ILE A CA 384 C C . ILE A 51 ? 1.1143 1.0879 1.1394 0.1355 0.0459 0.3691 51 ILE A C 385 O O . ILE A 51 ? 1.2536 1.2162 1.2769 0.1463 0.0497 0.3672 51 ILE A O 386 C CB . ILE A 51 ? 0.8294 0.8738 0.8612 0.1352 0.0406 0.3863 51 ILE A CB 387 C CG1 . ILE A 51 ? 0.8599 0.9421 0.8925 0.1347 0.0377 0.3954 51 ILE A CG1 388 C CG2 . ILE A 51 ? 0.9696 1.0050 1.0058 0.1149 0.0368 0.3825 51 ILE A CG2 389 C CD1 . ILE A 51 ? 0.9552 1.0326 0.9886 0.1186 0.0341 0.3944 51 ILE A CD1 390 N N . LEU A 52 ? 0.9857 0.9415 1.0116 0.1201 0.0434 0.3627 52 LEU A N 391 C CA . LEU A 52 ? 0.8918 0.8207 0.9176 0.1135 0.0445 0.3539 52 LEU A CA 392 C C . LEU A 52 ? 0.9774 0.9166 1.0091 0.0995 0.0402 0.3538 52 LEU A C 393 O O . LEU A 52 ? 1.1535 1.1022 1.1868 0.0885 0.0357 0.3551 52 LEU A O 394 C CB . LEU A 52 ? 0.8736 0.7750 0.8946 0.1079 0.0449 0.3457 52 LEU A CB 395 C CG . LEU A 52 ? 0.9212 0.8017 0.9430 0.0977 0.0446 0.3370 52 LEU A CG 396 C CD1 . LEU A 52 ? 0.9277 0.7851 0.9455 0.1056 0.0501 0.3327 52 LEU A CD1 397 C CD2 . LEU A 52 ? 0.9671 0.8361 0.9868 0.0860 0.0416 0.3309 52 LEU A CD2 398 N N . THR A 53 ? 0.8642 0.8000 0.8986 0.1001 0.0417 0.3523 53 THR A N 399 C CA . THR A 53 ? 0.7150 0.6563 0.7538 0.0875 0.0378 0.3514 53 THR A CA 400 C C . THR A 53 ? 0.9256 0.8385 0.9628 0.0814 0.0387 0.3411 53 THR A C 401 O O . THR A 53 ? 1.0967 0.9919 1.1316 0.0883 0.0434 0.3371 53 THR A O 402 C CB . THR A 53 ? 0.6765 0.6390 0.7197 0.0916 0.0383 0.3581 53 THR A CB 403 O OG1 . THR A 53 ? 0.7246 0.7161 0.7681 0.1003 0.0383 0.3678 53 THR A OG1 404 C CG2 . THR A 53 ? 0.6655 0.6356 0.7124 0.0773 0.0332 0.3582 53 THR A CG2 405 N N . ALA A 54 ? 0.7684 0.6763 0.8059 0.0690 0.0342 0.3368 54 ALA A N 406 C CA . ALA A 54 ? 0.6077 0.4925 0.6432 0.0640 0.0348 0.3275 54 ALA A CA 407 C C . ALA A 54 ? 0.8529 0.7392 0.8902 0.0538 0.0301 0.3254 54 ALA A C 408 O O . ALA A 54 ? 0.9378 0.8352 0.9754 0.0473 0.0254 0.3287 54 ALA A O 409 C CB . ALA A 54 ? 0.9288 0.7974 0.9587 0.0628 0.0351 0.3222 54 ALA A CB 410 N N . TYR A 55 ? 0.7949 0.6691 0.8329 0.0525 0.0315 0.3200 55 TYR A N 411 C CA . TYR A 55 ? 0.9633 0.8358 1.0019 0.0447 0.0274 0.3174 55 TYR A CA 412 C C . TYR A 55 ? 0.8641 0.7190 0.8983 0.0407 0.0264 0.3098 55 TYR A C 413 O O . TYR A 55 ? 0.7552 0.5972 0.7874 0.0436 0.0303 0.3055 55 TYR A O 414 C CB . TYR A 55 ? 1.2803 1.1541 1.3233 0.0464 0.0296 0.3176 55 TYR A CB 415 C CG . TYR A 55 ? 1.1602 1.0540 1.2080 0.0502 0.0305 0.3258 55 TYR A CG 416 C CD1 . TYR A 55 ? 1.2919 1.2050 1.3408 0.0471 0.0263 0.3328 55 TYR A CD1 417 C CD2 . TYR A 55 ? 1.1307 1.0249 1.1818 0.0568 0.0358 0.3272 55 TYR A CD2 418 C CE1 . TYR A 55 ? 1.3743 1.3091 1.4276 0.0504 0.0270 0.3412 55 TYR A CE1 419 C CE2 . TYR A 55 ? 1.2993 1.2138 1.3547 0.0612 0.0368 0.3353 55 TYR A CE2 420 C CZ . TYR A 55 ? 1.3687 1.3050 1.4252 0.0581 0.0322 0.3424 55 TYR A CZ 421 O OH . TYR A 55 ? 1.2969 1.2574 1.3573 0.0624 0.0330 0.3512 55 TYR A OH 422 N N . LEU A 56 ? 0.7316 0.5857 0.7635 0.0342 0.0212 0.3088 56 LEU A N 423 C CA . LEU A 56 ? 0.8806 0.7195 0.9083 0.0312 0.0201 0.3022 56 LEU A CA 424 C C . LEU A 56 ? 1.0126 0.8470 1.0386 0.0262 0.0152 0.3004 56 LEU A C 425 O O . LEU A 56 ? 0.8286 0.6705 0.8548 0.0231 0.0115 0.3046 56 LEU A O 426 C CB . LEU A 56 ? 0.7328 0.5701 0.7567 0.0302 0.0193 0.3023 56 LEU A CB 427 C CG . LEU A 56 ? 0.7818 0.6238 0.8055 0.0353 0.0226 0.3054 56 LEU A CG 428 C CD1 . LEU A 56 ? 0.8224 0.6642 0.8427 0.0321 0.0203 0.3060 56 LEU A CD1 429 C CD2 . LEU A 56 ? 0.7184 0.5493 0.7411 0.0405 0.0279 0.3020 56 LEU A CD2 430 N N . TRP A 57 ? 0.9879 0.8095 1.0115 0.0257 0.0153 0.2947 57 TRP A N 431 C CA . TRP A 57 ? 1.0553 0.8687 1.0757 0.0227 0.0109 0.2923 57 TRP A CA 432 C C . TRP A 57 ? 0.8315 0.6376 0.8474 0.0204 0.0095 0.2902 57 TRP A C 433 O O . TRP A 57 ? 0.6032 0.4067 0.6190 0.0220 0.0129 0.2881 57 TRP A O 434 C CB . TRP A 57 ? 0.8908 0.6980 0.9134 0.0249 0.0123 0.2888 57 TRP A CB 435 C CG . TRP A 57 ? 0.7538 0.5682 0.7806 0.0267 0.0129 0.2915 57 TRP A CG 436 C CD1 . TRP A 57 ? 0.8277 0.6479 0.8595 0.0295 0.0179 0.2927 57 TRP A CD1 437 C CD2 . TRP A 57 ? 0.7965 0.6133 0.8228 0.0260 0.0084 0.2944 57 TRP A CD2 438 N NE1 . TRP A 57 ? 1.1071 0.9356 1.1426 0.0306 0.0168 0.2964 57 TRP A NE1 439 C CE2 . TRP A 57 ? 0.9692 0.7961 1.0012 0.0285 0.0108 0.2976 57 TRP A CE2 440 C CE3 . TRP A 57 ? 0.7881 0.5982 0.8089 0.0236 0.0026 0.2950 57 TRP A CE3 441 C CZ2 . TRP A 57 ? 0.9633 0.7957 0.9960 0.0288 0.0075 0.3016 57 TRP A CZ2 442 C CZ3 . TRP A 57 ? 0.9222 0.7349 0.9426 0.0240 -0.0007 0.2987 57 TRP A CZ3 443 C CH2 . TRP A 57 ? 1.0021 0.8270 1.0286 0.0266 0.0016 0.3021 57 TRP A CH2 444 N N . ILE A 58 ? 0.6098 0.4119 0.6218 0.0167 0.0047 0.2914 58 ILE A N 445 C CA . ILE A 58 ? 1.0597 0.8571 1.0681 0.0139 0.0032 0.2911 58 ILE A CA 446 C C . ILE A 58 ? 1.1915 0.9756 1.1961 0.0131 -0.0004 0.2883 58 ILE A C 447 O O . ILE A 58 ? 1.1291 0.9077 1.1305 0.0113 -0.0045 0.2898 58 ILE A O 448 C CB . ILE A 58 ? 1.0043 0.8099 1.0115 0.0094 0.0010 0.2970 58 ILE A CB 449 C CG1 . ILE A 58 ? 1.0869 0.9072 1.0983 0.0120 0.0048 0.3006 58 ILE A CG1 450 C CG2 . ILE A 58 ? 0.9662 0.7658 0.9697 0.0056 -0.0013 0.2973 58 ILE A CG2 451 C CD1 . ILE A 58 ? 1.0988 0.9320 1.1106 0.0080 0.0031 0.3080 58 ILE A CD1 452 N N . ARG A 59 ? 1.3670 1.1458 1.3719 0.0151 0.0013 0.2847 59 ARG A N 453 C CA . ARG A 59 ? 1.1759 0.9430 1.1784 0.0158 -0.0016 0.2824 59 ARG A CA 454 C C . ARG A 59 ? 0.9736 0.7358 0.9725 0.0122 -0.0043 0.2838 59 ARG A C 455 O O . ARG A 59 ? 0.9702 0.7376 0.9701 0.0111 -0.0019 0.2846 59 ARG A O 456 C CB . ARG A 59 ? 1.0722 0.8386 1.0783 0.0193 0.0019 0.2791 59 ARG A CB 457 C CG . ARG A 59 ? 0.8374 0.5990 0.8453 0.0230 0.0005 0.2777 59 ARG A CG 458 C CD . ARG A 59 ? 1.0280 0.7889 1.0397 0.0256 0.0033 0.2759 59 ARG A CD 459 N NE . ARG A 59 ? 1.3089 1.0686 1.3236 0.0300 0.0021 0.2760 59 ARG A NE 460 C CZ . ARG A 59 ? 1.3057 1.0571 1.3178 0.0332 -0.0034 0.2764 59 ARG A CZ 461 N NH1 . ARG A 59 ? 1.3158 1.0579 1.3220 0.0314 -0.0077 0.2764 59 ARG A NH1 462 N NH2 . ARG A 59 ? 1.0894 0.8412 1.1044 0.0387 -0.0046 0.2773 59 ARG A NH2 463 N N . GLN A 60 ? 0.7218 0.4728 0.7159 0.0106 -0.0092 0.2847 60 GLN A N 464 C CA . GLN A 60 ? 0.8906 0.6338 0.8812 0.0067 -0.0122 0.2863 60 GLN A CA 465 C C . GLN A 60 ? 1.0914 0.8176 1.0785 0.0098 -0.0164 0.2843 60 GLN A C 466 O O . GLN A 60 ? 1.1573 0.8741 1.1405 0.0113 -0.0196 0.2843 60 GLN A O 467 C CB . GLN A 60 ? 0.9045 0.6489 0.8916 -0.0001 -0.0146 0.2913 60 GLN A CB 468 C CG . GLN A 60 ? 0.9152 0.6781 0.9060 -0.0029 -0.0115 0.2952 60 GLN A CG 469 C CD . GLN A 60 ? 1.1037 0.8680 1.0916 -0.0096 -0.0144 0.3008 60 GLN A CD 470 O OE1 . GLN A 60 ? 1.1180 0.8741 1.1019 -0.0157 -0.0177 0.3036 60 GLN A OE1 471 N NE2 . GLN A 60 ? 1.2847 1.0583 1.2746 -0.0091 -0.0135 0.3028 60 GLN A NE2 472 N N . ILE A 61 ? 1.1296 0.8514 1.1178 0.0107 -0.0169 0.2834 61 ILE A N 473 C CA . ILE A 61 ? 1.0343 0.7402 1.0204 0.0155 -0.0212 0.2816 61 ILE A CA 474 C C . ILE A 61 ? 0.9630 0.6583 0.9464 0.0117 -0.0248 0.2835 61 ILE A C 475 O O . ILE A 61 ? 0.8540 0.5590 0.8404 0.0075 -0.0226 0.2856 61 ILE A O 476 C CB . ILE A 61 ? 0.9651 0.6762 0.9576 0.0222 -0.0187 0.2790 61 ILE A CB 477 C CG1 . ILE A 61 ? 0.8991 0.6254 0.8965 0.0229 -0.0130 0.2780 61 ILE A CG1 478 C CG2 . ILE A 61 ? 0.6821 0.3805 0.6735 0.0296 -0.0230 0.2775 61 ILE A CG2 479 C CD1 . ILE A 61 ? 0.6484 0.3805 0.6523 0.0275 -0.0095 0.2768 61 ILE A CD1 480 N N . TRP A 62 ? 0.8804 0.5555 0.8578 0.0131 -0.0304 0.2833 62 TRP A N 481 C CA . TRP A 62 ? 0.8582 0.5204 0.8328 0.0085 -0.0346 0.2852 62 TRP A CA 482 C C . TRP A 62 ? 1.2029 0.8390 1.1713 0.0137 -0.0412 0.2834 62 TRP A C 483 O O . TRP A 62 ? 1.3749 1.0030 1.3392 0.0199 -0.0424 0.2818 62 TRP A O 484 C CB . TRP A 62 ? 0.9299 0.5957 0.9015 -0.0028 -0.0345 0.2898 62 TRP A CB 485 C CG . TRP A 62 ? 0.9122 0.5665 0.8762 -0.0061 -0.0368 0.2914 62 TRP A CG 486 C CD1 . TRP A 62 ? 0.9715 0.6030 0.9278 -0.0104 -0.0420 0.2930 62 TRP A CD1 487 C CD2 . TRP A 62 ? 1.0492 0.7144 1.0127 -0.0065 -0.0339 0.2925 62 TRP A CD2 488 N NE1 . TRP A 62 ? 1.1420 0.7698 1.0926 -0.0131 -0.0421 0.2955 62 TRP A NE1 489 C CE2 . TRP A 62 ? 1.1844 0.8337 1.1398 -0.0107 -0.0374 0.2953 62 TRP A CE2 490 C CE3 . TRP A 62 ? 1.0278 0.7136 0.9971 -0.0036 -0.0290 0.2915 62 TRP A CE3 491 C CZ2 . TRP A 62 ? 1.1448 0.8007 1.0982 -0.0121 -0.0361 0.2979 62 TRP A CZ2 492 C CZ3 . TRP A 62 ? 1.0945 0.7860 1.0624 -0.0048 -0.0282 0.2934 62 TRP A CZ3 493 C CH2 . TRP A 62 ? 1.1386 0.8163 1.0988 -0.0090 -0.0318 0.2968 62 TRP A CH2 494 N N . HIS A 63 ? 1.3368 0.9589 1.3043 0.0114 -0.0460 0.2838 63 HIS A N 495 C CA . HIS A 63 ? 1.3929 0.9869 1.3542 0.0178 -0.0533 0.2812 63 HIS A CA 496 C C . HIS A 63 ? 1.2832 0.8563 1.2348 0.0083 -0.0574 0.2834 63 HIS A C 497 O O . HIS A 63 ? 1.4238 1.0015 1.3759 -0.0040 -0.0574 0.2869 63 HIS A O 498 C CB . HIS A 63 ? 1.4809 1.0688 1.4478 0.0235 -0.0580 0.2789 63 HIS A CB 499 C CG . HIS A 63 ? 1.4142 1.0191 1.3909 0.0343 -0.0548 0.2772 63 HIS A CG 500 N ND1 . HIS A 63 ? 1.4384 1.0700 1.4243 0.0314 -0.0477 0.2797 63 HIS A ND1 501 C CD2 . HIS A 63 ? 1.2802 0.8799 1.2595 0.0481 -0.0576 0.2740 63 HIS A CD2 502 C CE1 . HIS A 63 ? 1.4235 1.0652 1.4168 0.0413 -0.0456 0.2781 63 HIS A CE1 503 N NE2 . HIS A 63 ? 1.3519 0.9786 1.3402 0.0517 -0.0508 0.2716 63 HIS A NE2 504 N N . ASP A 64 ? 1.3299 0.8808 1.2729 0.0141 -0.0609 0.2818 64 ASP A N 505 C CA . ASP A 64 ? 1.3043 0.8315 1.2374 0.0058 -0.0649 0.2839 64 ASP A CA 506 C C . ASP A 64 ? 1.4530 0.9478 1.3797 0.0141 -0.0731 0.2788 64 ASP A C 507 O O . ASP A 64 ? 1.6326 1.1164 1.5561 0.0280 -0.0747 0.2760 64 ASP A O 508 C CB . ASP A 64 ? 1.3674 0.8961 1.2950 0.0056 -0.0614 0.2873 64 ASP A CB 509 C CG . ASP A 64 ? 1.4885 0.9954 1.4065 -0.0051 -0.0646 0.2911 64 ASP A CG 510 O OD1 . ASP A 64 ? 1.4934 0.9703 1.4046 -0.0032 -0.0709 0.2886 64 ASP A OD1 511 O OD2 . ASP A 64 ? 1.6015 1.1211 1.5189 -0.0153 -0.0612 0.2966 64 ASP A OD2 512 N N . ALA A 65 ? 1.4411 0.9203 1.3653 0.0060 -0.0792 0.2771 65 ALA A N 513 C CA . ALA A 65 ? 1.4954 0.9429 1.4128 0.0146 -0.0887 0.2696 65 ALA A CA 514 C C . ALA A 65 ? 1.5093 0.9249 1.4141 0.0186 -0.0923 0.2679 65 ALA A C 515 O O . ALA A 65 ? 1.6554 1.0435 1.5528 0.0304 -0.0998 0.2603 65 ALA A O 516 C CB . ALA A 65 ? 1.5883 1.0243 1.5031 0.0026 -0.0952 0.2676 65 ALA A CB 517 N N . TYR A 66 ? 1.5111 0.9302 1.4129 0.0094 -0.0874 0.2748 66 TYR A N 518 C CA . TYR A 66 ? 1.6500 1.0401 1.5406 0.0114 -0.0902 0.2755 66 TYR A CA 519 C C . TYR A 66 ? 1.5052 0.9012 1.3963 0.0272 -0.0864 0.2777 66 TYR A C 520 O O . TYR A 66 ? 1.4513 0.8227 1.3340 0.0337 -0.0893 0.2781 66 TYR A O 521 C CB . TYR A 66 ? 1.7075 1.0943 1.5930 -0.0092 -0.0889 0.2825 66 TYR A CB 522 C CG . TYR A 66 ? 1.6822 1.0566 1.5639 -0.0253 -0.0945 0.2801 66 TYR A CG 523 C CD1 . TYR A 66 ? 1.7005 1.1017 1.5915 -0.0335 -0.0925 0.2813 66 TYR A CD1 524 C CD2 . TYR A 66 ? 1.6881 1.0234 1.5564 -0.0325 -0.1020 0.2767 66 TYR A CD2 525 C CE1 . TYR A 66 ? 1.7090 1.1005 1.5961 -0.0489 -0.0979 0.2800 66 TYR A CE1 526 C CE2 . TYR A 66 ? 1.7625 1.0855 1.6255 -0.0487 -0.1076 0.2738 66 TYR A CE2 527 C CZ . TYR A 66 ? 1.7980 1.1502 1.6707 -0.0571 -0.1056 0.2758 66 TYR A CZ 528 O OH . TYR A 66 ? 1.8108 1.1526 1.6779 -0.0740 -0.1114 0.2738 66 TYR A OH 529 N N . LEU A 67 ? 1.4519 0.8800 1.3522 0.0329 -0.0801 0.2792 67 LEU A N 530 C CA . LEU A 67 ? 1.4504 0.8864 1.3506 0.0468 -0.0769 0.2810 67 LEU A CA 531 C C . LEU A 67 ? 1.6376 1.0766 1.5425 0.0661 -0.0798 0.2748 67 LEU A C 532 O O . LEU A 67 ? 1.6234 1.0851 1.5334 0.0738 -0.0759 0.2755 67 LEU A O 533 C CB . LEU A 67 ? 1.3257 0.7931 1.2303 0.0401 -0.0693 0.2858 67 LEU A CB 534 C CG . LEU A 67 ? 1.3902 0.8579 1.2913 0.0217 -0.0673 0.2918 67 LEU A CG 535 C CD1 . LEU A 67 ? 1.4307 0.9298 1.3367 0.0160 -0.0611 0.2952 67 LEU A CD1 536 C CD2 . LEU A 67 ? 1.3333 0.7738 1.2239 0.0207 -0.0700 0.2961 67 LEU A CD2 537 N N . THR A 68 ? 1.7349 1.1507 1.6370 0.0738 -0.0878 0.2678 68 THR A N 538 C CA . THR A 68 ? 1.7334 1.1506 1.6390 0.0935 -0.0926 0.2607 68 THR A CA 539 C C . THR A 68 ? 1.7502 1.1442 1.6479 0.1101 -0.0979 0.2580 68 THR A C 540 O O . THR A 68 ? 1.8234 1.1871 1.7109 0.1071 -0.1019 0.2574 68 THR A O 541 C CB . THR A 68 ? 1.6532 1.0623 1.5594 0.0948 -0.0996 0.2519 68 THR A CB 542 O OG1 . THR A 68 ? 1.7350 1.1076 1.6286 0.0908 -0.1065 0.2470 68 THR A OG1 543 C CG2 . THR A 68 ? 1.5577 0.9928 1.4742 0.0798 -0.0945 0.2558 68 THR A CG2 544 N N . TRP A 69 ? 1.7277 1.1363 1.6303 0.1277 -0.0986 0.2561 69 TRP A N 545 C CA . TRP A 69 ? 1.7717 1.1628 1.6681 0.1467 -0.1047 0.2523 69 TRP A CA 546 C C . TRP A 69 ? 1.7668 1.1722 1.6666 0.1672 -0.1094 0.2434 69 TRP A C 547 O O . TRP A 69 ? 1.6950 1.1301 1.6046 0.1669 -0.1058 0.2449 69 TRP A O 548 C CB . TRP A 69 ? 1.8049 1.2009 1.7015 0.1472 -0.0998 0.2630 69 TRP A CB 549 C CG . TRP A 69 ? 1.7932 1.2227 1.6992 0.1552 -0.0954 0.2669 69 TRP A CG 550 C CD1 . TRP A 69 ? 1.7825 1.2218 1.6922 0.1751 -0.0999 0.2643 69 TRP A CD1 551 C CD2 . TRP A 69 ? 1.7121 1.1684 1.6220 0.1436 -0.0868 0.2719 69 TRP A CD2 552 N NE1 . TRP A 69 ? 1.6818 1.1529 1.5999 0.1754 -0.0943 0.2692 69 TRP A NE1 553 C CE2 . TRP A 69 ? 1.6642 1.1430 1.5789 0.1566 -0.0862 0.2727 69 TRP A CE2 554 C CE3 . TRP A 69 ? 1.6446 1.1077 1.5528 0.1233 -0.0810 0.2746 69 TRP A CE3 555 C CZ2 . TRP A 69 ? 1.5936 1.0962 1.5079 0.1487 -0.0820 0.2742 69 TRP A CZ2 556 C CZ3 . TRP A 69 ? 1.5827 1.0726 1.4937 0.1166 -0.0760 0.2764 69 TRP A CZ3 557 C CH2 . TRP A 69 ? 1.5608 1.0692 1.4752 0.1283 -0.0771 0.2758 69 TRP A CH2 558 N N . ASP A 70 ? 1.7604 1.1441 1.6501 0.1857 -0.1175 0.2330 70 ASP A N 559 C CA . ASP A 70 ? 1.7599 1.1578 1.6486 0.2091 -0.1218 0.2225 70 ASP A CA 560 C C . ASP A 70 ? 1.7911 1.2103 1.6854 0.2202 -0.1196 0.2285 70 ASP A C 561 O O . ASP A 70 ? 1.8857 1.2919 1.7770 0.2231 -0.1206 0.2339 70 ASP A O 562 C CB . ASP A 70 ? 1.7302 1.0998 1.6048 0.2271 -0.1303 0.2077 70 ASP A CB 563 C CG . ASP A 70 ? 1.6778 1.0716 1.5529 0.2520 -0.1321 0.1945 70 ASP A CG 564 O OD1 . ASP A 70 ? 1.5855 1.0271 1.4764 0.2473 -0.1241 0.1917 70 ASP A OD1 565 O OD2 . ASP A 70 ? 1.7140 1.0862 1.5766 0.2738 -0.1396 0.1855 70 ASP A OD2 566 N N . ARG A 71 ? 1.7851 1.2368 1.6863 0.2262 -0.1167 0.2279 71 ARG A N 567 C CA . ARG A 71 ? 1.7841 1.2594 1.6916 0.2327 -0.1139 0.2351 71 ARG A CA 568 C C . ARG A 71 ? 1.8990 1.3747 1.7993 0.2594 -0.1196 0.2272 71 ARG A C 569 O O . ARG A 71 ? 1.8964 1.3715 1.7980 0.2619 -0.1204 0.2347 71 ARG A O 570 C CB . ARG A 71 ? 1.7115 1.2321 1.6338 0.2253 -0.1051 0.2346 71 ARG A CB 571 C CG . ARG A 71 ? 1.7157 1.2665 1.6454 0.2294 -0.1015 0.2180 71 ARG A CG 572 C CD . ARG A 71 ? 1.7293 1.3266 1.6745 0.2207 -0.0918 0.2183 71 ARG A CD 573 N NE . ARG A 71 ? 1.7202 1.3490 1.6724 0.2225 -0.0877 0.2038 71 ARG A NE 574 C CZ . ARG A 71 ? 1.7108 1.3792 1.6753 0.2140 -0.0791 0.2020 71 ARG A CZ 575 N NH1 . ARG A 71 ? 1.6066 1.2864 1.5782 0.2032 -0.0737 0.2129 71 ARG A NH1 576 N NH2 . ARG A 71 ? 1.7635 1.4595 1.7328 0.2157 -0.0760 0.1892 71 ARG A NH2 577 N N . ASP A 72 ? 2.0853 1.5698 1.9816 0.2773 -0.1222 0.2111 72 ASP A N 578 C CA . ASP A 72 ? 2.1824 1.6734 2.0717 0.3057 -0.1273 0.2016 72 ASP A CA 579 C C . ASP A 72 ? 2.2623 1.7224 2.1444 0.3091 -0.1324 0.2082 72 ASP A C 580 O O . ASP A 72 ? 2.3630 1.8365 2.2452 0.3227 -0.1337 0.2103 72 ASP A O 581 C CB . ASP A 72 ? 2.2492 1.7505 2.1371 0.3189 -0.1293 0.1813 72 ASP A CB 582 C CG . ASP A 72 ? 2.2931 1.7511 2.1706 0.3129 -0.1345 0.1771 72 ASP A CG 583 O OD1 . ASP A 72 ? 2.3484 1.7639 2.2166 0.3050 -0.1384 0.1876 72 ASP A OD1 584 O OD2 . ASP A 72 ? 2.2394 1.7117 2.1201 0.3133 -0.1333 0.1624 72 ASP A OD2 585 N N . GLN A 73 ? 2.1995 1.6227 2.0768 0.2942 -0.1340 0.2116 73 GLN A N 586 C CA . GLN A 73 ? 2.2246 1.6164 2.0937 0.2976 -0.1381 0.2152 73 GLN A CA 587 C C . GLN A 73 ? 2.2998 1.6875 2.1758 0.2762 -0.1336 0.2339 73 GLN A C 588 O O . GLN A 73 ? 2.3042 1.6637 2.1734 0.2739 -0.1356 0.2398 73 GLN A O 589 C CB . GLN A 73 ? 2.2419 1.5934 2.0984 0.2978 -0.1429 0.2057 73 GLN A CB 590 C CG . GLN A 73 ? 2.2120 1.5648 2.0599 0.3231 -0.1486 0.1860 73 GLN A CG 591 C CD . GLN A 73 ? 2.2573 1.5670 2.0913 0.3243 -0.1542 0.1762 73 GLN A CD 592 O OE1 . GLN A 73 ? 2.2699 1.5483 2.1002 0.3049 -0.1536 0.1845 73 GLN A OE1 593 N NE2 . GLN A 73 ? 2.2069 1.5168 2.0332 0.3467 -0.1595 0.1578 73 GLN A NE2 594 N N . TYR A 74 ? 2.2167 1.6324 2.1053 0.2611 -0.1271 0.2429 74 TYR A N 595 C CA . TYR A 74 ? 2.1756 1.5998 2.0721 0.2477 -0.1228 0.2595 74 TYR A CA 596 C C . TYR A 74 ? 2.0643 1.5258 1.9688 0.2578 -0.1226 0.2615 74 TYR A C 597 O O . TYR A 74 ? 1.8801 1.3633 1.7953 0.2438 -0.1178 0.2714 74 TYR A O 598 C CB . TYR A 74 ? 2.1942 1.6209 2.0975 0.2211 -0.1144 0.2687 74 TYR A CB 599 C CG . TYR A 74 ? 2.2637 1.6551 2.1575 0.2074 -0.1133 0.2712 74 TYR A CG 600 C CD1 . TYR A 74 ? 2.3605 1.7182 2.2418 0.2165 -0.1205 0.2610 74 TYR A CD1 601 C CD2 . TYR A 74 ? 2.2276 1.6190 2.1219 0.1864 -0.1048 0.2823 74 TYR A CD2 602 C CE1 . TYR A 74 ? 2.3815 1.7054 2.2531 0.2027 -0.1205 0.2627 74 TYR A CE1 603 C CE2 . TYR A 74 ? 2.2524 1.6123 2.1362 0.1732 -0.1046 0.2836 74 TYR A CE2 604 C CZ . TYR A 74 ? 2.3031 1.6290 2.1766 0.1804 -0.1129 0.2744 74 TYR A CZ 605 O OH . TYR A 74 ? 2.2881 1.5817 2.1509 0.1660 -0.1135 0.2757 74 TYR A OH 606 N N . ASP A 75 ? 2.0311 1.4996 1.9290 0.2829 -0.1278 0.2518 75 ASP A N 607 C CA . ASP A 75 ? 2.0446 1.5506 1.9465 0.2969 -0.1272 0.2502 75 ASP A CA 608 C C . ASP A 75 ? 1.9815 1.5182 1.8916 0.2888 -0.1204 0.2486 75 ASP A C 609 O O . ASP A 75 ? 1.9459 1.5130 1.8617 0.2896 -0.1167 0.2530 75 ASP A O 610 C CB . ASP A 75 ? 2.0230 1.5355 1.9283 0.2937 -0.1282 0.2635 75 ASP A CB 611 C CG . ASP A 75 ? 2.0142 1.5573 1.9172 0.3170 -0.1299 0.2586 75 ASP A CG 612 O OD1 . ASP A 75 ? 1.9886 1.5595 1.8923 0.3302 -0.1271 0.2477 75 ASP A OD1 613 O OD2 . ASP A 75 ? 2.0200 1.5618 1.9207 0.3228 -0.1334 0.2660 75 ASP A OD2 614 N N . GLY A 76 ? 2.0990 1.6268 2.0085 0.2816 -0.1185 0.2425 76 GLY A N 615 C CA . GLY A 76 ? 2.0327 1.5856 1.9478 0.2760 -0.1115 0.2404 76 GLY A CA 616 C C . GLY A 76 ? 1.9763 1.5437 1.9024 0.2531 -0.1040 0.2527 76 GLY A C 617 O O . GLY A 76 ? 2.0436 1.6508 1.9833 0.2453 -0.0959 0.2483 76 GLY A O 618 N N . LEU A 77 ? 1.9355 1.4840 1.8649 0.2337 -0.1060 0.2632 77 LEU A N 619 C CA . LEU A 77 ? 1.7380 1.2985 1.6740 0.2121 -0.1020 0.2720 77 LEU A CA 620 C C . LEU A 77 ? 1.6004 1.1580 1.5374 0.1966 -0.0964 0.2699 77 LEU A C 621 O O . LEU A 77 ? 1.3767 0.9068 1.3009 0.1909 -0.0950 0.2675 77 LEU A O 622 C CB . LEU A 77 ? 1.7895 1.3313 1.7188 0.1979 -0.1084 0.2794 77 LEU A CB 623 C CG . LEU A 77 ? 1.8580 1.4133 1.7857 0.2079 -0.1110 0.2847 77 LEU A CG 624 C CD1 . LEU A 77 ? 1.8280 1.3852 1.7588 0.2324 -0.1138 0.2826 77 LEU A CD1 625 C CD2 . LEU A 77 ? 1.9432 1.4798 1.8497 0.1940 -0.1123 0.2888 77 LEU A CD2 626 N N . ASP A 78 ? 1.5588 1.1504 1.5097 0.1923 -0.0861 0.2709 78 ASP A N 627 C CA . ASP A 78 ? 1.5280 1.1275 1.4875 0.1775 -0.0801 0.2689 78 ASP A CA 628 C C . ASP A 78 ? 1.6924 1.2760 1.6433 0.1559 -0.0790 0.2725 78 ASP A C 629 O O . ASP A 78 ? 1.6263 1.1916 1.5716 0.1482 -0.0794 0.2704 78 ASP A O 630 C CB . ASP A 78 ? 1.6685 1.3117 1.6419 0.1730 -0.0707 0.2637 78 ASP A CB 631 C CG . ASP A 78 ? 1.8061 1.4582 1.7880 0.1538 -0.0636 0.2654 78 ASP A CG 632 O OD1 . ASP A 78 ? 1.7482 1.3779 1.7269 0.1432 -0.0652 0.2708 78 ASP A OD1 633 O OD2 . ASP A 78 ? 1.8361 1.5190 1.8277 0.1490 -0.0560 0.2613 78 ASP A OD2 634 N N . SER A 79 ? 1.8714 1.4654 1.8206 0.1469 -0.0759 0.2769 79 SER A N 635 C CA . SER A 79 ? 1.7463 1.3340 1.6885 0.1276 -0.0717 0.2792 79 SER A CA 636 C C . SER A 79 ? 1.7356 1.3254 1.6707 0.1210 -0.0705 0.2843 79 SER A C 637 O O . SER A 79 ? 1.8943 1.5043 1.8369 0.1256 -0.0698 0.2868 79 SER A O 638 C CB . SER A 79 ? 1.7820 1.3939 1.7386 0.1158 -0.0642 0.2784 79 SER A CB 639 O OG . SER A 79 ? 1.9343 1.5551 1.8895 0.1013 -0.0593 0.2813 79 SER A OG 640 N N . ILE A 80 ? 1.4051 0.9805 1.3297 0.1083 -0.0683 0.2866 80 ILE A N 641 C CA . ILE A 80 ? 1.1121 0.6889 1.0300 0.1016 -0.0671 0.2923 80 ILE A CA 642 C C . ILE A 80 ? 1.1484 0.7433 1.0731 0.0847 -0.0607 0.2936 80 ILE A C 643 O O . ILE A 80 ? 1.2619 0.8606 1.1917 0.0767 -0.0574 0.2906 80 ILE A O 644 C CB . ILE A 80 ? 1.0948 0.6396 0.9945 0.1024 -0.0692 0.2960 80 ILE A CB 645 C CG1 . ILE A 80 ? 1.1377 0.6682 1.0352 0.0916 -0.0662 0.2950 80 ILE A CG1 646 C CG2 . ILE A 80 ? 1.2425 0.7670 1.1338 0.1216 -0.0749 0.2951 80 ILE A CG2 647 C CD1 . ILE A 80 ? 1.2348 0.7340 1.1194 0.0932 -0.0670 0.2996 80 ILE A CD1 648 N N . ARG A 81 ? 1.1318 0.7408 1.0580 0.0806 -0.0591 0.2981 81 ARG A N 649 C CA . ARG A 81 ? 1.1296 0.7546 1.0609 0.0661 -0.0538 0.3000 81 ARG A CA 650 C C . ARG A 81 ? 1.1097 0.7169 1.0280 0.0586 -0.0547 0.3052 81 ARG A C 651 O O . ARG A 81 ? 1.1030 0.6951 1.0108 0.0646 -0.0583 0.3094 81 ARG A O 652 C CB . ARG A 81 ? 1.1147 0.7679 1.0576 0.0656 -0.0508 0.3021 81 ARG A CB 653 C CG . ARG A 81 ? 1.3233 0.9956 1.2806 0.0720 -0.0481 0.2983 81 ARG A CG 654 C CD . ARG A 81 ? 1.5828 1.2820 1.5515 0.0705 -0.0439 0.3013 81 ARG A CD 655 N NE . ARG A 81 ? 1.7290 1.4467 1.7116 0.0757 -0.0398 0.2990 81 ARG A NE 656 C CZ . ARG A 81 ? 1.8489 1.5893 1.8421 0.0769 -0.0356 0.3018 81 ARG A CZ 657 N NH1 . ARG A 81 ? 1.9589 1.7074 1.9510 0.0740 -0.0358 0.3068 81 ARG A NH1 658 N NH2 . ARG A 81 ? 1.7596 1.5149 1.7645 0.0811 -0.0309 0.3005 81 ARG A NH2 659 N N . ILE A 82 ? 1.1492 0.7577 1.0683 0.0460 -0.0515 0.3055 82 ILE A N 660 C CA . ILE A 82 ? 1.2547 0.8498 1.1643 0.0365 -0.0517 0.3115 82 ILE A CA 661 C C . ILE A 82 ? 1.4164 1.0312 1.3332 0.0220 -0.0477 0.3136 82 ILE A C 662 O O . ILE A 82 ? 1.2090 0.8419 1.1363 0.0198 -0.0445 0.3093 82 ILE A O 663 C CB . ILE A 82 ? 1.3769 0.9411 1.2765 0.0376 -0.0539 0.3109 82 ILE A CB 664 C CG1 . ILE A 82 ? 1.3754 0.9404 1.2816 0.0386 -0.0532 0.3041 82 ILE A CG1 665 C CG2 . ILE A 82 ? 1.2898 0.8305 1.1784 0.0515 -0.0580 0.3125 82 ILE A CG2 666 C CD1 . ILE A 82 ? 1.4486 0.9847 1.3475 0.0399 -0.0557 0.3035 82 ILE A CD1 667 N N . PRO A 83 ? 1.5322 1.1446 1.4438 0.0126 -0.0479 0.3208 83 PRO A N 668 C CA . PRO A 83 ? 1.5860 1.2179 1.5038 -0.0007 -0.0453 0.3245 83 PRO A CA 669 C C . PRO A 83 ? 1.6396 1.2748 1.5620 -0.0081 -0.0434 0.3215 83 PRO A C 670 O O . PRO A 83 ? 1.8522 1.4672 1.7685 -0.0115 -0.0452 0.3215 83 PRO A O 671 C CB . PRO A 83 ? 1.5989 1.2178 1.5070 -0.0083 -0.0475 0.3331 83 PRO A CB 672 C CG . PRO A 83 ? 1.5756 1.1822 1.4762 0.0027 -0.0500 0.3348 83 PRO A CG 673 C CD . PRO A 83 ? 1.5813 1.1769 1.4816 0.0160 -0.0510 0.3270 83 PRO A CD 674 N N . SER A 84 ? 1.5242 1.1857 1.4577 -0.0109 -0.0400 0.3200 84 SER A N 675 C CA . SER A 84 ? 1.4348 1.1030 1.3732 -0.0171 -0.0382 0.3180 84 SER A CA 676 C C . SER A 84 ? 1.4386 1.1006 1.3724 -0.0303 -0.0400 0.3242 84 SER A C 677 O O . SER A 84 ? 1.5111 1.1631 1.4436 -0.0345 -0.0409 0.3228 84 SER A O 678 C CB . SER A 84 ? 1.3529 1.0503 1.3032 -0.0168 -0.0341 0.3166 84 SER A CB 679 O OG . SER A 84 ? 1.4307 1.1461 1.3843 -0.0251 -0.0335 0.3234 84 SER A OG 680 N N . ASP A 85 ? 1.4246 1.0913 1.3558 -0.0374 -0.0411 0.3316 85 ASP A N 681 C CA . ASP A 85 ? 1.3808 1.0435 1.3081 -0.0519 -0.0433 0.3384 85 ASP A CA 682 C C . ASP A 85 ? 1.4675 1.0956 1.3836 -0.0531 -0.0467 0.3383 85 ASP A C 683 O O . ASP A 85 ? 1.5529 1.1719 1.4645 -0.0660 -0.0491 0.3434 85 ASP A O 684 C CB . ASP A 85 ? 1.7135 1.3928 1.6414 -0.0604 -0.0439 0.3472 85 ASP A CB 685 C CG . ASP A 85 ? 1.7781 1.4431 1.6977 -0.0560 -0.0458 0.3507 85 ASP A CG 686 O OD1 . ASP A 85 ? 1.7553 1.3958 1.6676 -0.0463 -0.0469 0.3469 85 ASP A OD1 687 O OD2 . ASP A 85 ? 1.7119 1.3917 1.6323 -0.0626 -0.0464 0.3582 85 ASP A OD2 688 N N . LEU A 86 ? 1.3318 0.9409 1.2434 -0.0400 -0.0472 0.3328 86 LEU A N 689 C CA . LEU A 86 ? 1.3904 0.9654 1.2912 -0.0383 -0.0505 0.3332 86 LEU A CA 690 C C . LEU A 86 ? 1.4423 1.0045 1.3445 -0.0340 -0.0513 0.3263 86 LEU A C 691 O O . LEU A 86 ? 1.5310 1.0648 1.4260 -0.0335 -0.0545 0.3258 86 LEU A O 692 C CB . LEU A 86 ? 1.4007 0.9624 1.2945 -0.0253 -0.0514 0.3336 86 LEU A CB 693 C CG . LEU A 86 ? 1.4638 0.9916 1.3450 -0.0234 -0.0546 0.3377 86 LEU A CG 694 C CD1 . LEU A 86 ? 1.6491 1.1683 1.5257 -0.0408 -0.0565 0.3454 86 LEU A CD1 695 C CD2 . LEU A 86 ? 1.3983 0.9243 1.2740 -0.0124 -0.0550 0.3407 86 LEU A CD2 696 N N . VAL A 87 ? 1.2816 0.8644 1.1933 -0.0310 -0.0486 0.3212 87 VAL A N 697 C CA . VAL A 87 ? 1.3212 0.8952 1.2351 -0.0287 -0.0496 0.3157 87 VAL A CA 698 C C . VAL A 87 ? 1.2677 0.8608 1.1889 -0.0405 -0.0483 0.3172 87 VAL A C 699 O O . VAL A 87 ? 1.2548 0.8733 1.1818 -0.0455 -0.0456 0.3205 87 VAL A O 700 C CB . VAL A 87 ? 1.1895 0.7690 1.1080 -0.0133 -0.0481 0.3084 87 VAL A CB 701 C CG1 . VAL A 87 ? 1.0962 0.6541 1.0069 -0.0010 -0.0507 0.3071 87 VAL A CG1 702 C CG2 . VAL A 87 ? 1.1356 0.7456 1.0628 -0.0113 -0.0439 0.3077 87 VAL A CG2 703 N N . TRP A 88 ? 1.2910 0.8727 1.2122 -0.0445 -0.0508 0.3152 88 TRP A N 704 C CA . TRP A 88 ? 1.1701 0.7709 1.0982 -0.0542 -0.0499 0.3168 88 TRP A CA 705 C C . TRP A 88 ? 1.1708 0.7981 1.1084 -0.0453 -0.0448 0.3135 88 TRP A C 706 O O . TRP A 88 ? 1.1467 0.7706 1.0858 -0.0326 -0.0437 0.3077 88 TRP A O 707 C CB . TRP A 88 ? 1.2369 0.8208 1.1637 -0.0583 -0.0539 0.3144 88 TRP A CB 708 C CG . TRP A 88 ? 1.2922 0.8969 1.2254 -0.0694 -0.0535 0.3176 88 TRP A CG 709 C CD1 . TRP A 88 ? 1.3127 0.9221 1.2439 -0.0865 -0.0560 0.3239 88 TRP A CD1 710 C CD2 . TRP A 88 ? 1.2298 0.8557 1.1723 -0.0641 -0.0502 0.3154 88 TRP A CD2 711 N NE1 . TRP A 88 ? 1.3675 1.0005 1.3062 -0.0915 -0.0546 0.3260 88 TRP A NE1 712 C CE2 . TRP A 88 ? 1.2708 0.9135 1.2165 -0.0774 -0.0508 0.3210 88 TRP A CE2 713 C CE3 . TRP A 88 ? 1.1588 0.7915 1.1068 -0.0499 -0.0469 0.3097 88 TRP A CE3 714 C CZ2 . TRP A 88 ? 1.1479 0.8135 1.1019 -0.0755 -0.0479 0.3216 88 TRP A CZ2 715 C CZ3 . TRP A 88 ? 1.2193 0.8731 1.1754 -0.0491 -0.0439 0.3099 88 TRP A CZ3 716 C CH2 . TRP A 88 ? 1.2221 0.8920 1.1812 -0.0611 -0.0443 0.3160 88 TRP A CH2 717 N N . ARG A 89 ? 1.2341 0.8878 1.1781 -0.0523 -0.0422 0.3175 89 ARG A N 718 C CA . ARG A 89 ? 1.3276 1.0067 1.2808 -0.0456 -0.0374 0.3152 89 ARG A CA 719 C C . ARG A 89 ? 1.2620 0.9587 1.2210 -0.0532 -0.0365 0.3187 89 ARG A C 720 O O . ARG A 89 ? 1.1934 0.8921 1.1505 -0.0661 -0.0392 0.3248 89 ARG A O 721 C CB . ARG A 89 ? 1.3272 1.0247 1.2834 -0.0439 -0.0346 0.3175 89 ARG A CB 722 C CG . ARG A 89 ? 1.2852 0.9729 1.2375 -0.0359 -0.0349 0.3152 89 ARG A CG 723 C CD . ARG A 89 ? 1.2057 0.9027 1.1567 -0.0428 -0.0354 0.3221 89 ARG A CD 724 N NE . ARG A 89 ? 1.4843 1.1660 1.4276 -0.0542 -0.0394 0.3278 89 ARG A NE 725 C CZ . ARG A 89 ? 1.7726 1.4642 1.7169 -0.0677 -0.0407 0.3340 89 ARG A CZ 726 N NH1 . ARG A 89 ? 1.7881 1.5068 1.7409 -0.0706 -0.0383 0.3362 89 ARG A NH1 727 N NH2 . ARG A 89 ? 1.8219 1.4960 1.7581 -0.0787 -0.0447 0.3387 89 ARG A NH2 728 N N . PRO A 90 ? 1.3800 1.0890 1.3455 -0.0459 -0.0331 0.3152 90 PRO A N 729 C CA . PRO A 90 ? 1.4693 1.1988 1.4403 -0.0521 -0.0319 0.3199 90 PRO A CA 730 C C . PRO A 90 ? 1.4119 1.1646 1.3867 -0.0543 -0.0294 0.3248 90 PRO A C 731 O O . PRO A 90 ? 1.6038 1.3652 1.5821 -0.0451 -0.0257 0.3216 90 PRO A O 732 C CB . PRO A 90 ? 1.4494 1.1848 1.4256 -0.0421 -0.0284 0.3151 90 PRO A CB 733 C CG . PRO A 90 ? 1.3418 1.0706 1.3176 -0.0312 -0.0263 0.3085 90 PRO A CG 734 C CD . PRO A 90 ? 1.3691 1.0769 1.3374 -0.0330 -0.0303 0.3082 90 PRO A CD 735 N N . ASP A 91 ? 0.9847 0.7481 0.9589 -0.0664 -0.0316 0.3326 91 ASP A N 736 C CA . ASP A 91 ? 0.9209 0.7066 0.8990 -0.0671 -0.0296 0.3373 91 ASP A CA 737 C C . ASP A 91 ? 0.8667 0.6763 0.8529 -0.0587 -0.0248 0.3375 91 ASP A C 738 O O . ASP A 91 ? 1.1738 1.0069 1.1640 -0.0632 -0.0242 0.3445 91 ASP A O 739 C CB . ASP A 91 ? 1.0111 0.8066 0.9869 -0.0828 -0.0333 0.3465 91 ASP A CB 740 C CG . ASP A 91 ? 1.4211 1.1927 1.3880 -0.0903 -0.0375 0.3469 91 ASP A CG 741 O OD1 . ASP A 91 ? 1.5727 1.3387 1.5382 -0.0842 -0.0366 0.3449 91 ASP A OD1 742 O OD2 . ASP A 91 ? 1.5160 1.2739 1.4770 -0.1024 -0.0418 0.3494 91 ASP A OD2 743 N N . ILE A 92 ? 0.7554 0.5587 0.7435 -0.0465 -0.0214 0.3299 92 ILE A N 744 C CA . ILE A 92 ? 0.8870 0.7068 0.8813 -0.0376 -0.0166 0.3288 92 ILE A CA 745 C C . ILE A 92 ? 0.8885 0.7251 0.8871 -0.0331 -0.0139 0.3310 92 ILE A C 746 O O . ILE A 92 ? 1.0600 0.8897 1.0580 -0.0289 -0.0134 0.3271 92 ILE A O 747 C CB . ILE A 92 ? 0.9698 0.7759 0.9639 -0.0281 -0.0142 0.3202 92 ILE A CB 748 C CG1 . ILE A 92 ? 0.9146 0.7122 0.9071 -0.0309 -0.0159 0.3198 92 ILE A CG1 749 C CG2 . ILE A 92 ? 0.9226 0.7426 0.9219 -0.0190 -0.0090 0.3187 92 ILE A CG2 750 C CD1 . ILE A 92 ? 0.8242 0.6167 0.8183 -0.0222 -0.0129 0.3136 92 ILE A CD1 751 N N . VAL A 93 ? 0.7574 0.6176 0.7606 -0.0336 -0.0122 0.3379 93 VAL A N 752 C CA . VAL A 93 ? 0.7153 0.5960 0.7231 -0.0303 -0.0102 0.3426 93 VAL A CA 753 C C . VAL A 93 ? 0.7552 0.6482 0.7676 -0.0190 -0.0051 0.3423 93 VAL A C 754 O O . VAL A 93 ? 0.9161 0.7975 0.9275 -0.0132 -0.0029 0.3363 93 VAL A O 755 C CB . VAL A 93 ? 0.7894 0.6900 0.7979 -0.0409 -0.0131 0.3528 93 VAL A CB 756 C CG1 . VAL A 93 ? 0.6590 0.5430 0.6611 -0.0535 -0.0183 0.3532 93 VAL A CG1 757 C CG2 . VAL A 93 ? 0.9057 0.8285 0.9174 -0.0401 -0.0116 0.3592 93 VAL A CG2 758 N N . LEU A 94 ? 0.8146 0.7279 0.8313 -0.0148 -0.0031 0.3478 94 LEU A N 759 C CA . LEU A 94 ? 0.8749 0.7989 0.8948 -0.0035 0.0016 0.3487 94 LEU A CA 760 C C . LEU A 94 ? 1.2365 1.1870 1.2584 -0.0048 0.0015 0.3589 94 LEU A C 761 O O . LEU A 94 ? 1.3525 1.3256 1.3767 -0.0085 0.0001 0.3672 94 LEU A O 762 C CB . LEU A 94 ? 0.6097 0.5380 0.6327 0.0048 0.0046 0.3480 94 LEU A CB 763 C CG . LEU A 94 ? 0.7367 0.6651 0.7608 0.0177 0.0099 0.3462 94 LEU A CG 764 C CD1 . LEU A 94 ? 0.6117 0.5149 0.6329 0.0204 0.0115 0.3358 94 LEU A CD1 765 C CD2 . LEU A 94 ? 0.6045 0.5460 0.6320 0.0269 0.0131 0.3501 94 LEU A CD2 766 N N . TYR A 95 ? 1.1150 1.0653 1.1359 -0.0018 0.0029 0.3589 95 TYR A N 767 C CA . TYR A 95 ? 0.9139 0.8913 0.9364 -0.0012 0.0033 0.3687 95 TYR A CA 768 C C . TYR A 95 ? 0.9644 0.9611 0.9897 0.0117 0.0073 0.3735 95 TYR A C 769 O O . TYR A 95 ? 1.0914 1.1177 1.1185 0.0119 0.0069 0.3831 95 TYR A O 770 C CB . TYR A 95 ? 0.8898 0.8618 0.9103 0.0005 0.0042 0.3673 95 TYR A CB 771 C CG . TYR A 95 ? 0.8828 0.8501 0.9010 -0.0128 -0.0001 0.3682 95 TYR A CG 772 C CD1 . TYR A 95 ? 0.9507 0.9065 0.9670 -0.0250 -0.0046 0.3666 95 TYR A CD1 773 C CD2 . TYR A 95 ? 0.6937 0.6661 0.7109 -0.0129 0.0003 0.3706 95 TYR A CD2 774 C CE1 . TYR A 95 ? 0.9865 0.9343 0.9996 -0.0374 -0.0087 0.3673 95 TYR A CE1 775 C CE2 . TYR A 95 ? 0.7697 0.7367 0.7847 -0.0255 -0.0039 0.3715 95 TYR A CE2 776 C CZ . TYR A 95 ? 0.8754 0.8290 0.8880 -0.0380 -0.0085 0.3698 95 TYR A CZ 777 O OH . TYR A 95 ? 0.8054 0.7501 0.8147 -0.0509 -0.0129 0.3707 95 TYR A OH 778 N N . ASN A 96 ? 0.9884 0.9684 1.0132 0.0226 0.0111 0.3668 96 ASN A N 779 C CA . ASN A 96 ? 1.0137 1.0052 1.0396 0.0369 0.0155 0.3701 96 ASN A CA 780 C C . ASN A 96 ? 1.1028 1.1125 1.1322 0.0400 0.0158 0.3754 96 ASN A C 781 O O . ASN A 96 ? 0.8332 0.8559 0.8632 0.0534 0.0193 0.3795 96 ASN A O 782 C CB . ASN A 96 ? 0.7404 0.7038 0.7635 0.0448 0.0191 0.3605 96 ASN A CB 783 C CG . ASN A 96 ? 0.9088 0.8765 0.9310 0.0600 0.0238 0.3629 96 ASN A CG 784 O OD1 . ASN A 96 ? 1.0474 1.0392 1.0701 0.0672 0.0248 0.3716 96 ASN A OD1 785 N ND2 . ASN A 96 ? 0.7574 0.7027 0.7775 0.0654 0.0268 0.3556 96 ASN A ND2 786 N N . LYS A 97 ? 1.0738 1.0849 1.1047 0.0282 0.0119 0.3757 97 LYS A N 787 C CA . LYS A 97 ? 1.0734 1.0984 1.1073 0.0280 0.0114 0.3796 97 LYS A CA 788 C C . LYS A 97 ? 1.0105 1.0689 1.0467 0.0384 0.0137 0.3893 97 LYS A C 789 O O . LYS A 97 ? 1.0906 1.1650 1.1259 0.0448 0.0150 0.3943 97 LYS A O 790 C CB . LYS A 97 ? 1.0279 1.0581 1.0617 0.0109 0.0058 0.3823 97 LYS A CB 791 C CG . LYS A 97 ? 1.2301 1.2585 1.2654 0.0070 0.0044 0.3816 97 LYS A CG 792 C CD . LYS A 97 ? 1.4132 1.4350 1.4459 -0.0102 -0.0012 0.3818 97 LYS A CD 793 C CE . LYS A 97 ? 1.4930 1.5299 1.5238 -0.0209 -0.0043 0.3884 97 LYS A CE 794 N NZ . LYS A 97 ? 1.5581 1.5752 1.5842 -0.0361 -0.0092 0.3856 97 LYS A NZ 795 N N . ALA A 98 ? 0.9120 0.9824 0.9507 0.0416 0.0143 0.3922 98 ALA A N 796 C CA . ALA A 98 ? 0.8622 0.9701 0.9024 0.0510 0.0157 0.4021 98 ALA A CA 797 C C . ALA A 98 ? 1.1508 1.2840 1.1939 0.0427 0.0128 0.4083 98 ALA A C 798 O O . ALA A 98 ? 0.9925 1.1653 1.0363 0.0437 0.0120 0.4177 98 ALA A O 799 C CB . ALA A 98 ? 0.7933 0.8938 0.8323 0.0720 0.0215 0.3998 98 ALA A CB 800 N N . ASP A 99 ? 1.0445 1.1564 1.0885 0.0341 0.0111 0.4029 99 ASP A N 801 C CA . ASP A 99 ? 1.0188 1.1489 1.0649 0.0252 0.0082 0.4077 99 ASP A CA 802 C C . ASP A 99 ? 1.1332 1.2385 1.1776 0.0084 0.0037 0.4025 99 ASP A C 803 O O . ASP A 99 ? 1.2151 1.3282 1.2577 -0.0065 -0.0007 0.4063 99 ASP A O 804 N N . PRO A 105 ? 1.2570 1.1353 1.2711 -0.0146 -0.0103 0.3380 105 PRO A N 805 C CA . PRO A 105 ? 1.3550 1.2539 1.3724 -0.0181 -0.0114 0.3467 105 PRO A CA 806 C C . PRO A 105 ? 1.6575 1.5536 1.6746 -0.0165 -0.0126 0.3468 105 PRO A C 807 O O . PRO A 105 ? 1.5487 1.4621 1.5722 -0.0119 -0.0101 0.3499 105 PRO A O 808 C CB . PRO A 105 ? 1.3550 1.2758 1.3803 -0.0114 -0.0069 0.3496 105 PRO A CB 809 C CG . PRO A 105 ? 0.9045 0.8164 0.9294 -0.0068 -0.0042 0.3441 105 PRO A CG 810 C CD . PRO A 105 ? 1.0776 0.9643 1.0954 -0.0106 -0.0068 0.3375 105 PRO A CD 811 N N . VAL A 106 ? 1.8136 1.6889 1.8234 -0.0191 -0.0160 0.3440 106 VAL A N 812 C CA . VAL A 106 ? 1.8651 1.7350 1.8728 -0.0172 -0.0179 0.3447 106 VAL A CA 813 C C . VAL A 106 ? 1.7570 1.5984 1.7563 -0.0154 -0.0202 0.3380 106 VAL A C 814 O O . VAL A 106 ? 1.7184 1.5501 1.7188 -0.0089 -0.0180 0.3304 106 VAL A O 815 C CB . VAL A 106 ? 1.3794 1.2627 1.3953 -0.0087 -0.0142 0.3438 106 VAL A CB 816 C CG1 . VAL A 106 ? 1.4486 1.3173 1.4620 -0.0035 -0.0153 0.3396 106 VAL A CG1 817 C CG2 . VAL A 106 ? 1.1937 1.1032 1.2147 -0.0113 -0.0143 0.3532 106 VAL A CG2 818 N N . ASN A 107 ? 1.6499 1.4780 1.6404 -0.0210 -0.0245 0.3416 107 ASN A N 819 C CA . ASN A 107 ? 1.4581 1.2584 1.4393 -0.0204 -0.0269 0.3366 107 ASN A CA 820 C C . ASN A 107 ? 1.4178 1.2048 1.3972 -0.0106 -0.0272 0.3310 107 ASN A C 821 O O . ASN A 107 ? 1.3900 1.1863 1.3729 -0.0064 -0.0270 0.3331 107 ASN A O 822 C CB . ASN A 107 ? 1.3794 1.1675 1.3508 -0.0298 -0.0311 0.3431 107 ASN A CB 823 C CG . ASN A 107 ? 1.2808 1.0415 1.2429 -0.0310 -0.0332 0.3392 107 ASN A CG 824 O OD1 . ASN A 107 ? 1.3729 1.1290 1.3372 -0.0270 -0.0313 0.3326 107 ASN A OD1 825 N ND2 . ASN A 107 ? 1.1475 0.8896 1.0992 -0.0365 -0.0368 0.3437 107 ASN A ND2 826 N N . THR A 108 ? 1.5207 1.2886 1.4957 -0.0069 -0.0277 0.3244 108 THR A N 827 C CA . THR A 108 ? 1.2959 1.0531 1.2699 0.0026 -0.0283 0.3194 108 THR A CA 828 C C . THR A 108 ? 1.3765 1.1069 1.3402 0.0044 -0.0317 0.3163 108 THR A C 829 O O . THR A 108 ? 1.3820 1.1002 1.3386 -0.0023 -0.0336 0.3187 108 THR A O 830 C CB . THR A 108 ? 1.0991 0.8664 1.0824 0.0084 -0.0241 0.3132 108 THR A CB 831 O OG1 . THR A 108 ? 1.2293 0.9883 1.2113 0.0071 -0.0231 0.3085 108 THR A OG1 832 C CG2 . THR A 108 ? 1.0230 0.8145 1.0164 0.0074 -0.0199 0.3156 108 THR A CG2 833 N N . ASN A 109 ? 1.3670 1.0893 1.3309 0.0134 -0.0323 0.3113 109 ASN A N 834 C CA . ASN A 109 ? 1.4730 1.1698 1.4271 0.0175 -0.0361 0.3091 109 ASN A CA 835 C C . ASN A 109 ? 1.3154 1.0079 1.2730 0.0228 -0.0350 0.3020 109 ASN A C 836 O O . ASN A 109 ? 1.1791 0.8876 1.1468 0.0248 -0.0312 0.2986 109 ASN A O 837 C CB . ASN A 109 ? 1.7769 1.4648 1.7254 0.0254 -0.0398 0.3118 109 ASN A CB 838 C CG . ASN A 109 ? 1.9935 1.6796 1.9352 0.0200 -0.0418 0.3199 109 ASN A CG 839 O OD1 . ASN A 109 ? 2.0351 1.7025 1.9663 0.0151 -0.0440 0.3231 109 ASN A OD1 840 N ND2 . ASN A 109 ? 1.9793 1.6857 1.9278 0.0205 -0.0407 0.3237 109 ASN A ND2 841 N N . VAL A 110 ? 1.2911 0.9611 1.2402 0.0249 -0.0383 0.3005 110 VAL A N 842 C CA . VAL A 110 ? 1.2608 0.9266 1.2131 0.0282 -0.0377 0.2949 110 VAL A CA 843 C C . VAL A 110 ? 1.3684 1.0208 1.3181 0.0400 -0.0415 0.2922 110 VAL A C 844 O O . VAL A 110 ? 1.4921 1.1260 1.4321 0.0450 -0.0459 0.2944 110 VAL A O 845 C CB . VAL A 110 ? 1.2674 0.9211 1.2148 0.0207 -0.0383 0.2951 110 VAL A CB 846 C CG1 . VAL A 110 ? 1.2989 0.9684 1.2498 0.0094 -0.0352 0.2987 110 VAL A CG1 847 C CG2 . VAL A 110 ? 1.1573 0.7835 1.0923 0.0217 -0.0430 0.2976 110 VAL A CG2 848 N N . VAL A 111 ? 1.2788 0.9405 1.2375 0.0448 -0.0397 0.2880 111 VAL A N 849 C CA . VAL A 111 ? 1.2595 0.9127 1.2186 0.0567 -0.0432 0.2857 111 VAL A CA 850 C C . VAL A 111 ? 1.3655 0.9983 1.3188 0.0582 -0.0465 0.2834 111 VAL A C 851 O O . VAL A 111 ? 1.5507 1.1901 1.5110 0.0570 -0.0443 0.2806 111 VAL A O 852 C CB . VAL A 111 ? 1.2905 0.9646 1.2635 0.0604 -0.0390 0.2834 111 VAL A CB 853 C CG1 . VAL A 111 ? 1.3374 1.0075 1.3132 0.0738 -0.0425 0.2822 111 VAL A CG1 854 C CG2 . VAL A 111 ? 1.1874 0.8825 1.1678 0.0574 -0.0345 0.2855 111 VAL A CG2 855 N N . LEU A 112 ? 1.3125 0.9205 1.2535 0.0614 -0.0513 0.2849 112 LEU A N 856 C CA . LEU A 112 ? 1.3189 0.9063 1.2555 0.0633 -0.0543 0.2826 112 LEU A CA 857 C C . LEU A 112 ? 1.2725 0.8537 1.2117 0.0787 -0.0587 0.2792 112 LEU A C 858 O O . LEU A 112 ? 1.3964 0.9693 1.3301 0.0894 -0.0624 0.2801 112 LEU A O 859 C CB . LEU A 112 ? 1.2821 0.8435 1.2053 0.0597 -0.0567 0.2859 112 LEU A CB 860 C CG . LEU A 112 ? 1.2019 0.7377 1.1208 0.0649 -0.0609 0.2835 112 LEU A CG 861 C CD1 . LEU A 112 ? 1.0970 0.6366 1.0226 0.0557 -0.0600 0.2812 112 LEU A CD1 862 C CD2 . LEU A 112 ? 1.0639 0.5709 0.9706 0.0659 -0.0636 0.2872 112 LEU A CD2 863 N N . ARG A 113 ? 1.2539 0.8368 1.2003 0.0807 -0.0592 0.2758 113 ARG A N 864 C CA . ARG A 113 ? 1.1847 0.7660 1.1366 0.0966 -0.0635 0.2728 113 ARG A CA 865 C C . ARG A 113 ? 1.3483 0.8986 1.2906 0.1052 -0.0705 0.2703 113 ARG A C 866 O O . ARG A 113 ? 1.3943 0.9253 1.3275 0.0965 -0.0707 0.2716 113 ARG A O 867 C CB . ARG A 113 ? 1.0429 0.6466 1.0104 0.0952 -0.0594 0.2714 113 ARG A CB 868 C CG . ARG A 113 ? 1.0293 0.6470 1.0085 0.1110 -0.0601 0.2703 113 ARG A CG 869 C CD . ARG A 113 ? 1.1743 0.8211 1.1670 0.1067 -0.0520 0.2686 113 ARG A CD 870 N NE . ARG A 113 ? 1.2033 0.8474 1.1956 0.0993 -0.0514 0.2648 113 ARG A NE 871 C CZ . ARG A 113 ? 1.2113 0.8773 1.2107 0.0931 -0.0447 0.2616 113 ARG A CZ 872 N NH1 . ARG A 113 ? 1.3817 1.0720 1.3884 0.0927 -0.0380 0.2611 113 ARG A NH1 873 N NH2 . ARG A 113 ? 0.9498 0.6133 0.9482 0.0868 -0.0448 0.2592 113 ARG A NH2 874 N N . TYR A 114 ? 1.4889 1.0356 1.4347 0.1227 -0.0760 0.2670 114 TYR A N 875 C CA . TYR A 114 ? 1.4965 1.0131 1.4336 0.1342 -0.0838 0.2628 114 TYR A CA 876 C C . TYR A 114 ? 1.4635 0.9688 1.4019 0.1260 -0.0865 0.2590 114 TYR A C 877 O O . TYR A 114 ? 1.5774 1.0537 1.5055 0.1268 -0.0919 0.2555 114 TYR A O 878 C CB . TYR A 114 ? 1.3981 0.9181 1.3387 0.1569 -0.0907 0.2572 114 TYR A CB 879 C CG . TYR A 114 ? 1.3885 0.9414 1.3383 0.1595 -0.0854 0.2437 114 TYR A CG 880 C CD1 . TYR A 114 ? 1.5193 1.0652 1.4655 0.1612 -0.0879 0.2321 114 TYR A CD1 881 C CD2 . TYR A 114 ? 1.4159 1.0071 1.3774 0.1595 -0.0779 0.2425 114 TYR A CD2 882 C CE1 . TYR A 114 ? 1.6580 1.2359 1.6123 0.1628 -0.0829 0.2206 114 TYR A CE1 883 C CE2 . TYR A 114 ? 1.5320 1.1530 1.5010 0.1603 -0.0729 0.2312 114 TYR A CE2 884 C CZ . TYR A 114 ? 1.6623 1.2775 1.6277 0.1621 -0.0754 0.2206 114 TYR A CZ 885 O OH . TYR A 114 ? 1.6833 1.3304 1.6560 0.1623 -0.0704 0.2100 114 TYR A OH 886 N N . ASP A 115 ? 1.2874 0.8174 1.2387 0.1181 -0.0821 0.2592 115 ASP A N 887 C CA . ASP A 115 ? 1.3713 0.9005 1.3227 0.1091 -0.0816 0.2532 115 ASP A CA 888 C C . ASP A 115 ? 1.4744 0.9966 1.4240 0.0894 -0.0791 0.2623 115 ASP A C 889 O O . ASP A 115 ? 1.6078 1.1351 1.5615 0.0799 -0.0784 0.2616 115 ASP A O 890 C CB . ASP A 115 ? 1.3388 0.9053 1.3014 0.1095 -0.0742 0.2452 115 ASP A CB 891 C CG . ASP A 115 ? 1.2844 0.8756 1.2578 0.0999 -0.0660 0.2550 115 ASP A CG 892 O OD1 . ASP A 115 ? 1.3296 0.9153 1.3029 0.0987 -0.0661 0.2650 115 ASP A OD1 893 O OD2 . ASP A 115 ? 1.2190 0.8345 1.2003 0.0938 -0.0596 0.2527 115 ASP A OD2 894 N N . GLY A 116 ? 1.3274 0.8472 1.2689 0.0834 -0.0747 0.2664 116 GLY A N 895 C CA . GLY A 116 ? 1.1622 0.6818 1.0993 0.0656 -0.0706 0.2706 116 GLY A CA 896 C C . GLY A 116 ? 1.1130 0.6639 1.0593 0.0552 -0.0630 0.2734 116 GLY A C 897 O O . GLY A 116 ? 1.1849 0.7404 1.1301 0.0413 -0.0601 0.2765 116 GLY A O 898 N N . LEU A 117 ? 1.0796 0.6524 1.0351 0.0621 -0.0598 0.2724 117 LEU A N 899 C CA . LEU A 117 ? 1.0594 0.6609 1.0232 0.0541 -0.0522 0.2743 117 LEU A CA 900 C C . LEU A 117 ? 1.3322 0.9423 1.2922 0.0503 -0.0487 0.2763 117 LEU A C 901 O O . LEU A 117 ? 1.5309 1.1370 1.4878 0.0585 -0.0506 0.2762 117 LEU A O 902 C CB . LEU A 117 ? 1.0036 0.6244 0.9799 0.0618 -0.0495 0.2730 117 LEU A CB 903 C CG . LEU A 117 ? 1.0613 0.7079 1.0441 0.0543 -0.0414 0.2744 117 LEU A CG 904 C CD1 . LEU A 117 ? 1.1581 0.8113 1.1426 0.0440 -0.0384 0.2759 117 LEU A CD1 905 C CD2 . LEU A 117 ? 0.9585 0.6233 0.9527 0.0614 -0.0375 0.2742 117 LEU A CD2 906 N N . ILE A 118 ? 1.3452 0.9684 1.3063 0.0388 -0.0441 0.2785 118 ILE A N 907 C CA . ILE A 118 ? 1.1878 0.8201 1.1465 0.0342 -0.0414 0.2808 118 ILE A CA 908 C C . ILE A 118 ? 1.2729 0.9314 1.2410 0.0312 -0.0352 0.2804 118 ILE A C 909 O O . ILE A 118 ? 1.3706 1.0399 1.3440 0.0265 -0.0319 0.2802 118 ILE A O 910 C CB . ILE A 118 ? 1.0620 0.6850 1.0133 0.0237 -0.0422 0.2845 118 ILE A CB 911 C CG1 . ILE A 118 ? 1.0109 0.6076 0.9511 0.0279 -0.0472 0.2858 118 ILE A CG1 912 C CG2 . ILE A 118 ? 1.0564 0.6987 1.0101 0.0161 -0.0379 0.2875 118 ILE A CG2 913 C CD1 . ILE A 118 ? 1.0426 0.6275 0.9757 0.0168 -0.0482 0.2904 118 ILE A CD1 914 N N . THR A 119 ? 1.2956 0.9635 1.2660 0.0347 -0.0337 0.2805 119 THR A N 915 C CA . THR A 119 ? 1.2594 0.9494 1.2383 0.0324 -0.0279 0.2802 119 THR A CA 916 C C . THR A 119 ? 1.1109 0.8090 1.0886 0.0284 -0.0266 0.2830 119 THR A C 917 O O . THR A 119 ? 1.1640 0.8603 1.1401 0.0327 -0.0286 0.2843 119 THR A O 918 C CB . THR A 119 ? 1.3478 1.0463 1.3346 0.0401 -0.0261 0.2784 119 THR A CB 919 O OG1 . THR A 119 ? 1.3552 1.0510 1.3455 0.0431 -0.0262 0.2767 119 THR A OG1 920 C CG2 . THR A 119 ? 1.2764 0.9941 1.2705 0.0369 -0.0198 0.2785 119 THR A CG2 921 N N . TRP A 120 ? 1.0740 0.7822 1.0530 0.0208 -0.0236 0.2845 120 TRP A N 922 C CA . TRP A 120 ? 0.8941 0.6127 0.8733 0.0159 -0.0223 0.2881 120 TRP A CA 923 C C . TRP A 120 ? 0.9469 0.6853 0.9347 0.0157 -0.0167 0.2873 120 TRP A C 924 O O . TRP A 120 ? 1.1166 0.8621 1.1068 0.0125 -0.0140 0.2872 120 TRP A O 925 C CB . TRP A 120 ? 0.8296 0.5438 0.8035 0.0075 -0.0240 0.2919 120 TRP A CB 926 C CG . TRP A 120 ? 1.1218 0.8445 1.0949 0.0021 -0.0240 0.2971 120 TRP A CG 927 C CD1 . TRP A 120 ? 1.0646 0.7920 1.0381 0.0042 -0.0244 0.2993 120 TRP A CD1 928 C CD2 . TRP A 120 ? 1.2922 1.0227 1.2652 -0.0068 -0.0238 0.3021 120 TRP A CD2 929 N NE1 . TRP A 120 ? 1.2158 0.9531 1.1892 -0.0028 -0.0245 0.3052 120 TRP A NE1 930 C CE2 . TRP A 120 ? 1.3798 1.1195 1.3530 -0.0097 -0.0241 0.3071 120 TRP A CE2 931 C CE3 . TRP A 120 ? 1.1883 0.9207 1.1617 -0.0128 -0.0235 0.3036 120 TRP A CE3 932 C CZ2 . TRP A 120 ? 1.3722 1.1233 1.3462 -0.0186 -0.0244 0.3137 120 TRP A CZ2 933 C CZ3 . TRP A 120 ? 1.0916 0.8354 1.0656 -0.0215 -0.0238 0.3102 120 TRP A CZ3 934 C CH2 . TRP A 120 ? 1.1968 0.9501 1.1713 -0.0243 -0.0242 0.3151 120 TRP A CH2 935 N N . ASP A 121 ? 1.0287 0.7754 1.0213 0.0196 -0.0149 0.2871 121 ASP A N 936 C CA . ASP A 121 ? 1.1064 0.8696 1.1058 0.0188 -0.0099 0.2877 121 ASP A CA 937 C C . ASP A 121 ? 1.0420 0.8130 1.0406 0.0153 -0.0110 0.2928 121 ASP A C 938 O O . ASP A 121 ? 0.9266 0.6908 0.9203 0.0146 -0.0150 0.2955 121 ASP A O 939 C CB . ASP A 121 ? 1.2214 0.9903 1.2274 0.0241 -0.0065 0.2856 121 ASP A CB 940 C CG . ASP A 121 ? 1.3944 1.1551 1.4009 0.0280 -0.0069 0.2823 121 ASP A CG 941 O OD1 . ASP A 121 ? 1.5709 1.3258 1.5750 0.0263 -0.0074 0.2807 121 ASP A OD1 942 O OD2 . ASP A 121 ? 1.3719 1.1337 1.3822 0.0330 -0.0067 0.2822 121 ASP A OD2 943 N N . ALA A 122 ? 1.0547 0.8395 1.0577 0.0133 -0.0076 0.2948 122 ALA A N 944 C CA . ALA A 122 ? 0.9742 0.7694 0.9775 0.0095 -0.0087 0.3009 122 ALA A CA 945 C C . ALA A 122 ? 0.9388 0.7509 0.9491 0.0108 -0.0040 0.3027 122 ALA A C 946 O O . ALA A 122 ? 0.8286 0.6415 0.8411 0.0131 -0.0004 0.2997 122 ALA A O 947 C CB . ALA A 122 ? 0.6857 0.4755 0.6830 0.0028 -0.0122 0.3043 122 ALA A CB 948 N N . PRO A 123 ? 0.9042 0.7296 0.9177 0.0100 -0.0040 0.3082 123 PRO A N 949 C CA . PRO A 123 ? 0.7609 0.5989 0.7810 0.0139 0.0011 0.3088 123 PRO A CA 950 C C . PRO A 123 ? 0.7242 0.5752 0.7452 0.0110 0.0012 0.3146 123 PRO A C 951 O O . PRO A 123 ? 0.6896 0.5434 0.7077 0.0050 -0.0027 0.3194 123 PRO A O 952 C CB . PRO A 123 ? 0.7253 0.5718 0.7502 0.0170 0.0022 0.3112 123 PRO A CB 953 C CG . PRO A 123 ? 0.8069 0.6518 0.8276 0.0127 -0.0032 0.3152 123 PRO A CG 954 C CD . PRO A 123 ? 0.8445 0.6737 0.8571 0.0082 -0.0071 0.3131 123 PRO A CD 955 N N . ALA A 124 ? 0.7043 0.5635 0.7291 0.0153 0.0054 0.3153 124 ALA A N 956 C CA . ALA A 124 ? 1.0908 0.9651 1.1169 0.0136 0.0054 0.3219 124 ALA A CA 957 C C . ALA A 124 ? 1.0674 0.9569 1.0992 0.0204 0.0098 0.3260 124 ALA A C 958 O O . ALA A 124 ? 0.8857 0.7692 0.9196 0.0266 0.0138 0.3221 124 ALA A O 959 C CB . ALA A 124 ? 0.8401 0.7083 0.8629 0.0123 0.0054 0.3200 124 ALA A CB 960 N N . ILE A 125 ? 0.9237 0.8333 0.9579 0.0190 0.0089 0.3346 125 ILE A N 961 C CA . ILE A 125 ? 0.8851 0.8096 0.9233 0.0272 0.0132 0.3393 125 ILE A CA 962 C C . ILE A 125 ? 1.0344 0.9687 1.0716 0.0271 0.0130 0.3438 125 ILE A C 963 O O . ILE A 125 ? 1.3217 1.2654 1.3579 0.0188 0.0090 0.3486 125 ILE A O 964 C CB . ILE A 125 ? 0.9174 0.8640 0.9604 0.0286 0.0134 0.3474 125 ILE A CB 965 C CG1 . ILE A 125 ? 1.0475 0.9877 1.0917 0.0272 0.0127 0.3446 125 ILE A CG1 966 C CG2 . ILE A 125 ? 0.7453 0.7029 0.7914 0.0405 0.0188 0.3509 125 ILE A CG2 967 C CD1 . ILE A 125 ? 1.0359 0.9994 1.0848 0.0289 0.0130 0.3528 125 ILE A CD1 968 N N . THR A 126 ? 0.9021 0.8351 0.9395 0.0363 0.0173 0.3431 126 THR A N 969 C CA . THR A 126 ? 0.6991 0.6417 0.7353 0.0380 0.0175 0.3475 126 THR A CA 970 C C . THR A 126 ? 0.8920 0.8504 0.9302 0.0502 0.0218 0.3537 126 THR A C 971 O O . THR A 126 ? 0.8274 0.7749 0.8652 0.0598 0.0263 0.3503 126 THR A O 972 C CB . THR A 126 ? 0.8108 0.7334 0.8427 0.0379 0.0183 0.3404 126 THR A CB 973 O OG1 . THR A 126 ? 0.8627 0.7707 0.8935 0.0468 0.0230 0.3350 126 THR A OG1 974 C CG2 . THR A 126 ? 0.9705 0.8769 0.9995 0.0283 0.0145 0.3340 126 THR A CG2 975 N N . LYS A 127 ? 0.9301 0.9141 0.9697 0.0501 0.0204 0.3629 127 LYS A N 976 C CA . LYS A 127 ? 0.9785 0.9790 1.0185 0.0637 0.0242 0.3691 127 LYS A CA 977 C C . LYS A 127 ? 1.0771 1.0773 1.1142 0.0642 0.0241 0.3698 127 LYS A C 978 O O . LYS A 127 ? 1.3386 1.3519 1.3760 0.0544 0.0202 0.3740 127 LYS A O 979 C CB . LYS A 127 ? 1.0583 1.0947 1.1017 0.0653 0.0232 0.3800 127 LYS A CB 980 C CG . LYS A 127 ? 1.1953 1.2400 1.2420 0.0568 0.0205 0.3817 127 LYS A CG 981 C CD . LYS A 127 ? 1.0490 1.1030 1.0977 0.0698 0.0245 0.3841 127 LYS A CD 982 C CE . LYS A 127 ? 1.2934 1.3824 1.3454 0.0670 0.0223 0.3934 127 LYS A CE 983 N NZ . LYS A 127 ? 1.1015 1.2277 1.1544 0.0572 0.0179 0.4033 127 LYS A NZ 984 N N . SER A 128 ? 0.7369 0.7209 0.7705 0.0748 0.0281 0.3657 128 SER A N 985 C CA . SER A 128 ? 0.7432 0.7252 0.7738 0.0750 0.0280 0.3659 128 SER A CA 986 C C . SER A 128 ? 1.0487 1.0370 1.0766 0.0923 0.0325 0.3699 128 SER A C 987 O O . SER A 128 ? 1.1370 1.1188 1.1642 0.1023 0.0358 0.3687 128 SER A O 988 C CB . SER A 128 ? 0.6904 0.6415 0.7175 0.0685 0.0277 0.3555 128 SER A CB 989 O OG . SER A 128 ? 0.6474 0.5761 0.6709 0.0771 0.0320 0.3493 128 SER A OG 990 N N . SER A 129 ? 1.0392 1.0398 1.0650 0.0968 0.0327 0.3747 129 SER A N 991 C CA . SER A 129 ? 0.9704 0.9784 0.9924 0.1151 0.0367 0.3789 129 SER A CA 992 C C . SER A 129 ? 0.9195 0.8948 0.9353 0.1214 0.0401 0.3717 129 SER A C 993 O O . SER A 129 ? 1.1700 1.1257 1.1845 0.1113 0.0389 0.3654 129 SER A O 994 C CB . SER A 129 ? 1.0498 1.0901 1.0719 0.1182 0.0353 0.3882 129 SER A CB 995 O OG . SER A 129 ? 1.1786 1.2452 1.2059 0.1050 0.0308 0.3937 129 SER A OG 996 N N . CYS A 130 ? 0.8678 0.8356 0.8792 0.1378 0.0443 0.3720 130 CYS A N 997 C CA . CYS A 130 ? 0.9280 0.8637 0.9320 0.1436 0.0476 0.3660 130 CYS A CA 998 C C . CYS A 130 ? 1.1072 1.0509 1.1052 0.1607 0.0501 0.3716 130 CYS A C 999 O O . CYS A 130 ? 1.2897 1.2636 1.2891 0.1711 0.0500 0.3792 130 CYS A O 1000 C CB . CYS A 130 ? 0.6846 0.5955 0.6866 0.1470 0.0507 0.3598 130 CYS A CB 1001 S SG . CYS A 130 ? 1.2523 1.1561 1.2610 0.1285 0.0478 0.3533 130 CYS A SG 1002 N N . VAL A 131 ? 1.0704 0.9885 1.0609 0.1639 0.0521 0.3680 131 VAL A N 1003 C CA . VAL A 131 ? 0.9507 0.8731 0.9341 0.1807 0.0544 0.3731 131 VAL A CA 1004 C C . VAL A 131 ? 1.1844 1.0694 1.1582 0.1890 0.0580 0.3680 131 VAL A C 1005 O O . VAL A 131 ? 1.3151 1.1718 1.2872 0.1774 0.0582 0.3608 131 VAL A O 1006 C CB . VAL A 131 ? 1.0567 0.9911 1.0399 0.1753 0.0524 0.3768 131 VAL A CB 1007 C CG1 . VAL A 131 ? 1.0551 0.9990 1.0311 0.1937 0.0546 0.3832 131 VAL A CG1 1008 C CG2 . VAL A 131 ? 1.1013 1.0679 1.0936 0.1634 0.0485 0.3810 131 VAL A CG2 1009 N N . VAL A 132 ? 1.1282 1.0133 1.0950 0.2089 0.0607 0.3715 132 VAL A N 1010 C CA . VAL A 132 ? 1.3845 1.2331 1.3401 0.2176 0.0639 0.3679 132 VAL A CA 1011 C C . VAL A 132 ? 1.8431 1.6924 1.7914 0.2259 0.0641 0.3728 132 VAL A C 1012 O O . VAL A 132 ? 1.8712 1.7529 1.8213 0.2348 0.0633 0.3799 132 VAL A O 1013 C CB . VAL A 132 ? 1.3974 1.2386 1.3481 0.2363 0.0671 0.3673 132 VAL A CB 1014 C CG1 . VAL A 132 ? 1.4621 1.2947 1.4182 0.2287 0.0677 0.3618 132 VAL A CG1 1015 C CG2 . VAL A 132 ? 1.4090 1.2894 1.3610 0.2539 0.0667 0.3748 132 VAL A CG2 1016 N N . ASP A 133 ? 2.2889 2.1046 2.2289 0.2222 0.0652 0.3696 133 ASP A N 1017 C CA . ASP A 133 ? 2.4449 2.2515 2.3744 0.2350 0.0664 0.3743 133 ASP A CA 1018 C C . ASP A 133 ? 2.6096 2.3710 2.5303 0.2304 0.0682 0.3684 133 ASP A C 1019 O O . ASP A 133 ? 2.6306 2.3771 2.5529 0.2124 0.0671 0.3639 133 ASP A O 1020 C CB . ASP A 133 ? 2.3794 2.2027 2.3100 0.2288 0.0645 0.3794 133 ASP A CB 1021 C CG . ASP A 133 ? 2.3766 2.1800 2.2948 0.2389 0.0660 0.3832 133 ASP A CG 1022 O OD1 . ASP A 133 ? 2.4119 2.1917 2.3206 0.2529 0.0683 0.3826 133 ASP A OD1 1023 O OD2 . ASP A 133 ? 2.3663 2.1760 2.2837 0.2329 0.0649 0.3868 133 ASP A OD2 1024 N N . VAL A 134 ? 2.6916 2.4312 2.6025 0.2465 0.0708 0.3682 134 VAL A N 1025 C CA . VAL A 134 ? 2.6793 2.3758 2.5826 0.2400 0.0725 0.3622 134 VAL A CA 1026 C C . VAL A 134 ? 2.4424 2.1066 2.3315 0.2461 0.0736 0.3647 134 VAL A C 1027 O O . VAL A 134 ? 2.5176 2.1657 2.3969 0.2641 0.0755 0.3662 134 VAL A O 1028 C CB . VAL A 134 ? 2.4033 2.0928 2.3082 0.2476 0.0749 0.3569 134 VAL A CB 1029 C CG1 . VAL A 134 ? 2.4068 2.0671 2.2989 0.2666 0.0781 0.3558 134 VAL A CG1 1030 C CG2 . VAL A 134 ? 2.3921 2.0710 2.3039 0.2277 0.0748 0.3496 134 VAL A CG2 1031 N N . THR A 135 ? 2.3136 1.9720 2.2018 0.2312 0.0718 0.3661 135 THR A N 1032 C CA . THR A 135 ? 2.2270 1.8485 2.1077 0.2178 0.0722 0.3628 135 THR A CA 1033 C C . THR A 135 ? 2.2199 1.8571 2.1082 0.1976 0.0696 0.3617 135 THR A C 1034 O O . THR A 135 ? 1.9103 1.5809 1.8067 0.1980 0.0679 0.3646 135 THR A O 1035 C CB . THR A 135 ? 2.1945 1.7874 2.0604 0.2268 0.0730 0.3682 135 THR A CB 1036 O OG1 . THR A 135 ? 2.3022 1.8584 2.1615 0.2125 0.0737 0.3642 135 THR A OG1 1037 C CG2 . THR A 135 ? 2.2468 1.8566 2.1109 0.2275 0.0712 0.3762 135 THR A CG2 1038 N N . TYR A 136 ? 2.4242 2.0372 2.3078 0.1822 0.0694 0.3589 136 TYR A N 1039 C CA . TYR A 136 ? 2.5099 2.1209 2.3997 0.1620 0.0686 0.3517 136 TYR A CA 1040 C C . TYR A 136 ? 2.5299 2.1170 2.4182 0.1623 0.0713 0.3453 136 TYR A C 1041 O O . TYR A 136 ? 2.4638 2.0534 2.3591 0.1505 0.0714 0.3386 136 TYR A O 1042 C CB . TYR A 136 ? 2.7422 2.3883 2.6458 0.1539 0.0663 0.3491 136 TYR A CB 1043 C CG . TYR A 136 ? 2.7663 2.4433 2.6744 0.1562 0.0641 0.3550 136 TYR A CG 1044 C CD1 . TYR A 136 ? 2.7999 2.4818 2.7079 0.1441 0.0626 0.3557 136 TYR A CD1 1045 C CD2 . TYR A 136 ? 2.7586 2.4633 2.6723 0.1690 0.0638 0.3592 136 TYR A CD2 1046 C CE1 . TYR A 136 ? 2.7716 2.4825 2.6843 0.1462 0.0610 0.3610 136 TYR A CE1 1047 C CE2 . TYR A 136 ? 2.7467 2.4804 2.6647 0.1707 0.0622 0.3648 136 TYR A CE2 1048 C CZ . TYR A 136 ? 2.7486 2.4851 2.6664 0.1591 0.0608 0.3655 136 TYR A CZ 1049 O OH . TYR A 136 ? 2.7454 2.5120 2.6681 0.1610 0.0595 0.3710 136 TYR A OH 1050 N N . PHE A 137 ? 2.5625 2.1262 2.4410 0.1767 0.0735 0.3475 137 PHE A N 1051 C CA . PHE A 137 ? 2.5775 2.1136 2.4522 0.1789 0.0768 0.3418 137 PHE A CA 1052 C C . PHE A 137 ? 2.6492 2.1672 2.5238 0.1577 0.0775 0.3360 137 PHE A C 1053 O O . PHE A 137 ? 2.7288 2.2407 2.5994 0.1458 0.0760 0.3384 137 PHE A O 1054 C CB . PHE A 137 ? 2.4810 1.9859 2.3416 0.1943 0.0789 0.3452 137 PHE A CB 1055 C CG . PHE A 137 ? 2.4011 1.9205 2.2606 0.2183 0.0794 0.3490 137 PHE A CG 1056 C CD1 . PHE A 137 ? 2.3724 1.9241 2.2426 0.2255 0.0793 0.3477 137 PHE A CD1 1057 C CD2 . PHE A 137 ? 2.4525 1.9534 2.2995 0.2341 0.0800 0.3546 137 PHE A CD2 1058 C CE1 . PHE A 137 ? 2.3971 1.9638 2.2654 0.2482 0.0799 0.3515 137 PHE A CE1 1059 C CE2 . PHE A 137 ? 2.4627 1.9785 2.3077 0.2580 0.0806 0.3582 137 PHE A CE2 1060 C CZ . PHE A 137 ? 2.4039 1.9538 2.2597 0.2647 0.0806 0.3564 137 PHE A CZ 1061 N N . PRO A 138 ? 2.7550 2.2648 2.6335 0.1532 0.0801 0.3287 138 PRO A N 1062 C CA . PRO A 138 ? 2.7797 2.2870 2.6612 0.1633 0.0833 0.3241 138 PRO A CA 1063 C C . PRO A 138 ? 3.1686 2.6952 3.0523 0.1855 0.0833 0.3274 138 PRO A C 1064 O O . PRO A 138 ? 3.1147 2.6753 3.0063 0.1887 0.0803 0.3316 138 PRO A O 1065 C CB . PRO A 138 ? 2.7658 2.2912 2.6593 0.1483 0.0830 0.3184 138 PRO A CB 1066 C CG . PRO A 138 ? 2.7330 2.2765 2.6310 0.1336 0.0790 0.3200 138 PRO A CG 1067 C CD . PRO A 138 ? 2.7059 2.2316 2.5927 0.1337 0.0782 0.3254 138 PRO A CD 1068 N N . PHE A 139 ? 3.1982 2.7024 3.0744 0.2003 0.0870 0.3252 139 PHE A N 1069 C CA . PHE A 139 ? 3.2470 2.7652 3.1232 0.2236 0.0880 0.3271 139 PHE A CA 1070 C C . PHE A 139 ? 3.1160 2.6831 3.0053 0.2275 0.0850 0.3315 139 PHE A C 1071 O O . PHE A 139 ? 3.1144 2.6998 3.0020 0.2419 0.0834 0.3378 139 PHE A O 1072 C CB . PHE A 139 ? 3.0682 2.5632 2.9411 0.2295 0.0929 0.3194 139 PHE A CB 1073 C CG . PHE A 139 ? 2.9243 2.4290 2.7953 0.2547 0.0946 0.3195 139 PHE A CG 1074 C CD1 . PHE A 139 ? 2.8878 2.3803 2.7471 0.2749 0.0947 0.3224 139 PHE A CD1 1075 C CD2 . PHE A 139 ? 2.8351 2.3577 2.7145 0.2586 0.0965 0.3159 139 PHE A CD2 1076 C CE1 . PHE A 139 ? 2.8467 2.3495 2.7035 0.2990 0.0962 0.3215 139 PHE A CE1 1077 C CE2 . PHE A 139 ? 2.7871 2.3197 2.6640 0.2825 0.0980 0.3156 139 PHE A CE2 1078 C CZ . PHE A 139 ? 2.7890 2.3124 2.6546 0.3029 0.0978 0.3178 139 PHE A CZ 1079 N N . ASP A 140 ? 2.9521 2.5401 2.8538 0.2138 0.0840 0.3287 140 ASP A N 1080 C CA . ASP A 140 ? 2.5319 2.1643 2.4461 0.2150 0.0810 0.3327 140 ASP A CA 1081 C C . ASP A 140 ? 2.5118 2.1645 2.4367 0.1944 0.0775 0.3320 140 ASP A C 1082 O O . ASP A 140 ? 2.4913 2.1473 2.4237 0.1840 0.0779 0.3275 140 ASP A O 1083 C CB . ASP A 140 ? 2.3398 1.9872 2.2607 0.2234 0.0830 0.3310 140 ASP A CB 1084 C CG . ASP A 140 ? 2.2483 1.8759 2.1597 0.2439 0.0870 0.3290 140 ASP A CG 1085 O OD1 . ASP A 140 ? 2.3051 1.9224 2.2063 0.2591 0.0873 0.3317 140 ASP A OD1 1086 O OD2 . ASP A 140 ? 2.1807 1.8015 2.0944 0.2448 0.0901 0.3241 140 ASP A OD2 1087 N N . ASN A 141 ? 2.4419 2.1105 2.3682 0.1896 0.0741 0.3363 141 ASN A N 1088 C CA . ASN A 141 ? 2.3501 2.0387 2.2865 0.1722 0.0708 0.3345 141 ASN A CA 1089 C C . ASN A 141 ? 2.1339 1.8615 2.0797 0.1774 0.0684 0.3397 141 ASN A C 1090 O O . ASN A 141 ? 2.2234 1.9666 2.1672 0.1921 0.0685 0.3460 141 ASN A O 1091 C CB . ASN A 141 ? 2.2413 1.9243 2.1747 0.1594 0.0685 0.3346 141 ASN A CB 1092 C CG . ASN A 141 ? 2.2637 1.9469 2.1893 0.1699 0.0682 0.3415 141 ASN A CG 1093 O OD1 . ASN A 141 ? 2.2686 1.9273 2.1838 0.1794 0.0705 0.3430 141 ASN A OD1 1094 N ND2 . ASN A 141 ? 2.2314 1.9415 2.1620 0.1679 0.0654 0.3459 141 ASN A ND2 1095 N N . GLN A 142 ? 1.6989 1.4424 1.6547 0.1646 0.0662 0.3370 142 GLN A N 1096 C CA . GLN A 142 ? 1.4192 1.1985 1.3846 0.1647 0.0635 0.3415 142 GLN A CA 1097 C C . GLN A 142 ? 1.2908 1.0792 1.2618 0.1472 0.0596 0.3391 142 GLN A C 1098 O O . GLN A 142 ? 1.2760 1.0482 1.2472 0.1344 0.0593 0.3325 142 GLN A O 1099 C CB . GLN A 142 ? 1.4995 1.2897 1.4714 0.1679 0.0644 0.3412 142 GLN A CB 1100 C CG . GLN A 142 ? 1.5646 1.3703 1.5348 0.1880 0.0663 0.3473 142 GLN A CG 1101 C CD . GLN A 142 ? 1.5538 1.3858 1.5329 0.1887 0.0654 0.3500 142 GLN A CD 1102 O OE1 . GLN A 142 ? 1.5525 1.3839 1.5381 0.1752 0.0642 0.3464 142 GLN A OE1 1103 N NE2 . GLN A 142 ? 1.5467 1.4051 1.5262 0.2044 0.0655 0.3568 142 GLN A NE2 1104 N N . GLN A 143 ? 1.1447 0.9582 1.1191 0.1471 0.0570 0.3446 143 GLN A N 1105 C CA . GLN A 143 ? 1.1113 0.9312 1.0898 0.1319 0.0535 0.3422 143 GLN A CA 1106 C C . GLN A 143 ? 0.8835 0.7287 0.8716 0.1257 0.0505 0.3439 143 GLN A C 1107 O O . GLN A 143 ? 0.8523 0.7225 0.8437 0.1332 0.0499 0.3510 143 GLN A O 1108 C CB . GLN A 143 ? 1.1695 0.9964 1.1443 0.1340 0.0528 0.3469 143 GLN A CB 1109 C CG . GLN A 143 ? 1.2538 1.0794 1.2303 0.1191 0.0501 0.3432 143 GLN A CG 1110 C CD . GLN A 143 ? 1.4032 1.2452 1.3789 0.1209 0.0490 0.3494 143 GLN A CD 1111 O OE1 . GLN A 143 ? 1.5534 1.4087 1.5270 0.1334 0.0502 0.3567 143 GLN A OE1 1112 N NE2 . GLN A 143 ? 1.3693 1.2121 1.3466 0.1092 0.0468 0.3468 143 GLN A NE2 1113 N N . CYS A 144 ? 0.6844 0.5246 0.6764 0.1121 0.0483 0.3378 144 CYS A N 1114 C CA . CYS A 144 ? 0.9355 0.7981 0.9356 0.1057 0.0449 0.3400 144 CYS A CA 1115 C C . CYS A 144 ? 0.8143 0.6773 0.8160 0.0923 0.0413 0.3367 144 CYS A C 1116 O O . CYS A 144 ? 0.9167 0.7619 0.9170 0.0843 0.0409 0.3291 144 CYS A O 1117 C CB . CYS A 144 ? 0.9952 0.8543 0.9992 0.1043 0.0455 0.3370 144 CYS A CB 1118 S SG . CYS A 144 ? 2.0053 1.8636 2.0070 0.1219 0.0503 0.3411 144 CYS A SG 1119 N N . ASN A 145 ? 0.6501 0.5339 0.6545 0.0901 0.0387 0.3424 145 ASN A N 1120 C CA . ASN A 145 ? 0.8803 0.7626 0.8854 0.0783 0.0355 0.3393 145 ASN A CA 1121 C C . ASN A 145 ? 0.6309 0.5213 0.6413 0.0688 0.0318 0.3383 145 ASN A C 1122 O O . ASN A 145 ? 0.7357 0.6438 0.7499 0.0707 0.0309 0.3440 145 ASN A O 1123 C CB . ASN A 145 ? 0.9572 0.8557 0.9618 0.0794 0.0345 0.3460 145 ASN A CB 1124 C CG . ASN A 145 ? 1.0809 0.9675 1.0792 0.0851 0.0373 0.3456 145 ASN A CG 1125 O OD1 . ASN A 145 ? 0.9161 0.7816 0.9096 0.0890 0.0401 0.3411 145 ASN A OD1 1126 N ND2 . ASN A 145 ? 1.2961 1.1970 1.2942 0.0851 0.0364 0.3511 145 ASN A ND2 1127 N N . LEU A 146 ? 0.7772 0.6560 0.7873 0.0587 0.0293 0.3319 146 LEU A N 1128 C CA . LEU A 146 ? 1.0241 0.9088 1.0380 0.0494 0.0252 0.3314 146 LEU A CA 1129 C C . LEU A 146 ? 0.9291 0.8149 0.9422 0.0410 0.0220 0.3313 146 LEU A C 1130 O O . LEU A 146 ? 1.0008 0.8711 1.0112 0.0378 0.0218 0.3251 146 LEU A O 1131 C CB . LEU A 146 ? 1.0864 0.9548 1.1003 0.0462 0.0252 0.3235 146 LEU A CB 1132 C CG . LEU A 146 ? 0.9452 0.8134 0.9606 0.0534 0.0283 0.3241 146 LEU A CG 1133 C CD1 . LEU A 146 ? 0.9806 0.8302 0.9948 0.0513 0.0295 0.3160 146 LEU A CD1 1134 C CD2 . LEU A 146 ? 0.9974 0.8846 1.0177 0.0518 0.0260 0.3302 146 LEU A CD2 1135 N N . THR A 147 ? 0.7130 0.6179 0.7284 0.0374 0.0194 0.3389 147 THR A N 1136 C CA . THR A 147 ? 0.6721 0.5771 0.6865 0.0297 0.0166 0.3395 147 THR A CA 1137 C C . THR A 147 ? 0.6380 0.5404 0.6531 0.0183 0.0118 0.3385 147 THR A C 1138 O O . THR A 147 ? 0.8507 0.7680 0.8680 0.0136 0.0094 0.3447 147 THR A O 1139 C CB . THR A 147 ? 0.6431 0.5702 0.6585 0.0323 0.0170 0.3489 147 THR A CB 1140 O OG1 . THR A 147 ? 0.7041 0.6280 0.7169 0.0430 0.0213 0.3487 147 THR A OG1 1141 C CG2 . THR A 147 ? 0.6891 0.6187 0.7039 0.0229 0.0137 0.3506 147 THR A CG2 1142 N N . PHE A 148 ? 0.6812 0.5652 0.6937 0.0136 0.0102 0.3316 148 PHE A N 1143 C CA . PHE A 148 ? 0.9080 0.7852 0.9196 0.0039 0.0055 0.3305 148 PHE A CA 1144 C C . PHE A 148 ? 0.8961 0.7731 0.9062 -0.0035 0.0025 0.3331 148 PHE A C 1145 O O . PHE A 148 ? 0.6599 0.5323 0.6690 -0.0010 0.0040 0.3311 148 PHE A O 1146 C CB . PHE A 148 ? 0.9492 0.8051 0.9586 0.0044 0.0053 0.3211 148 PHE A CB 1147 C CG . PHE A 148 ? 0.9951 0.8498 1.0060 0.0107 0.0081 0.3181 148 PHE A CG 1148 C CD1 . PHE A 148 ? 1.0808 0.9346 1.0919 0.0187 0.0127 0.3163 148 PHE A CD1 1149 C CD2 . PHE A 148 ? 0.7278 0.5819 0.7395 0.0084 0.0064 0.3178 148 PHE A CD2 1150 C CE1 . PHE A 148 ? 0.7728 0.6246 0.7851 0.0240 0.0154 0.3142 148 PHE A CE1 1151 C CE2 . PHE A 148 ? 0.8276 0.6824 0.8414 0.0141 0.0091 0.3160 148 PHE A CE2 1152 C CZ . PHE A 148 ? 0.7616 0.6148 0.7758 0.0218 0.0137 0.3141 148 PHE A CZ 1153 N N . GLY A 149 ? 0.6278 0.5097 0.6375 -0.0133 -0.0017 0.3379 149 GLY A N 1154 C CA . GLY A 149 ? 0.6353 0.5117 0.6428 -0.0219 -0.0053 0.3395 149 GLY A CA 1155 C C . GLY A 149 ? 0.6447 0.5171 0.6497 -0.0334 -0.0102 0.3424 149 GLY A C 1156 O O . GLY A 149 ? 0.6435 0.5262 0.6498 -0.0352 -0.0106 0.3459 149 GLY A O 1157 N N . SER A 150 ? 0.6554 0.5158 0.6570 -0.0423 -0.0142 0.3426 150 SER A N 1158 C CA . SER A 150 ? 0.6685 0.5199 0.6660 -0.0540 -0.0192 0.3448 150 SER A CA 1159 C C . SER A 150 ? 0.8005 0.6753 0.7993 -0.0637 -0.0209 0.3546 150 SER A C 1160 O O . SER A 150 ? 1.2490 1.1492 1.2515 -0.0630 -0.0191 0.3611 150 SER A O 1161 C CB . SER A 150 ? 0.6826 0.5151 0.6757 -0.0619 -0.0234 0.3435 150 SER A CB 1162 O OG . SER A 150 ? 0.7589 0.5829 0.7470 -0.0749 -0.0283 0.3469 150 SER A OG 1163 N N . TRP A 151 ? 0.7894 0.6575 0.7845 -0.0731 -0.0245 0.3563 151 TRP A N 1164 C CA . TRP A 151 ? 1.1326 1.0263 1.1287 -0.0840 -0.0263 0.3663 151 TRP A CA 1165 C C . TRP A 151 ? 1.4044 1.2969 1.3956 -0.1013 -0.0314 0.3714 151 TRP A C 1166 O O . TRP A 151 ? 1.5439 1.4634 1.5358 -0.1118 -0.0328 0.3802 151 TRP A O 1167 C CB . TRP A 151 ? 1.1385 1.0310 1.1335 -0.0857 -0.0272 0.3668 151 TRP A CB 1168 C CG . TRP A 151 ? 1.0399 0.9590 1.0354 -0.0979 -0.0295 0.3769 151 TRP A CG 1169 C CD1 . TRP A 151 ? 1.0917 1.0070 1.0812 -0.1155 -0.0345 0.3815 151 TRP A CD1 1170 C CD2 . TRP A 151 ? 1.1058 1.0604 1.1076 -0.0937 -0.0268 0.3839 151 TRP A CD2 1171 N NE1 . TRP A 151 ? 1.2209 1.1698 1.2127 -0.1237 -0.0352 0.3908 151 TRP A NE1 1172 C CE2 . TRP A 151 ? 1.2588 1.2336 1.2585 -0.1098 -0.0306 0.3927 151 TRP A CE2 1173 C CE3 . TRP A 151 ? 1.0970 1.0682 1.1054 -0.0778 -0.0217 0.3836 151 TRP A CE3 1174 C CZ2 . TRP A 151 ? 1.2672 1.2820 1.2717 -0.1099 -0.0293 0.4014 151 TRP A CZ2 1175 C CZ3 . TRP A 151 ? 1.1192 1.1271 1.1322 -0.0766 -0.0203 0.3924 151 TRP A CZ3 1176 C CH2 . TRP A 151 ? 1.1884 1.2195 1.1996 -0.0923 -0.0241 0.4012 151 TRP A CH2 1177 N N . THR A 152 ? 1.5783 1.4407 1.5641 -0.1048 -0.0343 0.3659 152 THR A N 1178 C CA . THR A 152 ? 1.6800 1.5352 1.6594 -0.1233 -0.0399 0.3698 152 THR A CA 1179 C C . THR A 152 ? 1.5580 1.3978 1.5353 -0.1256 -0.0420 0.3671 152 THR A C 1180 O O . THR A 152 ? 1.3688 1.2002 1.3398 -0.1425 -0.0473 0.3697 152 THR A O 1181 C CB . THR A 152 ? 1.4441 1.2725 1.4156 -0.1320 -0.0440 0.3678 152 THR A CB 1182 O OG1 . THR A 152 ? 1.4806 1.2750 1.4489 -0.1218 -0.0441 0.3586 152 THR A OG1 1183 C CG2 . THR A 152 ? 1.2645 1.1072 1.2380 -0.1299 -0.0424 0.3707 152 THR A CG2 1184 N N . TYR A 153 ? 1.2506 1.0872 1.2324 -0.1102 -0.0382 0.3619 153 TYR A N 1185 C CA . TYR A 153 ? 1.0374 0.8568 1.0176 -0.1101 -0.0402 0.3584 153 TYR A CA 1186 C C . TYR A 153 ? 1.2167 1.0557 1.2034 -0.1000 -0.0359 0.3596 153 TYR A C 1187 O O . TYR A 153 ? 1.0957 0.9378 1.0869 -0.0839 -0.0305 0.3551 153 TYR A O 1188 C CB . TYR A 153 ? 1.0767 0.8612 1.0537 -0.1007 -0.0410 0.3485 153 TYR A CB 1189 C CG . TYR A 153 ? 1.1576 0.9144 1.1261 -0.1099 -0.0461 0.3465 153 TYR A CG 1190 C CD1 . TYR A 153 ? 1.2898 1.0270 1.2509 -0.1248 -0.0528 0.3475 153 TYR A CD1 1191 C CD2 . TYR A 153 ? 1.0669 0.8152 1.0336 -0.1036 -0.0446 0.3435 153 TYR A CD2 1192 C CE1 . TYR A 153 ? 1.3247 1.0331 1.2764 -0.1327 -0.0575 0.3455 153 TYR A CE1 1193 C CE2 . TYR A 153 ? 1.2669 0.9897 1.2250 -0.1110 -0.0489 0.3425 153 TYR A CE2 1194 C CZ . TYR A 153 ? 1.3540 1.0558 1.3045 -0.1251 -0.0552 0.3434 153 TYR A CZ 1195 O OH . TYR A 153 ? 1.4780 1.1518 1.4188 -0.1318 -0.0593 0.3423 153 TYR A OH 1196 N N . ASN A 154 ? 1.2107 1.0615 1.1967 -0.1099 -0.0384 0.3655 154 ASN A N 1197 C CA . ASN A 154 ? 1.2558 1.1226 1.2465 -0.1009 -0.0347 0.3671 154 ASN A CA 1198 C C . ASN A 154 ? 1.1671 1.0103 1.1590 -0.0887 -0.0335 0.3587 154 ASN A C 1199 O O . ASN A 154 ? 1.1927 1.0055 1.1809 -0.0894 -0.0370 0.3521 154 ASN A O 1200 C CB . ASN A 154 ? 1.3115 1.1949 1.2995 -0.1142 -0.0378 0.3708 154 ASN A CB 1201 C CG . ASN A 154 ? 1.4549 1.3121 1.4350 -0.1287 -0.0446 0.3621 154 ASN A CG 1202 O OD1 . ASN A 154 ? 1.5380 1.3657 1.5161 -0.1238 -0.0467 0.3534 154 ASN A OD1 1203 N ND2 . ASN A 154 ? 1.4705 1.3370 1.4452 -0.1469 -0.0483 0.3643 154 ASN A ND2 1204 N N . GLY A 155 ? 1.0349 0.8930 1.0315 -0.0777 -0.0287 0.3594 155 GLY A N 1205 C CA . GLY A 155 ? 1.0711 0.9125 1.0691 -0.0684 -0.0277 0.3531 155 GLY A CA 1206 C C . GLY A 155 ? 1.2281 1.0520 1.2219 -0.0762 -0.0336 0.3462 155 GLY A C 1207 O O . GLY A 155 ? 1.2135 1.0262 1.2080 -0.0682 -0.0331 0.3381 155 GLY A O 1208 N N . ASN A 156 ? 1.3573 1.1823 1.3456 -0.0912 -0.0386 0.3445 156 ASN A N 1209 C CA . ASN A 156 ? 1.5196 1.3290 1.5017 -0.0990 -0.0440 0.3322 156 ASN A CA 1210 C C . ASN A 156 ? 1.4608 1.2333 1.4363 -0.1050 -0.0500 0.3291 156 ASN A C 1211 O O . ASN A 156 ? 1.4189 1.1690 1.3879 -0.1093 -0.0551 0.3183 156 ASN A O 1212 C CB . ASN A 156 ? 1.6521 1.4862 1.6312 -0.1129 -0.0456 0.3310 156 ASN A CB 1213 C CG . ASN A 156 ? 1.7077 1.5345 1.6824 -0.1169 -0.0492 0.3168 156 ASN A CG 1214 O OD1 . ASN A 156 ? 1.7915 1.5912 1.7585 -0.1263 -0.0552 0.3088 156 ASN A OD1 1215 N ND2 . ASN A 156 ? 1.6865 1.5371 1.6653 -0.1093 -0.0455 0.3136 156 ASN A ND2 1216 N N . GLN A 157 ? 1.4412 1.2078 1.4176 -0.1053 -0.0495 0.3390 157 GLN A N 1217 C CA . GLN A 157 ? 1.3708 1.1018 1.3418 -0.1064 -0.0542 0.3383 157 GLN A CA 1218 C C . GLN A 157 ? 1.2968 1.0217 1.2725 -0.0879 -0.0494 0.3342 157 GLN A C 1219 O O . GLN A 157 ? 1.2406 0.9386 1.2131 -0.0814 -0.0521 0.3273 157 GLN A O 1220 C CB . GLN A 157 ? 1.4505 1.1842 1.4173 -0.1191 -0.0557 0.3450 157 GLN A CB 1221 C CG . GLN A 157 ? 1.4595 1.2011 1.4200 -0.1400 -0.0602 0.3474 157 GLN A CG 1222 C CD . GLN A 157 ? 1.2899 1.0601 1.2519 -0.1506 -0.0585 0.3594 157 GLN A CD 1223 O OE1 . GLN A 157 ? 1.1156 0.9182 1.0856 -0.1412 -0.0523 0.3635 157 GLN A OE1 1224 N NE2 . GLN A 157 ? 1.2830 1.0423 1.2365 -0.1681 -0.0632 0.3609 157 GLN A NE2 1225 N N . VAL A 158 ? 1.2180 0.9694 1.2001 -0.0790 -0.0419 0.3358 158 VAL A N 1226 C CA . VAL A 158 ? 1.0663 0.8162 1.0513 -0.0632 -0.0365 0.3290 158 VAL A CA 1227 C C . VAL A 158 ? 1.0733 0.8477 1.0650 -0.0537 -0.0297 0.3301 158 VAL A C 1228 O O . VAL A 158 ? 1.1342 0.9319 1.1283 -0.0550 -0.0265 0.3354 158 VAL A O 1229 C CB . VAL A 158 ? 1.1412 0.8912 1.1237 -0.0628 -0.0348 0.3279 158 VAL A CB 1230 C CG1 . VAL A 158 ? 1.1993 0.9504 1.1842 -0.0486 -0.0295 0.3213 158 VAL A CG1 1231 C CG2 . VAL A 158 ? 1.0074 0.7312 0.9819 -0.0713 -0.0409 0.3267 158 VAL A CG2 1232 N N . ASP A 159 ? 1.0125 0.7818 1.0067 -0.0441 -0.0276 0.3255 159 ASP A N 1233 C CA . ASP A 159 ? 1.1376 0.9271 1.1366 -0.0354 -0.0209 0.3260 159 ASP A CA 1234 C C . ASP A 159 ? 1.1450 0.9287 1.1437 -0.0260 -0.0170 0.3186 159 ASP A C 1235 O O . ASP A 159 ? 1.1675 0.9322 1.1638 -0.0239 -0.0195 0.3131 159 ASP A O 1236 C CB . ASP A 159 ? 1.2819 1.0735 1.2839 -0.0325 -0.0206 0.3272 159 ASP A CB 1237 C CG . ASP A 159 ? 1.2683 1.0827 1.2735 -0.0261 -0.0138 0.3301 159 ASP A CG 1238 O OD1 . ASP A 159 ? 1.1792 1.0030 1.1845 -0.0214 -0.0094 0.3290 159 ASP A OD1 1239 O OD2 . ASP A 159 ? 1.3373 1.1591 1.3446 -0.0252 -0.0132 0.3335 159 ASP A OD2 1240 N N . ILE A 160 ? 1.0210 0.8203 1.0218 -0.0205 -0.0115 0.3187 160 ILE A N 1241 C CA . ILE A 160 ? 0.9593 0.7533 0.9596 -0.0138 -0.0086 0.3123 160 ILE A CA 1242 C C . ILE A 160 ? 1.0607 0.8617 1.0632 -0.0062 -0.0030 0.3100 160 ILE A C 1243 O O . ILE A 160 ? 0.9506 0.7666 0.9544 -0.0046 0.0002 0.3144 160 ILE A O 1244 C CB . ILE A 160 ? 1.2233 1.0248 1.2229 -0.0157 -0.0083 0.3143 160 ILE A CB 1245 C CG1 . ILE A 160 ? 1.3306 1.1534 1.3330 -0.0133 -0.0044 0.3194 160 ILE A CG1 1246 C CG2 . ILE A 160 ? 1.1237 0.9193 1.1205 -0.0254 -0.0137 0.3179 160 ILE A CG2 1247 C CD1 . ILE A 160 ? 1.3067 1.1315 1.3099 -0.0057 -0.0001 0.3155 160 ILE A CD1 1248 N N . PHE A 161 ? 1.2146 1.0045 1.2171 -0.0017 -0.0021 0.3040 161 PHE A N 1249 C CA . PHE A 161 ? 1.1867 0.9804 1.1908 0.0038 0.0030 0.3018 161 PHE A CA 1250 C C . PHE A 161 ? 1.1188 0.9092 1.1224 0.0076 0.0059 0.2967 161 PHE A C 1251 O O . PHE A 161 ? 1.1456 0.9269 1.1485 0.0078 0.0036 0.2930 161 PHE A O 1252 C CB . PHE A 161 ? 1.2506 1.0375 1.2564 0.0049 0.0020 0.3006 161 PHE A CB 1253 C CG . PHE A 161 ? 1.3418 1.1306 1.3486 0.0011 -0.0014 0.3058 161 PHE A CG 1254 C CD1 . PHE A 161 ? 1.4066 1.2098 1.4146 0.0004 0.0011 0.3116 161 PHE A CD1 1255 C CD2 . PHE A 161 ? 1.4344 1.2101 1.4403 -0.0020 -0.0076 0.3054 161 PHE A CD2 1256 C CE1 . PHE A 161 ? 1.4729 1.2798 1.4821 -0.0040 -0.0024 0.3173 161 PHE A CE1 1257 C CE2 . PHE A 161 ? 1.5261 1.3019 1.5329 -0.0068 -0.0115 0.3106 161 PHE A CE2 1258 C CZ . PHE A 161 ? 1.4864 1.2793 1.4953 -0.0081 -0.0089 0.3168 161 PHE A CZ 1259 N N . ASN A 162 ? 0.9279 0.7248 0.9315 0.0107 0.0108 0.2970 162 ASN A N 1260 C CA . ASN A 162 ? 1.0720 0.8643 1.0754 0.0137 0.0140 0.2926 162 ASN A CA 1261 C C . ASN A 162 ? 1.1632 0.9482 1.1681 0.0146 0.0150 0.2892 162 ASN A C 1262 O O . ASN A 162 ? 1.1116 0.8981 1.1175 0.0143 0.0161 0.2911 162 ASN A O 1263 C CB . ASN A 162 ? 1.1140 0.9121 1.1160 0.0166 0.0187 0.2946 162 ASN A CB 1264 C CG . ASN A 162 ? 1.3317 1.1357 1.3329 0.0168 0.0205 0.2989 162 ASN A CG 1265 O OD1 . ASN A 162 ? 1.4334 1.2423 1.4356 0.0144 0.0177 0.3022 162 ASN A OD1 1266 N ND2 . ASN A 162 ? 1.4352 1.2382 1.4340 0.0192 0.0250 0.2995 162 ASN A ND2 1267 N N . ALA A 163 ? 1.3523 1.1316 1.3581 0.0157 0.0150 0.2853 163 ALA A N 1268 C CA . ALA A 163 ? 1.4439 1.2188 1.4524 0.0169 0.0163 0.2831 163 ALA A CA 1269 C C . ALA A 163 ? 1.5461 1.3233 1.5545 0.0165 0.0222 0.2842 163 ALA A C 1270 O O . ALA A 163 ? 1.6625 1.4397 1.6734 0.0163 0.0239 0.2851 163 ALA A O 1271 C CB . ALA A 163 ? 1.4270 1.1979 1.4369 0.0183 0.0154 0.2800 163 ALA A CB 1272 N N . LEU A 164 ? 1.5111 1.2898 1.5164 0.0167 0.0254 0.2848 164 LEU A N 1273 C CA . LEU A 164 ? 1.4217 1.2005 1.4244 0.0160 0.0304 0.2869 164 LEU A CA 1274 C C . LEU A 164 ? 1.2438 1.0237 1.2423 0.0180 0.0320 0.2887 164 LEU A C 1275 O O . LEU A 164 ? 1.1646 0.9467 1.1633 0.0199 0.0299 0.2884 164 LEU A O 1276 C CB . LEU A 164 ? 1.2586 1.0321 1.2622 0.0143 0.0348 0.2853 164 LEU A CB 1277 C CG . LEU A 164 ? 1.2225 0.9912 1.2274 0.0146 0.0361 0.2820 164 LEU A CG 1278 C CD1 . LEU A 164 ? 1.3096 1.0737 1.3101 0.0156 0.0390 0.2818 164 LEU A CD1 1279 C CD2 . LEU A 164 ? 1.1739 0.9411 1.1816 0.0117 0.0401 0.2824 164 LEU A CD2 1280 N N . ASP A 165 ? 1.0727 0.8517 1.0674 0.0178 0.0358 0.2917 165 ASP A N 1281 C CA . ASP A 165 ? 1.2004 0.9807 1.1906 0.0209 0.0373 0.2952 165 ASP A CA 1282 C C . ASP A 165 ? 1.1758 0.9468 1.1628 0.0230 0.0402 0.2935 165 ASP A C 1283 O O . ASP A 165 ? 1.1549 0.9208 1.1363 0.0255 0.0430 0.2963 165 ASP A O 1284 C CB . ASP A 165 ? 1.4911 1.2735 1.4778 0.0200 0.0400 0.2999 165 ASP A CB 1285 C CG . ASP A 165 ? 1.5433 1.3365 1.5339 0.0184 0.0372 0.3027 165 ASP A CG 1286 O OD1 . ASP A 165 ? 1.6187 1.4189 1.6122 0.0194 0.0333 0.3034 165 ASP A OD1 1287 O OD2 . ASP A 165 ? 1.4511 1.2460 1.4418 0.0157 0.0391 0.3049 165 ASP A OD2 1288 N N . SER A 166 ? 1.1439 0.9123 1.1342 0.0224 0.0392 0.2894 166 SER A N 1289 C CA . SER A 166 ? 1.2735 1.0359 1.2623 0.0252 0.0410 0.2883 166 SER A CA 1290 C C . SER A 166 ? 1.2701 1.0384 1.2641 0.0257 0.0375 0.2861 166 SER A C 1291 O O . SER A 166 ? 1.3046 1.0766 1.3023 0.0231 0.0345 0.2844 166 SER A O 1292 C CB . SER A 166 ? 1.4522 1.2022 1.4384 0.0222 0.0455 0.2863 166 SER A CB 1293 O OG . SER A 166 ? 1.5937 1.3365 1.5734 0.0209 0.0488 0.2893 166 SER A OG 1294 N N . GLY A 167 ? 1.3025 1.0715 1.2969 0.0294 0.0378 0.2867 167 GLY A N 1295 C CA . GLY A 167 ? 1.2877 1.0619 1.2868 0.0294 0.0352 0.2852 167 GLY A CA 1296 C C . GLY A 167 ? 1.2578 1.0237 1.2580 0.0280 0.0382 0.2820 167 GLY A C 1297 O O . GLY A 167 ? 1.2375 0.9945 1.2345 0.0291 0.0425 0.2823 167 GLY A O 1298 N N . ASP A 168 ? 1.3294 1.0977 1.3339 0.0254 0.0361 0.2796 168 ASP A N 1299 C CA . ASP A 168 ? 1.4127 1.1763 1.4200 0.0239 0.0390 0.2775 168 ASP A CA 1300 C C . ASP A 168 ? 1.4841 1.2452 1.4921 0.0266 0.0421 0.2781 168 ASP A C 1301 O O . ASP A 168 ? 1.3413 1.1099 1.3523 0.0292 0.0398 0.2794 168 ASP A O 1302 C CB . ASP A 168 ? 1.4030 1.1719 1.4152 0.0229 0.0352 0.2763 168 ASP A CB 1303 C CG . ASP A 168 ? 1.5356 1.3024 1.5518 0.0218 0.0385 0.2753 168 ASP A CG 1304 O OD1 . ASP A 168 ? 1.5659 1.3259 1.5808 0.0194 0.0437 0.2751 168 ASP A OD1 1305 O OD2 . ASP A 168 ? 1.6571 1.4291 1.6777 0.0230 0.0360 0.2756 168 ASP A OD2 1306 N N . LEU A 169 ? 1.6373 1.3874 1.6421 0.0257 0.0475 0.2778 169 LEU A N 1307 C CA . LEU A 169 ? 1.6121 1.3570 1.6180 0.0277 0.0514 0.2782 169 LEU A CA 1308 C C . LEU A 169 ? 1.6541 1.4011 1.6660 0.0243 0.0531 0.2768 169 LEU A C 1309 O O . LEU A 169 ? 1.8072 1.5620 1.8242 0.0267 0.0518 0.2777 169 LEU A O 1310 C CB . LEU A 169 ? 1.5309 1.2599 1.5299 0.0278 0.0566 0.2787 169 LEU A CB 1311 C CG . LEU A 169 ? 1.5480 1.2756 1.5410 0.0324 0.0550 0.2813 169 LEU A CG 1312 C CD1 . LEU A 169 ? 1.6049 1.3141 1.5901 0.0336 0.0599 0.2825 169 LEU A CD1 1313 C CD2 . LEU A 169 ? 1.4593 1.1997 1.4555 0.0390 0.0516 0.2840 169 LEU A CD2 1314 N N . SER A 170 ? 1.5375 1.2796 1.5493 0.0189 0.0559 0.2756 170 SER A N 1315 C CA . SER A 170 ? 1.6968 1.4411 1.7148 0.0153 0.0591 0.2756 170 SER A CA 1316 C C . SER A 170 ? 1.7331 1.4832 1.7571 0.0183 0.0597 0.2767 170 SER A C 1317 O O . SER A 170 ? 1.8069 1.5505 1.8322 0.0159 0.0662 0.2771 170 SER A O 1318 C CB . SER A 170 ? 1.1028 0.8560 1.1249 0.0139 0.0555 0.2757 170 SER A CB 1319 O OG . SER A 170 ? 0.9469 0.7110 0.9742 0.0179 0.0500 0.2763 170 SER A OG 1320 N N . ASP A 171 ? 1.7186 1.4805 1.7458 0.0225 0.0536 0.2777 171 ASP A N 1321 C CA . ASP A 171 ? 1.6602 1.4297 1.6927 0.0258 0.0538 0.2801 171 ASP A CA 1322 C C . ASP A 171 ? 1.5495 1.3185 1.5793 0.0303 0.0537 0.2814 171 ASP A C 1323 O O . ASP A 171 ? 1.4273 1.2072 1.4604 0.0337 0.0508 0.2842 171 ASP A O 1324 C CB . ASP A 171 ? 1.6329 1.4157 1.6700 0.0275 0.0474 0.2816 171 ASP A CB 1325 C CG . ASP A 171 ? 1.7234 1.5072 1.7623 0.0255 0.0457 0.2809 171 ASP A CG 1326 O OD1 . ASP A 171 ? 1.8428 1.6240 1.8845 0.0226 0.0512 0.2815 171 ASP A OD1 1327 O OD2 . ASP A 171 ? 1.7248 1.5122 1.7625 0.0268 0.0392 0.2805 171 ASP A OD2 1328 N N . PHE A 172 ? 1.5715 1.3284 1.5951 0.0307 0.0569 0.2804 172 PHE A N 1329 C CA . PHE A 172 ? 1.5239 1.2784 1.5451 0.0367 0.0583 0.2826 172 PHE A CA 1330 C C . PHE A 172 ? 1.5773 1.3247 1.6008 0.0381 0.0650 0.2835 172 PHE A C 1331 O O . PHE A 172 ? 1.5694 1.3073 1.5933 0.0328 0.0702 0.2817 172 PHE A O 1332 C CB . PHE A 172 ? 1.4535 1.1967 1.4665 0.0377 0.0589 0.2819 172 PHE A CB 1333 C CG . PHE A 172 ? 1.3813 1.1158 1.3905 0.0446 0.0624 0.2842 172 PHE A CG 1334 C CD1 . PHE A 172 ? 1.3240 1.0706 1.3359 0.0521 0.0603 0.2882 172 PHE A CD1 1335 C CD2 . PHE A 172 ? 1.4000 1.1134 1.4021 0.0439 0.0679 0.2829 172 PHE A CD2 1336 C CE1 . PHE A 172 ? 1.3517 1.0904 1.3600 0.0607 0.0639 0.2910 172 PHE A CE1 1337 C CE2 . PHE A 172 ? 1.4283 1.1305 1.4257 0.0520 0.0712 0.2850 172 PHE A CE2 1338 C CZ . PHE A 172 ? 1.4249 1.1402 1.4257 0.0613 0.0693 0.2891 172 PHE A CZ 1339 N N . ILE A 173 ? 1.6480 1.4006 1.6732 0.0451 0.0656 0.2870 173 ILE A N 1340 C CA . ILE A 173 ? 1.6676 1.4180 1.6969 0.0478 0.0715 0.2891 173 ILE A CA 1341 C C . ILE A 173 ? 1.6795 1.4156 1.7031 0.0557 0.0764 0.2902 173 ILE A C 1342 O O . ILE A 173 ? 1.7283 1.4744 1.7535 0.0642 0.0752 0.2945 173 ILE A O 1343 C CB . ILE A 173 ? 1.5906 1.3639 1.6282 0.0500 0.0674 0.2936 173 ILE A CB 1344 C CG1 . ILE A 173 ? 1.4926 1.2756 1.5334 0.0435 0.0621 0.2920 173 ILE A CG1 1345 C CG2 . ILE A 173 ? 1.5376 1.3115 1.5800 0.0530 0.0738 0.2968 173 ILE A CG2 1346 C CD1 . ILE A 173 ? 1.3206 1.1236 1.3676 0.0443 0.0571 0.2962 173 ILE A CD1 1347 N N . GLU A 174 ? 1.7608 1.4731 1.7771 0.0528 0.0817 0.2865 174 GLU A N 1348 C CA . GLU A 174 ? 1.7679 1.4582 1.7757 0.0595 0.0868 0.2862 174 GLU A CA 1349 C C . GLU A 174 ? 1.8144 1.5062 1.8233 0.0724 0.0898 0.2901 174 GLU A C 1350 O O . GLU A 174 ? 1.7871 1.4709 1.7961 0.0734 0.0957 0.2862 174 GLU A O 1351 C CB . GLU A 174 ? 1.8012 1.4654 1.8034 0.0515 0.0947 0.2816 174 GLU A CB 1352 C CG . GLU A 174 ? 1.9010 1.5703 1.9060 0.0387 0.0936 0.2790 174 GLU A CG 1353 C CD . GLU A 174 ? 2.0579 1.7018 2.0548 0.0290 0.1004 0.2750 174 GLU A CD 1354 O OE1 . GLU A 174 ? 2.1244 1.7434 2.1128 0.0315 0.1061 0.2733 174 GLU A OE1 1355 O OE2 . GLU A 174 ? 2.1748 1.8231 2.1734 0.0187 0.1003 0.2735 174 GLU A OE2 1356 N N . ASP A 175 ? 1.6791 1.3848 1.6878 0.0812 0.0850 0.2943 175 ASP A N 1357 C CA . ASP A 175 ? 1.7020 1.4117 1.7112 0.0952 0.0876 0.2990 175 ASP A CA 1358 C C . ASP A 175 ? 1.7211 1.3980 1.7199 0.1028 0.0955 0.2960 175 ASP A C 1359 O O . ASP A 175 ? 1.8284 1.4823 1.8185 0.0978 0.0968 0.2917 175 ASP A O 1360 C CB . ASP A 175 ? 1.8301 1.5609 1.8400 0.1022 0.0813 0.3042 175 ASP A CB 1361 C CG . ASP A 175 ? 1.9377 1.6763 1.9474 0.1186 0.0837 0.3100 175 ASP A CG 1362 O OD1 . ASP A 175 ? 2.0144 1.7721 2.0308 0.1202 0.0835 0.3103 175 ASP A OD1 1363 O OD2 . ASP A 175 ? 1.9043 1.6350 1.9067 0.1292 0.0844 0.3112 175 ASP A OD2 1364 N N . VAL A 176 ? 1.6595 1.3421 1.6577 0.1120 0.0972 0.2900 176 VAL A N 1365 C CA . VAL A 176 ? 1.5591 1.2128 1.5466 0.1168 0.1033 0.2801 176 VAL A CA 1366 C C . VAL A 176 ? 1.5533 1.1876 1.5306 0.1325 0.1048 0.2866 176 VAL A C 1367 O O . VAL A 176 ? 1.6236 1.2217 1.5888 0.1345 0.1100 0.2827 176 VAL A O 1368 C CB . VAL A 176 ? 1.5668 1.2370 1.5577 0.1200 0.1039 0.2680 176 VAL A CB 1369 C CG1 . VAL A 176 ? 1.5272 1.2364 1.5269 0.1287 0.0984 0.2738 176 VAL A CG1 1370 C CG2 . VAL A 176 ? 1.5983 1.2397 1.5772 0.1292 0.1095 0.2578 176 VAL A CG2 1371 N N . GLU A 177 ? 1.5179 1.1757 1.4990 0.1436 0.1005 0.2966 177 GLU A N 1372 C CA . GLU A 177 ? 1.5774 1.2212 1.5487 0.1583 0.1010 0.3021 177 GLU A CA 1373 C C . GLU A 177 ? 1.6051 1.2605 1.5768 0.1491 0.0940 0.3041 177 GLU A C 1374 O O . GLU A 177 ? 1.5026 1.1467 1.4659 0.1557 0.0932 0.3048 177 GLU A O 1375 C CB . GLU A 177 ? 1.6529 1.3189 1.6249 0.1776 0.0996 0.3042 177 GLU A CB 1376 C CG . GLU A 177 ? 1.7330 1.4452 1.7181 0.1752 0.0939 0.3069 177 GLU A CG 1377 C CD . GLU A 177 ? 1.7962 1.5245 1.7865 0.1729 0.0943 0.2946 177 GLU A CD 1378 O OE1 . GLU A 177 ? 1.8281 1.5316 1.8128 0.1707 0.0990 0.2827 177 GLU A OE1 1379 O OE2 . GLU A 177 ? 1.7873 1.5539 1.7870 0.1724 0.0899 0.2969 177 GLU A OE2 1380 N N . TRP A 178 ? 1.7010 1.3784 1.6818 0.1349 0.0888 0.3048 178 TRP A N 1381 C CA . TRP A 178 ? 1.7322 1.4184 1.7118 0.1286 0.0829 0.3061 178 TRP A CA 1382 C C . TRP A 178 ? 1.8434 1.5208 1.8227 0.1107 0.0811 0.3009 178 TRP A C 1383 O O . TRP A 178 ? 1.8657 1.5509 1.8519 0.1002 0.0805 0.2983 178 TRP A O 1384 C CB . TRP A 178 ? 1.7594 1.4820 1.7476 0.1314 0.0774 0.3123 178 TRP A CB 1385 C CG . TRP A 178 ? 1.8475 1.5791 1.8326 0.1506 0.0786 0.3184 178 TRP A CG 1386 C CD1 . TRP A 178 ? 1.8467 1.5948 1.8359 0.1626 0.0803 0.3227 178 TRP A CD1 1387 C CD2 . TRP A 178 ? 1.8335 1.5598 1.8104 0.1610 0.0782 0.3210 178 TRP A CD2 1388 N NE1 . TRP A 178 ? 1.8571 1.6111 1.8409 0.1804 0.0809 0.3272 178 TRP A NE1 1389 C CE2 . TRP A 178 ? 1.8297 1.5701 1.8060 0.1798 0.0797 0.3263 178 TRP A CE2 1390 C CE3 . TRP A 178 ? 1.7856 1.4984 1.7556 0.1570 0.0767 0.3200 178 TRP A CE3 1391 C CZ2 . TRP A 178 ? 1.7886 1.5298 1.7575 0.1949 0.0798 0.3300 178 TRP A CZ2 1392 C CZ3 . TRP A 178 ? 1.7953 1.5082 1.7584 0.1713 0.0768 0.3245 178 TRP A CZ3 1393 C CH2 . TRP A 178 ? 1.7772 1.5040 1.7398 0.1902 0.0784 0.3292 178 TRP A CH2 1394 N N . GLU A 179 ? 1.8849 1.5471 1.8557 0.1087 0.0803 0.3001 179 GLU A N 1395 C CA . GLU A 179 ? 1.7356 1.3833 1.7027 0.0942 0.0802 0.2956 179 GLU A CA 1396 C C . GLU A 179 ? 1.5084 1.1699 1.4760 0.0876 0.0745 0.2968 179 GLU A C 1397 O O . GLU A 179 ? 1.4502 1.1063 1.4110 0.0920 0.0734 0.2997 179 GLU A O 1398 C CB . GLU A 179 ? 2.0419 1.6547 1.9966 0.0946 0.0850 0.2936 179 GLU A CB 1399 C CG . GLU A 179 ? 2.1633 1.7534 2.1152 0.0965 0.0921 0.2899 179 GLU A CG 1400 C CD . GLU A 179 ? 2.2807 1.8887 2.2439 0.0947 0.0933 0.2889 179 GLU A CD 1401 O OE1 . GLU A 179 ? 2.2923 1.9070 2.2613 0.0818 0.0932 0.2861 179 GLU A OE1 1402 O OE2 . GLU A 179 ? 2.2815 1.8982 2.2476 0.1078 0.0944 0.2917 179 GLU A OE2 1403 N N . VAL A 180 ? 1.4493 1.1275 1.4243 0.0777 0.0713 0.2945 180 VAL A N 1404 C CA . VAL A 180 ? 1.5463 1.2355 1.5212 0.0717 0.0666 0.2948 180 VAL A CA 1405 C C . VAL A 180 ? 1.5962 1.2655 1.5622 0.0655 0.0682 0.2935 180 VAL A C 1406 O O . VAL A 180 ? 1.6058 1.2637 1.5705 0.0561 0.0708 0.2897 180 VAL A O 1407 C CB . VAL A 180 ? 1.5131 1.2188 1.4961 0.0627 0.0633 0.2919 180 VAL A CB 1408 C CG1 . VAL A 180 ? 1.2865 0.9975 1.2678 0.0560 0.0597 0.2911 180 VAL A CG1 1409 C CG2 . VAL A 180 ? 1.4978 1.2252 1.4890 0.0675 0.0604 0.2946 180 VAL A CG2 1410 N N . HIS A 181 ? 1.7553 1.4227 1.7152 0.0709 0.0669 0.2975 181 HIS A N 1411 C CA . HIS A 181 ? 1.8667 1.5184 1.8176 0.0660 0.0677 0.2983 181 HIS A CA 1412 C C . HIS A 181 ? 1.8899 1.5568 1.8431 0.0587 0.0640 0.2982 181 HIS A C 1413 O O . HIS A 181 ? 2.1164 1.7749 2.0657 0.0496 0.0650 0.2968 181 HIS A O 1414 C CB . HIS A 181 ? 1.9493 1.5896 1.8918 0.0771 0.0685 0.3036 181 HIS A CB 1415 C CG . HIS A 181 ? 2.1027 1.7128 2.0365 0.0789 0.0731 0.3029 181 HIS A CG 1416 N ND1 . HIS A 181 ? 2.1565 1.7482 2.0865 0.0668 0.0761 0.2992 181 HIS A ND1 1417 C CD2 . HIS A 181 ? 2.1760 1.7706 2.1039 0.0915 0.0756 0.3054 181 HIS A CD2 1418 C CE1 . HIS A 181 ? 2.2271 1.7912 2.1488 0.0706 0.0802 0.2992 181 HIS A CE1 1419 N NE2 . HIS A 181 ? 2.2552 1.8197 2.1754 0.0861 0.0798 0.3027 181 HIS A NE2 1420 N N . GLY A 182 ? 1.4586 1.1480 1.4183 0.0624 0.0602 0.2999 182 GLY A N 1421 C CA . GLY A 182 ? 1.3606 1.0635 1.3229 0.0558 0.0571 0.2993 182 GLY A CA 1422 C C . GLY A 182 ? 1.2316 0.9566 1.2031 0.0564 0.0533 0.2988 182 GLY A C 1423 O O . GLY A 182 ? 1.0918 0.8246 1.0666 0.0635 0.0529 0.3011 182 GLY A O 1424 N N . MET A 183 ? 1.2893 1.0237 1.2647 0.0491 0.0507 0.2962 183 MET A N 1425 C CA . MET A 183 ? 1.3629 1.1167 1.3451 0.0494 0.0465 0.2970 183 MET A CA 1426 C C . MET A 183 ? 1.2085 0.9700 1.1912 0.0444 0.0439 0.2972 183 MET A C 1427 O O . MET A 183 ? 1.0748 0.8429 1.0622 0.0395 0.0411 0.2943 183 MET A O 1428 C CB . MET A 183 ? 1.6118 1.3702 1.6004 0.0462 0.0451 0.2933 183 MET A CB 1429 C CG . MET A 183 ? 1.7512 1.5269 1.7452 0.0486 0.0415 0.2961 183 MET A CG 1430 S SD . MET A 183 ? 1.0288 0.8137 1.0297 0.0433 0.0377 0.2933 183 MET A SD 1431 C CE . MET A 183 ? 1.1752 0.9784 1.1794 0.0484 0.0355 0.3002 183 MET A CE 1432 N N . PRO A 184 ? 1.1755 0.9364 1.1534 0.0465 0.0448 0.3012 184 PRO A N 1433 C CA . PRO A 184 ? 1.1147 0.8826 1.0932 0.0420 0.0432 0.3020 184 PRO A CA 1434 C C . PRO A 184 ? 1.0522 0.8372 1.0366 0.0415 0.0390 0.3035 184 PRO A C 1435 O O . PRO A 184 ? 1.1746 0.9679 1.1618 0.0454 0.0378 0.3057 184 PRO A O 1436 C CB . PRO A 184 ? 1.1089 0.8736 1.0808 0.0461 0.0454 0.3075 184 PRO A CB 1437 C CG . PRO A 184 ? 1.0558 0.8183 1.0257 0.0550 0.0466 0.3107 184 PRO A CG 1438 C CD . PRO A 184 ? 1.0555 0.8095 1.0273 0.0541 0.0474 0.3060 184 PRO A CD 1439 N N . ALA A 185 ? 0.8716 0.6612 0.8583 0.0362 0.0369 0.3025 185 ALA A N 1440 C CA . ALA A 185 ? 0.8628 0.6662 0.8540 0.0348 0.0329 0.3047 185 ALA A CA 1441 C C . ALA A 185 ? 0.9126 0.7246 0.9026 0.0351 0.0330 0.3101 185 ALA A C 1442 O O . ALA A 185 ? 0.9313 0.7377 0.9174 0.0355 0.0357 0.3110 185 ALA A O 1443 C CB . ALA A 185 ? 0.6929 0.4946 0.6877 0.0292 0.0298 0.3001 185 ALA A CB 1444 N N . VAL A 186 ? 1.0434 0.8699 1.0363 0.0354 0.0303 0.3148 186 VAL A N 1445 C CA . VAL A 186 ? 0.9630 0.8027 0.9560 0.0360 0.0300 0.3216 186 VAL A CA 1446 C C . VAL A 186 ? 0.9546 0.8057 0.9522 0.0306 0.0257 0.3239 186 VAL A C 1447 O O . VAL A 186 ? 1.1432 0.9964 1.1432 0.0288 0.0233 0.3231 186 VAL A O 1448 C CB . VAL A 186 ? 0.8905 0.7392 0.8813 0.0438 0.0323 0.3282 186 VAL A CB 1449 C CG1 . VAL A 186 ? 0.9276 0.7938 0.9195 0.0440 0.0314 0.3357 186 VAL A CG1 1450 C CG2 . VAL A 186 ? 1.0188 0.8533 1.0033 0.0484 0.0364 0.3272 186 VAL A CG2 1451 N N . LYS A 187 ? 0.8610 0.7184 0.8594 0.0271 0.0244 0.3269 187 LYS A N 1452 C CA . LYS A 187 ? 0.8382 0.7031 0.8400 0.0208 0.0199 0.3292 187 LYS A CA 1453 C C . LYS A 187 ? 0.9922 0.8781 0.9951 0.0210 0.0193 0.3387 187 LYS A C 1454 O O . LYS A 187 ? 1.2944 1.1872 1.2961 0.0228 0.0211 0.3426 187 LYS A O 1455 C CB . LYS A 187 ? 0.7617 0.6165 0.7643 0.0153 0.0176 0.3252 187 LYS A CB 1456 C CG . LYS A 187 ? 0.8434 0.7018 0.8483 0.0082 0.0125 0.3279 187 LYS A CG 1457 C CD . LYS A 187 ? 0.9429 0.7909 0.9486 0.0039 0.0098 0.3252 187 LYS A CD 1458 C CE . LYS A 187 ? 0.9751 0.8234 0.9818 -0.0041 0.0040 0.3285 187 LYS A CE 1459 N NZ . LYS A 187 ? 1.0450 0.8830 1.0525 -0.0079 0.0005 0.3276 187 LYS A NZ 1460 N N . ASN A 188 ? 0.8400 0.7385 0.8450 0.0188 0.0169 0.3433 188 ASN A N 1461 C CA . ASN A 188 ? 0.7943 0.7167 0.8003 0.0186 0.0163 0.3532 188 ASN A CA 1462 C C . ASN A 188 ? 0.8791 0.8099 0.8874 0.0076 0.0112 0.3572 188 ASN A C 1463 O O . ASN A 188 ? 1.0556 0.9723 1.0643 0.0011 0.0080 0.3523 188 ASN A O 1464 C CB . ASN A 188 ? 0.8653 0.8017 0.8710 0.0275 0.0191 0.3583 188 ASN A CB 1465 C CG . ASN A 188 ? 1.0586 0.9847 1.0604 0.0377 0.0239 0.3557 188 ASN A CG 1466 O OD1 . ASN A 188 ? 1.1476 1.0631 1.1470 0.0373 0.0254 0.3527 188 ASN A OD1 1467 N ND2 . ASN A 188 ? 0.9462 0.8756 0.9469 0.0465 0.0263 0.3577 188 ASN A ND2 1468 N N . VAL A 189 ? 0.8727 0.8266 0.8815 0.0050 0.0101 0.3663 189 VAL A N 1469 C CA . VAL A 189 ? 0.9442 0.9095 0.9541 -0.0070 0.0051 0.3717 189 VAL A CA 1470 C C . VAL A 189 ? 0.8898 0.8835 0.9005 -0.0048 0.0057 0.3803 189 VAL A C 1471 O O . VAL A 189 ? 0.7728 0.7803 0.7830 0.0065 0.0097 0.3838 189 VAL A O 1472 C CB . VAL A 189 ? 0.8546 0.8269 0.8638 -0.0154 0.0023 0.3761 189 VAL A CB 1473 C CG1 . VAL A 189 ? 0.9503 0.8949 0.9591 -0.0197 0.0002 0.3683 189 VAL A CG1 1474 C CG2 . VAL A 189 ? 0.7097 0.7031 0.7181 -0.0075 0.0060 0.3820 189 VAL A CG2 1475 N N . ILE A 190 ? 0.8990 0.9002 0.9105 -0.0152 0.0017 0.3836 190 ILE A N 1476 C CA . ILE A 190 ? 0.9318 0.9657 0.9441 -0.0159 0.0014 0.3930 190 ILE A CA 1477 C C . ILE A 190 ? 0.9715 1.0229 0.9821 -0.0330 -0.0037 0.4000 190 ILE A C 1478 O O . ILE A 190 ? 0.8837 0.9180 0.8929 -0.0472 -0.0083 0.3974 190 ILE A O 1479 C CB . ILE A 190 ? 1.1214 1.1549 1.1353 -0.0147 0.0013 0.3922 190 ILE A CB 1480 C CG1 . ILE A 190 ? 1.2312 1.2359 1.2456 -0.0044 0.0045 0.3821 190 ILE A CG1 1481 C CG2 . ILE A 190 ? 1.0917 1.1625 1.1067 -0.0086 0.0029 0.4018 190 ILE A CG2 1482 C CD1 . ILE A 190 ? 1.3023 1.3101 1.3162 0.0123 0.0100 0.3818 190 ILE A CD1 1483 N N . SER A 191 ? 1.0192 1.1057 1.0290 -0.0316 -0.0029 0.4088 191 SER A N 1484 C CA . SER A 191 ? 0.9794 1.0902 0.9861 -0.0473 -0.0068 0.4159 191 SER A CA 1485 C C . SER A 191 ? 1.1822 1.3078 1.1873 -0.0650 -0.0114 0.4196 191 SER A C 1486 O O . SER A 191 ? 1.2765 1.3891 1.2791 -0.0825 -0.0163 0.4125 191 SER A O 1487 C CB . SER A 191 ? 0.8209 0.9669 0.8268 -0.0368 -0.0035 0.4227 191 SER A CB 1488 O OG . SER A 191 ? 0.7782 0.9187 0.7866 -0.0165 0.0016 0.4203 191 SER A OG 1489 N N . TYR A 192 ? 1.1566 1.3090 1.1631 -0.0601 -0.0100 0.4250 192 TYR A N 1490 C CA . TYR A 192 ? 1.1885 1.3583 1.1933 -0.0770 -0.0139 0.4292 192 TYR A CA 1491 C C . TYR A 192 ? 1.1501 1.3478 1.1515 -0.0962 -0.0179 0.4261 192 TYR A C 1492 O O . TYR A 192 ? 0.9319 1.1086 0.9303 -0.1127 -0.0221 0.4182 192 TYR A O 1493 C CB . TYR A 192 ? 1.3786 1.5085 1.3834 -0.0865 -0.0172 0.4223 192 TYR A CB 1494 C CG . TYR A 192 ? 1.0948 1.2072 1.1040 -0.0707 -0.0139 0.4173 192 TYR A CG 1495 C CD1 . TYR A 192 ? 1.1505 1.2899 1.1619 -0.0651 -0.0123 0.4222 192 TYR A CD1 1496 C CD2 . TYR A 192 ? 0.8352 0.9078 0.8458 -0.0615 -0.0123 0.4075 192 TYR A CD2 1497 C CE1 . TYR A 192 ? 1.1807 1.3063 1.1955 -0.0516 -0.0094 0.4180 192 TYR A CE1 1498 C CE2 . TYR A 192 ? 0.9429 1.0033 0.9564 -0.0490 -0.0093 0.4027 192 TYR A CE2 1499 C CZ . TYR A 192 ? 1.2000 1.2858 1.2156 -0.0441 -0.0079 0.4081 192 TYR A CZ 1500 O OH . TYR A 192 ? 1.3469 1.4212 1.3650 -0.0323 -0.0049 0.4036 192 TYR A OH 1501 N N . GLY A 193 ? 1.2283 1.4739 1.2298 -0.0952 -0.0169 0.4318 193 GLY A N 1502 C CA . GLY A 193 ? 1.2390 1.5189 1.2375 -0.1111 -0.0197 0.4288 193 GLY A CA 1503 C C . GLY A 193 ? 1.1356 1.4060 1.1299 -0.1391 -0.0255 0.4234 193 GLY A C 1504 O O . GLY A 193 ? 1.1440 1.4394 1.1350 -0.1556 -0.0282 0.4194 193 GLY A O 1505 N N . CYS A 194 ? 1.0913 1.3246 1.0848 -0.1451 -0.0276 0.4232 194 CYS A N 1506 C CA . CYS A 194 ? 1.3977 1.6215 1.3857 -0.1717 -0.0332 0.4203 194 CYS A CA 1507 C C . CYS A 194 ? 1.3594 1.5583 1.3429 -0.1844 -0.0366 0.4093 194 CYS A C 1508 O O . CYS A 194 ? 1.5062 1.7171 1.4843 -0.2065 -0.0405 0.4049 194 CYS A O 1509 C CB . CYS A 194 ? 1.4493 1.6362 1.4368 -0.1734 -0.0346 0.4232 194 CYS A CB 1510 S SG . CYS A 194 ? 1.6884 1.8173 1.6781 -0.1572 -0.0334 0.4176 194 CYS A SG 1511 N N . CYS A 195 ? 1.1489 1.3143 1.1346 -0.1698 -0.0350 0.4045 195 CYS A N 1512 C CA . CYS A 195 ? 1.3932 1.5281 1.3752 -0.1775 -0.0381 0.3930 195 CYS A CA 1513 C C . CYS A 195 ? 1.5128 1.6209 1.4995 -0.1547 -0.0344 0.3916 195 CYS A C 1514 O O . CYS A 195 ? 1.4306 1.5628 1.4219 -0.1374 -0.0294 0.3965 195 CYS A O 1515 C CB . CYS A 195 ? 1.2387 1.3401 1.2135 -0.1992 -0.0441 0.3888 195 CYS A CB 1516 S SG . CYS A 195 ? 1.8621 1.9261 1.8369 -0.1960 -0.0450 0.3958 195 CYS A SG 1517 N N . SER A 196 ? 1.9975 2.0592 1.9829 -0.1530 -0.0362 0.3852 196 SER A N 1518 C CA . SER A 196 ? 2.1537 2.1817 2.1338 -0.1637 -0.0410 0.3732 196 SER A CA 1519 C C . SER A 196 ? 2.2627 2.2634 2.2469 -0.1441 -0.0380 0.3710 196 SER A C 1520 O O . SER A 196 ? 2.3835 2.3539 2.3680 -0.1398 -0.0386 0.3728 196 SER A O 1521 C CB . SER A 196 ? 2.1516 2.1459 2.1245 -0.1814 -0.0469 0.3708 196 SER A CB 1522 O OG . SER A 196 ? 2.1789 2.1870 2.1451 -0.2047 -0.0511 0.3684 196 SER A OG 1523 N N . GLU A 197 ? 1.8901 1.9044 1.8776 -0.1321 -0.0345 0.3682 197 GLU A N 1524 C CA . GLU A 197 ? 1.4386 1.4309 1.4298 -0.1145 -0.0312 0.3663 197 GLU A CA 1525 C C . GLU A 197 ? 1.2645 1.2634 1.2608 -0.0994 -0.0259 0.3778 197 GLU A C 1526 O O . GLU A 197 ? 1.2533 1.2664 1.2498 -0.1032 -0.0259 0.3857 197 GLU A O 1527 C CB . GLU A 197 ? 1.2005 1.1474 1.1886 -0.1173 -0.0353 0.3574 197 GLU A CB 1528 C CG . GLU A 197 ? 1.8963 1.8255 1.8766 -0.1363 -0.0423 0.3473 197 GLU A CG 1529 C CD . GLU A 197 ? 1.9937 1.9512 1.9710 -0.1486 -0.0440 0.3416 197 GLU A CD 1530 O OE1 . GLU A 197 ? 2.0756 2.0637 2.0567 -0.1407 -0.0402 0.3422 197 GLU A OE1 1531 O OE2 . GLU A 197 ? 1.9686 1.9182 1.9390 -0.1673 -0.0492 0.3370 197 GLU A OE2 1532 N N . PRO A 198 ? 1.1632 1.1530 1.1631 -0.0827 -0.0214 0.3787 198 PRO A N 1533 C CA . PRO A 198 ? 1.1661 1.1578 1.1695 -0.0697 -0.0167 0.3885 198 PRO A CA 1534 C C . PRO A 198 ? 1.2934 1.2533 1.2975 -0.0676 -0.0175 0.3826 198 PRO A C 1535 O O . PRO A 198 ? 1.3058 1.2372 1.3076 -0.0747 -0.0217 0.3771 198 PRO A O 1536 C CB . PRO A 198 ? 1.1656 1.1610 1.1714 -0.0537 -0.0112 0.3899 198 PRO A CB 1537 C CG . PRO A 198 ? 1.2685 1.2502 1.2729 -0.0571 -0.0133 0.3794 198 PRO A CG 1538 C CD . PRO A 198 ? 1.2991 1.2844 1.2997 -0.0749 -0.0195 0.3723 198 PRO A CD 1539 N N . TYR A 199 ? 1.2826 1.2492 1.2892 -0.0570 -0.0136 0.3814 199 TYR A N 1540 C CA . TYR A 199 ? 0.9071 0.8508 0.9138 -0.0541 -0.0136 0.3738 199 TYR A CA 1541 C C . TYR A 199 ? 0.8563 0.7886 0.8648 -0.0377 -0.0082 0.3662 199 TYR A C 1542 O O . TYR A 199 ? 0.8642 0.8126 0.8745 -0.0271 -0.0036 0.3686 199 TYR A O 1543 C CB . TYR A 199 ? 0.7673 0.7294 0.7748 -0.0576 -0.0141 0.3790 199 TYR A CB 1544 C CG . TYR A 199 ? 0.8496 0.8143 0.8535 -0.0771 -0.0202 0.3839 199 TYR A CG 1545 C CD1 . TYR A 199 ? 0.9646 0.8980 0.9645 -0.0861 -0.0246 0.3780 199 TYR A CD1 1546 C CD2 . TYR A 199 ? 0.8557 0.8547 0.8589 -0.0872 -0.0216 0.3942 199 TYR A CD2 1547 C CE1 . TYR A 199 ? 0.9314 0.8626 0.9263 -0.1052 -0.0304 0.3819 199 TYR A CE1 1548 C CE2 . TYR A 199 ? 0.8507 0.8514 0.8491 -0.1080 -0.0273 0.3980 199 TYR A CE2 1549 C CZ . TYR A 199 ? 0.9518 0.9158 0.9458 -0.1174 -0.0318 0.3916 199 TYR A CZ 1550 O OH . TYR A 199 ? 0.9809 0.9397 0.9684 -0.1388 -0.0377 0.3941 199 TYR A OH 1551 N N . PRO A 200 ? 0.9095 0.8144 0.9168 -0.0360 -0.0087 0.3574 200 PRO A N 1552 C CA . PRO A 200 ? 0.8088 0.7012 0.8165 -0.0237 -0.0042 0.3495 200 PRO A CA 1553 C C . PRO A 200 ? 0.9657 0.8557 0.9738 -0.0177 -0.0018 0.3458 200 PRO A C 1554 O O . PRO A 200 ? 0.9191 0.8063 0.9267 -0.0236 -0.0047 0.3460 200 PRO A O 1555 C CB . PRO A 200 ? 0.7473 0.6143 0.7532 -0.0266 -0.0070 0.3424 200 PRO A CB 1556 C CG . PRO A 200 ? 0.9479 0.8063 0.9515 -0.0380 -0.0127 0.3438 200 PRO A CG 1557 C CD . PRO A 200 ? 0.9795 0.8628 0.9838 -0.0467 -0.0144 0.3544 200 PRO A CD 1558 N N . ASP A 201 ? 0.9596 0.8512 0.9682 -0.0069 0.0031 0.3431 201 ASP A N 1559 C CA . ASP A 201 ? 0.9911 0.8800 1.0001 -0.0014 0.0052 0.3398 201 ASP A CA 1560 C C . ASP A 201 ? 1.0256 0.9039 1.0334 0.0079 0.0097 0.3335 201 ASP A C 1561 O O . ASP A 201 ? 0.8937 0.7786 0.9008 0.0133 0.0128 0.3361 201 ASP A O 1562 C CB . ASP A 201 ? 0.8612 0.7741 0.8724 0.0003 0.0059 0.3484 201 ASP A CB 1563 C CG . ASP A 201 ? 1.0825 1.0094 1.0939 0.0100 0.0100 0.3528 201 ASP A CG 1564 O OD1 . ASP A 201 ? 1.3480 1.2885 1.3594 0.0086 0.0098 0.3587 201 ASP A OD1 1565 O OD2 . ASP A 201 ? 1.1243 1.0476 1.1353 0.0192 0.0136 0.3503 201 ASP A OD2 1566 N N . VAL A 202 ? 0.9296 0.7934 0.9366 0.0097 0.0102 0.3263 202 VAL A N 1567 C CA . VAL A 202 ? 0.9926 0.8470 0.9980 0.0170 0.0145 0.3210 202 VAL A CA 1568 C C . VAL A 202 ? 0.8184 0.6787 0.8244 0.0231 0.0170 0.3227 202 VAL A C 1569 O O . VAL A 202 ? 0.6267 0.4944 0.6350 0.0212 0.0151 0.3252 202 VAL A O 1570 C CB . VAL A 202 ? 1.1428 0.9783 1.1470 0.0156 0.0141 0.3121 202 VAL A CB 1571 C CG1 . VAL A 202 ? 1.1405 0.9692 1.1443 0.0108 0.0114 0.3106 202 VAL A CG1 1572 C CG2 . VAL A 202 ? 1.2752 1.1067 1.2801 0.0142 0.0123 0.3094 202 VAL A CG2 1573 N N . THR A 203 ? 0.6524 0.5098 0.6564 0.0302 0.0211 0.3221 203 THR A N 1574 C CA . THR A 203 ? 0.6304 0.4909 0.6342 0.0377 0.0240 0.3241 203 THR A CA 1575 C C . THR A 203 ? 0.8898 0.7328 0.8905 0.0411 0.0272 0.3177 203 THR A C 1576 O O . THR A 203 ? 0.8212 0.6562 0.8182 0.0437 0.0300 0.3169 203 THR A O 1577 C CB . THR A 203 ? 0.8398 0.7149 0.8429 0.0445 0.0260 0.3321 203 THR A CB 1578 O OG1 . THR A 203 ? 1.1429 1.0387 1.1497 0.0421 0.0233 0.3393 203 THR A OG1 1579 C CG2 . THR A 203 ? 0.8230 0.6947 0.8238 0.0546 0.0298 0.3331 203 THR A CG2 1580 N N . PHE A 204 ? 0.9529 0.7906 0.9554 0.0401 0.0267 0.3138 204 PHE A N 1581 C CA . PHE A 204 ? 0.9416 0.7656 0.9418 0.0435 0.0300 0.3094 204 PHE A CA 1582 C C . PHE A 204 ? 0.8457 0.6736 0.8448 0.0527 0.0331 0.3143 204 PHE A C 1583 O O . PHE A 204 ? 0.8953 0.7373 0.8977 0.0559 0.0323 0.3193 204 PHE A O 1584 C CB . PHE A 204 ? 1.0069 0.8256 1.0097 0.0397 0.0286 0.3044 204 PHE A CB 1585 C CG . PHE A 204 ? 1.0130 0.8269 1.0163 0.0327 0.0255 0.3001 204 PHE A CG 1586 C CD1 . PHE A 204 ? 0.9866 0.7882 0.9881 0.0308 0.0271 0.2949 204 PHE A CD1 1587 C CD2 . PHE A 204 ? 0.9489 0.7703 0.9542 0.0281 0.0212 0.3020 204 PHE A CD2 1588 C CE1 . PHE A 204 ? 1.0233 0.8213 1.0255 0.0260 0.0244 0.2918 204 PHE A CE1 1589 C CE2 . PHE A 204 ? 1.0160 0.8304 1.0210 0.0229 0.0183 0.2984 204 PHE A CE2 1590 C CZ . PHE A 204 ? 1.0428 0.8461 1.0465 0.0226 0.0199 0.2932 204 PHE A CZ 1591 N N . THR A 205 ? 0.6703 0.4858 0.6642 0.0570 0.0366 0.3135 205 THR A N 1592 C CA . THR A 205 ? 0.8587 0.6746 0.8496 0.0673 0.0397 0.3186 205 THR A CA 1593 C C . THR A 205 ? 0.9856 0.7834 0.9732 0.0705 0.0430 0.3150 205 THR A C 1594 O O . THR A 205 ? 1.1601 0.9409 1.1429 0.0672 0.0448 0.3112 205 THR A O 1595 C CB . THR A 205 ? 1.0347 0.8503 1.0207 0.0703 0.0409 0.3225 205 THR A CB 1596 O OG1 . THR A 205 ? 1.0915 0.9272 1.0812 0.0686 0.0381 0.3275 205 THR A OG1 1597 C CG2 . THR A 205 ? 0.6820 0.4917 0.6625 0.0818 0.0443 0.3271 205 THR A CG2 1598 N N . LEU A 206 ? 0.9680 0.7700 0.9582 0.0767 0.0441 0.3170 206 LEU A N 1599 C CA . LEU A 206 ? 1.0780 0.8632 1.0664 0.0781 0.0471 0.3131 206 LEU A CA 1600 C C . LEU A 206 ? 1.0653 0.8402 1.0477 0.0897 0.0509 0.3168 206 LEU A C 1601 O O . LEU A 206 ? 1.0768 0.8650 1.0601 0.0997 0.0512 0.3231 206 LEU A O 1602 C CB . LEU A 206 ? 1.1049 0.9001 1.1004 0.0766 0.0459 0.3123 206 LEU A CB 1603 C CG . LEU A 206 ? 1.1594 0.9429 1.1562 0.0749 0.0482 0.3077 206 LEU A CG 1604 C CD1 . LEU A 206 ? 1.2551 1.0208 1.2487 0.0668 0.0494 0.3012 206 LEU A CD1 1605 C CD2 . LEU A 206 ? 1.0734 0.8728 1.0778 0.0702 0.0449 0.3078 206 LEU A CD2 1606 N N . LEU A 207 ? 1.0515 0.8027 1.0272 0.0887 0.0539 0.3134 207 LEU A N 1607 C CA . LEU A 207 ? 1.3102 1.0466 1.2785 0.0997 0.0574 0.3167 207 LEU A CA 1608 C C . LEU A 207 ? 1.4665 1.1829 1.4327 0.1007 0.0611 0.3129 207 LEU A C 1609 O O . LEU A 207 ? 1.6387 1.3397 1.6029 0.0910 0.0623 0.3077 207 LEU A O 1610 C CB . LEU A 207 ? 1.4430 1.1658 1.4028 0.0982 0.0579 0.3179 207 LEU A CB 1611 C CG . LEU A 207 ? 1.5655 1.3024 1.5237 0.1034 0.0563 0.3242 207 LEU A CG 1612 C CD1 . LEU A 207 ? 1.5112 1.2710 1.4771 0.0954 0.0525 0.3239 207 LEU A CD1 1613 C CD2 . LEU A 207 ? 1.6968 1.4148 1.6452 0.1018 0.0576 0.3255 207 LEU A CD2 1614 N N . LEU A 208 ? 1.3762 1.0926 1.3421 0.1132 0.0635 0.3159 208 LEU A N 1615 C CA . LEU A 208 ? 1.3964 1.0958 1.3613 0.1155 0.0676 0.3126 208 LEU A CA 1616 C C . LEU A 208 ? 1.4575 1.1327 1.4118 0.1278 0.0715 0.3145 208 LEU A C 1617 O O . LEU A 208 ? 1.4955 1.1746 1.4453 0.1370 0.0706 0.3195 208 LEU A O 1618 C CB . LEU A 208 ? 1.3013 1.0219 1.2753 0.1206 0.0673 0.3146 208 LEU A CB 1619 C CG . LEU A 208 ? 1.1812 0.9308 1.1648 0.1126 0.0622 0.3159 208 LEU A CG 1620 C CD1 . LEU A 208 ? 0.9197 0.6894 0.9107 0.1180 0.0620 0.3195 208 LEU A CD1 1621 C CD2 . LEU A 208 ? 1.2617 1.0071 1.2480 0.0970 0.0602 0.3096 208 LEU A CD2 1622 N N . LYS A 209 ? 1.3590 1.0093 1.3088 0.1290 0.0761 0.3107 209 LYS A N 1623 C CA . LYS A 209 ? 1.4733 1.1025 1.4139 0.1447 0.0801 0.3122 209 LYS A CA 1624 C C . LYS A 209 ? 1.5941 1.2109 1.5356 0.1498 0.0853 0.3083 209 LYS A C 1625 O O . LYS A 209 ? 1.6008 1.2335 1.5518 0.1434 0.0851 0.3067 209 LYS A O 1626 C CB . LYS A 209 ? 1.7545 1.3542 1.6829 0.1412 0.0809 0.3119 209 LYS A CB 1627 C CG . LYS A 209 ? 1.8899 1.4545 1.8066 0.1506 0.0857 0.3103 209 LYS A CG 1628 C CD . LYS A 209 ? 2.0731 1.6437 1.9870 0.1733 0.0867 0.3144 209 LYS A CD 1629 C CE . LYS A 209 ? 2.1992 1.7318 2.1002 0.1841 0.0914 0.3115 209 LYS A CE 1630 N NZ . LYS A 209 ? 2.2502 1.7861 2.1495 0.2061 0.0940 0.3117 209 LYS A NZ 1631 N N . ARG A 210 ? 1.6347 1.2245 1.5663 0.1623 0.0900 0.3070 210 ARG A N 1632 C CA . ARG A 210 ? 1.7463 1.3193 1.6767 0.1666 0.0958 0.3021 210 ARG A CA 1633 C C . ARG A 210 ? 2.1165 1.6450 2.0318 0.1749 0.1017 0.2973 210 ARG A C 1634 O O . ARG A 210 ? 2.0710 1.5866 1.9769 0.1899 0.1020 0.2990 210 ARG A O 1635 C CB . ARG A 210 ? 1.8372 1.4412 1.7765 0.1800 0.0952 0.3060 210 ARG A CB 1636 C CG . ARG A 210 ? 2.0105 1.6052 1.9495 0.1902 0.1012 0.3026 210 ARG A CG 1637 C CD . ARG A 210 ? 2.1526 1.7170 2.0885 0.1764 0.1064 0.2950 210 ARG A CD 1638 N NE . ARG A 210 ? 2.3016 1.8778 2.2473 0.1554 0.1049 0.2937 210 ARG A NE 1639 C CZ . ARG A 210 ? 2.4000 1.9645 2.3440 0.1375 0.1039 0.2906 210 ARG A CZ 1640 N NH1 . ARG A 210 ? 2.4299 1.9767 2.3646 0.1337 0.1022 0.2904 210 ARG A NH1 1641 N NH2 . ARG A 210 ? 2.3782 1.9555 2.3313 0.1229 0.1035 0.2888 210 ARG A NH2 1642 N N . ARG A 211 ? 2.0270 1.5337 1.9410 0.1637 0.1066 0.2906 211 ARG A N 1643 C CA . ARG A 211 ? 2.1719 1.6356 2.0737 0.1647 0.1137 0.2831 211 ARG A CA 1644 C C . ARG A 211 ? 2.2485 1.7040 2.1448 0.1882 0.1174 0.2812 211 ARG A C 1645 O O . ARG A 211 ? 2.2888 1.7708 2.1942 0.1980 0.1176 0.2831 211 ARG A O 1646 C CB . ARG A 211 ? 2.1363 1.5914 2.0426 0.1460 0.1189 0.2765 211 ARG A CB 1647 C CG . ARG A 211 ? 2.3870 1.8709 2.3081 0.1446 0.1206 0.2765 211 ARG A CG 1648 C CD . ARG A 211 ? 2.4504 1.9314 2.3775 0.1234 0.1249 0.2715 211 ARG A CD 1649 N NE . ARG A 211 ? 2.3421 1.8320 2.2720 0.1054 0.1201 0.2729 211 ARG A NE 1650 C CZ . ARG A 211 ? 2.1429 1.6648 2.0854 0.0952 0.1154 0.2757 211 ARG A CZ 1651 N NH1 . ARG A 211 ? 2.0580 1.6068 2.0130 0.0981 0.1150 0.2779 211 ARG A NH1 1652 N NH2 . ARG A 211 ? 2.0995 1.6248 2.0413 0.0818 0.1113 0.2761 211 ARG A NH2 1653 N N . SER A 212 ? 2.3054 1.7246 2.1861 0.1977 0.1196 0.2779 212 SER A N 1654 C CA . SER A 212 ? 2.2314 1.6356 2.1027 0.2221 0.1226 0.2743 212 SER A CA 1655 C C . SER A 212 ? 2.1347 1.4845 1.9890 0.2184 0.1282 0.2647 212 SER A C 1656 O O . SER A 212 ? 2.0984 1.4247 1.9451 0.2285 0.1339 0.2555 212 SER A O 1657 C CB . SER A 212 ? 2.1197 1.5399 1.9879 0.2419 0.1175 0.2817 212 SER A CB 1658 O OG . SER A 212 ? 2.0708 1.5348 1.9519 0.2375 0.1114 0.2910 212 SER A OG 1659 N N . TYR B 5 ? 2.4226 2.0834 2.2836 -0.2329 -0.0778 0.4363 5 TYR B N 1660 C CA . TYR B 5 ? 2.4437 2.1412 2.3136 -0.2270 -0.0759 0.4408 5 TYR B CA 1661 C C . TYR B 5 ? 2.5614 2.2413 2.4288 -0.2079 -0.0738 0.4398 5 TYR B C 1662 O O . TYR B 5 ? 2.5155 2.1781 2.3727 -0.2119 -0.0758 0.4471 5 TYR B O 1663 C CB . TYR B 5 ? 2.3633 2.1003 2.2491 -0.2198 -0.0727 0.4358 5 TYR B CB 1664 C CG . TYR B 5 ? 2.3470 2.0701 2.2373 -0.2070 -0.0701 0.4246 5 TYR B CG 1665 C CD1 . TYR B 5 ? 2.3373 2.0586 2.2269 -0.2184 -0.0717 0.4222 5 TYR B CD1 1666 C CD2 . TYR B 5 ? 2.3461 2.0609 2.2412 -0.1845 -0.0662 0.4166 5 TYR B CD2 1667 C CE1 . TYR B 5 ? 2.3305 2.0412 2.2244 -0.2071 -0.0695 0.4127 5 TYR B CE1 1668 C CE2 . TYR B 5 ? 2.3784 2.0825 2.2774 -0.1735 -0.0640 0.4068 5 TYR B CE2 1669 C CZ . TYR B 5 ? 2.3582 2.0602 2.2569 -0.1846 -0.0656 0.4051 5 TYR B CZ 1670 O OH . TYR B 5 ? 2.3139 2.0066 2.2166 -0.1738 -0.0636 0.3959 5 TYR B OH 1671 N N . ALA B 6 ? 2.6750 2.3571 2.5508 -0.1877 -0.0699 0.4305 6 ALA B N 1672 C CA . ALA B 6 ? 2.7876 2.4631 2.6638 -0.1682 -0.0675 0.4280 6 ALA B CA 1673 C C . ALA B 6 ? 2.7529 2.3837 2.6147 -0.1627 -0.0688 0.4290 6 ALA B C 1674 O O . ALA B 6 ? 2.7283 2.3513 2.5879 -0.1474 -0.0675 0.4283 6 ALA B O 1675 C CB . ALA B 6 ? 2.8338 2.5179 2.7206 -0.1503 -0.0635 0.4168 6 ALA B CB 1676 N N . GLN B 7 ? 2.7568 2.3587 2.6087 -0.1748 -0.0716 0.4303 7 GLN B N 1677 C CA . GLN B 7 ? 2.6827 2.2405 2.5195 -0.1735 -0.0736 0.4336 7 GLN B CA 1678 C C . GLN B 7 ? 2.5026 2.0436 2.3376 -0.1491 -0.0711 0.4287 7 GLN B C 1679 O O . GLN B 7 ? 2.5160 2.0623 2.3587 -0.1346 -0.0684 0.4188 7 GLN B O 1680 C CB . GLN B 7 ? 2.5476 2.1074 2.3758 -0.1904 -0.0768 0.4470 7 GLN B CB 1681 C CG . GLN B 7 ? 2.7825 2.3621 2.6117 -0.1838 -0.0760 0.4545 7 GLN B CG 1682 C CD . GLN B 7 ? 2.7387 2.3679 2.5839 -0.1804 -0.0738 0.4527 7 GLN B CD 1683 O OE1 . GLN B 7 ? 2.6980 2.3594 2.5502 -0.1954 -0.0749 0.4561 7 GLN B OE1 1684 N NE2 . GLN B 7 ? 2.7246 2.3605 2.5758 -0.1603 -0.0709 0.4470 7 GLN B NE2 1685 N N . LYS B 8 ? 2.4315 1.9532 2.2558 -0.1447 -0.0721 0.4360 8 LYS B N 1686 C CA . LYS B 8 ? 2.3199 1.8517 2.1466 -0.1262 -0.0700 0.4351 8 LYS B CA 1687 C C . LYS B 8 ? 2.2950 1.8313 2.1144 -0.1319 -0.0718 0.4480 8 LYS B C 1688 O O . LYS B 8 ? 2.3608 1.8657 2.1665 -0.1361 -0.0740 0.4555 8 LYS B O 1689 C CB . LYS B 8 ? 2.2978 1.7990 2.1199 -0.1055 -0.0687 0.4268 8 LYS B CB 1690 C CG . LYS B 8 ? 2.3377 1.8071 2.1464 -0.0941 -0.0697 0.4320 8 LYS B CG 1691 C CD . LYS B 8 ? 2.3550 1.8158 2.1652 -0.0714 -0.0678 0.4225 8 LYS B CD 1692 C CE . LYS B 8 ? 2.4024 1.8342 2.2003 -0.0550 -0.0686 0.4265 8 LYS B CE 1693 N NZ . LYS B 8 ? 2.3613 1.8104 2.1642 -0.0353 -0.0671 0.4195 8 LYS B NZ 1694 N N . LEU B 9 ? 2.1190 1.6968 1.9486 -0.1355 -0.0713 0.4512 9 LEU B N 1695 C CA . LEU B 9 ? 1.9557 1.5479 1.7828 -0.1337 -0.0722 0.4607 9 LEU B CA 1696 C C . LEU B 9 ? 2.0286 1.6310 1.8623 -0.1123 -0.0699 0.4530 9 LEU B C 1697 O O . LEU B 9 ? 1.9405 1.5640 1.7772 -0.1071 -0.0701 0.4574 9 LEU B O 1698 C CB . LEU B 9 ? 1.8343 1.4683 1.6698 -0.1507 -0.0735 0.4686 9 LEU B CB 1699 C CG . LEU B 9 ? 1.9158 1.5430 1.7409 -0.1721 -0.0771 0.4816 9 LEU B CG 1700 C CD1 . LEU B 9 ? 1.8545 1.5281 1.6881 -0.1834 -0.0784 0.4903 9 LEU B CD1 1701 C CD2 . LEU B 9 ? 1.9146 1.4980 1.7209 -0.1696 -0.0789 0.4897 9 LEU B CD2 1702 N N . PHE B 10 ? 2.0542 1.6451 1.8915 -0.1017 -0.0678 0.4412 10 PHE B N 1703 C CA . PHE B 10 ? 2.2428 1.8194 2.0783 -0.0800 -0.0665 0.4332 10 PHE B CA 1704 C C . PHE B 10 ? 2.4546 1.9881 2.2721 -0.0743 -0.0683 0.4392 10 PHE B C 1705 O O . PHE B 10 ? 2.4683 1.9820 2.2797 -0.0563 -0.0682 0.4354 10 PHE B O 1706 C CB . PHE B 10 ? 1.9234 1.5014 1.7681 -0.0749 -0.0641 0.4200 10 PHE B CB 1707 C CG . PHE B 10 ? 1.9008 1.4597 1.7427 -0.0545 -0.0631 0.4107 10 PHE B CG 1708 C CD1 . PHE B 10 ? 1.9328 1.5042 1.7772 -0.0400 -0.0630 0.4086 10 PHE B CD1 1709 C CD2 . PHE B 10 ? 1.9151 1.4491 1.7546 -0.0510 -0.0625 0.4031 10 PHE B CD2 1710 C CE1 . PHE B 10 ? 1.8925 1.4495 1.7348 -0.0226 -0.0629 0.4002 10 PHE B CE1 1711 C CE2 . PHE B 10 ? 1.9213 1.4421 1.7596 -0.0332 -0.0619 0.3946 10 PHE B CE2 1712 C CZ . PHE B 10 ? 1.8847 1.4173 1.7240 -0.0190 -0.0622 0.3932 10 PHE B CZ 1713 N N . ASN B 11 ? 2.6224 2.1436 2.4317 -0.0907 -0.0704 0.4495 11 ASN B N 1714 C CA . ASN B 11 ? 2.8342 2.3129 2.6270 -0.0923 -0.0723 0.4569 11 ASN B CA 1715 C C . ASN B 11 ? 2.9720 2.4237 2.7535 -0.0716 -0.0724 0.4584 11 ASN B C 1716 O O . ASN B 11 ? 3.0179 2.4498 2.7982 -0.0560 -0.0714 0.4502 11 ASN B O 1717 C CB . ASN B 11 ? 2.7890 2.2738 2.5761 -0.1121 -0.0748 0.4708 11 ASN B CB 1718 C CG . ASN B 11 ? 2.6164 2.1356 2.4078 -0.1110 -0.0751 0.4775 11 ASN B CG 1719 O OD1 . ASN B 11 ? 2.5369 2.0838 2.3393 -0.0997 -0.0735 0.4709 11 ASN B OD1 1720 N ND2 . ASN B 11 ? 2.6354 2.1509 2.4174 -0.1222 -0.0775 0.4910 11 ASN B ND2 1721 N N . ASP B 12 ? 3.0807 2.5341 2.8541 -0.0710 -0.0739 0.4697 12 ASP B N 1722 C CA . ASP B 12 ? 3.1131 2.5496 2.8768 -0.0501 -0.0742 0.4716 12 ASP B CA 1723 C C . ASP B 12 ? 2.9821 2.4538 2.7497 -0.0499 -0.0754 0.4774 12 ASP B C 1724 O O . ASP B 12 ? 3.1452 2.6102 2.9018 -0.0457 -0.0772 0.4882 12 ASP B O 1725 C CB . ASP B 12 ? 3.2612 2.6516 3.0079 -0.0483 -0.0755 0.4808 12 ASP B CB 1726 C CG . ASP B 12 ? 3.3561 2.7142 3.1024 -0.0405 -0.0746 0.4721 12 ASP B CG 1727 O OD1 . ASP B 12 ? 3.3437 2.7114 3.0983 -0.0267 -0.0731 0.4600 12 ASP B OD1 1728 O OD2 . ASP B 12 ? 3.4169 2.7411 3.1553 -0.0486 -0.0760 0.4771 12 ASP B OD2 1729 N N . LEU B 13 ? 2.6432 2.1541 2.4280 -0.0552 -0.0741 0.4698 13 LEU B N 1730 C CA . LEU B 13 ? 2.2952 1.8418 2.0900 -0.0468 -0.0744 0.4679 13 LEU B CA 1731 C C . LEU B 13 ? 2.1796 1.7094 1.9705 -0.0241 -0.0745 0.4592 13 LEU B C 1732 O O . LEU B 13 ? 2.3043 1.8521 2.0983 -0.0122 -0.0759 0.4585 13 LEU B O 1733 C CB . LEU B 13 ? 1.9697 1.5588 1.7850 -0.0560 -0.0725 0.4608 13 LEU B CB 1734 C CG . LEU B 13 ? 1.7704 1.3878 1.5941 -0.0775 -0.0725 0.4672 13 LEU B CG 1735 C CD1 . LEU B 13 ? 1.4774 1.1349 1.3214 -0.0794 -0.0701 0.4585 13 LEU B CD1 1736 C CD2 . LEU B 13 ? 1.9104 1.5431 1.7301 -0.0834 -0.0749 0.4810 13 LEU B CD2 1737 N N . PHE B 14 ? 2.0959 1.5922 1.8804 -0.0187 -0.0733 0.4532 14 PHE B N 1738 C CA . PHE B 14 ? 1.9041 1.3863 1.6869 0.0018 -0.0732 0.4434 14 PHE B CA 1739 C C . PHE B 14 ? 2.0039 1.4408 1.7697 0.0150 -0.0738 0.4469 14 PHE B C 1740 O O . PHE B 14 ? 2.0117 1.4362 1.7768 0.0318 -0.0737 0.4386 14 PHE B O 1741 C CB . PHE B 14 ? 1.7151 1.2081 1.5116 -0.0015 -0.0706 0.4303 14 PHE B CB 1742 C CG . PHE B 14 ? 1.6861 1.2236 1.5003 -0.0080 -0.0696 0.4257 14 PHE B CG 1743 C CD1 . PHE B 14 ? 1.7492 1.3092 1.5717 -0.0271 -0.0685 0.4301 14 PHE B CD1 1744 C CD2 . PHE B 14 ? 1.6742 1.2328 1.4973 0.0050 -0.0700 0.4184 14 PHE B CD2 1745 C CE1 . PHE B 14 ? 1.7375 1.3390 1.5771 -0.0316 -0.0671 0.4268 14 PHE B CE1 1746 C CE2 . PHE B 14 ? 1.6494 1.2486 1.4906 -0.0008 -0.0683 0.4150 14 PHE B CE2 1747 C CZ . PHE B 14 ? 1.6678 1.2881 1.5171 -0.0183 -0.0666 0.4193 14 PHE B CZ 1748 N N . GLU B 15 ? 1.9667 1.3801 1.7200 0.0081 -0.0746 0.4596 15 GLU B N 1749 C CA . GLU B 15 ? 2.1063 1.4795 1.8445 0.0236 -0.0752 0.4654 15 GLU B CA 1750 C C . GLU B 15 ? 2.1648 1.5448 1.8938 0.0405 -0.0778 0.4707 15 GLU B C 1751 O O . GLU B 15 ? 2.1360 1.5055 1.8600 0.0625 -0.0788 0.4667 15 GLU B O 1752 C CB . GLU B 15 ? 2.2204 1.5643 1.9489 0.0094 -0.0755 0.4779 15 GLU B CB 1753 C CG . GLU B 15 ? 2.3305 1.6320 2.0456 0.0240 -0.0761 0.4861 15 GLU B CG 1754 C CD . GLU B 15 ? 2.3979 1.6714 2.1044 0.0056 -0.0772 0.4984 15 GLU B CD 1755 O OE1 . GLU B 15 ? 2.3509 1.6308 2.0637 -0.0170 -0.0774 0.4960 15 GLU B OE1 1756 O OE2 . GLU B 15 ? 2.4839 1.7301 2.1773 0.0134 -0.0784 0.5107 15 GLU B OE2 1757 N N . ASP B 16 ? 2.1913 1.5933 1.9194 0.0297 -0.0796 0.4795 16 ASP B N 1758 C CA . ASP B 16 ? 2.2410 1.6546 1.9617 0.0429 -0.0833 0.4850 16 ASP B CA 1759 C C . ASP B 16 ? 2.1259 1.5872 1.8649 0.0403 -0.0846 0.4765 16 ASP B C 1760 O O . ASP B 16 ? 2.1604 1.6533 1.9064 0.0307 -0.0860 0.4828 16 ASP B O 1761 C CB . ASP B 16 ? 2.3191 1.7259 2.0278 0.0333 -0.0847 0.5021 16 ASP B CB 1762 C CG . ASP B 16 ? 2.3435 1.7803 2.0641 0.0074 -0.0839 0.5061 16 ASP B CG 1763 O OD1 . ASP B 16 ? 2.3115 1.7375 2.0351 -0.0090 -0.0816 0.5059 16 ASP B OD1 1764 O OD2 . ASP B 16 ? 2.3616 1.8347 2.0894 0.0035 -0.0859 0.5099 16 ASP B OD2 1765 N N . TYR B 17 ? 2.0453 1.5128 1.7939 0.0493 -0.0840 0.4626 17 TYR B N 1766 C CA . TYR B 17 ? 1.9747 1.4856 1.7423 0.0489 -0.0849 0.4548 17 TYR B CA 1767 C C . TYR B 17 ? 1.9598 1.4668 1.7285 0.0686 -0.0874 0.4437 17 TYR B C 1768 O O . TYR B 17 ? 1.9825 1.4609 1.7446 0.0765 -0.0861 0.4374 17 TYR B O 1769 C CB . TYR B 17 ? 1.9137 1.4486 1.6992 0.0305 -0.0806 0.4489 17 TYR B CB 1770 C CG . TYR B 17 ? 1.8611 1.4434 1.6681 0.0287 -0.0801 0.4436 17 TYR B CG 1771 C CD1 . TYR B 17 ? 1.8173 1.4117 1.6363 0.0379 -0.0795 0.4311 17 TYR B CD1 1772 C CD2 . TYR B 17 ? 1.8359 1.4521 1.6522 0.0177 -0.0799 0.4519 17 TYR B CD2 1773 C CE1 . TYR B 17 ? 1.7955 1.4328 1.6353 0.0363 -0.0779 0.4273 17 TYR B CE1 1774 C CE2 . TYR B 17 ? 1.7878 1.4477 1.6248 0.0169 -0.0784 0.4479 17 TYR B CE2 1775 C CZ . TYR B 17 ? 1.7960 1.4654 1.6447 0.0262 -0.0770 0.4357 17 TYR B CZ 1776 O OH . TYR B 17 ? 1.7666 1.4782 1.6362 0.0256 -0.0745 0.4325 17 TYR B OH 1777 N N . SER B 18 ? 2.0354 1.5739 1.8144 0.0763 -0.0909 0.4419 18 SER B N 1778 C CA . SER B 18 ? 2.0529 1.5997 1.8406 0.0902 -0.0931 0.4301 18 SER B CA 1779 C C . SER B 18 ? 1.9728 1.5695 1.7851 0.0853 -0.0916 0.4273 18 SER B C 1780 O O . SER B 18 ? 1.9437 1.5669 1.7625 0.0778 -0.0909 0.4357 18 SER B O 1781 C CB . SER B 18 ? 2.1527 1.6803 1.9255 0.1118 -0.1005 0.4315 18 SER B CB 1782 O OG . SER B 18 ? 2.1859 1.7458 1.9667 0.1159 -0.1045 0.4374 18 SER B OG 1783 N N . ASN B 19 ? 1.9018 1.5123 1.7286 0.0895 -0.0902 0.4158 19 ASN B N 1784 C CA . ASN B 19 ? 1.7966 1.4525 1.6479 0.0838 -0.0862 0.4129 19 ASN B CA 1785 C C . ASN B 19 ? 1.6940 1.3756 1.5540 0.0984 -0.0894 0.4142 19 ASN B C 1786 O O . ASN B 19 ? 1.6149 1.3335 1.4957 0.0987 -0.0855 0.4106 19 ASN B O 1787 C CB . ASN B 19 ? 1.7661 1.4265 1.6299 0.0781 -0.0814 0.4012 19 ASN B CB 1788 C CG . ASN B 19 ? 1.7758 1.4167 1.6363 0.0914 -0.0839 0.3915 19 ASN B CG 1789 O OD1 . ASN B 19 ? 1.7919 1.4306 1.6491 0.1069 -0.0891 0.3917 19 ASN B OD1 1790 N ND2 . ASN B 19 ? 1.7192 1.3500 1.5827 0.0855 -0.0805 0.3830 19 ASN B ND2 1791 N N . ALA B 20 ? 1.6230 1.2840 1.4665 0.1112 -0.0961 0.4197 20 ALA B N 1792 C CA . ALA B 20 ? 1.6988 1.3836 1.5495 0.1267 -0.1000 0.4217 20 ALA B CA 1793 C C . ALA B 20 ? 1.8549 1.5719 1.7110 0.1230 -0.0990 0.4332 20 ALA B C 1794 O O . ALA B 20 ? 1.9049 1.6643 1.7796 0.1275 -0.0960 0.4332 20 ALA B O 1795 C CB . ALA B 20 ? 1.7477 1.3975 1.5789 0.1438 -0.1090 0.4219 20 ALA B CB 1796 N N . LEU B 21 ? 1.8485 1.5471 1.6884 0.1151 -0.1007 0.4434 21 LEU B N 1797 C CA . LEU B 21 ? 1.8715 1.6004 1.7154 0.1126 -0.1006 0.4550 21 LEU B CA 1798 C C . LEU B 21 ? 1.8096 1.5641 1.6657 0.0933 -0.0941 0.4582 21 LEU B C 1799 O O . LEU B 21 ? 1.7499 1.4850 1.6005 0.0799 -0.0919 0.4574 21 LEU B O 1800 C CB . LEU B 21 ? 1.9648 1.6619 1.7834 0.1181 -0.1074 0.4663 21 LEU B CB 1801 C CG . LEU B 21 ? 2.0558 1.7709 1.8713 0.1105 -0.1073 0.4807 21 LEU B CG 1802 C CD1 . LEU B 21 ? 2.0037 1.7738 1.8393 0.1165 -0.1057 0.4836 21 LEU B CD1 1803 C CD2 . LEU B 21 ? 2.1165 1.7895 1.9030 0.1176 -0.1143 0.4909 21 LEU B CD2 1804 N N . ARG B 22 ? 1.7466 1.5481 1.6199 0.0934 -0.0913 0.4622 22 ARG B N 1805 C CA . ARG B 22 ? 1.5742 1.4118 1.4637 0.0788 -0.0854 0.4644 22 ARG B CA 1806 C C . ARG B 22 ? 1.5398 1.3646 1.4178 0.0639 -0.0863 0.4741 22 ARG B C 1807 O O . ARG B 22 ? 1.7005 1.5110 1.5626 0.0662 -0.0908 0.4846 22 ARG B O 1808 C CB . ARG B 22 ? 1.4990 1.3856 1.4035 0.0854 -0.0835 0.4690 22 ARG B CB 1809 C CG . ARG B 22 ? 1.5001 1.4053 1.4173 0.0996 -0.0815 0.4603 22 ARG B CG 1810 C CD . ARG B 22 ? 1.6033 1.5521 1.5292 0.1081 -0.0807 0.4671 22 ARG B CD 1811 N NE . ARG B 22 ? 1.6988 1.6815 1.6341 0.0953 -0.0768 0.4737 22 ARG B NE 1812 C CZ . ARG B 22 ? 1.6735 1.6804 1.6067 0.0955 -0.0783 0.4848 22 ARG B CZ 1813 N NH1 . ARG B 22 ? 1.6882 1.6887 1.6101 0.1081 -0.0834 0.4907 22 ARG B NH1 1814 N NH2 . ARG B 22 ? 1.6097 1.6489 1.5522 0.0835 -0.0747 0.4899 22 ARG B NH2 1815 N N . PRO B 23 ? 1.3614 1.1923 1.2472 0.0487 -0.0820 0.4712 23 PRO B N 1816 C CA . PRO B 23 ? 1.3718 1.1938 1.2491 0.0326 -0.0822 0.4795 23 PRO B CA 1817 C C . PRO B 23 ? 1.2924 1.1545 1.1774 0.0248 -0.0815 0.4911 23 PRO B C 1818 O O . PRO B 23 ? 1.1321 1.0139 1.0258 0.0104 -0.0786 0.4927 23 PRO B O 1819 C CB . PRO B 23 ? 1.3660 1.1888 1.2532 0.0215 -0.0777 0.4704 23 PRO B CB 1820 C CG . PRO B 23 ? 1.3240 1.1792 1.2316 0.0284 -0.0738 0.4616 23 PRO B CG 1821 C CD . PRO B 23 ? 1.2631 1.1115 1.1671 0.0463 -0.0767 0.4596 23 PRO B CD 1822 N N . VAL B 24 ? 1.4782 1.3545 1.3604 0.0344 -0.0843 0.4990 24 VAL B N 1823 C CA . VAL B 24 ? 1.6674 1.5776 1.5534 0.0262 -0.0842 0.5114 24 VAL B CA 1824 C C . VAL B 24 ? 1.7094 1.5879 1.5719 0.0255 -0.0896 0.5238 24 VAL B C 1825 O O . VAL B 24 ? 1.6641 1.5028 1.5093 0.0372 -0.0936 0.5231 24 VAL B O 1826 C CB . VAL B 24 ? 1.2338 1.1945 1.1362 0.0353 -0.0822 0.5130 24 VAL B CB 1827 C CG1 . VAL B 24 ? 1.2859 1.2928 1.2026 0.0219 -0.0787 0.5186 24 VAL B CG1 1828 C CG2 . VAL B 24 ? 1.1589 1.1312 1.0754 0.0471 -0.0789 0.5001 24 VAL B CG2 1829 N N . GLU B 25 ? 1.8039 1.7013 1.6660 0.0119 -0.0896 0.5354 25 GLU B N 1830 C CA . GLU B 25 ? 1.9333 1.8035 1.7738 0.0065 -0.0937 0.5492 25 GLU B CA 1831 C C . GLU B 25 ? 2.0713 1.9288 1.8978 0.0234 -0.0985 0.5559 25 GLU B C 1832 O O . GLU B 25 ? 2.0632 1.8765 1.8657 0.0260 -0.1025 0.5630 25 GLU B O 1833 C CB . GLU B 25 ? 1.9534 1.8588 1.8011 -0.0116 -0.0925 0.5598 25 GLU B CB 1834 C CG . GLU B 25 ? 2.1233 2.0449 1.9858 -0.0268 -0.0883 0.5524 25 GLU B CG 1835 C CD . GLU B 25 ? 2.1557 2.1030 2.0210 -0.0460 -0.0883 0.5632 25 GLU B CD 1836 O OE1 . GLU B 25 ? 2.2475 2.1888 2.0995 -0.0498 -0.0916 0.5768 25 GLU B OE1 1837 O OE2 . GLU B 25 ? 2.0891 2.0625 1.9691 -0.0570 -0.0853 0.5585 25 GLU B OE2 1838 N N . ASP B 26 ? 2.0124 1.9071 1.8529 0.0359 -0.0979 0.5534 26 ASP B N 1839 C CA . ASP B 26 ? 2.0098 1.8912 1.8383 0.0551 -0.1027 0.5567 26 ASP B CA 1840 C C . ASP B 26 ? 1.7501 1.6735 1.5999 0.0678 -0.1000 0.5477 26 ASP B C 1841 O O . ASP B 26 ? 1.5423 1.5064 1.4139 0.0611 -0.0943 0.5422 26 ASP B O 1842 C CB . ASP B 26 ? 2.1236 2.0085 1.9383 0.0551 -0.1066 0.5736 26 ASP B CB 1843 C CG . ASP B 26 ? 2.2469 2.1966 2.0813 0.0484 -0.1034 0.5804 26 ASP B CG 1844 O OD1 . ASP B 26 ? 2.1879 2.1793 2.0458 0.0472 -0.0982 0.5713 26 ASP B OD1 1845 O OD2 . ASP B 26 ? 2.2338 2.1943 2.0599 0.0442 -0.1057 0.5949 26 ASP B OD2 1846 N N . THR B 27 ? 1.7417 1.6559 1.5846 0.0866 -0.1039 0.5467 27 THR B N 1847 C CA . THR B 27 ? 1.7065 1.6430 1.5655 0.1002 -0.1016 0.5348 27 THR B CA 1848 C C . THR B 27 ? 1.7388 1.7400 1.6239 0.0985 -0.0949 0.5325 27 THR B C 1849 O O . THR B 27 ? 1.6975 1.7136 1.5985 0.0990 -0.0901 0.5209 27 THR B O 1850 C CB . THR B 27 ? 2.0082 1.9306 1.8555 0.1222 -0.1077 0.5359 27 THR B CB 1851 O OG1 . THR B 27 ? 2.0020 1.9532 1.8672 0.1342 -0.1045 0.5246 27 THR B OG1 1852 C CG2 . THR B 27 ? 1.9633 1.9084 1.8049 0.1282 -0.1107 0.5494 27 THR B CG2 1853 N N . ASP B 28 ? 1.8382 1.8772 1.7268 0.0962 -0.0944 0.5431 28 ASP B N 1854 C CA . ASP B 28 ? 1.8399 1.9413 1.7509 0.0988 -0.0885 0.5402 28 ASP B CA 1855 C C . ASP B 28 ? 1.7511 1.8847 1.6773 0.0819 -0.0828 0.5395 28 ASP B C 1856 O O . ASP B 28 ? 1.5596 1.7463 1.4998 0.0816 -0.0789 0.5413 28 ASP B O 1857 C CB . ASP B 28 ? 2.0147 2.1490 1.9236 0.1094 -0.0904 0.5500 28 ASP B CB 1858 C CG . ASP B 28 ? 2.1489 2.2601 2.0386 0.1038 -0.0960 0.5651 28 ASP B CG 1859 O OD1 . ASP B 28 ? 2.2046 2.2614 2.0765 0.0981 -0.1002 0.5671 28 ASP B OD1 1860 O OD2 . ASP B 28 ? 2.1421 2.2893 2.0333 0.1054 -0.0962 0.5749 28 ASP B OD2 1861 N N . LYS B 29 ? 1.7547 1.8591 1.6785 0.0685 -0.0823 0.5361 29 LYS B N 1862 C CA . LYS B 29 ? 1.5738 1.7109 1.5154 0.0568 -0.0763 0.5311 29 LYS B CA 1863 C C . LYS B 29 ? 1.4477 1.5813 1.4003 0.0626 -0.0724 0.5168 29 LYS B C 1864 O O . LYS B 29 ? 1.5384 1.6443 1.4851 0.0743 -0.0743 0.5108 29 LYS B O 1865 C CB . LYS B 29 ? 1.6057 1.7261 1.5429 0.0382 -0.0768 0.5348 29 LYS B CB 1866 C CG . LYS B 29 ? 1.6511 1.7574 1.5727 0.0298 -0.0814 0.5487 29 LYS B CG 1867 C CD . LYS B 29 ? 1.7359 1.7804 1.6356 0.0281 -0.0862 0.5503 29 LYS B CD 1868 C CE . LYS B 29 ? 1.9624 2.0020 1.8533 0.0106 -0.0879 0.5618 29 LYS B CE 1869 N NZ . LYS B 29 ? 2.0056 1.9970 1.8703 0.0096 -0.0936 0.5722 29 LYS B NZ 1870 N N . VAL B 30 ? 1.3195 1.4823 1.2877 0.0549 -0.0668 0.5116 30 VAL B N 1871 C CA . VAL B 30 ? 1.1931 1.3567 1.1721 0.0602 -0.0625 0.4991 30 VAL B CA 1872 C C . VAL B 30 ? 1.2996 1.4401 1.2800 0.0477 -0.0608 0.4936 30 VAL B C 1873 O O . VAL B 30 ? 1.3673 1.5143 1.3473 0.0345 -0.0610 0.4990 30 VAL B O 1874 C CB . VAL B 30 ? 0.9833 1.2025 0.9787 0.0652 -0.0568 0.4965 30 VAL B CB 1875 C CG1 . VAL B 30 ? 0.9902 1.2195 0.9980 0.0585 -0.0511 0.4881 30 VAL B CG1 1876 C CG2 . VAL B 30 ? 0.7601 0.9862 0.7568 0.0815 -0.0566 0.4920 30 VAL B CG2 1877 N N . LEU B 31 ? 1.2510 1.3649 1.2325 0.0520 -0.0596 0.4829 31 LEU B N 1878 C CA . LEU B 31 ? 1.1462 1.2414 1.1305 0.0422 -0.0573 0.4760 31 LEU B CA 1879 C C . LEU B 31 ? 1.1458 1.2733 1.1473 0.0444 -0.0507 0.4687 31 LEU B C 1880 O O . LEU B 31 ? 1.1045 1.2287 1.1106 0.0542 -0.0485 0.4611 31 LEU B O 1881 C CB . LEU B 31 ? 1.1058 1.1496 1.0787 0.0456 -0.0603 0.4690 31 LEU B CB 1882 C CG . LEU B 31 ? 1.1323 1.1444 1.1016 0.0358 -0.0599 0.4624 31 LEU B CG 1883 C CD1 . LEU B 31 ? 1.1754 1.1391 1.1286 0.0414 -0.0644 0.4587 31 LEU B CD1 1884 C CD2 . LEU B 31 ? 1.0600 1.0859 1.0443 0.0373 -0.0540 0.4521 31 LEU B CD2 1885 N N . ASN B 32 ? 1.1629 1.3217 1.1731 0.0358 -0.0474 0.4712 32 ASN B N 1886 C CA . ASN B 32 ? 1.2157 1.4004 1.2394 0.0394 -0.0412 0.4644 32 ASN B CA 1887 C C . ASN B 32 ? 1.2383 1.3942 1.2637 0.0347 -0.0390 0.4553 32 ASN B C 1888 O O . ASN B 32 ? 1.2835 1.4090 1.3008 0.0265 -0.0421 0.4553 32 ASN B O 1889 C CB . ASN B 32 ? 1.3019 1.5357 1.3340 0.0350 -0.0380 0.4696 32 ASN B CB 1890 C CG . ASN B 32 ? 1.5503 1.8151 1.5798 0.0363 -0.0406 0.4796 32 ASN B CG 1891 O OD1 . ASN B 32 ? 1.4684 1.7613 1.5016 0.0462 -0.0391 0.4797 32 ASN B OD1 1892 N ND2 . ASN B 32 ? 1.7269 1.9920 1.7508 0.0258 -0.0441 0.4882 32 ASN B ND2 1893 N N . VAL B 33 ? 1.1500 1.3150 1.1849 0.0399 -0.0336 0.4478 33 VAL B N 1894 C CA . VAL B 33 ? 1.0397 1.1753 1.0759 0.0374 -0.0314 0.4386 33 VAL B CA 1895 C C . VAL B 33 ? 1.0955 1.2538 1.1425 0.0380 -0.0248 0.4347 33 VAL B C 1896 O O . VAL B 33 ? 1.1087 1.2939 1.1619 0.0455 -0.0210 0.4348 33 VAL B O 1897 C CB . VAL B 33 ? 1.0075 1.1118 1.0402 0.0458 -0.0324 0.4312 33 VAL B CB 1898 C CG1 . VAL B 33 ? 0.8393 0.9197 0.8749 0.0437 -0.0292 0.4212 33 VAL B CG1 1899 C CG2 . VAL B 33 ? 1.0826 1.1560 1.1017 0.0457 -0.0391 0.4339 33 VAL B CG2 1900 N N . THR B 34 ? 1.0645 1.2115 1.1125 0.0306 -0.0235 0.4315 34 THR B N 1901 C CA . THR B 34 ? 0.9037 1.0688 0.9600 0.0314 -0.0175 0.4287 34 THR B CA 1902 C C . THR B 34 ? 0.8794 1.0158 0.9375 0.0355 -0.0143 0.4188 34 THR B C 1903 O O . THR B 34 ? 0.9724 1.0750 1.0252 0.0325 -0.0171 0.4138 34 THR B O 1904 C CB . THR B 34 ? 1.0579 1.2327 1.1143 0.0221 -0.0178 0.4319 34 THR B CB 1905 O OG1 . THR B 34 ? 1.1947 1.3870 1.2470 0.0156 -0.0223 0.4412 34 THR B OG1 1906 C CG2 . THR B 34 ? 0.8680 1.0718 0.9319 0.0257 -0.0117 0.4315 34 THR B CG2 1907 N N . LEU B 35 ? 0.8455 0.9956 0.9102 0.0424 -0.0084 0.4162 35 LEU B N 1908 C CA . LEU B 35 ? 0.8242 0.9482 0.8912 0.0461 -0.0048 0.4048 35 LEU B CA 1909 C C . LEU B 35 ? 0.7509 0.8802 0.8239 0.0463 0.0023 0.3912 35 LEU B C 1910 O O . LEU B 35 ? 0.6813 0.8394 0.7591 0.0481 0.0064 0.3829 35 LEU B O 1911 C CB . LEU B 35 ? 1.0257 1.1521 1.0941 0.0532 -0.0037 0.3953 35 LEU B CB 1912 C CG . LEU B 35 ? 0.9197 1.0201 0.9894 0.0564 -0.0007 0.3830 35 LEU B CG 1913 C CD1 . LEU B 35 ? 0.9782 1.0668 1.0431 0.0615 -0.0057 0.3875 35 LEU B CD1 1914 C CD2 . LEU B 35 ? 0.6908 0.8076 0.7674 0.0587 0.0070 0.3640 35 LEU B CD2 1915 N N . GLN B 36 ? 0.8105 0.9120 0.8830 0.0450 0.0038 0.3883 36 GLN B N 1916 C CA . GLN B 36 ? 1.0311 1.1353 1.1081 0.0463 0.0104 0.3763 36 GLN B CA 1917 C C . GLN B 36 ? 1.1928 1.2649 1.2696 0.0478 0.0132 0.3677 36 GLN B C 1918 O O . GLN B 36 ? 1.4416 1.4887 1.5148 0.0452 0.0102 0.3748 36 GLN B O 1919 C CB . GLN B 36 ? 1.1586 1.2744 1.2344 0.0419 0.0086 0.3867 36 GLN B CB 1920 C CG . GLN B 36 ? 1.2382 1.3741 1.3179 0.0443 0.0137 0.3793 36 GLN B CG 1921 C CD . GLN B 36 ? 1.3989 1.5458 1.4834 0.0509 0.0209 0.3606 36 GLN B CD 1922 O OE1 . GLN B 36 ? 1.5344 1.6783 1.6202 0.0543 0.0253 0.3527 36 GLN B OE1 1923 N NE2 . GLN B 36 ? 1.5855 1.7356 1.6717 0.0527 0.0221 0.3526 36 GLN B NE2 1924 N N . ILE B 37 ? 1.1374 1.2117 1.2179 0.0512 0.0192 0.3518 37 ILE B N 1925 C CA . ILE B 37 ? 0.9575 1.0053 1.0379 0.0519 0.0232 0.3423 37 ILE B CA 1926 C C . ILE B 37 ? 1.0183 1.0615 1.0991 0.0520 0.0266 0.3410 37 ILE B C 1927 O O . ILE B 37 ? 1.1271 1.1913 1.2101 0.0539 0.0293 0.3371 37 ILE B O 1928 C CB . ILE B 37 ? 0.9219 0.9749 1.0052 0.0538 0.0287 0.3258 37 ILE B CB 1929 C CG1 . ILE B 37 ? 0.9819 1.0347 1.0643 0.0548 0.0252 0.3269 37 ILE B CG1 1930 C CG2 . ILE B 37 ? 0.7506 0.7821 0.8340 0.0534 0.0350 0.3141 37 ILE B CG2 1931 C CD1 . ILE B 37 ? 0.9634 0.9920 1.0414 0.0544 0.0194 0.3381 37 ILE B CD1 1932 N N . THR B 38 ? 1.1198 1.1371 1.1981 0.0507 0.0262 0.3441 38 THR B N 1933 C CA . THR B 38 ? 1.1027 1.1129 1.1807 0.0523 0.0299 0.3420 38 THR B CA 1934 C C . THR B 38 ? 1.1444 1.1281 1.2214 0.0529 0.0342 0.3325 38 THR B C 1935 O O . THR B 38 ? 1.2987 1.2622 1.3735 0.0506 0.0316 0.3369 38 THR B O 1936 C CB . THR B 38 ? 0.8335 0.8407 0.9089 0.0495 0.0254 0.3559 38 THR B CB 1937 O OG1 . THR B 38 ? 0.7409 0.7709 0.8159 0.0463 0.0203 0.3671 38 THR B OG1 1938 C CG2 . THR B 38 ? 1.0054 1.0137 1.0810 0.0535 0.0297 0.3523 38 THR B CG2 1939 N N . LEU B 39 ? 1.0649 1.0488 1.1430 0.0554 0.0406 0.3191 39 LEU B N 1940 C CA . LEU B 39 ? 0.9424 0.9017 1.0187 0.0548 0.0454 0.3098 39 LEU B CA 1941 C C . LEU B 39 ? 1.0499 0.9879 1.1230 0.0562 0.0467 0.3137 39 LEU B C 1942 O O . LEU B 39 ? 1.2270 1.1710 1.2995 0.0600 0.0472 0.3170 39 LEU B O 1943 C CB . LEU B 39 ? 0.8399 0.8042 0.9170 0.0557 0.0520 0.2943 39 LEU B CB 1944 C CG . LEU B 39 ? 0.9136 0.8518 0.9873 0.0544 0.0581 0.2846 39 LEU B CG 1945 C CD1 . LEU B 39 ? 0.8155 0.7552 0.8895 0.0503 0.0630 0.2698 39 LEU B CD1 1946 C CD2 . LEU B 39 ? 0.8842 0.8192 0.9557 0.0600 0.0616 0.2824 39 LEU B CD2 1947 N N . SER B 40 ? 1.0807 0.9963 1.1518 0.0536 0.0470 0.3136 40 SER B N 1948 C CA . SER B 40 ? 1.1802 1.0758 1.2479 0.0551 0.0487 0.3165 40 SER B CA 1949 C C . SER B 40 ? 1.2300 1.1061 1.2948 0.0548 0.0556 0.3053 40 SER B C 1950 O O . SER B 40 ? 1.0942 0.9606 1.1558 0.0589 0.0597 0.3032 40 SER B O 1951 C CB . SER B 40 ? 1.1127 0.9978 1.1783 0.0513 0.0431 0.3226 40 SER B CB 1952 O OG . SER B 40 ? 1.2024 1.1030 1.2674 0.0492 0.0360 0.3270 40 SER B OG 1953 N N . GLN B 41 ? 1.2971 1.1684 1.3624 0.0500 0.0571 0.2980 41 GLN B N 1954 C CA . GLN B 41 ? 1.1334 0.9858 1.1951 0.0473 0.0636 0.2879 41 GLN B CA 1955 C C . GLN B 41 ? 0.9959 0.8525 1.0587 0.0413 0.0659 0.2773 41 GLN B C 1956 O O . GLN B 41 ? 0.9178 0.7868 0.9838 0.0396 0.0617 0.2791 41 GLN B O 1957 C CB . GLN B 41 ? 1.1471 0.9775 1.2052 0.0465 0.0635 0.2938 41 GLN B CB 1958 C CG . GLN B 41 ? 1.8850 1.6984 1.9399 0.0402 0.0677 0.2864 41 GLN B CG 1959 C CD . GLN B 41 ? 1.8163 1.6142 1.8661 0.0386 0.0754 0.2768 41 GLN B CD 1960 O OE1 . GLN B 41 ? 1.7589 1.5624 1.8084 0.0413 0.0780 0.2709 41 GLN B OE1 1961 N NE2 . GLN B 41 ? 1.7591 1.5370 1.8041 0.0336 0.0789 0.2748 41 GLN B NE2 1962 N N . ILE B 42 ? 0.9250 0.7712 0.9844 0.0382 0.0726 0.2661 42 ILE B N 1963 C CA . ILE B 42 ? 0.9487 0.7933 1.0072 0.0302 0.0763 0.2553 42 ILE B CA 1964 C C . ILE B 42 ? 0.9874 0.8108 1.0420 0.0252 0.0779 0.2566 42 ILE B C 1965 O O . ILE B 42 ? 0.9834 0.7849 1.0320 0.0228 0.0833 0.2535 42 ILE B O 1966 C CB . ILE B 42 ? 1.2962 1.1367 1.3515 0.0271 0.0833 0.2419 42 ILE B CB 1967 C CG1 . ILE B 42 ? 1.2599 1.1226 1.3188 0.0323 0.0823 0.2394 42 ILE B CG1 1968 C CG2 . ILE B 42 ? 1.2996 1.1420 1.3538 0.0166 0.0873 0.2300 42 ILE B CG2 1969 C CD1 . ILE B 42 ? 1.2542 1.1142 1.3098 0.0293 0.0888 0.2247 42 ILE B CD1 1970 N N . LYS B 43 ? 1.0886 0.9176 1.1457 0.0242 0.0734 0.2614 43 LYS B N 1971 C CA . LYS B 43 ? 1.0265 0.8389 1.0802 0.0199 0.0745 0.2627 43 LYS B CA 1972 C C . LYS B 43 ? 0.8651 0.6718 0.9151 0.0103 0.0810 0.2510 43 LYS B C 1973 O O . LYS B 43 ? 0.9461 0.7338 0.9909 0.0056 0.0846 0.2511 43 LYS B O 1974 C CB . LYS B 43 ? 1.0099 0.8316 1.0668 0.0213 0.0681 0.2681 43 LYS B CB 1975 C CG . LYS B 43 ? 1.1164 0.9276 1.1704 0.0159 0.0698 0.2660 43 LYS B CG 1976 C CD . LYS B 43 ? 1.2900 1.0908 1.3433 0.0196 0.0652 0.2764 43 LYS B CD 1977 C CE . LYS B 43 ? 1.3962 1.1783 1.4442 0.0146 0.0698 0.2763 43 LYS B CE 1978 N NZ . LYS B 43 ? 1.4886 1.2654 1.5361 0.0165 0.0655 0.2834 43 LYS B NZ 1979 N N . ASP B 44 ? 1.0903 0.9146 1.1427 0.0066 0.0828 0.2410 44 ASP B N 1980 C CA . ASP B 44 ? 1.2329 1.0557 1.2819 -0.0044 0.0889 0.2290 44 ASP B CA 1981 C C . ASP B 44 ? 1.1265 0.9718 1.1786 -0.0068 0.0905 0.2182 44 ASP B C 1982 O O . ASP B 44 ? 0.8769 0.7479 0.9350 -0.0025 0.0858 0.2189 44 ASP B O 1983 C CB . ASP B 44 ? 1.2979 1.1268 1.3475 -0.0091 0.0873 0.2287 44 ASP B CB 1984 C CG . ASP B 44 ? 1.3008 1.1319 1.3467 -0.0222 0.0936 0.2165 44 ASP B CG 1985 O OD1 . ASP B 44 ? 1.4143 1.2686 1.4631 -0.0261 0.0945 0.2068 44 ASP B OD1 1986 O OD2 . ASP B 44 ? 1.2450 1.0559 1.2846 -0.0292 0.0976 0.2168 44 ASP B OD2 1987 N N . MET B 45 ? 1.0265 0.8607 1.0737 -0.0133 0.0970 0.2086 45 MET B N 1988 C CA . MET B 45 ? 0.9446 0.7990 0.9934 -0.0191 0.1000 0.1955 45 MET B CA 1989 C C . MET B 45 ? 1.0606 0.9152 1.1057 -0.0332 0.1047 0.1858 45 MET B C 1990 O O . MET B 45 ? 1.2133 1.0463 1.2508 -0.0428 0.1112 0.1788 45 MET B O 1991 C CB . MET B 45 ? 0.9877 0.8304 1.0328 -0.0182 0.1043 0.1892 45 MET B CB 1992 C CG . MET B 45 ? 0.9819 0.8501 1.0298 -0.0228 0.1066 0.1755 45 MET B CG 1993 S SD . MET B 45 ? 1.3148 1.2246 1.3735 -0.0126 0.0985 0.1819 45 MET B SD 1994 C CE . MET B 45 ? 0.7578 0.7007 0.8192 -0.0230 0.1006 0.1675 45 MET B CE 1995 N N . ASP B 46 ? 0.9527 0.8311 1.0024 -0.0342 0.1013 0.1857 46 ASP B N 1996 C CA . ASP B 46 ? 0.9264 0.8143 0.9737 -0.0476 0.1053 0.1758 46 ASP B CA 1997 C C . ASP B 46 ? 1.0226 0.9225 1.0684 -0.0577 0.1109 0.1605 46 ASP B C 1998 O O . ASP B 46 ? 0.9678 0.9003 1.0194 -0.0556 0.1089 0.1546 46 ASP B O 1999 C CB . ASP B 46 ? 0.7195 0.6365 0.7730 -0.0429 0.0996 0.1781 46 ASP B CB 2000 C CG . ASP B 46 ? 0.7816 0.7103 0.8326 -0.0553 0.1029 0.1697 46 ASP B CG 2001 O OD1 . ASP B 46 ? 0.7798 0.7058 0.8258 -0.0703 0.1099 0.1585 46 ASP B OD1 2002 O OD2 . ASP B 46 ? 0.8007 0.7440 0.8550 -0.0498 0.0981 0.1738 46 ASP B OD2 2003 N N . GLU B 47 ? 1.0430 0.9161 1.0803 -0.0685 0.1178 0.1541 47 GLU B N 2004 C CA . GLU B 47 ? 1.1574 1.0394 1.1924 -0.0787 0.1231 0.1387 47 GLU B CA 2005 C C . GLU B 47 ? 1.4313 1.3468 1.4685 -0.0910 0.1249 0.1271 47 GLU B C 2006 O O . GLU B 47 ? 1.5698 1.5164 1.6120 -0.0905 0.1242 0.1187 47 GLU B O 2007 C CB . GLU B 47 ? 1.1355 0.9787 1.1592 -0.0890 0.1303 0.1333 47 GLU B CB 2008 C CG . GLU B 47 ? 1.2092 1.0278 1.2304 -0.0777 0.1302 0.1374 47 GLU B CG 2009 C CD . GLU B 47 ? 1.3092 1.0999 1.3196 -0.0883 0.1377 0.1253 47 GLU B CD 2010 O OE1 . GLU B 47 ? 1.4332 1.1960 1.4336 -0.1010 0.1428 0.1235 47 GLU B OE1 2011 O OE2 . GLU B 47 ? 1.2872 1.0836 1.2986 -0.0839 0.1385 0.1174 47 GLU B OE2 2012 N N . ARG B 48 ? 1.3642 1.2778 1.3978 -0.1016 0.1269 0.1266 48 ARG B N 2013 C CA . ARG B 48 ? 1.2579 1.2027 1.2917 -0.1165 0.1302 0.1129 48 ARG B CA 2014 C C . ARG B 48 ? 1.1496 1.1377 1.1929 -0.1072 0.1239 0.1148 48 ARG B C 2015 O O . ARG B 48 ? 1.2890 1.3118 1.3343 -0.1157 0.1254 0.1039 48 ARG B O 2016 C CB . ARG B 48 ? 1.4400 1.3673 1.4646 -0.1349 0.1361 0.1094 48 ARG B CB 2017 C CG . ARG B 48 ? 1.6263 1.5231 1.6397 -0.1517 0.1443 0.0993 48 ARG B CG 2018 C CD . ARG B 48 ? 1.7243 1.6522 1.7387 -0.1646 0.1481 0.0813 48 ARG B CD 2019 N NE . ARG B 48 ? 1.7475 1.6476 1.7518 -0.1784 0.1552 0.0698 48 ARG B NE 2020 C CZ . ARG B 48 ? 1.7443 1.6110 1.7447 -0.1700 0.1560 0.0715 48 ARG B CZ 2021 N NH1 . ARG B 48 ? 1.6807 1.5384 1.6867 -0.1483 0.1503 0.0849 48 ARG B NH1 2022 N NH2 . ARG B 48 ? 1.7808 1.6232 1.7709 -0.1837 0.1627 0.0591 48 ARG B NH2 2023 N N . ASN B 49 ? 1.0829 1.0697 1.1317 -0.0891 0.1167 0.1284 49 ASN B N 2024 C CA . ASN B 49 ? 1.0777 1.1024 1.1348 -0.0773 0.1101 0.1305 49 ASN B CA 2025 C C . ASN B 49 ? 1.2205 1.2570 1.2828 -0.0654 0.1066 0.1326 49 ASN B C 2026 O O . ASN B 49 ? 1.4475 1.5140 1.5158 -0.0549 0.1010 0.1351 49 ASN B O 2027 C CB . ASN B 49 ? 1.0735 1.0914 1.1326 -0.0656 0.1038 0.1437 49 ASN B CB 2028 C CG . ASN B 49 ? 1.1171 1.1295 1.1717 -0.0763 0.1068 0.1417 49 ASN B CG 2029 O OD1 . ASN B 49 ? 1.1359 1.1696 1.1886 -0.0900 0.1112 0.1298 49 ASN B OD1 2030 N ND2 . ASN B 49 ? 1.0985 1.0841 1.1509 -0.0713 0.1046 0.1530 49 ASN B ND2 2031 N N . GLN B 50 ? 1.3070 1.3189 1.3664 -0.0665 0.1096 0.1323 50 GLN B N 2032 C CA . GLN B 50 ? 1.0812 1.1004 1.1449 -0.0552 0.1065 0.1356 50 GLN B CA 2033 C C . GLN B 50 ? 1.0671 1.0918 1.1362 -0.0382 0.0980 0.1510 50 GLN B C 2034 O O . GLN B 50 ? 1.1341 1.1862 1.2084 -0.0297 0.0938 0.1525 50 GLN B O 2035 C CB . GLN B 50 ? 1.0130 1.0706 1.0802 -0.0592 0.1080 0.1228 50 GLN B CB 2036 C CG . GLN B 50 ? 1.1701 1.2211 1.2354 -0.0629 0.1123 0.1143 50 GLN B CG 2037 C CD . GLN B 50 ? 1.2496 1.2689 1.3058 -0.0786 0.1203 0.1047 50 GLN B CD 2038 O OE1 . GLN B 50 ? 1.4202 1.4406 1.4727 -0.0921 0.1240 0.0979 50 GLN B OE1 2039 N NE2 . GLN B 50 ? 1.2651 1.2574 1.3171 -0.0772 0.1230 0.1034 50 GLN B NE2 2040 N N . ILE B 51 ? 0.9275 0.9264 0.9946 -0.0336 0.0954 0.1625 51 ILE B N 2041 C CA . ILE B 51 ? 0.8814 0.8818 0.9525 -0.0188 0.0874 0.1770 51 ILE B CA 2042 C C . ILE B 51 ? 0.9920 0.9610 1.0609 -0.0139 0.0869 0.1869 51 ILE B C 2043 O O . ILE B 51 ? 1.2118 1.1527 1.2753 -0.0202 0.0915 0.1859 51 ILE B O 2044 C CB . ILE B 51 ? 0.7913 0.7937 0.8626 -0.0160 0.0835 0.1819 51 ILE B CB 2045 C CG1 . ILE B 51 ? 0.8241 0.8642 0.8984 -0.0168 0.0825 0.1732 51 ILE B CG1 2046 C CG2 . ILE B 51 ? 0.8453 0.8403 0.9188 -0.0020 0.0755 0.1970 51 ILE B CG2 2047 C CD1 . ILE B 51 ? 0.6799 0.7460 0.7591 -0.0051 0.0769 0.1770 51 ILE B CD1 2048 N N . LEU B 52 ? 0.8454 0.8201 0.9178 -0.0029 0.0815 0.1964 52 LEU B N 2049 C CA . LEU B 52 ? 0.7064 0.6565 0.7773 0.0030 0.0801 0.2071 52 LEU B CA 2050 C C . LEU B 52 ? 0.7689 0.7115 0.8408 0.0110 0.0731 0.2212 52 LEU B C 2051 O O . LEU B 52 ? 0.8813 0.8420 0.9564 0.0171 0.0673 0.2257 52 LEU B O 2052 C CB . LEU B 52 ? 0.7608 0.7236 0.8343 0.0084 0.0791 0.2080 52 LEU B CB 2053 C CG . LEU B 52 ? 0.8685 0.8155 0.9417 0.0166 0.0756 0.2213 52 LEU B CG 2054 C CD1 . LEU B 52 ? 0.8694 0.7919 0.9380 0.0148 0.0811 0.2181 52 LEU B CD1 2055 C CD2 . LEU B 52 ? 0.8536 0.8248 0.9313 0.0241 0.0703 0.2279 52 LEU B CD2 2056 N N . THR B 53 ? 0.9468 0.8619 1.0153 0.0110 0.0736 0.2279 53 THR B N 2057 C CA . THR B 53 ? 0.8862 0.7931 0.9553 0.0180 0.0671 0.2408 53 THR B CA 2058 C C . THR B 53 ? 0.7959 0.6911 0.8647 0.0237 0.0649 0.2512 53 THR B C 2059 O O . THR B 53 ? 0.7432 0.6238 0.8092 0.0219 0.0696 0.2494 53 THR B O 2060 C CB . THR B 53 ? 0.9260 0.8152 0.9917 0.0139 0.0684 0.2411 53 THR B CB 2061 O OG1 . THR B 53 ? 0.9076 0.8103 0.9731 0.0068 0.0716 0.2297 53 THR B OG1 2062 C CG2 . THR B 53 ? 0.5974 0.4817 0.6640 0.0212 0.0609 0.2527 53 THR B CG2 2063 N N . ALA B 54 ? 0.6898 0.5921 0.7609 0.0305 0.0580 0.2620 54 ALA B N 2064 C CA . ALA B 54 ? 0.8830 0.7802 0.9540 0.0347 0.0560 0.2713 54 ALA B CA 2065 C C . ALA B 54 ? 1.0119 0.9031 1.0826 0.0391 0.0487 0.2851 54 ALA B C 2066 O O . ALA B 54 ? 1.1165 1.0135 1.1878 0.0412 0.0436 0.2882 54 ALA B O 2067 C CB . ALA B 54 ? 1.0505 0.9698 1.1243 0.0367 0.0562 0.2688 54 ALA B CB 2068 N N . TYR B 55 ? 0.8306 0.7098 0.8998 0.0405 0.0484 0.2927 55 TYR B N 2069 C CA . TYR B 55 ? 0.9470 0.8225 1.0156 0.0431 0.0419 0.3059 55 TYR B CA 2070 C C . TYR B 55 ? 0.9384 0.8315 1.0088 0.0455 0.0396 0.3117 55 TYR B C 2071 O O . TYR B 55 ? 0.9818 0.8813 1.0530 0.0464 0.0439 0.3075 55 TYR B O 2072 C CB . TYR B 55 ? 1.1517 1.0076 1.2171 0.0424 0.0429 0.3096 55 TYR B CB 2073 C CG . TYR B 55 ? 1.2017 1.0422 1.2641 0.0394 0.0442 0.3034 55 TYR B CG 2074 C CD1 . TYR B 55 ? 1.2126 1.0537 1.2752 0.0392 0.0402 0.3028 55 TYR B CD1 2075 C CD2 . TYR B 55 ? 1.1412 0.9672 1.2005 0.0374 0.0497 0.2991 55 TYR B CD2 2076 C CE1 . TYR B 55 ? 1.2043 1.0344 1.2649 0.0368 0.0416 0.2986 55 TYR B CE1 2077 C CE2 . TYR B 55 ? 1.1795 0.9941 1.2362 0.0340 0.0510 0.2946 55 TYR B CE2 2078 C CZ . TYR B 55 ? 1.2305 1.0484 1.2884 0.0336 0.0472 0.2946 55 TYR B CZ 2079 O OH . TYR B 55 ? 1.2188 1.0278 1.2746 0.0306 0.0486 0.2913 55 TYR B OH 2080 N N . LEU B 56 ? 0.7589 0.6599 0.8295 0.0466 0.0328 0.3210 56 LEU B N 2081 C CA . LEU B 56 ? 0.8570 0.7764 0.9287 0.0477 0.0301 0.3279 56 LEU B CA 2082 C C . LEU B 56 ? 0.9050 0.8229 0.9723 0.0453 0.0221 0.3332 56 LEU B C 2083 O O . LEU B 56 ? 0.9935 0.8977 1.0560 0.0436 0.0178 0.3286 56 LEU B O 2084 C CB . LEU B 56 ? 0.9111 0.8524 0.9852 0.0492 0.0297 0.3235 56 LEU B CB 2085 C CG . LEU B 56 ? 0.7523 0.7047 0.8289 0.0491 0.0353 0.3091 56 LEU B CG 2086 C CD1 . LEU B 56 ? 0.7057 0.6812 0.7838 0.0513 0.0315 0.3112 56 LEU B CD1 2087 C CD2 . LEU B 56 ? 0.7247 0.6816 0.8026 0.0485 0.0419 0.3003 56 LEU B CD2 2088 N N . TRP B 57 ? 0.6985 0.6320 0.7660 0.0445 0.0202 0.3392 57 TRP B N 2089 C CA . TRP B 57 ? 0.6776 0.6143 0.7402 0.0403 0.0130 0.3420 57 TRP B CA 2090 C C . TRP B 57 ? 0.7934 0.7511 0.8583 0.0417 0.0110 0.3505 57 TRP B C 2091 O O . TRP B 57 ? 0.9745 0.9502 1.0448 0.0450 0.0154 0.3555 57 TRP B O 2092 C CB . TRP B 57 ? 0.9652 0.9049 1.0262 0.0372 0.0128 0.3430 57 TRP B CB 2093 C CG . TRP B 57 ? 0.8158 0.7352 0.8728 0.0356 0.0134 0.3350 57 TRP B CG 2094 C CD1 . TRP B 57 ? 0.8435 0.7551 0.9022 0.0385 0.0190 0.3306 57 TRP B CD1 2095 C CD2 . TRP B 57 ? 0.7708 0.6748 0.8206 0.0311 0.0083 0.3310 57 TRP B CD2 2096 N NE1 . TRP B 57 ? 1.0834 0.9783 1.1367 0.0358 0.0173 0.3243 57 TRP B NE1 2097 C CE2 . TRP B 57 ? 1.0479 0.9385 1.0960 0.0313 0.0109 0.3244 57 TRP B CE2 2098 C CE3 . TRP B 57 ? 0.7838 0.6829 0.8276 0.0270 0.0019 0.3327 57 TRP B CE3 2099 C CZ2 . TRP B 57 ? 1.1656 1.0412 1.2070 0.0277 0.0074 0.3199 57 TRP B CZ2 2100 C CZ3 . TRP B 57 ? 0.8466 0.7279 0.8831 0.0236 -0.0013 0.3280 57 TRP B CZ3 2101 C CH2 . TRP B 57 ? 1.0624 0.9335 1.0982 0.0240 0.0014 0.3218 57 TRP B CH2 2102 N N . ILE B 58 ? 0.6762 0.6313 0.7361 0.0399 0.0046 0.3525 58 ILE B N 2103 C CA . ILE B 58 ? 0.7046 0.6789 0.7659 0.0422 0.0024 0.3604 58 ILE B CA 2104 C C . ILE B 58 ? 0.9467 0.9247 1.0019 0.0368 -0.0039 0.3658 58 ILE B C 2105 O O . ILE B 58 ? 1.0044 0.9648 1.0518 0.0351 -0.0092 0.3644 58 ILE B O 2106 C CB . ILE B 58 ? 0.9874 0.9555 1.0481 0.0476 0.0011 0.3591 58 ILE B CB 2107 C CG1 . ILE B 58 ? 1.0494 1.0152 1.1163 0.0519 0.0080 0.3549 58 ILE B CG1 2108 C CG2 . ILE B 58 ? 0.9576 0.9462 1.0181 0.0508 -0.0022 0.3678 58 ILE B CG2 2109 C CD1 . ILE B 58 ? 1.1034 1.0699 1.1705 0.0575 0.0072 0.3513 58 ILE B CD1 2110 N N . ARG B 59 ? 0.9381 0.9401 0.9963 0.0346 -0.0031 0.3731 59 ARG B N 2111 C CA . ARG B 59 ? 1.0114 1.0207 1.0645 0.0282 -0.0084 0.3797 59 ARG B CA 2112 C C . ARG B 59 ? 1.1016 1.1251 1.1531 0.0302 -0.0117 0.3871 59 ARG B C 2113 O O . ARG B 59 ? 1.2507 1.2989 1.3082 0.0352 -0.0089 0.3915 59 ARG B O 2114 C CB . ARG B 59 ? 1.1915 1.2230 1.2484 0.0246 -0.0062 0.3847 59 ARG B CB 2115 C CG . ARG B 59 ? 1.2684 1.3200 1.3226 0.0185 -0.0105 0.3944 59 ARG B CG 2116 C CD . ARG B 59 ? 1.3790 1.4586 1.4375 0.0160 -0.0083 0.4001 59 ARG B CD 2117 N NE . ARG B 59 ? 1.3380 1.4083 1.3968 0.0139 -0.0064 0.3960 59 ARG B NE 2118 C CZ . ARG B 59 ? 1.0953 1.1477 1.1482 0.0065 -0.0099 0.3940 59 ARG B CZ 2119 N NH1 . ARG B 59 ? 0.9785 1.0155 1.0236 0.0002 -0.0154 0.3954 59 ARG B NH1 2120 N NH2 . ARG B 59 ? 0.9786 1.0283 1.0328 0.0061 -0.0077 0.3911 59 ARG B NH2 2121 N N . GLN B 60 ? 0.9815 0.9889 1.0240 0.0266 -0.0178 0.3887 60 GLN B N 2122 C CA . GLN B 60 ? 0.9163 0.9337 0.9551 0.0282 -0.0218 0.3963 60 GLN B CA 2123 C C . GLN B 60 ? 1.0935 1.1075 1.1243 0.0188 -0.0266 0.4024 60 GLN B C 2124 O O . GLN B 60 ? 1.1497 1.1401 1.1737 0.0128 -0.0286 0.3990 60 GLN B O 2125 C CB . GLN B 60 ? 0.9644 0.9610 0.9979 0.0355 -0.0245 0.3928 60 GLN B CB 2126 C CG . GLN B 60 ? 0.9055 0.9051 0.9466 0.0443 -0.0199 0.3872 60 GLN B CG 2127 C CD . GLN B 60 ? 1.0591 1.0338 1.0940 0.0504 -0.0231 0.3823 60 GLN B CD 2128 O OE1 . GLN B 60 ? 1.0546 1.0250 1.0824 0.0541 -0.0281 0.3867 60 GLN B OE1 2129 N NE2 . GLN B 60 ? 1.1774 1.1355 1.2145 0.0519 -0.0203 0.3735 60 GLN B NE2 2130 N N . ILE B 61 ? 1.1425 1.1832 1.1744 0.0166 -0.0279 0.4120 61 ILE B N 2131 C CA . ILE B 61 ? 1.0840 1.1260 1.1089 0.0065 -0.0321 0.4196 61 ILE B CA 2132 C C . ILE B 61 ? 0.9826 1.0345 1.0027 0.0080 -0.0358 0.4284 61 ILE B C 2133 O O . ILE B 61 ? 0.9255 1.0019 0.9519 0.0154 -0.0339 0.4308 61 ILE B O 2134 C CB . ILE B 61 ? 1.1101 1.1812 1.1417 -0.0004 -0.0296 0.4239 61 ILE B CB 2135 C CG1 . ILE B 61 ? 1.1038 1.1735 1.1426 0.0023 -0.0245 0.4159 61 ILE B CG1 2136 C CG2 . ILE B 61 ? 1.1296 1.1925 1.1532 -0.0125 -0.0338 0.4290 61 ILE B CG2 2137 C CD1 . ILE B 61 ? 1.1203 1.2217 1.1656 -0.0016 -0.0218 0.4205 61 ILE B CD1 2138 N N . TRP B 62 ? 0.8743 0.9051 0.8821 0.0017 -0.0411 0.4330 62 TRP B N 2139 C CA . TRP B 62 ? 0.9700 1.0018 0.9698 0.0030 -0.0454 0.4418 62 TRP B CA 2140 C C . TRP B 62 ? 1.1198 1.1271 1.1056 -0.0073 -0.0502 0.4473 62 TRP B C 2141 O O . TRP B 62 ? 1.2601 1.2459 1.2419 -0.0137 -0.0502 0.4427 62 TRP B O 2142 C CB . TRP B 62 ? 1.0662 1.0816 1.0625 0.0158 -0.0467 0.4382 62 TRP B CB 2143 C CG . TRP B 62 ? 1.2105 1.1833 1.1965 0.0171 -0.0489 0.4309 62 TRP B CG 2144 C CD1 . TRP B 62 ? 1.2322 1.1706 1.2016 0.0168 -0.0542 0.4334 62 TRP B CD1 2145 C CD2 . TRP B 62 ? 1.3633 1.3220 1.3541 0.0191 -0.0457 0.4196 62 TRP B CD2 2146 N NE1 . TRP B 62 ? 1.3236 1.2294 1.2877 0.0188 -0.0543 0.4237 62 TRP B NE1 2147 C CE2 . TRP B 62 ? 1.3254 1.2442 1.3027 0.0198 -0.0492 0.4153 62 TRP B CE2 2148 C CE3 . TRP B 62 ? 1.3720 1.3476 1.3761 0.0206 -0.0400 0.4131 62 TRP B CE3 2149 C CZ2 . TRP B 62 ? 1.2814 1.1802 1.2596 0.0212 -0.0473 0.4046 62 TRP B CZ2 2150 C CZ3 . TRP B 62 ? 1.3690 1.3219 1.3732 0.0220 -0.0383 0.4027 62 TRP B CZ3 2151 C CH2 . TRP B 62 ? 1.3027 1.2193 1.2945 0.0223 -0.0420 0.3985 62 TRP B CH2 2152 N N . HIS B 63 ? 1.3129 1.3228 1.2906 -0.0087 -0.0540 0.4574 63 HIS B N 2153 C CA . HIS B 63 ? 1.3432 1.3289 1.3060 -0.0191 -0.0584 0.4643 63 HIS B CA 2154 C C . HIS B 63 ? 1.4523 1.3949 1.3976 -0.0125 -0.0627 0.4645 63 HIS B C 2155 O O . HIS B 63 ? 1.6169 1.5593 1.5605 -0.0006 -0.0641 0.4653 63 HIS B O 2156 C CB . HIS B 63 ? 1.3972 1.4138 1.3607 -0.0272 -0.0600 0.4772 63 HIS B CB 2157 C CG . HIS B 63 ? 1.5469 1.6024 1.5235 -0.0364 -0.0569 0.4788 63 HIS B CG 2158 N ND1 . HIS B 63 ? 1.6077 1.7030 1.5997 -0.0306 -0.0526 0.4766 63 HIS B ND1 2159 C CD2 . HIS B 63 ? 1.5947 1.6567 1.5704 -0.0506 -0.0576 0.4828 63 HIS B CD2 2160 C CE1 . HIS B 63 ? 1.6219 1.7458 1.6215 -0.0398 -0.0508 0.4789 63 HIS B CE1 2161 N NE2 . HIS B 63 ? 1.5996 1.7055 1.5902 -0.0521 -0.0539 0.4827 63 HIS B NE2 2162 N N . ASP B 64 ? 1.3207 1.2280 1.2527 -0.0198 -0.0648 0.4641 64 ASP B N 2163 C CA . ASP B 64 ? 1.4535 1.3178 1.3658 -0.0145 -0.0690 0.4661 64 ASP B CA 2164 C C . ASP B 64 ? 1.6517 1.5057 1.5508 -0.0270 -0.0720 0.4783 64 ASP B C 2165 O O . ASP B 64 ? 1.8129 1.6543 1.7080 -0.0394 -0.0717 0.4784 64 ASP B O 2166 C CB . ASP B 64 ? 1.4646 1.2916 1.3702 -0.0112 -0.0686 0.4551 64 ASP B CB 2167 C CG . ASP B 64 ? 1.5726 1.3549 1.4571 -0.0035 -0.0727 0.4568 64 ASP B CG 2168 O OD1 . ASP B 64 ? 1.5612 1.3260 1.4310 -0.0099 -0.0754 0.4670 64 ASP B OD1 2169 O OD2 . ASP B 64 ? 1.6631 1.4273 1.5453 0.0094 -0.0732 0.4482 64 ASP B OD2 2170 N N . ALA B 65 ? 1.5988 1.4585 1.4911 -0.0241 -0.0750 0.4890 65 ALA B N 2171 C CA . ALA B 65 ? 1.5748 1.4321 1.4564 -0.0370 -0.0775 0.5023 65 ALA B CA 2172 C C . ALA B 65 ? 1.7057 1.5112 1.5660 -0.0414 -0.0797 0.5041 65 ALA B C 2173 O O . ALA B 65 ? 1.7626 1.5617 1.6142 -0.0554 -0.0811 0.5140 65 ALA B O 2174 C CB . ALA B 65 ? 1.4935 1.3679 1.3721 -0.0312 -0.0801 0.5132 65 ALA B CB 2175 N N . TYR B 66 ? 1.7014 1.4716 1.5540 -0.0298 -0.0798 0.4946 66 TYR B N 2176 C CA . TYR B 66 ? 1.7318 1.4515 1.5640 -0.0312 -0.0812 0.4956 66 TYR B CA 2177 C C . TYR B 66 ? 1.7378 1.4479 1.5738 -0.0430 -0.0784 0.4883 66 TYR B C 2178 O O . TYR B 66 ? 1.8731 1.5481 1.6948 -0.0496 -0.0789 0.4911 66 TYR B O 2179 C CB . TYR B 66 ? 1.6892 1.3761 1.5096 -0.0114 -0.0831 0.4900 66 TYR B CB 2180 C CG . TYR B 66 ? 1.6588 1.3488 1.4713 0.0009 -0.0869 0.4984 66 TYR B CG 2181 C CD1 . TYR B 66 ? 1.6711 1.3317 1.4622 0.0011 -0.0899 0.5108 66 TYR B CD1 2182 C CD2 . TYR B 66 ? 1.6603 1.3829 1.4870 0.0127 -0.0872 0.4944 66 TYR B CD2 2183 C CE1 . TYR B 66 ? 1.7375 1.4011 1.5205 0.0134 -0.0939 0.5189 66 TYR B CE1 2184 C CE2 . TYR B 66 ? 1.6671 1.3957 1.4876 0.0243 -0.0910 0.5022 66 TYR B CE2 2185 C CZ . TYR B 66 ? 1.6875 1.3865 1.4858 0.0249 -0.0946 0.5143 66 TYR B CZ 2186 O OH . TYR B 66 ? 1.6421 1.3479 1.4338 0.0371 -0.0988 0.5224 66 TYR B OH 2187 N N . LEU B 67 ? 1.5961 1.3382 1.4513 -0.0459 -0.0754 0.4798 67 LEU B N 2188 C CA . LEU B 67 ? 1.5055 1.2447 1.3660 -0.0568 -0.0729 0.4732 67 LEU B CA 2189 C C . LEU B 67 ? 1.5300 1.2994 1.3978 -0.0756 -0.0729 0.4813 67 LEU B C 2190 O O . LEU B 67 ? 1.4118 1.2105 1.2948 -0.0815 -0.0705 0.4764 67 LEU B O 2191 C CB . LEU B 67 ? 1.3946 1.1491 1.2706 -0.0484 -0.0697 0.4596 67 LEU B CB 2192 C CG . LEU B 67 ? 1.3517 1.0830 1.2224 -0.0299 -0.0702 0.4515 67 LEU B CG 2193 C CD1 . LEU B 67 ? 1.2562 1.0049 1.1430 -0.0230 -0.0669 0.4387 67 LEU B CD1 2194 C CD2 . LEU B 67 ? 1.4343 1.1164 1.2858 -0.0272 -0.0717 0.4504 67 LEU B CD2 2195 N N . THR B 68 ? 1.6449 1.4090 1.5016 -0.0846 -0.0757 0.4944 68 THR B N 2196 C CA . THR B 68 ? 1.7665 1.5604 1.6289 -0.1032 -0.0764 0.5032 68 THR B CA 2197 C C . THR B 68 ? 1.8764 1.6434 1.7274 -0.1188 -0.0776 0.5068 68 THR B C 2198 O O . THR B 68 ? 1.9480 1.6712 1.7815 -0.1173 -0.0789 0.5096 68 THR B O 2199 C CB . THR B 68 ? 2.0317 1.8466 1.8915 -0.1055 -0.0789 0.5169 68 THR B CB 2200 O OG1 . THR B 68 ? 2.0473 1.8983 1.9147 -0.1236 -0.0796 0.5250 68 THR B OG1 2201 C CG2 . THR B 68 ? 2.0935 1.8657 1.9308 -0.1033 -0.0818 0.5260 68 THR B CG2 2202 N N . TRP B 69 ? 1.9439 1.7382 1.8053 -0.1335 -0.0770 0.5065 69 TRP B N 2203 C CA . TRP B 69 ? 2.0098 1.7910 1.8629 -0.1525 -0.0789 0.5123 69 TRP B CA 2204 C C . TRP B 69 ? 2.1115 1.9433 1.9780 -0.1676 -0.0795 0.5173 69 TRP B C 2205 O O . TRP B 69 ? 2.1253 1.9920 2.0085 -0.1622 -0.0771 0.5107 69 TRP B O 2206 C CB . TRP B 69 ? 1.9868 1.7376 1.8369 -0.1524 -0.0774 0.5022 69 TRP B CB 2207 C CG . TRP B 69 ? 1.9635 1.7448 1.8302 -0.1549 -0.0751 0.4933 69 TRP B CG 2208 C CD1 . TRP B 69 ? 1.9559 1.7596 1.8281 -0.1725 -0.0760 0.4956 69 TRP B CD1 2209 C CD2 . TRP B 69 ? 1.9230 1.7162 1.8024 -0.1393 -0.0717 0.4812 69 TRP B CD2 2210 N NE1 . TRP B 69 ? 1.9182 1.7465 1.8055 -0.1674 -0.0731 0.4860 69 TRP B NE1 2211 C CE2 . TRP B 69 ? 1.9243 1.7454 1.8162 -0.1474 -0.0703 0.4771 69 TRP B CE2 2212 C CE3 . TRP B 69 ? 1.8859 1.6694 1.7669 -0.1195 -0.0699 0.4738 69 TRP B CE3 2213 C CZ2 . TRP B 69 ? 1.9221 1.7590 1.8274 -0.1360 -0.0668 0.4662 69 TRP B CZ2 2214 C CZ3 . TRP B 69 ? 1.8876 1.6879 1.7825 -0.1096 -0.0666 0.4626 69 TRP B CZ3 2215 C CH2 . TRP B 69 ? 1.9095 1.7349 1.8162 -0.1176 -0.0649 0.4591 69 TRP B CH2 2216 N N . ASP B 70 ? 2.1729 2.0101 2.0322 -0.1861 -0.0826 0.5293 70 ASP B N 2217 C CA . ASP B 70 ? 2.1554 2.0418 2.0268 -0.2014 -0.0835 0.5336 70 ASP B CA 2218 C C . ASP B 70 ? 2.2051 2.0894 2.0793 -0.2118 -0.0831 0.5272 70 ASP B C 2219 O O . ASP B 70 ? 2.2576 2.1036 2.1190 -0.2195 -0.0844 0.5271 70 ASP B O 2220 C CB . ASP B 70 ? 2.1554 2.0546 2.0189 -0.2182 -0.0874 0.5490 70 ASP B CB 2221 C CG . ASP B 70 ? 2.1522 2.1071 2.0285 -0.2332 -0.0885 0.5534 70 ASP B CG 2222 O OD1 . ASP B 70 ? 2.0875 2.0793 1.9808 -0.2247 -0.0858 0.5465 70 ASP B OD1 2223 O OD2 . ASP B 70 ? 2.2038 2.1664 2.0728 -0.2532 -0.0921 0.5640 70 ASP B OD2 2224 N N . ARG B 71 ? 2.0677 1.9938 1.9586 -0.2114 -0.0812 0.5221 71 ARG B N 2225 C CA . ARG B 71 ? 1.9031 1.8328 1.7991 -0.2173 -0.0802 0.5148 71 ARG B CA 2226 C C . ARG B 71 ? 1.9845 1.9174 1.8725 -0.2416 -0.0841 0.5229 71 ARG B C 2227 O O . ARG B 71 ? 1.9601 1.8684 1.8423 -0.2484 -0.0846 0.5187 71 ARG B O 2228 C CB . ARG B 71 ? 1.7371 1.7144 1.6523 -0.2098 -0.0772 0.5094 71 ARG B CB 2229 C CG . ARG B 71 ? 1.7552 1.7780 1.6780 -0.2126 -0.0781 0.5184 71 ARG B CG 2230 C CD . ARG B 71 ? 1.6847 1.7594 1.6255 -0.2079 -0.0754 0.5154 71 ARG B CD 2231 N NE . ARG B 71 ? 1.6541 1.7657 1.6013 -0.2061 -0.0757 0.5228 71 ARG B NE 2232 C CZ . ARG B 71 ? 1.5092 1.6703 1.4716 -0.2008 -0.0732 0.5223 71 ARG B CZ 2233 N NH1 . ARG B 71 ? 1.3156 1.4951 1.2878 -0.1967 -0.0703 0.5153 71 ARG B NH1 2234 N NH2 . ARG B 71 ? 1.4795 1.6723 1.4465 -0.1994 -0.0737 0.5291 71 ARG B NH2 2235 N N . ASP B 72 ? 2.1003 2.0626 1.9875 -0.2549 -0.0871 0.5347 72 ASP B N 2236 C CA . ASP B 72 ? 2.2395 2.2167 2.1209 -0.2801 -0.0912 0.5434 72 ASP B CA 2237 C C . ASP B 72 ? 2.3182 2.2499 2.1855 -0.2907 -0.0928 0.5415 72 ASP B C 2238 O O . ASP B 72 ? 2.3482 2.2914 2.2170 -0.3039 -0.0939 0.5394 72 ASP B O 2239 C CB . ASP B 72 ? 2.2172 2.2012 2.0899 -0.2911 -0.0947 0.5574 72 ASP B CB 2240 C CG . ASP B 72 ? 2.1575 2.2051 2.0427 -0.2983 -0.0959 0.5640 72 ASP B CG 2241 O OD1 . ASP B 72 ? 2.0759 2.1647 1.9738 -0.3014 -0.0950 0.5601 72 ASP B OD1 2242 O OD2 . ASP B 72 ? 2.2211 2.2780 2.1026 -0.3010 -0.0978 0.5738 72 ASP B OD2 2243 N N . GLN B 73 ? 2.4354 2.3152 2.2890 -0.2832 -0.0927 0.5417 73 GLN B N 2244 C CA . GLN B 73 ? 2.4940 2.3288 2.3311 -0.2960 -0.0950 0.5436 73 GLN B CA 2245 C C . GLN B 73 ? 2.5076 2.3021 2.3427 -0.2830 -0.0922 0.5312 73 GLN B C 2246 O O . GLN B 73 ? 2.4827 2.2352 2.3044 -0.2905 -0.0937 0.5312 73 GLN B O 2247 C CB . GLN B 73 ? 2.5565 2.3599 2.3769 -0.3000 -0.0973 0.5550 73 GLN B CB 2248 C CG . GLN B 73 ? 2.6827 2.4524 2.4861 -0.3215 -0.1009 0.5612 73 GLN B CG 2249 C CD . GLN B 73 ? 2.7287 2.5379 2.5329 -0.3483 -0.1049 0.5698 73 GLN B CD 2250 O OE1 . GLN B 73 ? 2.7202 2.5536 2.5317 -0.3586 -0.1055 0.5646 73 GLN B OE1 2251 N NE2 . GLN B 73 ? 2.7136 2.5310 2.5099 -0.3600 -0.1079 0.5832 73 GLN B NE2 2252 N N . TYR B 74 ? 2.4259 2.2326 2.2741 -0.2639 -0.0883 0.5204 74 TYR B N 2253 C CA . TYR B 74 ? 2.4341 2.2156 2.2829 -0.2577 -0.0864 0.5089 74 TYR B CA 2254 C C . TYR B 74 ? 2.2890 2.1117 2.1532 -0.2603 -0.0850 0.5030 74 TYR B C 2255 O O . TYR B 74 ? 2.2448 2.0756 2.1202 -0.2430 -0.0813 0.4933 74 TYR B O 2256 C CB . TYR B 74 ? 2.5544 2.3027 2.4022 -0.2334 -0.0829 0.4995 74 TYR B CB 2257 C CG . TYR B 74 ? 2.6824 2.3913 2.5229 -0.2348 -0.0828 0.4920 74 TYR B CG 2258 C CD1 . TYR B 74 ? 2.6952 2.4199 2.5438 -0.2418 -0.0824 0.4854 74 TYR B CD1 2259 C CD2 . TYR B 74 ? 2.7786 2.4360 2.6038 -0.2303 -0.0835 0.4924 74 TYR B CD2 2260 C CE1 . TYR B 74 ? 2.7758 2.4677 2.6182 -0.2446 -0.0828 0.4791 74 TYR B CE1 2261 C CE2 . TYR B 74 ? 2.8287 2.4521 2.6480 -0.2325 -0.0838 0.4857 74 TYR B CE2 2262 C CZ . TYR B 74 ? 2.8453 2.4868 2.6735 -0.2402 -0.0835 0.4789 74 TYR B CZ 2263 O OH . TYR B 74 ? 2.8984 2.5083 2.7212 -0.2430 -0.0842 0.4723 74 TYR B OH 2264 N N . ASP B 75 ? 2.2021 2.0504 2.0660 -0.2823 -0.0881 0.5093 75 ASP B N 2265 C CA . ASP B 75 ? 2.0892 1.9780 1.9658 -0.2870 -0.0873 0.5054 75 ASP B CA 2266 C C . ASP B 75 ? 2.0572 1.9883 1.9508 -0.2715 -0.0840 0.5027 75 ASP B C 2267 O O . ASP B 75 ? 2.0452 1.9996 1.9504 -0.2655 -0.0815 0.4962 75 ASP B O 2268 C CB . ASP B 75 ? 2.0045 1.8647 1.8800 -0.2825 -0.0857 0.4948 75 ASP B CB 2269 C CG . ASP B 75 ? 1.8508 1.7417 1.7319 -0.2968 -0.0868 0.4939 75 ASP B CG 2270 O OD1 . ASP B 75 ? 1.8410 1.7251 1.7118 -0.3186 -0.0908 0.4988 75 ASP B OD1 2271 O OD2 . ASP B 75 ? 1.6948 1.6159 1.5898 -0.2863 -0.0837 0.4884 75 ASP B OD2 2272 N N . GLY B 76 ? 2.0747 2.0153 1.9691 -0.2654 -0.0840 0.5084 76 GLY B N 2273 C CA . GLY B 76 ? 1.9829 1.9647 1.8925 -0.2524 -0.0813 0.5075 76 GLY B CA 2274 C C . GLY B 76 ? 1.8902 1.8622 1.8088 -0.2291 -0.0764 0.4956 76 GLY B C 2275 O O . GLY B 76 ? 1.8675 1.8765 1.8004 -0.2202 -0.0737 0.4930 76 GLY B O 2276 N N . LEU B 77 ? 1.8454 1.7692 1.7558 -0.2186 -0.0753 0.4888 77 LEU B N 2277 C CA . LEU B 77 ? 1.7409 1.6552 1.6591 -0.1981 -0.0710 0.4769 77 LEU B CA 2278 C C . LEU B 77 ? 1.7586 1.6861 1.6845 -0.1810 -0.0685 0.4753 77 LEU B C 2279 O O . LEU B 77 ? 1.8442 1.7491 1.7624 -0.1743 -0.0692 0.4772 77 LEU B O 2280 C CB . LEU B 77 ? 1.7154 1.5770 1.6222 -0.1924 -0.0707 0.4698 77 LEU B CB 2281 C CG . LEU B 77 ? 1.7025 1.5595 1.6161 -0.1845 -0.0677 0.4585 77 LEU B CG 2282 C CD1 . LEU B 77 ? 1.7765 1.6504 1.6915 -0.2019 -0.0694 0.4608 77 LEU B CD1 2283 C CD2 . LEU B 77 ? 1.6881 1.4966 1.5924 -0.1733 -0.0668 0.4502 77 LEU B CD2 2284 N N . ASP B 78 ? 1.6777 1.6421 1.6186 -0.1738 -0.0655 0.4719 78 ASP B N 2285 C CA . ASP B 78 ? 1.6744 1.6606 1.6253 -0.1592 -0.0629 0.4705 78 ASP B CA 2286 C C . ASP B 78 ? 1.5959 1.5536 1.5467 -0.1401 -0.0601 0.4605 78 ASP B C 2287 O O . ASP B 78 ? 1.5871 1.5429 1.5371 -0.1318 -0.0601 0.4622 78 ASP B O 2288 C CB . ASP B 78 ? 1.6729 1.7058 1.6391 -0.1577 -0.0602 0.4700 78 ASP B CB 2289 C CG . ASP B 78 ? 1.8095 1.8379 1.7785 -0.1580 -0.0585 0.4632 78 ASP B CG 2290 O OD1 . ASP B 78 ? 1.8400 1.8432 1.7993 -0.1686 -0.0609 0.4632 78 ASP B OD1 2291 O OD2 . ASP B 78 ? 1.8374 1.8863 1.8177 -0.1474 -0.0546 0.4580 78 ASP B OD2 2292 N N . SER B 79 ? 1.5442 1.4822 1.4960 -0.1335 -0.0578 0.4504 79 SER B N 2293 C CA . SER B 79 ? 1.5910 1.5074 1.5440 -0.1159 -0.0550 0.4402 79 SER B CA 2294 C C . SER B 79 ? 1.7116 1.5898 1.6571 -0.1126 -0.0546 0.4313 79 SER B C 2295 O O . SER B 79 ? 1.7437 1.6206 1.6892 -0.1207 -0.0546 0.4298 79 SER B O 2296 C CB . SER B 79 ? 1.6159 1.5624 1.5843 -0.1055 -0.0508 0.4349 79 SER B CB 2297 O OG . SER B 79 ? 1.6939 1.6336 1.6653 -0.1041 -0.0486 0.4272 79 SER B OG 2298 N N . ILE B 80 ? 1.5867 1.4362 1.5263 -0.1002 -0.0542 0.4255 80 ILE B N 2299 C CA . ILE B 80 ? 1.5244 1.3398 1.4576 -0.0949 -0.0535 0.4163 80 ILE B CA 2300 C C . ILE B 80 ? 1.6562 1.4689 1.5953 -0.0776 -0.0505 0.4065 80 ILE B C 2301 O O . ILE B 80 ? 1.6300 1.4525 1.5721 -0.0695 -0.0504 0.4079 80 ILE B O 2302 C CB . ILE B 80 ? 1.3521 1.1285 1.2684 -0.0983 -0.0566 0.4195 80 ILE B CB 2303 C CG1 . ILE B 80 ? 1.2916 1.0569 1.2014 -0.0886 -0.0579 0.4226 80 ILE B CG1 2304 C CG2 . ILE B 80 ? 1.4073 1.1871 1.3178 -0.1173 -0.0596 0.4300 80 ILE B CG2 2305 C CD1 . ILE B 80 ? 1.3412 1.0699 1.2335 -0.0930 -0.0609 0.4284 80 ILE B CD1 2306 N N . ARG B 81 ? 1.6854 1.4855 1.6261 -0.0727 -0.0485 0.3970 81 ARG B N 2307 C CA . ARG B 81 ? 1.7083 1.5030 1.6533 -0.0576 -0.0460 0.3874 81 ARG B CA 2308 C C . ARG B 81 ? 1.6198 1.3764 1.5517 -0.0511 -0.0480 0.3834 81 ARG B C 2309 O O . ARG B 81 ? 1.5924 1.3257 1.5156 -0.0567 -0.0493 0.3830 81 ARG B O 2310 C CB . ARG B 81 ? 1.7445 1.5500 1.6990 -0.0559 -0.0426 0.3799 81 ARG B CB 2311 C CG . ARG B 81 ? 1.8166 1.6565 1.7813 -0.0638 -0.0412 0.3855 81 ARG B CG 2312 C CD . ARG B 81 ? 1.8411 1.7054 1.8189 -0.0546 -0.0371 0.3816 81 ARG B CD 2313 N NE . ARG B 81 ? 1.9851 1.8805 1.9715 -0.0609 -0.0357 0.3868 81 ARG B NE 2314 C CZ . ARG B 81 ? 2.0568 1.9659 2.0519 -0.0558 -0.0319 0.3826 81 ARG B CZ 2315 N NH1 . ARG B 81 ? 2.1266 2.0210 2.1233 -0.0455 -0.0292 0.3729 81 ARG B NH1 2316 N NH2 . ARG B 81 ? 2.0371 1.9754 2.0388 -0.0607 -0.0310 0.3887 81 ARG B NH2 2317 N N . ILE B 82 ? 1.5162 1.2673 1.4469 -0.0390 -0.0484 0.3811 82 ILE B N 2318 C CA . ILE B 82 ? 1.4411 1.1581 1.3594 -0.0305 -0.0505 0.3778 82 ILE B CA 2319 C C . ILE B 82 ? 1.5616 1.2811 1.4850 -0.0157 -0.0496 0.3703 82 ILE B C 2320 O O . ILE B 82 ? 1.5555 1.3024 1.4911 -0.0127 -0.0475 0.3699 82 ILE B O 2321 C CB . ILE B 82 ? 1.3893 1.0901 1.2946 -0.0326 -0.0541 0.3873 82 ILE B CB 2322 C CG1 . ILE B 82 ? 1.4948 1.2251 1.4068 -0.0347 -0.0544 0.3952 82 ILE B CG1 2323 C CG2 . ILE B 82 ? 1.3530 1.0370 1.2492 -0.0462 -0.0554 0.3929 82 ILE B CG2 2324 C CD1 . ILE B 82 ? 1.6070 1.3236 1.5062 -0.0369 -0.0579 0.4056 82 ILE B CD1 2325 N N . PRO B 83 ? 1.6376 1.3299 1.5526 -0.0067 -0.0510 0.3645 83 PRO B N 2326 C CA . PRO B 83 ? 1.6558 1.3509 1.5758 0.0068 -0.0507 0.3576 83 PRO B CA 2327 C C . PRO B 83 ? 1.5899 1.2994 1.5128 0.0142 -0.0523 0.3623 83 PRO B C 2328 O O . PRO B 83 ? 1.5270 1.2253 1.4395 0.0156 -0.0557 0.3696 83 PRO B O 2329 C CB . PRO B 83 ? 1.7403 1.4010 1.6475 0.0143 -0.0534 0.3536 83 PRO B CB 2330 C CG . PRO B 83 ? 1.7877 1.4338 1.6896 0.0036 -0.0525 0.3540 83 PRO B CG 2331 C CD . PRO B 83 ? 1.7657 1.4263 1.6687 -0.0095 -0.0523 0.3632 83 PRO B CD 2332 N N . SER B 84 ? 1.5565 1.2906 1.4937 0.0191 -0.0495 0.3583 84 SER B N 2333 C CA . SER B 84 ? 1.6090 1.3596 1.5517 0.0275 -0.0503 0.3617 84 SER B CA 2334 C C . SER B 84 ? 1.6817 1.4094 1.6132 0.0395 -0.0551 0.3614 84 SER B C 2335 O O . SER B 84 ? 1.8263 1.5599 1.7558 0.0460 -0.0578 0.3675 84 SER B O 2336 C CB . SER B 84 ? 1.5722 1.3481 1.5318 0.0313 -0.0456 0.3562 84 SER B CB 2337 O OG . SER B 84 ? 1.5580 1.3211 1.5176 0.0401 -0.0459 0.3485 84 SER B OG 2338 N N . ASP B 85 ? 1.6121 1.3148 1.5364 0.0431 -0.0563 0.3547 85 ASP B N 2339 C CA . ASP B 85 ? 1.6718 1.3517 1.5854 0.0560 -0.0610 0.3534 85 ASP B CA 2340 C C . ASP B 85 ? 1.6124 1.2696 1.5083 0.0565 -0.0654 0.3620 85 ASP B C 2341 O O . ASP B 85 ? 1.6888 1.3287 1.5742 0.0686 -0.0701 0.3635 85 ASP B O 2342 C CB . ASP B 85 ? 1.7630 1.4216 1.6729 0.0580 -0.0609 0.3447 85 ASP B CB 2343 C CG . ASP B 85 ? 1.8424 1.4806 1.7438 0.0735 -0.0659 0.3419 85 ASP B CG 2344 O OD1 . ASP B 85 ? 1.8560 1.4988 1.7558 0.0836 -0.0697 0.3461 85 ASP B OD1 2345 O OD2 . ASP B 85 ? 1.8733 1.4923 1.7703 0.0762 -0.0664 0.3358 85 ASP B OD2 2346 N N . LEU B 86 ? 1.5657 1.2243 1.4584 0.0438 -0.0639 0.3686 86 LEU B N 2347 C CA . LEU B 86 ? 1.6087 1.2412 1.4834 0.0431 -0.0672 0.3769 86 LEU B CA 2348 C C . LEU B 86 ? 1.6065 1.2557 1.4808 0.0389 -0.0684 0.3881 86 LEU B C 2349 O O . LEU B 86 ? 1.6461 1.2746 1.5054 0.0367 -0.0707 0.3966 86 LEU B O 2350 C CB . LEU B 86 ? 1.6763 1.2873 1.5438 0.0317 -0.0651 0.3767 86 LEU B CB 2351 C CG . LEU B 86 ? 1.7391 1.3102 1.5865 0.0362 -0.0677 0.3816 86 LEU B CG 2352 C CD1 . LEU B 86 ? 1.7348 1.2884 1.5741 0.0559 -0.0715 0.3779 86 LEU B CD1 2353 C CD2 . LEU B 86 ? 1.7172 1.2678 1.5614 0.0271 -0.0652 0.3789 86 LEU B CD2 2354 N N . VAL B 87 ? 1.5222 1.2088 1.4130 0.0373 -0.0664 0.3890 87 VAL B N 2355 C CA . VAL B 87 ? 1.4329 1.1388 1.3245 0.0345 -0.0677 0.3999 87 VAL B CA 2356 C C . VAL B 87 ? 1.5728 1.2975 1.4706 0.0479 -0.0696 0.4013 87 VAL B C 2357 O O . VAL B 87 ? 1.6456 1.3781 1.5531 0.0566 -0.0684 0.3930 87 VAL B O 2358 C CB . VAL B 87 ? 1.2216 0.9597 1.1274 0.0206 -0.0635 0.4023 87 VAL B CB 2359 C CG1 . VAL B 87 ? 1.2412 0.9637 1.1391 0.0066 -0.0630 0.4052 87 VAL B CG1 2360 C CG2 . VAL B 87 ? 1.0775 0.8369 1.0006 0.0220 -0.0590 0.3928 87 VAL B CG2 2361 N N . TRP B 88 ? 1.6196 1.3514 1.5118 0.0500 -0.0726 0.4119 88 TRP B N 2362 C CA . TRP B 88 ? 1.6575 1.4130 1.5569 0.0627 -0.0743 0.4147 88 TRP B CA 2363 C C . TRP B 88 ? 1.5388 1.3336 1.4601 0.0613 -0.0690 0.4109 88 TRP B C 2364 O O . TRP B 88 ? 1.6287 1.4441 1.5571 0.0509 -0.0661 0.4151 88 TRP B O 2365 C CB . TRP B 88 ? 1.6659 1.4309 1.5587 0.0616 -0.0771 0.4277 88 TRP B CB 2366 C CG . TRP B 88 ? 1.5058 1.3061 1.4100 0.0727 -0.0774 0.4314 88 TRP B CG 2367 C CD1 . TRP B 88 ? 1.5562 1.3513 1.4538 0.0885 -0.0822 0.4333 88 TRP B CD1 2368 C CD2 . TRP B 88 ? 1.4300 1.2779 1.3558 0.0703 -0.0720 0.4315 88 TRP B CD2 2369 N NE1 . TRP B 88 ? 1.6340 1.4719 1.5470 0.0945 -0.0798 0.4362 88 TRP B NE1 2370 C CE2 . TRP B 88 ? 1.5382 1.4076 1.4681 0.0836 -0.0734 0.4349 88 TRP B CE2 2371 C CE3 . TRP B 88 ? 1.3782 1.2522 1.3188 0.0589 -0.0663 0.4298 88 TRP B CE3 2372 C CZ2 . TRP B 88 ? 1.4903 1.4061 1.4381 0.0851 -0.0686 0.4366 88 TRP B CZ2 2373 C CZ3 . TRP B 88 ? 1.2911 1.2085 1.2487 0.0611 -0.0620 0.4315 88 TRP B CZ3 2374 C CH2 . TRP B 88 ? 1.3117 1.2494 1.2725 0.0738 -0.0630 0.4348 88 TRP B CH2 2375 N N . ARG B 89 ? 1.4993 1.3101 1.4323 0.0717 -0.0673 0.4050 89 ARG B N 2376 C CA . ARG B 89 ? 1.4858 1.3334 1.4388 0.0668 -0.0606 0.4028 89 ARG B CA 2377 C C . ARG B 89 ? 1.5478 1.4299 1.5153 0.0766 -0.0576 0.4031 89 ARG B C 2378 O O . ARG B 89 ? 1.5967 1.4767 1.5633 0.0896 -0.0597 0.4012 89 ARG B O 2379 C CB . ARG B 89 ? 1.6840 1.5212 1.6420 0.0606 -0.0569 0.3927 89 ARG B CB 2380 C CG . ARG B 89 ? 1.8835 1.6984 1.8308 0.0475 -0.0578 0.3937 89 ARG B CG 2381 C CD . ARG B 89 ? 1.9837 1.8183 1.9329 0.0346 -0.0568 0.4030 89 ARG B CD 2382 N NE . ARG B 89 ? 2.0041 1.8178 1.9372 0.0266 -0.0607 0.4111 89 ARG B NE 2383 C CZ . ARG B 89 ? 1.9620 1.7793 1.8874 0.0247 -0.0639 0.4224 89 ARG B CZ 2384 N NH1 . ARG B 89 ? 2.0027 1.8488 1.9350 0.0298 -0.0642 0.4289 89 ARG B NH1 2385 N NH2 . ARG B 89 ? 1.9435 1.7339 1.8527 0.0178 -0.0669 0.4279 89 ARG B NH2 2386 N N . PRO B 90 ? 1.3489 1.2655 1.3297 0.0710 -0.0527 0.4062 90 PRO B N 2387 C CA . PRO B 90 ? 1.3938 1.3460 1.3872 0.0800 -0.0492 0.4078 90 PRO B CA 2388 C C . PRO B 90 ? 1.3341 1.2856 1.3361 0.0868 -0.0455 0.3985 90 PRO B C 2389 O O . PRO B 90 ? 1.4958 1.4432 1.5044 0.0805 -0.0411 0.3919 90 PRO B O 2390 C CB . PRO B 90 ? 1.3535 1.3378 1.3575 0.0710 -0.0446 0.4121 90 PRO B CB 2391 C CG . PRO B 90 ? 1.2535 1.2192 1.2558 0.0588 -0.0434 0.4079 90 PRO B CG 2392 C CD . PRO B 90 ? 1.2389 1.1643 1.2245 0.0572 -0.0493 0.4069 90 PRO B CD 2393 N N . ASP B 91 ? 1.0403 0.9962 1.0416 0.1004 -0.0474 0.3984 91 ASP B N 2394 C CA . ASP B 91 ? 1.0120 0.9668 1.0198 0.1078 -0.0446 0.3907 91 ASP B CA 2395 C C . ASP B 91 ? 1.0072 0.9965 1.0306 0.1065 -0.0369 0.3905 91 ASP B C 2396 O O . ASP B 91 ? 1.1616 1.1780 1.1911 0.1168 -0.0349 0.3922 91 ASP B O 2397 C CB . ASP B 91 ? 1.1447 1.0996 1.1475 0.1241 -0.0491 0.3914 91 ASP B CB 2398 C CG . ASP B 91 ? 1.3650 1.2806 1.3506 0.1266 -0.0570 0.3911 91 ASP B CG 2399 O OD1 . ASP B 91 ? 1.5656 1.4499 1.5453 0.1196 -0.0580 0.3852 91 ASP B OD1 2400 O OD2 . ASP B 91 ? 1.4170 1.3325 1.3938 0.1364 -0.0624 0.3967 91 ASP B OD2 2401 N N . ILE B 92 ? 0.8127 0.8030 0.8414 0.0946 -0.0325 0.3889 92 ILE B N 2402 C CA . ILE B 92 ? 0.8422 0.8622 0.8836 0.0937 -0.0252 0.3894 92 ILE B CA 2403 C C . ILE B 92 ? 0.8734 0.8872 0.9212 0.0946 -0.0198 0.3782 92 ILE B C 2404 O O . ILE B 92 ? 0.9603 0.9509 1.0084 0.0881 -0.0182 0.3755 92 ILE B O 2405 C CB . ILE B 92 ? 0.9292 0.9566 0.9737 0.0820 -0.0223 0.3914 92 ILE B CB 2406 C CG1 . ILE B 92 ? 1.2761 1.3220 1.3166 0.0806 -0.0260 0.4007 92 ILE B CG1 2407 C CG2 . ILE B 92 ? 0.7049 0.7546 0.7603 0.0801 -0.0139 0.3835 92 ILE B CG2 2408 C CD1 . ILE B 92 ? 1.5010 1.5671 1.5465 0.0718 -0.0228 0.4045 92 ILE B CD1 2409 N N . VAL B 93 ? 0.7198 0.7568 0.7723 0.0999 -0.0160 0.3650 93 VAL B N 2410 C CA . VAL B 93 ? 0.7394 0.7718 0.7966 0.0985 -0.0105 0.3491 93 VAL B CA 2411 C C . VAL B 93 ? 0.7132 0.7716 0.7788 0.0920 -0.0018 0.3347 93 VAL B C 2412 O O . VAL B 93 ? 0.8250 0.9101 0.8934 0.0908 -0.0002 0.3352 93 VAL B O 2413 C CB . VAL B 93 ? 0.9920 1.0268 1.0465 0.1093 -0.0131 0.3433 93 VAL B CB 2414 C CG1 . VAL B 93 ? 1.0169 1.0392 1.0620 0.1191 -0.0223 0.3585 93 VAL B CG1 2415 C CG2 . VAL B 93 ? 0.8292 0.9033 0.8894 0.1120 -0.0085 0.3305 93 VAL B CG2 2416 N N . LEU B 94 ? 0.6556 0.7071 0.7247 0.0883 0.0038 0.3214 94 LEU B N 2417 C CA . LEU B 94 ? 0.7212 0.7944 0.7966 0.0824 0.0118 0.3066 94 LEU B CA 2418 C C . LEU B 94 ? 0.8895 0.9902 0.9662 0.0880 0.0123 0.2972 94 LEU B C 2419 O O . LEU B 94 ? 0.8289 0.9239 0.9041 0.0918 0.0115 0.2920 94 LEU B O 2420 C CB . LEU B 94 ? 0.6965 0.7507 0.7739 0.0750 0.0177 0.2969 94 LEU B CB 2421 C CG . LEU B 94 ? 0.9022 0.9759 0.9845 0.0682 0.0257 0.2830 94 LEU B CG 2422 C CD1 . LEU B 94 ? 1.0929 1.1649 1.1765 0.0643 0.0273 0.2878 94 LEU B CD1 2423 C CD2 . LEU B 94 ? 1.0333 1.0941 1.1165 0.0619 0.0318 0.2706 94 LEU B CD2 2424 N N . TYR B 95 ? 0.9774 1.1099 1.0567 0.0887 0.0134 0.2953 95 TYR B N 2425 C CA . TYR B 95 ? 0.8376 1.0047 0.9189 0.0934 0.0144 0.2861 95 TYR B CA 2426 C C . TYR B 95 ? 0.7026 0.8786 0.7881 0.0855 0.0223 0.2670 95 TYR B C 2427 O O . TYR B 95 ? 0.7624 0.9567 0.8484 0.0887 0.0229 0.2580 95 TYR B O 2428 C CB . TYR B 95 ? 1.3412 1.5420 1.4248 0.0939 0.0146 0.2881 95 TYR B CB 2429 C CG . TYR B 95 ? 1.0100 1.2189 1.0888 0.1033 0.0067 0.3055 95 TYR B CG 2430 C CD1 . TYR B 95 ? 0.8929 1.0709 0.9650 0.1080 -0.0005 0.3223 95 TYR B CD1 2431 C CD2 . TYR B 95 ? 1.1027 1.3507 1.1830 0.1075 0.0062 0.3046 95 TYR B CD2 2432 C CE1 . TYR B 95 ? 0.7454 0.9280 0.8116 0.1157 -0.0077 0.3386 95 TYR B CE1 2433 C CE2 . TYR B 95 ? 1.0912 1.3467 1.1662 0.1163 -0.0010 0.3212 95 TYR B CE2 2434 C CZ . TYR B 95 ? 1.0130 1.2344 1.0806 0.1201 -0.0080 0.3385 95 TYR B CZ 2435 O OH . TYR B 95 ? 1.0210 1.2478 1.0819 0.1280 -0.0151 0.3555 95 TYR B OH 2436 N N . ASN B 96 ? 0.6895 0.8526 0.7775 0.0751 0.0283 0.2612 96 ASN B N 2437 C CA . ASN B 96 ? 0.7626 0.9294 0.8535 0.0649 0.0367 0.2437 96 ASN B CA 2438 C C . ASN B 96 ? 1.1926 1.3350 1.2818 0.0609 0.0390 0.2380 96 ASN B C 2439 O O . ASN B 96 ? 1.0114 1.1543 1.1018 0.0511 0.0460 0.2241 96 ASN B O 2440 C CB . ASN B 96 ? 0.6654 0.8259 0.7582 0.0575 0.0414 0.2414 96 ASN B CB 2441 C CG . ASN B 96 ? 0.9026 1.0682 0.9973 0.0467 0.0502 0.2230 96 ASN B CG 2442 O OD1 . ASN B 96 ? 1.1191 1.3036 1.2147 0.0434 0.0531 0.2110 96 ASN B OD1 2443 N ND2 . ASN B 96 ? 0.7927 0.9416 0.8872 0.0411 0.0545 0.2204 96 ASN B ND2 2444 N N . LYS B 97 ? 1.2418 1.3628 1.3275 0.0680 0.0330 0.2489 97 LYS B N 2445 C CA . LYS B 97 ? 1.1631 1.2597 1.2468 0.0658 0.0337 0.2465 97 LYS B CA 2446 C C . LYS B 97 ? 1.1240 1.2354 1.2090 0.0590 0.0396 0.2302 97 LYS B C 2447 O O . LYS B 97 ? 1.0769 1.2207 1.1643 0.0580 0.0419 0.2207 97 LYS B O 2448 C CB . LYS B 97 ? 1.1645 1.2503 1.2441 0.0775 0.0253 0.2574 97 LYS B CB 2449 C CG . LYS B 97 ? 1.4912 1.5428 1.5679 0.0765 0.0239 0.2618 97 LYS B CG 2450 C CD . LYS B 97 ? 1.5374 1.5739 1.6091 0.0880 0.0149 0.2743 97 LYS B CD 2451 C CE . LYS B 97 ? 1.4780 1.5247 1.5478 0.0955 0.0092 0.2857 97 LYS B CE 2452 N NZ . LYS B 97 ? 1.4314 1.4628 1.4946 0.1073 0.0003 0.2969 97 LYS B NZ 2453 N N . ALA B 98 ? 1.0873 1.1777 1.1707 0.0542 0.0418 0.2271 98 ALA B N 2454 C CA . ALA B 98 ? 1.0288 1.1338 1.1127 0.0466 0.0473 0.2125 98 ALA B CA 2455 C C . ALA B 98 ? 1.1507 1.2470 1.2322 0.0510 0.0442 0.2132 98 ALA B C 2456 O O . ALA B 98 ? 1.2918 1.4070 1.3736 0.0474 0.0470 0.2023 98 ALA B O 2457 C CB . ALA B 98 ? 0.8653 0.9571 0.9491 0.0316 0.0558 0.2037 98 ALA B CB 2458 N N . ASP B 99 ? 1.2149 1.2838 1.2939 0.0581 0.0387 0.2255 99 ASP B N 2459 C CA . ASP B 99 ? 1.2773 1.3353 1.3537 0.0630 0.0354 0.2264 99 ASP B CA 2460 C C . ASP B 99 ? 1.2365 1.2832 1.3099 0.0776 0.0261 0.2392 99 ASP B C 2461 O O . ASP B 99 ? 1.1112 1.1774 1.1842 0.0875 0.0217 0.2414 99 ASP B O 2462 N N . PRO B 105 ? 1.6513 1.4960 1.6863 0.0653 -0.0125 0.3216 105 PRO B N 2463 C CA . PRO B 105 ? 1.6474 1.4813 1.6828 0.0680 -0.0116 0.3160 105 PRO B CA 2464 C C . PRO B 105 ? 1.8112 1.6278 1.8402 0.0604 -0.0124 0.3099 105 PRO B C 2465 O O . PRO B 105 ? 1.6740 1.4884 1.7064 0.0576 -0.0080 0.3054 105 PRO B O 2466 C CB . PRO B 105 ? 1.6525 1.5016 1.6992 0.0684 -0.0034 0.3166 105 PRO B CB 2467 C CG . PRO B 105 ? 1.6621 1.5312 1.7141 0.0689 -0.0009 0.3232 105 PRO B CG 2468 C CD . PRO B 105 ? 1.6923 1.5604 1.7373 0.0680 -0.0072 0.3267 105 PRO B CD 2469 N N . VAL B 106 ? 1.8747 1.6796 1.8939 0.0572 -0.0179 0.3108 106 VAL B N 2470 C CA . VAL B 106 ? 1.9131 1.7037 1.9247 0.0497 -0.0192 0.3071 106 VAL B CA 2471 C C . VAL B 106 ? 1.9762 1.7629 1.9797 0.0453 -0.0234 0.3119 106 VAL B C 2472 O O . VAL B 106 ? 1.9986 1.7990 2.0056 0.0403 -0.0212 0.3155 106 VAL B O 2473 C CB . VAL B 106 ? 1.8482 1.6465 1.8655 0.0434 -0.0131 0.3039 106 VAL B CB 2474 C CG1 . VAL B 106 ? 1.8444 1.6624 1.8707 0.0429 -0.0082 0.3075 106 VAL B CG1 2475 C CG2 . VAL B 106 ? 1.8355 1.6256 1.8456 0.0360 -0.0149 0.3031 106 VAL B CG2 2476 N N . ASN B 107 ? 1.9350 1.7029 1.9273 0.0474 -0.0294 0.3128 107 ASN B N 2477 C CA . ASN B 107 ? 1.8347 1.6000 1.8195 0.0441 -0.0330 0.3193 107 ASN B CA 2478 C C . ASN B 107 ? 1.5849 1.3487 1.5664 0.0333 -0.0319 0.3200 107 ASN B C 2479 O O . ASN B 107 ? 1.6029 1.3598 1.5836 0.0297 -0.0304 0.3153 107 ASN B O 2480 C CB . ASN B 107 ? 1.8956 1.6389 1.8677 0.0502 -0.0395 0.3211 107 ASN B CB 2481 C CG . ASN B 107 ? 1.9362 1.6773 1.9002 0.0472 -0.0428 0.3292 107 ASN B CG 2482 O OD1 . ASN B 107 ? 1.9617 1.7230 1.9321 0.0423 -0.0405 0.3339 107 ASN B OD1 2483 N ND2 . ASN B 107 ? 1.9215 1.6379 1.8711 0.0504 -0.0482 0.3313 107 ASN B ND2 2484 N N . THR B 108 ? 1.3764 1.1496 1.3569 0.0286 -0.0327 0.3269 108 THR B N 2485 C CA . THR B 108 ? 1.1802 0.9599 1.1604 0.0186 -0.0315 0.3300 108 THR B CA 2486 C C . THR B 108 ? 1.2506 1.0240 1.2214 0.0140 -0.0356 0.3380 108 THR B C 2487 O O . THR B 108 ? 1.3403 1.0981 1.3023 0.0188 -0.0396 0.3400 108 THR B O 2488 C CB . THR B 108 ? 1.0190 0.8260 1.0118 0.0170 -0.0267 0.3317 108 THR B CB 2489 O OG1 . THR B 108 ? 0.9775 0.7997 0.9732 0.0187 -0.0275 0.3388 108 THR B OG1 2490 C CG2 . THR B 108 ? 0.8120 0.6247 0.8139 0.0227 -0.0220 0.3249 108 THR B CG2 2491 N N . ASN B 109 ? 1.4499 1.2360 1.4225 0.0049 -0.0347 0.3432 109 ASN B N 2492 C CA . ASN B 109 ? 1.6072 1.3864 1.5706 -0.0015 -0.0384 0.3514 109 ASN B CA 2493 C C . ASN B 109 ? 1.5309 1.3374 1.5011 -0.0056 -0.0377 0.3597 109 ASN B C 2494 O O . ASN B 109 ? 1.6562 1.4870 1.6385 -0.0049 -0.0339 0.3590 109 ASN B O 2495 C CB . ASN B 109 ? 1.7483 1.5140 1.7049 -0.0109 -0.0391 0.3515 109 ASN B CB 2496 C CG . ASN B 109 ? 1.9219 1.6598 1.8707 -0.0068 -0.0401 0.3442 109 ASN B CG 2497 O OD1 . ASN B 109 ? 2.0131 1.7270 1.9504 -0.0032 -0.0435 0.3452 109 ASN B OD1 2498 N ND2 . ASN B 109 ? 1.8932 1.6345 1.8479 -0.0066 -0.0372 0.3375 109 ASN B ND2 2499 N N . VAL B 110 ? 1.4215 1.2236 1.3836 -0.0097 -0.0413 0.3680 110 VAL B N 2500 C CA . VAL B 110 ? 1.4651 1.2942 1.4333 -0.0125 -0.0412 0.3767 110 VAL B CA 2501 C C . VAL B 110 ? 1.4706 1.3046 1.4348 -0.0258 -0.0429 0.3847 110 VAL B C 2502 O O . VAL B 110 ? 1.5054 1.3153 1.4577 -0.0317 -0.0455 0.3862 110 VAL B O 2503 C CB . VAL B 110 ? 1.1832 1.0104 1.1471 -0.0050 -0.0442 0.3816 110 VAL B CB 2504 C CG1 . VAL B 110 ? 0.8239 0.6488 0.7927 0.0080 -0.0429 0.3744 110 VAL B CG1 2505 C CG2 . VAL B 110 ? 1.0356 0.8342 0.9824 -0.0074 -0.0491 0.3868 110 VAL B CG2 2506 N N . VAL B 111 ? 1.4009 1.2672 1.3752 -0.0305 -0.0411 0.3901 111 VAL B N 2507 C CA . VAL B 111 ? 1.4673 1.3456 1.4396 -0.0436 -0.0428 0.3989 111 VAL B CA 2508 C C . VAL B 111 ? 1.5480 1.4324 1.5149 -0.0473 -0.0462 0.4094 111 VAL B C 2509 O O . VAL B 111 ? 1.6180 1.5319 1.5934 -0.0455 -0.0452 0.4146 111 VAL B O 2510 C CB . VAL B 111 ? 1.4352 1.3482 1.4207 -0.0467 -0.0395 0.4004 111 VAL B CB 2511 C CG1 . VAL B 111 ? 1.3808 1.3070 1.3640 -0.0612 -0.0417 0.4092 111 VAL B CG1 2512 C CG2 . VAL B 111 ? 1.4401 1.3478 1.4310 -0.0412 -0.0358 0.3905 111 VAL B CG2 2513 N N . LEU B 112 ? 1.5268 1.3831 1.4792 -0.0522 -0.0499 0.4131 112 LEU B N 2514 C CA . LEU B 112 ? 1.4831 1.3417 1.4282 -0.0570 -0.0533 0.4242 112 LEU B CA 2515 C C . LEU B 112 ? 1.3986 1.2796 1.3456 -0.0728 -0.0543 0.4333 112 LEU B C 2516 O O . LEU B 112 ? 1.2773 1.1519 1.2224 -0.0819 -0.0543 0.4322 112 LEU B O 2517 C CB . LEU B 112 ? 1.4433 1.2600 1.3706 -0.0551 -0.0566 0.4251 112 LEU B CB 2518 C CG . LEU B 112 ? 1.4135 1.2239 1.3292 -0.0630 -0.0603 0.4376 112 LEU B CG 2519 C CD1 . LEU B 112 ? 1.3953 1.2274 1.3149 -0.0566 -0.0611 0.4437 112 LEU B CD1 2520 C CD2 . LEU B 112 ? 1.4729 1.2369 1.3699 -0.0613 -0.0627 0.4378 112 LEU B CD2 2521 N N . ARG B 113 ? 1.3994 1.3095 1.3508 -0.0762 -0.0552 0.4426 113 ARG B N 2522 C CA . ARG B 113 ? 1.4515 1.3874 1.4049 -0.0915 -0.0567 0.4521 113 ARG B CA 2523 C C . ARG B 113 ? 1.5310 1.4484 1.4695 -0.1013 -0.0611 0.4623 113 ARG B C 2524 O O . ARG B 113 ? 1.5813 1.4685 1.5088 -0.0941 -0.0626 0.4623 113 ARG B O 2525 C CB . ARG B 113 ? 1.4166 1.4005 1.3845 -0.0899 -0.0547 0.4563 113 ARG B CB 2526 C CG . ARG B 113 ? 1.4113 1.4295 1.3859 -0.1028 -0.0547 0.4620 113 ARG B CG 2527 C CD . ARG B 113 ? 1.3346 1.3991 1.3245 -0.0973 -0.0513 0.4631 113 ARG B CD 2528 N NE . ARG B 113 ? 1.3758 1.4604 1.3673 -0.0945 -0.0522 0.4701 113 ARG B NE 2529 C CZ . ARG B 113 ? 1.3274 1.4519 1.3310 -0.0884 -0.0492 0.4715 113 ARG B CZ 2530 N NH1 . ARG B 113 ? 1.2857 1.4309 1.2997 -0.0839 -0.0451 0.4666 113 ARG B NH1 2531 N NH2 . ARG B 113 ? 1.2444 1.3881 1.2491 -0.0862 -0.0501 0.4781 113 ARG B NH2 2532 N N . TYR B 114 ? 1.5260 1.4611 1.4635 -0.1176 -0.0631 0.4712 114 TYR B N 2533 C CA . TYR B 114 ? 1.5907 1.5079 1.5136 -0.1293 -0.0672 0.4818 114 TYR B CA 2534 C C . TYR B 114 ? 1.6314 1.5574 1.5517 -0.1244 -0.0688 0.4900 114 TYR B C 2535 O O . TYR B 114 ? 1.6684 1.5647 1.5735 -0.1255 -0.0715 0.4961 114 TYR B O 2536 C CB . TYR B 114 ? 1.5587 1.4995 1.4828 -0.1491 -0.0692 0.4897 114 TYR B CB 2537 C CG . TYR B 114 ? 1.4685 1.4630 1.4052 -0.1535 -0.0690 0.4966 114 TYR B CG 2538 C CD1 . TYR B 114 ? 1.4186 1.4494 1.3713 -0.1486 -0.0656 0.4913 114 TYR B CD1 2539 C CD2 . TYR B 114 ? 1.4170 1.4265 1.3491 -0.1621 -0.0721 0.5088 114 TYR B CD2 2540 C CE1 . TYR B 114 ? 1.3434 1.4244 1.3072 -0.1514 -0.0652 0.4975 114 TYR B CE1 2541 C CE2 . TYR B 114 ? 1.3853 1.4466 1.3291 -0.1658 -0.0719 0.5150 114 TYR B CE2 2542 C CZ . TYR B 114 ? 1.3653 1.4626 1.3251 -0.1601 -0.0683 0.5089 114 TYR B CZ 2543 O OH . TYR B 114 ? 1.4047 1.5547 1.3758 -0.1625 -0.0677 0.5146 114 TYR B OH 2544 N N . ASP B 115 ? 1.5764 1.5428 1.5110 -0.1181 -0.0668 0.4902 115 ASP B N 2545 C CA . ASP B 115 ? 1.4549 1.4360 1.3893 -0.1128 -0.0680 0.4976 115 ASP B CA 2546 C C . ASP B 115 ? 1.4994 1.4586 1.4320 -0.0944 -0.0668 0.4903 115 ASP B C 2547 O O . ASP B 115 ? 1.6179 1.5926 1.5530 -0.0866 -0.0671 0.4945 115 ASP B O 2548 C CB . ASP B 115 ? 1.3141 1.3517 1.2647 -0.1147 -0.0663 0.5016 115 ASP B CB 2549 C CG . ASP B 115 ? 1.2628 1.3199 1.2288 -0.1031 -0.0615 0.4909 115 ASP B CG 2550 O OD1 . ASP B 115 ? 1.2395 1.2724 1.2052 -0.0992 -0.0598 0.4811 115 ASP B OD1 2551 O OD2 . ASP B 115 ? 1.2267 1.3230 1.2047 -0.0977 -0.0593 0.4924 115 ASP B OD2 2552 N N . GLY B 116 ? 1.3997 1.3254 1.3284 -0.0876 -0.0655 0.4797 116 GLY B N 2553 C CA . GLY B 116 ? 1.4201 1.3232 1.3457 -0.0708 -0.0650 0.4726 116 GLY B CA 2554 C C . GLY B 116 ? 1.3406 1.2705 1.2825 -0.0587 -0.0613 0.4648 116 GLY B C 2555 O O . GLY B 116 ? 1.2647 1.1878 1.2061 -0.0455 -0.0613 0.4618 116 GLY B O 2556 N N . LEU B 117 ? 1.2497 1.2110 1.2059 -0.0630 -0.0581 0.4621 117 LEU B N 2557 C CA . LEU B 117 ? 1.1198 1.1035 1.0909 -0.0522 -0.0537 0.4544 117 LEU B CA 2558 C C . LEU B 117 ? 1.3564 1.3120 1.3270 -0.0452 -0.0517 0.4418 117 LEU B C 2559 O O . LEU B 117 ? 1.5611 1.5004 1.5279 -0.0522 -0.0517 0.4384 117 LEU B O 2560 C CB . LEU B 117 ? 1.0487 1.0753 1.0335 -0.0582 -0.0509 0.4569 117 LEU B CB 2561 C CG . LEU B 117 ? 0.9275 0.9745 0.9266 -0.0476 -0.0456 0.4490 117 LEU B CG 2562 C CD1 . LEU B 117 ? 0.7606 0.8358 0.7671 -0.0395 -0.0441 0.4524 117 LEU B CD1 2563 C CD2 . LEU B 117 ? 1.0979 1.1700 1.1057 -0.0533 -0.0428 0.4485 117 LEU B CD2 2564 N N . ILE B 118 ? 1.2296 1.1820 1.2047 -0.0319 -0.0498 0.4350 118 ILE B N 2565 C CA . ILE B 118 ? 1.0607 0.9867 1.0348 -0.0257 -0.0482 0.4233 118 ILE B CA 2566 C C . ILE B 118 ? 1.1434 1.0905 1.1326 -0.0191 -0.0429 0.4160 118 ILE B C 2567 O O . ILE B 118 ? 1.0097 0.9784 1.0076 -0.0115 -0.0408 0.4167 118 ILE B O 2568 C CB . ILE B 118 ? 0.8845 0.7807 0.8484 -0.0155 -0.0508 0.4204 118 ILE B CB 2569 C CG1 . ILE B 118 ? 0.9701 0.8314 0.9158 -0.0212 -0.0552 0.4244 118 ILE B CG1 2570 C CG2 . ILE B 118 ? 0.7629 0.6459 0.7308 -0.0064 -0.0483 0.4086 118 ILE B CG2 2571 C CD1 . ILE B 118 ? 0.8308 0.6611 0.7649 -0.0097 -0.0580 0.4216 118 ILE B CD1 2572 N N . THR B 119 ? 1.3792 1.3181 1.3708 -0.0216 -0.0406 0.4088 119 THR B N 2573 C CA . THR B 119 ? 1.3315 1.2871 1.3359 -0.0156 -0.0354 0.4023 119 THR B CA 2574 C C . THR B 119 ? 1.2494 1.1801 1.2530 -0.0085 -0.0336 0.3909 119 THR B C 2575 O O . THR B 119 ? 1.2871 1.1989 1.2859 -0.0124 -0.0339 0.3860 119 THR B O 2576 C CB . THR B 119 ? 1.1343 1.1100 1.1447 -0.0231 -0.0332 0.4044 119 THR B CB 2577 O OG1 . THR B 119 ? 1.0295 1.0337 1.0417 -0.0298 -0.0348 0.4154 119 THR B OG1 2578 C CG2 . THR B 119 ? 1.0169 1.0058 1.0388 -0.0153 -0.0275 0.3980 119 THR B CG2 2579 N N . TRP B 120 ? 1.0947 1.0288 1.1037 0.0016 -0.0315 0.3873 120 TRP B N 2580 C CA . TRP B 120 ? 0.9935 0.9072 1.0022 0.0087 -0.0300 0.3774 120 TRP B CA 2581 C C . TRP B 120 ? 1.0740 1.0034 1.0951 0.0133 -0.0239 0.3724 120 TRP B C 2582 O O . TRP B 120 ? 1.0573 1.0034 1.0859 0.0198 -0.0213 0.3738 120 TRP B O 2583 C CB . TRP B 120 ? 0.9418 0.8450 0.9460 0.0169 -0.0328 0.3776 120 TRP B CB 2584 C CG . TRP B 120 ? 1.1995 1.0805 1.2016 0.0236 -0.0324 0.3683 120 TRP B CG 2585 C CD1 . TRP B 120 ? 1.2120 1.0745 1.2114 0.0211 -0.0315 0.3605 120 TRP B CD1 2586 C CD2 . TRP B 120 ? 1.3115 1.1896 1.3147 0.0341 -0.0330 0.3663 120 TRP B CD2 2587 N NE1 . TRP B 120 ? 1.2728 1.1208 1.2713 0.0290 -0.0316 0.3537 120 TRP B NE1 2588 C CE2 . TRP B 120 ? 1.2879 1.1453 1.2890 0.0371 -0.0326 0.3572 120 TRP B CE2 2589 C CE3 . TRP B 120 ? 1.3720 1.2653 1.3778 0.0414 -0.0341 0.3720 120 TRP B CE3 2590 C CZ2 . TRP B 120 ? 1.3277 1.1797 1.3298 0.0472 -0.0331 0.3539 120 TRP B CZ2 2591 C CZ3 . TRP B 120 ? 1.3848 1.2730 1.3915 0.0519 -0.0345 0.3686 120 TRP B CZ3 2592 C CH2 . TRP B 120 ? 1.3614 1.2293 1.3665 0.0546 -0.0341 0.3598 120 TRP B CH2 2593 N N . ASP B 121 ? 1.1476 1.0706 1.1698 0.0101 -0.0216 0.3670 121 ASP B N 2594 C CA . ASP B 121 ? 1.0282 0.9550 1.0588 0.0155 -0.0160 0.3605 121 ASP B CA 2595 C C . ASP B 121 ? 1.1325 1.0340 1.1590 0.0196 -0.0163 0.3516 121 ASP B C 2596 O O . ASP B 121 ? 1.2742 1.1545 1.2910 0.0170 -0.0205 0.3496 121 ASP B O 2597 C CB . ASP B 121 ? 0.9161 0.8500 0.9498 0.0114 -0.0132 0.3598 121 ASP B CB 2598 C CG . ASP B 121 ? 1.0432 1.0072 1.0843 0.0110 -0.0107 0.3674 121 ASP B CG 2599 O OD1 . ASP B 121 ? 1.1786 1.1553 1.2173 0.0047 -0.0139 0.3752 121 ASP B OD1 2600 O OD2 . ASP B 121 ? 1.0618 1.0365 1.1104 0.0171 -0.0053 0.3659 121 ASP B OD2 2601 N N . ALA B 122 ? 1.0270 0.9309 1.0604 0.0260 -0.0119 0.3470 122 ALA B N 2602 C CA . ALA B 122 ? 0.9239 0.8079 0.9546 0.0300 -0.0120 0.3393 122 ALA B CA 2603 C C . ALA B 122 ? 0.9720 0.8613 1.0115 0.0346 -0.0056 0.3349 122 ALA B C 2604 O O . ALA B 122 ? 0.8809 0.7885 0.9281 0.0365 -0.0012 0.3385 122 ALA B O 2605 C CB . ALA B 122 ? 0.9168 0.7940 0.9429 0.0345 -0.0164 0.3415 122 ALA B CB 2606 N N . PRO B 123 ? 0.9972 0.8701 1.0351 0.0359 -0.0045 0.3274 123 PRO B N 2607 C CA . PRO B 123 ? 0.9830 0.8599 1.0283 0.0385 0.0022 0.3240 123 PRO B CA 2608 C C . PRO B 123 ? 0.9473 0.8248 0.9965 0.0443 0.0038 0.3236 123 PRO B C 2609 O O . PRO B 123 ? 1.0120 0.8833 1.0571 0.0473 -0.0010 0.3242 123 PRO B O 2610 C CB . PRO B 123 ? 0.9621 0.8237 1.0034 0.0354 0.0030 0.3171 123 PRO B CB 2611 C CG . PRO B 123 ? 1.0151 0.8622 1.0476 0.0336 -0.0034 0.3157 123 PRO B CG 2612 C CD . PRO B 123 ? 0.9555 0.8069 0.9850 0.0343 -0.0082 0.3220 123 PRO B CD 2613 N N . ALA B 124 ? 0.8675 0.7526 0.9241 0.0463 0.0106 0.3236 124 ALA B N 2614 C CA . ALA B 124 ? 1.0021 0.8923 1.0633 0.0514 0.0127 0.3254 124 ALA B CA 2615 C C . ALA B 124 ? 1.0690 0.9553 1.1352 0.0510 0.0207 0.3221 124 ALA B C 2616 O O . ALA B 124 ? 0.9817 0.8652 1.0491 0.0479 0.0258 0.3201 124 ALA B O 2617 C CB . ALA B 124 ? 0.8620 0.7740 0.9272 0.0550 0.0125 0.3341 124 ALA B CB 2618 N N . ILE B 125 ? 1.0325 0.9209 1.0989 0.0531 0.0214 0.3141 125 ILE B N 2619 C CA . ILE B 125 ? 0.9249 0.8189 0.9935 0.0498 0.0287 0.3011 125 ILE B CA 2620 C C . ILE B 125 ? 0.9094 0.8281 0.9804 0.0519 0.0297 0.2927 125 ILE B C 2621 O O . ILE B 125 ? 0.6782 0.6063 0.7484 0.0578 0.0242 0.2958 125 ILE B O 2622 C CB . ILE B 125 ? 0.8573 0.7362 0.9242 0.0481 0.0300 0.2967 125 ILE B CB 2623 C CG1 . ILE B 125 ? 0.9970 0.8553 1.0610 0.0483 0.0261 0.3066 125 ILE B CG1 2624 C CG2 . ILE B 125 ? 0.9935 0.8714 1.0612 0.0418 0.0385 0.2859 125 ILE B CG2 2625 C CD1 . ILE B 125 ? 0.7484 0.5925 0.8106 0.0462 0.0278 0.3024 125 ILE B CD1 2626 N N . THR B 126 ? 0.7618 0.6916 0.8353 0.0473 0.0366 0.2827 126 THR B N 2627 C CA . THR B 126 ? 0.9265 0.8822 1.0024 0.0481 0.0380 0.2741 126 THR B CA 2628 C C . THR B 126 ? 0.9944 0.9553 1.0711 0.0410 0.0455 0.2595 126 THR B C 2629 O O . THR B 126 ? 0.9858 0.9341 1.0616 0.0349 0.0513 0.2553 126 THR B O 2630 C CB . THR B 126 ? 0.9617 0.9359 1.0399 0.0492 0.0380 0.2763 126 THR B CB 2631 O OG1 . THR B 126 ? 0.9455 0.9161 1.0245 0.0438 0.0446 0.2700 126 THR B OG1 2632 C CG2 . THR B 126 ? 0.7861 0.7567 0.8628 0.0541 0.0309 0.2917 126 THR B CG2 2633 N N . LYS B 127 ? 0.9736 0.9536 1.0512 0.0419 0.0453 0.2519 127 LYS B N 2634 C CA . LYS B 127 ? 1.0814 1.0729 1.1598 0.0337 0.0524 0.2372 127 LYS B CA 2635 C C . LYS B 127 ? 1.0484 1.0719 1.1297 0.0352 0.0525 0.2314 127 LYS B C 2636 O O . LYS B 127 ? 1.1314 1.1733 1.2136 0.0431 0.0472 0.2343 127 LYS B O 2637 C CB . LYS B 127 ? 1.0424 1.0331 1.1193 0.0315 0.0530 0.2314 127 LYS B CB 2638 C CG . LYS B 127 ? 1.0387 1.0059 1.1130 0.0363 0.0481 0.2412 127 LYS B CG 2639 C CD . LYS B 127 ? 0.9157 0.8713 0.9878 0.0293 0.0522 0.2353 127 LYS B CD 2640 C CE . LYS B 127 ? 1.0715 1.0176 1.1418 0.0362 0.0462 0.2410 127 LYS B CE 2641 N NZ . LYS B 127 ? 1.0723 1.0369 1.1425 0.0371 0.0460 0.2321 127 LYS B NZ 2642 N N . SER B 128 ? 0.9440 0.9734 1.0264 0.0287 0.0583 0.2236 128 SER B N 2643 C CA . SER B 128 ? 0.8792 0.9404 0.9646 0.0296 0.0587 0.2176 128 SER B CA 2644 C C . SER B 128 ? 0.8857 0.9553 0.9709 0.0179 0.0670 0.2007 128 SER B C 2645 O O . SER B 128 ? 0.7705 0.8161 0.8526 0.0098 0.0723 0.1962 128 SER B O 2646 C CB . SER B 128 ? 0.8983 0.9622 0.9851 0.0346 0.0562 0.2263 128 SER B CB 2647 O OG . SER B 128 ? 0.8817 0.9305 0.9676 0.0292 0.0615 0.2226 128 SER B OG 2648 N N . SER B 129 ? 0.9880 1.0912 1.0757 0.0165 0.0682 0.1913 129 SER B N 2649 C CA . SER B 129 ? 1.0433 1.1534 1.1299 0.0035 0.0762 0.1745 129 SER B CA 2650 C C . SER B 129 ? 0.9818 1.0902 1.0686 0.0002 0.0801 0.1695 129 SER B C 2651 O O . SER B 129 ? 0.9901 1.1143 1.0798 0.0077 0.0767 0.1749 129 SER B O 2652 C CB . SER B 129 ? 1.1730 1.3221 1.2619 0.0016 0.0765 0.1643 129 SER B CB 2653 O OG . SER B 129 ? 1.1943 1.3516 1.2818 -0.0132 0.0844 0.1473 129 SER B OG 2654 N N . CYS B 130 ? 0.9194 1.0085 1.0023 -0.0111 0.0873 0.1591 130 CYS B N 2655 C CA . CYS B 130 ? 0.8681 0.9503 0.9496 -0.0143 0.0918 0.1521 130 CYS B CA 2656 C C . CYS B 130 ? 1.0015 1.1013 1.0818 -0.0270 0.0985 0.1329 130 CYS B C 2657 O O . CYS B 130 ? 1.0735 1.1875 1.1534 -0.0353 0.1005 0.1250 130 CYS B O 2658 C CB . CYS B 130 ? 0.6588 0.6978 0.7350 -0.0158 0.0946 0.1563 130 CYS B CB 2659 S SG . CYS B 130 ? 1.8171 1.8383 1.8947 -0.0023 0.0872 0.1774 130 CYS B SG 2660 N N . VAL B 131 ? 1.0344 1.1353 1.1139 -0.0289 0.1021 0.1246 131 VAL B N 2661 C CA . VAL B 131 ? 0.9909 1.1065 1.0684 -0.0421 0.1088 0.1048 131 VAL B CA 2662 C C . VAL B 131 ? 1.0569 1.1384 1.1276 -0.0481 0.1150 0.0963 131 VAL B C 2663 O O . VAL B 131 ? 0.8982 0.9582 0.9678 -0.0386 0.1134 0.1047 131 VAL B O 2664 C CB . VAL B 131 ? 0.9232 1.0868 1.0068 -0.0391 0.1072 0.0981 131 VAL B CB 2665 C CG1 . VAL B 131 ? 0.7727 0.9531 0.8539 -0.0545 0.1143 0.0764 131 VAL B CG1 2666 C CG2 . VAL B 131 ? 0.8915 1.0883 0.9808 -0.0307 0.1005 0.1075 131 VAL B CG2 2667 N N . VAL B 132 ? 1.2648 1.3420 1.3301 -0.0641 0.1220 0.0794 132 VAL B N 2668 C CA . VAL B 132 ? 1.3858 1.4314 1.4428 -0.0720 0.1287 0.0677 132 VAL B CA 2669 C C . VAL B 132 ? 1.6053 1.6750 1.6644 -0.0707 0.1303 0.0549 132 VAL B C 2670 O O . VAL B 132 ? 1.5815 1.6959 1.6478 -0.0692 0.1279 0.0514 132 VAL B O 2671 C CB . VAL B 132 ? 1.4249 1.4543 1.4738 -0.0919 0.1356 0.0547 132 VAL B CB 2672 C CG1 . VAL B 132 ? 1.4505 1.5243 1.5027 -0.1037 0.1379 0.0390 132 VAL B CG1 2673 C CG2 . VAL B 132 ? 1.3275 1.3124 1.3655 -0.0985 0.1420 0.0459 132 VAL B CG2 2674 N N . ASP B 133 ? 1.6652 1.7046 1.7178 -0.0701 0.1341 0.0485 133 ASP B N 2675 C CA . ASP B 133 ? 1.7910 1.8462 1.8443 -0.0673 0.1358 0.0363 133 ASP B CA 2676 C C . ASP B 133 ? 1.7181 1.7338 1.7597 -0.0768 0.1434 0.0203 133 ASP B C 2677 O O . ASP B 133 ? 1.8473 1.8180 1.8814 -0.0727 0.1446 0.0263 133 ASP B O 2678 C CB . ASP B 133 ? 1.8809 1.9429 1.9400 -0.0478 0.1298 0.0509 133 ASP B CB 2679 C CG . ASP B 133 ? 2.0593 2.1254 2.1170 -0.0423 0.1317 0.0403 133 ASP B CG 2680 O OD1 . ASP B 133 ? 2.2174 2.2859 2.2708 -0.0532 0.1373 0.0208 133 ASP B OD1 2681 O OD2 . ASP B 133 ? 2.0874 2.1531 2.1478 -0.0274 0.1278 0.0510 133 ASP B OD2 2682 N N . VAL B 134 ? 1.7875 1.8188 1.8266 -0.0894 0.1483 -0.0002 134 VAL B N 2683 C CA . VAL B 134 ? 1.8006 1.7942 1.8278 -0.0970 0.1551 -0.0164 134 VAL B CA 2684 C C . VAL B 134 ? 1.9349 1.9535 1.9658 -0.0871 0.1544 -0.0266 134 VAL B C 2685 O O . VAL B 134 ? 2.0014 2.0345 2.0299 -0.0976 0.1587 -0.0464 134 VAL B O 2686 C CB . VAL B 134 ? 1.7820 1.7682 1.8012 -0.1217 0.1620 -0.0337 134 VAL B CB 2687 C CG1 . VAL B 134 ? 1.8429 1.7781 1.8469 -0.1302 0.1688 -0.0482 134 VAL B CG1 2688 C CG2 . VAL B 134 ? 1.7379 1.7162 1.7566 -0.1305 0.1614 -0.0225 134 VAL B CG2 2689 N N . THR B 135 ? 1.9502 1.9775 1.9875 -0.0673 0.1487 -0.0120 135 THR B N 2690 C CA . THR B 135 ? 1.9656 2.0204 2.0081 -0.0538 0.1464 -0.0157 135 THR B CA 2691 C C . THR B 135 ? 1.9893 2.0111 2.0291 -0.0371 0.1436 -0.0005 135 THR B C 2692 O O . THR B 135 ? 2.0940 2.0854 2.1308 -0.0372 0.1426 0.0130 135 THR B O 2693 C CB . THR B 135 ? 1.6773 1.7939 1.7334 -0.0483 0.1405 -0.0081 135 THR B CB 2694 O OG1 . THR B 135 ? 1.7602 1.9131 1.8182 -0.0601 0.1437 -0.0271 135 THR B OG1 2695 C CG2 . THR B 135 ? 1.5867 1.7221 1.6490 -0.0291 0.1350 0.0038 135 THR B CG2 2696 N N . TYR B 136 ? 2.0336 2.0599 2.0736 -0.0233 0.1426 -0.0033 136 TYR B N 2697 C CA . TYR B 136 ? 2.0153 2.0253 2.0557 -0.0056 0.1384 0.0140 136 TYR B CA 2698 C C . TYR B 136 ? 2.0589 2.0086 2.0869 -0.0059 0.1421 0.0149 136 TYR B C 2699 O O . TYR B 136 ? 1.8999 1.8286 1.9268 -0.0085 0.1408 0.0287 136 TYR B O 2700 C CB . TYR B 136 ? 2.0510 2.0844 2.1015 -0.0001 0.1313 0.0373 136 TYR B CB 2701 C CG . TYR B 136 ? 2.1662 2.1851 2.2173 0.0161 0.1268 0.0557 136 TYR B CG 2702 C CD1 . TYR B 136 ? 2.2063 2.2523 2.2623 0.0300 0.1231 0.0597 136 TYR B CD1 2703 C CD2 . TYR B 136 ? 2.2437 2.2247 2.2903 0.0167 0.1262 0.0689 136 TYR B CD2 2704 C CE1 . TYR B 136 ? 2.2461 2.2822 2.3025 0.0436 0.1191 0.0762 136 TYR B CE1 2705 C CE2 . TYR B 136 ? 2.2802 2.2506 2.3272 0.0306 0.1222 0.0851 136 TYR B CE2 2706 C CZ . TYR B 136 ? 2.2684 2.2665 2.3202 0.0438 0.1187 0.0886 136 TYR B CZ 2707 O OH . TYR B 136 ? 2.2222 2.2126 2.2743 0.0564 0.1148 0.1043 136 TYR B OH 2708 N N . PHE B 137 ? 2.1766 2.0992 2.1948 -0.0021 0.1465 0.0003 137 PHE B N 2709 C CA . PHE B 137 ? 2.2364 2.0987 2.2404 -0.0013 0.1505 -0.0006 137 PHE B CA 2710 C C . PHE B 137 ? 2.2368 2.0785 2.2414 0.0088 0.1465 0.0228 137 PHE B C 2711 O O . PHE B 137 ? 2.1278 1.9936 2.1405 0.0234 0.1410 0.0362 137 PHE B O 2712 C CB . PHE B 137 ? 2.3778 2.2249 2.3741 0.0114 0.1530 -0.0146 137 PHE B CB 2713 C CG . PHE B 137 ? 2.4509 2.3298 2.4557 0.0327 0.1473 -0.0049 137 PHE B CG 2714 C CD1 . PHE B 137 ? 2.4364 2.3704 2.4520 0.0357 0.1447 -0.0102 137 PHE B CD1 2715 C CD2 . PHE B 137 ? 2.4644 2.3205 2.4661 0.0490 0.1447 0.0102 137 PHE B CD2 2716 C CE1 . PHE B 137 ? 2.3968 2.3614 2.4197 0.0536 0.1396 -0.0005 137 PHE B CE1 2717 C CE2 . PHE B 137 ? 2.4597 2.3474 2.4689 0.0668 0.1396 0.0193 137 PHE B CE2 2718 C CZ . PHE B 137 ? 2.4024 2.3441 2.4221 0.0686 0.1371 0.0140 137 PHE B CZ 2719 N N . PRO B 138 ? 2.2262 2.0261 2.2222 -0.0001 0.1491 0.0282 138 PRO B N 2720 C CA . PRO B 138 ? 2.2585 2.0246 2.2436 -0.0195 0.1554 0.0169 138 PRO B CA 2721 C C . PRO B 138 ? 2.2378 2.0417 2.2317 -0.0368 0.1552 0.0133 138 PRO B C 2722 O O . PRO B 138 ? 2.2436 2.0958 2.2503 -0.0317 0.1507 0.0169 138 PRO B O 2723 C CB . PRO B 138 ? 2.2537 1.9762 2.2313 -0.0180 0.1555 0.0329 138 PRO B CB 2724 C CG . PRO B 138 ? 2.2023 1.9444 2.1896 -0.0008 0.1486 0.0531 138 PRO B CG 2725 C CD . PRO B 138 ? 2.2201 2.0027 2.2165 0.0121 0.1452 0.0494 138 PRO B CD 2726 N N . PHE B 139 ? 2.2615 2.0476 2.2487 -0.0567 0.1598 0.0062 139 PHE B N 2727 C CA . PHE B 139 ? 2.2588 2.0879 2.2554 -0.0705 0.1589 0.0036 139 PHE B CA 2728 C C . PHE B 139 ? 2.3836 2.2069 2.3807 -0.0816 0.1584 0.0151 139 PHE B C 2729 O O . PHE B 139 ? 2.3906 2.2244 2.3865 -0.1005 0.1617 0.0058 139 PHE B O 2730 C CB . PHE B 139 ? 2.1996 2.0395 2.1921 -0.0863 0.1645 -0.0205 139 PHE B CB 2731 C CG . PHE B 139 ? 2.1719 2.0219 2.1645 -0.0751 0.1648 -0.0330 139 PHE B CG 2732 C CD1 . PHE B 139 ? 2.1003 2.0019 2.1064 -0.0627 0.1596 -0.0296 139 PHE B CD1 2733 C CD2 . PHE B 139 ? 2.1965 2.0030 2.1751 -0.0753 0.1699 -0.0469 139 PHE B CD2 2734 C CE1 . PHE B 139 ? 2.0608 1.9745 2.0672 -0.0520 0.1598 -0.0408 139 PHE B CE1 2735 C CE2 . PHE B 139 ? 2.1773 1.9940 2.1558 -0.0635 0.1701 -0.0590 139 PHE B CE2 2736 C CZ . PHE B 139 ? 2.1063 1.9785 2.0992 -0.0520 0.1650 -0.0562 139 PHE B CZ 2737 N N . ASP B 140 ? 2.3390 2.1529 2.3395 -0.0689 0.1536 0.0352 140 ASP B N 2738 C CA . ASP B 140 ? 2.3674 2.1762 2.3691 -0.0751 0.1520 0.0484 140 ASP B CA 2739 C C . ASP B 140 ? 2.3621 2.2109 2.3780 -0.0617 0.1442 0.0630 140 ASP B C 2740 O O . ASP B 140 ? 2.3059 2.1480 2.3246 -0.0540 0.1400 0.0801 140 ASP B O 2741 C CB . ASP B 140 ? 2.3437 2.0999 2.3346 -0.0711 0.1535 0.0589 140 ASP B CB 2742 C CG . ASP B 140 ? 2.2763 2.0324 2.2711 -0.0705 0.1498 0.0764 140 ASP B CG 2743 O OD1 . ASP B 140 ? 2.2612 2.0272 2.2564 -0.0858 0.1514 0.0740 140 ASP B OD1 2744 O OD2 . ASP B 140 ? 2.2401 1.9910 2.2383 -0.0544 0.1451 0.0921 140 ASP B OD2 2745 N N . ASN B 141 ? 2.5280 2.4207 2.5528 -0.0598 0.1421 0.0563 141 ASN B N 2746 C CA . ASN B 141 ? 2.4943 2.4130 2.5294 -0.0437 0.1347 0.0719 141 ASN B CA 2747 C C . ASN B 141 ? 2.2419 2.1961 2.2866 -0.0452 0.1298 0.0807 141 ASN B C 2748 O O . ASN B 141 ? 2.3225 2.3021 2.3695 -0.0564 0.1313 0.0712 141 ASN B O 2749 C CB . ASN B 141 ? 2.7008 2.6421 2.7398 -0.0330 0.1335 0.0659 141 ASN B CB 2750 C CG . ASN B 141 ? 2.8264 2.7307 2.8559 -0.0260 0.1371 0.0602 141 ASN B CG 2751 O OD1 . ASN B 141 ? 2.8370 2.7566 2.8692 -0.0148 0.1356 0.0573 141 ASN B OD1 2752 N ND2 . ASN B 141 ? 2.9020 2.7594 2.9201 -0.0321 0.1416 0.0584 141 ASN B ND2 2753 N N . GLN B 142 ? 1.6733 1.6271 1.7226 -0.0329 0.1237 0.0993 142 GLN B N 2754 C CA . GLN B 142 ? 1.4745 1.4501 1.5310 -0.0306 0.1179 0.1117 142 GLN B CA 2755 C C . GLN B 142 ? 1.1503 1.1521 1.2150 -0.0162 0.1108 0.1243 142 GLN B C 2756 O O . GLN B 142 ? 1.1170 1.1040 1.1811 -0.0057 0.1085 0.1344 142 GLN B O 2757 C CB . GLN B 142 ? 1.3939 1.3365 1.4464 -0.0307 0.1171 0.1239 142 GLN B CB 2758 C CG . GLN B 142 ? 1.5328 1.4636 1.5806 -0.0456 0.1210 0.1185 142 GLN B CG 2759 C CD . GLN B 142 ? 1.5456 1.5020 1.6000 -0.0450 0.1159 0.1264 142 GLN B CD 2760 O OE1 . GLN B 142 ? 1.5801 1.5698 1.6423 -0.0371 0.1107 0.1305 142 GLN B OE1 2761 N NE2 . GLN B 142 ? 1.5550 1.4941 1.6057 -0.0518 0.1170 0.1298 142 GLN B NE2 2762 N N . GLN B 143 ? 1.1211 1.1623 1.1927 -0.0159 0.1073 0.1244 143 GLN B N 2763 C CA . GLN B 143 ? 1.1096 1.1780 1.1881 -0.0038 0.1005 0.1367 143 GLN B CA 2764 C C . GLN B 143 ? 1.0356 1.1088 1.1173 -0.0003 0.0944 0.1513 143 GLN B C 2765 O O . GLN B 143 ? 1.0315 1.1137 1.1135 -0.0070 0.0950 0.1469 143 GLN B O 2766 C CB . GLN B 143 ? 1.1820 1.2930 1.2653 -0.0043 0.1007 0.1267 143 GLN B CB 2767 C CG . GLN B 143 ? 1.1624 1.3002 1.2513 0.0078 0.0945 0.1385 143 GLN B CG 2768 C CD . GLN B 143 ? 1.2483 1.4336 1.3425 0.0074 0.0932 0.1323 143 GLN B CD 2769 O OE1 . GLN B 143 ? 1.2846 1.4920 1.3822 0.0093 0.0888 0.1394 143 GLN B OE1 2770 N NE2 . GLN B 143 ? 1.3572 1.5585 1.4515 0.0058 0.0970 0.1186 143 GLN B NE2 2771 N N . CYS B 144 ? 0.9052 0.9720 0.9886 0.0099 0.0887 0.1680 144 CYS B N 2772 C CA . CYS B 144 ? 0.8800 0.9501 0.9657 0.0142 0.0823 0.1818 144 CYS B CA 2773 C C . CYS B 144 ? 0.8784 0.9733 0.9685 0.0237 0.0755 0.1941 144 CYS B C 2774 O O . CYS B 144 ? 1.0245 1.1138 1.1147 0.0295 0.0734 0.2028 144 CYS B O 2775 C CB . CYS B 144 ? 0.7325 0.7658 0.8145 0.0153 0.0815 0.1916 144 CYS B CB 2776 S SG . CYS B 144 ? 1.2921 1.2960 1.3678 0.0036 0.0892 0.1794 144 CYS B SG 2777 N N . ASN B 145 ? 1.0628 1.1864 1.1561 0.0253 0.0720 0.1952 145 ASN B N 2778 C CA . ASN B 145 ? 1.1366 1.2819 1.2327 0.0339 0.0653 0.2084 145 ASN B CA 2779 C C . ASN B 145 ? 1.1865 1.3144 1.2811 0.0389 0.0589 0.2241 145 ASN B C 2780 O O . ASN B 145 ? 1.3227 1.4397 1.4159 0.0368 0.0591 0.2219 145 ASN B O 2781 C CB . ASN B 145 ? 1.1316 1.3178 1.2310 0.0347 0.0642 0.2028 145 ASN B CB 2782 C CG . ASN B 145 ? 1.1016 1.3115 1.2031 0.0319 0.0686 0.1904 145 ASN B CG 2783 O OD1 . ASN B 145 ? 0.9422 1.1358 1.0421 0.0290 0.0731 0.1838 145 ASN B OD1 2784 N ND2 . ASN B 145 ? 1.1789 1.4281 1.2835 0.0333 0.0674 0.1867 145 ASN B ND2 2785 N N . LEU B 146 ? 1.1149 1.2415 1.2095 0.0450 0.0533 0.2395 146 LEU B N 2786 C CA . LEU B 146 ? 1.0454 1.1583 1.1379 0.0498 0.0465 0.2544 146 LEU B CA 2787 C C . LEU B 146 ? 0.9559 1.0925 1.0490 0.0560 0.0399 0.2664 146 LEU B C 2788 O O . LEU B 146 ? 1.0457 1.1855 1.1388 0.0574 0.0376 0.2760 146 LEU B O 2789 C CB . LEU B 146 ? 1.0532 1.1342 1.1432 0.0496 0.0456 0.2636 146 LEU B CB 2790 C CG . LEU B 146 ? 0.9003 0.9519 0.9882 0.0448 0.0506 0.2566 146 LEU B CG 2791 C CD1 . LEU B 146 ? 0.7911 0.8231 0.8774 0.0457 0.0506 0.2644 146 LEU B CD1 2792 C CD2 . LEU B 146 ? 0.8559 0.8935 0.9420 0.0458 0.0470 0.2611 146 LEU B CD2 2793 N N . THR B 147 ? 0.6616 0.8142 0.7546 0.0600 0.0367 0.2670 147 THR B N 2794 C CA . THR B 147 ? 0.6249 0.8006 0.7174 0.0663 0.0306 0.2784 147 THR B CA 2795 C C . THR B 147 ? 0.7418 0.8982 0.8292 0.0725 0.0224 0.2957 147 THR B C 2796 O O . THR B 147 ? 0.8194 0.9621 0.9046 0.0755 0.0206 0.2949 147 THR B O 2797 C CB . THR B 147 ? 0.6721 0.8828 0.7668 0.0683 0.0320 0.2684 147 THR B CB 2798 O OG1 . THR B 147 ? 0.7680 0.9953 0.8667 0.0615 0.0394 0.2525 147 THR B OG1 2799 C CG2 . THR B 147 ? 0.5619 0.7974 0.6553 0.0758 0.0255 0.2816 147 THR B CG2 2800 N N . PHE B 148 ? 0.8218 0.9761 0.9069 0.0736 0.0177 0.3110 148 PHE B N 2801 C CA . PHE B 148 ? 0.7798 0.9129 0.8588 0.0775 0.0099 0.3283 148 PHE B CA 2802 C C . PHE B 148 ? 0.8291 0.9856 0.9055 0.0831 0.0043 0.3395 148 PHE B C 2803 O O . PHE B 148 ? 0.8360 1.0198 0.9150 0.0813 0.0057 0.3402 148 PHE B O 2804 C CB . PHE B 148 ? 0.5797 0.6899 0.6570 0.0723 0.0087 0.3384 148 PHE B CB 2805 C CG . PHE B 148 ? 0.5954 0.6848 0.6750 0.0673 0.0145 0.3282 148 PHE B CG 2806 C CD1 . PHE B 148 ? 0.6038 0.7055 0.6882 0.0635 0.0218 0.3150 148 PHE B CD1 2807 C CD2 . PHE B 148 ? 0.5790 0.6358 0.6554 0.0669 0.0126 0.3314 148 PHE B CD2 2808 C CE1 . PHE B 148 ? 0.6849 0.7651 0.7701 0.0595 0.0270 0.3067 148 PHE B CE1 2809 C CE2 . PHE B 148 ? 0.5757 0.6144 0.6537 0.0627 0.0178 0.3228 148 PHE B CE2 2810 C CZ . PHE B 148 ? 0.7290 0.7780 0.8111 0.0591 0.0251 0.3109 148 PHE B CZ 2811 N N . GLY B 149 ? 0.7296 0.8753 0.8000 0.0904 -0.0021 0.3488 149 GLY B N 2812 C CA . GLY B 149 ? 0.7949 0.9569 0.8607 0.0962 -0.0083 0.3629 149 GLY B CA 2813 C C . GLY B 149 ? 0.8785 1.0104 0.9354 0.1031 -0.0159 0.3748 149 GLY B C 2814 O O . GLY B 149 ? 1.0659 1.1703 1.1219 0.1031 -0.0155 0.3701 149 GLY B O 2815 N N . SER B 150 ? 0.8100 0.9453 0.8597 0.1089 -0.0227 0.3904 150 SER B N 2816 C CA . SER B 150 ? 0.9611 1.0659 1.0009 0.1169 -0.0303 0.4014 150 SER B CA 2817 C C . SER B 150 ? 1.0814 1.1928 1.1212 0.1291 -0.0305 0.3904 150 SER B C 2818 O O . SER B 150 ? 1.0107 1.1572 1.0566 0.1322 -0.0263 0.3786 150 SER B O 2819 C CB . SER B 150 ? 1.0042 1.1088 1.0349 0.1180 -0.0370 0.4167 150 SER B CB 2820 O OG . SER B 150 ? 1.0919 1.1648 1.1109 0.1241 -0.0434 0.4159 150 SER B OG 2821 N N . TRP B 151 ? 1.2659 1.3449 1.2987 0.1358 -0.0353 0.3935 151 TRP B N 2822 C CA . TRP B 151 ? 1.2374 1.3234 1.2696 0.1483 -0.0359 0.3833 151 TRP B CA 2823 C C . TRP B 151 ? 1.0840 1.1746 1.1068 0.1628 -0.0435 0.3955 151 TRP B C 2824 O O . TRP B 151 ? 1.3946 1.5059 1.4176 0.1749 -0.0439 0.3878 151 TRP B O 2825 C CB . TRP B 151 ? 1.3701 1.4218 1.4003 0.1496 -0.0367 0.3773 151 TRP B CB 2826 C CG . TRP B 151 ? 1.5287 1.5886 1.5567 0.1644 -0.0386 0.3686 151 TRP B CG 2827 C CD1 . TRP B 151 ? 1.6556 1.6978 1.6729 0.1793 -0.0467 0.3771 151 TRP B CD1 2828 C CD2 . TRP B 151 ? 1.6213 1.7106 1.6572 0.1660 -0.0326 0.3498 151 TRP B CD2 2829 N NE1 . TRP B 151 ? 1.7163 1.7776 1.7350 0.1914 -0.0461 0.3646 151 TRP B NE1 2830 C CE2 . TRP B 151 ? 1.6606 1.7521 1.6908 0.1825 -0.0375 0.3478 151 TRP B CE2 2831 C CE3 . TRP B 151 ? 1.6211 1.7342 1.6675 0.1547 -0.0236 0.3345 151 TRP B CE3 2832 C CZ2 . TRP B 151 ? 1.6311 1.7516 1.6664 0.1874 -0.0335 0.3310 151 TRP B CZ2 2833 C CZ3 . TRP B 151 ? 1.6210 1.7597 1.6719 0.1582 -0.0197 0.3180 151 TRP B CZ3 2834 C CH2 . TRP B 151 ? 1.6156 1.7599 1.6613 0.1740 -0.0246 0.3165 151 TRP B CH2 2835 N N . THR B 152 ? 0.9027 0.9727 0.9161 0.1590 -0.0488 0.4076 152 THR B N 2836 C CA . THR B 152 ? 1.0212 1.0846 1.0223 0.1698 -0.0560 0.4124 152 THR B CA 2837 C C . THR B 152 ? 1.1207 1.1968 1.1173 0.1644 -0.0580 0.4224 152 THR B C 2838 O O . THR B 152 ? 1.2132 1.2773 1.1977 0.1712 -0.0643 0.4278 152 THR B O 2839 C CB . THR B 152 ? 1.1649 1.1753 1.1515 0.1708 -0.0627 0.4096 152 THR B CB 2840 O OG1 . THR B 152 ? 1.2476 1.2287 1.2265 0.1551 -0.0646 0.4130 152 THR B OG1 2841 C CG2 . THR B 152 ? 1.1399 1.1341 1.1305 0.1737 -0.0608 0.3996 152 THR B CG2 2842 N N . TYR B 153 ? 1.1497 1.2477 1.1549 0.1521 -0.0531 0.4253 153 TYR B N 2843 C CA . TYR B 153 ? 1.2476 1.3559 1.2484 0.1451 -0.0550 0.4349 153 TYR B CA 2844 C C . TYR B 153 ? 1.3842 1.5468 1.3966 0.1441 -0.0500 0.4382 153 TYR B C 2845 O O . TYR B 153 ? 1.4939 1.6706 1.5165 0.1357 -0.0442 0.4352 153 TYR B O 2846 C CB . TYR B 153 ? 1.2067 1.2820 1.2028 0.1280 -0.0557 0.4360 153 TYR B CB 2847 C CG . TYR B 153 ? 1.1044 1.1272 1.0845 0.1272 -0.0622 0.4349 153 TYR B CG 2848 C CD1 . TYR B 153 ? 1.1481 1.1544 1.1128 0.1313 -0.0690 0.4428 153 TYR B CD1 2849 C CD2 . TYR B 153 ? 0.8803 0.8698 0.8592 0.1222 -0.0616 0.4261 153 TYR B CD2 2850 C CE1 . TYR B 153 ? 1.2139 1.1703 1.1614 0.1310 -0.0752 0.4420 153 TYR B CE1 2851 C CE2 . TYR B 153 ? 0.9465 0.8891 0.9089 0.1218 -0.0677 0.4247 153 TYR B CE2 2852 C CZ . TYR B 153 ? 1.1074 1.0327 1.0537 0.1262 -0.0745 0.4326 153 TYR B CZ 2853 O OH . TYR B 153 ? 1.0589 0.9359 0.9864 0.1263 -0.0808 0.4316 153 TYR B OH 2854 N N . ASN B 154 ? 1.2991 1.4911 1.3085 0.1528 -0.0524 0.4444 154 ASN B N 2855 C CA . ASN B 154 ? 1.2771 1.5233 1.2946 0.1523 -0.0489 0.4480 154 ASN B CA 2856 C C . ASN B 154 ? 1.2854 1.5368 1.3056 0.1363 -0.0468 0.4533 154 ASN B C 2857 O O . ASN B 154 ? 1.2308 1.4464 1.2434 0.1269 -0.0499 0.4572 154 ASN B O 2858 C CB . ASN B 154 ? 1.2414 1.5116 1.2527 0.1643 -0.0529 0.4536 154 ASN B CB 2859 C CG . ASN B 154 ? 1.3422 1.5716 1.3387 0.1638 -0.0595 0.4611 154 ASN B CG 2860 O OD1 . ASN B 154 ? 1.5347 1.7519 1.5273 0.1512 -0.0606 0.4680 154 ASN B OD1 2861 N ND2 . ASN B 154 ? 1.1562 1.3619 1.1434 0.1770 -0.0643 0.4593 154 ASN B ND2 2862 N N . GLY B 155 ? 1.3041 1.6034 1.3333 0.1341 -0.0425 0.4538 155 GLY B N 2863 C CA . GLY B 155 ? 1.2904 1.6039 1.3221 0.1211 -0.0408 0.4592 155 GLY B CA 2864 C C . GLY B 155 ? 1.2070 1.5141 1.2299 0.1167 -0.0455 0.4695 155 GLY B C 2865 O O . GLY B 155 ? 1.1480 1.4658 1.1724 0.1053 -0.0447 0.4746 155 GLY B O 2866 N N . ASN B 156 ? 1.1850 1.4762 1.1983 0.1264 -0.0506 0.4729 156 ASN B N 2867 C CA . ASN B 156 ? 1.3633 1.6429 1.3656 0.1233 -0.0558 0.4837 156 ASN B CA 2868 C C . ASN B 156 ? 1.3638 1.5821 1.3529 0.1178 -0.0609 0.4856 156 ASN B C 2869 O O . ASN B 156 ? 1.3441 1.5456 1.3223 0.1121 -0.0652 0.4947 156 ASN B O 2870 C CB . ASN B 156 ? 1.4687 1.7723 1.4665 0.1380 -0.0585 0.4877 156 ASN B CB 2871 C CG . ASN B 156 ? 1.5708 1.8779 1.5597 0.1343 -0.0625 0.5002 156 ASN B CG 2872 O OD1 . ASN B 156 ? 1.6268 1.8914 1.6013 0.1342 -0.0683 0.5065 156 ASN B OD1 2873 N ND2 . ASN B 156 ? 1.6611 2.0188 1.6577 0.1307 -0.0594 0.5040 156 ASN B ND2 2874 N N . GLN B 157 ? 1.3839 1.5688 1.3726 0.1193 -0.0606 0.4767 157 GLN B N 2875 C CA . GLN B 157 ? 1.3255 1.4581 1.3032 0.1104 -0.0642 0.4766 157 GLN B CA 2876 C C . GLN B 157 ? 1.3145 1.4430 1.3013 0.0968 -0.0594 0.4705 157 GLN B C 2877 O O . GLN B 157 ? 1.3671 1.4719 1.3477 0.0842 -0.0610 0.4731 157 GLN B O 2878 C CB . GLN B 157 ? 1.3146 1.4059 1.2811 0.1216 -0.0689 0.4718 157 GLN B CB 2879 C CG . GLN B 157 ? 1.4058 1.5131 1.3788 0.1378 -0.0675 0.4645 157 GLN B CG 2880 C CD . GLN B 157 ? 1.4922 1.5658 1.4506 0.1515 -0.0743 0.4641 157 GLN B CD 2881 O OE1 . GLN B 157 ? 1.6148 1.6544 1.5569 0.1494 -0.0804 0.4707 157 GLN B OE1 2882 N NE2 . GLN B 157 ? 1.5113 1.5907 1.4743 0.1652 -0.0735 0.4559 157 GLN B NE2 2883 N N . VAL B 158 ? 1.0438 1.1928 1.0439 0.0995 -0.0537 0.4623 158 VAL B N 2884 C CA . VAL B 158 ? 0.8758 1.0238 0.8843 0.0876 -0.0490 0.4575 158 VAL B CA 2885 C C . VAL B 158 ? 0.9951 1.1889 1.0185 0.0885 -0.0423 0.4548 158 VAL B C 2886 O O . VAL B 158 ? 1.0034 1.2166 1.0324 0.0989 -0.0397 0.4505 158 VAL B O 2887 C CB . VAL B 158 ? 1.1497 1.2535 1.1553 0.0859 -0.0493 0.4481 158 VAL B CB 2888 C CG1 . VAL B 158 ? 1.0681 1.1322 1.0584 0.0927 -0.0559 0.4484 158 VAL B CG1 2889 C CG2 . VAL B 158 ? 1.2195 1.3342 1.2364 0.0917 -0.0438 0.4391 158 VAL B CG2 2890 N N . ASP B 159 ? 0.9569 1.1718 0.9852 0.0781 -0.0398 0.4581 159 ASP B N 2891 C CA . ASP B 159 ? 1.0715 1.3262 1.1112 0.0784 -0.0336 0.4554 159 ASP B CA 2892 C C . ASP B 159 ? 1.1376 1.3714 1.1816 0.0708 -0.0299 0.4489 159 ASP B C 2893 O O . ASP B 159 ? 1.1208 1.3287 1.1608 0.0612 -0.0319 0.4495 159 ASP B O 2894 C CB . ASP B 159 ? 1.1656 1.4633 1.2073 0.0739 -0.0333 0.4632 159 ASP B CB 2895 C CG . ASP B 159 ? 1.1512 1.4962 1.2024 0.0776 -0.0274 0.4561 159 ASP B CG 2896 O OD1 . ASP B 159 ? 1.0183 1.3557 1.0770 0.0791 -0.0215 0.4364 159 ASP B OD1 2897 O OD2 . ASP B 159 ? 1.1737 1.5597 1.2264 0.0765 -0.0272 0.4601 159 ASP B OD2 2898 N N . ILE B 160 ? 1.1171 1.3623 1.1693 0.0742 -0.0240 0.4389 160 ILE B N 2899 C CA . ILE B 160 ? 1.0811 1.3025 1.1369 0.0682 -0.0203 0.4310 160 ILE B CA 2900 C C . ILE B 160 ? 1.1109 1.3631 1.1762 0.0649 -0.0130 0.4169 160 ILE B C 2901 O O . ILE B 160 ? 1.0795 1.3551 1.1510 0.0691 -0.0081 0.4013 160 ILE B O 2902 C CB . ILE B 160 ? 1.2192 1.4087 1.2754 0.0734 -0.0190 0.4199 160 ILE B CB 2903 C CG1 . ILE B 160 ? 1.1313 1.3422 1.1943 0.0798 -0.0136 0.4010 160 ILE B CG1 2904 C CG2 . ILE B 160 ? 1.2631 1.4241 1.3095 0.0779 -0.0261 0.4285 160 ILE B CG2 2905 C CD1 . ILE B 160 ? 1.1569 1.3621 1.2274 0.0764 -0.0060 0.3825 160 ILE B CD1 2906 N N . PHE B 161 ? 1.1086 1.3619 1.1742 0.0573 -0.0126 0.4224 161 PHE B N 2907 C CA . PHE B 161 ? 1.0223 1.3040 1.0956 0.0551 -0.0064 0.4104 161 PHE B CA 2908 C C . PHE B 161 ? 0.8754 1.1328 0.9519 0.0529 -0.0020 0.4003 161 PHE B C 2909 O O . PHE B 161 ? 1.0526 1.2803 1.1245 0.0489 -0.0050 0.4098 161 PHE B O 2910 C CB . PHE B 161 ? 1.0670 1.3777 1.1386 0.0494 -0.0091 0.4240 161 PHE B CB 2911 C CG . PHE B 161 ? 0.9795 1.3137 1.0465 0.0507 -0.0140 0.4373 161 PHE B CG 2912 C CD1 . PHE B 161 ? 1.0327 1.4049 1.1046 0.0559 -0.0112 0.4279 161 PHE B CD1 2913 C CD2 . PHE B 161 ? 0.9873 1.3041 1.0450 0.0463 -0.0213 0.4571 161 PHE B CD2 2914 C CE1 . PHE B 161 ? 1.1801 1.5749 1.2474 0.0581 -0.0160 0.4409 161 PHE B CE1 2915 C CE2 . PHE B 161 ? 1.0151 1.3489 1.0689 0.0472 -0.0254 0.4643 161 PHE B CE2 2916 C CZ . PHE B 161 ? 1.1197 1.4961 1.1765 0.0547 -0.0236 0.4641 161 PHE B CZ 2917 N N . ASN B 162 ? 0.6877 0.9577 0.7711 0.0552 0.0052 0.3814 162 ASN B N 2918 C CA . ASN B 162 ? 0.8609 1.1116 0.9466 0.0537 0.0095 0.3730 162 ASN B CA 2919 C C . ASN B 162 ? 1.0249 1.2874 1.1094 0.0491 0.0078 0.3836 162 ASN B C 2920 O O . ASN B 162 ? 1.1542 1.4522 1.2397 0.0480 0.0068 0.3882 162 ASN B O 2921 C CB . ASN B 162 ? 0.9250 1.1852 1.0168 0.0571 0.0175 0.3507 162 ASN B CB 2922 C CG . ASN B 162 ? 1.0530 1.3565 1.1487 0.0589 0.0196 0.3440 162 ASN B CG 2923 O OD1 . ASN B 162 ? 1.2335 1.5601 1.3278 0.0591 0.0155 0.3534 162 ASN B OD1 2924 N ND2 . ASN B 162 ? 1.0792 1.3932 1.1791 0.0607 0.0260 0.3273 162 ASN B ND2 2925 N N . ALA B 163 ? 0.8518 1.0875 0.9341 0.0460 0.0072 0.3880 163 ALA B N 2926 C CA . ALA B 163 ? 0.8355 1.0849 0.9167 0.0414 0.0057 0.3975 163 ALA B CA 2927 C C . ALA B 163 ? 0.8080 1.0839 0.8949 0.0456 0.0117 0.3838 163 ALA B C 2928 O O . ALA B 163 ? 0.9946 1.2993 1.0818 0.0433 0.0105 0.3902 163 ALA B O 2929 C CB . ALA B 163 ? 1.0765 1.2936 1.1542 0.0372 0.0039 0.4044 163 ALA B CB 2930 N N . LEU B 164 ? 0.7889 1.0547 0.8796 0.0516 0.0179 0.3651 164 LEU B N 2931 C CA . LEU B 164 ? 1.0006 1.2918 1.0957 0.0569 0.0236 0.3500 164 LEU B CA 2932 C C . LEU B 164 ? 1.2106 1.4896 1.3085 0.0615 0.0299 0.3295 164 LEU B C 2933 O O . LEU B 164 ? 1.2749 1.5251 1.3717 0.0606 0.0304 0.3268 164 LEU B O 2934 C CB . LEU B 164 ? 0.9917 1.2843 1.0867 0.0586 0.0252 0.3502 164 LEU B CB 2935 C CG . LEU B 164 ? 1.1294 1.3933 1.2233 0.0620 0.0284 0.3447 164 LEU B CG 2936 C CD1 . LEU B 164 ? 1.2071 1.4676 1.3032 0.0702 0.0358 0.3235 164 LEU B CD1 2937 C CD2 . LEU B 164 ? 0.9687 1.2493 1.0611 0.0604 0.0256 0.3562 164 LEU B CD2 2938 N N . ASP B 165 ? 1.3271 1.6299 1.4283 0.0660 0.0347 0.3150 165 ASP B N 2939 C CA . ASP B 165 ? 1.4155 1.7164 1.5190 0.0685 0.0405 0.2952 165 ASP B CA 2940 C C . ASP B 165 ? 1.3495 1.6132 1.4513 0.0706 0.0459 0.2827 165 ASP B C 2941 O O . ASP B 165 ? 1.2182 1.4808 1.3209 0.0730 0.0518 0.2645 165 ASP B O 2942 C CB . ASP B 165 ? 1.5753 1.9156 1.6820 0.0721 0.0436 0.2834 165 ASP B CB 2943 C CG . ASP B 165 ? 1.6601 2.0401 1.7687 0.0698 0.0393 0.2925 165 ASP B CG 2944 O OD1 . ASP B 165 ? 1.6655 2.0468 1.7717 0.0659 0.0331 0.3123 165 ASP B OD1 2945 O OD2 . ASP B 165 ? 1.6636 2.0726 1.7751 0.0714 0.0421 0.2799 165 ASP B OD2 2946 N N . SER B 166 ? 1.4028 1.6355 1.5017 0.0690 0.0438 0.2927 166 SER B N 2947 C CA . SER B 166 ? 1.5883 1.7828 1.6850 0.0696 0.0480 0.2837 166 SER B CA 2948 C C . SER B 166 ? 1.6066 1.7747 1.7009 0.0656 0.0437 0.2973 166 SER B C 2949 O O . SER B 166 ? 1.5869 1.7641 1.6805 0.0628 0.0376 0.3131 166 SER B O 2950 C CB . SER B 166 ? 1.7067 1.8914 1.8016 0.0755 0.0519 0.2776 166 SER B CB 2951 O OG . SER B 166 ? 1.7983 2.0031 1.8946 0.0802 0.0565 0.2621 166 SER B OG 2952 N N . GLY B 167 ? 1.6671 1.8029 1.7596 0.0646 0.0467 0.2906 167 GLY B N 2953 C CA . GLY B 167 ? 1.7217 1.8298 1.8114 0.0620 0.0433 0.3018 167 GLY B CA 2954 C C . GLY B 167 ? 1.6915 1.7855 1.7791 0.0651 0.0450 0.3036 167 GLY B C 2955 O O . GLY B 167 ? 1.7104 1.7965 1.7972 0.0691 0.0508 0.2912 167 GLY B O 2956 N N . ASP B 168 ? 1.6824 1.7731 1.7684 0.0635 0.0400 0.3187 168 ASP B N 2957 C CA . ASP B 168 ? 1.5972 1.6799 1.6812 0.0668 0.0409 0.3221 168 ASP B CA 2958 C C . ASP B 168 ? 1.4398 1.4905 1.5212 0.0698 0.0461 0.3131 168 ASP B C 2959 O O . ASP B 168 ? 1.2718 1.2969 1.3514 0.0664 0.0454 0.3158 168 ASP B O 2960 C CB . ASP B 168 ? 1.6610 1.7414 1.7432 0.0620 0.0347 0.3394 168 ASP B CB 2961 C CG . ASP B 168 ? 1.8213 1.9003 1.9017 0.0655 0.0354 0.3430 168 ASP B CG 2962 O OD1 . ASP B 168 ? 1.7997 1.8941 1.8810 0.0724 0.0391 0.3355 168 ASP B OD1 2963 O OD2 . ASP B 168 ? 1.9045 1.9678 1.9825 0.0619 0.0324 0.3525 168 ASP B OD2 2964 N N . LEU B 169 ? 1.3919 1.4444 1.4725 0.0766 0.0513 0.3026 169 LEU B N 2965 C CA . LEU B 169 ? 1.3194 1.3414 1.3959 0.0805 0.0563 0.2952 169 LEU B CA 2966 C C . LEU B 169 ? 1.4194 1.4306 1.4935 0.0820 0.0537 0.3071 169 LEU B C 2967 O O . LEU B 169 ? 1.3422 1.3284 1.4144 0.0784 0.0533 0.3106 169 LEU B O 2968 C CB . LEU B 169 ? 1.3514 1.3764 1.4262 0.0885 0.0622 0.2807 169 LEU B CB 2969 C CG . LEU B 169 ? 1.2666 1.3250 1.3432 0.0958 0.0622 0.2775 169 LEU B CG 2970 C CD1 . LEU B 169 ? 1.2122 1.2825 1.2875 0.1033 0.0602 0.2864 169 LEU B CD1 2971 C CD2 . LEU B 169 ? 1.0807 1.1365 1.1554 0.1012 0.0685 0.2586 169 LEU B CD2 2972 N N . SER B 170 ? 1.5006 1.5350 1.5753 0.0865 0.0515 0.3137 170 SER B N 2973 C CA . SER B 170 ? 1.6114 1.6438 1.6837 0.0895 0.0495 0.3238 170 SER B CA 2974 C C . SER B 170 ? 1.6547 1.6544 1.7237 0.0873 0.0497 0.3279 170 SER B C 2975 O O . SER B 170 ? 1.5661 1.5519 1.6314 0.0946 0.0529 0.3259 170 SER B O 2976 C CB . SER B 170 ? 1.5119 1.5733 1.5865 0.0839 0.0431 0.3379 170 SER B CB 2977 O OG . SER B 170 ? 1.5245 1.5720 1.5984 0.0746 0.0384 0.3489 170 SER B OG 2978 N N . ASP B 171 ? 1.7296 1.7179 1.7994 0.0782 0.0463 0.3336 171 ASP B N 2979 C CA . ASP B 171 ? 1.6313 1.5899 1.6984 0.0753 0.0465 0.3361 171 ASP B CA 2980 C C . ASP B 171 ? 1.7149 1.6506 1.7811 0.0740 0.0510 0.3248 171 ASP B C 2981 O O . ASP B 171 ? 1.8584 1.7764 1.9240 0.0685 0.0499 0.3263 171 ASP B O 2982 C CB . ASP B 171 ? 1.5947 1.5538 1.6626 0.0666 0.0399 0.3480 171 ASP B CB 2983 C CG . ASP B 171 ? 1.7210 1.7077 1.7900 0.0641 0.0350 0.3588 171 ASP B CG 2984 O OD1 . ASP B 171 ? 1.7725 1.7721 1.8407 0.0690 0.0357 0.3614 171 ASP B OD1 2985 O OD2 . ASP B 171 ? 1.6322 1.6292 1.7023 0.0571 0.0302 0.3619 171 ASP B OD2 2986 N N . PHE B 172 ? 1.6681 1.6055 1.7339 0.0786 0.0561 0.3128 172 PHE B N 2987 C CA . PHE B 172 ? 1.4539 1.3688 1.5173 0.0770 0.0616 0.3008 172 PHE B CA 2988 C C . PHE B 172 ? 1.6429 1.5311 1.7003 0.0818 0.0654 0.3002 172 PHE B C 2989 O O . PHE B 172 ? 1.6776 1.5705 1.7332 0.0893 0.0649 0.3055 172 PHE B O 2990 C CB . PHE B 172 ? 1.2153 1.1431 1.2799 0.0789 0.0653 0.2879 172 PHE B CB 2991 C CG . PHE B 172 ? 1.1768 1.0803 1.2371 0.0777 0.0719 0.2744 172 PHE B CG 2992 C CD1 . PHE B 172 ? 1.1252 1.0140 1.1853 0.0691 0.0731 0.2707 172 PHE B CD1 2993 C CD2 . PHE B 172 ? 1.2164 1.1123 1.2723 0.0850 0.0770 0.2648 172 PHE B CD2 2994 C CE1 . PHE B 172 ? 1.1253 0.9930 1.1808 0.0657 0.0793 0.2584 172 PHE B CE1 2995 C CE2 . PHE B 172 ? 1.2554 1.1261 1.3059 0.0823 0.0832 0.2524 172 PHE B CE2 2996 C CZ . PHE B 172 ? 1.2214 1.0785 1.2718 0.0716 0.0844 0.2494 172 PHE B CZ 2997 N N . ILE B 173 ? 1.6838 1.5459 1.7378 0.0777 0.0693 0.2941 173 ILE B N 2998 C CA . ILE B 173 ? 1.7335 1.5688 1.7815 0.0804 0.0719 0.2968 173 ILE B CA 2999 C C . ILE B 173 ? 1.7910 1.6020 1.8320 0.0831 0.0792 0.2853 173 ILE B C 3000 O O . ILE B 173 ? 2.0395 1.8298 2.0740 0.0888 0.0818 0.2877 173 ILE B O 3001 C CB . ILE B 173 ? 1.2617 1.0847 1.3103 0.0721 0.0694 0.3027 173 ILE B CB 3002 C CG1 . ILE B 173 ? 1.2700 1.1114 1.3233 0.0701 0.0622 0.3145 173 ILE B CG1 3003 C CG2 . ILE B 173 ? 1.0863 0.8835 1.1285 0.0742 0.0722 0.3060 173 ILE B CG2 3004 C CD1 . ILE B 173 ? 1.2338 1.0672 1.2852 0.0619 0.0576 0.3114 173 ILE B CD1 3005 N N . GLU B 174 ? 1.6143 1.4286 1.6560 0.0797 0.0823 0.2730 174 GLU B N 3006 C CA . GLU B 174 ? 1.5418 1.3310 1.5759 0.0801 0.0891 0.2613 174 GLU B CA 3007 C C . GLU B 174 ? 1.7207 1.4798 1.7492 0.0727 0.0920 0.2622 174 GLU B C 3008 O O . GLU B 174 ? 1.7220 1.4601 1.7441 0.0780 0.0934 0.2679 174 GLU B O 3009 C CB . GLU B 174 ? 1.6733 1.4554 1.7015 0.0939 0.0914 0.2602 174 GLU B CB 3010 C CG . GLU B 174 ? 1.7967 1.6034 1.8278 0.1011 0.0912 0.2531 174 GLU B CG 3011 C CD . GLU B 174 ? 2.0056 1.8465 2.0434 0.1072 0.0852 0.2636 174 GLU B CD 3012 O OE1 . GLU B 174 ? 2.0430 1.8903 2.0843 0.1038 0.0807 0.2762 174 GLU B OE1 3013 O OE2 . GLU B 174 ? 2.0896 1.9518 2.1289 0.1148 0.0851 0.2587 174 GLU B OE2 3014 N N . ASP B 175 ? 1.7523 1.5108 1.7828 0.0609 0.0929 0.2569 175 ASP B N 3015 C CA . ASP B 175 ? 1.8826 1.6135 1.9068 0.0537 0.0962 0.2572 175 ASP B CA 3016 C C . ASP B 175 ? 1.9186 1.6181 1.9318 0.0542 0.1034 0.2485 175 ASP B C 3017 O O . ASP B 175 ? 1.8225 1.5206 1.8329 0.0633 0.1049 0.2444 175 ASP B O 3018 C CB . ASP B 175 ? 2.0708 1.8129 2.1002 0.0414 0.0947 0.2545 175 ASP B CB 3019 C CG . ASP B 175 ? 2.1165 1.8633 2.1458 0.0323 0.0987 0.2401 175 ASP B CG 3020 O OD1 . ASP B 175 ? 2.1510 1.8831 2.1742 0.0311 0.1042 0.2302 175 ASP B OD1 3021 O OD2 . ASP B 175 ? 2.1251 1.8922 2.1607 0.0262 0.0960 0.2386 175 ASP B OD2 3022 N N . VAL B 176 ? 2.0411 1.7139 2.0467 0.0456 0.1078 0.2460 176 VAL B N 3023 C CA . VAL B 176 ? 1.9530 1.5922 1.9463 0.0494 0.1137 0.2413 176 VAL B CA 3024 C C . VAL B 176 ? 2.0398 1.6720 2.0291 0.0427 0.1189 0.2245 176 VAL B C 3025 O O . VAL B 176 ? 2.0934 1.7023 2.0734 0.0487 0.1229 0.2187 176 VAL B O 3026 C CB . VAL B 176 ? 2.1704 1.7780 2.1543 0.0455 0.1164 0.2488 176 VAL B CB 3027 C CG1 . VAL B 176 ? 2.1829 1.7517 2.1523 0.0477 0.1227 0.2435 176 VAL B CG1 3028 C CG2 . VAL B 176 ? 2.1337 1.7471 2.1199 0.0568 0.1117 0.2642 176 VAL B CG2 3029 N N . GLU B 177 ? 1.9627 1.6120 1.9575 0.0295 0.1192 0.2166 177 GLU B N 3030 C CA . GLU B 177 ? 2.1718 1.8564 2.1765 0.0307 0.1164 0.2099 177 GLU B CA 3031 C C . GLU B 177 ? 1.9275 1.6306 1.9358 0.0200 0.1184 0.1957 177 GLU B C 3032 O O . GLU B 177 ? 2.0002 1.6875 2.0014 0.0118 0.1242 0.1825 177 GLU B O 3033 C CB . GLU B 177 ? 2.3519 2.0431 2.3567 0.0456 0.1154 0.2087 177 GLU B CB 3034 C CG . GLU B 177 ? 2.4649 2.1929 2.4815 0.0526 0.1081 0.2190 177 GLU B CG 3035 C CD . GLU B 177 ? 2.4315 2.1758 2.4505 0.0669 0.1057 0.2213 177 GLU B CD 3036 O OE1 . GLU B 177 ? 2.3707 2.1332 2.3926 0.0681 0.1062 0.2117 177 GLU B OE1 3037 O OE2 . GLU B 177 ? 2.4275 2.1668 2.4449 0.0771 0.1035 0.2319 177 GLU B OE2 3038 N N . TRP B 178 ? 1.7976 1.5366 1.8173 0.0217 0.1127 0.2001 178 TRP B N 3039 C CA . TRP B 178 ? 1.8676 1.6397 1.8948 0.0204 0.1113 0.1917 178 TRP B CA 3040 C C . TRP B 178 ? 1.8798 1.6722 1.9128 0.0346 0.1062 0.1999 178 TRP B C 3041 O O . TRP B 178 ? 1.9407 1.7390 1.9775 0.0405 0.1010 0.2141 178 TRP B O 3042 C CB . TRP B 178 ? 1.6824 1.4796 1.7169 0.0114 0.1085 0.1919 178 TRP B CB 3043 C CG . TRP B 178 ? 1.6357 1.4239 1.6658 -0.0034 0.1136 0.1810 178 TRP B CG 3044 C CD1 . TRP B 178 ? 1.6632 1.4398 1.6909 -0.0116 0.1143 0.1846 178 TRP B CD1 3045 C CD2 . TRP B 178 ? 1.6760 1.4668 1.7029 -0.0127 0.1190 0.1641 178 TRP B CD2 3046 N NE1 . TRP B 178 ? 1.6599 1.4336 1.6833 -0.0261 0.1197 0.1715 178 TRP B NE1 3047 C CE2 . TRP B 178 ? 1.6695 1.4508 1.6921 -0.0275 0.1228 0.1586 178 TRP B CE2 3048 C CE3 . TRP B 178 ? 1.8060 1.6081 1.8332 -0.0105 0.1211 0.1525 178 TRP B CE3 3049 C CZ2 . TRP B 178 ? 1.7810 1.5631 1.7993 -0.0413 0.1286 0.1422 178 TRP B CZ2 3050 C CZ3 . TRP B 178 ? 1.8750 1.6769 1.8980 -0.0235 0.1268 0.1356 178 TRP B CZ3 3051 C CH2 . TRP B 178 ? 1.8754 1.6671 1.8939 -0.0392 0.1305 0.1306 178 TRP B CH2 3052 N N . GLU B 179 ? 1.9411 1.7464 1.9745 0.0384 0.1079 0.1897 179 GLU B N 3053 C CA . GLU B 179 ? 1.8390 1.6553 1.8737 0.0522 0.1058 0.1927 179 GLU B CA 3054 C C . GLU B 179 ? 1.5931 1.4501 1.6364 0.0551 0.1024 0.1904 179 GLU B C 3055 O O . GLU B 179 ? 1.6144 1.4814 1.6573 0.0525 0.1057 0.1761 179 GLU B O 3056 C CB . GLU B 179 ? 2.0318 1.8197 2.0562 0.0575 0.1117 0.1820 179 GLU B CB 3057 C CG . GLU B 179 ? 2.1437 1.9188 2.1627 0.0458 0.1177 0.1650 179 GLU B CG 3058 C CD . GLU B 179 ? 2.3391 2.0894 2.3533 0.0327 0.1204 0.1662 179 GLU B CD 3059 O OE1 . GLU B 179 ? 2.3578 2.0766 2.3648 0.0347 0.1215 0.1742 179 GLU B OE1 3060 O OE2 . GLU B 179 ? 2.3782 2.1474 2.3977 0.0210 0.1201 0.1619 179 GLU B OE2 3061 N N . VAL B 180 ? 1.2199 1.0994 1.2699 0.0605 0.0961 0.2044 180 VAL B N 3062 C CA . VAL B 180 ? 1.3556 1.2742 1.4131 0.0629 0.0924 0.2047 180 VAL B CA 3063 C C . VAL B 180 ? 1.7252 1.6544 1.7812 0.0712 0.0948 0.1950 180 VAL B C 3064 O O . VAL B 180 ? 1.7839 1.7087 1.8373 0.0818 0.0942 0.1997 180 VAL B O 3065 C CB . VAL B 180 ? 1.2611 1.1958 1.3238 0.0669 0.0853 0.2227 180 VAL B CB 3066 C CG1 . VAL B 180 ? 0.8635 0.8390 0.9324 0.0725 0.0811 0.2263 180 VAL B CG1 3067 C CG2 . VAL B 180 ? 1.0234 0.9532 1.0884 0.0587 0.0823 0.2302 180 VAL B CG2 3068 N N . HIS B 181 ? 2.1470 2.0924 2.2045 0.0663 0.0975 0.1807 181 HIS B N 3069 C CA . HIS B 181 ? 2.2111 2.1717 2.2679 0.0731 0.0998 0.1690 181 HIS B CA 3070 C C . HIS B 181 ? 2.0882 2.0946 2.1538 0.0761 0.0945 0.1753 181 HIS B C 3071 O O . HIS B 181 ? 2.1598 2.1854 2.2264 0.0858 0.0932 0.1757 181 HIS B O 3072 C CB . HIS B 181 ? 2.3601 2.3117 2.4128 0.0649 0.1060 0.1489 181 HIS B CB 3073 C CG . HIS B 181 ? 2.5499 2.4548 2.5915 0.0639 0.1118 0.1413 181 HIS B CG 3074 N ND1 . HIS B 181 ? 2.6690 2.5416 2.7062 0.0603 0.1121 0.1508 181 HIS B ND1 3075 C CD2 . HIS B 181 ? 2.6307 2.5140 2.6638 0.0667 0.1173 0.1258 181 HIS B CD2 3076 C CE1 . HIS B 181 ? 2.7147 2.5484 2.7411 0.0603 0.1176 0.1423 181 HIS B CE1 3077 N NE2 . HIS B 181 ? 2.7208 2.5582 2.7439 0.0643 0.1208 0.1270 181 HIS B NE2 3078 N N . GLY B 182 ? 1.7754 1.7998 1.8466 0.0679 0.0914 0.1806 182 GLY B N 3079 C CA . GLY B 182 ? 1.5634 1.6285 1.6420 0.0697 0.0858 0.1896 182 GLY B CA 3080 C C . GLY B 182 ? 1.3790 1.4477 1.4612 0.0635 0.0809 0.2026 182 GLY B C 3081 O O . GLY B 182 ? 1.2076 1.2576 1.2880 0.0564 0.0829 0.1989 182 GLY B O 3082 N N . MET B 183 ? 1.4675 1.5604 1.5540 0.0662 0.0746 0.2175 183 MET B N 3083 C CA . MET B 183 ? 1.4363 1.5380 1.5259 0.0615 0.0694 0.2289 183 MET B CA 3084 C C . MET B 183 ? 1.2662 1.4087 1.3604 0.0630 0.0646 0.2359 183 MET B C 3085 O O . MET B 183 ? 1.2039 1.3536 1.2991 0.0637 0.0585 0.2527 183 MET B O 3086 C CB . MET B 183 ? 1.5095 1.5870 1.5971 0.0620 0.0654 0.2447 183 MET B CB 3087 C CG . MET B 183 ? 1.5520 1.6246 1.6405 0.0571 0.0614 0.2526 183 MET B CG 3088 S SD . MET B 183 ? 1.1358 1.1896 1.2226 0.0577 0.0549 0.2728 183 MET B SD 3089 C CE . MET B 183 ? 1.0495 1.0987 1.1368 0.0534 0.0518 0.2749 183 MET B CE 3090 N N . PRO B 184 ? 1.2582 1.4276 1.3547 0.0625 0.0674 0.2231 184 PRO B N 3091 C CA . PRO B 184 ? 1.1789 1.3893 1.2795 0.0644 0.0629 0.2304 184 PRO B CA 3092 C C . PRO B 184 ? 1.0478 1.2663 1.1498 0.0613 0.0572 0.2434 184 PRO B C 3093 O O . PRO B 184 ? 1.2059 1.4109 1.3072 0.0576 0.0582 0.2392 184 PRO B O 3094 C CB . PRO B 184 ? 1.2163 1.4512 1.3187 0.0638 0.0678 0.2115 184 PRO B CB 3095 C CG . PRO B 184 ? 1.2242 1.4316 1.3239 0.0582 0.0735 0.1965 184 PRO B CG 3096 C CD . PRO B 184 ? 1.2210 1.3861 1.3163 0.0592 0.0743 0.2021 184 PRO B CD 3097 N N . ALA B 185 ? 0.8444 1.0858 0.9475 0.0630 0.0513 0.2587 185 ALA B N 3098 C CA . ALA B 185 ? 0.7359 0.9826 0.8387 0.0614 0.0453 0.2723 185 ALA B CA 3099 C C . ALA B 185 ? 0.9093 1.1975 1.0150 0.0621 0.0439 0.2712 185 ALA B C 3100 O O . ALA B 185 ? 0.9714 1.2875 1.0791 0.0639 0.0450 0.2681 185 ALA B O 3101 C CB . ALA B 185 ? 0.8380 1.0740 0.9382 0.0615 0.0391 0.2928 185 ALA B CB 3102 N N . VAL B 186 ? 0.9325 1.2260 1.0381 0.0616 0.0414 0.2740 186 VAL B N 3103 C CA . VAL B 186 ? 0.6112 0.9440 0.7192 0.0626 0.0405 0.2711 186 VAL B CA 3104 C C . VAL B 186 ? 0.7040 1.0391 0.8094 0.0646 0.0336 0.2873 186 VAL B C 3105 O O . VAL B 186 ? 0.9880 1.2946 1.0908 0.0647 0.0319 0.2909 186 VAL B O 3106 C CB . VAL B 186 ? 0.5893 0.9296 0.6998 0.0603 0.0472 0.2487 186 VAL B CB 3107 C CG1 . VAL B 186 ? 0.6481 1.0321 0.7612 0.0615 0.0460 0.2457 186 VAL B CG1 3108 C CG2 . VAL B 186 ? 0.5587 0.8951 0.6703 0.0589 0.0540 0.2322 186 VAL B CG2 3109 N N . LYS B 187 ? 0.6871 1.0558 0.7926 0.0667 0.0295 0.2971 187 LYS B N 3110 C CA . LYS B 187 ? 0.7008 1.0717 0.8024 0.0699 0.0227 0.3132 187 LYS B CA 3111 C C . LYS B 187 ? 0.8256 1.2332 0.9295 0.0730 0.0235 0.3052 187 LYS B C 3112 O O . LYS B 187 ? 0.9408 1.3858 1.0481 0.0726 0.0255 0.2994 187 LYS B O 3113 C CB . LYS B 187 ? 0.7438 1.1218 0.8417 0.0694 0.0164 0.3347 187 LYS B CB 3114 C CG . LYS B 187 ? 0.8507 1.2296 0.9427 0.0730 0.0088 0.3530 187 LYS B CG 3115 C CD . LYS B 187 ? 1.0039 1.3953 1.0919 0.0703 0.0034 0.3734 187 LYS B CD 3116 C CE . LYS B 187 ? 1.0428 1.4317 1.1231 0.0737 -0.0044 0.3929 187 LYS B CE 3117 N NZ . LYS B 187 ? 1.0941 1.5122 1.1761 0.0804 -0.0038 0.3859 187 LYS B NZ 3118 N N . ASN B 188 ? 0.6154 1.0146 0.7175 0.0763 0.0219 0.3044 188 ASN B N 3119 C CA . ASN B 188 ? 0.7273 1.1620 0.8313 0.0799 0.0225 0.2968 188 ASN B CA 3120 C C . ASN B 188 ? 0.7778 1.2111 0.8760 0.0875 0.0147 0.3146 188 ASN B C 3121 O O . ASN B 188 ? 0.7213 1.1227 0.8140 0.0889 0.0094 0.3311 188 ASN B O 3122 C CB . ASN B 188 ? 0.8579 1.2892 0.9653 0.0769 0.0290 0.2748 188 ASN B CB 3123 C CG . ASN B 188 ? 1.0596 1.4875 1.1710 0.0696 0.0367 0.2570 188 ASN B CG 3124 O OD1 . ASN B 188 ? 1.1507 1.5920 1.2635 0.0685 0.0375 0.2582 188 ASN B OD1 3125 N ND2 . ASN B 188 ? 1.0310 1.4400 1.1433 0.0648 0.0422 0.2407 188 ASN B ND2 3126 N N . VAL B 189 ? 0.8947 1.3637 0.9936 0.0928 0.0138 0.3118 189 VAL B N 3127 C CA . VAL B 189 ? 0.9667 1.4321 1.0595 0.1022 0.0070 0.3256 189 VAL B CA 3128 C C . VAL B 189 ? 0.9872 1.4654 1.0822 0.1059 0.0098 0.3101 189 VAL B C 3129 O O . VAL B 189 ? 1.1057 1.6090 1.2070 0.1007 0.0165 0.2903 189 VAL B O 3130 C CB . VAL B 189 ? 0.9719 1.4689 1.0611 0.1077 0.0016 0.3417 189 VAL B CB 3131 C CG1 . VAL B 189 ? 0.8726 1.3534 0.9578 0.1033 -0.0023 0.3602 189 VAL B CG1 3132 C CG2 . VAL B 189 ? 1.0330 1.5825 1.1287 0.1064 0.0063 0.3274 189 VAL B CG2 3133 N N . ILE B 190 ? 0.8592 1.3177 0.9486 0.1143 0.0048 0.3183 190 ILE B N 3134 C CA . ILE B 190 ? 0.6453 1.1182 0.7357 0.1200 0.0060 0.3065 190 ILE B CA 3135 C C . ILE B 190 ? 0.7850 1.2770 0.8690 0.1340 -0.0014 0.3211 190 ILE B C 3136 O O . ILE B 190 ? 0.8808 1.3494 0.9571 0.1400 -0.0086 0.3420 190 ILE B O 3137 C CB . ILE B 190 ? 0.7894 1.2228 0.8783 0.1193 0.0066 0.3017 190 ILE B CB 3138 C CG1 . ILE B 190 ? 0.7815 1.1846 0.8738 0.1072 0.0119 0.2946 190 ILE B CG1 3139 C CG2 . ILE B 190 ? 1.0110 1.4668 1.1033 0.1203 0.0107 0.2832 190 ILE B CG2 3140 C CD1 . ILE B 190 ? 0.7719 1.1958 0.8715 0.0970 0.0210 0.2717 190 ILE B CD1 3141 N N . SER B 191 ? 0.8029 1.3389 0.8899 0.1388 0.0004 0.3105 191 SER B N 3142 C CA . SER B 191 ? 0.9784 1.5423 1.0597 0.1531 -0.0061 0.3233 191 SER B CA 3143 C C . SER B 191 ? 0.8954 1.4399 0.9690 0.1680 -0.0125 0.3317 191 SER B C 3144 O O . SER B 191 ? 0.8951 1.4274 0.9596 0.1789 -0.0203 0.3523 191 SER B O 3145 C CB . SER B 191 ? 1.0467 1.6695 1.1345 0.1522 -0.0014 0.3078 191 SER B CB 3146 O OG . SER B 191 ? 1.1280 1.7528 1.2228 0.1422 0.0064 0.2838 191 SER B OG 3147 N N . TYR B 192 ? 0.6964 1.2428 0.7729 0.1689 -0.0091 0.3152 192 TYR B N 3148 C CA . TYR B 192 ? 0.8051 1.3368 0.8749 0.1839 -0.0147 0.3199 192 TYR B CA 3149 C C . TYR B 192 ? 0.9807 1.5458 1.0445 0.2019 -0.0208 0.3297 192 TYR B C 3150 O O . TYR B 192 ? 1.1740 1.7351 1.2305 0.2091 -0.0270 0.3501 192 TYR B O 3151 C CB . TYR B 192 ? 0.9881 1.4606 1.0504 0.1857 -0.0200 0.3356 192 TYR B CB 3152 C CG . TYR B 192 ? 0.8242 1.2638 0.8915 0.1719 -0.0145 0.3238 192 TYR B CG 3153 C CD1 . TYR B 192 ? 0.6861 1.1246 0.7566 0.1714 -0.0108 0.3073 192 TYR B CD1 3154 C CD2 . TYR B 192 ? 0.6929 1.1058 0.7617 0.1596 -0.0128 0.3292 192 TYR B CD2 3155 C CE1 . TYR B 192 ? 0.8024 1.2126 0.8770 0.1587 -0.0056 0.2972 192 TYR B CE1 3156 C CE2 . TYR B 192 ? 0.6537 1.0382 0.7266 0.1481 -0.0076 0.3188 192 TYR B CE2 3157 C CZ . TYR B 192 ? 0.7757 1.1580 0.8513 0.1476 -0.0041 0.3033 192 TYR B CZ 3158 O OH . TYR B 192 ? 0.9565 1.3097 1.0355 0.1359 0.0010 0.2944 192 TYR B OH 3159 N N . GLY B 193 ? 0.9357 1.5343 1.0018 0.2092 -0.0190 0.3155 193 GLY B N 3160 C CA . GLY B 193 ? 0.8454 1.4861 0.9072 0.2264 -0.0236 0.3213 193 GLY B CA 3161 C C . GLY B 193 ? 0.9778 1.5887 1.0264 0.2465 -0.0338 0.3433 193 GLY B C 3162 O O . GLY B 193 ? 1.1226 1.7616 1.1650 0.2636 -0.0391 0.3527 193 GLY B O 3163 N N . CYS B 194 ? 1.0280 1.5806 1.0715 0.2444 -0.0367 0.3517 194 CYS B N 3164 C CA . CYS B 194 ? 1.1665 1.6798 1.1967 0.2617 -0.0460 0.3700 194 CYS B CA 3165 C C . CYS B 194 ? 1.1044 1.6137 1.1248 0.2691 -0.0530 0.3945 194 CYS B C 3166 O O . CYS B 194 ? 1.0628 1.5603 1.0710 0.2884 -0.0610 0.4091 194 CYS B O 3167 C CB . CYS B 194 ? 1.2552 1.7079 1.2833 0.2536 -0.0466 0.3721 194 CYS B CB 3168 S SG . CYS B 194 ? 2.4573 2.8903 2.4912 0.2298 -0.0420 0.3764 194 CYS B SG 3169 N N . CYS B 195 ? 1.2220 1.7380 1.2467 0.2538 -0.0500 0.3994 195 CYS B N 3170 C CA . CYS B 195 ? 1.2576 1.7657 1.2727 0.2571 -0.0563 0.4240 195 CYS B CA 3171 C C . CYS B 195 ? 1.1926 1.7210 1.2149 0.2394 -0.0517 0.4252 195 CYS B C 3172 O O . CYS B 195 ? 1.1908 1.7188 1.2238 0.2227 -0.0444 0.4098 195 CYS B O 3173 C CB . CYS B 195 ? 1.3396 1.7772 1.3428 0.2563 -0.0618 0.4365 195 CYS B CB 3174 S SG . CYS B 195 ? 1.4393 1.8303 1.4475 0.2396 -0.0590 0.4344 195 CYS B SG 3175 N N . SER B 196 ? 1.2033 1.7495 1.2193 0.2434 -0.0557 0.4418 196 SER B N 3176 C CA . SER B 196 ? 1.2157 1.7577 1.2322 0.2279 -0.0545 0.4516 196 SER B CA 3177 C C . SER B 196 ? 1.3684 1.8562 1.3843 0.2141 -0.0542 0.4547 196 SER B C 3178 O O . SER B 196 ? 1.6718 2.1152 1.6832 0.2177 -0.0563 0.4524 196 SER B O 3179 C CB . SER B 196 ? 1.1597 1.6917 1.1650 0.2318 -0.0587 0.4645 196 SER B CB 3180 O OG . SER B 196 ? 1.2087 1.6856 1.2016 0.2404 -0.0643 0.4686 196 SER B OG 3181 N N . GLU B 197 ? 1.1758 1.6685 1.1959 0.1986 -0.0516 0.4593 197 GLU B N 3182 C CA . GLU B 197 ? 1.0154 1.4671 1.0372 0.1842 -0.0501 0.4602 197 GLU B CA 3183 C C . GLU B 197 ? 1.1354 1.5958 1.1702 0.1777 -0.0420 0.4359 197 GLU B C 3184 O O . GLU B 197 ? 1.3917 1.8329 1.4266 0.1838 -0.0415 0.4256 197 GLU B O 3185 C CB . GLU B 197 ? 1.5218 1.9049 1.5334 0.1836 -0.0543 0.4634 197 GLU B CB 3186 C CG . GLU B 197 ? 1.6657 2.0154 1.6624 0.1898 -0.0611 0.4723 197 GLU B CG 3187 C CD . GLU B 197 ? 1.8723 2.2388 1.8644 0.1852 -0.0629 0.4838 197 GLU B CD 3188 O OE1 . GLU B 197 ? 1.8671 2.2610 1.8668 0.1730 -0.0592 0.4861 197 GLU B OE1 3189 O OE2 . GLU B 197 ? 1.9794 2.3315 1.9596 0.1942 -0.0683 0.4908 197 GLU B OE2 3190 N N . PRO B 198 ? 1.0126 1.4972 1.0577 0.1643 -0.0351 0.4243 198 PRO B N 3191 C CA . PRO B 198 ? 0.9991 1.4821 1.0550 0.1566 -0.0270 0.3995 198 PRO B CA 3192 C C . PRO B 198 ? 1.1292 1.5594 1.1840 0.1481 -0.0266 0.4007 198 PRO B C 3193 O O . PRO B 198 ? 1.1518 1.5529 1.1989 0.1460 -0.0320 0.4198 198 PRO B O 3194 C CB . PRO B 198 ? 0.9119 1.4391 0.9775 0.1469 -0.0204 0.3873 198 PRO B CB 3195 C CG . PRO B 198 ? 1.0716 1.6066 1.1322 0.1445 -0.0248 0.4076 198 PRO B CG 3196 C CD . PRO B 198 ? 1.1128 1.6301 1.1602 0.1565 -0.0341 0.4311 198 PRO B CD 3197 N N . TYR B 199 ? 1.1476 1.5660 1.2094 0.1430 -0.0206 0.3814 199 TYR B N 3198 C CA . TYR B 199 ? 1.0888 1.4574 1.1494 0.1366 -0.0204 0.3821 199 TYR B CA 3199 C C . TYR B 199 ? 0.9098 1.2743 0.9782 0.1227 -0.0134 0.3709 199 TYR B C 3200 O O . TYR B 199 ? 1.0375 1.4177 1.1138 0.1184 -0.0063 0.3507 199 TYR B O 3201 C CB . TYR B 199 ? 1.0333 1.3819 1.0935 0.1428 -0.0199 0.3712 199 TYR B CB 3202 C CG . TYR B 199 ? 1.3190 1.6465 1.3683 0.1570 -0.0284 0.3856 199 TYR B CG 3203 C CD1 . TYR B 199 ? 1.4098 1.7508 1.4511 0.1665 -0.0350 0.4030 199 TYR B CD1 3204 C CD2 . TYR B 199 ? 1.4303 1.7238 1.4765 0.1615 -0.0299 0.3818 199 TYR B CD2 3205 C CE1 . TYR B 199 ? 1.4343 1.7521 1.4642 0.1808 -0.0429 0.4160 199 TYR B CE1 3206 C CE2 . TYR B 199 ? 1.4514 1.7242 1.4870 0.1758 -0.0378 0.3937 199 TYR B CE2 3207 C CZ . TYR B 199 ? 1.3941 1.6774 1.4212 0.1858 -0.0443 0.4106 199 TYR B CZ 3208 O OH . TYR B 199 ? 1.2908 1.5493 1.3061 0.2011 -0.0522 0.4220 199 TYR B OH 3209 N N . PRO B 200 ? 0.7788 1.1200 0.8443 0.1157 -0.0156 0.3839 200 PRO B N 3210 C CA . PRO B 200 ? 0.5992 0.9324 0.6701 0.1040 -0.0105 0.3778 200 PRO B CA 3211 C C . PRO B 200 ? 0.6998 1.0002 0.7738 0.0999 -0.0062 0.3650 200 PRO B C 3212 O O . PRO B 200 ? 0.6012 0.8707 0.6704 0.1042 -0.0096 0.3687 200 PRO B O 3213 C CB . PRO B 200 ? 0.6302 0.9442 0.6940 0.1002 -0.0165 0.3998 200 PRO B CB 3214 C CG . PRO B 200 ? 0.8478 1.1336 0.9016 0.1086 -0.0241 0.4137 200 PRO B CG 3215 C CD . PRO B 200 ? 0.8563 1.1723 0.9107 0.1198 -0.0243 0.4074 200 PRO B CD 3216 N N . ASP B 201 ? 0.6549 0.9624 0.7361 0.0923 0.0011 0.3499 201 ASP B N 3217 C CA . ASP B 201 ? 0.7001 0.9782 0.7838 0.0877 0.0057 0.3382 201 ASP B CA 3218 C C . ASP B 201 ? 1.0815 1.3622 1.1700 0.0797 0.0113 0.3309 201 ASP B C 3219 O O . ASP B 201 ? 1.4133 1.7270 1.5053 0.0784 0.0137 0.3267 201 ASP B O 3220 C CB . ASP B 201 ? 0.6707 0.9565 0.7576 0.0900 0.0100 0.3205 201 ASP B CB 3221 C CG . ASP B 201 ? 0.8019 1.1232 0.8957 0.0858 0.0172 0.3018 201 ASP B CG 3222 O OD1 . ASP B 201 ? 0.7912 1.1244 0.8882 0.0807 0.0206 0.2984 201 ASP B OD1 3223 O OD2 . ASP B 201 ? 0.9505 1.2884 1.0463 0.0875 0.0199 0.2890 201 ASP B OD2 3224 N N . VAL B 202 ? 0.9883 1.2363 1.0762 0.0753 0.0127 0.3312 202 VAL B N 3225 C CA . VAL B 202 ? 0.9022 1.1533 0.9945 0.0698 0.0189 0.3210 202 VAL B CA 3226 C C . VAL B 202 ? 0.7763 1.0061 0.8709 0.0668 0.0254 0.3040 202 VAL B C 3227 O O . VAL B 202 ? 0.8301 1.0325 0.9224 0.0672 0.0244 0.3048 202 VAL B O 3228 C CB . VAL B 202 ? 1.1282 1.3673 1.2181 0.0668 0.0159 0.3352 202 VAL B CB 3229 C CG1 . VAL B 202 ? 1.3245 1.5876 1.4115 0.0680 0.0098 0.3519 202 VAL B CG1 3230 C CG2 . VAL B 202 ? 1.0604 1.2593 1.1461 0.0656 0.0130 0.3434 202 VAL B CG2 3231 N N . THR B 203 ? 0.6714 0.9133 0.7700 0.0635 0.0322 0.2888 203 THR B N 3232 C CA . THR B 203 ? 0.5551 0.7794 0.6549 0.0597 0.0389 0.2719 203 THR B CA 3233 C C . THR B 203 ? 0.9015 1.1089 1.0016 0.0568 0.0438 0.2655 203 THR B C 3234 O O . THR B 203 ? 0.9224 1.1478 1.0248 0.0562 0.0477 0.2563 203 THR B O 3235 C CB . THR B 203 ? 0.5974 0.8498 0.7003 0.0583 0.0430 0.2559 203 THR B CB 3236 O OG1 . THR B 203 ? 0.9059 1.1619 1.0075 0.0614 0.0394 0.2594 203 THR B OG1 3237 C CG2 . THR B 203 ? 0.5907 0.8299 0.6943 0.0521 0.0511 0.2366 203 THR B CG2 3238 N N . PHE B 204 ? 0.8717 1.0439 0.9690 0.0558 0.0433 0.2704 204 PHE B N 3239 C CA . PHE B 204 ? 0.7368 0.8871 0.8333 0.0541 0.0480 0.2646 204 PHE B CA 3240 C C . PHE B 204 ? 0.7946 0.9363 0.8911 0.0499 0.0551 0.2462 204 PHE B C 3241 O O . PHE B 204 ? 0.8826 1.0176 0.9785 0.0473 0.0556 0.2420 204 PHE B O 3242 C CB . PHE B 204 ? 0.5634 0.6830 0.6567 0.0545 0.0446 0.2773 204 PHE B CB 3243 C CG . PHE B 204 ? 0.6742 0.8022 0.7666 0.0566 0.0375 0.2955 204 PHE B CG 3244 C CD1 . PHE B 204 ? 0.5603 0.6985 0.6530 0.0575 0.0369 0.3016 204 PHE B CD1 3245 C CD2 . PHE B 204 ? 0.5898 0.7177 0.6803 0.0578 0.0313 0.3063 204 PHE B CD2 3246 C CE1 . PHE B 204 ? 0.6680 0.8158 0.7591 0.0574 0.0305 0.3184 204 PHE B CE1 3247 C CE2 . PHE B 204 ? 0.6153 0.7489 0.7034 0.0584 0.0247 0.3236 204 PHE B CE2 3248 C CZ . PHE B 204 ? 0.6882 0.8325 0.7767 0.0572 0.0244 0.3298 204 PHE B CZ 3249 N N . THR B 205 ? 0.7351 0.8807 0.8319 0.0492 0.0605 0.2344 205 THR B N 3250 C CA . THR B 205 ? 0.7510 0.8932 0.8472 0.0437 0.0675 0.2153 205 THR B CA 3251 C C . THR B 205 ? 0.8087 0.9195 0.9009 0.0431 0.0722 0.2098 205 THR B C 3252 O O . THR B 205 ? 1.0428 1.1562 1.1346 0.0473 0.0735 0.2084 205 THR B O 3253 C CB . THR B 205 ? 1.1367 1.3156 1.2360 0.0430 0.0700 0.2028 205 THR B CB 3254 O OG1 . THR B 205 ? 1.1353 1.3449 1.2376 0.0441 0.0654 0.2085 205 THR B OG1 3255 C CG2 . THR B 205 ? 0.9620 1.1340 1.0594 0.0356 0.0778 0.1815 205 THR B CG2 3256 N N . LEU B 206 ? 1.0359 1.1179 1.1249 0.0384 0.0748 0.2067 206 LEU B N 3257 C CA . LEU B 206 ? 1.0839 1.1308 1.1681 0.0388 0.0781 0.2063 206 LEU B CA 3258 C C . LEU B 206 ? 1.1370 1.1701 1.2172 0.0324 0.0858 0.1882 206 LEU B C 3259 O O . LEU B 206 ? 1.2810 1.3182 1.3610 0.0244 0.0884 0.1787 206 LEU B O 3260 C CB . LEU B 206 ? 1.0543 1.0776 1.1369 0.0379 0.0750 0.2178 206 LEU B CB 3261 C CG . LEU B 206 ? 1.0403 1.0305 1.1183 0.0401 0.0763 0.2233 206 LEU B CG 3262 C CD1 . LEU B 206 ? 1.1681 1.1643 1.2462 0.0476 0.0755 0.2273 206 LEU B CD1 3263 C CD2 . LEU B 206 ? 0.9933 0.9775 1.0724 0.0414 0.0702 0.2383 206 LEU B CD2 3264 N N . LEU B 207 ? 1.0895 1.1070 1.1657 0.0358 0.0895 0.1827 207 LEU B N 3265 C CA . LEU B 207 ? 1.2492 1.2504 1.3200 0.0294 0.0969 0.1650 207 LEU B CA 3266 C C . LEU B 207 ? 1.3796 1.3386 1.4427 0.0314 0.1002 0.1661 207 LEU B C 3267 O O . LEU B 207 ? 1.4455 1.3980 1.5075 0.0414 0.0986 0.1735 207 LEU B O 3268 C CB . LEU B 207 ? 1.3645 1.3898 1.4367 0.0318 0.0992 0.1523 207 LEU B CB 3269 C CG . LEU B 207 ? 1.4812 1.4936 1.5476 0.0239 0.1067 0.1314 207 LEU B CG 3270 C CD1 . LEU B 207 ? 1.3733 1.3816 1.4385 0.0104 0.1095 0.1244 207 LEU B CD1 3271 C CD2 . LEU B 207 ? 1.6071 1.6544 1.6770 0.0258 0.1075 0.1196 207 LEU B CD2 3272 N N . LEU B 208 ? 1.3675 1.2994 1.4246 0.0220 0.1050 0.1589 208 LEU B N 3273 C CA . LEU B 208 ? 1.3764 1.2666 1.4255 0.0233 0.1076 0.1630 208 LEU B CA 3274 C C . LEU B 208 ? 1.5568 1.4243 1.5972 0.0198 0.1149 0.1463 208 LEU B C 3275 O O . LEU B 208 ? 1.7774 1.6656 1.8199 0.0211 0.1159 0.1360 208 LEU B O 3276 C CB . LEU B 208 ? 1.1998 1.0762 1.2480 0.0149 0.1071 0.1692 208 LEU B CB 3277 C CG . LEU B 208 ? 0.9759 0.8813 1.0327 0.0146 0.1008 0.1786 208 LEU B CG 3278 C CD1 . LEU B 208 ? 0.9557 0.8473 1.0110 0.0075 0.1005 0.1832 208 LEU B CD1 3279 C CD2 . LEU B 208 ? 0.9507 0.8684 1.0123 0.0261 0.0942 0.1939 208 LEU B CD2 3280 N N . LYS B 209 ? 1.5422 1.3682 1.5724 0.0165 0.1195 0.1443 209 LYS B N 3281 C CA . LYS B 209 ? 1.6893 1.4880 1.7091 0.0067 0.1271 0.1271 209 LYS B CA 3282 C C . LYS B 209 ? 1.6416 1.3902 1.6484 0.0074 0.1314 0.1281 209 LYS B C 3283 O O . LYS B 209 ? 1.6842 1.4132 1.6833 0.0134 0.1347 0.1197 209 LYS B O 3284 C CB . LYS B 209 ? 1.8218 1.6337 1.8409 0.0093 0.1297 0.1109 209 LYS B CB 3285 C CG . LYS B 209 ? 1.9174 1.7712 1.9451 0.0007 0.1288 0.1026 209 LYS B CG 3286 C CD . LYS B 209 ? 1.9203 1.7713 1.9483 -0.0131 0.1293 0.1052 209 LYS B CD 3287 C CE . LYS B 209 ? 1.8578 1.7529 1.8979 -0.0123 0.1236 0.1124 209 LYS B CE 3288 N NZ . LYS B 209 ? 1.7858 1.6884 1.8319 -0.0061 0.1172 0.1310 209 LYS B NZ 3289 N N . ARG B 210 ? 1.7469 1.4765 1.7509 0.0009 0.1315 0.1376 210 ARG B N 3290 C CA . ARG B 210 ? 1.7617 1.4443 1.7531 -0.0012 0.1355 0.1410 210 ARG B CA 3291 C C . ARG B 210 ? 1.7556 1.4005 1.7345 0.0081 0.1393 0.1368 210 ARG B C 3292 O O . ARG B 210 ? 1.7868 1.4258 1.7608 0.0076 0.1429 0.1218 210 ARG B O 3293 C CB . ARG B 210 ? 1.8231 1.4918 1.8083 -0.0220 0.1406 0.1322 210 ARG B CB 3294 C CG . ARG B 210 ? 1.9042 1.5649 1.8823 -0.0341 0.1469 0.1117 210 ARG B CG 3295 C CD . ARG B 210 ? 1.9188 1.5714 1.8918 -0.0564 0.1513 0.1056 210 ARG B CD 3296 N NE . ARG B 210 ? 1.8493 1.5459 1.8352 -0.0620 0.1473 0.1084 210 ARG B NE 3297 C CZ . ARG B 210 ? 1.8539 1.5615 1.8397 -0.0798 0.1497 0.1027 210 ARG B CZ 3298 N NH1 . ARG B 210 ? 1.9692 1.6481 1.9427 -0.0968 0.1563 0.0932 210 ARG B NH1 3299 N NH2 . ARG B 210 ? 1.7840 1.5332 1.7817 -0.0807 0.1453 0.1058 210 ARG B NH2 3300 N N . ARG B 211 ? 1.8494 1.4671 1.8223 0.0164 0.1385 0.1500 211 ARG B N 3301 C CA . ARG B 211 ? 1.8564 1.4317 1.8150 0.0247 0.1424 0.1478 211 ARG B CA 3302 C C . ARG B 211 ? 2.0511 1.5925 1.9991 0.0073 0.1474 0.1465 211 ARG B C 3303 O O . ARG B 211 ? 1.9366 1.4838 1.8884 -0.0001 0.1457 0.1570 211 ARG B O 3304 C CB . ARG B 211 ? 2.1059 1.6760 2.0644 0.0440 0.1386 0.1634 211 ARG B CB 3305 C CG . ARG B 211 ? 1.9992 1.6145 1.9732 0.0517 0.1315 0.1735 211 ARG B CG 3306 C CD . ARG B 211 ? 1.9231 1.5299 1.8952 0.0676 0.1284 0.1891 211 ARG B CD 3307 N NE . ARG B 211 ? 1.7993 1.4439 1.7844 0.0731 0.1217 0.2011 211 ARG B NE 3308 C CZ . ARG B 211 ? 1.7741 1.4463 1.7655 0.0858 0.1181 0.2024 211 ARG B CZ 3309 N NH1 . ARG B 211 ? 1.8564 1.5245 1.8428 0.0952 0.1206 0.1914 211 ARG B NH1 3310 N NH2 . ARG B 211 ? 1.7641 1.4677 1.7659 0.0888 0.1120 0.2141 211 ARG B NH2 3311 N N . SER B 212 ? 2.0182 1.5273 1.9532 -0.0004 0.1536 0.1326 212 SER B N 3312 C CA . SER B 212 ? 2.0903 1.5659 2.0131 -0.0202 0.1592 0.1287 212 SER B CA 3313 C C . SER B 212 ? 2.0736 1.5279 1.9913 -0.0251 0.1593 0.1446 212 SER B C 3314 O O . SER B 212 ? 2.0247 1.5003 1.9520 -0.0189 0.1543 0.1588 212 SER B O 3315 C CB . SER B 212 ? 2.1467 1.5758 2.0519 -0.0198 0.1651 0.1168 212 SER B CB 3316 O OG . SER B 212 ? 2.1585 1.5417 2.0484 -0.0297 0.1692 0.1228 212 SER B OG 3317 N N . ILE C 1 ? 0.9286 1.4191 0.8947 0.0946 0.0331 0.4830 1 ILE C N 3318 C CA . ILE C 1 ? 0.8404 1.3525 0.8088 0.0825 0.0286 0.4797 1 ILE C CA 3319 C C . ILE C 1 ? 0.7372 1.2119 0.7063 0.0673 0.0263 0.4735 1 ILE C C 3320 O O . ILE C 1 ? 0.8913 1.3203 0.8609 0.0712 0.0289 0.4716 1 ILE C O 3321 C CB . ILE C 1 ? 0.9516 1.4715 0.9224 0.0949 0.0294 0.4824 1 ILE C CB 3322 C CG1 . ILE C 1 ? 0.7408 1.2719 0.7139 0.0817 0.0251 0.4788 1 ILE C CG1 3323 C CG2 . ILE C 1 ? 1.1471 1.6161 1.1176 0.1075 0.0333 0.4825 1 ILE C CG2 3324 C CD1 . ILE C 1 ? 0.6686 1.2382 0.6399 0.0613 0.0202 0.4758 1 ILE C CD1 3325 N N . VAL C 2 ? 0.7380 1.2319 0.7072 0.0490 0.0216 0.4683 2 VAL C N 3326 C CA . VAL C 2 ? 0.7855 1.2408 0.7602 0.0332 0.0186 0.4535 2 VAL C CA 3327 C C . VAL C 2 ? 1.0709 1.5237 1.0488 0.0273 0.0159 0.4507 2 VAL C C 3328 O O . VAL C 2 ? 1.2937 1.7824 1.2732 0.0169 0.0125 0.4454 2 VAL C O 3329 C CB . VAL C 2 ? 0.7834 1.2500 0.7614 0.0143 0.0145 0.4362 2 VAL C CB 3330 C CG1 . VAL C 2 ? 0.9771 1.4060 0.9596 -0.0007 0.0109 0.4216 2 VAL C CG1 3331 C CG2 . VAL C 2 ? 0.7308 1.1971 0.7064 0.0183 0.0169 0.4369 2 VAL C CG2 3332 N N . CYS C 3 ? 1.0475 1.4593 1.0263 0.0322 0.0173 0.4536 3 CYS C N 3333 C CA . CYS C 3 ? 0.8053 1.2125 0.7869 0.0285 0.0153 0.4527 3 CYS C CA 3334 C C . CYS C 3 ? 0.7783 1.1432 0.7642 0.0135 0.0123 0.4400 3 CYS C C 3335 O O . CYS C 3 ? 0.7779 1.1129 0.7641 0.0125 0.0132 0.4352 3 CYS C O 3336 C CB . CYS C 3 ? 0.7177 1.1117 0.6984 0.0487 0.0194 0.4623 3 CYS C CB 3337 S SG . CYS C 3 ? 2.0259 2.4438 2.0045 0.0700 0.0240 0.4681 3 CYS C SG 3338 N N . HIS C 4 ? 0.6497 1.0130 0.6384 0.0019 0.0088 0.4345 4 HIS C N 3339 C CA . HIS C 4 ? 1.0496 1.3665 1.0412 -0.0073 0.0068 0.4262 4 HIS C CA 3340 C C . HIS C 4 ? 0.8622 1.1495 0.8537 0.0082 0.0107 0.4360 4 HIS C C 3341 O O . HIS C 4 ? 0.8498 1.1538 0.8398 0.0198 0.0128 0.4464 4 HIS C O 3342 C CB . HIS C 4 ? 1.0077 1.3294 1.0013 -0.0260 0.0016 0.4178 4 HIS C CB 3343 C CG . HIS C 4 ? 1.1085 1.4591 1.1015 -0.0433 -0.0026 0.4074 4 HIS C CG 3344 N ND1 . HIS C 4 ? 1.0977 1.4267 1.0910 -0.0591 -0.0066 0.3927 4 HIS C ND1 3345 C CD2 . HIS C 4 ? 0.9957 1.3961 0.9875 -0.0480 -0.0037 0.4089 4 HIS C CD2 3346 C CE1 . HIS C 4 ? 1.1302 1.4922 1.1221 -0.0731 -0.0098 0.3854 4 HIS C CE1 3347 N NE2 . HIS C 4 ? 0.9529 1.3598 0.9441 -0.0674 -0.0081 0.3950 4 HIS C NE2 3348 N N . THR C 5 ? 1.0832 1.3273 1.0759 0.0083 0.0116 0.4319 5 THR C N 3349 C CA . THR C 5 ? 1.0596 1.2750 1.0529 0.0210 0.0151 0.4360 5 THR C CA 3350 C C . THR C 5 ? 0.9257 1.1102 0.9218 0.0092 0.0120 0.4299 5 THR C C 3351 O O . THR C 5 ? 0.9143 1.0860 0.9117 -0.0030 0.0089 0.4192 5 THR C O 3352 C CB . THR C 5 ? 1.0779 1.2700 1.0702 0.0334 0.0199 0.4329 5 THR C CB 3353 O OG1 . THR C 5 ? 1.0955 1.2536 1.0893 0.0412 0.0224 0.4267 5 THR C OG1 3354 C CG2 . THR C 5 ? 1.0410 1.2163 1.0329 0.0239 0.0187 0.4292 5 THR C CG2 3355 N N . THR C 6 ? 1.0198 1.1900 1.0185 0.0139 0.0127 0.4271 6 THR C N 3356 C CA . THR C 6 ? 0.9704 1.1141 0.9718 0.0034 0.0096 0.4214 6 THR C CA 3357 C C . THR C 6 ? 1.0922 1.1942 1.0951 0.0099 0.0121 0.4118 6 THR C C 3358 O O . THR C 6 ? 1.2246 1.3017 1.2295 0.0031 0.0099 0.4055 6 THR C O 3359 C CB . THR C 6 ? 0.8614 1.0201 0.8642 0.0026 0.0083 0.4243 6 THR C CB 3360 O OG1 . THR C 6 ? 0.7781 0.9575 0.7804 0.0193 0.0122 0.4285 6 THR C OG1 3361 C CG2 . THR C 6 ? 0.6400 0.8238 0.6419 -0.0165 0.0028 0.4270 6 THR C CG2 3362 N N . ALA C 7 ? 1.1156 1.2114 1.1168 0.0225 0.0167 0.4106 7 ALA C N 3363 C CA . ALA C 7 ? 1.1317 1.1919 1.1325 0.0273 0.0196 0.4016 7 ALA C CA 3364 C C . ALA C 7 ? 1.1048 1.1455 1.1067 0.0168 0.0171 0.3962 7 ALA C C 3365 O O . ALA C 7 ? 1.0054 1.0179 1.0073 0.0184 0.0186 0.3879 7 ALA C O 3366 C CB . ALA C 7 ? 1.0337 1.0959 1.0306 0.0399 0.0245 0.4037 7 ALA C CB 3367 N N . THR C 8 ? 1.0844 1.1403 1.0868 0.0053 0.0128 0.4007 8 THR C N 3368 C CA . THR C 8 ? 1.2124 1.2563 1.2149 -0.0030 0.0105 0.3982 8 THR C CA 3369 C C . THR C 8 ? 1.1182 1.1496 1.1224 -0.0164 0.0046 0.3905 8 THR C C 3370 O O . THR C 8 ? 1.1504 1.1957 1.1545 -0.0234 0.0016 0.3919 8 THR C O 3371 C CB . THR C 8 ? 0.8591 0.9325 0.8595 -0.0052 0.0101 0.3986 8 THR C CB 3372 O OG1 . THR C 8 ? 0.8909 0.9518 0.8916 -0.0092 0.0091 0.3884 8 THR C OG1 3373 C CG2 . THR C 8 ? 0.7440 0.8425 0.7444 -0.0168 0.0053 0.3944 8 THR C CG2 3374 N N . SER C 9 ? 1.0510 1.0562 1.0561 -0.0200 0.0027 0.3807 9 SER C N 3375 C CA . SER C 9 ? 0.9917 0.9786 0.9972 -0.0311 -0.0031 0.3719 9 SER C CA 3376 C C . SER C 9 ? 1.1674 1.1472 1.1717 -0.0376 -0.0067 0.3585 9 SER C C 3377 O O . SER C 9 ? 1.2449 1.2136 1.2498 -0.0315 -0.0046 0.3545 9 SER C O 3378 C CB . SER C 9 ? 0.8632 0.8213 0.8706 -0.0267 -0.0020 0.3736 9 SER C CB 3379 O OG . SER C 9 ? 1.0237 0.9603 1.0306 -0.0360 -0.0076 0.3651 9 SER C OG 3380 N N . PRO C 10 ? 1.1595 1.1491 1.1616 -0.0498 -0.0119 0.3514 10 PRO C N 3381 C CA . PRO C 10 ? 1.2180 1.2300 1.2186 -0.0589 -0.0140 0.3557 10 PRO C CA 3382 C C . PRO C 10 ? 1.0911 1.1413 1.0920 -0.0535 -0.0102 0.3643 10 PRO C C 3383 O O . PRO C 10 ? 0.8782 0.9360 0.8795 -0.0432 -0.0060 0.3669 10 PRO C O 3384 C CB . PRO C 10 ? 1.2354 1.2445 1.2326 -0.0735 -0.0203 0.3426 10 PRO C CB 3385 C CG . PRO C 10 ? 1.1573 1.1622 1.1546 -0.0686 -0.0198 0.3335 10 PRO C CG 3386 C CD . PRO C 10 ? 1.1810 1.1643 1.1811 -0.0555 -0.0158 0.3372 10 PRO C CD 3387 N N . ILE C 11 ? 1.1983 1.2739 1.1981 -0.0617 -0.0121 0.3677 11 ILE C N 3388 C CA . ILE C 11 ? 1.1591 1.2743 1.1587 -0.0556 -0.0088 0.3769 11 ILE C CA 3389 C C . ILE C 11 ? 1.0251 1.1624 1.0231 -0.0600 -0.0098 0.3697 11 ILE C C 3390 O O . ILE C 11 ? 0.9884 1.1206 0.9847 -0.0736 -0.0147 0.3573 11 ILE C O 3391 C CB . ILE C 11 ? 1.5267 1.6674 1.5256 -0.0632 -0.0105 0.3827 11 ILE C CB 3392 C CG1 . ILE C 11 ? 1.2406 1.4213 1.2394 -0.0522 -0.0064 0.3941 11 ILE C CG1 3393 C CG2 . ILE C 11 ? 1.5523 1.7023 1.5486 -0.0836 -0.0165 0.3725 11 ILE C CG2 3394 C CD1 . ILE C 11 ? 1.2127 1.3823 1.2127 -0.0351 -0.0015 0.4047 11 ILE C CD1 3395 N N . SER C 12 ? 0.9525 1.1148 0.9503 -0.0482 -0.0053 0.3779 12 SER C N 3396 C CA . SER C 12 ? 0.8433 1.0231 0.8401 -0.0479 -0.0049 0.3726 12 SER C CA 3397 C C . SER C 12 ? 0.9131 1.1292 0.9087 -0.0360 -0.0004 0.3855 12 SER C C 3398 O O . SER C 12 ? 0.9380 1.1624 0.9334 -0.0276 0.0022 0.3973 12 SER C O 3399 C CB . SER C 12 ? 0.8811 1.0309 0.8786 -0.0425 -0.0035 0.3667 12 SER C CB 3400 O OG . SER C 12 ? 0.7749 0.9110 0.7729 -0.0276 0.0021 0.3779 12 SER C OG 3401 N N . ALA C 13 ? 0.9617 1.1977 0.9560 -0.0337 0.0008 0.3835 13 ALA C N 3402 C CA . ALA C 13 ? 0.7728 1.0461 0.7648 -0.0233 0.0045 0.3952 13 ALA C CA 3403 C C . ALA C 13 ? 0.6574 0.9208 0.6475 -0.0082 0.0099 0.4043 13 ALA C C 3404 O O . ALA C 13 ? 0.6716 0.9178 0.6620 -0.0097 0.0102 0.3974 13 ALA C O 3405 C CB . ALA C 13 ? 0.8374 1.1480 0.8285 -0.0329 0.0017 0.3873 13 ALA C CB 3406 N N . VAL C 14 ? 0.7402 1.0166 0.7276 0.0063 0.0142 0.4200 14 VAL C N 3407 C CA . VAL C 14 ? 0.7752 1.0417 0.7589 0.0201 0.0195 0.4302 14 VAL C CA 3408 C C . VAL C 14 ? 0.9068 1.2133 0.8859 0.0306 0.0221 0.4426 14 VAL C C 3409 O O . VAL C 14 ? 0.9260 1.2646 0.9049 0.0309 0.0205 0.4457 14 VAL C O 3410 C CB . VAL C 14 ? 0.7967 1.0278 0.7795 0.0305 0.0231 0.4388 14 VAL C CB 3411 C CG1 . VAL C 14 ? 0.6781 0.8980 0.6581 0.0446 0.0285 0.4413 14 VAL C CG1 3412 C CG2 . VAL C 14 ? 1.1800 1.3738 1.1667 0.0215 0.0211 0.4272 14 VAL C CG2 3413 N N . THR C 15 ? 0.7495 1.0559 0.7245 0.0383 0.0258 0.4492 15 THR C N 3414 C CA . THR C 15 ? 0.6711 1.0069 0.6422 0.0508 0.0287 0.4587 15 THR C CA 3415 C C . THR C 15 ? 0.7516 1.0602 0.7232 0.0660 0.0327 0.4594 15 THR C C 3416 O O . THR C 15 ? 1.0145 1.2865 0.9852 0.0692 0.0356 0.4564 15 THR C O 3417 C CB . THR C 15 ? 0.7184 1.0633 0.6861 0.0501 0.0305 0.4603 15 THR C CB 3418 O OG1 . THR C 15 ? 0.8921 1.2421 0.8641 0.0335 0.0262 0.4448 15 THR C OG1 3419 C CG2 . THR C 15 ? 0.6965 1.0820 0.6614 0.0592 0.0319 0.4670 15 THR C CG2 3420 N N . CYS C 16 ? 0.9120 1.2400 0.8840 0.0751 0.0328 0.4632 16 CYS C N 3421 C CA . CYS C 16 ? 1.1582 1.4614 1.1291 0.0902 0.0365 0.4639 16 CYS C CA 3422 C C . CYS C 16 ? 0.7179 1.0043 0.6834 0.1000 0.0411 0.4668 16 CYS C C 3423 O O . CYS C 16 ? 0.7185 1.0220 0.6821 0.0969 0.0413 0.4696 16 CYS C O 3424 C CB . CYS C 16 ? 1.1447 1.4824 1.1163 0.0996 0.0360 0.4690 16 CYS C CB 3425 S SG . CYS C 16 ? 2.1185 2.4874 2.0947 0.0847 0.0301 0.4673 16 CYS C SG 3426 N N . PRO C 17 ? 0.8584 1.1091 0.8207 0.1100 0.0444 0.4656 17 PRO C N 3427 C CA . PRO C 17 ? 0.8727 1.1051 0.8275 0.1201 0.0486 0.4696 17 PRO C CA 3428 C C . PRO C 17 ? 0.9655 1.2333 0.9169 0.1316 0.0499 0.4789 17 PRO C C 3429 O O . PRO C 17 ? 1.1067 1.4157 1.0620 0.1324 0.0476 0.4818 17 PRO C O 3430 C CB . PRO C 17 ? 0.7585 0.9538 0.7102 0.1287 0.0506 0.4663 17 PRO C CB 3431 C CG . PRO C 17 ? 0.9633 1.1444 0.9216 0.1182 0.0478 0.4578 17 PRO C CG 3432 C CD . PRO C 17 ? 0.9270 1.1464 0.8918 0.1085 0.0438 0.4588 17 PRO C CD 3433 N N . PRO C 18 ? 1.1973 1.4509 1.1412 0.1394 0.0534 0.4839 18 PRO C N 3434 C CA . PRO C 18 ? 1.3836 1.6647 1.3229 0.1537 0.0552 0.4935 18 PRO C CA 3435 C C . PRO C 18 ? 1.4877 1.7644 1.4246 0.1695 0.0564 0.4958 18 PRO C C 3436 O O . PRO C 18 ? 1.4752 1.7104 1.4079 0.1728 0.0579 0.4922 18 PRO C O 3437 C CB . PRO C 18 ? 1.3740 1.6308 1.3045 0.1553 0.0584 0.4977 18 PRO C CB 3438 C CG . PRO C 18 ? 1.2901 1.5230 1.2227 0.1390 0.0576 0.4904 18 PRO C CG 3439 C CD . PRO C 18 ? 1.2340 1.4501 1.1728 0.1331 0.0554 0.4813 18 PRO C CD 3440 N N . GLY C 19 ? 1.5613 1.8815 1.5002 0.1790 0.0559 0.5012 19 GLY C N 3441 C CA . GLY C 19 ? 1.6041 1.9245 1.5403 0.1957 0.0574 0.5040 19 GLY C CA 3442 C C . GLY C 19 ? 1.5284 1.8610 1.4723 0.1915 0.0547 0.4984 19 GLY C C 3443 O O . GLY C 19 ? 1.6018 1.9549 1.5461 0.2037 0.0550 0.5010 19 GLY C O 3444 N N . GLU C 20 ? 1.4219 1.7406 1.3714 0.1744 0.0520 0.4909 20 GLU C N 3445 C CA . GLU C 20 ? 1.3529 1.6859 1.3095 0.1680 0.0488 0.4865 20 GLU C CA 3446 C C . GLU C 20 ? 1.3205 1.7042 1.2828 0.1570 0.0450 0.4878 20 GLU C C 3447 O O . GLU C 20 ? 1.1822 1.5623 1.1478 0.1400 0.0421 0.4832 20 GLU C O 3448 C CB . GLU C 20 ? 1.3412 1.6313 1.3002 0.1558 0.0476 0.4777 20 GLU C CB 3449 C CG . GLU C 20 ? 1.3437 1.5867 1.2971 0.1651 0.0507 0.4748 20 GLU C CG 3450 C CD . GLU C 20 ? 1.4123 1.6187 1.3690 0.1533 0.0493 0.4653 20 GLU C CD 3451 O OE1 . GLU C 20 ? 1.3717 1.5866 1.3349 0.1384 0.0461 0.4613 20 GLU C OE1 3452 O OE2 . GLU C 20 ? 1.5033 1.6725 1.4555 0.1589 0.0514 0.4616 20 GLU C OE2 3453 N N . ASN C 21 ? 1.3602 1.7910 1.3230 0.1667 0.0449 0.4935 21 ASN C N 3454 C CA . ASN C 21 ? 1.1808 1.6672 1.1472 0.1581 0.0417 0.4954 21 ASN C CA 3455 C C . ASN C 21 ? 1.0710 1.5868 1.0428 0.1454 0.0371 0.4919 21 ASN C C 3456 O O . ASN C 21 ? 1.0710 1.6226 1.0446 0.1310 0.0333 0.4906 21 ASN C O 3457 C CB . ASN C 21 ? 0.9944 1.5211 0.9585 0.1747 0.0441 0.5028 21 ASN C CB 3458 C CG . ASN C 21 ? 1.0029 1.5042 0.9603 0.1861 0.0484 0.5077 21 ASN C CG 3459 O OD1 . ASN C 21 ? 1.1282 1.6033 1.0838 0.1766 0.0485 0.5059 21 ASN C OD1 3460 N ND2 . ASN C 21 ? 0.9884 1.4990 0.9412 0.2060 0.0519 0.5143 21 ASN C ND2 3461 N N . LEU C 22 ? 0.9898 1.4906 0.9631 0.1495 0.0371 0.4901 22 LEU C N 3462 C CA . LEU C 22 ? 0.9106 1.4388 0.8882 0.1381 0.0330 0.4877 22 LEU C CA 3463 C C . LEU C 22 ? 0.7914 1.2857 0.7710 0.1197 0.0299 0.4817 22 LEU C C 3464 O O . LEU C 22 ? 0.8272 1.2706 0.8061 0.1213 0.0319 0.4784 22 LEU C O 3465 C CB . LEU C 22 ? 1.0608 1.5971 1.0392 0.1530 0.0346 0.4896 22 LEU C CB 3466 C CG . LEU C 22 ? 1.2039 1.7791 1.1805 0.1723 0.0375 0.4956 22 LEU C CG 3467 C CD1 . LEU C 22 ? 1.3742 1.9509 1.3510 0.1871 0.0393 0.4965 22 LEU C CD1 3468 C CD2 . LEU C 22 ? 1.1714 1.8095 1.1512 0.1613 0.0339 0.4963 22 LEU C CD2 3469 N N . CYS C 23 ? 0.7233 1.2462 0.7049 0.1017 0.0251 0.4798 23 CYS C N 3470 C CA . CYS C 23 ? 0.7927 1.2869 0.7760 0.0852 0.0221 0.4750 23 CYS C CA 3471 C C . CYS C 23 ? 0.9264 1.4362 0.9122 0.0873 0.0210 0.4757 23 CYS C C 3472 O O . CYS C 23 ? 0.9414 1.4999 0.9276 0.0930 0.0205 0.4791 23 CYS C O 3473 C CB . CYS C 23 ? 0.7482 1.2568 0.7298 0.0613 0.0174 0.4724 23 CYS C CB 3474 S SG . CYS C 23 ? 0.9791 1.4611 0.9579 0.0572 0.0187 0.4704 23 CYS C SG 3475 N N . TYR C 24 ? 1.0080 1.4780 0.9958 0.0840 0.0208 0.4722 24 TYR C N 3476 C CA . TYR C 24 ? 0.9829 1.4636 0.9731 0.0860 0.0199 0.4726 24 TYR C CA 3477 C C . TYR C 24 ? 0.9335 1.3979 0.9253 0.0643 0.0157 0.4691 24 TYR C C 3478 O O . TYR C 24 ? 0.9492 1.3836 0.9404 0.0507 0.0142 0.4655 24 TYR C O 3479 C CB . TYR C 24 ? 1.0416 1.4909 1.0320 0.1074 0.0246 0.4723 24 TYR C CB 3480 C CG . TYR C 24 ? 1.0909 1.4804 1.0820 0.1045 0.0258 0.4662 24 TYR C CG 3481 C CD1 . TYR C 24 ? 1.2932 1.6660 1.2873 0.0936 0.0234 0.4627 24 TYR C CD1 3482 C CD2 . TYR C 24 ? 1.1880 1.5393 1.1763 0.1126 0.0294 0.4637 24 TYR C CD2 3483 C CE1 . TYR C 24 ? 1.2992 1.6200 1.2942 0.0912 0.0244 0.4560 24 TYR C CE1 3484 C CE2 . TYR C 24 ? 1.1794 1.4798 1.1682 0.1092 0.0304 0.4569 24 TYR C CE2 3485 C CZ . TYR C 24 ? 1.1965 1.4826 1.1889 0.0991 0.0280 0.4528 24 TYR C CZ 3486 O OH . TYR C 24 ? 1.1999 1.4385 1.1927 0.0964 0.0291 0.4452 24 TYR C OH 3487 N N . ARG C 25 ? 0.8570 1.3414 0.8506 0.0616 0.0140 0.4701 25 ARG C N 3488 C CA . ARG C 25 ? 0.8469 1.3106 0.8419 0.0433 0.0107 0.4672 25 ARG C CA 3489 C C . ARG C 25 ? 0.9712 1.4303 0.9691 0.0555 0.0124 0.4675 25 ARG C C 3490 O O . ARG C 25 ? 0.9961 1.4944 0.9943 0.0675 0.0135 0.4712 25 ARG C O 3491 C CB . ARG C 25 ? 0.8126 1.3137 0.8051 0.0183 0.0055 0.4682 25 ARG C CB 3492 C CG . ARG C 25 ? 0.6398 1.1092 0.6351 -0.0015 0.0023 0.4609 25 ARG C CG 3493 C CD . ARG C 25 ? 0.7718 1.2589 0.7676 -0.0292 -0.0027 0.4516 25 ARG C CD 3494 N NE . ARG C 25 ? 1.0542 1.5970 1.0494 -0.0344 -0.0042 0.4547 25 ARG C NE 3495 C CZ . ARG C 25 ? 1.1183 1.6797 1.1134 -0.0604 -0.0086 0.4479 25 ARG C CZ 3496 N NH1 . ARG C 25 ? 1.0989 1.6230 1.0937 -0.0815 -0.0120 0.4378 25 ARG C NH1 3497 N NH2 . ARG C 25 ? 1.1359 1.7518 1.1304 -0.0654 -0.0096 0.4510 25 ARG C NH2 3498 N N . LYS C 26 ? 0.9553 1.3683 0.9553 0.0536 0.0128 0.4632 26 LYS C N 3499 C CA . LYS C 26 ? 0.9744 1.3824 0.9768 0.0633 0.0141 0.4629 26 LYS C CA 3500 C C . LYS C 26 ? 0.9192 1.3181 0.9234 0.0428 0.0101 0.4611 26 LYS C C 3501 O O . LYS C 26 ? 0.9073 1.2698 0.9117 0.0293 0.0084 0.4567 26 LYS C O 3502 C CB . LYS C 26 ? 0.9833 1.3437 0.9859 0.0806 0.0188 0.4583 26 LYS C CB 3503 C CG . LYS C 26 ? 1.1489 1.5197 1.1508 0.1033 0.0225 0.4603 26 LYS C CG 3504 C CD . LYS C 26 ? 1.3326 1.6563 1.3318 0.1188 0.0273 0.4557 26 LYS C CD 3505 C CE . LYS C 26 ? 1.4145 1.7388 1.4119 0.1397 0.0309 0.4564 26 LYS C CE 3506 N NZ . LYS C 26 ? 1.4525 1.7458 1.4441 0.1569 0.0357 0.4546 26 LYS C NZ 3507 N N . MET C 27 ? 0.9949 1.4262 1.0002 0.0405 0.0086 0.4641 27 MET C N 3508 C CA . MET C 27 ? 1.0849 1.5014 1.0919 0.0230 0.0054 0.4623 27 MET C CA 3509 C C . MET C 27 ? 1.2721 1.6985 1.2816 0.0340 0.0067 0.4634 27 MET C C 3510 O O . MET C 27 ? 1.3071 1.7824 1.3166 0.0376 0.0063 0.4677 27 MET C O 3511 C CB . MET C 27 ? 0.9572 1.4044 0.9615 -0.0040 0.0003 0.4646 27 MET C CB 3512 C CG . MET C 27 ? 0.8318 1.2695 0.8331 -0.0177 -0.0016 0.4622 27 MET C CG 3513 S SD . MET C 27 ? 0.9715 1.4543 0.9716 -0.0470 -0.0069 0.4571 27 MET C SD 3514 C CE . MET C 27 ? 0.6440 1.0799 0.6446 -0.0727 -0.0113 0.4497 27 MET C CE 3515 N N . TRP C 28 ? 1.2872 1.6702 1.2990 0.0401 0.0085 0.4588 28 TRP C N 3516 C CA . TRP C 28 ? 1.0199 1.4097 1.0339 0.0465 0.0092 0.4593 28 TRP C CA 3517 C C . TRP C 28 ? 1.0209 1.3901 1.0366 0.0252 0.0054 0.4569 28 TRP C C 3518 O O . TRP C 28 ? 0.8413 1.1995 0.8556 0.0041 0.0018 0.4557 28 TRP C O 3519 C CB . TRP C 28 ? 1.1245 1.4831 1.1389 0.0704 0.0143 0.4555 28 TRP C CB 3520 C CG . TRP C 28 ? 1.1866 1.4863 1.2015 0.0676 0.0155 0.4474 28 TRP C CG 3521 C CD1 . TRP C 28 ? 0.9759 1.2433 0.9931 0.0607 0.0147 0.4419 28 TRP C CD1 3522 C CD2 . TRP C 28 ? 1.2247 1.4949 1.2376 0.0710 0.0174 0.4433 28 TRP C CD2 3523 N NE1 . TRP C 28 ? 0.9332 1.1544 0.9499 0.0602 0.0161 0.4339 28 TRP C NE1 3524 C CE2 . TRP C 28 ? 1.1474 1.3694 1.1614 0.0659 0.0178 0.4347 28 TRP C CE2 3525 C CE3 . TRP C 28 ? 1.0800 1.3620 1.0901 0.0778 0.0189 0.4458 28 TRP C CE3 3526 C CZ2 . TRP C 28 ? 1.1653 1.3526 1.1775 0.0668 0.0195 0.4284 28 TRP C CZ2 3527 C CZ3 . TRP C 28 ? 1.2633 1.5092 1.2718 0.0786 0.0207 0.4405 28 TRP C CZ3 3528 C CH2 . TRP C 28 ? 1.2368 1.4366 1.2463 0.0730 0.0209 0.4317 28 TRP C CH2 3529 N N . CYS C 29 ? 1.1346 1.4968 1.1526 0.0314 0.0064 0.4558 29 CYS C N 3530 C CA . CYS C 29 ? 1.2053 1.5516 1.2249 0.0127 0.0030 0.4539 29 CYS C CA 3531 C C . CYS C 29 ? 1.2580 1.5603 1.2801 0.0220 0.0054 0.4473 29 CYS C C 3532 O O . CYS C 29 ? 1.2484 1.5561 1.2715 0.0398 0.0087 0.4475 29 CYS C O 3533 C CB . CYS C 29 ? 1.1535 1.5486 1.1733 0.0038 0.0004 0.4599 29 CYS C CB 3534 S SG . CYS C 29 ? 1.0782 1.5073 1.0946 -0.0293 -0.0057 0.4639 29 CYS C SG 3535 N N . ASP C 30 ? 1.2101 1.4693 1.2323 0.0106 0.0038 0.4407 30 ASP C N 3536 C CA . ASP C 30 ? 1.4914 1.7198 1.5154 0.0022 0.0022 0.4352 30 ASP C CA 3537 C C . ASP C 30 ? 1.7389 1.9965 1.7641 -0.0066 -0.0003 0.4406 30 ASP C C 3538 O O . ASP C 30 ? 1.7928 2.0969 1.8175 -0.0061 -0.0007 0.4480 30 ASP C O 3539 C CB . ASP C 30 ? 1.5286 1.7272 1.5508 -0.0156 -0.0014 0.4304 30 ASP C CB 3540 C CG . ASP C 30 ? 1.5338 1.7593 1.5533 -0.0373 -0.0063 0.4366 30 ASP C CG 3541 O OD1 . ASP C 30 ? 1.6126 1.8767 1.6320 -0.0434 -0.0078 0.4433 30 ASP C OD1 3542 O OD2 . ASP C 30 ? 1.5976 1.8087 1.6145 -0.0481 -0.0085 0.4346 30 ASP C OD2 3543 N N . VAL C 31 ? 1.8380 2.0730 1.8645 -0.0149 -0.0021 0.4367 31 VAL C N 3544 C CA . VAL C 31 ? 1.9518 2.2137 1.9778 -0.0334 -0.0064 0.4423 31 VAL C CA 3545 C C . VAL C 31 ? 1.8761 2.1076 1.8992 -0.0559 -0.0112 0.4383 31 VAL C C 3546 O O . VAL C 31 ? 1.9702 2.2086 1.9920 -0.0731 -0.0152 0.4406 31 VAL C O 3547 C CB . VAL C 31 ? 1.7983 2.0731 1.8272 -0.0270 -0.0053 0.4439 31 VAL C CB 3548 C CG1 . VAL C 31 ? 1.6917 2.0090 1.7196 -0.0445 -0.0092 0.4513 31 VAL C CG1 3549 C CG2 . VAL C 31 ? 1.8844 2.1769 1.9150 -0.0011 0.0000 0.4455 31 VAL C CG2 3550 N N . PHE C 32 ? 1.4950 1.6955 1.5165 -0.0561 -0.0112 0.4328 32 PHE C N 3551 C CA . PHE C 32 ? 1.2929 1.4708 1.3102 -0.0770 -0.0160 0.4301 32 PHE C CA 3552 C C . PHE C 32 ? 1.3155 1.5300 1.3291 -0.0940 -0.0191 0.4377 32 PHE C C 3553 O O . PHE C 32 ? 1.2570 1.4601 1.2658 -0.1148 -0.0237 0.4371 32 PHE C O 3554 C CB . PHE C 32 ? 1.2950 1.4326 1.3113 -0.0716 -0.0150 0.4218 32 PHE C CB 3555 C CG . PHE C 32 ? 1.2110 1.3044 1.2275 -0.0686 -0.0151 0.4118 32 PHE C CG 3556 C CD1 . PHE C 32 ? 1.1402 1.2106 1.1527 -0.0851 -0.0199 0.4088 32 PHE C CD1 3557 C CD2 . PHE C 32 ? 1.0992 1.1730 1.1184 -0.0498 -0.0105 0.4047 32 PHE C CD2 3558 C CE1 . PHE C 32 ? 0.9025 0.9352 0.9142 -0.0810 -0.0199 0.3994 32 PHE C CE1 3559 C CE2 . PHE C 32 ? 0.8457 0.8831 0.8643 -0.0479 -0.0105 0.3949 32 PHE C CE2 3560 C CZ . PHE C 32 ? 0.7723 0.7907 0.7872 -0.0627 -0.0152 0.3924 32 PHE C CZ 3561 N N . CYS C 33 ? 1.5071 1.7659 1.5221 -0.0843 -0.0165 0.4442 33 CYS C N 3562 C CA . CYS C 33 ? 1.6302 1.9344 1.6419 -0.0959 -0.0181 0.4509 33 CYS C CA 3563 C C . CYS C 33 ? 1.5200 1.8357 1.5268 -0.1254 -0.0236 0.4531 33 CYS C C 3564 O O . CYS C 33 ? 1.4665 1.7873 1.4683 -0.1428 -0.0263 0.4535 33 CYS C O 3565 C CB . CYS C 33 ? 1.7375 2.0916 1.7521 -0.0789 -0.0146 0.4568 33 CYS C CB 3566 S SG . CYS C 33 ? 0.9436 1.3467 0.9563 -0.0702 -0.0126 0.4617 33 CYS C SG 3567 N N . SER C 34 ? 1.3420 1.6647 1.3500 -0.1310 -0.0250 0.4544 34 SER C N 3568 C CA . SER C 34 ? 1.3655 1.6908 1.3687 -0.1586 -0.0303 0.4554 34 SER C CA 3569 C C . SER C 34 ? 1.3988 1.6716 1.3965 -0.1738 -0.0341 0.4494 34 SER C C 3570 O O . SER C 34 ? 1.3852 1.6618 1.3764 -0.1967 -0.0379 0.4499 34 SER C O 3571 C CB . SER C 34 ? 1.4129 1.7431 1.4189 -0.1567 -0.0306 0.4567 34 SER C CB 3572 O OG . SER C 34 ? 1.5032 1.7943 1.5135 -0.1370 -0.0277 0.4517 34 SER C OG 3573 N N . SER C 35 ? 1.4402 1.6656 1.4402 -0.1601 -0.0328 0.4430 35 SER C N 3574 C CA . SER C 35 ? 1.3934 1.5658 1.3887 -0.1693 -0.0361 0.4358 35 SER C CA 3575 C C . SER C 35 ? 1.3316 1.4902 1.3242 -0.1710 -0.0363 0.4333 35 SER C C 3576 O O . SER C 35 ? 1.3332 1.4683 1.3190 -0.1891 -0.0406 0.4305 35 SER C O 3577 C CB . SER C 35 ? 1.3620 1.4961 1.3612 -0.1517 -0.0339 0.4288 35 SER C CB 3578 O OG . SER C 35 ? 1.3300 1.4718 1.3357 -0.1274 -0.0283 0.4279 35 SER C OG 3579 N N . ARG C 36 ? 1.2215 1.3914 1.2190 -0.1510 -0.0316 0.4337 36 ARG C N 3580 C CA . ARG C 36 ? 1.3723 1.5356 1.3679 -0.1509 -0.0313 0.4323 36 ARG C CA 3581 C C . ARG C 36 ? 1.4494 1.6585 1.4483 -0.1373 -0.0270 0.4385 36 ARG C C 3582 O O . ARG C 36 ? 1.4554 1.6643 1.4594 -0.1138 -0.0223 0.4375 36 ARG C O 3583 C CB . ARG C 36 ? 1.4039 1.5182 1.4011 -0.1379 -0.0302 0.4234 36 ARG C CB 3584 C CG . ARG C 36 ? 1.3524 1.4496 1.3557 -0.1149 -0.0257 0.4182 36 ARG C CG 3585 C CD . ARG C 36 ? 1.3521 1.3998 1.3538 -0.1125 -0.0268 0.4081 36 ARG C CD 3586 N NE . ARG C 36 ? 1.3191 1.3457 1.3250 -0.0929 -0.0226 0.4005 36 ARG C NE 3587 C CZ . ARG C 36 ? 1.3393 1.3273 1.3434 -0.0906 -0.0234 0.3911 36 ARG C CZ 3588 N NH1 . ARG C 36 ? 1.4099 1.3751 1.4085 -0.1048 -0.0283 0.3887 36 ARG C NH1 3589 N NH2 . ARG C 36 ? 1.2567 1.2291 1.2636 -0.0746 -0.0194 0.3837 36 ARG C NH2 3590 N N . GLY C 37 ? 1.3294 1.5777 1.3246 -0.1524 -0.0287 0.4426 37 GLY C N 3591 C CA . GLY C 37 ? 1.3763 1.6763 1.3741 -0.1405 -0.0254 0.4468 37 GLY C CA 3592 C C . GLY C 37 ? 1.4178 1.7196 1.4192 -0.1147 -0.0204 0.4468 37 GLY C C 3593 O O . GLY C 37 ? 1.6043 1.8880 1.6049 -0.1137 -0.0203 0.4411 37 GLY C O 3594 N N . LYS C 38 ? 1.3122 1.6323 1.3172 -0.0935 -0.0163 0.4521 38 LYS C N 3595 C CA . LYS C 38 ? 1.1169 1.4550 1.1237 -0.0704 -0.0118 0.4539 38 LYS C CA 3596 C C . LYS C 38 ? 1.0496 1.3459 1.0577 -0.0570 -0.0091 0.4483 38 LYS C C 3597 O O . LYS C 38 ? 1.0193 1.2932 1.0248 -0.0692 -0.0114 0.4451 38 LYS C O 3598 C CB . LYS C 38 ? 1.2995 1.6852 1.3036 -0.0802 -0.0132 0.4552 38 LYS C CB 3599 C CG . LYS C 38 ? 1.5417 1.9665 1.5463 -0.0586 -0.0094 0.4606 38 LYS C CG 3600 C CD . LYS C 38 ? 1.6420 2.0954 1.6488 -0.0490 -0.0082 0.4653 38 LYS C CD 3601 C CE . LYS C 38 ? 1.6951 2.1726 1.7037 -0.0207 -0.0037 0.4674 38 LYS C CE 3602 N NZ . LYS C 38 ? 1.7887 2.2579 1.8008 -0.0066 -0.0017 0.4671 38 LYS C NZ 3603 N N . VAL C 39 ? 1.0091 1.2953 1.0203 -0.0326 -0.0043 0.4465 39 VAL C N 3604 C CA . VAL C 39 ? 0.9435 1.1905 0.9551 -0.0239 -0.0021 0.4402 39 VAL C CA 3605 C C . VAL C 39 ? 1.0122 1.2820 1.0222 -0.0121 0.0006 0.4437 39 VAL C C 3606 O O . VAL C 39 ? 1.0136 1.3129 1.0240 0.0037 0.0034 0.4480 39 VAL C O 3607 C CB . VAL C 39 ? 1.1528 1.3637 1.1676 -0.0075 0.0016 0.4333 39 VAL C CB 3608 C CG1 . VAL C 39 ? 1.1343 1.3696 1.1508 0.0077 0.0044 0.4372 39 VAL C CG1 3609 C CG2 . VAL C 39 ? 0.6279 0.8147 0.6421 0.0069 0.0056 0.4284 39 VAL C CG2 3610 N N . VAL C 40 ? 1.0874 1.3402 1.0954 -0.0182 -0.0002 0.4412 40 VAL C N 3611 C CA . VAL C 40 ? 0.8316 1.1072 0.8371 -0.0122 0.0013 0.4447 40 VAL C CA 3612 C C . VAL C 40 ? 0.8296 1.0764 0.8356 0.0035 0.0054 0.4401 40 VAL C C 3613 O O . VAL C 40 ? 1.0679 1.2770 1.0744 -0.0013 0.0049 0.4336 40 VAL C O 3614 C CB . VAL C 40 ? 0.8214 1.1056 0.8243 -0.0339 -0.0031 0.4417 40 VAL C CB 3615 C CG1 . VAL C 40 ? 0.8981 1.2134 0.8992 -0.0272 -0.0015 0.4435 40 VAL C CG1 3616 C CG2 . VAL C 40 ? 0.9835 1.2912 0.9860 -0.0541 -0.0075 0.4400 40 VAL C CG2 3617 N N . GLU C 41 ? 0.8022 1.0673 0.8075 0.0219 0.0093 0.4432 41 GLU C N 3618 C CA . GLU C 41 ? 0.7484 0.9897 0.7526 0.0344 0.0131 0.4397 41 GLU C CA 3619 C C . GLU C 41 ? 1.0533 1.3291 1.0545 0.0364 0.0133 0.4456 41 GLU C C 3620 O O . GLU C 41 ? 1.1177 1.4320 1.1179 0.0460 0.0143 0.4516 41 GLU C O 3621 C CB . GLU C 41 ? 0.7231 0.9489 0.7276 0.0546 0.0178 0.4376 41 GLU C CB 3622 C CG . GLU C 41 ? 0.8067 1.0207 0.8080 0.0694 0.0222 0.4368 41 GLU C CG 3623 C CD . GLU C 41 ? 1.0421 1.2349 1.0420 0.0865 0.0265 0.4339 41 GLU C CD 3624 O OE1 . GLU C 41 ? 1.0961 1.2673 1.0980 0.0840 0.0262 0.4287 41 GLU C OE1 3625 O OE2 . GLU C 41 ? 1.0134 1.2104 1.0093 0.1018 0.0301 0.4367 41 GLU C OE2 3626 N N . LEU C 42 ? 1.1262 1.3907 1.1258 0.0279 0.0123 0.4437 42 LEU C N 3627 C CA . LEU C 42 ? 0.8149 1.1115 0.8114 0.0287 0.0125 0.4486 42 LEU C CA 3628 C C . LEU C 42 ? 0.7855 1.0590 0.7808 0.0428 0.0169 0.4463 42 LEU C C 3629 O O . LEU C 42 ? 0.9855 1.2174 0.9818 0.0419 0.0180 0.4396 42 LEU C O 3630 C CB . LEU C 42 ? 0.7362 1.0405 0.7314 0.0065 0.0078 0.4456 42 LEU C CB 3631 C CG . LEU C 42 ? 0.9234 1.2350 0.9208 -0.0139 0.0026 0.4387 42 LEU C CG 3632 C CD1 . LEU C 42 ? 0.6458 0.9513 0.6433 -0.0351 -0.0019 0.4261 42 LEU C CD1 3633 C CD2 . LEU C 42 ? 1.0405 1.4022 1.0370 -0.0129 0.0021 0.4448 42 LEU C CD2 3634 N N . GLY C 43 ? 0.8400 1.1406 0.8329 0.0555 0.0194 0.4513 43 GLY C N 3635 C CA . GLY C 43 ? 0.7277 1.0085 0.7183 0.0662 0.0233 0.4501 43 GLY C CA 3636 C C . GLY C 43 ? 0.7654 1.0797 0.7528 0.0787 0.0257 0.4566 43 GLY C C 3637 O O . GLY C 43 ? 0.7831 1.1424 0.7699 0.0748 0.0234 0.4615 43 GLY C O 3638 N N . CYS C 44 ? 0.8620 1.1536 0.8466 0.0926 0.0301 0.4562 44 CYS C N 3639 C CA . CYS C 44 ? 0.9121 1.2271 0.8929 0.1061 0.0330 0.4624 44 CYS C CA 3640 C C . CYS C 44 ? 0.9322 1.2408 0.9107 0.1250 0.0365 0.4645 44 CYS C C 3641 O O . CYS C 44 ? 0.9374 1.2144 0.9163 0.1271 0.0374 0.4599 44 CYS C O 3642 C CB . CYS C 44 ? 1.1316 1.4240 1.1090 0.1059 0.0353 0.4612 44 CYS C CB 3643 S SG . CYS C 44 ? 1.4295 1.7349 1.4082 0.0862 0.0316 0.4597 44 CYS C SG 3644 N N . ALA C 45 ? 0.9648 1.3021 0.9401 0.1391 0.0386 0.4712 45 ALA C N 3645 C CA . ALA C 45 ? 0.8804 1.2083 0.8517 0.1588 0.0423 0.4735 45 ALA C CA 3646 C C . ALA C 45 ? 0.9671 1.3176 0.9336 0.1726 0.0450 0.4806 45 ALA C C 3647 O O . ALA C 45 ? 0.9859 1.3739 0.9541 0.1674 0.0433 0.4840 45 ALA C O 3648 C CB . ALA C 45 ? 0.7585 1.1113 0.7333 0.1627 0.0408 0.4743 45 ALA C CB 3649 N N . ALA C 46 ? 1.0102 1.3371 0.9697 0.1896 0.0490 0.4828 46 ALA C N 3650 C CA . ALA C 46 ? 1.2253 1.5737 1.1793 0.2047 0.0517 0.4906 46 ALA C CA 3651 C C . ALA C 46 ? 1.3375 1.7366 1.2936 0.2170 0.0515 0.4954 46 ALA C C 3652 O O . ALA C 46 ? 1.3884 1.8336 1.3462 0.2181 0.0508 0.5001 46 ALA C O 3653 C CB . ALA C 46 ? 1.2652 1.5686 1.2092 0.2176 0.0557 0.4918 46 ALA C CB 3654 N N . THR C 47 ? 1.3980 1.7909 1.3540 0.2256 0.0521 0.4936 47 THR C N 3655 C CA . THR C 47 ? 1.3687 1.8098 1.3269 0.2367 0.0518 0.4970 47 THR C CA 3656 C C . THR C 47 ? 1.4350 1.8872 1.4009 0.2232 0.0480 0.4921 47 THR C C 3657 O O . THR C 47 ? 1.4170 1.8271 1.3836 0.2152 0.0475 0.4866 47 THR C O 3658 C CB . THR C 47 ? 1.3918 1.8184 1.3417 0.2611 0.0560 0.4999 47 THR C CB 3659 O OG1 . THR C 47 ? 1.5341 1.9172 1.4825 0.2611 0.0564 0.4944 47 THR C OG1 3660 C CG2 . THR C 47 ? 1.3917 1.7934 1.3322 0.2716 0.0594 0.5046 47 THR C CG2 3661 N N . CYS C 48 ? 1.3596 1.8678 1.3308 0.2196 0.0454 0.4940 48 CYS C N 3662 C CA . CYS C 48 ? 1.4795 1.9978 1.4571 0.2038 0.0412 0.4900 48 CYS C CA 3663 C C . CYS C 48 ? 1.4973 1.9865 1.4734 0.2140 0.0430 0.4874 48 CYS C C 3664 O O . CYS C 48 ? 1.4398 1.9444 1.4127 0.2340 0.0459 0.4900 48 CYS C O 3665 C CB . CYS C 48 ? 1.4854 2.0718 1.4678 0.1977 0.0380 0.4922 48 CYS C CB 3666 S SG . CYS C 48 ? 1.3106 1.9089 1.2994 0.1687 0.0314 0.4877 48 CYS C SG 3667 N N . PRO C 49 ? 1.4300 1.8788 1.4084 0.2006 0.0414 0.4819 49 PRO C N 3668 C CA . PRO C 49 ? 1.3970 1.8144 1.3742 0.2084 0.0430 0.4783 49 PRO C CA 3669 C C . PRO C 49 ? 1.4437 1.9041 1.4234 0.2162 0.0422 0.4804 49 PRO C C 3670 O O . PRO C 49 ? 1.3470 1.8425 1.3325 0.2008 0.0381 0.4808 49 PRO C O 3671 C CB . PRO C 49 ? 1.2338 1.6162 1.2152 0.1872 0.0401 0.4722 49 PRO C CB 3672 C CG . PRO C 49 ? 1.2817 1.6939 1.2675 0.1671 0.0358 0.4735 49 PRO C CG 3673 C CD . PRO C 49 ? 1.3279 1.7639 1.3103 0.1764 0.0376 0.4784 49 PRO C CD 3674 N N . SER C 50 ? 1.6510 2.1073 1.6256 0.2386 0.0459 0.4814 50 SER C N 3675 C CA . SER C 50 ? 1.8518 2.3484 1.8279 0.2493 0.0458 0.4828 50 SER C CA 3676 C C . SER C 50 ? 2.0579 2.5505 2.0388 0.2398 0.0434 0.4792 50 SER C C 3677 O O . SER C 50 ? 2.0090 2.5499 1.9944 0.2361 0.0410 0.4807 50 SER C O 3678 C CB . SER C 50 ? 1.8946 2.3811 1.8619 0.2776 0.0508 0.4844 50 SER C CB 3679 O OG . SER C 50 ? 1.9619 2.4985 1.9298 0.2912 0.0513 0.4863 50 SER C OG 3680 N N . LYS C 51 ? 2.3635 2.8021 2.3429 0.2375 0.0443 0.4744 51 LYS C N 3681 C CA . LYS C 51 ? 2.3730 2.8042 2.3580 0.2230 0.0413 0.4710 51 LYS C CA 3682 C C . LYS C 51 ? 2.3589 2.8266 2.3470 0.2264 0.0400 0.4718 51 LYS C C 3683 O O . LYS C 51 ? 2.3603 2.8796 2.3486 0.2363 0.0401 0.4753 51 LYS C O 3684 C CB . LYS C 51 ? 2.3024 2.7434 2.2931 0.1970 0.0368 0.4711 51 LYS C CB 3685 C CG . LYS C 51 ? 2.2563 2.7444 2.2526 0.1824 0.0323 0.4732 51 LYS C CG 3686 C CD . LYS C 51 ? 2.1729 2.6799 2.1709 0.1660 0.0293 0.4748 51 LYS C CD 3687 C CE . LYS C 51 ? 2.1455 2.6885 2.1408 0.1809 0.0314 0.4788 51 LYS C CE 3688 N NZ . LYS C 51 ? 2.1385 2.6688 2.1321 0.1755 0.0316 0.4793 51 LYS C NZ 3689 N N . LYS C 52 ? 2.2634 2.7009 2.2540 0.2176 0.0389 0.4677 52 LYS C N 3690 C CA . LYS C 52 ? 2.0627 2.5230 2.0588 0.2058 0.0355 0.4676 52 LYS C CA 3691 C C . LYS C 52 ? 2.0281 2.5551 2.0268 0.2092 0.0338 0.4715 52 LYS C C 3692 O O . LYS C 52 ? 2.1730 2.7400 2.1701 0.2203 0.0349 0.4746 52 LYS C O 3693 C CB . LYS C 52 ? 1.9776 2.4284 1.9787 0.1768 0.0310 0.4667 52 LYS C CB 3694 C CG . LYS C 52 ? 1.8290 2.2271 1.8291 0.1681 0.0316 0.4625 52 LYS C CG 3695 C CD . LYS C 52 ? 1.8390 2.1848 1.8362 0.1781 0.0351 0.4568 52 LYS C CD 3696 C CE . LYS C 52 ? 1.8012 2.1037 1.7972 0.1691 0.0357 0.4524 52 LYS C CE 3697 N NZ . LYS C 52 ? 1.7499 2.0015 1.7435 0.1737 0.0383 0.4453 52 LYS C NZ 3698 N N . PRO C 53 ? 1.7751 2.3156 1.7779 0.1994 0.0312 0.4709 53 PRO C N 3699 C CA . PRO C 53 ? 1.7499 2.3544 1.7557 0.1983 0.0290 0.4735 53 PRO C CA 3700 C C . PRO C 53 ? 2.0009 2.6387 2.0116 0.1673 0.0231 0.4757 53 PRO C C 3701 O O . PRO C 53 ? 1.8669 2.5641 1.8799 0.1622 0.0210 0.4775 53 PRO C O 3702 C CB . PRO C 53 ? 1.6926 2.2850 1.6984 0.2075 0.0302 0.4710 53 PRO C CB 3703 C CG . PRO C 53 ? 1.6179 2.1397 1.6230 0.2010 0.0310 0.4671 53 PRO C CG 3704 C CD . PRO C 53 ? 1.6882 2.1851 1.6929 0.1889 0.0303 0.4672 53 PRO C CD 3705 N N . TYR C 54 ? 2.1037 2.7013 2.1152 0.1464 0.0207 0.4745 54 TYR C N 3706 C CA . TYR C 54 ? 2.1574 2.7680 2.1714 0.1148 0.0152 0.4755 54 TYR C CA 3707 C C . TYR C 54 ? 1.6651 2.2563 1.6778 0.0967 0.0131 0.4752 54 TYR C C 3708 O O . TYR C 54 ? 1.4757 2.0250 1.4886 0.0799 0.0112 0.4729 54 TYR C O 3709 C CB . TYR C 54 ? 2.2329 2.8098 2.2488 0.1049 0.0140 0.4734 54 TYR C CB 3710 C CG . TYR C 54 ? 2.3169 2.8882 2.3339 0.0728 0.0090 0.4736 54 TYR C CG 3711 C CD1 . TYR C 54 ? 2.3553 2.9768 2.3724 0.0525 0.0049 0.4763 54 TYR C CD1 3712 C CD2 . TYR C 54 ? 2.3738 2.8872 2.3909 0.0621 0.0085 0.4700 54 TYR C CD2 3713 C CE1 . TYR C 54 ? 2.4256 3.0356 2.4419 0.0219 0.0004 0.4760 54 TYR C CE1 3714 C CE2 . TYR C 54 ? 2.4552 2.9584 2.4724 0.0343 0.0041 0.4696 54 TYR C CE2 3715 C CZ . TYR C 54 ? 2.5182 3.0673 2.5343 0.0138 0.0001 0.4729 54 TYR C CZ 3716 O OH . TYR C 54 ? 2.5956 3.1286 2.6102 -0.0154 -0.0042 0.4719 54 TYR C OH 3717 N N . GLU C 55 ? 1.7239 2.3469 1.7352 0.0994 0.0131 0.4771 55 GLU C N 3718 C CA . GLU C 55 ? 1.5362 2.1355 1.5457 0.0859 0.0118 0.4763 55 GLU C CA 3719 C C . GLU C 55 ? 1.4363 2.0764 1.4445 0.0647 0.0078 0.4777 55 GLU C C 3720 O O . GLU C 55 ? 1.4119 2.1107 1.4208 0.0626 0.0065 0.4794 55 GLU C O 3721 C CB . GLU C 55 ? 1.5157 2.0914 1.5229 0.1095 0.0166 0.4759 55 GLU C CB 3722 C CG . GLU C 55 ? 1.6369 2.1721 1.6435 0.1300 0.0209 0.4735 55 GLU C CG 3723 C CD . GLU C 55 ? 1.7595 2.2496 1.7680 0.1173 0.0196 0.4696 55 GLU C CD 3724 O OE1 . GLU C 55 ? 1.7544 2.2134 1.7633 0.0994 0.0174 0.4671 55 GLU C OE1 3725 O OE2 . GLU C 55 ? 1.8303 2.3192 1.8399 0.1253 0.0206 0.4689 55 GLU C OE2 3726 N N . GLU C 56 ? 1.3419 1.9503 1.3480 0.0494 0.0062 0.4761 56 GLU C N 3727 C CA . GLU C 56 ? 1.3978 2.0378 1.4013 0.0286 0.0027 0.4765 56 GLU C CA 3728 C C . GLU C 56 ? 1.3823 1.9983 1.3838 0.0368 0.0048 0.4758 56 GLU C C 3729 O O . GLU C 56 ? 1.4568 2.0624 1.4554 0.0183 0.0024 0.4743 56 GLU C O 3730 C CB . GLU C 56 ? 1.2214 1.8487 1.2228 -0.0037 -0.0019 0.4748 56 GLU C CB 3731 C CG . GLU C 56 ? 1.0667 1.7039 1.0704 -0.0083 -0.0031 0.4754 56 GLU C CG 3732 C CD . GLU C 56 ? 1.1612 1.8301 1.1624 -0.0391 -0.0076 0.4751 56 GLU C CD 3733 O OE1 . GLU C 56 ? 1.0261 1.6981 1.0253 -0.0594 -0.0102 0.4703 56 GLU C OE1 3734 O OE2 . GLU C 56 ? 1.3928 2.0792 1.3960 -0.0441 -0.0087 0.4759 56 GLU C OE2 3735 N N . VAL C 57 ? 1.1392 1.7462 1.1418 0.0652 0.0095 0.4768 57 VAL C N 3736 C CA . VAL C 57 ? 0.8750 1.4726 0.8759 0.0810 0.0128 0.4773 57 VAL C CA 3737 C C . VAL C 57 ? 0.7981 1.4437 0.7975 0.0782 0.0118 0.4792 57 VAL C C 3738 O O . VAL C 57 ? 0.9059 1.6053 0.9066 0.0801 0.0110 0.4808 57 VAL C O 3739 C CB . VAL C 57 ? 0.7298 1.3168 0.7310 0.1095 0.0179 0.4783 57 VAL C CB 3740 C CG1 . VAL C 57 ? 0.6611 1.2522 0.6594 0.1276 0.0217 0.4803 57 VAL C CG1 3741 C CG2 . VAL C 57 ? 0.9872 1.5141 0.9893 0.1091 0.0189 0.4744 57 VAL C CG2 3742 N N . THR C 58 ? 0.7962 1.4231 0.7934 0.0737 0.0119 0.4784 58 THR C N 3743 C CA . THR C 58 ? 0.7343 1.4024 0.7295 0.0669 0.0105 0.4792 58 THR C CA 3744 C C . THR C 58 ? 1.0120 1.6521 1.0054 0.0800 0.0138 0.4797 58 THR C C 3745 O O . THR C 58 ? 1.1172 1.7045 1.1099 0.0776 0.0147 0.4775 58 THR C O 3746 C CB . THR C 58 ? 0.8518 1.5292 0.8440 0.0328 0.0049 0.4763 58 THR C CB 3747 O OG1 . THR C 58 ? 0.8348 1.5072 0.8279 0.0180 0.0023 0.4753 58 THR C OG1 3748 C CG2 . THR C 58 ? 0.6447 1.3831 0.6349 0.0210 0.0025 0.4756 58 THR C CG2 3749 N N . CYS C 59 ? 0.8971 1.5729 0.8902 0.0942 0.0160 0.4824 59 CYS C N 3750 C CA . CYS C 59 ? 0.8772 1.5387 0.8680 0.1047 0.0189 0.4838 59 CYS C CA 3751 C C . CYS C 59 ? 0.9622 1.6621 0.9515 0.0873 0.0155 0.4827 59 CYS C C 3752 O O . CYS C 59 ? 0.8629 1.6100 0.8526 0.0722 0.0119 0.4812 59 CYS C O 3753 C CB . CYS C 59 ? 0.8833 1.5637 0.8739 0.1331 0.0239 0.4881 59 CYS C CB 3754 S SG . CYS C 59 ? 1.2607 1.8834 1.2479 0.1610 0.0306 0.4900 59 CYS C SG 3755 N N . CYS C 60 ? 1.0451 1.7273 1.0321 0.0892 0.0170 0.4829 60 CYS C N 3756 C CA . CYS C 60 ? 0.8867 1.6083 0.8717 0.0768 0.0146 0.4817 60 CYS C CA 3757 C C . CYS C 60 ? 0.8759 1.5766 0.8591 0.0889 0.0180 0.4838 60 CYS C C 3758 O O . CYS C 60 ? 0.9093 1.5586 0.8921 0.0993 0.0212 0.4846 60 CYS C O 3759 C CB . CYS C 60 ? 0.9156 1.6347 0.8973 0.0462 0.0095 0.4767 60 CYS C CB 3760 S SG . CYS C 60 ? 1.2228 1.8668 1.2032 0.0358 0.0091 0.4741 60 CYS C SG 3761 N N . SER C 61 ? 0.9655 1.7077 0.9476 0.0860 0.0173 0.4839 61 SER C N 3762 C CA . SER C 61 ? 0.8705 1.6048 0.8513 0.0998 0.0209 0.4871 61 SER C CA 3763 C C . SER C 61 ? 0.9522 1.6984 0.9299 0.0816 0.0181 0.4835 61 SER C C 3764 O O . SER C 61 ? 0.8699 1.6123 0.8461 0.0887 0.0204 0.4855 61 SER C O 3765 C CB . SER C 61 ? 0.8533 1.6291 0.8359 0.1205 0.0241 0.4921 61 SER C CB 3766 O OG . SER C 61 ? 1.1814 1.9539 1.1660 0.1346 0.0261 0.4943 61 SER C OG 3767 N N . THR C 62 ? 0.9901 1.7489 0.9658 0.0573 0.0133 0.4779 62 THR C N 3768 C CA . THR C 62 ? 0.8969 1.6666 0.8679 0.0359 0.0102 0.4723 62 THR C CA 3769 C C . THR C 62 ? 1.1661 1.8688 1.1391 0.0300 0.0107 0.4656 62 THR C C 3770 O O . THR C 62 ? 1.2188 1.8784 1.1922 0.0374 0.0122 0.4699 62 THR C O 3771 C CB . THR C 62 ? 1.1244 1.9236 1.0993 0.0101 0.0053 0.4584 62 THR C CB 3772 O OG1 . THR C 62 ? 1.3913 2.2531 1.3646 0.0169 0.0052 0.4654 62 THR C OG1 3773 C CG2 . THR C 62 ? 0.8814 1.6836 0.8585 -0.0149 0.0017 0.4408 62 THR C CG2 3774 N N . ASP C 63 ? 1.1015 1.7971 1.0754 0.0181 0.0095 0.4552 63 ASP C N 3775 C CA . ASP C 63 ? 1.0085 1.6480 0.9852 0.0070 0.0085 0.4443 63 ASP C CA 3776 C C . ASP C 63 ? 1.0965 1.7235 1.0770 -0.0123 0.0042 0.4329 63 ASP C C 3777 O O . ASP C 63 ? 0.9842 1.6480 0.9649 -0.0166 0.0026 0.4343 63 ASP C O 3778 C CB . ASP C 63 ? 0.8777 1.5206 0.8548 -0.0035 0.0072 0.4329 63 ASP C CB 3779 C CG . ASP C 63 ? 0.9872 1.6167 0.9607 0.0136 0.0117 0.4433 63 ASP C CG 3780 O OD1 . ASP C 63 ? 1.0521 1.6596 1.0228 0.0318 0.0156 0.4580 63 ASP C OD1 3781 O OD2 . ASP C 63 ? 1.0778 1.7194 1.0509 0.0085 0.0114 0.4368 63 ASP C OD2 3782 N N . LYS C 64 ? 1.3629 1.9399 1.3460 -0.0235 0.0024 0.4225 64 LYS C N 3783 C CA . LYS C 64 ? 1.4518 2.0206 1.4372 -0.0457 -0.0025 0.4098 64 LYS C CA 3784 C C . LYS C 64 ? 1.2843 1.8538 1.2706 -0.0448 -0.0028 0.4166 64 LYS C C 3785 O O . LYS C 64 ? 1.1963 1.7434 1.1840 -0.0613 -0.0063 0.4081 64 LYS C O 3786 C CB . LYS C 64 ? 1.6917 2.3092 1.6765 -0.0630 -0.0060 0.3997 64 LYS C CB 3787 C CG . LYS C 64 ? 1.8877 2.5043 1.8722 -0.0745 -0.0081 0.3855 64 LYS C CG 3788 C CD . LYS C 64 ? 1.8810 2.5417 1.8645 -0.0954 -0.0121 0.3740 64 LYS C CD 3789 C CE . LYS C 64 ? 1.9225 2.5650 1.9062 -0.1152 -0.0162 0.3662 64 LYS C CE 3790 N NZ . LYS C 64 ? 1.9071 2.4846 1.8916 -0.1186 -0.0176 0.3590 64 LYS C NZ 3791 N N . CYS C 65 ? 1.2476 1.8429 1.2323 -0.0255 0.0006 0.4316 65 CYS C N 3792 C CA . CYS C 65 ? 1.1738 1.8030 1.1589 -0.0288 -0.0007 0.4354 65 CYS C CA 3793 C C . CYS C 65 ? 1.2226 1.8219 1.2092 -0.0257 -0.0005 0.4396 65 CYS C C 3794 O O . CYS C 65 ? 1.2240 1.8530 1.2110 -0.0303 -0.0019 0.4418 65 CYS C O 3795 C CB . CYS C 65 ? 1.0983 1.7818 1.0806 -0.0097 0.0021 0.4485 65 CYS C CB 3796 S SG . CYS C 65 ? 0.9773 1.6435 0.9557 0.0260 0.0082 0.4677 65 CYS C SG 3797 N N . ASN C 66 ? 1.2483 1.7931 1.2359 -0.0181 0.0013 0.4409 66 ASN C N 3798 C CA . ASN C 66 ? 1.1556 1.6735 1.1449 -0.0172 0.0012 0.4435 66 ASN C CA 3799 C C . ASN C 66 ? 0.9190 1.3895 0.9106 -0.0361 -0.0022 0.4315 66 ASN C C 3800 O O . ASN C 66 ? 0.8078 1.2327 0.8004 -0.0290 -0.0005 0.4323 66 ASN C O 3801 C CB . ASN C 66 ? 1.0810 1.5759 1.0689 0.0094 0.0063 0.4562 66 ASN C CB 3802 C CG . ASN C 66 ? 0.9479 1.3918 0.9356 0.0149 0.0086 0.4545 66 ASN C CG 3803 O OD1 . ASN C 66 ? 1.0201 1.4610 1.0074 0.0087 0.0081 0.4484 66 ASN C OD1 3804 N ND2 . ASN C 66 ? 0.8791 1.2853 0.8670 0.0266 0.0113 0.4596 66 ASN C ND2 3805 N N . PRO C 67 ? 0.9810 1.4619 0.9727 -0.0606 -0.0070 0.4203 67 PRO C N 3806 C CA . PRO C 67 ? 1.0212 1.4536 1.0138 -0.0761 -0.0103 0.4102 67 PRO C CA 3807 C C . PRO C 67 ? 1.2120 1.6309 1.2056 -0.0799 -0.0113 0.4139 67 PRO C C 3808 O O . PRO C 67 ? 1.3501 1.8075 1.3436 -0.0803 -0.0114 0.4201 67 PRO C O 3809 C CB . PRO C 67 ? 0.9559 1.4029 0.9466 -0.1006 -0.0152 0.3968 67 PRO C CB 3810 C CG . PRO C 67 ? 0.9466 1.4547 0.9362 -0.1033 -0.0152 0.4013 67 PRO C CG 3811 C CD . PRO C 67 ? 0.9739 1.5058 0.9642 -0.0756 -0.0098 0.4155 67 PRO C CD 3812 N N . HIS C 68 ? 1.2472 1.6147 1.2418 -0.0827 -0.0123 0.4099 68 HIS C N 3813 C CA . HIS C 68 ? 1.2926 1.6426 1.2879 -0.0902 -0.0142 0.4115 68 HIS C CA 3814 C C . HIS C 68 ? 1.4443 1.8197 1.4370 -0.1155 -0.0191 0.4056 68 HIS C C 3815 O O . HIS C 68 ? 1.5947 1.9862 1.5852 -0.1280 -0.0214 0.3974 68 HIS C O 3816 C CB . HIS C 68 ? 1.2166 1.5079 1.2127 -0.0908 -0.0150 0.4062 68 HIS C CB 3817 C CG . HIS C 68 ? 1.2986 1.5682 1.2953 -0.0966 -0.0166 0.4085 68 HIS C CG 3818 N ND1 . HIS C 68 ? 1.3189 1.5770 1.3129 -0.1192 -0.0219 0.4021 68 HIS C ND1 3819 C CD2 . HIS C 68 ? 1.3432 1.6015 1.3422 -0.0829 -0.0137 0.4167 68 HIS C CD2 3820 C CE1 . HIS C 68 ? 1.3991 1.6409 1.3941 -0.1189 -0.0221 0.4071 68 HIS C CE1 3821 N NE2 . HIS C 68 ? 1.4189 1.6616 1.4173 -0.0969 -0.0172 0.4154 68 HIS C NE2 3822 N N . PRO C 69 ? 1.2556 1.6364 1.2481 -0.1242 -0.0207 0.4095 69 PRO C N 3823 C CA . PRO C 69 ? 1.1634 1.5629 1.1523 -0.1515 -0.0256 0.4035 69 PRO C CA 3824 C C . PRO C 69 ? 1.2400 1.5974 1.2251 -0.1713 -0.0303 0.3905 69 PRO C C 3825 O O . PRO C 69 ? 1.0799 1.4407 1.0605 -0.1957 -0.0347 0.3848 69 PRO C O 3826 C CB . PRO C 69 ? 1.2146 1.6188 1.2040 -0.1547 -0.0260 0.4110 69 PRO C CB 3827 C CG . PRO C 69 ? 1.1391 1.5618 1.1324 -0.1266 -0.0206 0.4221 69 PRO C CG 3828 C CD . PRO C 69 ? 1.0398 1.4273 1.0347 -0.1089 -0.0177 0.4206 69 PRO C CD 3829 N N . LYS C 70 ? 1.5632 1.8818 1.5495 -0.1602 -0.0292 0.3858 70 LYS C N 3830 C CA . LYS C 70 ? 1.7400 2.0222 1.7229 -0.1730 -0.0331 0.3724 70 LYS C CA 3831 C C . LYS C 70 ? 1.9663 2.2721 1.9441 -0.1962 -0.0372 0.3623 70 LYS C C 3832 O O . LYS C 70 ? 2.0141 2.3027 1.9867 -0.2181 -0.0419 0.3567 70 LYS C O 3833 C CB . LYS C 70 ? 1.7413 2.0044 1.7270 -0.1538 -0.0300 0.3699 70 LYS C CB 3834 C CG . LYS C 70 ? 1.6912 1.9966 1.6787 -0.1421 -0.0264 0.3724 70 LYS C CG 3835 C CD . LYS C 70 ? 1.5631 1.8549 1.5543 -0.1170 -0.0212 0.3791 70 LYS C CD 3836 C CE . LYS C 70 ? 1.4477 1.7314 1.4385 -0.1135 -0.0209 0.3706 70 LYS C CE 3837 N NZ . LYS C 70 ? 1.4022 1.6775 1.3956 -0.0906 -0.0154 0.3787 70 LYS C NZ 3838 N N . GLN C 71 ? 2.0476 2.3918 2.0263 -0.1922 -0.0355 0.3601 71 GLN C N 3839 C CA . GLN C 71 ? 2.0705 2.4452 2.0447 -0.2141 -0.0389 0.3507 71 GLN C CA 3840 C C . GLN C 71 ? 2.0486 2.4915 2.0247 -0.2104 -0.0362 0.3568 71 GLN C C 3841 O O . GLN C 71 ? 1.9750 2.4504 1.9521 -0.2109 -0.0352 0.3664 71 GLN C O 3842 C CB . GLN C 71 ? 2.0647 2.4153 2.0363 -0.2190 -0.0413 0.3356 71 GLN C CB 3843 C CG . GLN C 71 ? 2.1145 2.3995 2.0835 -0.2213 -0.0443 0.3279 71 GLN C CG 3844 C CD . GLN C 71 ? 2.1851 2.4497 2.1469 -0.2429 -0.0500 0.3107 71 GLN C CD 3845 O OE1 . GLN C 71 ? 2.2556 2.5485 2.2162 -0.2488 -0.0505 0.3020 71 GLN C OE1 3846 N NE2 . GLN C 71 ? 2.1554 2.3709 2.1116 -0.2547 -0.0543 0.3058 71 GLN C NE2 3847 N N . ARG C 72 ? 2.0777 2.5435 2.0541 -0.2062 -0.0353 0.3511 72 ARG C N 3848 C CA . ARG C 72 ? 2.1828 2.7139 2.1606 -0.2011 -0.0328 0.3561 72 ARG C CA 3849 C C . ARG C 72 ? 2.2644 2.7993 2.2450 -0.1793 -0.0292 0.3573 72 ARG C C 3850 O O . ARG C 72 ? 2.2479 2.7400 2.2283 -0.1772 -0.0299 0.3495 72 ARG C O 3851 C CB . ARG C 72 ? 1.9241 2.4881 1.8971 -0.2298 -0.0370 0.3449 72 ARG C CB 3852 C CG . ARG C 72 ? 1.9602 2.5741 1.9330 -0.2296 -0.0362 0.3396 72 ARG C CG 3853 C CD . ARG C 72 ? 1.9958 2.6671 1.9656 -0.2513 -0.0383 0.3365 72 ARG C CD 3854 N NE . ARG C 72 ? 2.0383 2.7660 2.0090 -0.2457 -0.0365 0.3349 72 ARG C NE 3855 C CZ . ARG C 72 ? 1.9402 2.7258 1.9137 -0.2297 -0.0330 0.3471 72 ARG C CZ 3856 N NH1 . ARG C 72 ? 1.8698 2.6671 1.8454 -0.2176 -0.0308 0.3612 72 ARG C NH1 3857 N NH2 . ARG C 72 ? 1.9153 2.7493 1.8890 -0.2254 -0.0318 0.3448 72 ARG C NH2 3858 N N . PRO C 73 ? 2.2208 2.8058 2.2033 -0.1624 -0.0253 0.3678 73 PRO C N 3859 C CA . PRO C 73 ? 2.2285 2.8100 2.2130 -0.1386 -0.0211 0.3731 73 PRO C CA 3860 C C . PRO C 73 ? 2.2758 2.8316 2.2595 -0.1434 -0.0226 0.3600 73 PRO C C 3861 O O . PRO C 73 ? 2.3053 2.8735 2.2866 -0.1621 -0.0261 0.3464 73 PRO C O 3862 C CB . PRO C 73 ? 2.1907 2.8384 2.1751 -0.1281 -0.0185 0.3818 73 PRO C CB 3863 C CG . PRO C 73 ? 2.2141 2.9031 2.1969 -0.1485 -0.0215 0.3780 73 PRO C CG 3864 C CD . PRO C 73 ? 2.2350 2.8845 2.2170 -0.1659 -0.0249 0.3735 73 PRO C CD 3865 N N . ILE D 1 ? 0.5449 2.0165 0.6932 0.0934 0.0456 0.1257 1 ILE D N 3866 C CA . ILE D 1 ? 0.5162 1.9848 0.6625 0.1064 0.0406 0.1488 1 ILE D CA 3867 C C . ILE D 1 ? 0.7556 2.1873 0.9083 0.1139 0.0375 0.1778 1 ILE D C 3868 O O . ILE D 1 ? 0.7448 2.1304 0.8986 0.1058 0.0402 0.1729 1 ILE D O 3869 C CB . ILE D 1 ? 0.5501 2.0107 0.6999 0.1021 0.0449 0.1303 1 ILE D CB 3870 C CG1 . ILE D 1 ? 0.5809 2.0409 0.7283 0.1171 0.0395 0.1514 1 ILE D CG1 3871 C CG2 . ILE D 1 ? 0.5044 1.9253 0.6654 0.0909 0.0528 0.1158 1 ILE D CG2 3872 C CD1 . ILE D 1 ? 0.8717 2.3655 1.0064 0.1308 0.0318 0.1711 1 ILE D CD1 3873 N N . VAL D 2 ? 0.9174 2.3475 1.0631 0.1281 0.0293 0.2071 2 VAL D N 3874 C CA . VAL D 2 ? 0.8788 2.2449 1.0176 0.1333 0.0235 0.2330 2 VAL D CA 3875 C C . VAL D 2 ? 0.8938 2.2180 1.0291 0.1380 0.0223 0.2339 2 VAL D C 3876 O O . VAL D 2 ? 0.9139 2.2640 1.0466 0.1483 0.0195 0.2374 2 VAL D O 3877 C CB . VAL D 2 ? 0.8906 2.2675 1.0214 0.1459 0.0146 0.2672 2 VAL D CB 3878 C CG1 . VAL D 2 ? 0.5404 1.8463 0.6626 0.1518 0.0085 0.2915 2 VAL D CG1 3879 C CG2 . VAL D 2 ? 0.5272 1.9398 0.6600 0.1414 0.0146 0.2723 2 VAL D CG2 3880 N N . CYS D 3 ? 0.9759 2.2381 1.1115 0.1306 0.0246 0.2293 3 CYS D N 3881 C CA . CYS D 3 ? 0.7389 1.9553 0.8717 0.1331 0.0240 0.2286 3 CYS D CA 3882 C C . CYS D 3 ? 0.5355 1.6912 0.6609 0.1389 0.0176 0.2551 3 CYS D C 3883 O O . CYS D 3 ? 0.5352 1.6715 0.6602 0.1342 0.0169 0.2639 3 CYS D O 3884 C CB . CYS D 3 ? 0.6281 1.8222 0.7671 0.1179 0.0328 0.1991 3 CYS D CB 3885 S SG . CYS D 3 ? 1.3537 2.6090 1.5015 0.1045 0.0420 0.1644 3 CYS D SG 3886 N N . HIS D 4 ? 0.5578 1.6820 0.6774 0.1483 0.0132 0.2660 4 HIS D N 3887 C CA . HIS D 4 ? 0.6785 1.7358 0.7923 0.1494 0.0091 0.2837 4 HIS D CA 3888 C C . HIS D 4 ? 0.7888 1.8014 0.9073 0.1363 0.0154 0.2656 4 HIS D C 3889 O O . HIS D 4 ? 0.9207 1.9401 1.0442 0.1300 0.0215 0.2419 4 HIS D O 3890 C CB . HIS D 4 ? 0.7485 1.7817 0.8538 0.1640 0.0022 0.3007 4 HIS D CB 3891 C CG . HIS D 4 ? 0.6683 1.7273 0.7656 0.1786 -0.0057 0.3254 4 HIS D CG 3892 N ND1 . HIS D 4 ? 0.7985 1.8934 0.8927 0.1929 -0.0087 0.3271 4 HIS D ND1 3893 C CD2 . HIS D 4 ? 0.5851 1.6380 0.6758 0.1817 -0.0115 0.3507 4 HIS D CD2 3894 C CE1 . HIS D 4 ? 0.7068 1.8159 0.7926 0.2046 -0.0160 0.3523 4 HIS D CE1 3895 N NE2 . HIS D 4 ? 0.7545 1.8371 0.8376 0.1974 -0.0179 0.3676 4 HIS D NE2 3896 N N . THR D 5 ? 0.7987 1.7663 0.9151 0.1319 0.0140 0.2771 5 THR D N 3897 C CA . THR D 5 ? 0.6823 1.6015 0.8015 0.1216 0.0189 0.2640 5 THR D CA 3898 C C . THR D 5 ? 0.5934 1.4515 0.7060 0.1249 0.0138 0.2833 5 THR D C 3899 O O . THR D 5 ? 0.5565 1.4038 0.6624 0.1316 0.0068 0.3081 5 THR D O 3900 C CB . THR D 5 ? 0.7818 1.7074 0.9070 0.1096 0.0250 0.2499 5 THR D CB 3901 O OG1 . THR D 5 ? 0.5313 1.4031 0.6573 0.1017 0.0286 0.2418 5 THR D OG1 3902 C CG2 . THR D 5 ? 0.5347 1.4755 0.6574 0.1119 0.0204 0.2702 5 THR D CG2 3903 N N . THR D 6 ? 0.6115 1.4301 0.7257 0.1193 0.0176 0.2710 6 THR D N 3904 C CA . THR D 6 ? 0.8462 1.6064 0.9548 0.1215 0.0136 0.2854 6 THR D CA 3905 C C . THR D 6 ? 0.8268 1.5502 0.9372 0.1113 0.0165 0.2837 6 THR D C 3906 O O . THR D 6 ? 0.9119 1.5914 1.0173 0.1127 0.0123 0.2995 6 THR D O 3907 C CB . THR D 6 ? 0.5900 1.3277 0.6981 0.1237 0.0148 0.2753 6 THR D CB 3908 O OG1 . THR D 6 ? 0.5441 1.3003 0.6592 0.1136 0.0233 0.2479 6 THR D OG1 3909 C CG2 . THR D 6 ? 0.5611 1.3181 0.6640 0.1381 0.0089 0.2855 6 THR D CG2 3910 N N . ALA D 7 ? 0.8911 1.6345 1.0080 0.1020 0.0233 0.2658 7 ALA D N 3911 C CA . ALA D 7 ? 0.9130 1.6294 1.0318 0.0938 0.0264 0.2631 7 ALA D CA 3912 C C . ALA D 7 ? 0.5745 1.2838 0.6892 0.0960 0.0204 0.2870 7 ALA D C 3913 O O . ALA D 7 ? 0.8402 1.5317 0.9559 0.0906 0.0221 0.2871 7 ALA D O 3914 C CB . ALA D 7 ? 0.9846 1.7315 1.1101 0.0858 0.0341 0.2390 7 ALA D CB 3915 N N . THR D 8 ? 0.5481 1.2702 0.6573 0.1042 0.0133 0.3073 8 THR D N 3916 C CA . THR D 8 ? 0.5545 1.2844 0.6586 0.1064 0.0071 0.3313 8 THR D CA 3917 C C . THR D 8 ? 0.6992 1.3910 0.7936 0.1132 -0.0009 0.3551 8 THR D C 3918 O O . THR D 8 ? 0.8367 1.5149 0.9286 0.1200 -0.0025 0.3538 8 THR D O 3919 C CB . THR D 8 ? 0.7646 1.5564 0.8702 0.1103 0.0063 0.3322 8 THR D CB 3920 O OG1 . THR D 8 ? 0.6162 1.4392 0.7267 0.1038 0.0097 0.3259 8 THR D OG1 3921 C CG2 . THR D 8 ? 0.7659 1.5622 0.8628 0.1188 -0.0020 0.3583 8 THR D CG2 3922 N N . SER D 9 ? 0.9338 1.6063 1.0228 0.1105 -0.0056 0.3755 9 SER D N 3923 C CA . SER D 9 ? 1.0347 1.6648 1.1135 0.1145 -0.0131 0.3980 9 SER D CA 3924 C C . SER D 9 ? 1.0732 1.7182 1.1446 0.1143 -0.0195 0.4233 9 SER D C 3925 O O . SER D 9 ? 1.0115 1.6647 1.0847 0.1055 -0.0184 0.4273 9 SER D O 3926 C CB . SER D 9 ? 1.0941 1.6723 1.1729 0.1079 -0.0118 0.3961 9 SER D CB 3927 O OG . SER D 9 ? 1.1577 1.6956 1.2261 0.1101 -0.0191 0.4182 9 SER D OG 3928 N N . PRO D 10 ? 1.0404 1.6901 1.1028 0.1240 -0.0261 0.4407 10 PRO D N 3929 C CA . PRO D 10 ? 1.0066 1.6566 1.0658 0.1370 -0.0284 0.4386 10 PRO D CA 3930 C C . PRO D 10 ? 0.9658 1.6699 1.0341 0.1398 -0.0228 0.4182 10 PRO D C 3931 O O . PRO D 10 ? 0.9146 1.6446 0.9912 0.1309 -0.0171 0.4051 10 PRO D O 3932 C CB . PRO D 10 ? 0.8814 1.5291 0.9274 0.1448 -0.0374 0.4671 10 PRO D CB 3933 C CG . PRO D 10 ? 0.8643 1.5425 0.9107 0.1362 -0.0375 0.4774 10 PRO D CG 3934 C CD . PRO D 10 ? 0.9194 1.5836 0.9737 0.1225 -0.0321 0.4657 10 PRO D CD 3935 N N . ILE D 11 ? 0.9364 1.6576 1.0027 0.1518 -0.0244 0.4154 11 ILE D N 3936 C CA . ILE D 11 ? 0.6037 1.3748 0.6789 0.1537 -0.0187 0.3932 11 ILE D CA 3937 C C . ILE D 11 ? 1.1458 1.9754 1.2215 0.1559 -0.0196 0.3990 11 ILE D C 3938 O O . ILE D 11 ? 0.9365 1.7700 1.0028 0.1620 -0.0265 0.4237 11 ILE D O 3939 C CB . ILE D 11 ? 0.8680 1.6355 0.9405 0.1660 -0.0203 0.3878 11 ILE D CB 3940 C CG1 . ILE D 11 ? 0.5929 1.4007 0.6759 0.1633 -0.0126 0.3594 11 ILE D CG1 3941 C CG2 . ILE D 11 ? 0.9987 1.7742 1.0598 0.1817 -0.0290 0.4113 11 ILE D CG2 3942 C CD1 . ILE D 11 ? 0.5819 1.3590 0.6711 0.1525 -0.0063 0.3407 11 ILE D CD1 3943 N N . SER D 12 ? 1.0863 1.9622 1.1722 0.1509 -0.0126 0.3761 12 SER D N 3944 C CA . SER D 12 ? 1.1052 2.0348 1.1934 0.1487 -0.0121 0.3791 12 SER D CA 3945 C C . SER D 12 ? 1.1579 2.1444 1.2552 0.1476 -0.0058 0.3546 12 SER D C 3946 O O . SER D 12 ? 1.2869 2.2711 1.3894 0.1466 -0.0010 0.3332 12 SER D O 3947 C CB . SER D 12 ? 1.0349 1.9559 1.1268 0.1363 -0.0094 0.3784 12 SER D CB 3948 O OG . SER D 12 ? 1.0390 1.9566 1.1406 0.1280 -0.0010 0.3496 12 SER D OG 3949 N N . ALA D 13 ? 1.0055 2.0431 1.1049 0.1460 -0.0056 0.3572 13 ALA D N 3950 C CA . ALA D 13 ? 0.7373 1.8374 0.8447 0.1450 -0.0003 0.3358 13 ALA D CA 3951 C C . ALA D 13 ? 0.5451 1.6687 0.6609 0.1328 0.0062 0.3179 13 ALA D C 3952 O O . ALA D 13 ? 0.5466 1.6749 0.6609 0.1295 0.0041 0.3314 13 ALA D O 3953 C CB . ALA D 13 ? 0.5659 1.7121 0.6682 0.1554 -0.0055 0.3524 13 ALA D CB 3954 N N . VAL D 14 ? 0.5344 1.6739 0.6587 0.1259 0.0141 0.2874 14 VAL D N 3955 C CA . VAL D 14 ? 0.7386 1.9026 0.8701 0.1157 0.0201 0.2694 14 VAL D CA 3956 C C . VAL D 14 ? 0.6911 1.9099 0.8295 0.1126 0.0261 0.2428 14 VAL D C 3957 O O . VAL D 14 ? 0.7919 2.0224 0.9308 0.1156 0.0272 0.2334 14 VAL D O 3958 C CB . VAL D 14 ? 0.7167 1.8312 0.8512 0.1062 0.0250 0.2560 14 VAL D CB 3959 C CG1 . VAL D 14 ? 1.0060 2.0595 1.1339 0.1087 0.0199 0.2778 14 VAL D CG1 3960 C CG2 . VAL D 14 ? 0.8221 1.9300 0.9618 0.1000 0.0324 0.2263 14 VAL D CG2 3961 N N . THR D 15 ? 0.5837 1.8379 0.7273 0.1065 0.0299 0.2305 15 THR D N 3962 C CA . THR D 15 ? 0.6049 1.9116 0.7552 0.1015 0.0362 0.2027 15 THR D CA 3963 C C . THR D 15 ? 0.5062 1.7822 0.6611 0.0904 0.0444 0.1725 15 THR D C 3964 O O . THR D 15 ? 0.6139 1.8602 0.7700 0.0848 0.0473 0.1660 15 THR D O 3965 C CB . THR D 15 ? 0.6631 2.0251 0.8164 0.1004 0.0365 0.2021 15 THR D CB 3966 O OG1 . THR D 15 ? 0.5093 1.8921 0.6569 0.1095 0.0284 0.2342 15 THR D OG1 3967 C CG2 . THR D 15 ? 0.5012 1.9233 0.6604 0.0968 0.0419 0.1755 15 THR D CG2 3968 N N . CYS D 16 ? 0.6600 1.9432 0.8166 0.0875 0.0482 0.1545 16 CYS D N 3969 C CA . CYS D 16 ? 0.7456 1.9977 0.9050 0.0758 0.0559 0.1267 16 CYS D CA 3970 C C . CYS D 16 ? 0.6534 1.9254 0.8173 0.0670 0.0622 0.1032 16 CYS D C 3971 O O . CYS D 16 ? 0.5742 1.8959 0.7403 0.0698 0.0610 0.1051 16 CYS D O 3972 C CB . CYS D 16 ? 0.8882 2.1585 1.0485 0.0733 0.0586 0.1117 16 CYS D CB 3973 S SG . CYS D 16 ? 1.9199 3.1769 2.0743 0.0876 0.0503 0.1400 16 CYS D SG 3974 N N . PRO D 17 ? 0.7678 1.9980 0.9324 0.0573 0.0685 0.0825 17 PRO D N 3975 C CA . PRO D 17 ? 0.7737 2.0171 0.9414 0.0493 0.0751 0.0565 17 PRO D CA 3976 C C . PRO D 17 ? 0.8163 2.1222 0.9878 0.0439 0.0791 0.0338 17 PRO D C 3977 O O . PRO D 17 ? 1.0446 2.3813 1.2164 0.0458 0.0774 0.0371 17 PRO D O 3978 C CB . PRO D 17 ? 0.8657 2.0471 1.0314 0.0401 0.0808 0.0396 17 PRO D CB 3979 C CG . PRO D 17 ? 0.9079 2.0390 1.0699 0.0452 0.0761 0.0626 17 PRO D CG 3980 C CD . PRO D 17 ? 0.9488 2.1126 1.1102 0.0545 0.0694 0.0845 17 PRO D CD 3981 N N . PRO D 18 ? 0.8321 2.1572 1.0061 0.0375 0.0846 0.0099 18 PRO D N 3982 C CA . PRO D 18 ? 0.8993 2.2784 1.0765 0.0294 0.0897 -0.0170 18 PRO D CA 3983 C C . PRO D 18 ? 0.9888 2.3476 1.1647 0.0170 0.0956 -0.0391 18 PRO D C 3984 O O . PRO D 18 ? 1.1402 2.4403 1.3130 0.0097 0.0996 -0.0493 18 PRO D O 3985 C CB . PRO D 18 ? 0.8169 2.2062 0.9957 0.0259 0.0941 -0.0374 18 PRO D CB 3986 C CG . PRO D 18 ? 0.6952 2.0310 0.8715 0.0318 0.0918 -0.0223 18 PRO D CG 3987 C CD . PRO D 18 ? 0.7245 2.0441 0.8990 0.0412 0.0841 0.0127 18 PRO D CD 3988 N N . GLY D 19 ? 0.9578 2.3671 1.1356 0.0144 0.0960 -0.0460 19 GLY D N 3989 C CA . GLY D 19 ? 0.9469 2.3482 1.1237 0.0008 0.1018 -0.0686 19 GLY D CA 3990 C C . GLY D 19 ? 1.1320 2.5078 1.3064 0.0049 0.0982 -0.0507 19 GLY D C 3991 O O . GLY D 19 ? 1.1819 2.5756 1.3564 -0.0029 0.1009 -0.0634 19 GLY D O 3992 N N . GLU D 20 ? 1.1442 2.4818 1.3165 0.0173 0.0918 -0.0215 20 GLU D N 3993 C CA . GLU D 20 ? 1.0566 2.3668 1.2261 0.0242 0.0871 -0.0011 20 GLU D CA 3994 C C . GLU D 20 ? 1.0691 2.4322 1.2392 0.0384 0.0800 0.0199 20 GLU D C 3995 O O . GLU D 20 ? 1.0565 2.4166 1.2250 0.0517 0.0730 0.0475 20 GLU D O 3996 C CB . GLU D 20 ? 0.9383 2.1794 1.1043 0.0298 0.0837 0.0191 20 GLU D CB 3997 C CG . GLU D 20 ? 0.9369 2.1190 1.1009 0.0177 0.0900 0.0016 20 GLU D CG 3998 C CD . GLU D 20 ? 1.0407 2.1582 1.2012 0.0243 0.0861 0.0236 20 GLU D CD 3999 O OE1 . GLU D 20 ? 1.0501 2.1691 1.2097 0.0371 0.0786 0.0511 20 GLU D OE1 4000 O OE2 . GLU D 20 ? 1.0827 2.1475 1.2409 0.0167 0.0904 0.0137 20 GLU D OE2 4001 N N . ASN D 21 ? 0.9243 2.3323 1.0959 0.0345 0.0822 0.0061 21 ASN D N 4002 C CA . ASN D 21 ? 0.8015 2.2484 0.9635 0.0441 0.0731 0.0153 21 ASN D CA 4003 C C . ASN D 21 ? 0.7491 2.1920 0.9093 0.0590 0.0672 0.0407 21 ASN D C 4004 O O . ASN D 21 ? 0.6220 2.0872 0.7752 0.0737 0.0588 0.0621 21 ASN D O 4005 C CB . ASN D 21 ? 1.1374 2.6102 1.2954 0.0293 0.0764 -0.0165 21 ASN D CB 4006 C CG . ASN D 21 ? 1.2277 2.7203 1.3843 0.0187 0.0790 -0.0392 21 ASN D CG 4007 O OD1 . ASN D 21 ? 1.3227 2.8426 1.4752 0.0074 0.0802 -0.0635 21 ASN D OD1 4008 N ND2 . ASN D 21 ? 1.3337 2.8235 1.4911 0.0259 0.0766 -0.0265 21 ASN D ND2 4009 N N . LEU D 22 ? 0.7919 2.2018 0.9583 0.0556 0.0720 0.0396 22 LEU D N 4010 C CA . LEU D 22 ? 0.6519 2.0469 0.8144 0.0674 0.0665 0.0573 22 LEU D CA 4011 C C . LEU D 22 ? 0.6133 1.9454 0.7709 0.0783 0.0601 0.0853 22 LEU D C 4012 O O . LEU D 22 ? 0.5120 1.7965 0.6695 0.0719 0.0620 0.0854 22 LEU D O 4013 C CB . LEU D 22 ? 0.7218 2.1022 0.8847 0.0544 0.0724 0.0355 22 LEU D CB 4014 C CG . LEU D 22 ? 0.7730 2.2020 0.9355 0.0405 0.0771 0.0061 22 LEU D CG 4015 C CD1 . LEU D 22 ? 0.7471 2.1634 0.9119 0.0249 0.0847 -0.0151 22 LEU D CD1 4016 C CD2 . LEU D 22 ? 0.7980 2.2727 0.9496 0.0525 0.0676 0.0134 22 LEU D CD2 4017 N N . CYS D 23 ? 0.5829 1.9159 0.7361 0.0951 0.0526 0.1087 23 CYS D N 4018 C CA . CYS D 23 ? 0.5160 1.7854 0.6637 0.1037 0.0471 0.1314 23 CYS D CA 4019 C C . CYS D 23 ? 0.9040 2.1509 1.0498 0.1044 0.0475 0.1263 23 CYS D C 4020 O O . CYS D 23 ? 0.9015 2.1931 1.0479 0.1078 0.0480 0.1177 23 CYS D O 4021 C CB . CYS D 23 ? 0.5259 1.8059 0.6685 0.1220 0.0379 0.1625 23 CYS D CB 4022 S SG . CYS D 23 ? 0.5169 1.8140 0.6615 0.1189 0.0375 0.1702 23 CYS D SG 4023 N N . TYR D 24 ? 1.0477 2.2286 1.1911 0.1010 0.0477 0.1307 24 TYR D N 4024 C CA . TYR D 24 ? 0.8681 2.0222 1.0094 0.1011 0.0481 0.1265 24 TYR D CA 4025 C C . TYR D 24 ? 0.7567 1.8528 0.8920 0.1132 0.0411 0.1515 24 TYR D C 4026 O O . TYR D 24 ? 0.7241 1.7917 0.8569 0.1173 0.0372 0.1696 24 TYR D O 4027 C CB . TYR D 24 ? 0.7848 1.9132 0.9293 0.0804 0.0571 0.1008 24 TYR D CB 4028 C CG . TYR D 24 ? 0.7663 1.8291 0.9095 0.0749 0.0578 0.1074 24 TYR D CG 4029 C CD1 . TYR D 24 ? 0.7833 1.8421 0.9282 0.0714 0.0588 0.1090 24 TYR D CD1 4030 C CD2 . TYR D 24 ? 0.8705 1.8779 1.0105 0.0746 0.0570 0.1127 24 TYR D CD2 4031 C CE1 . TYR D 24 ? 1.1106 2.1119 1.2540 0.0675 0.0593 0.1152 24 TYR D CE1 4032 C CE2 . TYR D 24 ? 0.7799 1.7282 0.9185 0.0702 0.0575 0.1194 24 TYR D CE2 4033 C CZ . TYR D 24 ? 0.8419 1.7881 0.9822 0.0669 0.0586 0.1207 24 TYR D CZ 4034 O OH . TYR D 24 ? 0.7038 1.5973 0.8427 0.0635 0.0590 0.1271 24 TYR D OH 4035 N N . ARG D 25 ? 0.6359 1.7162 0.7686 0.1175 0.0400 0.1505 25 ARG D N 4036 C CA . ARG D 25 ? 0.5641 1.5881 0.6911 0.1271 0.0345 0.1686 25 ARG D CA 4037 C C . ARG D 25 ? 0.7401 1.7374 0.8679 0.1177 0.0390 0.1532 25 ARG D C 4038 O O . ARG D 25 ? 0.9744 2.0087 1.1040 0.1156 0.0419 0.1380 25 ARG D O 4039 C CB . ARG D 25 ? 0.5440 1.5842 0.6647 0.1499 0.0254 0.1896 25 ARG D CB 4040 C CG . ARG D 25 ? 0.5524 1.5347 0.6663 0.1605 0.0193 0.2077 25 ARG D CG 4041 C CD . ARG D 25 ? 0.7345 1.7251 0.8404 0.1833 0.0097 0.2318 25 ARG D CD 4042 N NE . ARG D 25 ? 1.1328 2.1741 1.2381 0.1948 0.0086 0.2247 25 ARG D NE 4043 C CZ . ARG D 25 ? 1.2927 2.3426 1.3900 0.2173 0.0004 0.2423 25 ARG D CZ 4044 N NH1 . ARG D 25 ? 1.4420 2.4503 1.5308 0.2293 -0.0074 0.2683 25 ARG D NH1 4045 N NH2 . ARG D 25 ? 1.1727 2.2735 1.2701 0.2279 -0.0001 0.2338 25 ARG D NH2 4046 N N . LYS D 26 ? 0.6892 1.6250 0.8154 0.1122 0.0395 0.1579 26 LYS D N 4047 C CA . LYS D 26 ? 0.6979 1.6009 0.8239 0.1035 0.0433 0.1464 26 LYS D CA 4048 C C . LYS D 26 ? 0.7484 1.6033 0.8686 0.1164 0.0365 0.1660 26 LYS D C 4049 O O . LYS D 26 ? 0.6974 1.5184 0.8145 0.1225 0.0318 0.1849 26 LYS D O 4050 C CB . LYS D 26 ? 0.6876 1.5574 0.8166 0.0834 0.0511 0.1316 26 LYS D CB 4051 C CG . LYS D 26 ? 0.7509 1.6581 0.8847 0.0663 0.0597 0.1056 26 LYS D CG 4052 C CD . LYS D 26 ? 0.9958 1.8575 1.1301 0.0486 0.0666 0.0933 26 LYS D CD 4053 C CE . LYS D 26 ? 1.1118 2.0021 1.2494 0.0300 0.0755 0.0662 26 LYS D CE 4054 N NZ . LYS D 26 ? 1.0353 1.8871 1.1729 0.0178 0.0807 0.0584 26 LYS D NZ 4055 N N . MET D 27 ? 0.8841 1.7366 1.0027 0.1199 0.0361 0.1610 27 MET D N 4056 C CA . MET D 27 ? 0.9121 1.7144 1.0254 0.1294 0.0308 0.1755 27 MET D CA 4057 C C . MET D 27 ? 1.0798 1.8613 1.1944 0.1173 0.0363 0.1597 27 MET D C 4058 O O . MET D 27 ? 1.1634 1.9796 1.2791 0.1169 0.0384 0.1466 27 MET D O 4059 C CB . MET D 27 ? 0.7580 1.5773 0.8655 0.1530 0.0220 0.1912 27 MET D CB 4060 C CG . MET D 27 ? 0.7964 1.6337 0.9009 0.1655 0.0160 0.2095 27 MET D CG 4061 S SD . MET D 27 ? 0.9977 1.8719 1.0954 0.1927 0.0071 0.2228 27 MET D SD 4062 C CE . MET D 27 ? 0.7176 1.6746 0.8223 0.1868 0.0132 0.2009 27 MET D CE 4063 N N . TRP D 28 ? 1.2076 1.9362 1.3219 0.1068 0.0389 0.1603 28 TRP D N 4064 C CA . TRP D 28 ? 1.2322 1.9351 1.3460 0.0982 0.0425 0.1502 28 TRP D CA 4065 C C . TRP D 28 ? 1.1754 1.8324 1.2839 0.1119 0.0353 0.1689 28 TRP D C 4066 O O . TRP D 28 ? 1.0928 1.7426 1.1977 0.1266 0.0280 0.1877 28 TRP D O 4067 C CB . TRP D 28 ? 1.2585 1.9349 1.3751 0.0763 0.0510 0.1366 28 TRP D CB 4068 C CG . TRP D 28 ? 1.4984 2.1328 1.6142 0.0753 0.0497 0.1491 28 TRP D CG 4069 C CD1 . TRP D 28 ? 1.5198 2.1008 1.6327 0.0769 0.0474 0.1608 28 TRP D CD1 4070 C CD2 . TRP D 28 ? 1.6432 2.2881 1.7615 0.0715 0.0513 0.1495 28 TRP D CD2 4071 N NE1 . TRP D 28 ? 1.5981 2.1568 1.7113 0.0749 0.0470 0.1693 28 TRP D NE1 4072 C CE2 . TRP D 28 ? 1.7323 2.3294 1.8488 0.0718 0.0495 0.1625 28 TRP D CE2 4073 C CE3 . TRP D 28 ? 1.6306 2.3230 1.7524 0.0682 0.0540 0.1398 28 TRP D CE3 4074 C CZ2 . TRP D 28 ? 1.7073 2.3033 1.8254 0.0692 0.0502 0.1662 28 TRP D CZ2 4075 C CZ3 . TRP D 28 ? 1.6128 2.3028 1.7362 0.0657 0.0547 0.1432 28 TRP D CZ3 4076 C CH2 . TRP D 28 ? 1.7087 2.3512 1.8302 0.0664 0.0528 0.1564 28 TRP D CH2 4077 N N . CYS D 29 ? 1.3032 1.9274 1.4105 0.1059 0.0373 0.1643 29 CYS D N 4078 C CA . CYS D 29 ? 1.2825 1.8595 1.3847 0.1173 0.0308 0.1808 29 CYS D CA 4079 C C . CYS D 29 ? 1.2735 1.7957 1.3751 0.1077 0.0326 0.1857 29 CYS D C 4080 O O . CYS D 29 ? 1.2804 1.7896 1.3840 0.0926 0.0392 0.1729 29 CYS D O 4081 C CB . CYS D 29 ? 1.1948 1.7756 1.2946 0.1248 0.0289 0.1763 29 CYS D CB 4082 S SG . CYS D 29 ? 1.6948 2.3079 1.7896 0.1520 0.0195 0.1869 29 CYS D SG 4083 N N . ASP D 30 ? 1.1296 1.6204 1.2277 0.1162 0.0266 0.2048 30 ASP D N 4084 C CA . ASP D 30 ? 1.0010 1.4384 1.0972 0.1108 0.0266 0.2114 30 ASP D CA 4085 C C . ASP D 30 ? 1.0740 1.4875 1.1645 0.1249 0.0194 0.2223 30 ASP D C 4086 O O . ASP D 30 ? 1.1377 1.5731 1.2250 0.1404 0.0139 0.2270 30 ASP D O 4087 C CB . ASP D 30 ? 0.8536 1.2681 0.9497 0.1078 0.0255 0.2237 30 ASP D CB 4088 C CG . ASP D 30 ? 0.8491 1.2515 0.9396 0.1228 0.0161 0.2459 30 ASP D CG 4089 O OD1 . ASP D 30 ? 0.6327 1.0306 0.7181 0.1367 0.0098 0.2535 30 ASP D OD1 4090 O OD2 . ASP D 30 ? 0.5733 0.9682 0.6638 0.1202 0.0152 0.2557 30 ASP D OD2 4091 N N . VAL D 31 ? 1.0594 1.4273 1.1481 0.1205 0.0193 0.2271 31 VAL D N 4092 C CA . VAL D 31 ? 1.0061 1.3459 1.0895 0.1310 0.0136 0.2345 31 VAL D CA 4093 C C . VAL D 31 ? 0.9339 1.2624 1.0104 0.1490 0.0038 0.2534 31 VAL D C 4094 O O . VAL D 31 ? 1.1565 1.4508 1.2274 0.1566 -0.0016 0.2625 31 VAL D O 4095 C CB . VAL D 31 ? 1.0463 1.3408 1.1297 0.1201 0.0162 0.2358 31 VAL D CB 4096 C CG1 . VAL D 31 ? 1.0308 1.3335 1.1193 0.1029 0.0258 0.2177 31 VAL D CG1 4097 C CG2 . VAL D 31 ? 1.1105 1.3805 1.1932 0.1169 0.0146 0.2492 31 VAL D CG2 4098 N N . PHE D 32 ? 0.6905 1.0476 0.7665 0.1559 0.0012 0.2594 32 PHE D N 4099 C CA . PHE D 32 ? 0.7058 1.0531 0.7738 0.1729 -0.0080 0.2773 32 PHE D CA 4100 C C . PHE D 32 ? 0.9366 1.3252 1.0025 0.1888 -0.0112 0.2743 32 PHE D C 4101 O O . PHE D 32 ? 1.0748 1.4591 1.1328 0.2056 -0.0193 0.2890 32 PHE D O 4102 C CB . PHE D 32 ? 0.7782 1.1195 0.8454 0.1690 -0.0097 0.2914 32 PHE D CB 4103 C CG . PHE D 32 ? 1.0967 1.3892 1.1616 0.1611 -0.0109 0.3019 32 PHE D CG 4104 C CD1 . PHE D 32 ? 1.1193 1.3746 1.1753 0.1704 -0.0188 0.3184 32 PHE D CD1 4105 C CD2 . PHE D 32 ? 1.1407 1.4241 1.2120 0.1443 -0.0038 0.2942 32 PHE D CD2 4106 C CE1 . PHE D 32 ? 0.9828 1.1971 1.0368 0.1619 -0.0197 0.3271 32 PHE D CE1 4107 C CE2 . PHE D 32 ? 0.9658 1.2088 1.0352 0.1376 -0.0048 0.3034 32 PHE D CE2 4108 C CZ . PHE D 32 ? 1.0033 1.2134 1.0645 0.1458 -0.0126 0.3196 32 PHE D CZ 4109 N N . CYS D 33 ? 0.9437 1.3739 1.0159 0.1833 -0.0050 0.2559 33 CYS D N 4110 C CA . CYS D 33 ? 0.9816 1.4588 1.0526 0.1978 -0.0074 0.2518 33 CYS D CA 4111 C C . CYS D 33 ? 0.9539 1.4161 1.0155 0.2205 -0.0167 0.2633 33 CYS D C 4112 O O . CYS D 33 ? 0.9974 1.4734 1.0531 0.2367 -0.0229 0.2752 33 CYS D O 4113 C CB . CYS D 33 ? 0.8257 1.3416 0.9036 0.1878 0.0003 0.2285 33 CYS D CB 4114 S SG . CYS D 33 ? 1.6221 2.1604 1.7094 0.1630 0.0108 0.2135 33 CYS D SG 4115 N N . SER D 34 ? 0.9943 1.4266 1.0538 0.2217 -0.0174 0.2597 34 SER D N 4116 C CA . SER D 34 ? 1.0030 1.4128 1.0529 0.2427 -0.0261 0.2694 34 SER D CA 4117 C C . SER D 34 ? 1.0993 1.4753 1.1400 0.2525 -0.0341 0.2921 34 SER D C 4118 O O . SER D 34 ? 0.9370 1.3194 0.9693 0.2726 -0.0414 0.3025 34 SER D O 4119 C CB . SER D 34 ? 0.7777 1.1508 0.8271 0.2383 -0.0254 0.2636 34 SER D CB 4120 O OG . SER D 34 ? 0.6901 1.0787 0.7488 0.2186 -0.0160 0.2461 34 SER D OG 4121 N N . SER D 35 ? 1.3825 1.7248 1.4246 0.2375 -0.0325 0.3001 35 SER D N 4122 C CA . SER D 35 ? 1.4075 1.7091 1.4400 0.2436 -0.0400 0.3214 35 SER D CA 4123 C C . SER D 35 ? 1.3028 1.6249 1.3316 0.2500 -0.0436 0.3352 35 SER D C 4124 O O . SER D 35 ? 1.2905 1.5967 1.3081 0.2665 -0.0519 0.3508 35 SER D O 4125 C CB . SER D 35 ? 1.3676 1.6290 1.4028 0.2249 -0.0370 0.3252 35 SER D CB 4126 O OG . SER D 35 ? 1.2736 1.5586 1.3194 0.2068 -0.0284 0.3149 35 SER D OG 4127 N N . ARG D 36 ? 1.3072 1.6633 1.3446 0.2372 -0.0374 0.3297 36 ARG D N 4128 C CA . ARG D 36 ? 1.3776 1.7557 1.4119 0.2419 -0.0405 0.3432 36 ARG D CA 4129 C C . ARG D 36 ? 1.3675 1.8056 1.4111 0.2366 -0.0341 0.3295 36 ARG D C 4130 O O . ARG D 36 ? 1.5213 1.9704 1.5733 0.2191 -0.0274 0.3223 36 ARG D O 4131 C CB . ARG D 36 ? 1.3496 1.6958 1.3823 0.2290 -0.0412 0.3577 36 ARG D CB 4132 C CG . ARG D 36 ? 1.2720 1.6136 1.3153 0.2075 -0.0326 0.3451 36 ARG D CG 4133 C CD . ARG D 36 ? 1.3092 1.6069 1.3491 0.1979 -0.0346 0.3586 36 ARG D CD 4134 N NE . ARG D 36 ? 1.2215 1.5188 1.2711 0.1790 -0.0266 0.3478 36 ARG D NE 4135 C CZ . ARG D 36 ? 1.0363 1.2951 1.0851 0.1689 -0.0264 0.3538 36 ARG D CZ 4136 N NH1 . ARG D 36 ? 1.0189 1.2378 1.0580 0.1749 -0.0337 0.3690 36 ARG D NH1 4137 N NH2 . ARG D 36 ? 0.8965 1.1563 0.9534 0.1536 -0.0192 0.3441 36 ARG D NH2 4138 N N . GLY D 37 ? 1.1810 1.6590 1.2227 0.2522 -0.0363 0.3264 37 GLY D N 4139 C CA . GLY D 37 ? 1.0538 1.5910 1.1047 0.2463 -0.0297 0.3101 37 GLY D CA 4140 C C . GLY D 37 ? 1.0007 1.5471 1.0633 0.2237 -0.0194 0.2889 37 GLY D C 4141 O O . GLY D 37 ? 0.9216 1.4322 0.9863 0.2133 -0.0164 0.2828 37 GLY D O 4142 N N . LYS D 38 ? 1.0727 1.6666 1.1425 0.2154 -0.0139 0.2783 38 LYS D N 4143 C CA . LYS D 38 ? 1.0649 1.6715 1.1446 0.1939 -0.0040 0.2584 38 LYS D CA 4144 C C . LYS D 38 ? 1.1174 1.7295 1.2008 0.1822 -0.0012 0.2623 38 LYS D C 4145 O O . LYS D 38 ? 0.8604 1.4751 0.9392 0.1907 -0.0068 0.2799 38 LYS D O 4146 C CB . LYS D 38 ? 1.1668 1.8287 1.2512 0.1941 0.0003 0.2391 38 LYS D CB 4147 C CG . LYS D 38 ? 1.1794 1.8553 1.2720 0.1735 0.0100 0.2171 38 LYS D CG 4148 C CD . LYS D 38 ? 1.4716 2.1771 1.5654 0.1762 0.0119 0.2020 38 LYS D CD 4149 C CE . LYS D 38 ? 1.5164 2.2333 1.6172 0.1535 0.0217 0.1807 38 LYS D CE 4150 N NZ . LYS D 38 ? 1.6442 2.4039 1.7493 0.1470 0.0251 0.1752 38 LYS D NZ 4151 N N . VAL D 39 ? 1.1970 1.8082 1.2878 0.1629 0.0071 0.2468 39 VAL D N 4152 C CA . VAL D 39 ? 1.1768 1.7892 1.2703 0.1539 0.0090 0.2515 39 VAL D CA 4153 C C . VAL D 39 ? 1.0999 1.7673 1.1995 0.1473 0.0144 0.2368 39 VAL D C 4154 O O . VAL D 39 ? 0.8762 1.5648 0.9807 0.1377 0.0210 0.2160 39 VAL D O 4155 C CB . VAL D 39 ? 1.2232 1.7942 1.3196 0.1379 0.0139 0.2471 39 VAL D CB 4156 C CG1 . VAL D 39 ? 1.3283 1.8979 1.4249 0.1347 0.0128 0.2588 39 VAL D CG1 4157 C CG2 . VAL D 39 ? 1.2024 1.7221 1.2944 0.1407 0.0109 0.2541 39 VAL D CG2 4158 N N . VAL D 40 ? 1.2184 1.9046 1.3171 0.1512 0.0114 0.2486 40 VAL D N 4159 C CA . VAL D 40 ? 1.0519 1.7939 1.1547 0.1498 0.0138 0.2418 40 VAL D CA 4160 C C . VAL D 40 ? 0.7762 1.5168 0.8835 0.1360 0.0185 0.2377 40 VAL D C 4161 O O . VAL D 40 ? 0.7397 1.4552 0.8442 0.1372 0.0148 0.2543 40 VAL D O 4162 C CB . VAL D 40 ? 1.1204 1.8834 1.2167 0.1679 0.0054 0.2626 40 VAL D CB 4163 C CG1 . VAL D 40 ? 1.2667 2.0941 1.3671 0.1681 0.0077 0.2543 40 VAL D CG1 4164 C CG2 . VAL D 40 ? 1.1360 1.8888 1.2255 0.1848 -0.0008 0.2703 40 VAL D CG2 4165 N N . GLU D 41 ? 0.7408 1.5126 0.8549 0.1236 0.0262 0.2157 41 GLU D N 4166 C CA . GLU D 41 ? 0.5421 1.3194 0.6605 0.1119 0.0309 0.2087 41 GLU D CA 4167 C C . GLU D 41 ? 0.7375 1.5783 0.8586 0.1147 0.0312 0.2044 41 GLU D C 4168 O O . GLU D 41 ? 0.6291 1.5108 0.7527 0.1144 0.0339 0.1900 41 GLU D O 4169 C CB . GLU D 41 ? 0.5381 1.2968 0.6607 0.0952 0.0396 0.1861 41 GLU D CB 4170 C CG . GLU D 41 ? 0.6087 1.3919 0.7363 0.0831 0.0462 0.1696 41 GLU D CG 4171 C CD . GLU D 41 ? 0.7929 1.5450 0.9223 0.0674 0.0541 0.1502 41 GLU D CD 4172 O OE1 . GLU D 41 ? 0.8018 1.5027 0.9284 0.0665 0.0533 0.1572 41 GLU D OE1 4173 O OE2 . GLU D 41 ? 0.7740 1.5522 0.9068 0.0557 0.0611 0.1281 41 GLU D OE2 4174 N N . LEU D 42 ? 0.7264 1.5778 0.8466 0.1187 0.0277 0.2190 42 LEU D N 4175 C CA . LEU D 42 ? 0.5994 1.5114 0.7219 0.1216 0.0276 0.2169 42 LEU D CA 4176 C C . LEU D 42 ? 0.6776 1.6040 0.8055 0.1093 0.0333 0.2047 42 LEU D C 4177 O O . LEU D 42 ? 0.8759 1.7715 1.0030 0.1062 0.0325 0.2140 42 LEU D O 4178 C CB . LEU D 42 ? 0.5462 1.4660 0.6621 0.1372 0.0185 0.2450 42 LEU D CB 4179 C CG . LEU D 42 ? 0.6320 1.5331 0.7398 0.1536 0.0105 0.2641 42 LEU D CG 4180 C CD1 . LEU D 42 ? 0.5686 1.4644 0.6689 0.1642 0.0023 0.2928 42 LEU D CD1 4181 C CD2 . LEU D 42 ? 0.6624 1.6124 0.7706 0.1627 0.0104 0.2551 42 LEU D CD2 4182 N N . GLY D 43 ? 0.6740 1.6512 0.8070 0.1033 0.0384 0.1852 43 GLY D N 4183 C CA . GLY D 43 ? 0.6458 1.6416 0.7832 0.0941 0.0429 0.1746 43 GLY D CA 4184 C C . GLY D 43 ? 0.6849 1.7456 0.8273 0.0895 0.0474 0.1546 43 GLY D C 4185 O O . GLY D 43 ? 0.5525 1.6549 0.6946 0.0965 0.0454 0.1547 43 GLY D O 4186 N N . CYS D 44 ? 0.8322 1.8986 0.9787 0.0774 0.0538 0.1359 44 CYS D N 4187 C CA . CYS D 44 ? 0.5163 1.6385 0.6677 0.0702 0.0591 0.1140 44 CYS D CA 4188 C C . CYS D 44 ? 0.6707 1.7806 0.8241 0.0547 0.0675 0.0849 44 CYS D C 4189 O O . CYS D 44 ? 1.0841 2.1391 1.2355 0.0489 0.0697 0.0823 44 CYS D O 4190 C CB . CYS D 44 ? 0.5842 1.7174 0.7378 0.0677 0.0602 0.1130 44 CYS D CB 4191 S SG . CYS D 44 ? 0.6746 1.8342 0.8261 0.0818 0.0514 0.1446 44 CYS D SG 4192 N N . ALA D 45 ? 0.6438 1.8049 0.8006 0.0471 0.0723 0.0630 45 ALA D N 4193 C CA . ALA D 45 ? 0.7701 1.9226 0.9281 0.0295 0.0810 0.0332 45 ALA D CA 4194 C C . ALA D 45 ? 0.9529 2.1701 1.1147 0.0213 0.0858 0.0101 45 ALA D C 4195 O O . ALA D 45 ? 0.8509 2.1253 1.0145 0.0301 0.0821 0.0168 45 ALA D O 4196 C CB . ALA D 45 ? 0.8345 1.9666 0.9902 0.0267 0.0816 0.0312 45 ALA D CB 4197 N N . ALA D 46 ? 1.0812 2.2894 1.2437 0.0046 0.0938 -0.0171 46 ALA D N 4198 C CA . ALA D 46 ? 1.2068 2.4742 1.3724 -0.0053 0.0989 -0.0420 46 ALA D CA 4199 C C . ALA D 46 ? 1.1430 2.4404 1.3087 -0.0128 0.1013 -0.0543 46 ALA D C 4200 O O . ALA D 46 ? 0.9313 2.2940 1.0998 -0.0096 0.1002 -0.0577 46 ALA D O 4201 C CB . ALA D 46 ? 1.2277 2.4737 1.3927 -0.0204 0.1065 -0.0676 46 ALA D CB 4202 N N . THR D 47 ? 1.2937 2.5460 1.4561 -0.0229 0.1047 -0.0612 47 THR D N 4203 C CA . THR D 47 ? 1.3181 2.5977 1.4803 -0.0294 0.1064 -0.0708 47 THR D CA 4204 C C . THR D 47 ? 1.1226 2.3679 1.2822 -0.0185 0.1011 -0.0492 47 THR D C 4205 O O . THR D 47 ? 0.8420 2.0248 0.9988 -0.0152 0.0994 -0.0362 47 THR D O 4206 C CB . THR D 47 ? 1.4682 2.7373 1.6284 -0.0547 0.1161 -0.1027 47 THR D CB 4207 O OG1 . THR D 47 ? 1.4804 2.6734 1.6361 -0.0617 0.1186 -0.1019 47 THR D OG1 4208 C CG2 . THR D 47 ? 1.4851 2.7860 1.6471 -0.0653 0.1213 -0.1254 47 THR D CG2 4209 N N . CYS D 48 ? 1.2032 2.4914 1.3634 -0.0124 0.0985 -0.0462 48 CYS D N 4210 C CA . CYS D 48 ? 1.2584 2.5204 1.4160 0.0008 0.0927 -0.0256 48 CYS D CA 4211 C C . CYS D 48 ? 1.2675 2.4657 1.4218 -0.0118 0.0967 -0.0317 48 CYS D C 4212 O O . CYS D 48 ? 1.2752 2.4773 1.4288 -0.0311 0.1038 -0.0547 48 CYS D O 4213 C CB . CYS D 48 ? 1.2244 2.5448 1.3827 0.0078 0.0903 -0.0264 48 CYS D CB 4214 S SG . CYS D 48 ? 2.0626 3.4267 2.2211 0.0369 0.0799 0.0019 48 CYS D SG 4215 N N . PRO D 49 ? 1.0563 2.1960 1.2080 -0.0017 0.0923 -0.0107 49 PRO D N 4216 C CA . PRO D 49 ? 0.9788 2.0557 1.1270 -0.0117 0.0954 -0.0133 49 PRO D CA 4217 C C . PRO D 49 ? 0.9484 2.0377 1.0953 -0.0173 0.0970 -0.0212 49 PRO D C 4218 O O . PRO D 49 ? 0.9423 2.0679 1.0899 -0.0026 0.0915 -0.0105 49 PRO D O 4219 C CB . PRO D 49 ? 0.8928 1.9225 1.0390 0.0056 0.0880 0.0150 49 PRO D CB 4220 C CG . PRO D 49 ? 0.8723 1.9453 1.0198 0.0259 0.0801 0.0339 49 PRO D CG 4221 C CD . PRO D 49 ? 0.8451 1.9763 0.9964 0.0195 0.0837 0.0176 49 PRO D CD 4222 N N . SER D 50 ? 0.9750 2.0411 1.1197 -0.0385 0.1045 -0.0409 50 SER D N 4223 C CA . SER D 50 ? 0.9230 1.9917 1.0657 -0.0458 0.1063 -0.0473 50 SER D CA 4224 C C . SER D 50 ? 1.1104 2.1387 1.2508 -0.0305 0.1000 -0.0249 50 SER D C 4225 O O . SER D 50 ? 1.0840 2.0871 1.2243 -0.0133 0.0937 -0.0034 50 SER D O 4226 C CB . SER D 50 ? 0.9541 1.9943 1.0934 -0.0725 0.1156 -0.0701 50 SER D CB 4227 O OG . SER D 50 ? 1.0428 2.0974 1.1804 -0.0817 0.1178 -0.0782 50 SER D OG 4228 N N . LYS D 51 ? 1.3875 2.4058 1.5255 -0.0380 0.1020 -0.0303 51 LYS D N 4229 C CA . LYS D 51 ? 1.6033 2.5786 1.7389 -0.0249 0.0966 -0.0108 51 LYS D CA 4230 C C . LYS D 51 ? 1.7288 2.6824 1.8613 -0.0391 0.1009 -0.0202 51 LYS D C 4231 O O . LYS D 51 ? 1.7683 2.7521 1.9004 -0.0577 0.1073 -0.0411 51 LYS D O 4232 C CB . LYS D 51 ? 1.6821 2.6931 1.8188 -0.0001 0.0878 0.0063 51 LYS D CB 4233 C CG . LYS D 51 ? 1.7443 2.8105 1.8840 0.0127 0.0841 0.0104 51 LYS D CG 4234 C CD . LYS D 51 ? 1.8876 2.9591 2.0255 0.0375 0.0751 0.0317 51 LYS D CD 4235 C CE . LYS D 51 ? 1.9153 2.9167 2.0508 0.0424 0.0720 0.0495 51 LYS D CE 4236 N NZ . LYS D 51 ? 1.9700 2.9426 2.1042 0.0573 0.0656 0.0722 51 LYS D NZ 4237 N N . LYS D 52 ? 1.8243 2.7268 1.9541 -0.0310 0.0973 -0.0046 52 LYS D N 4238 C CA . LYS D 52 ? 1.8667 2.7433 1.9931 -0.0431 0.1007 -0.0106 52 LYS D CA 4239 C C . LYS D 52 ? 1.9684 2.8367 2.0940 -0.0214 0.0926 0.0086 52 LYS D C 4240 O O . LYS D 52 ? 1.9463 2.8586 2.0737 -0.0043 0.0870 0.0148 52 LYS D O 4241 C CB . LYS D 52 ? 1.8742 2.6872 1.9969 -0.0599 0.1064 -0.0146 52 LYS D CB 4242 C CG . LYS D 52 ? 1.8046 2.5862 1.9231 -0.0719 0.1096 -0.0179 52 LYS D CG 4243 C CD . LYS D 52 ? 1.7883 2.5510 1.9027 -0.1000 0.1193 -0.0377 52 LYS D CD 4244 C CE . LYS D 52 ? 1.7285 2.4847 1.8389 -0.1141 0.1228 -0.0443 52 LYS D CE 4245 N NZ . LYS D 52 ? 1.7241 2.4846 1.8299 -0.1443 0.1325 -0.0674 52 LYS D NZ 4246 N N . PRO D 53 ? 2.1267 2.9384 2.2492 -0.0198 0.0912 0.0193 53 PRO D N 4247 C CA . PRO D 53 ? 2.1723 2.9831 2.2930 -0.0111 0.0875 0.0252 53 PRO D CA 4248 C C . PRO D 53 ? 2.1523 2.9977 2.2741 0.0150 0.0788 0.0383 53 PRO D C 4249 O O . PRO D 53 ? 2.2460 3.1412 2.3685 0.0192 0.0780 0.0311 53 PRO D O 4250 C CB . PRO D 53 ? 2.1731 2.9145 2.2908 -0.0102 0.0863 0.0380 53 PRO D CB 4251 C CG . PRO D 53 ? 2.1781 2.8903 2.2966 -0.0085 0.0859 0.0458 53 PRO D CG 4252 C CD . PRO D 53 ? 2.2081 2.9700 2.3300 -0.0096 0.0873 0.0369 53 PRO D CD 4253 N N . TYR D 54 ? 1.6416 2.4594 1.7628 0.0321 0.0722 0.0577 54 TYR D N 4254 C CA . TYR D 54 ? 1.3117 2.1469 1.4319 0.0578 0.0632 0.0739 54 TYR D CA 4255 C C . TYR D 54 ? 1.2026 2.0450 1.3243 0.0640 0.0609 0.0825 54 TYR D C 4256 O O . TYR D 54 ? 1.1694 1.9699 1.2897 0.0705 0.0573 0.0983 54 TYR D O 4257 C CB . TYR D 54 ? 1.2250 2.0117 1.3413 0.0719 0.0569 0.0912 54 TYR D CB 4258 C CG . TYR D 54 ? 1.3426 2.1444 1.4561 0.0994 0.0472 0.1082 54 TYR D CG 4259 C CD1 . TYR D 54 ? 1.3985 2.2099 1.5118 0.1111 0.0426 0.1209 54 TYR D CD1 4260 C CD2 . TYR D 54 ? 1.4269 2.2337 1.5372 0.1139 0.0424 0.1115 54 TYR D CD2 4261 C CE1 . TYR D 54 ? 1.4826 2.3068 1.5920 0.1350 0.0341 0.1364 54 TYR D CE1 4262 C CE2 . TYR D 54 ? 1.5281 2.3447 1.6344 0.1400 0.0333 0.1270 54 TYR D CE2 4263 C CZ . TYR D 54 ? 1.6140 2.4373 1.7195 0.1505 0.0291 0.1403 54 TYR D CZ 4264 O OH . TYR D 54 ? 1.7190 2.5495 1.8189 0.1766 0.0198 0.1573 54 TYR D OH 4265 N N . GLU D 55 ? 1.3205 2.2153 1.4454 0.0595 0.0638 0.0712 55 GLU D N 4266 C CA . GLU D 55 ? 1.4554 2.3529 1.5814 0.0670 0.0608 0.0820 55 GLU D CA 4267 C C . GLU D 55 ? 1.0980 2.0587 1.2248 0.0831 0.0562 0.0855 55 GLU D C 4268 O O . GLU D 55 ? 1.1135 2.1228 1.2410 0.0847 0.0570 0.0747 55 GLU D O 4269 C CB . GLU D 55 ? 1.5183 2.4047 1.6470 0.0459 0.0686 0.0683 55 GLU D CB 4270 C CG . GLU D 55 ? 1.4366 2.2681 1.5641 0.0277 0.0746 0.0610 55 GLU D CG 4271 C CD . GLU D 55 ? 1.4167 2.2418 1.5460 0.0128 0.0806 0.0503 55 GLU D CD 4272 O OE1 . GLU D 55 ? 1.2815 2.1183 1.4124 0.0220 0.0773 0.0593 55 GLU D OE1 4273 O OE2 . GLU D 55 ? 1.4716 2.2842 1.6003 -0.0079 0.0886 0.0320 55 GLU D OE2 4274 N N . GLU D 56 ? 1.0652 2.0258 1.1915 0.0949 0.0513 0.1012 56 GLU D N 4275 C CA . GLU D 56 ? 1.0049 2.0173 1.1305 0.1132 0.0455 0.1100 56 GLU D CA 4276 C C . GLU D 56 ? 0.8966 1.9423 1.0250 0.1121 0.0461 0.1109 56 GLU D C 4277 O O . GLU D 56 ? 0.8288 1.8827 0.9544 0.1296 0.0391 0.1303 56 GLU D O 4278 C CB . GLU D 56 ? 0.9900 1.9731 1.1091 0.1376 0.0355 0.1355 56 GLU D CB 4279 C CG . GLU D 56 ? 1.0126 1.9800 1.1287 0.1435 0.0339 0.1334 56 GLU D CG 4280 C CD . GLU D 56 ? 1.0507 2.0247 1.1602 0.1719 0.0240 0.1514 56 GLU D CD 4281 O OE1 . GLU D 56 ? 1.1460 2.1151 1.2513 0.1877 0.0173 0.1712 56 GLU D OE1 4282 O OE2 . GLU D 56 ? 0.8619 1.8504 0.9698 0.1789 0.0231 0.1451 56 GLU D OE2 4283 N N . VAL D 57 ? 0.8068 1.8690 0.9400 0.0910 0.0545 0.0898 57 VAL D N 4284 C CA . VAL D 57 ? 0.8625 1.9694 0.9991 0.0883 0.0561 0.0846 57 VAL D CA 4285 C C . VAL D 57 ? 0.7553 1.9259 0.8916 0.1044 0.0515 0.0897 57 VAL D C 4286 O O . VAL D 57 ? 0.5971 1.8064 0.7334 0.1083 0.0516 0.0814 57 VAL D O 4287 C CB . VAL D 57 ? 1.1452 2.2741 1.2865 0.0627 0.0665 0.0554 57 VAL D CB 4288 C CG1 . VAL D 57 ? 1.0163 2.2089 1.1609 0.0630 0.0674 0.0478 57 VAL D CG1 4289 C CG2 . VAL D 57 ? 0.9584 2.0318 1.0999 0.0478 0.0711 0.0515 57 VAL D CG2 4290 N N . THR D 58 ? 0.6216 1.8018 0.7573 0.1148 0.0471 0.1052 58 THR D N 4291 C CA . THR D 58 ? 0.6650 1.9062 0.8001 0.1300 0.0427 0.1121 58 THR D CA 4292 C C . THR D 58 ? 0.8619 2.1156 1.0006 0.1210 0.0453 0.1099 58 THR D C 4293 O O . THR D 58 ? 0.9458 2.1550 1.0831 0.1210 0.0434 0.1233 58 THR D O 4294 C CB . THR D 58 ? 0.5713 1.7987 0.6991 0.1567 0.0322 0.1404 58 THR D CB 4295 O OG1 . THR D 58 ? 0.6933 1.8531 0.8177 0.1577 0.0290 0.1580 58 THR D OG1 4296 C CG2 . THR D 58 ? 0.7057 1.9337 0.8307 0.1655 0.0304 0.1373 58 THR D CG2 4297 N N . CYS D 59 ? 0.8479 2.1626 0.9915 0.1117 0.0504 0.0907 59 CYS D N 4298 C CA . CYS D 59 ? 0.8215 2.1576 0.9687 0.1036 0.0532 0.0857 59 CYS D CA 4299 C C . CYS D 59 ? 0.8955 2.2960 1.0423 0.1196 0.0481 0.0970 59 CYS D C 4300 O O . CYS D 59 ? 0.8117 2.2526 0.9567 0.1320 0.0449 0.0992 59 CYS D O 4301 C CB . CYS D 59 ? 0.7515 2.1078 0.9043 0.0788 0.0635 0.0530 59 CYS D CB 4302 S SG . CYS D 59 ? 1.0184 2.3062 1.1709 0.0570 0.0709 0.0359 59 CYS D SG 4303 N N . CYS D 60 ? 0.9313 2.3465 1.0796 0.1190 0.0476 0.1024 60 CYS D N 4304 C CA . CYS D 60 ? 0.7905 2.2611 0.9340 0.1318 0.0423 0.1116 60 CYS D CA 4305 C C . CYS D 60 ? 0.7359 2.2176 0.8776 0.1218 0.0437 0.1056 60 CYS D C 4306 O O . CYS D 60 ? 0.7300 2.1877 0.8799 0.1073 0.0499 0.0946 60 CYS D O 4307 C CB . CYS D 60 ? 0.7707 2.2358 0.9105 0.1577 0.0328 0.1453 60 CYS D CB 4308 S SG . CYS D 60 ? 0.9646 2.3422 1.0986 0.1620 0.0276 0.1712 60 CYS D SG 4309 N N . SER D 61 ? 0.8708 2.3910 1.0008 0.1291 0.0384 0.1103 61 SER D N 4310 C CA . SER D 61 ? 0.9841 2.5246 1.1104 0.1178 0.0396 0.0977 61 SER D CA 4311 C C . SER D 61 ? 0.8972 2.4497 1.0171 0.1312 0.0338 0.1238 61 SER D C 4312 O O . SER D 61 ? 1.0148 2.5865 1.1307 0.1244 0.0338 0.1169 61 SER D O 4313 C CB . SER D 61 ? 1.0435 2.6280 1.1599 0.1099 0.0391 0.0735 61 SER D CB 4314 O OG . SER D 61 ? 1.0105 2.5918 1.1295 0.1011 0.0427 0.0543 61 SER D OG 4315 N N . THR D 62 ? 0.7587 2.3026 0.8764 0.1506 0.0285 0.1530 62 THR D N 4316 C CA . THR D 62 ? 0.7206 2.2720 0.8308 0.1653 0.0228 0.1828 62 THR D CA 4317 C C . THR D 62 ? 0.8599 2.3716 0.9795 0.1675 0.0206 0.2055 62 THR D C 4318 O O . THR D 62 ? 0.8246 2.2990 0.9570 0.1635 0.0222 0.2040 62 THR D O 4319 C CB . THR D 62 ? 0.7047 2.2693 0.8044 0.1857 0.0182 0.2004 62 THR D CB 4320 O OG1 . THR D 62 ? 0.7255 2.3402 0.8107 0.1866 0.0187 0.1907 62 THR D OG1 4321 C CG2 . THR D 62 ? 0.7158 2.2559 0.8121 0.2031 0.0122 0.2368 62 THR D CG2 4322 N N . ASP D 63 ? 0.9218 2.4424 1.0346 0.1729 0.0170 0.2264 63 ASP D N 4323 C CA . ASP D 63 ? 0.8689 2.3517 0.9868 0.1769 0.0122 0.2529 63 ASP D CA 4324 C C . ASP D 63 ? 0.7947 2.2350 0.9103 0.1921 0.0043 0.2771 63 ASP D C 4325 O O . ASP D 63 ? 0.8791 2.3234 0.9817 0.2069 0.0009 0.2920 63 ASP D O 4326 C CB . ASP D 63 ? 0.5601 2.0610 0.6674 0.1799 0.0100 0.2725 63 ASP D CB 4327 C CG . ASP D 63 ? 0.6387 2.1531 0.7505 0.1642 0.0144 0.2575 63 ASP D CG 4328 O OD1 . ASP D 63 ? 0.5385 2.0389 0.6613 0.1516 0.0193 0.2339 63 ASP D OD1 4329 O OD2 . ASP D 63 ? 0.9264 2.4623 1.0297 0.1644 0.0137 0.2692 63 ASP D OD2 4330 N N . LYS D 64 ? 0.6101 1.9852 0.7270 0.1852 0.0047 0.2779 64 LYS D N 4331 C CA . LYS D 64 ? 0.5649 1.8785 0.6721 0.1962 -0.0023 0.3015 64 LYS D CA 4332 C C . LYS D 64 ? 0.7825 2.1023 0.8877 0.2074 -0.0034 0.2949 64 LYS D C 4333 O O . LYS D 64 ? 0.7714 2.0833 0.8669 0.2256 -0.0110 0.3165 64 LYS D O 4334 C CB . LYS D 64 ? 0.9460 2.2574 1.0425 0.2090 -0.0114 0.3365 64 LYS D CB 4335 C CG . LYS D 64 ? 0.8126 2.0969 0.9076 0.1992 -0.0127 0.3516 64 LYS D CG 4336 C CD . LYS D 64 ? 1.1954 2.4413 1.2755 0.2087 -0.0190 0.3853 64 LYS D CD 4337 C CE . LYS D 64 ? 1.3677 2.5480 1.4401 0.2176 -0.0242 0.3962 64 LYS D CE 4338 N NZ . LYS D 64 ? 1.2624 2.3786 1.3229 0.2204 -0.0287 0.4224 64 LYS D NZ 4339 N N . CYS D 65 ? 0.8319 2.1725 0.9459 0.1969 0.0044 0.2646 65 CYS D N 4340 C CA . CYS D 65 ? 0.9755 2.3353 1.0888 0.2057 0.0044 0.2545 65 CYS D CA 4341 C C . CYS D 65 ? 1.0051 2.3049 1.1175 0.2028 0.0055 0.2486 65 CYS D C 4342 O O . CYS D 65 ? 0.9403 2.2491 1.0509 0.2119 0.0045 0.2434 65 CYS D O 4343 C CB . CYS D 65 ? 0.9571 2.3854 1.0796 0.1958 0.0120 0.2250 65 CYS D CB 4344 S SG . CYS D 65 ? 0.9619 2.3831 1.0956 0.1672 0.0240 0.1884 65 CYS D SG 4345 N N . ASN D 66 ? 0.9415 2.1841 1.0552 0.1903 0.0077 0.2490 66 ASN D N 4346 C CA . ASN D 66 ? 0.6807 1.8605 0.7931 0.1867 0.0084 0.2463 66 ASN D CA 4347 C C . ASN D 66 ? 0.7039 1.8207 0.8079 0.1938 0.0014 0.2734 66 ASN D C 4348 O O . ASN D 66 ? 0.7245 1.7962 0.8303 0.1818 0.0038 0.2729 66 ASN D O 4349 C CB . ASN D 66 ? 0.6564 1.8206 0.7774 0.1643 0.0180 0.2198 66 ASN D CB 4350 C CG . ASN D 66 ? 0.6685 1.8272 0.7928 0.1530 0.0205 0.2204 66 ASN D CG 4351 O OD1 . ASN D 66 ? 0.7695 1.9731 0.8946 0.1557 0.0193 0.2252 66 ASN D OD1 4352 N ND2 . ASN D 66 ? 0.5469 1.6515 0.6726 0.1416 0.0235 0.2169 66 ASN D ND2 4353 N N . PRO D 67 ? 0.7080 1.8208 0.8021 0.2134 -0.0073 0.2972 67 PRO D N 4354 C CA . PRO D 67 ? 0.7887 1.8365 0.8747 0.2168 -0.0132 0.3204 67 PRO D CA 4355 C C . PRO D 67 ? 1.0952 2.0901 1.1795 0.2172 -0.0132 0.3157 67 PRO D C 4356 O O . PRO D 67 ? 1.2355 2.2440 1.3217 0.2215 -0.0114 0.3014 67 PRO D O 4357 C CB . PRO D 67 ? 0.8679 1.9265 0.9424 0.2371 -0.0227 0.3480 67 PRO D CB 4358 C CG . PRO D 67 ? 0.8149 1.9305 0.8905 0.2492 -0.0225 0.3378 67 PRO D CG 4359 C CD . PRO D 67 ? 0.7515 1.9128 0.8403 0.2323 -0.0126 0.3071 67 PRO D CD 4360 N N . HIS D 68 ? 1.1448 2.0807 1.2258 0.2115 -0.0151 0.3275 68 HIS D N 4361 C CA . HIS D 68 ? 1.0148 1.8941 1.0916 0.2145 -0.0172 0.3299 68 HIS D CA 4362 C C . HIS D 68 ? 1.1408 2.0235 1.2078 0.2370 -0.0249 0.3432 68 HIS D C 4363 O O . HIS D 68 ? 1.2277 2.1434 1.2891 0.2498 -0.0300 0.3576 68 HIS D O 4364 C CB . HIS D 68 ? 1.0590 1.8811 1.1315 0.2075 -0.0200 0.3467 68 HIS D CB 4365 C CG . HIS D 68 ? 1.1311 1.8917 1.1981 0.2107 -0.0231 0.3523 68 HIS D CG 4366 N ND1 . HIS D 68 ? 1.1940 1.9238 1.2487 0.2267 -0.0320 0.3741 68 HIS D ND1 4367 C CD2 . HIS D 68 ? 0.9234 1.6468 0.9948 0.2000 -0.0186 0.3392 68 HIS D CD2 4368 C CE1 . HIS D 68 ? 1.0554 1.7335 1.1077 0.2256 -0.0328 0.3731 68 HIS D CE1 4369 N NE2 . HIS D 68 ? 0.9990 1.6735 1.0616 0.2095 -0.0247 0.3524 68 HIS D NE2 4370 N N . PRO D 69 ? 1.0065 1.8582 1.0711 0.2430 -0.0260 0.3382 69 PRO D N 4371 C CA . PRO D 69 ? 0.9821 1.8312 1.0349 0.2669 -0.0349 0.3556 69 PRO D CA 4372 C C . PRO D 69 ? 1.2928 2.0992 1.3328 0.2747 -0.0436 0.3866 69 PRO D C 4373 O O . PRO D 69 ? 1.2836 2.0561 1.3121 0.2912 -0.0510 0.4011 69 PRO D O 4374 C CB . PRO D 69 ? 0.8354 1.6583 0.8881 0.2715 -0.0344 0.3438 69 PRO D CB 4375 C CG . PRO D 69 ? 0.7365 1.5902 0.8028 0.2529 -0.0239 0.3143 69 PRO D CG 4376 C CD . PRO D 69 ? 0.6678 1.5146 0.7402 0.2333 -0.0192 0.3134 69 PRO D CD 4377 N N . LYS D 70 ? 1.3419 2.1511 1.3838 0.2623 -0.0425 0.3953 70 LYS D N 4378 C CA . LYS D 70 ? 1.3638 2.1471 1.3943 0.2658 -0.0493 0.4231 70 LYS D CA 4379 C C . LYS D 70 ? 1.4219 2.2000 1.4406 0.2809 -0.0527 0.4328 70 LYS D C 4380 O O . LYS D 70 ? 0.9869 1.7117 0.9947 0.2894 -0.0572 0.4404 70 LYS D O 4381 C CB . LYS D 70 ? 1.5578 2.3712 1.5951 0.2501 -0.0457 0.4248 70 LYS D CB 4382 C CG . LYS D 70 ? 1.4609 2.3498 1.5058 0.2504 -0.0417 0.4133 70 LYS D CG 4383 C CD . LYS D 70 ? 1.3849 2.2924 1.4279 0.2439 -0.0418 0.4267 70 LYS D CD 4384 C CE . LYS D 70 ? 1.3802 2.3459 1.4233 0.2523 -0.0398 0.4233 70 LYS D CE 4385 N NZ . LYS D 70 ? 1.3402 2.3253 1.3832 0.2438 -0.0384 0.4337 70 LYS D NZ 4386 N N . GLN D 71 ? 1.8409 2.6751 1.8616 0.2848 -0.0505 0.4310 71 GLN D N 4387 C CA . GLN D 71 ? 2.1062 2.9446 2.1164 0.2998 -0.0532 0.4399 71 GLN D CA 4388 C C . GLN D 71 ? 2.2251 3.1297 2.2403 0.3109 -0.0499 0.4247 71 GLN D C 4389 O O . GLN D 71 ? 2.3094 3.2082 2.3177 0.3273 -0.0522 0.4228 71 GLN D O 4390 C CB . GLN D 71 ? 1.9606 2.8071 1.9671 0.2938 -0.0535 0.4553 71 GLN D CB 4391 C CG . GLN D 71 ? 1.8991 2.7030 1.9027 0.2777 -0.0552 0.4707 71 GLN D CG 4392 C CD . GLN D 71 ? 1.9971 2.7275 1.9947 0.2728 -0.0591 0.4761 71 GLN D CD 4393 O OE1 . GLN D 71 ? 2.0692 2.7675 2.0614 0.2836 -0.0620 0.4721 71 GLN D OE1 4394 N NE2 . GLN D 71 ? 1.9529 2.6560 1.9504 0.2566 -0.0594 0.4855 71 GLN D NE2 4395 N N . ARG D 72 ? 2.2547 3.2209 2.2814 0.3008 -0.0447 0.4138 72 ARG D N 4396 C CA . ARG D 72 ? 2.2555 3.2987 2.2901 0.3038 -0.0398 0.3959 72 ARG D CA 4397 C C . ARG D 72 ? 2.1136 3.1901 2.1494 0.2960 -0.0372 0.4038 72 ARG D C 4398 O O . ARG D 72 ? 2.1930 3.2320 2.2208 0.2953 -0.0403 0.4237 72 ARG D O 4399 C CB . ARG D 72 ? 2.1838 3.2476 2.2124 0.3234 -0.0402 0.3896 72 ARG D CB 4400 C CG . ARG D 72 ? 2.2554 3.2840 2.2801 0.3348 -0.0434 0.3843 72 ARG D CG 4401 C CD . ARG D 72 ? 2.0532 3.0641 2.0881 0.3213 -0.0428 0.3739 72 ARG D CD 4402 N NE . ARG D 72 ? 2.0886 3.0442 2.1170 0.3305 -0.0471 0.3767 72 ARG D NE 4403 C CZ . ARG D 72 ? 2.1209 3.0186 2.1481 0.3222 -0.0495 0.3850 72 ARG D CZ 4404 N NH1 . ARG D 72 ? 2.0847 2.9741 2.1151 0.3071 -0.0485 0.3931 72 ARG D NH1 4405 N NH2 . ARG D 72 ? 2.1995 3.0475 2.2209 0.3296 -0.0529 0.3864 72 ARG D NH2 4406 N N . PRO D 73 ? 1.9510 3.0985 1.9960 0.2905 -0.0316 0.3879 73 PRO D N 4407 C CA . PRO D 73 ? 1.7577 2.9367 1.8100 0.2748 -0.0282 0.3868 73 PRO D CA 4408 C C . PRO D 73 ? 1.5420 2.6903 1.5878 0.2708 -0.0305 0.4103 73 PRO D C 4409 O O . PRO D 73 ? 1.4806 2.6376 1.5196 0.2779 -0.0309 0.4233 73 PRO D O 4410 C CB . PRO D 73 ? 1.8272 3.0826 1.8837 0.2767 -0.0225 0.3715 73 PRO D CB 4411 C CG . PRO D 73 ? 1.8696 3.1308 1.9187 0.2951 -0.0233 0.3697 73 PRO D CG 4412 C CD . PRO D 73 ? 1.9000 3.1007 1.9449 0.3020 -0.0285 0.3742 73 PRO D CD 4413 C C1 . NAG E . ? 1.4279 1.1694 1.4281 -0.0125 -0.0310 0.2930 1214 NAG A C1 4414 C C2 . NAG E . ? 1.3524 1.0783 1.3478 -0.0086 -0.0369 0.2784 1214 NAG A C2 4415 C C3 . NAG E . ? 1.3955 1.1404 1.3922 -0.0051 -0.0350 0.2694 1214 NAG A C3 4416 C C4 . NAG E . ? 1.4262 1.1886 1.4290 0.0014 -0.0276 0.2734 1214 NAG A C4 4417 C C5 . NAG E . ? 1.2651 1.0389 1.2713 -0.0031 -0.0221 0.2881 1214 NAG A C5 4418 C C6 . NAG E . ? 1.1419 0.9280 1.1526 0.0022 -0.0147 0.2933 1214 NAG A C6 4419 C C7 . NAG E . ? 1.5522 1.2389 1.5340 -0.0144 -0.0503 0.2640 1214 NAG A C7 4420 C C8 . NAG E . ? 1.5015 1.1692 1.4751 -0.0258 -0.0568 0.2624 1214 NAG A C8 4421 N N2 . NAG E . ? 1.4462 1.1544 1.4345 -0.0170 -0.0438 0.2756 1214 NAG A N2 4422 O O3 . NAG E . ? 1.4672 1.1993 1.4595 0.0004 -0.0405 0.2549 1214 NAG A O3 4423 O O4 . NAG E . ? 1.5357 1.3174 1.5392 0.0037 -0.0259 0.2658 1214 NAG A O4 4424 O O5 . NAG E . ? 1.2254 0.9826 1.2309 -0.0055 -0.0241 0.2951 1214 NAG A O5 4425 O O6 . NAG E . ? 1.0247 0.8144 1.0376 0.0002 -0.0102 0.3065 1214 NAG A O6 4426 O O7 . NAG E . ? 1.6733 1.3560 1.6553 -0.0034 -0.0510 0.2548 1214 NAG A O7 4427 C C1 . NAG F . ? 1.4777 1.3721 1.4702 0.0896 0.0385 0.3526 1215 NAG A C1 4428 C C2 . NAG F . ? 1.5302 1.4458 1.5214 0.1012 0.0399 0.3624 1215 NAG A C2 4429 C C3 . NAG F . ? 1.5621 1.4692 1.5468 0.1056 0.0420 0.3640 1215 NAG A C3 4430 C C4 . NAG F . ? 1.6809 1.5841 1.6665 0.0934 0.0401 0.3607 1215 NAG A C4 4431 C C5 . NAG F . ? 1.5645 1.4507 1.5526 0.0817 0.0382 0.3512 1215 NAG A C5 4432 C C6 . NAG F . ? 1.4800 1.3689 1.4706 0.0706 0.0356 0.3491 1215 NAG A C6 4433 C C7 . NAG F . ? 1.4410 1.3870 1.4356 0.1182 0.0412 0.3722 1215 NAG A C7 4434 C C8 . NAG F . ? 1.4694 1.4169 1.4620 0.1325 0.0439 0.3746 1215 NAG A C8 4435 N N2 . NAG F . ? 1.4829 1.4015 1.4732 0.1134 0.0421 0.3652 1215 NAG A N2 4436 O O3 . NAG F . ? 1.3612 1.2920 1.3449 0.1166 0.0429 0.3737 1215 NAG A O3 4437 O O4 . NAG F . ? 1.9373 1.8266 1.9159 0.0964 0.0425 0.3608 1215 NAG A O4 4438 O O5 . NAG F . ? 1.5130 1.4072 1.5064 0.0796 0.0363 0.3505 1215 NAG A O5 4439 O O6 . NAG F . ? 1.3553 1.2516 1.3516 0.0624 0.0320 0.3474 1215 NAG A O6 4440 O O7 . NAG F . ? 1.3984 1.3679 1.3979 0.1109 0.0382 0.3766 1215 NAG A O7 4441 C C1 . NAG G . ? 1.6925 1.9898 1.7146 0.0268 -0.0461 0.4980 1214 NAG B C1 4442 C C2 . NAG G . ? 1.6333 1.9260 1.6472 0.0146 -0.0506 0.5089 1214 NAG B C2 4443 C C3 . NAG G . ? 1.4982 1.8425 1.5163 0.0136 -0.0503 0.5174 1214 NAG B C3 4444 C C4 . NAG G . ? 1.3991 1.7894 1.4301 0.0106 -0.0449 0.5134 1214 NAG B C4 4445 C C5 . NAG G . ? 1.3008 1.6829 1.3386 0.0183 -0.0402 0.5012 1214 NAG B C5 4446 C C6 . NAG G . ? 1.2165 1.5738 1.2556 0.0103 -0.0389 0.4962 1214 NAG B C6 4447 C C7 . NAG G . ? 1.8346 2.0499 1.8231 0.0039 -0.0598 0.5171 1214 NAG B C7 4448 C C8 . NAG G . ? 1.8680 2.0347 1.8385 0.0070 -0.0654 0.5209 1214 NAG B C8 4449 N N2 . NAG G . ? 1.7727 2.0187 1.7714 0.0155 -0.0563 0.5129 1214 NAG B N2 4450 O O3 . NAG G . ? 1.4051 1.7436 1.4141 0.0035 -0.0550 0.5291 1214 NAG B O3 4451 O O4 . NAG G . ? 1.3391 1.7821 1.3751 0.0144 -0.0435 0.5175 1214 NAG B O4 4452 O O5 . NAG G . ? 1.4308 1.7832 1.4646 0.0292 -0.0412 0.4968 1214 NAG B O5 4453 O O6 . NAG G . ? 1.2575 1.6098 1.3030 0.0171 -0.0341 0.4857 1214 NAG B O6 4454 O O7 . NAG G . ? 1.7482 1.9752 1.7409 -0.0082 -0.0586 0.5181 1214 NAG B O7 4455 C C1 . NAG H . ? 1.3229 1.5982 1.4296 0.0310 0.0711 0.1749 1215 NAG B C1 4456 C C2 . NAG H . ? 1.3180 1.6209 1.4261 0.0234 0.0762 0.1557 1215 NAG B C2 4457 C C3 . NAG H . ? 1.3304 1.6560 1.4402 0.0209 0.0803 0.1427 1215 NAG B C3 4458 C C4 . NAG H . ? 1.4200 1.7711 1.5328 0.0305 0.0747 0.1561 1215 NAG B C4 4459 C C5 . NAG H . ? 1.4165 1.7415 1.5277 0.0380 0.0688 0.1776 1215 NAG B C5 4460 C C6 . NAG H . ? 1.3251 1.6784 1.4384 0.0460 0.0623 0.1934 1215 NAG B C6 4461 C C7 . NAG H . ? 1.2119 1.4839 1.3159 0.0126 0.0799 0.1472 1215 NAG B C7 4462 C C8 . NAG H . ? 1.2554 1.5030 1.3556 0.0008 0.0862 0.1346 1215 NAG B C8 4463 N N2 . NAG H . ? 1.1956 1.4727 1.3004 0.0135 0.0817 0.1440 1215 NAG B N2 4464 O O3 . NAG H . ? 1.1095 1.4664 1.2208 0.0137 0.0840 0.1262 1215 NAG B O3 4465 O O4 . NAG H . ? 1.5259 1.8882 1.6395 0.0291 0.0787 0.1446 1215 NAG B O4 4466 O O5 . NAG H . ? 1.4182 1.7204 1.5274 0.0388 0.0657 0.1868 1215 NAG B O5 4467 O O6 . NAG H . ? 1.2302 1.5876 1.3428 0.0511 0.0557 0.2087 1215 NAG B O6 4468 O O7 . NAG H . ? 1.1627 1.4486 1.2683 0.0212 0.0735 0.1600 1215 NAG B O7 # loop_ _pdbx_poly_seq_scheme.asym_id _pdbx_poly_seq_scheme.entity_id _pdbx_poly_seq_scheme.seq_id _pdbx_poly_seq_scheme.mon_id _pdbx_poly_seq_scheme.ndb_seq_num _pdbx_poly_seq_scheme.pdb_seq_num _pdbx_poly_seq_scheme.auth_seq_num _pdbx_poly_seq_scheme.pdb_mon_id _pdbx_poly_seq_scheme.auth_mon_id _pdbx_poly_seq_scheme.pdb_strand_id _pdbx_poly_seq_scheme.pdb_ins_code _pdbx_poly_seq_scheme.hetero A 1 1 ALA 1 1 ? ? ? A . n A 1 2 ASP 2 2 ? ? ? A . n A 1 3 GLY 3 3 ? ? ? A . n A 1 4 LYS 4 4 ? ? ? A . n A 1 5 TYR 5 5 5 TYR TYR A . n A 1 6 ALA 6 6 6 ALA ALA A . n A 1 7 GLN 7 7 7 GLN GLN A . n A 1 8 LYS 8 8 8 LYS LYS A . n A 1 9 LEU 9 9 9 LEU LEU A . n A 1 10 PHE 10 10 10 PHE PHE A . n A 1 11 ASN 11 11 11 ASN ASN A . n A 1 12 ASP 12 12 12 ASP ASP A . n A 1 13 LEU 13 13 13 LEU LEU A . n A 1 14 PHE 14 14 14 PHE PHE A . n A 1 15 GLU 15 15 15 GLU GLU A . n A 1 16 ASP 16 16 16 ASP ASP A . n A 1 17 TYR 17 17 17 TYR TYR A . n A 1 18 SER 18 18 18 SER SER A . n A 1 19 ASN 19 19 19 ASN ASN A . n A 1 20 ALA 20 20 20 ALA ALA A . n A 1 21 LEU 21 21 21 LEU LEU A . n A 1 22 ARG 22 22 22 ARG ARG A . n A 1 23 PRO 23 23 23 PRO PRO A . n A 1 24 VAL 24 24 24 VAL VAL A . n A 1 25 GLU 25 25 25 GLU GLU A . n A 1 26 ASP 26 26 26 ASP ASP A . n A 1 27 THR 27 27 27 THR THR A . n A 1 28 ASP 28 28 28 ASP ASP A . n A 1 29 LYS 29 29 29 LYS LYS A . n A 1 30 VAL 30 30 30 VAL VAL A . n A 1 31 LEU 31 31 31 LEU LEU A . n A 1 32 ASN 32 32 32 ASN ASN A . n A 1 33 VAL 33 33 33 VAL VAL A . n A 1 34 THR 34 34 34 THR THR A . n A 1 35 LEU 35 35 35 LEU LEU A . n A 1 36 GLN 36 36 36 GLN GLN A . n A 1 37 ILE 37 37 37 ILE ILE A . n A 1 38 THR 38 38 38 THR THR A . n A 1 39 LEU 39 39 39 LEU LEU A . n A 1 40 SER 40 40 40 SER SER A . n A 1 41 GLN 41 41 41 GLN GLN A . n A 1 42 ILE 42 42 42 ILE ILE A . n A 1 43 LYS 43 43 43 LYS LYS A . n A 1 44 ASP 44 44 44 ASP ASP A . n A 1 45 MET 45 45 45 MET MET A . n A 1 46 ASP 46 46 46 ASP ASP A . n A 1 47 GLU 47 47 47 GLU GLU A . n A 1 48 ARG 48 48 48 ARG ARG A . n A 1 49 ASN 49 49 49 ASN ASN A . n A 1 50 GLN 50 50 50 GLN GLN A . n A 1 51 ILE 51 51 51 ILE ILE A . n A 1 52 LEU 52 52 52 LEU LEU A . n A 1 53 THR 53 53 53 THR THR A . n A 1 54 ALA 54 54 54 ALA ALA A . n A 1 55 TYR 55 55 55 TYR TYR A . n A 1 56 LEU 56 56 56 LEU LEU A . n A 1 57 TRP 57 57 57 TRP TRP A . n A 1 58 ILE 58 58 58 ILE ILE A . n A 1 59 ARG 59 59 59 ARG ARG A . n A 1 60 GLN 60 60 60 GLN GLN A . n A 1 61 ILE 61 61 61 ILE ILE A . n A 1 62 TRP 62 62 62 TRP TRP A . n A 1 63 HIS 63 63 63 HIS HIS A . n A 1 64 ASP 64 64 64 ASP ASP A . n A 1 65 ALA 65 65 65 ALA ALA A . n A 1 66 TYR 66 66 66 TYR TYR A . n A 1 67 LEU 67 67 67 LEU LEU A . n A 1 68 THR 68 68 68 THR THR A . n A 1 69 TRP 69 69 69 TRP TRP A . n A 1 70 ASP 70 70 70 ASP ASP A . n A 1 71 ARG 71 71 71 ARG ARG A . n A 1 72 ASP 72 72 72 ASP ASP A . n A 1 73 GLN 73 73 73 GLN GLN A . n A 1 74 TYR 74 74 74 TYR TYR A . n A 1 75 ASP 75 75 75 ASP ASP A . n A 1 76 GLY 76 76 76 GLY GLY A . n A 1 77 LEU 77 77 77 LEU LEU A . n A 1 78 ASP 78 78 78 ASP ASP A . n A 1 79 SER 79 79 79 SER SER A . n A 1 80 ILE 80 80 80 ILE ILE A . n A 1 81 ARG 81 81 81 ARG ARG A . n A 1 82 ILE 82 82 82 ILE ILE A . n A 1 83 PRO 83 83 83 PRO PRO A . n A 1 84 SER 84 84 84 SER SER A . n A 1 85 ASP 85 85 85 ASP ASP A . n A 1 86 LEU 86 86 86 LEU LEU A . n A 1 87 VAL 87 87 87 VAL VAL A . n A 1 88 TRP 88 88 88 TRP TRP A . n A 1 89 ARG 89 89 89 ARG ARG A . n A 1 90 PRO 90 90 90 PRO PRO A . n A 1 91 ASP 91 91 91 ASP ASP A . n A 1 92 ILE 92 92 92 ILE ILE A . n A 1 93 VAL 93 93 93 VAL VAL A . n A 1 94 LEU 94 94 94 LEU LEU A . n A 1 95 TYR 95 95 95 TYR TYR A . n A 1 96 ASN 96 96 96 ASN ASN A . n A 1 97 LYS 97 97 97 LYS LYS A . n A 1 98 ALA 98 98 98 ALA ALA A . n A 1 99 ASP 99 99 99 ASP ASP A . n A 1 100 ASP 100 100 ? ? ? A . n A 1 101 GLU 101 101 ? ? ? A . n A 1 102 SER 102 102 ? ? ? A . n A 1 103 SER 103 103 ? ? ? A . n A 1 104 GLU 104 104 ? ? ? A . n A 1 105 PRO 105 105 105 PRO PRO A . n A 1 106 VAL 106 106 106 VAL VAL A . n A 1 107 ASN 107 107 107 ASN ASN A . n A 1 108 THR 108 108 108 THR THR A . n A 1 109 ASN 109 109 109 ASN ASN A . n A 1 110 VAL 110 110 110 VAL VAL A . n A 1 111 VAL 111 111 111 VAL VAL A . n A 1 112 LEU 112 112 112 LEU LEU A . n A 1 113 ARG 113 113 113 ARG ARG A . n A 1 114 TYR 114 114 114 TYR TYR A . n A 1 115 ASP 115 115 115 ASP ASP A . n A 1 116 GLY 116 116 116 GLY GLY A . n A 1 117 LEU 117 117 117 LEU LEU A . n A 1 118 ILE 118 118 118 ILE ILE A . n A 1 119 THR 119 119 119 THR THR A . n A 1 120 TRP 120 120 120 TRP TRP A . n A 1 121 ASP 121 121 121 ASP ASP A . n A 1 122 ALA 122 122 122 ALA ALA A . n A 1 123 PRO 123 123 123 PRO PRO A . n A 1 124 ALA 124 124 124 ALA ALA A . n A 1 125 ILE 125 125 125 ILE ILE A . n A 1 126 THR 126 126 126 THR THR A . n A 1 127 LYS 127 127 127 LYS LYS A . n A 1 128 SER 128 128 128 SER SER A . n A 1 129 SER 129 129 129 SER SER A . n A 1 130 CYS 130 130 130 CYS CYS A . n A 1 131 VAL 131 131 131 VAL VAL A . n A 1 132 VAL 132 132 132 VAL VAL A . n A 1 133 ASP 133 133 133 ASP ASP A . n A 1 134 VAL 134 134 134 VAL VAL A . n A 1 135 THR 135 135 135 THR THR A . n A 1 136 TYR 136 136 136 TYR TYR A . n A 1 137 PHE 137 137 137 PHE PHE A . n A 1 138 PRO 138 138 138 PRO PRO A . n A 1 139 PHE 139 139 139 PHE PHE A . n A 1 140 ASP 140 140 140 ASP ASP A . n A 1 141 ASN 141 141 141 ASN ASN A . n A 1 142 GLN 142 142 142 GLN GLN A . n A 1 143 GLN 143 143 143 GLN GLN A . n A 1 144 CYS 144 144 144 CYS CYS A . n A 1 145 ASN 145 145 145 ASN ASN A . n A 1 146 LEU 146 146 146 LEU LEU A . n A 1 147 THR 147 147 147 THR THR A . n A 1 148 PHE 148 148 148 PHE PHE A . n A 1 149 GLY 149 149 149 GLY GLY A . n A 1 150 SER 150 150 150 SER SER A . n A 1 151 TRP 151 151 151 TRP TRP A . n A 1 152 THR 152 152 152 THR THR A . n A 1 153 TYR 153 153 153 TYR TYR A . n A 1 154 ASN 154 154 154 ASN ASN A . n A 1 155 GLY 155 155 155 GLY GLY A . n A 1 156 ASN 156 156 156 ASN ASN A . n A 1 157 GLN 157 157 157 GLN GLN A . n A 1 158 VAL 158 158 158 VAL VAL A . n A 1 159 ASP 159 159 159 ASP ASP A . n A 1 160 ILE 160 160 160 ILE ILE A . n A 1 161 PHE 161 161 161 PHE PHE A . n A 1 162 ASN 162 162 162 ASN ASN A . n A 1 163 ALA 163 163 163 ALA ALA A . n A 1 164 LEU 164 164 164 LEU LEU A . n A 1 165 ASP 165 165 165 ASP ASP A . n A 1 166 SER 166 166 166 SER SER A . n A 1 167 GLY 167 167 167 GLY GLY A . n A 1 168 ASP 168 168 168 ASP ASP A . n A 1 169 LEU 169 169 169 LEU LEU A . n A 1 170 SER 170 170 170 SER SER A . n A 1 171 ASP 171 171 171 ASP ASP A . n A 1 172 PHE 172 172 172 PHE PHE A . n A 1 173 ILE 173 173 173 ILE ILE A . n A 1 174 GLU 174 174 174 GLU GLU A . n A 1 175 ASP 175 175 175 ASP ASP A . n A 1 176 VAL 176 176 176 VAL VAL A . n A 1 177 GLU 177 177 177 GLU GLU A . n A 1 178 TRP 178 178 178 TRP TRP A . n A 1 179 GLU 179 179 179 GLU GLU A . n A 1 180 VAL 180 180 180 VAL VAL A . n A 1 181 HIS 181 181 181 HIS HIS A . n A 1 182 GLY 182 182 182 GLY GLY A . n A 1 183 MET 183 183 183 MET MET A . n A 1 184 PRO 184 184 184 PRO PRO A . n A 1 185 ALA 185 185 185 ALA ALA A . n A 1 186 VAL 186 186 186 VAL VAL A . n A 1 187 LYS 187 187 187 LYS LYS A . n A 1 188 ASN 188 188 188 ASN ASN A . n A 1 189 VAL 189 189 189 VAL VAL A . n A 1 190 ILE 190 190 190 ILE ILE A . n A 1 191 SER 191 191 191 SER SER A . n A 1 192 TYR 192 192 192 TYR TYR A . n A 1 193 GLY 193 193 193 GLY GLY A . n A 1 194 CYS 194 194 194 CYS CYS A . n A 1 195 CYS 195 195 195 CYS CYS A . n A 1 196 SER 196 196 196 SER SER A . n A 1 197 GLU 197 197 197 GLU GLU A . n A 1 198 PRO 198 198 198 PRO PRO A . n A 1 199 TYR 199 199 199 TYR TYR A . n A 1 200 PRO 200 200 200 PRO PRO A . n A 1 201 ASP 201 201 201 ASP ASP A . n A 1 202 VAL 202 202 202 VAL VAL A . n A 1 203 THR 203 203 203 THR THR A . n A 1 204 PHE 204 204 204 PHE PHE A . n A 1 205 THR 205 205 205 THR THR A . n A 1 206 LEU 206 206 206 LEU LEU A . n A 1 207 LEU 207 207 207 LEU LEU A . n A 1 208 LEU 208 208 208 LEU LEU A . n A 1 209 LYS 209 209 209 LYS LYS A . n A 1 210 ARG 210 210 210 ARG ARG A . n A 1 211 ARG 211 211 211 ARG ARG A . n A 1 212 SER 212 212 212 SER SER A . n A 1 213 HIS 213 213 ? ? ? A . n A 1 214 HIS 214 214 ? ? ? A . n A 1 215 HIS 215 215 ? ? ? A . n A 1 216 HIS 216 216 ? ? ? A . n A 1 217 HIS 217 217 ? ? ? A . n A 1 218 HIS 218 218 ? ? ? A . n B 1 1 ALA 1 1 ? ? ? B . n B 1 2 ASP 2 2 ? ? ? B . n B 1 3 GLY 3 3 ? ? ? B . n B 1 4 LYS 4 4 ? ? ? B . n B 1 5 TYR 5 5 5 TYR TYR B . n B 1 6 ALA 6 6 6 ALA ALA B . n B 1 7 GLN 7 7 7 GLN GLN B . n B 1 8 LYS 8 8 8 LYS LYS B . n B 1 9 LEU 9 9 9 LEU LEU B . n B 1 10 PHE 10 10 10 PHE PHE B . n B 1 11 ASN 11 11 11 ASN ASN B . n B 1 12 ASP 12 12 12 ASP ASP B . n B 1 13 LEU 13 13 13 LEU LEU B . n B 1 14 PHE 14 14 14 PHE PHE B . n B 1 15 GLU 15 15 15 GLU GLU B . n B 1 16 ASP 16 16 16 ASP ASP B . n B 1 17 TYR 17 17 17 TYR TYR B . n B 1 18 SER 18 18 18 SER SER B . n B 1 19 ASN 19 19 19 ASN ASN B . n B 1 20 ALA 20 20 20 ALA ALA B . n B 1 21 LEU 21 21 21 LEU LEU B . n B 1 22 ARG 22 22 22 ARG ARG B . n B 1 23 PRO 23 23 23 PRO PRO B . n B 1 24 VAL 24 24 24 VAL VAL B . n B 1 25 GLU 25 25 25 GLU GLU B . n B 1 26 ASP 26 26 26 ASP ASP B . n B 1 27 THR 27 27 27 THR THR B . n B 1 28 ASP 28 28 28 ASP ASP B . n B 1 29 LYS 29 29 29 LYS LYS B . n B 1 30 VAL 30 30 30 VAL VAL B . n B 1 31 LEU 31 31 31 LEU LEU B . n B 1 32 ASN 32 32 32 ASN ASN B . n B 1 33 VAL 33 33 33 VAL VAL B . n B 1 34 THR 34 34 34 THR THR B . n B 1 35 LEU 35 35 35 LEU LEU B . n B 1 36 GLN 36 36 36 GLN GLN B . n B 1 37 ILE 37 37 37 ILE ILE B . n B 1 38 THR 38 38 38 THR THR B . n B 1 39 LEU 39 39 39 LEU LEU B . n B 1 40 SER 40 40 40 SER SER B . n B 1 41 GLN 41 41 41 GLN GLN B . n B 1 42 ILE 42 42 42 ILE ILE B . n B 1 43 LYS 43 43 43 LYS LYS B . n B 1 44 ASP 44 44 44 ASP ASP B . n B 1 45 MET 45 45 45 MET MET B . n B 1 46 ASP 46 46 46 ASP ASP B . n B 1 47 GLU 47 47 47 GLU GLU B . n B 1 48 ARG 48 48 48 ARG ARG B . n B 1 49 ASN 49 49 49 ASN ASN B . n B 1 50 GLN 50 50 50 GLN GLN B . n B 1 51 ILE 51 51 51 ILE ILE B . n B 1 52 LEU 52 52 52 LEU LEU B . n B 1 53 THR 53 53 53 THR THR B . n B 1 54 ALA 54 54 54 ALA ALA B . n B 1 55 TYR 55 55 55 TYR TYR B . n B 1 56 LEU 56 56 56 LEU LEU B . n B 1 57 TRP 57 57 57 TRP TRP B . n B 1 58 ILE 58 58 58 ILE ILE B . n B 1 59 ARG 59 59 59 ARG ARG B . n B 1 60 GLN 60 60 60 GLN GLN B . n B 1 61 ILE 61 61 61 ILE ILE B . n B 1 62 TRP 62 62 62 TRP TRP B . n B 1 63 HIS 63 63 63 HIS HIS B . n B 1 64 ASP 64 64 64 ASP ASP B . n B 1 65 ALA 65 65 65 ALA ALA B . n B 1 66 TYR 66 66 66 TYR TYR B . n B 1 67 LEU 67 67 67 LEU LEU B . n B 1 68 THR 68 68 68 THR THR B . n B 1 69 TRP 69 69 69 TRP TRP B . n B 1 70 ASP 70 70 70 ASP ASP B . n B 1 71 ARG 71 71 71 ARG ARG B . n B 1 72 ASP 72 72 72 ASP ASP B . n B 1 73 GLN 73 73 73 GLN GLN B . n B 1 74 TYR 74 74 74 TYR TYR B . n B 1 75 ASP 75 75 75 ASP ASP B . n B 1 76 GLY 76 76 76 GLY GLY B . n B 1 77 LEU 77 77 77 LEU LEU B . n B 1 78 ASP 78 78 78 ASP ASP B . n B 1 79 SER 79 79 79 SER SER B . n B 1 80 ILE 80 80 80 ILE ILE B . n B 1 81 ARG 81 81 81 ARG ARG B . n B 1 82 ILE 82 82 82 ILE ILE B . n B 1 83 PRO 83 83 83 PRO PRO B . n B 1 84 SER 84 84 84 SER SER B . n B 1 85 ASP 85 85 85 ASP ASP B . n B 1 86 LEU 86 86 86 LEU LEU B . n B 1 87 VAL 87 87 87 VAL VAL B . n B 1 88 TRP 88 88 88 TRP TRP B . n B 1 89 ARG 89 89 89 ARG ARG B . n B 1 90 PRO 90 90 90 PRO PRO B . n B 1 91 ASP 91 91 91 ASP ASP B . n B 1 92 ILE 92 92 92 ILE ILE B . n B 1 93 VAL 93 93 93 VAL VAL B . n B 1 94 LEU 94 94 94 LEU LEU B . n B 1 95 TYR 95 95 95 TYR TYR B . n B 1 96 ASN 96 96 96 ASN ASN B . n B 1 97 LYS 97 97 97 LYS LYS B . n B 1 98 ALA 98 98 98 ALA ALA B . n B 1 99 ASP 99 99 99 ASP ASP B . n B 1 100 ASP 100 100 ? ? ? B . n B 1 101 GLU 101 101 ? ? ? B . n B 1 102 SER 102 102 ? ? ? B . n B 1 103 SER 103 103 ? ? ? B . n B 1 104 GLU 104 104 ? ? ? B . n B 1 105 PRO 105 105 105 PRO PRO B . n B 1 106 VAL 106 106 106 VAL VAL B . n B 1 107 ASN 107 107 107 ASN ASN B . n B 1 108 THR 108 108 108 THR THR B . n B 1 109 ASN 109 109 109 ASN ASN B . n B 1 110 VAL 110 110 110 VAL VAL B . n B 1 111 VAL 111 111 111 VAL VAL B . n B 1 112 LEU 112 112 112 LEU LEU B . n B 1 113 ARG 113 113 113 ARG ARG B . n B 1 114 TYR 114 114 114 TYR TYR B . n B 1 115 ASP 115 115 115 ASP ASP B . n B 1 116 GLY 116 116 116 GLY GLY B . n B 1 117 LEU 117 117 117 LEU LEU B . n B 1 118 ILE 118 118 118 ILE ILE B . n B 1 119 THR 119 119 119 THR THR B . n B 1 120 TRP 120 120 120 TRP TRP B . n B 1 121 ASP 121 121 121 ASP ASP B . n B 1 122 ALA 122 122 122 ALA ALA B . n B 1 123 PRO 123 123 123 PRO PRO B . n B 1 124 ALA 124 124 124 ALA ALA B . n B 1 125 ILE 125 125 125 ILE ILE B . n B 1 126 THR 126 126 126 THR THR B . n B 1 127 LYS 127 127 127 LYS LYS B . n B 1 128 SER 128 128 128 SER SER B . n B 1 129 SER 129 129 129 SER SER B . n B 1 130 CYS 130 130 130 CYS CYS B . n B 1 131 VAL 131 131 131 VAL VAL B . n B 1 132 VAL 132 132 132 VAL VAL B . n B 1 133 ASP 133 133 133 ASP ASP B . n B 1 134 VAL 134 134 134 VAL VAL B . n B 1 135 THR 135 135 135 THR THR B . n B 1 136 TYR 136 136 136 TYR TYR B . n B 1 137 PHE 137 137 137 PHE PHE B . n B 1 138 PRO 138 138 138 PRO PRO B . n B 1 139 PHE 139 139 139 PHE PHE B . n B 1 140 ASP 140 140 140 ASP ASP B . n B 1 141 ASN 141 141 141 ASN ASN B . n B 1 142 GLN 142 142 142 GLN GLN B . n B 1 143 GLN 143 143 143 GLN GLN B . n B 1 144 CYS 144 144 144 CYS CYS B . n B 1 145 ASN 145 145 145 ASN ASN B . n B 1 146 LEU 146 146 146 LEU LEU B . n B 1 147 THR 147 147 147 THR THR B . n B 1 148 PHE 148 148 148 PHE PHE B . n B 1 149 GLY 149 149 149 GLY GLY B . n B 1 150 SER 150 150 150 SER SER B . n B 1 151 TRP 151 151 151 TRP TRP B . n B 1 152 THR 152 152 152 THR THR B . n B 1 153 TYR 153 153 153 TYR TYR B . n B 1 154 ASN 154 154 154 ASN ASN B . n B 1 155 GLY 155 155 155 GLY GLY B . n B 1 156 ASN 156 156 156 ASN ASN B . n B 1 157 GLN 157 157 157 GLN GLN B . n B 1 158 VAL 158 158 158 VAL VAL B . n B 1 159 ASP 159 159 159 ASP ASP B . n B 1 160 ILE 160 160 160 ILE ILE B . n B 1 161 PHE 161 161 161 PHE PHE B . n B 1 162 ASN 162 162 162 ASN ASN B . n B 1 163 ALA 163 163 163 ALA ALA B . n B 1 164 LEU 164 164 164 LEU LEU B . n B 1 165 ASP 165 165 165 ASP ASP B . n B 1 166 SER 166 166 166 SER SER B . n B 1 167 GLY 167 167 167 GLY GLY B . n B 1 168 ASP 168 168 168 ASP ASP B . n B 1 169 LEU 169 169 169 LEU LEU B . n B 1 170 SER 170 170 170 SER SER B . n B 1 171 ASP 171 171 171 ASP ASP B . n B 1 172 PHE 172 172 172 PHE PHE B . n B 1 173 ILE 173 173 173 ILE ILE B . n B 1 174 GLU 174 174 174 GLU GLU B . n B 1 175 ASP 175 175 175 ASP ASP B . n B 1 176 VAL 176 176 176 VAL VAL B . n B 1 177 GLU 177 177 177 GLU GLU B . n B 1 178 TRP 178 178 178 TRP TRP B . n B 1 179 GLU 179 179 179 GLU GLU B . n B 1 180 VAL 180 180 180 VAL VAL B . n B 1 181 HIS 181 181 181 HIS HIS B . n B 1 182 GLY 182 182 182 GLY GLY B . n B 1 183 MET 183 183 183 MET MET B . n B 1 184 PRO 184 184 184 PRO PRO B . n B 1 185 ALA 185 185 185 ALA ALA B . n B 1 186 VAL 186 186 186 VAL VAL B . n B 1 187 LYS 187 187 187 LYS LYS B . n B 1 188 ASN 188 188 188 ASN ASN B . n B 1 189 VAL 189 189 189 VAL VAL B . n B 1 190 ILE 190 190 190 ILE ILE B . n B 1 191 SER 191 191 191 SER SER B . n B 1 192 TYR 192 192 192 TYR TYR B . n B 1 193 GLY 193 193 193 GLY GLY B . n B 1 194 CYS 194 194 194 CYS CYS B . n B 1 195 CYS 195 195 195 CYS CYS B . n B 1 196 SER 196 196 196 SER SER B . n B 1 197 GLU 197 197 197 GLU GLU B . n B 1 198 PRO 198 198 198 PRO PRO B . n B 1 199 TYR 199 199 199 TYR TYR B . n B 1 200 PRO 200 200 200 PRO PRO B . n B 1 201 ASP 201 201 201 ASP ASP B . n B 1 202 VAL 202 202 202 VAL VAL B . n B 1 203 THR 203 203 203 THR THR B . n B 1 204 PHE 204 204 204 PHE PHE B . n B 1 205 THR 205 205 205 THR THR B . n B 1 206 LEU 206 206 206 LEU LEU B . n B 1 207 LEU 207 207 207 LEU LEU B . n B 1 208 LEU 208 208 208 LEU LEU B . n B 1 209 LYS 209 209 209 LYS LYS B . n B 1 210 ARG 210 210 210 ARG ARG B . n B 1 211 ARG 211 211 211 ARG ARG B . n B 1 212 SER 212 212 212 SER SER B . n B 1 213 HIS 213 213 ? ? ? B . n B 1 214 HIS 214 214 ? ? ? B . n B 1 215 HIS 215 215 ? ? ? B . n B 1 216 HIS 216 216 ? ? ? B . n B 1 217 HIS 217 217 ? ? ? B . n B 1 218 HIS 218 218 ? ? ? B . n C 2 1 ILE 1 1 1 ILE ILE C . n C 2 2 VAL 2 2 2 VAL VAL C . n C 2 3 CYS 3 3 3 CYS CYS C . n C 2 4 HIS 4 4 4 HIS HIS C . n C 2 5 THR 5 5 5 THR THR C . n C 2 6 THR 6 6 6 THR THR C . n C 2 7 ALA 7 7 7 ALA ALA C . n C 2 8 THR 8 8 8 THR THR C . n C 2 9 SER 9 9 9 SER SER C . n C 2 10 PRO 10 10 10 PRO PRO C . n C 2 11 ILE 11 11 11 ILE ILE C . n C 2 12 SER 12 12 12 SER SER C . n C 2 13 ALA 13 13 13 ALA ALA C . n C 2 14 VAL 14 14 14 VAL VAL C . n C 2 15 THR 15 15 15 THR THR C . n C 2 16 CYS 16 16 16 CYS CYS C . n C 2 17 PRO 17 17 17 PRO PRO C . n C 2 18 PRO 18 18 18 PRO PRO C . n C 2 19 GLY 19 19 19 GLY GLY C . n C 2 20 GLU 20 20 20 GLU GLU C . n C 2 21 ASN 21 21 21 ASN ASN C . n C 2 22 LEU 22 22 22 LEU LEU C . n C 2 23 CYS 23 23 23 CYS CYS C . n C 2 24 TYR 24 24 24 TYR TYR C . n C 2 25 ARG 25 25 25 ARG ARG C . n C 2 26 LYS 26 26 26 LYS LYS C . n C 2 27 MET 27 27 27 MET MET C . n C 2 28 TRP 28 28 28 TRP TRP C . n C 2 29 CYS 29 29 29 CYS CYS C . n C 2 30 ASP 30 30 30 ASP ASP C . n C 2 31 VAL 31 31 31 VAL VAL C . n C 2 32 PHE 32 32 32 PHE PHE C . n C 2 33 CYS 33 33 33 CYS CYS C . n C 2 34 SER 34 34 34 SER SER C . n C 2 35 SER 35 35 35 SER SER C . n C 2 36 ARG 36 36 36 ARG ARG C . n C 2 37 GLY 37 37 37 GLY GLY C . n C 2 38 LYS 38 38 38 LYS LYS C . n C 2 39 VAL 39 39 39 VAL VAL C . n C 2 40 VAL 40 40 40 VAL VAL C . n C 2 41 GLU 41 41 41 GLU GLU C . n C 2 42 LEU 42 42 42 LEU LEU C . n C 2 43 GLY 43 43 43 GLY GLY C . n C 2 44 CYS 44 44 44 CYS CYS C . n C 2 45 ALA 45 45 45 ALA ALA C . n C 2 46 ALA 46 46 46 ALA ALA C . n C 2 47 THR 47 47 47 THR THR C . n C 2 48 CYS 48 48 48 CYS CYS C . n C 2 49 PRO 49 49 49 PRO PRO C . n C 2 50 SER 50 50 50 SER SER C . n C 2 51 LYS 51 51 51 LYS LYS C . n C 2 52 LYS 52 52 52 LYS LYS C . n C 2 53 PRO 53 53 53 PRO PRO C . n C 2 54 TYR 54 54 54 TYR TYR C . n C 2 55 GLU 55 55 55 GLU GLU C . n C 2 56 GLU 56 56 56 GLU GLU C . n C 2 57 VAL 57 57 57 VAL VAL C . n C 2 58 THR 58 58 58 THR THR C . n C 2 59 CYS 59 59 59 CYS CYS C . n C 2 60 CYS 60 60 60 CYS CYS C . n C 2 61 SER 61 61 61 SER SER C . n C 2 62 THR 62 62 62 THR THR C . n C 2 63 ASP 63 63 63 ASP ASP C . n C 2 64 LYS 64 64 64 LYS LYS C . n C 2 65 CYS 65 65 65 CYS CYS C . n C 2 66 ASN 66 66 66 ASN ASN C . n C 2 67 PRO 67 67 67 PRO PRO C . n C 2 68 HIS 68 68 68 HIS HIS C . n C 2 69 PRO 69 69 69 PRO PRO C . n C 2 70 LYS 70 70 70 LYS LYS C . n C 2 71 GLN 71 71 71 GLN GLN C . n C 2 72 ARG 72 72 72 ARG ARG C . n C 2 73 PRO 73 73 73 PRO PRO C . n C 2 74 GLY 74 74 ? ? ? C . n D 2 1 ILE 1 1 1 ILE ILE D . n D 2 2 VAL 2 2 2 VAL VAL D . n D 2 3 CYS 3 3 3 CYS CYS D . n D 2 4 HIS 4 4 4 HIS HIS D . n D 2 5 THR 5 5 5 THR THR D . n D 2 6 THR 6 6 6 THR THR D . n D 2 7 ALA 7 7 7 ALA ALA D . n D 2 8 THR 8 8 8 THR THR D . n D 2 9 SER 9 9 9 SER SER D . n D 2 10 PRO 10 10 10 PRO PRO D . n D 2 11 ILE 11 11 11 ILE ILE D . n D 2 12 SER 12 12 12 SER SER D . n D 2 13 ALA 13 13 13 ALA ALA D . n D 2 14 VAL 14 14 14 VAL VAL D . n D 2 15 THR 15 15 15 THR THR D . n D 2 16 CYS 16 16 16 CYS CYS D . n D 2 17 PRO 17 17 17 PRO PRO D . n D 2 18 PRO 18 18 18 PRO PRO D . n D 2 19 GLY 19 19 19 GLY GLY D . n D 2 20 GLU 20 20 20 GLU GLU D . n D 2 21 ASN 21 21 21 ASN ASN D . n D 2 22 LEU 22 22 22 LEU LEU D . n D 2 23 CYS 23 23 23 CYS CYS D . n D 2 24 TYR 24 24 24 TYR TYR D . n D 2 25 ARG 25 25 25 ARG ARG D . n D 2 26 LYS 26 26 26 LYS LYS D . n D 2 27 MET 27 27 27 MET MET D . n D 2 28 TRP 28 28 28 TRP TRP D . n D 2 29 CYS 29 29 29 CYS CYS D . n D 2 30 ASP 30 30 30 ASP ASP D . n D 2 31 VAL 31 31 31 VAL VAL D . n D 2 32 PHE 32 32 32 PHE PHE D . n D 2 33 CYS 33 33 33 CYS CYS D . n D 2 34 SER 34 34 34 SER SER D . n D 2 35 SER 35 35 35 SER SER D . n D 2 36 ARG 36 36 36 ARG ARG D . n D 2 37 GLY 37 37 37 GLY GLY D . n D 2 38 LYS 38 38 38 LYS LYS D . n D 2 39 VAL 39 39 39 VAL VAL D . n D 2 40 VAL 40 40 40 VAL VAL D . n D 2 41 GLU 41 41 41 GLU GLU D . n D 2 42 LEU 42 42 42 LEU LEU D . n D 2 43 GLY 43 43 43 GLY GLY D . n D 2 44 CYS 44 44 44 CYS CYS D . n D 2 45 ALA 45 45 45 ALA ALA D . n D 2 46 ALA 46 46 46 ALA ALA D . n D 2 47 THR 47 47 47 THR THR D . n D 2 48 CYS 48 48 48 CYS CYS D . n D 2 49 PRO 49 49 49 PRO PRO D . n D 2 50 SER 50 50 50 SER SER D . n D 2 51 LYS 51 51 51 LYS LYS D . n D 2 52 LYS 52 52 52 LYS LYS D . n D 2 53 PRO 53 53 53 PRO PRO D . n D 2 54 TYR 54 54 54 TYR TYR D . n D 2 55 GLU 55 55 55 GLU GLU D . n D 2 56 GLU 56 56 56 GLU GLU D . n D 2 57 VAL 57 57 57 VAL VAL D . n D 2 58 THR 58 58 58 THR THR D . n D 2 59 CYS 59 59 59 CYS CYS D . n D 2 60 CYS 60 60 60 CYS CYS D . n D 2 61 SER 61 61 61 SER SER D . n D 2 62 THR 62 62 62 THR THR D . n D 2 63 ASP 63 63 63 ASP ASP D . n D 2 64 LYS 64 64 64 LYS LYS D . n D 2 65 CYS 65 65 65 CYS CYS D . n D 2 66 ASN 66 66 66 ASN ASN D . n D 2 67 PRO 67 67 67 PRO PRO D . n D 2 68 HIS 68 68 68 HIS HIS D . n D 2 69 PRO 69 69 69 PRO PRO D . n D 2 70 LYS 70 70 70 LYS LYS D . n D 2 71 GLN 71 71 71 GLN GLN D . n D 2 72 ARG 72 72 72 ARG ARG D . n D 2 73 PRO 73 73 73 PRO PRO D . n D 2 74 GLY 74 74 ? ? ? D . 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 E 3 NAG 1 1214 1214 NAG NAG A . F 3 NAG 1 1215 1215 NAG NAG A . G 3 NAG 1 1214 1214 NAG NAG B . H 3 NAG 1 1215 1215 NAG NAG B . # loop_ _pdbx_struct_mod_residue.id _pdbx_struct_mod_residue.label_asym_id _pdbx_struct_mod_residue.label_comp_id _pdbx_struct_mod_residue.label_seq_id _pdbx_struct_mod_residue.auth_asym_id _pdbx_struct_mod_residue.auth_comp_id _pdbx_struct_mod_residue.auth_seq_id _pdbx_struct_mod_residue.PDB_ins_code _pdbx_struct_mod_residue.parent_comp_id _pdbx_struct_mod_residue.details 1 A ASN 32 A ASN 32 ? ASN 'GLYCOSYLATION SITE' 2 A ASN 145 A ASN 145 ? ASN 'GLYCOSYLATION SITE' 3 B ASN 32 B ASN 32 ? ASN 'GLYCOSYLATION SITE' 4 B ASN 145 B ASN 145 ? ASN 'GLYCOSYLATION SITE' # loop_ _pdbx_struct_assembly.id _pdbx_struct_assembly.details _pdbx_struct_assembly.method_details _pdbx_struct_assembly.oligomeric_details _pdbx_struct_assembly.oligomeric_count 1 author_and_software_defined_assembly PISA dimeric 2 2 author_and_software_defined_assembly PISA dimeric 2 # loop_ _pdbx_struct_assembly_gen.assembly_id _pdbx_struct_assembly_gen.oper_expression _pdbx_struct_assembly_gen.asym_id_list 1 1 A,C,E,F 2 1 B,D,G,H # loop_ _pdbx_struct_assembly_prop.biol_id _pdbx_struct_assembly_prop.type _pdbx_struct_assembly_prop.value _pdbx_struct_assembly_prop.details 1 'ABSA (A^2)' 1600 ? 1 MORE 0.4 ? 1 'SSA (A^2)' 15250 ? 2 'ABSA (A^2)' 1740 ? 2 MORE -0.5 ? 2 'SSA (A^2)' 15080 ? # _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 2014-10-01 2 'Structure model' 1 1 2014-10-08 3 'Structure model' 1 2 2014-10-15 4 'Structure model' 1 3 2014-11-19 # _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' 3 4 'Structure model' 'Database references' # _pdbx_refine_tls.pdbx_refine_id 'X-RAY DIFFRACTION' _pdbx_refine_tls.id 1 _pdbx_refine_tls.details ? _pdbx_refine_tls.method refined _pdbx_refine_tls.origin_x 13.3562 _pdbx_refine_tls.origin_y -2.5146 _pdbx_refine_tls.origin_z 7.5095 _pdbx_refine_tls.T[1][1] 0.6051 _pdbx_refine_tls.T[2][2] 0.4330 _pdbx_refine_tls.T[3][3] 0.6552 _pdbx_refine_tls.T[1][2] 0.0298 _pdbx_refine_tls.T[1][3] 0.0020 _pdbx_refine_tls.T[2][3] 0.3801 _pdbx_refine_tls.L[1][1] 1.2931 _pdbx_refine_tls.L[2][2] 0.0020 _pdbx_refine_tls.L[3][3] 2.1428 _pdbx_refine_tls.L[1][2] 0.0146 _pdbx_refine_tls.L[1][3] 0.0676 _pdbx_refine_tls.L[2][3] 0.1785 _pdbx_refine_tls.S[1][1] -0.0859 _pdbx_refine_tls.S[1][2] 0.3037 _pdbx_refine_tls.S[1][3] 0.0969 _pdbx_refine_tls.S[2][1] 0.0321 _pdbx_refine_tls.S[2][2] -0.1242 _pdbx_refine_tls.S[2][3] 0.0166 _pdbx_refine_tls.S[3][1] -0.1897 _pdbx_refine_tls.S[3][2] 0.1402 _pdbx_refine_tls.S[3][3] 0.1330 # _pdbx_refine_tls_group.pdbx_refine_id 'X-RAY DIFFRACTION' _pdbx_refine_tls_group.id 1 _pdbx_refine_tls_group.refine_tls_id 1 _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 ALL # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal PHENIX refinement '(PHENIX.REFINE)' ? 1 XDS 'data reduction' . ? 2 SCALA 'data scaling' . ? 3 PHASER phasing . ? 4 # loop_ _pdbx_validate_close_contact.id _pdbx_validate_close_contact.PDB_model_num _pdbx_validate_close_contact.auth_atom_id_1 _pdbx_validate_close_contact.auth_asym_id_1 _pdbx_validate_close_contact.auth_comp_id_1 _pdbx_validate_close_contact.auth_seq_id_1 _pdbx_validate_close_contact.PDB_ins_code_1 _pdbx_validate_close_contact.label_alt_id_1 _pdbx_validate_close_contact.auth_atom_id_2 _pdbx_validate_close_contact.auth_asym_id_2 _pdbx_validate_close_contact.auth_comp_id_2 _pdbx_validate_close_contact.auth_seq_id_2 _pdbx_validate_close_contact.PDB_ins_code_2 _pdbx_validate_close_contact.label_alt_id_2 _pdbx_validate_close_contact.dist 1 1 OE2 A GLU 179 ? ? NH2 A ARG 210 ? ? 1.96 2 1 ND2 A ASN 96 ? ? O A ASN 145 ? ? 2.00 3 1 ND2 A ASN 32 ? ? O5 A NAG 1214 ? ? 2.06 4 1 O C PRO 49 ? ? NZ C LYS 51 ? ? 2.07 5 1 N B GLY 193 ? ? O D LYS 38 ? ? 2.12 6 1 OH A TYR 17 ? ? N A TRP 88 ? ? 2.14 7 1 ND2 B ASN 96 ? ? O B ASN 145 ? ? 2.18 8 1 N B ASP 133 ? ? O B ASN 141 ? ? 2.18 # loop_ _pdbx_validate_rmsd_angle.id _pdbx_validate_rmsd_angle.PDB_model_num _pdbx_validate_rmsd_angle.auth_atom_id_1 _pdbx_validate_rmsd_angle.auth_asym_id_1 _pdbx_validate_rmsd_angle.auth_comp_id_1 _pdbx_validate_rmsd_angle.auth_seq_id_1 _pdbx_validate_rmsd_angle.PDB_ins_code_1 _pdbx_validate_rmsd_angle.label_alt_id_1 _pdbx_validate_rmsd_angle.auth_atom_id_2 _pdbx_validate_rmsd_angle.auth_asym_id_2 _pdbx_validate_rmsd_angle.auth_comp_id_2 _pdbx_validate_rmsd_angle.auth_seq_id_2 _pdbx_validate_rmsd_angle.PDB_ins_code_2 _pdbx_validate_rmsd_angle.label_alt_id_2 _pdbx_validate_rmsd_angle.auth_atom_id_3 _pdbx_validate_rmsd_angle.auth_asym_id_3 _pdbx_validate_rmsd_angle.auth_comp_id_3 _pdbx_validate_rmsd_angle.auth_seq_id_3 _pdbx_validate_rmsd_angle.PDB_ins_code_3 _pdbx_validate_rmsd_angle.label_alt_id_3 _pdbx_validate_rmsd_angle.angle_value _pdbx_validate_rmsd_angle.angle_target_value _pdbx_validate_rmsd_angle.angle_deviation _pdbx_validate_rmsd_angle.angle_standard_deviation _pdbx_validate_rmsd_angle.linker_flag 1 1 N A ASP 12 ? ? CA A ASP 12 ? ? C A ASP 12 ? ? 129.95 111.00 18.95 2.70 N 2 1 CA A ASP 12 ? ? C A ASP 12 ? ? N A LEU 13 ? ? 103.98 117.20 -13.22 2.20 Y 3 1 C A ALA 122 ? ? N A PRO 123 ? ? CA A PRO 123 ? ? 108.11 119.30 -11.19 1.50 Y 4 1 CD A LYS 127 ? ? CE A LYS 127 ? ? NZ A LYS 127 ? ? 128.67 111.70 16.97 2.30 N 5 1 C A PHE 137 ? ? N A PRO 138 ? ? CD A PRO 138 ? ? 99.61 120.60 -20.99 2.20 Y 6 1 NE A ARG 210 ? ? CZ A ARG 210 ? ? NH1 A ARG 210 ? ? 125.89 120.30 5.59 0.50 N 7 1 CA B GLN 36 ? ? CB B GLN 36 ? ? CG B GLN 36 ? ? 127.16 113.40 13.76 2.20 N 8 1 CD B ARG 89 ? ? NE B ARG 89 ? ? CZ B ARG 89 ? ? 132.10 123.60 8.50 1.40 N 9 1 NE B ARG 89 ? ? CZ B ARG 89 ? ? NH1 B ARG 89 ? ? 125.57 120.30 5.27 0.50 N 10 1 CA B LEU 164 ? ? CB B LEU 164 ? ? CG B LEU 164 ? ? 135.55 115.30 20.25 2.30 N 11 1 N B GLU 177 ? ? CA B GLU 177 ? ? C B GLU 177 ? ? 131.75 111.00 20.75 2.70 N 12 1 C B TYR 199 ? ? N B PRO 200 ? ? CA B PRO 200 ? ? 129.44 119.30 10.14 1.50 Y 13 1 CD B LYS 209 ? ? CE B LYS 209 ? ? NZ B LYS 209 ? ? 125.78 111.70 14.08 2.30 N 14 1 CG1 C VAL 57 ? ? CB C VAL 57 ? ? CG2 C VAL 57 ? ? 123.06 110.90 12.16 1.60 N 15 1 CA C CYS 59 ? ? CB C CYS 59 ? ? SG C CYS 59 ? ? 123.60 114.20 9.40 1.10 N 16 1 CD D LYS 51 ? ? CE D LYS 51 ? ? NZ D LYS 51 ? ? 135.85 111.70 24.15 2.30 N 17 1 C D HIS 68 ? ? N D PRO 69 ? ? CA D PRO 69 ? ? 109.84 119.30 -9.46 1.50 Y 18 1 NE D ARG 72 ? ? CZ D ARG 72 ? ? NH1 D ARG 72 ? ? 116.20 120.30 -4.10 0.50 N # loop_ _pdbx_validate_torsion.id _pdbx_validate_torsion.PDB_model_num _pdbx_validate_torsion.auth_comp_id _pdbx_validate_torsion.auth_asym_id _pdbx_validate_torsion.auth_seq_id _pdbx_validate_torsion.PDB_ins_code _pdbx_validate_torsion.label_alt_id _pdbx_validate_torsion.phi _pdbx_validate_torsion.psi 1 1 ASN A 11 ? ? -46.69 -74.71 2 1 ASP A 12 ? ? 161.88 171.71 3 1 ASP A 16 ? ? -102.61 70.28 4 1 TYR A 17 ? ? 169.39 131.65 5 1 ASN A 19 ? ? -51.02 5.82 6 1 ASP A 44 ? ? -176.35 122.84 7 1 ASP A 46 ? ? -62.02 93.99 8 1 LEU A 67 ? ? -100.08 44.05 9 1 TYR A 74 ? ? -113.57 50.04 10 1 ASP A 91 ? ? -66.48 63.66 11 1 LYS A 97 ? ? -39.39 166.19 12 1 VAL A 106 ? ? 155.42 111.03 13 1 TYR A 136 ? ? 85.76 22.04 14 1 PRO A 138 ? ? -15.93 131.43 15 1 PHE A 139 ? ? -16.70 -55.24 16 1 ASP A 165 ? ? -82.86 32.17 17 1 ASP A 168 ? ? -53.69 108.18 18 1 SER A 170 ? ? 9.07 -63.45 19 1 ASP A 171 ? ? -93.81 35.78 20 1 GLU A 174 ? ? -26.03 88.37 21 1 MET A 183 ? ? -140.70 57.89 22 1 TYR A 192 ? ? 64.05 104.48 23 1 CYS A 195 ? ? -179.13 -127.93 24 1 GLU A 197 ? ? 73.86 163.05 25 1 GLN B 7 ? ? 36.20 -135.61 26 1 PHE B 10 ? ? -67.45 1.47 27 1 ASN B 11 ? ? -33.58 -96.22 28 1 ASP B 16 ? ? -103.17 64.58 29 1 ASP B 44 ? ? -170.20 122.24 30 1 ASP B 46 ? ? -60.41 96.56 31 1 LEU B 67 ? ? -94.94 49.08 32 1 TYR B 74 ? ? -115.23 67.85 33 1 LYS B 97 ? ? -39.88 166.09 34 1 VAL B 106 ? ? 160.01 94.30 35 1 VAL B 134 ? ? -109.76 58.11 36 1 TYR B 136 ? ? 70.51 84.07 37 1 PRO B 138 ? ? -70.76 -169.68 38 1 ASP B 165 ? ? -79.12 30.51 39 1 SER B 170 ? ? -1.99 -59.47 40 1 ASP B 171 ? ? -94.54 34.67 41 1 GLU B 174 ? ? 58.69 84.92 42 1 ASP B 175 ? ? -66.92 -167.73 43 1 GLU B 177 ? ? 145.86 139.44 44 1 TYR B 192 ? ? 63.42 114.79 45 1 SER B 196 ? ? -35.19 159.68 46 1 GLU B 197 ? ? 77.22 103.53 47 1 LEU B 208 ? ? -110.51 -161.09 48 1 LYS B 209 ? ? 164.27 66.79 49 1 ARG B 210 ? ? 11.53 135.85 50 1 PRO C 10 ? ? -69.02 -177.68 51 1 PRO C 17 ? ? -55.67 172.59 52 1 TRP C 28 ? ? -109.07 -162.72 53 1 ASP C 30 ? ? -32.50 -178.30 54 1 LYS C 38 ? ? 64.15 129.51 55 1 LYS C 51 ? ? 56.07 155.84 56 1 LYS C 52 ? ? 23.42 169.20 57 1 LYS C 64 ? ? 70.40 -21.84 58 1 ASN C 66 ? ? -113.48 67.48 59 1 PRO C 69 ? ? -60.43 8.58 60 1 LYS C 70 ? ? -35.42 -74.25 61 1 GLN C 71 ? ? -132.49 -109.42 62 1 ALA D 7 ? ? -58.64 3.03 63 1 PRO D 10 ? ? -68.46 -170.66 64 1 PRO D 17 ? ? -58.54 173.52 65 1 VAL D 31 ? ? -63.40 21.67 66 1 SER D 50 ? ? -60.75 -166.80 67 1 LYS D 52 ? ? -134.06 -125.21 68 1 ASN D 66 ? ? -115.78 67.81 69 1 PRO D 69 ? ? -63.28 32.44 70 1 LYS D 70 ? ? -43.81 -78.52 71 1 GLN D 71 ? ? -126.67 -58.39 72 1 ARG D 72 ? ? 129.76 160.87 # loop_ _pdbx_validate_peptide_omega.id _pdbx_validate_peptide_omega.PDB_model_num _pdbx_validate_peptide_omega.auth_comp_id_1 _pdbx_validate_peptide_omega.auth_asym_id_1 _pdbx_validate_peptide_omega.auth_seq_id_1 _pdbx_validate_peptide_omega.PDB_ins_code_1 _pdbx_validate_peptide_omega.label_alt_id_1 _pdbx_validate_peptide_omega.auth_comp_id_2 _pdbx_validate_peptide_omega.auth_asym_id_2 _pdbx_validate_peptide_omega.auth_seq_id_2 _pdbx_validate_peptide_omega.PDB_ins_code_2 _pdbx_validate_peptide_omega.label_alt_id_2 _pdbx_validate_peptide_omega.omega 1 1 ASN A 11 ? ? ASP A 12 ? ? 92.71 2 1 VAL A 134 ? ? THR A 135 ? ? 119.12 3 1 THR A 135 ? ? TYR A 136 ? ? -124.37 4 1 CYS A 195 ? ? SER A 196 ? ? -56.34 5 1 GLN B 7 ? ? LYS B 8 ? ? 141.60 6 1 LEU B 9 ? ? PHE B 10 ? ? 145.89 7 1 ASP B 12 ? ? LEU B 13 ? ? 147.06 8 1 VAL B 176 ? ? GLU B 177 ? ? 102.33 9 1 GLU B 177 ? ? TRP B 178 ? ? 149.06 10 1 CYS B 195 ? ? SER B 196 ? ? 149.52 11 1 CYS C 29 ? ? ASP C 30 ? ? 134.52 12 1 LYS C 51 ? ? LYS C 52 ? ? 149.72 13 1 LYS C 64 ? ? CYS C 65 ? ? -145.22 14 1 LYS D 52 ? ? PRO D 53 ? ? -143.30 15 1 ARG D 72 ? ? PRO D 73 ? ? -141.27 # loop_ _pdbx_unobs_or_zero_occ_atoms.id _pdbx_unobs_or_zero_occ_atoms.PDB_model_num _pdbx_unobs_or_zero_occ_atoms.polymer_flag _pdbx_unobs_or_zero_occ_atoms.occupancy_flag _pdbx_unobs_or_zero_occ_atoms.auth_asym_id _pdbx_unobs_or_zero_occ_atoms.auth_comp_id _pdbx_unobs_or_zero_occ_atoms.auth_seq_id _pdbx_unobs_or_zero_occ_atoms.PDB_ins_code _pdbx_unobs_or_zero_occ_atoms.auth_atom_id _pdbx_unobs_or_zero_occ_atoms.label_alt_id _pdbx_unobs_or_zero_occ_atoms.label_asym_id _pdbx_unobs_or_zero_occ_atoms.label_comp_id _pdbx_unobs_or_zero_occ_atoms.label_seq_id _pdbx_unobs_or_zero_occ_atoms.label_atom_id 1 1 Y 1 A ASP 99 ? CB ? A ASP 99 CB 2 1 Y 1 A ASP 99 ? CG ? A ASP 99 CG 3 1 Y 1 A ASP 99 ? OD1 ? A ASP 99 OD1 4 1 Y 1 A ASP 99 ? OD2 ? A ASP 99 OD2 5 1 Y 1 B ASP 99 ? CB ? B ASP 99 CB 6 1 Y 1 B ASP 99 ? CG ? B ASP 99 CG 7 1 Y 1 B ASP 99 ? OD1 ? B ASP 99 OD1 8 1 Y 1 B ASP 99 ? OD2 ? B ASP 99 OD2 # 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 ALA 1 ? A ALA 1 2 1 Y 1 A ASP 2 ? A ASP 2 3 1 Y 1 A GLY 3 ? A GLY 3 4 1 Y 1 A LYS 4 ? A LYS 4 5 1 Y 1 A ASP 100 ? A ASP 100 6 1 Y 1 A GLU 101 ? A GLU 101 7 1 Y 1 A SER 102 ? A SER 102 8 1 Y 1 A SER 103 ? A SER 103 9 1 Y 1 A GLU 104 ? A GLU 104 10 1 Y 1 A HIS 213 ? A HIS 213 11 1 Y 1 A HIS 214 ? A HIS 214 12 1 Y 1 A HIS 215 ? A HIS 215 13 1 Y 1 A HIS 216 ? A HIS 216 14 1 Y 1 A HIS 217 ? A HIS 217 15 1 Y 1 A HIS 218 ? A HIS 218 16 1 Y 1 B ALA 1 ? B ALA 1 17 1 Y 1 B ASP 2 ? B ASP 2 18 1 Y 1 B GLY 3 ? B GLY 3 19 1 Y 1 B LYS 4 ? B LYS 4 20 1 Y 1 B ASP 100 ? B ASP 100 21 1 Y 1 B GLU 101 ? B GLU 101 22 1 Y 1 B SER 102 ? B SER 102 23 1 Y 1 B SER 103 ? B SER 103 24 1 Y 1 B GLU 104 ? B GLU 104 25 1 Y 1 B HIS 213 ? B HIS 213 26 1 Y 1 B HIS 214 ? B HIS 214 27 1 Y 1 B HIS 215 ? B HIS 215 28 1 Y 1 B HIS 216 ? B HIS 216 29 1 Y 1 B HIS 217 ? B HIS 217 30 1 Y 1 B HIS 218 ? B HIS 218 31 1 Y 1 C GLY 74 ? C GLY 74 32 1 Y 1 D GLY 74 ? D GLY 74 # _pdbx_entity_nonpoly.entity_id 3 _pdbx_entity_nonpoly.name N-ACETYL-D-GLUCOSAMINE _pdbx_entity_nonpoly.comp_id NAG #