data_4RKO # _entry.id 4RKO # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.281 _audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic # loop_ _database_2.database_id _database_2.database_code PDB 4RKO RCSB RCSB087465 WWPDB D_1000087465 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.details _pdbx_database_related.content_type PDB 1SHH 'Slow form of thrombin bound with PPACK.' unspecified PDB 4RKJ . unspecified # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 4RKO _pdbx_database_status.recvd_initial_deposition_date 2014-10-13 _pdbx_database_status.deposit_site RCSB _pdbx_database_status.process_site RCSB _pdbx_database_status.status_code_sf REL _pdbx_database_status.status_code_mr ? _pdbx_database_status.SG_entry ? _pdbx_database_status.status_code_cs ? _pdbx_database_status.methods_development_category ? _pdbx_database_status.pdb_format_compatible Y # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Pelc, A.L.' 1 'Chen, Z.' 2 'Gohara, D.W.' 3 'Vogt, A.D.' 4 'Pozzi, N.' 5 'Di Cera, E.' 6 # loop_ _citation.id _citation.title _citation.journal_abbrev _citation.journal_volume _citation.page_first _citation.page_last _citation.year _citation.journal_id_ASTM _citation.country _citation.journal_id_ISSN _citation.journal_id_CSD _citation.book_publisher _citation.pdbx_database_id_PubMed _citation.pdbx_database_id_DOI primary 'Why ser and not thr brokers catalysis in the trypsin fold.' Biochemistry 54 1457 1464 2015 BICHAW US 0006-2960 0033 ? 25664608 10.1021/acs.biochem.5b00014 1 'Molecular dissection of Na+ binding to thrombin.' J.Biol.Chem. 279 31842 31853 2004 JBCHA3 US 0021-9258 0071 ? 15152000 10.1074/jbc.M401756200 # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Pelc, L.A.' 1 primary 'Chen, Z.' 2 primary 'Gohara, D.W.' 3 primary 'Vogt, A.D.' 4 primary 'Pozzi, N.' 5 primary 'Di Cera, E.' 6 1 'Pineda, A.O.' 7 1 'Carrell, C.J.' 8 1 'Bush, L.A.' 9 1 'Prasad, S.' 10 1 'Caccia, S.' 11 1 'Chen, Z.W.' 12 1 'Mathews, F.S.' 13 1 'Di Cera, E.' 14 # _cell.entry_id 4RKO _cell.length_a 44.593 _cell.length_b 73.310 _cell.length_c 48.706 _cell.angle_alpha 90.00 _cell.angle_beta 113.43 _cell.angle_gamma 90.00 _cell.Z_PDB 2 _cell.pdbx_unique_axis ? _cell.length_a_esd ? _cell.length_b_esd ? _cell.length_c_esd ? _cell.angle_alpha_esd ? _cell.angle_beta_esd ? _cell.angle_gamma_esd ? # _symmetry.entry_id 4RKO _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 _symmetry.space_group_name_Hall ? # loop_ _entity.id _entity.type _entity.src_method _entity.pdbx_description _entity.formula_weight _entity.pdbx_number_of_molecules _entity.pdbx_ec _entity.pdbx_mutation _entity.pdbx_fragment _entity.details 1 polymer man 'Thrombin heavy chain' 29794.246 1 3.4.21.5 S195T ? ? 2 polymer man 'Thrombin light chain' 4860.396 1 3.4.21.5 ? ? ? 3 non-polymer syn 'D-phenylalanyl-N-[(2S,3S)-6-{[amino(iminio)methyl]amino}-1-chloro-2-hydroxyhexan-3-yl]-L-prolinamide' 453.986 1 ? ? ? ? 4 non-polymer syn '2-(N-MORPHOLINO)-ETHANESULFONIC ACID' 195.237 1 ? ? ? ? 5 non-polymer syn GLYCEROL 92.094 2 ? ? ? ? 6 non-polymer syn 'SODIUM ION' 22.990 1 ? ? ? ? 7 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 1 ? ? ? ? 8 water nat water 18.015 145 ? ? ? ? # 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 ;IVEGSDAEIGMSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPWDKNFTENDLLVRIGKHSRTRYERNIEKISM LEKIYIHPRYNWRENLDRDIALMKLKKPVAFSDYIHPVCLPDRETAASLLQAGYKGRVTGWGNLKETWTANVGKGQPSVL QVVNLPIVERPVCKDSTRIRITDNMFCAGYKPDEGKRGDACEGDTGGPFVMKSPFNNRWYQMGIVSWGEGCDRDGKYGFY THVFRLKKWIQKVIDQFGE ; ;IVEGSDAEIGMSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPWDKNFTENDLLVRIGKHSRTRYERNIEKISM LEKIYIHPRYNWRENLDRDIALMKLKKPVAFSDYIHPVCLPDRETAASLLQAGYKGRVTGWGNLKETWTANVGKGQPSVL QVVNLPIVERPVCKDSTRIRITDNMFCAGYKPDEGKRGDACEGDTGGPFVMKSPFNNRWYQMGIVSWGEGCDRDGKYGFY THVFRLKKWIQKVIDQFGE ; B ? 2 'polypeptide(L)' no no TFFNPRTFGSGEADCGLRPLFEKKSLEDKTERELLESYIDGR TFFNPRTFGSGEADCGLRPLFEKKSLEDKTERELLESYIDGR A ? # loop_ _entity_poly_seq.entity_id _entity_poly_seq.num _entity_poly_seq.mon_id _entity_poly_seq.hetero 1 1 ILE n 1 2 VAL n 1 3 GLU n 1 4 GLY n 1 5 SER n 1 6 ASP n 1 7 ALA n 1 8 GLU n 1 9 ILE n 1 10 GLY n 1 11 MET n 1 12 SER n 1 13 PRO n 1 14 TRP n 1 15 GLN n 1 16 VAL n 1 17 MET n 1 18 LEU n 1 19 PHE n 1 20 ARG n 1 21 LYS n 1 22 SER n 1 23 PRO n 1 24 GLN n 1 25 GLU n 1 26 LEU n 1 27 LEU n 1 28 CYS n 1 29 GLY n 1 30 ALA n 1 31 SER n 1 32 LEU n 1 33 ILE n 1 34 SER n 1 35 ASP n 1 36 ARG n 1 37 TRP n 1 38 VAL n 1 39 LEU n 1 40 THR n 1 41 ALA n 1 42 ALA n 1 43 HIS n 1 44 CYS n 1 45 LEU n 1 46 LEU n 1 47 TYR n 1 48 PRO n 1 49 PRO n 1 50 TRP n 1 51 ASP n 1 52 LYS n 1 53 ASN n 1 54 PHE n 1 55 THR n 1 56 GLU n 1 57 ASN n 1 58 ASP n 1 59 LEU n 1 60 LEU n 1 61 VAL n 1 62 ARG n 1 63 ILE n 1 64 GLY n 1 65 LYS n 1 66 HIS n 1 67 SER n 1 68 ARG n 1 69 THR n 1 70 ARG n 1 71 TYR n 1 72 GLU n 1 73 ARG n 1 74 ASN n 1 75 ILE n 1 76 GLU n 1 77 LYS n 1 78 ILE n 1 79 SER n 1 80 MET n 1 81 LEU n 1 82 GLU n 1 83 LYS n 1 84 ILE n 1 85 TYR n 1 86 ILE n 1 87 HIS n 1 88 PRO n 1 89 ARG n 1 90 TYR n 1 91 ASN n 1 92 TRP n 1 93 ARG n 1 94 GLU n 1 95 ASN n 1 96 LEU n 1 97 ASP n 1 98 ARG n 1 99 ASP n 1 100 ILE n 1 101 ALA n 1 102 LEU n 1 103 MET n 1 104 LYS n 1 105 LEU n 1 106 LYS n 1 107 LYS n 1 108 PRO n 1 109 VAL n 1 110 ALA n 1 111 PHE n 1 112 SER n 1 113 ASP n 1 114 TYR n 1 115 ILE n 1 116 HIS n 1 117 PRO n 1 118 VAL n 1 119 CYS n 1 120 LEU n 1 121 PRO n 1 122 ASP n 1 123 ARG n 1 124 GLU n 1 125 THR n 1 126 ALA n 1 127 ALA n 1 128 SER n 1 129 LEU n 1 130 LEU n 1 131 GLN n 1 132 ALA n 1 133 GLY n 1 134 TYR n 1 135 LYS n 1 136 GLY n 1 137 ARG n 1 138 VAL n 1 139 THR n 1 140 GLY n 1 141 TRP n 1 142 GLY n 1 143 ASN n 1 144 LEU n 1 145 LYS n 1 146 GLU n 1 147 THR n 1 148 TRP n 1 149 THR n 1 150 ALA n 1 151 ASN n 1 152 VAL n 1 153 GLY n 1 154 LYS n 1 155 GLY n 1 156 GLN n 1 157 PRO n 1 158 SER n 1 159 VAL n 1 160 LEU n 1 161 GLN n 1 162 VAL n 1 163 VAL n 1 164 ASN n 1 165 LEU n 1 166 PRO n 1 167 ILE n 1 168 VAL n 1 169 GLU n 1 170 ARG n 1 171 PRO n 1 172 VAL n 1 173 CYS n 1 174 LYS n 1 175 ASP n 1 176 SER n 1 177 THR n 1 178 ARG n 1 179 ILE n 1 180 ARG n 1 181 ILE n 1 182 THR n 1 183 ASP n 1 184 ASN n 1 185 MET n 1 186 PHE n 1 187 CYS n 1 188 ALA n 1 189 GLY n 1 190 TYR n 1 191 LYS n 1 192 PRO n 1 193 ASP n 1 194 GLU n 1 195 GLY n 1 196 LYS n 1 197 ARG n 1 198 GLY n 1 199 ASP n 1 200 ALA n 1 201 CYS n 1 202 GLU n 1 203 GLY n 1 204 ASP n 1 205 THR n 1 206 GLY n 1 207 GLY n 1 208 PRO n 1 209 PHE n 1 210 VAL n 1 211 MET n 1 212 LYS n 1 213 SER n 1 214 PRO n 1 215 PHE n 1 216 ASN n 1 217 ASN n 1 218 ARG n 1 219 TRP n 1 220 TYR n 1 221 GLN n 1 222 MET n 1 223 GLY n 1 224 ILE n 1 225 VAL n 1 226 SER n 1 227 TRP n 1 228 GLY n 1 229 GLU n 1 230 GLY n 1 231 CYS n 1 232 ASP n 1 233 ARG n 1 234 ASP n 1 235 GLY n 1 236 LYS n 1 237 TYR n 1 238 GLY n 1 239 PHE n 1 240 TYR n 1 241 THR n 1 242 HIS n 1 243 VAL n 1 244 PHE n 1 245 ARG n 1 246 LEU n 1 247 LYS n 1 248 LYS n 1 249 TRP n 1 250 ILE n 1 251 GLN n 1 252 LYS n 1 253 VAL n 1 254 ILE n 1 255 ASP n 1 256 GLN n 1 257 PHE n 1 258 GLY n 1 259 GLU n 2 1 THR n 2 2 PHE n 2 3 PHE n 2 4 ASN n 2 5 PRO n 2 6 ARG n 2 7 THR n 2 8 PHE n 2 9 GLY n 2 10 SER n 2 11 GLY n 2 12 GLU n 2 13 ALA n 2 14 ASP n 2 15 CYS n 2 16 GLY n 2 17 LEU n 2 18 ARG n 2 19 PRO n 2 20 LEU n 2 21 PHE n 2 22 GLU n 2 23 LYS n 2 24 LYS n 2 25 SER n 2 26 LEU n 2 27 GLU n 2 28 ASP n 2 29 LYS n 2 30 THR n 2 31 GLU n 2 32 ARG n 2 33 GLU n 2 34 LEU n 2 35 LEU n 2 36 GLU n 2 37 SER n 2 38 TYR n 2 39 ILE n 2 40 ASP n 2 41 GLY n 2 42 ARG n # loop_ _entity_src_gen.entity_id _entity_src_gen.pdbx_src_id _entity_src_gen.pdbx_alt_source_flag _entity_src_gen.pdbx_seq_type _entity_src_gen.pdbx_beg_seq_num _entity_src_gen.pdbx_end_seq_num _entity_src_gen.gene_src_common_name _entity_src_gen.gene_src_genus _entity_src_gen.pdbx_gene_src_gene _entity_src_gen.gene_src_species _entity_src_gen.gene_src_strain _entity_src_gen.gene_src_tissue _entity_src_gen.gene_src_tissue_fraction _entity_src_gen.gene_src_details _entity_src_gen.pdbx_gene_src_fragment _entity_src_gen.pdbx_gene_src_scientific_name _entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id _entity_src_gen.pdbx_gene_src_variant _entity_src_gen.pdbx_gene_src_cell_line _entity_src_gen.pdbx_gene_src_atcc _entity_src_gen.pdbx_gene_src_organ _entity_src_gen.pdbx_gene_src_organelle _entity_src_gen.pdbx_gene_src_cell _entity_src_gen.pdbx_gene_src_cellular_location _entity_src_gen.host_org_common_name _entity_src_gen.pdbx_host_org_scientific_name _entity_src_gen.pdbx_host_org_ncbi_taxonomy_id _entity_src_gen.host_org_genus _entity_src_gen.pdbx_host_org_gene _entity_src_gen.pdbx_host_org_organ _entity_src_gen.host_org_species _entity_src_gen.pdbx_host_org_tissue _entity_src_gen.pdbx_host_org_tissue_fraction _entity_src_gen.pdbx_host_org_strain _entity_src_gen.pdbx_host_org_variant _entity_src_gen.pdbx_host_org_cell_line _entity_src_gen.pdbx_host_org_atcc _entity_src_gen.pdbx_host_org_culture_collection _entity_src_gen.pdbx_host_org_cell _entity_src_gen.pdbx_host_org_organelle _entity_src_gen.pdbx_host_org_cellular_location _entity_src_gen.pdbx_host_org_vector_type _entity_src_gen.pdbx_host_org_vector _entity_src_gen.host_org_details _entity_src_gen.expression_system_id _entity_src_gen.plasmid_name _entity_src_gen.plasmid_details _entity_src_gen.pdbx_description 1 1 sample ? ? ? human ? F2 ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? 'Chinese hamster' 'Cricetulus griseus' 10029 ? ? ? ? ? ? ? ? 'BHK cells' ? ? ? ? ? ? ? ? ? ? ? ? 2 1 sample ? ? ? human ? F2 ? ? ? ? ? ? 'Homo sapiens' 9606 ? ? ? ? ? ? ? 'Chinese hamster' 'Cricetulus griseus' 10029 ? ? ? ? ? ? ? ? 'BHK cells' ? ? ? ? ? ? ? ? ? ? ? ? # loop_ _struct_ref.id _struct_ref.db_name _struct_ref.db_code _struct_ref.pdbx_db_accession _struct_ref.entity_id _struct_ref.pdbx_seq_one_letter_code _struct_ref.pdbx_align_begin _struct_ref.pdbx_db_isoform 1 UNP THRB_HUMAN P00734 1 ;IVEGSDAEIGMSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPWDKNFTENDLLVRIGKHSRTRYERNIEKISM LEKIYIHPRYNWRENLDRDIALMKLKKPVAFSDYIHPVCLPDRETAASLLQAGYKGRVTGWGNLKETWTANVGKGQPSVL QVVNLPIVERPVCKDSTRIRITDNMFCAGYKPDEGKRGDACEGDSGGPFVMKSPFNNRWYQMGIVSWGEGCDRDGKYGFY THVFRLKKWIQKVIDQFGE ; 364 ? 2 UNP THRB_HUMAN P00734 2 TFFNPRTFGSGEADCGLRPLFEKKSLEDKTERELLESYIDGR 322 ? # 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 4RKO B 1 ? 259 ? P00734 364 ? 622 ? 16 247 2 2 4RKO A 1 N 42 ? P00734 322 ? 363 ? 1 15 # _struct_ref_seq_dif.align_id 1 _struct_ref_seq_dif.pdbx_pdb_id_code 4RKO _struct_ref_seq_dif.mon_id THR _struct_ref_seq_dif.pdbx_pdb_strand_id B _struct_ref_seq_dif.seq_num 205 _struct_ref_seq_dif.pdbx_pdb_ins_code ? _struct_ref_seq_dif.pdbx_seq_db_name UNP _struct_ref_seq_dif.pdbx_seq_db_accession_code P00734 _struct_ref_seq_dif.db_mon_id SER _struct_ref_seq_dif.pdbx_seq_db_seq_num 568 _struct_ref_seq_dif.details 'ENGINEERED MUTATION' _struct_ref_seq_dif.pdbx_auth_seq_num 195 _struct_ref_seq_dif.pdbx_ordinal 1 # 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 0G6 peptide-like . 'D-phenylalanyl-N-[(2S,3S)-6-{[amino(iminio)methyl]amino}-1-chloro-2-hydroxyhexan-3-yl]-L-prolinamide' PPACK 'C21 H34 Cl N6 O3 1' 453.986 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 GOL non-polymer . GLYCEROL 'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3' 92.094 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 MES non-polymer . '2-(N-MORPHOLINO)-ETHANESULFONIC ACID' ? 'C6 H13 N O4 S' 195.237 MET 'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S' 149.211 NA non-polymer . 'SODIUM ION' ? 'Na 1' 22.990 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 4RKO _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 2.11 _exptl_crystal.density_percent_sol 41.65 _exptl_crystal.description ? _exptl_crystal.F_000 ? _exptl_crystal.preparation ? # _exptl_crystal_grow.crystal_id 1 _exptl_crystal_grow.method 'VAPOR DIFFUSION, HANGING DROP' _exptl_crystal_grow.temp 293 _exptl_crystal_grow.temp_details ? _exptl_crystal_grow.pH 6.5 _exptl_crystal_grow.pdbx_details '0.1 M MES, pH 6.5, 15% PEG 6000 and 5% MPD, VAPOR DIFFUSION, HANGING DROP, temperature 293K' _exptl_crystal_grow.pdbx_pH_range ? # _diffrn.id 1 _diffrn.ambient_temp 100 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector 'IMAGE PLATE' _diffrn_detector.type 'RIGAKU RAXIS IV++' _diffrn_detector.pdbx_collection_date 2014-06-20 _diffrn_detector.details ? # _diffrn_radiation.diffrn_id 1 _diffrn_radiation.wavelength_id 1 _diffrn_radiation.pdbx_monochromatic_or_laue_m_l M _diffrn_radiation.monochromator Mirror _diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' _diffrn_radiation.pdbx_scattering_type x-ray # _diffrn_radiation_wavelength.id 1 _diffrn_radiation_wavelength.wavelength 1.5418 _diffrn_radiation_wavelength.wt 1.0 # _diffrn_source.diffrn_id 1 _diffrn_source.source 'ROTATING ANODE' _diffrn_source.type 'RIGAKU MICROMAX-007 HF' _diffrn_source.pdbx_synchrotron_site ? _diffrn_source.pdbx_synchrotron_beamline ? _diffrn_source.pdbx_wavelength ? _diffrn_source.pdbx_wavelength_list 1.5418 # _reflns.entry_id 4RKO _reflns.observed_criterion_sigma_I -1.0 _reflns.observed_criterion_sigma_F -1.0 _reflns.d_resolution_low 40.0 _reflns.d_resolution_high 1.84 _reflns.number_obs 22779 _reflns.number_all 24760 _reflns.percent_possible_obs 92.0 _reflns.pdbx_Rmerge_I_obs 0.081 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI 13.4 _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy 3.7 _reflns.R_free_details ? _reflns.limit_h_max ? _reflns.limit_h_min ? _reflns.limit_k_max ? _reflns.limit_k_min ? _reflns.limit_l_max ? _reflns.limit_l_min ? _reflns.observed_criterion_F_max ? _reflns.observed_criterion_F_min ? _reflns.pdbx_chi_squared ? _reflns.pdbx_scaling_rejects ? _reflns.pdbx_ordinal 1 _reflns.pdbx_diffrn_id 1 # loop_ _reflns_shell.d_res_high _reflns_shell.d_res_low _reflns_shell.percent_possible_all _reflns_shell.Rmerge_I_obs _reflns_shell.pdbx_Rsym_value _reflns_shell.meanI_over_sigI_obs _reflns_shell.pdbx_redundancy _reflns_shell.percent_possible_obs _reflns_shell.number_unique_all _reflns_shell.number_measured_all _reflns_shell.number_measured_obs _reflns_shell.number_unique_obs _reflns_shell.pdbx_chi_squared _reflns_shell.pdbx_ordinal _reflns_shell.pdbx_diffrn_id 1.84 1.88 86.8 0.518 ? 1.8 3.1 ? 1072 ? ? ? ? 1 1 1.88 1.92 88.1 0.434 ? 2.2 3.1 ? 1071 ? ? ? ? 2 1 1.92 1.95 89.8 0.402 ? 2.5 3.1 ? 1131 ? ? ? ? 3 1 1.95 1.99 91.2 0.346 ? 2.9 3.2 ? 1096 ? ? ? ? 4 1 1.99 2.04 90.9 0.298 ? 3.1 3.1 ? 1142 ? ? ? ? 5 1 2.04 2.08 91.3 0.271 ? 3.7 3.3 ? 1097 ? ? ? ? 6 1 # _refine.entry_id 4RKO _refine.ls_number_reflns_obs 21578 _refine.ls_number_reflns_all 23608 _refine.pdbx_ls_sigma_I -1.0 _refine.pdbx_ls_sigma_F -1.0 _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 40.0 _refine.ls_d_res_high 1.84 _refine.ls_percent_reflns_obs 91.40 _refine.ls_R_factor_obs 0.16796 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.16609 _refine.ls_R_factor_R_free 0.20224 _refine.ls_R_factor_R_free_error ? _refine.ls_R_factor_R_free_error_details ? _refine.ls_percent_reflns_R_free 5.1 _refine.ls_number_reflns_R_free 1157 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc 0.969 _refine.correlation_coeff_Fo_to_Fc_free 0.954 _refine.B_iso_mean 40.172 _refine.aniso_B[1][1] -1.08 _refine.aniso_B[2][2] -1.31 _refine.aniso_B[3][3] 1.60 _refine.aniso_B[1][2] -0.00 _refine.aniso_B[1][3] 0.21 _refine.aniso_B[2][3] 0.00 _refine.solvent_model_details MASK _refine.solvent_model_param_ksol ? _refine.solvent_model_param_bsol ? _refine.pdbx_solvent_vdw_probe_radii 1.10 _refine.pdbx_solvent_ion_probe_radii 0.70 _refine.pdbx_solvent_shrinkage_radii 0.70 _refine.pdbx_ls_cross_valid_method THROUGHOUT _refine.details 'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' _refine.pdbx_starting_model 'PDB ID 1SHH' _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_isotropic_thermal_model Isotropic _refine.pdbx_stereochemistry_target_values 'MAXIMUM LIKELIHOOD' _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details RANDOM _refine.pdbx_overall_ESU_R 0.153 _refine.pdbx_overall_ESU_R_Free 0.135 _refine.overall_SU_ML 0.118 _refine.pdbx_overall_phase_error ? _refine.overall_SU_B 8.221 _refine.overall_SU_R_Cruickshank_DPI ? _refine.ls_redundancy_reflns_obs ? _refine.B_iso_min ? _refine.B_iso_max ? _refine.overall_SU_R_free ? _refine.ls_wR_factor_R_free ? _refine.ls_wR_factor_R_work ? _refine.overall_FOM_free_R_set ? _refine.overall_FOM_work_R_set ? _refine.pdbx_diffrn_id 1 _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.pdbx_TLS_residual_ADP_flag ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 2352 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 69 _refine_hist.number_atoms_solvent 145 _refine_hist.number_atoms_total 2566 _refine_hist.d_res_high 1.84 _refine_hist.d_res_low 40.0 # loop_ _refine_ls_restr.type _refine_ls_restr.dev_ideal _refine_ls_restr.dev_ideal_target _refine_ls_restr.weight _refine_ls_restr.number _refine_ls_restr.pdbx_restraint_function _refine_ls_restr.pdbx_refine_id r_bond_refined_d 0.008 0.019 ? 2495 ? 'X-RAY DIFFRACTION' r_bond_other_d 0.001 0.020 ? 2361 ? 'X-RAY DIFFRACTION' r_angle_refined_deg 1.326 1.985 ? 3364 ? 'X-RAY DIFFRACTION' r_angle_other_deg 0.836 3.001 ? 5437 ? 'X-RAY DIFFRACTION' r_dihedral_angle_1_deg 7.910 5.034 ? 292 ? 'X-RAY DIFFRACTION' r_dihedral_angle_2_deg 33.972 23.190 ? 116 ? 'X-RAY DIFFRACTION' r_dihedral_angle_3_deg 13.343 15.000 ? 429 ? 'X-RAY DIFFRACTION' r_dihedral_angle_4_deg 13.068 15.000 ? 21 ? 'X-RAY DIFFRACTION' r_chiral_restr 0.150 0.200 ? 351 ? 'X-RAY DIFFRACTION' r_gen_planes_refined 0.005 0.021 ? 2739 ? 'X-RAY DIFFRACTION' r_gen_planes_other 0.001 0.020 ? 584 ? 'X-RAY DIFFRACTION' r_mcbond_it 2.428 2.387 ? 1164 ? 'X-RAY DIFFRACTION' r_mcbond_other 2.428 2.387 ? 1164 ? 'X-RAY DIFFRACTION' r_mcangle_it 3.425 3.557 ? 1449 ? 'X-RAY DIFFRACTION' r_mcangle_other 3.424 3.557 ? 1450 ? 'X-RAY DIFFRACTION' r_scbond_it 3.649 2.988 ? 1331 ? 'X-RAY DIFFRACTION' r_scbond_other 3.649 2.988 ? 1331 ? 'X-RAY DIFFRACTION' r_scangle_other 5.592 4.292 ? 1914 ? 'X-RAY DIFFRACTION' r_long_range_B_refined 7.696 20.837 ? 2901 ? 'X-RAY DIFFRACTION' r_long_range_B_other 7.641 20.458 ? 2848 ? 'X-RAY DIFFRACTION' # _refine_ls_shell.pdbx_total_number_of_bins_used 20 _refine_ls_shell.d_res_high 1.844 _refine_ls_shell.d_res_low 1.892 _refine_ls_shell.number_reflns_R_work 1404 _refine_ls_shell.R_factor_R_work 0.319 _refine_ls_shell.percent_reflns_obs 81.47 _refine_ls_shell.R_factor_R_free 0.319 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free 78 _refine_ls_shell.number_reflns_all ? _refine_ls_shell.R_factor_all ? _refine_ls_shell.number_reflns_obs 1404 _refine_ls_shell.redundancy_reflns_obs ? _refine_ls_shell.pdbx_refine_id 'X-RAY DIFFRACTION' # _struct.entry_id 4RKO _struct.title 'Crystal structure of thrombin mutant S195T bound with PPACK' _struct.pdbx_descriptor 'Thrombin heavy chain (E.C.3.4.21.5), Thrombin light chain (E.C.3.4.21.5)' _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 4RKO _struct_keywords.pdbx_keywords 'HYDROLASE/HYDROLASE INHIBITOR' _struct_keywords.text 'Trypsin-like proteases, catalysis, allosteric regulation, HYDROLASE-HYDROLASE INHIBITOR complex' # loop_ _struct_asym.id _struct_asym.pdbx_blank_PDB_chainid_flag _struct_asym.pdbx_modified _struct_asym.entity_id _struct_asym.details A N N 1 ? B N N 2 ? C N N 3 ? D N N 4 ? E N N 5 ? F N N 5 ? G N N 6 ? H N N 7 ? I N N 8 ? J N N 8 ? # _struct_biol.id 1 _struct_biol.details ? # loop_ _struct_conf.conf_type_id _struct_conf.id _struct_conf.pdbx_PDB_helix_id _struct_conf.beg_label_comp_id _struct_conf.beg_label_asym_id _struct_conf.beg_label_seq_id _struct_conf.pdbx_beg_PDB_ins_code _struct_conf.end_label_comp_id _struct_conf.end_label_asym_id _struct_conf.end_label_seq_id _struct_conf.pdbx_end_PDB_ins_code _struct_conf.beg_auth_comp_id _struct_conf.beg_auth_asym_id _struct_conf.beg_auth_seq_id _struct_conf.end_auth_comp_id _struct_conf.end_auth_asym_id _struct_conf.end_auth_seq_id _struct_conf.pdbx_PDB_helix_class _struct_conf.details _struct_conf.pdbx_PDB_helix_length HELX_P HELX_P1 1 ALA A 41 ? CYS A 44 ? ALA B 55 CYS B 58 5 ? 4 HELX_P HELX_P2 2 PRO A 48 B ASP A 51 E PRO B 60 ASP B 60 5 ? 4 HELX_P HELX_P3 3 THR A 55 I ASN A 57 ? THR B 60 ASN B 62 5 ? 3 HELX_P HELX_P4 4 ASP A 122 ? LEU A 130 ? ASP B 125 LEU B 130 1 ? 9 HELX_P HELX_P5 5 GLU A 169 ? SER A 176 ? GLU B 164 SER B 171 1 ? 8 HELX_P HELX_P6 6 LYS A 191 ? GLY A 195 C LYS B 185 GLY B 186 5 ? 5 HELX_P HELX_P7 7 LEU A 246 ? PHE A 257 ? LEU B 234 PHE B 245 1 ? 12 HELX_P HELX_P8 8 ASN B 4 K GLY B 9 F ASN A 1 GLY A 1 1 ? 6 HELX_P HELX_P9 9 PHE B 21 ? SER B 25 ? PHE A 7 SER A 11 5 ? 5 HELX_P HELX_P10 10 THR B 30 B ASP B 40 L THR A 14 ASP A 14 1 ? 11 # _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 28 SG B ? ? 1_555 A CYS 44 SG B ? B CYS 42 B CYS 58 1_555 ? ? ? ? ? ? ? 2.025 ? disulf2 disulf ? ? A CYS 28 SG A ? ? 1_555 A CYS 44 SG A ? B CYS 42 B CYS 58 1_555 ? ? ? ? ? ? ? 2.040 ? disulf3 disulf ? ? A CYS 119 SG ? ? ? 1_555 B CYS 15 SG ? ? B CYS 122 A CYS 1 1_555 ? ? ? ? ? ? ? 2.064 ? disulf4 disulf ? ? A CYS 173 SG ? ? ? 1_555 A CYS 187 SG ? ? B CYS 168 B CYS 182 1_555 ? ? ? ? ? ? ? 2.057 ? disulf5 disulf ? ? A CYS 201 SG ? ? ? 1_555 A CYS 231 SG ? ? B CYS 191 B CYS 220 1_555 ? ? ? ? ? ? ? 2.069 ? covale1 covale ? ? A ASN 53 ND2 ? G ? 1_555 H NAG . C1 ? ? B ASN 60 B NAG 306 1_555 ? ? ? ? ? ? ? 1.457 ? metalc1 metalc ? ? A ARG 233 O ? A ? 1_555 G NA . NA ? ? B ARG 221 B NA 305 1_555 ? ? ? ? ? ? ? 2.236 ? metalc2 metalc ? ? A LYS 236 O ? ? ? 1_555 G NA . NA ? ? B LYS 224 B NA 305 1_555 ? ? ? ? ? ? ? 2.257 ? metalc3 metalc ? ? G NA . NA ? ? ? 1_555 I HOH . O ? ? B NA 305 B HOH 465 1_555 ? ? ? ? ? ? ? 2.326 ? metalc4 metalc ? ? G NA . NA ? ? ? 1_555 I HOH . O ? ? B NA 305 B HOH 464 1_555 ? ? ? ? ? ? ? 2.365 ? metalc5 metalc ? ? G NA . NA ? ? ? 1_555 I HOH . O ? ? B NA 305 B HOH 463 1_555 ? ? ? ? ? ? ? 2.372 ? metalc6 metalc ? ? G NA . NA ? ? ? 1_555 I HOH . O ? ? B NA 305 B HOH 448 1_555 ? ? ? ? ? ? ? 2.765 ? covale2 covale ? ? A THR 205 OG1 ? ? ? 1_555 C 0G6 . C2 ? ? B THR 195 B 0G6 301 1_555 ? ? ? ? ? ? ? 1.363 ? covale3 covale ? ? A HIS 43 NE2 ? ? ? 1_555 C 0G6 . C3 ? ? B HIS 57 B 0G6 301 1_555 ? ? ? ? ? ? ? 1.475 ? # loop_ _struct_conn_type.id _struct_conn_type.criteria _struct_conn_type.reference disulf ? ? covale ? ? metalc ? ? # _struct_mon_prot_cis.pdbx_id 1 _struct_mon_prot_cis.label_comp_id SER _struct_mon_prot_cis.label_seq_id 22 _struct_mon_prot_cis.label_asym_id A _struct_mon_prot_cis.label_alt_id . _struct_mon_prot_cis.pdbx_PDB_ins_code A _struct_mon_prot_cis.auth_comp_id SER _struct_mon_prot_cis.auth_seq_id 36 _struct_mon_prot_cis.auth_asym_id B _struct_mon_prot_cis.pdbx_label_comp_id_2 PRO _struct_mon_prot_cis.pdbx_label_seq_id_2 23 _struct_mon_prot_cis.pdbx_label_asym_id_2 A _struct_mon_prot_cis.pdbx_PDB_ins_code_2 ? _struct_mon_prot_cis.pdbx_auth_comp_id_2 PRO _struct_mon_prot_cis.pdbx_auth_seq_id_2 37 _struct_mon_prot_cis.pdbx_auth_asym_id_2 B _struct_mon_prot_cis.pdbx_PDB_model_num 1 _struct_mon_prot_cis.pdbx_omega_angle -4.38 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details A ? 7 ? B ? 7 ? C ? 2 ? # loop_ _struct_sheet_order.sheet_id _struct_sheet_order.range_id_1 _struct_sheet_order.range_id_2 _struct_sheet_order.offset _struct_sheet_order.sense A 1 2 ? anti-parallel A 2 3 ? anti-parallel A 3 4 ? anti-parallel A 4 5 ? anti-parallel A 5 6 ? anti-parallel A 6 7 ? anti-parallel B 1 2 ? anti-parallel B 2 3 ? anti-parallel B 3 4 ? anti-parallel B 4 5 ? anti-parallel B 5 6 ? anti-parallel B 6 7 ? anti-parallel C 1 2 ? anti-parallel # loop_ _struct_sheet_range.sheet_id _struct_sheet_range.id _struct_sheet_range.beg_label_comp_id _struct_sheet_range.beg_label_asym_id _struct_sheet_range.beg_label_seq_id _struct_sheet_range.pdbx_beg_PDB_ins_code _struct_sheet_range.end_label_comp_id _struct_sheet_range.end_label_asym_id _struct_sheet_range.end_label_seq_id _struct_sheet_range.pdbx_end_PDB_ins_code _struct_sheet_range.beg_auth_comp_id _struct_sheet_range.beg_auth_asym_id _struct_sheet_range.beg_auth_seq_id _struct_sheet_range.end_auth_comp_id _struct_sheet_range.end_auth_asym_id _struct_sheet_range.end_auth_seq_id A 1 SER A 5 ? ASP A 6 ? SER B 20 ASP B 21 A 2 GLN A 161 ? PRO A 166 ? GLN B 156 PRO B 161 A 3 LYS A 135 ? GLY A 140 ? LYS B 135 GLY B 140 A 4 PRO A 208 ? LYS A 212 ? PRO B 198 LYS B 202 A 5 TRP A 219 ? TRP A 227 ? TRP B 207 TRP B 215 A 6 GLY A 238 ? HIS A 242 ? GLY B 226 HIS B 230 A 7 MET A 185 ? ALA A 188 ? MET B 180 ALA B 183 B 1 GLN A 15 ? ARG A 20 ? GLN B 30 ARG B 35 B 2 GLU A 25 ? LEU A 32 ? GLU B 39 LEU B 46 B 3 TRP A 37 ? THR A 40 ? TRP B 51 THR B 54 B 4 ALA A 101 ? LEU A 105 ? ALA B 104 LEU B 108 B 5 LYS A 77 ? ILE A 86 ? LYS B 81 ILE B 90 B 6 LEU A 59 ? ILE A 63 ? LEU B 64 ILE B 68 B 7 GLN A 15 ? ARG A 20 ? GLN B 30 ARG B 35 C 1 LEU A 46 ? TYR A 47 A LEU B 60 TYR B 60 C 2 LYS A 52 F ASN A 53 G LYS B 60 ASN B 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 A 1 2 N SER A 5 ? N SER B 20 O VAL A 162 ? O VAL B 157 A 2 3 O VAL A 163 ? O VAL B 158 N VAL A 138 ? N VAL B 138 A 3 4 N ARG A 137 ? N ARG B 137 O VAL A 210 ? O VAL B 200 A 4 5 N MET A 211 ? N MET B 201 O TYR A 220 ? O TYR B 208 A 5 6 N TRP A 227 ? N TRP B 215 O PHE A 239 ? O PHE B 227 A 6 7 O TYR A 240 ? O TYR B 228 N PHE A 186 ? N PHE B 181 B 1 2 N ARG A 20 ? N ARG B 35 O GLU A 25 ? O GLU B 39 B 2 3 N SER A 31 ? N SER B 45 O LEU A 39 ? O LEU B 53 B 3 4 N VAL A 38 ? N VAL B 52 O MET A 103 ? O MET B 106 B 4 5 O LYS A 104 ? O LYS B 107 N GLU A 82 ? N GLU B 86 B 5 6 O LYS A 77 ? O LYS B 81 N ILE A 63 ? N ILE B 68 B 6 7 O LEU A 60 ? O LEU B 65 N PHE A 19 ? N PHE B 34 C 1 2 N TYR A 47 A N TYR B 60 O LYS A 52 F O LYS B 60 # 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 ? ? ? ? 19 'BINDING SITE FOR RESIDUE 0G6 B 301' AC2 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE MES B 302' AC3 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE GOL B 303' AC4 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE GOL B 304' AC5 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE NA B 305' AC6 Software ? ? ? ? 1 'BINDING SITE FOR RESIDUE NAG B 306' # 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 19 HIS A 43 ? HIS B 57 . ? 1_555 ? 2 AC1 19 TYR A 47 A TYR B 60 . ? 1_555 ? 3 AC1 19 TRP A 50 D TRP B 60 . ? 1_555 ? 4 AC1 19 GLU A 94 A GLU B 97 . ? 1_555 ? 5 AC1 19 LEU A 96 ? LEU B 99 . ? 1_555 ? 6 AC1 19 ASP A 199 ? ASP B 189 . ? 1_555 ? 7 AC1 19 ALA A 200 ? ALA B 190 . ? 1_555 ? 8 AC1 19 GLY A 203 ? GLY B 193 . ? 1_555 ? 9 AC1 19 THR A 205 ? THR B 195 . ? 1_555 ? 10 AC1 19 SER A 226 ? SER B 214 . ? 1_555 ? 11 AC1 19 TRP A 227 ? TRP B 215 . ? 1_555 ? 12 AC1 19 GLY A 228 ? GLY B 216 . ? 1_555 ? 13 AC1 19 GLY A 230 ? GLY B 219 . ? 1_555 ? 14 AC1 19 GLY A 238 ? GLY B 226 . ? 1_555 ? 15 AC1 19 HOH I . ? HOH B 429 . ? 1_555 ? 16 AC1 19 HOH I . ? HOH B 434 . ? 1_555 ? 17 AC1 19 HOH I . ? HOH B 455 . ? 1_555 ? 18 AC1 19 HOH I . ? HOH B 466 . ? 1_555 ? 19 AC1 19 HOH I . ? HOH B 517 . ? 1_555 ? 20 AC2 4 HIS A 87 ? HIS B 91 . ? 1_555 ? 21 AC2 4 LYS A 248 ? LYS B 236 . ? 1_555 ? 22 AC2 4 TRP A 249 ? TRP B 237 . ? 1_555 ? 23 AC2 4 HOH I . ? HOH B 506 . ? 1_555 ? 24 AC3 8 GLU B 22 ? GLU A 8 . ? 1_555 ? 25 AC3 8 SER B 25 ? SER A 11 . ? 1_555 ? 26 AC3 8 LEU B 26 ? LEU A 12 . ? 1_555 ? 27 AC3 8 GLU B 27 ? GLU A 13 . ? 1_555 ? 28 AC3 8 GLU B 31 C GLU A 14 . ? 1_555 ? 29 AC3 8 HOH J . ? HOH A 103 . ? 1_555 ? 30 AC3 8 LYS A 212 ? LYS B 202 . ? 1_555 ? 31 AC3 8 ASN A 217 ? ASN B 205 . ? 1_555 ? 32 AC4 4 LEU A 130 ? LEU B 130 . ? 1_555 ? 33 AC4 4 ARG A 170 ? ARG B 165 . ? 1_555 ? 34 AC4 4 PHE A 186 ? PHE B 181 . ? 1_555 ? 35 AC4 4 HOH I . ? HOH B 427 . ? 1_555 ? 36 AC5 6 ARG A 233 A ARG B 221 . ? 1_555 ? 37 AC5 6 LYS A 236 ? LYS B 224 . ? 1_555 ? 38 AC5 6 HOH I . ? HOH B 448 . ? 1_555 ? 39 AC5 6 HOH I . ? HOH B 463 . ? 1_555 ? 40 AC5 6 HOH I . ? HOH B 464 . ? 1_555 ? 41 AC5 6 HOH I . ? HOH B 465 . ? 1_555 ? 42 AC6 1 ASN A 53 G ASN B 60 . ? 1_555 ? # _database_PDB_matrix.entry_id 4RKO _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 4RKO _atom_sites.fract_transf_matrix[1][1] 0.022425 _atom_sites.fract_transf_matrix[1][2] 0.000000 _atom_sites.fract_transf_matrix[1][3] 0.009718 _atom_sites.fract_transf_matrix[2][1] -0.000000 _atom_sites.fract_transf_matrix[2][2] 0.013641 _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] 0.022376 _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 NA 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 . ILE A 1 1 ? 8.426 1.175 23.977 1.00 29.37 ? 16 ILE B N 1 ATOM 2 C CA . ILE A 1 1 ? 9.588 2.032 24.373 1.00 25.29 ? 16 ILE B CA 1 ATOM 3 C C . ILE A 1 1 ? 9.462 2.347 25.853 1.00 24.67 ? 16 ILE B C 1 ATOM 4 O O . ILE A 1 1 ? 8.455 2.905 26.293 1.00 26.43 ? 16 ILE B O 1 ATOM 5 C CB . ILE A 1 1 ? 9.651 3.349 23.572 1.00 27.71 ? 16 ILE B CB 1 ATOM 6 C CG1 . ILE A 1 1 ? 9.715 3.085 22.057 1.00 25.67 ? 16 ILE B CG1 1 ATOM 7 C CG2 . ILE A 1 1 ? 10.831 4.205 24.016 1.00 26.06 ? 16 ILE B CG2 1 ATOM 8 C CD1 . ILE A 1 1 ? 10.924 2.298 21.578 1.00 30.47 ? 16 ILE B CD1 1 ATOM 9 N N . VAL A 1 2 ? 10.485 1.985 26.614 1.00 24.59 ? 17 VAL B N 1 ATOM 10 C CA . VAL A 1 2 ? 10.525 2.244 28.046 1.00 29.03 ? 17 VAL B CA 1 ATOM 11 C C . VAL A 1 2 ? 11.340 3.509 28.278 1.00 30.16 ? 17 VAL B C 1 ATOM 12 O O . VAL A 1 2 ? 12.395 3.700 27.652 1.00 28.49 ? 17 VAL B O 1 ATOM 13 C CB . VAL A 1 2 ? 11.150 1.069 28.833 1.00 29.38 ? 17 VAL B CB 1 ATOM 14 C CG1 . VAL A 1 2 ? 11.232 1.396 30.318 1.00 33.61 ? 17 VAL B CG1 1 ATOM 15 C CG2 . VAL A 1 2 ? 10.353 -0.213 28.606 1.00 32.07 ? 17 VAL B CG2 1 ATOM 16 N N . GLU A 1 3 ? 10.830 4.355 29.176 1.00 30.33 ? 18 GLU B N 1 ATOM 17 C CA . GLU A 1 3 ? 11.495 5.591 29.605 1.00 33.98 ? 18 GLU B CA 1 ATOM 18 C C . GLU A 1 3 ? 11.817 6.528 28.432 1.00 32.02 ? 18 GLU B C 1 ATOM 19 O O . GLU A 1 3 ? 12.832 7.206 28.436 1.00 31.88 ? 18 GLU B O 1 ATOM 20 C CB . GLU A 1 3 ? 12.753 5.262 30.425 1.00 35.02 ? 18 GLU B CB 1 ATOM 21 C CG . GLU A 1 3 ? 12.454 4.680 31.806 1.00 40.62 ? 18 GLU B CG 1 ATOM 22 C CD . GLU A 1 3 ? 12.122 5.736 32.860 1.00 47.08 ? 18 GLU B CD 1 ATOM 23 O OE1 . GLU A 1 3 ? 11.665 5.368 33.973 1.00 54.87 ? 18 GLU B OE1 1 ATOM 24 O OE2 . GLU A 1 3 ? 12.320 6.936 32.593 1.00 44.72 ? 18 GLU B OE2 1 ATOM 25 N N . GLY A 1 4 ? 10.934 6.568 27.437 1.00 30.72 ? 19 GLY B N 1 ATOM 26 C CA . GLY A 1 4 ? 11.065 7.470 26.293 1.00 32.23 ? 19 GLY B CA 1 ATOM 27 C C . GLY A 1 4 ? 10.095 8.631 26.484 1.00 31.84 ? 19 GLY B C 1 ATOM 28 O O . GLY A 1 4 ? 9.762 9.000 27.610 1.00 31.10 ? 19 GLY B O 1 ATOM 29 N N . SER A 1 5 ? 9.644 9.218 25.391 1.00 27.55 ? 20 SER B N 1 ATOM 30 C CA . SER A 1 5 ? 8.606 10.227 25.476 1.00 30.54 ? 20 SER B CA 1 ATOM 31 C C . SER A 1 5 ? 7.775 10.183 24.210 1.00 27.01 ? 20 SER B C 1 ATOM 32 O O . SER A 1 5 ? 8.151 9.498 23.253 1.00 25.61 ? 20 SER B O 1 ATOM 33 C CB . SER A 1 5 ? 9.208 11.627 25.682 1.00 36.27 ? 20 SER B CB 1 ATOM 34 O OG . SER A 1 5 ? 10.173 11.924 24.693 1.00 37.01 ? 20 SER B OG 1 ATOM 35 N N . ASP A 1 6 ? 6.660 10.915 24.214 1.00 25.73 ? 21 ASP B N 1 ATOM 36 C CA . ASP A 1 6 ? 5.805 11.038 23.027 1.00 26.82 ? 21 ASP B CA 1 ATOM 37 C C . ASP A 1 6 ? 6.589 11.618 21.850 1.00 28.18 ? 21 ASP B C 1 ATOM 38 O O . ASP A 1 6 ? 7.301 12.606 22.004 1.00 28.82 ? 21 ASP B O 1 ATOM 39 C CB . ASP A 1 6 ? 4.640 11.988 23.303 1.00 26.78 ? 21 ASP B CB 1 ATOM 40 C CG . ASP A 1 6 ? 3.658 11.454 24.345 1.00 27.83 ? 21 ASP B CG 1 ATOM 41 O OD1 . ASP A 1 6 ? 3.766 10.300 24.789 1.00 28.64 ? 21 ASP B OD1 1 ATOM 42 O OD2 . ASP A 1 6 ? 2.752 12.201 24.717 1.00 34.12 ? 21 ASP B OD2 1 ATOM 43 N N . ALA A 1 7 ? 6.440 11.034 20.671 1.00 28.80 ? 22 ALA B N 1 ATOM 44 C CA . ALA A 1 7 ? 7.011 11.626 19.460 1.00 29.58 ? 22 ALA B CA 1 ATOM 45 C C . ALA A 1 7 ? 6.330 12.943 19.196 1.00 30.12 ? 22 ALA B C 1 ATOM 46 O O . ALA A 1 7 ? 5.142 13.107 19.526 1.00 32.04 ? 22 ALA B O 1 ATOM 47 C CB . ALA A 1 7 ? 6.804 10.713 18.261 1.00 29.86 ? 22 ALA B CB 1 ATOM 48 N N . GLU A 1 8 ? 7.054 13.874 18.576 1.00 27.87 ? 23 GLU B N 1 ATOM 49 C CA . GLU A 1 8 ? 6.411 15.055 18.001 1.00 30.67 ? 23 GLU B CA 1 ATOM 50 C C . GLU A 1 8 ? 5.731 14.633 16.707 1.00 27.60 ? 23 GLU B C 1 ATOM 51 O O . GLU A 1 8 ? 6.119 13.636 16.089 1.00 27.74 ? 23 GLU B O 1 ATOM 52 C CB . GLU A 1 8 ? 7.426 16.155 17.698 1.00 34.13 ? 23 GLU B CB 1 ATOM 53 C CG . GLU A 1 8 ? 8.001 16.845 18.927 1.00 38.83 ? 23 GLU B CG 1 ATOM 54 C CD . GLU A 1 8 ? 9.052 17.872 18.552 1.00 43.39 ? 23 GLU B CD 1 ATOM 55 O OE1 . GLU A 1 8 ? 8.766 19.085 18.594 1.00 51.30 ? 23 GLU B OE1 1 ATOM 56 O OE2 . GLU A 1 8 ? 10.151 17.453 18.168 1.00 45.45 ? 23 GLU B OE2 1 ATOM 57 N N . ILE A 1 9 ? 4.726 15.384 16.289 1.00 29.46 ? 24 ILE B N 1 ATOM 58 C CA . ILE A 1 9 ? 4.052 15.097 15.018 1.00 31.86 ? 24 ILE B CA 1 ATOM 59 C C . ILE A 1 9 ? 5.049 15.180 13.863 1.00 31.69 ? 24 ILE B C 1 ATOM 60 O O . ILE A 1 9 ? 5.786 16.159 13.731 1.00 32.33 ? 24 ILE B O 1 ATOM 61 C CB . ILE A 1 9 ? 2.815 15.990 14.817 1.00 36.44 ? 24 ILE B CB 1 ATOM 62 C CG1 . ILE A 1 9 ? 1.758 15.565 15.861 1.00 45.17 ? 24 ILE B CG1 1 ATOM 63 C CG2 . ILE A 1 9 ? 2.316 15.874 13.381 1.00 37.80 ? 24 ILE B CG2 1 ATOM 64 C CD1 . ILE A 1 9 ? 0.353 16.075 15.644 1.00 55.11 ? 24 ILE B CD1 1 ATOM 65 N N . GLY A 1 10 ? 5.121 14.111 13.077 1.00 28.92 ? 25 GLY B N 1 ATOM 66 C CA . GLY A 1 10 ? 6.027 14.063 11.930 1.00 29.66 ? 25 GLY B CA 1 ATOM 67 C C . GLY A 1 10 ? 7.495 13.865 12.249 1.00 26.21 ? 25 GLY B C 1 ATOM 68 O O . GLY A 1 10 ? 8.357 14.007 11.370 1.00 27.50 ? 25 GLY B O 1 ATOM 69 N N . MET A 1 11 ? 7.794 13.532 13.500 1.00 25.78 ? 26 MET B N 1 ATOM 70 C CA . MET A 1 11 ? 9.169 13.335 13.939 1.00 27.52 ? 26 MET B CA 1 ATOM 71 C C . MET A 1 11 ? 9.802 12.092 13.305 1.00 27.68 ? 26 MET B C 1 ATOM 72 O O . MET A 1 11 ? 11.023 12.032 13.106 1.00 27.44 ? 26 MET B O 1 ATOM 73 C CB . MET A 1 11 ? 9.167 13.176 15.449 1.00 30.62 ? 26 MET B CB 1 ATOM 74 C CG . MET A 1 11 ? 10.519 13.159 16.109 1.00 35.40 ? 26 MET B CG 1 ATOM 75 S SD . MET A 1 11 ? 10.259 12.888 17.864 1.00 37.12 ? 26 MET B SD 1 ATOM 76 C CE . MET A 1 11 ? 11.484 14.001 18.543 1.00 39.49 ? 26 MET B CE 1 ATOM 77 N N . SER A 1 12 ? 8.963 11.104 13.007 1.00 27.13 ? 27 SER B N 1 ATOM 78 C CA . SER A 1 12 ? 9.409 9.821 12.478 1.00 28.81 ? 27 SER B CA 1 ATOM 79 C C . SER A 1 12 ? 8.465 9.392 11.336 1.00 28.28 ? 27 SER B C 1 ATOM 80 O O . SER A 1 12 ? 7.704 8.427 11.460 1.00 26.46 ? 27 SER B O 1 ATOM 81 C CB . SER A 1 12 ? 9.464 8.780 13.610 1.00 30.49 ? 27 SER B CB 1 ATOM 82 O OG . SER A 1 12 ? 10.152 7.613 13.195 1.00 36.03 ? 27 SER B OG 1 ATOM 83 N N . PRO A 1 13 ? 8.521 10.116 10.208 1.00 26.47 ? 28 PRO B N 1 ATOM 84 C CA . PRO A 1 13 ? 7.562 9.878 9.125 1.00 26.61 ? 28 PRO B CA 1 ATOM 85 C C . PRO A 1 13 ? 7.802 8.586 8.334 1.00 25.47 ? 28 PRO B C 1 ATOM 86 O O . PRO A 1 13 ? 7.018 8.267 7.446 1.00 27.22 ? 28 PRO B O 1 ATOM 87 C CB . PRO A 1 13 ? 7.747 11.109 8.229 1.00 28.64 ? 28 PRO B CB 1 ATOM 88 C CG . PRO A 1 13 ? 9.156 11.524 8.442 1.00 25.05 ? 28 PRO B CG 1 ATOM 89 C CD . PRO A 1 13 ? 9.413 11.255 9.904 1.00 25.79 ? 28 PRO B CD 1 ATOM 90 N N . TRP A 1 14 ? 8.884 7.873 8.650 1.00 22.84 ? 29 TRP B N 1 ATOM 91 C CA . TRP A 1 14 ? 9.181 6.549 8.069 1.00 24.15 ? 29 TRP B CA 1 ATOM 92 C C . TRP A 1 14 ? 8.651 5.412 8.937 1.00 26.15 ? 29 TRP B C 1 ATOM 93 O O . TRP A 1 14 ? 8.788 4.249 8.583 1.00 24.87 ? 29 TRP B O 1 ATOM 94 C CB . TRP A 1 14 ? 10.683 6.380 7.845 1.00 23.83 ? 29 TRP B CB 1 ATOM 95 C CG . TRP A 1 14 ? 11.486 7.047 8.912 1.00 24.96 ? 29 TRP B CG 1 ATOM 96 C CD1 . TRP A 1 14 ? 11.709 6.594 10.183 1.00 24.91 ? 29 TRP B CD1 1 ATOM 97 C CD2 . TRP A 1 14 ? 12.120 8.321 8.825 1.00 27.37 ? 29 TRP B CD2 1 ATOM 98 N NE1 . TRP A 1 14 ? 12.453 7.506 10.886 1.00 26.30 ? 29 TRP B NE1 1 ATOM 99 C CE2 . TRP A 1 14 ? 12.717 8.577 10.077 1.00 26.53 ? 29 TRP B CE2 1 ATOM 100 C CE3 . TRP A 1 14 ? 12.241 9.274 7.811 1.00 28.57 ? 29 TRP B CE3 1 ATOM 101 C CZ2 . TRP A 1 14 ? 13.439 9.733 10.331 1.00 26.88 ? 29 TRP B CZ2 1 ATOM 102 C CZ3 . TRP A 1 14 ? 12.954 10.427 8.074 1.00 29.68 ? 29 TRP B CZ3 1 ATOM 103 C CH2 . TRP A 1 14 ? 13.543 10.642 9.326 1.00 26.98 ? 29 TRP B CH2 1 ATOM 104 N N . GLN A 1 15 ? 8.051 5.749 10.071 1.00 24.80 ? 30 GLN B N 1 ATOM 105 C CA . GLN A 1 15 ? 7.488 4.757 10.959 1.00 28.03 ? 30 GLN B CA 1 ATOM 106 C C . GLN A 1 15 ? 6.292 4.063 10.333 1.00 26.29 ? 30 GLN B C 1 ATOM 107 O O . GLN A 1 15 ? 5.357 4.719 9.891 1.00 29.91 ? 30 GLN B O 1 ATOM 108 C CB . GLN A 1 15 ? 6.992 5.410 12.236 1.00 32.06 ? 30 GLN B CB 1 ATOM 109 C CG . GLN A 1 15 ? 6.888 4.450 13.385 1.00 32.63 ? 30 GLN B CG 1 ATOM 110 C CD . GLN A 1 15 ? 8.252 4.157 13.958 1.00 38.61 ? 30 GLN B CD 1 ATOM 111 O OE1 . GLN A 1 15 ? 9.172 4.960 13.824 1.00 52.41 ? 30 GLN B OE1 1 ATOM 112 N NE2 . GLN A 1 15 ? 8.392 3.027 14.590 1.00 33.66 ? 30 GLN B NE2 1 ATOM 113 N N . VAL A 1 16 ? 6.302 2.732 10.368 1.00 25.55 ? 31 VAL B N 1 ATOM 114 C CA . VAL A 1 16 ? 5.183 1.928 9.892 1.00 27.23 ? 31 VAL B CA 1 ATOM 115 C C . VAL A 1 16 ? 4.638 1.057 11.026 1.00 25.03 ? 31 VAL B C 1 ATOM 116 O O . VAL A 1 16 ? 5.369 0.659 11.938 1.00 26.28 ? 31 VAL B O 1 ATOM 117 C CB . VAL A 1 16 ? 5.624 1.047 8.711 1.00 29.00 ? 31 VAL B CB 1 ATOM 118 C CG1 . VAL A 1 16 ? 4.492 0.158 8.221 1.00 31.92 ? 31 VAL B CG1 1 ATOM 119 C CG2 . VAL A 1 16 ? 6.163 1.918 7.583 1.00 28.53 ? 31 VAL B CG2 1 ATOM 120 N N . MET A 1 17 ? 3.337 0.821 10.980 1.00 27.25 ? 32 MET B N 1 ATOM 121 C CA . MET A 1 17 ? 2.668 -0.098 11.889 1.00 28.03 ? 32 MET B CA 1 ATOM 122 C C . MET A 1 17 ? 2.211 -1.301 11.080 1.00 26.58 ? 32 MET B C 1 ATOM 123 O O . MET A 1 17 ? 1.472 -1.147 10.116 1.00 28.48 ? 32 MET B O 1 ATOM 124 C CB . MET A 1 17 ? 1.474 0.604 12.531 1.00 28.50 ? 32 MET B CB 1 ATOM 125 C CG . MET A 1 17 ? 0.799 -0.208 13.620 1.00 32.86 ? 32 MET B CG 1 ATOM 126 S SD . MET A 1 17 ? -0.740 0.512 14.239 1.00 33.06 ? 32 MET B SD 1 ATOM 127 C CE . MET A 1 17 ? -0.101 1.867 15.225 1.00 36.96 ? 32 MET B CE 1 ATOM 128 N N . LEU A 1 18 ? 2.685 -2.494 11.441 1.00 26.53 ? 33 LEU B N 1 ATOM 129 C CA . LEU A 1 18 ? 2.141 -3.740 10.917 1.00 31.51 ? 33 LEU B CA 1 ATOM 130 C C . LEU A 1 18 ? 0.934 -4.129 11.750 1.00 31.51 ? 33 LEU B C 1 ATOM 131 O O . LEU A 1 18 ? 0.986 -4.148 12.991 1.00 30.95 ? 33 LEU B O 1 ATOM 132 C CB . LEU A 1 18 ? 3.170 -4.862 10.916 1.00 35.12 ? 33 LEU B CB 1 ATOM 133 C CG . LEU A 1 18 ? 4.479 -4.550 10.187 1.00 42.49 ? 33 LEU B CG 1 ATOM 134 C CD1 . LEU A 1 18 ? 5.251 -5.841 9.912 1.00 45.11 ? 33 LEU B CD1 1 ATOM 135 C CD2 . LEU A 1 18 ? 4.233 -3.773 8.896 1.00 47.08 ? 33 LEU B CD2 1 ATOM 136 N N . PHE A 1 19 ? -0.147 -4.414 11.042 1.00 28.96 ? 34 PHE B N 1 ATOM 137 C CA . PHE A 1 19 ? -1.452 -4.603 11.650 1.00 34.98 ? 34 PHE B CA 1 ATOM 138 C C . PHE A 1 19 ? -2.065 -5.890 11.111 1.00 36.10 ? 34 PHE B C 1 ATOM 139 O O . PHE A 1 19 ? -2.112 -6.103 9.905 1.00 38.29 ? 34 PHE B O 1 ATOM 140 C CB . PHE A 1 19 ? -2.353 -3.408 11.299 1.00 36.02 ? 34 PHE B CB 1 ATOM 141 C CG . PHE A 1 19 ? -3.509 -3.223 12.239 1.00 37.09 ? 34 PHE B CG 1 ATOM 142 C CD1 . PHE A 1 19 ? -3.293 -2.752 13.533 1.00 39.46 ? 34 PHE B CD1 1 ATOM 143 C CD2 . PHE A 1 19 ? -4.799 -3.504 11.841 1.00 42.66 ? 34 PHE B CD2 1 ATOM 144 C CE1 . PHE A 1 19 ? -4.349 -2.579 14.412 1.00 42.04 ? 34 PHE B CE1 1 ATOM 145 C CE2 . PHE A 1 19 ? -5.867 -3.330 12.714 1.00 46.12 ? 34 PHE B CE2 1 ATOM 146 C CZ . PHE A 1 19 ? -5.641 -2.869 14.003 1.00 41.30 ? 34 PHE B CZ 1 ATOM 147 N N . ARG A 1 20 ? -2.550 -6.737 12.004 1.00 36.88 ? 35 ARG B N 1 ATOM 148 C CA . ARG A 1 20 ? -3.216 -7.963 11.590 1.00 41.28 ? 35 ARG B CA 1 ATOM 149 C C . ARG A 1 20 ? -4.677 -7.681 11.246 1.00 43.52 ? 35 ARG B C 1 ATOM 150 O O . ARG A 1 20 ? -5.360 -6.940 11.961 1.00 40.55 ? 35 ARG B O 1 ATOM 151 C CB . ARG A 1 20 ? -3.140 -8.979 12.715 1.00 44.47 ? 35 ARG B CB 1 ATOM 152 C CG . ARG A 1 20 ? -3.504 -10.391 12.323 1.00 46.77 ? 35 ARG B CG 1 ATOM 153 C CD . ARG A 1 20 ? -3.379 -11.268 13.543 1.00 49.13 ? 35 ARG B CD 1 ATOM 154 N NE . ARG A 1 20 ? -3.681 -12.659 13.243 1.00 55.86 ? 35 ARG B NE 1 ATOM 155 C CZ . ARG A 1 20 ? -3.397 -13.677 14.049 1.00 59.91 ? 35 ARG B CZ 1 ATOM 156 N NH1 . ARG A 1 20 ? -2.785 -13.474 15.218 1.00 55.59 ? 35 ARG B NH1 1 ATOM 157 N NH2 . ARG A 1 20 ? -3.723 -14.907 13.678 1.00 62.55 ? 35 ARG B NH2 1 ATOM 158 N N . LYS A 1 21 ? -5.142 -8.277 10.153 1.00 46.15 ? 36 LYS B N 1 ATOM 159 C CA . LYS A 1 21 ? -6.515 -8.090 9.681 1.00 51.66 ? 36 LYS B CA 1 ATOM 160 C C . LYS A 1 21 ? -7.574 -8.715 10.595 1.00 56.75 ? 36 LYS B C 1 ATOM 161 O O . LYS A 1 21 ? -8.597 -8.095 10.874 1.00 57.99 ? 36 LYS B O 1 ATOM 162 C CB . LYS A 1 21 ? -6.677 -8.674 8.280 1.00 53.23 ? 36 LYS B CB 1 ATOM 163 C CG . LYS A 1 21 ? -5.869 -7.979 7.200 1.00 53.35 ? 36 LYS B CG 1 ATOM 164 C CD . LYS A 1 21 ? -6.381 -8.371 5.826 1.00 56.92 ? 36 LYS B CD 1 ATOM 165 C CE . LYS A 1 21 ? -5.410 -7.982 4.729 1.00 57.96 ? 36 LYS B CE 1 ATOM 166 N NZ . LYS A 1 21 ? -5.858 -8.515 3.414 1.00 61.13 ? 36 LYS B NZ 1 ATOM 167 N N . SER A 1 22 A -7.345 -9.949 11.036 1.00 59.89 ? 36 SER B N 1 ATOM 168 C CA . SER A 1 22 A -8.334 -10.669 11.849 1.00 62.48 ? 36 SER B CA 1 ATOM 169 C C . SER A 1 22 A -7.673 -11.775 12.676 1.00 59.93 ? 36 SER B C 1 ATOM 170 O O . SER A 1 22 A -7.068 -12.682 12.116 1.00 59.81 ? 36 SER B O 1 ATOM 171 C CB . SER A 1 22 A -9.428 -11.265 10.963 1.00 69.52 ? 36 SER B CB 1 ATOM 172 O OG . SER A 1 22 A -8.865 -12.081 9.956 1.00 73.53 ? 36 SER B OG 1 ATOM 173 N N . PRO A 1 23 ? -7.745 -11.681 14.014 1.00 63.28 ? 37 PRO B N 1 ATOM 174 C CA . PRO A 1 23 ? -8.324 -10.564 14.751 1.00 63.69 ? 37 PRO B CA 1 ATOM 175 C C . PRO A 1 23 ? -7.500 -9.313 14.501 1.00 60.02 ? 37 PRO B C 1 ATOM 176 O O . PRO A 1 23 ? -6.303 -9.415 14.236 1.00 59.44 ? 37 PRO B O 1 ATOM 177 C CB . PRO A 1 23 ? -8.202 -11.003 16.211 1.00 65.64 ? 37 PRO B CB 1 ATOM 178 C CG . PRO A 1 23 ? -7.028 -11.921 16.230 1.00 64.75 ? 37 PRO B CG 1 ATOM 179 C CD . PRO A 1 23 ? -7.048 -12.627 14.905 1.00 62.72 ? 37 PRO B CD 1 ATOM 180 N N . GLN A 1 24 ? -8.141 -8.152 14.559 1.00 60.79 ? 38 GLN B N 1 ATOM 181 C CA . GLN A 1 24 ? -7.448 -6.884 14.360 1.00 55.56 ? 38 GLN B CA 1 ATOM 182 C C . GLN A 1 24 ? -6.522 -6.622 15.539 1.00 58.95 ? 38 GLN B C 1 ATOM 183 O O . GLN A 1 24 ? -6.982 -6.520 16.681 1.00 56.46 ? 38 GLN B O 1 ATOM 184 C CB . GLN A 1 24 ? -8.453 -5.740 14.200 1.00 57.96 ? 38 GLN B CB 1 ATOM 185 C CG . GLN A 1 24 ? -9.306 -5.874 12.950 1.00 60.54 ? 38 GLN B CG 1 ATOM 186 C CD . GLN A 1 24 ? -10.043 -4.603 12.589 1.00 64.85 ? 38 GLN B CD 1 ATOM 187 O OE1 . GLN A 1 24 ? -11.197 -4.410 12.970 1.00 65.41 ? 38 GLN B OE1 1 ATOM 188 N NE2 . GLN A 1 24 ? -9.381 -3.731 11.843 1.00 60.14 ? 38 GLN B NE2 1 ATOM 189 N N . GLU A 1 25 ? -5.218 -6.544 15.274 1.00 47.24 ? 39 GLU B N 1 ATOM 190 C CA . GLU A 1 25 ? -4.264 -6.285 16.336 1.00 48.10 ? 39 GLU B CA 1 ATOM 191 C C . GLU A 1 25 ? -2.958 -5.712 15.806 1.00 43.85 ? 39 GLU B C 1 ATOM 192 O O . GLU A 1 25 ? -2.531 -5.999 14.687 1.00 36.36 ? 39 GLU B O 1 ATOM 193 C CB . GLU A 1 25 ? -3.995 -7.553 17.160 1.00 52.25 ? 39 GLU B CB 1 ATOM 194 C CG . GLU A 1 25 ? -3.223 -8.643 16.436 1.00 56.46 ? 39 GLU B CG 1 ATOM 195 C CD . GLU A 1 25 ? -3.112 -9.933 17.239 1.00 63.71 ? 39 GLU B CD 1 ATOM 196 O OE1 . GLU A 1 25 ? -1.975 -10.383 17.488 1.00 65.66 ? 39 GLU B OE1 1 ATOM 197 O OE2 . GLU A 1 25 ? -4.156 -10.504 17.624 1.00 68.53 ? 39 GLU B OE2 1 ATOM 198 N N . LEU A 1 26 ? -2.334 -4.887 16.631 1.00 42.86 ? 40 LEU B N 1 ATOM 199 C CA . LEU A 1 26 ? -1.023 -4.358 16.330 1.00 41.02 ? 40 LEU B CA 1 ATOM 200 C C . LEU A 1 26 ? -0.037 -5.505 16.433 1.00 39.84 ? 40 LEU B C 1 ATOM 201 O O . LEU A 1 26 ? -0.050 -6.214 17.418 1.00 41.10 ? 40 LEU B O 1 ATOM 202 C CB . LEU A 1 26 ? -0.685 -3.267 17.335 1.00 43.85 ? 40 LEU B CB 1 ATOM 203 C CG . LEU A 1 26 ? 0.730 -2.694 17.389 1.00 47.71 ? 40 LEU B CG 1 ATOM 204 C CD1 . LEU A 1 26 ? 1.327 -2.475 16.014 1.00 51.90 ? 40 LEU B CD1 1 ATOM 205 C CD2 . LEU A 1 26 ? 0.681 -1.394 18.177 1.00 53.17 ? 40 LEU B CD2 1 ATOM 206 N N . LEU A 1 27 ? 0.793 -5.699 15.410 1.00 38.18 ? 41 LEU B N 1 ATOM 207 C CA . LEU A 1 27 ? 1.786 -6.780 15.415 1.00 38.08 ? 41 LEU B CA 1 ATOM 208 C C . LEU A 1 27 ? 3.182 -6.313 15.754 1.00 37.80 ? 41 LEU B C 1 ATOM 209 O O . LEU A 1 27 ? 3.842 -6.901 16.609 1.00 38.20 ? 41 LEU B O 1 ATOM 210 C CB . LEU A 1 27 ? 1.834 -7.470 14.051 1.00 42.00 ? 41 LEU B CB 1 ATOM 211 C CG . LEU A 1 27 ? 0.626 -8.348 13.752 1.00 45.27 ? 41 LEU B CG 1 ATOM 212 C CD1 . LEU A 1 27 ? 0.667 -8.805 12.307 1.00 46.86 ? 41 LEU B CD1 1 ATOM 213 C CD2 . LEU A 1 27 ? 0.556 -9.531 14.710 1.00 46.87 ? 41 LEU B CD2 1 ATOM 214 N N . CYS A 1 28 ? 3.622 -5.257 15.072 1.00 33.58 ? 42 CYS B N 1 ATOM 215 C CA A CYS A 1 28 ? 5.011 -4.816 15.094 0.49 35.24 ? 42 CYS B CA 1 ATOM 216 C CA B CYS A 1 28 ? 4.942 -4.695 15.314 0.51 31.53 ? 42 CYS B CA 1 ATOM 217 C C . CYS A 1 28 ? 5.163 -3.411 14.515 1.00 30.26 ? 42 CYS B C 1 ATOM 218 O O . CYS A 1 28 ? 4.227 -2.869 13.890 1.00 28.11 ? 42 CYS B O 1 ATOM 219 C CB A CYS A 1 28 ? 5.855 -5.747 14.209 0.49 37.50 ? 42 CYS B CB 1 ATOM 220 C CB B CYS A 1 28 ? 6.022 -5.705 14.952 0.51 29.52 ? 42 CYS B CB 1 ATOM 221 S SG A CYS A 1 28 ? 6.611 -7.185 14.982 0.49 44.72 ? 42 CYS B SG 1 ATOM 222 S SG B CYS A 1 28 ? 6.052 -6.035 13.191 0.51 28.25 ? 42 CYS B SG 1 ATOM 223 N N . GLY A 1 29 ? 6.385 -2.898 14.628 1.00 25.30 ? 43 GLY B N 1 ATOM 224 C CA . GLY A 1 29 ? 6.839 -1.728 13.924 1.00 26.23 ? 43 GLY B CA 1 ATOM 225 C C . GLY A 1 29 ? 7.555 -2.143 12.649 1.00 24.44 ? 43 GLY B C 1 ATOM 226 O O . GLY A 1 29 ? 7.774 -3.316 12.399 1.00 24.14 ? 43 GLY B O 1 ATOM 227 N N . ALA A 1 30 ? 7.903 -1.148 11.855 1.00 26.72 ? 44 ALA B N 1 ATOM 228 C CA . ALA A 1 30 ? 8.558 -1.328 10.562 1.00 24.76 ? 44 ALA B CA 1 ATOM 229 C C . ALA A 1 30 ? 8.981 0.069 10.080 1.00 25.77 ? 44 ALA B C 1 ATOM 230 O O . ALA A 1 30 ? 8.611 1.087 10.696 1.00 23.29 ? 44 ALA B O 1 ATOM 231 C CB . ALA A 1 30 ? 7.603 -1.980 9.584 1.00 27.73 ? 44 ALA B CB 1 ATOM 232 N N . SER A 1 31 ? 9.751 0.141 8.994 1.00 24.03 ? 45 SER B N 1 ATOM 233 C CA . SER A 1 31 ? 10.163 1.426 8.477 1.00 26.55 ? 45 SER B CA 1 ATOM 234 C C . SER A 1 31 ? 9.934 1.527 6.961 1.00 25.49 ? 45 SER B C 1 ATOM 235 O O . SER A 1 31 ? 10.052 0.528 6.246 1.00 25.42 ? 45 SER B O 1 ATOM 236 C CB . SER A 1 31 ? 11.621 1.659 8.793 1.00 28.29 ? 45 SER B CB 1 ATOM 237 O OG . SER A 1 31 ? 12.411 0.697 8.132 1.00 32.89 ? 45 SER B OG 1 ATOM 238 N N . LEU A 1 32 ? 9.622 2.731 6.488 1.00 23.86 ? 46 LEU B N 1 ATOM 239 C CA . LEU A 1 32 ? 9.434 2.988 5.066 1.00 24.95 ? 46 LEU B CA 1 ATOM 240 C C . LEU A 1 32 ? 10.764 3.372 4.456 1.00 25.56 ? 46 LEU B C 1 ATOM 241 O O . LEU A 1 32 ? 11.385 4.320 4.917 1.00 26.21 ? 46 LEU B O 1 ATOM 242 C CB . LEU A 1 32 ? 8.457 4.150 4.883 1.00 26.73 ? 46 LEU B CB 1 ATOM 243 C CG . LEU A 1 32 ? 7.976 4.392 3.454 1.00 29.53 ? 46 LEU B CG 1 ATOM 244 C CD1 . LEU A 1 32 ? 7.028 3.298 3.006 1.00 28.99 ? 46 LEU B CD1 1 ATOM 245 C CD2 . LEU A 1 32 ? 7.321 5.759 3.341 1.00 34.23 ? 46 LEU B CD2 1 ATOM 246 N N . ILE A 1 33 ? 11.200 2.652 3.426 1.00 25.75 ? 47 ILE B N 1 ATOM 247 C CA . ILE A 1 33 ? 12.498 2.946 2.782 1.00 26.51 ? 47 ILE B CA 1 ATOM 248 C C . ILE A 1 33 ? 12.357 3.456 1.349 1.00 29.38 ? 47 ILE B C 1 ATOM 249 O O . ILE A 1 33 ? 13.330 3.915 0.745 1.00 31.49 ? 47 ILE B O 1 ATOM 250 C CB . ILE A 1 33 ? 13.478 1.744 2.855 1.00 27.72 ? 47 ILE B CB 1 ATOM 251 C CG1 . ILE A 1 33 ? 12.916 0.487 2.178 1.00 28.55 ? 47 ILE B CG1 1 ATOM 252 C CG2 . ILE A 1 33 ? 13.833 1.440 4.317 1.00 28.44 ? 47 ILE B CG2 1 ATOM 253 C CD1 . ILE A 1 33 ? 13.882 -0.687 2.097 1.00 29.16 ? 47 ILE B CD1 1 ATOM 254 N N . SER A 1 34 ? 11.146 3.370 0.807 1.00 27.81 ? 48 SER B N 1 ATOM 255 C CA . SER A 1 34 ? 10.823 3.960 -0.472 1.00 30.06 ? 48 SER B CA 1 ATOM 256 C C . SER A 1 34 ? 9.314 4.045 -0.523 1.00 31.21 ? 48 SER B C 1 ATOM 257 O O . SER A 1 34 ? 8.649 3.788 0.484 1.00 32.12 ? 48 SER B O 1 ATOM 258 C CB . SER A 1 34 ? 11.371 3.121 -1.619 1.00 31.89 ? 48 SER B CB 1 ATOM 259 O OG . SER A 1 34 ? 10.625 1.927 -1.791 1.00 30.62 ? 48 SER B OG 1 ATOM 260 N N . ASP A 1 35 ? 8.768 4.430 -1.669 1.00 33.06 ? 49 ASP B N 1 ATOM 261 C CA . ASP A 1 35 ? 7.318 4.533 -1.817 1.00 35.99 ? 49 ASP B CA 1 ATOM 262 C C . ASP A 1 35 ? 6.633 3.163 -1.801 1.00 36.23 ? 49 ASP B C 1 ATOM 263 O O . ASP A 1 35 ? 5.419 3.091 -1.658 1.00 36.64 ? 49 ASP B O 1 ATOM 264 C CB . ASP A 1 35 ? 6.941 5.293 -3.097 1.00 40.22 ? 49 ASP B CB 1 ATOM 265 C CG . ASP A 1 35 ? 7.443 4.609 -4.356 1.00 42.53 ? 49 ASP B CG 1 ATOM 266 O OD1 . ASP A 1 35 ? 8.125 3.569 -4.263 1.00 42.25 ? 49 ASP B OD1 1 ATOM 267 O OD2 . ASP A 1 35 ? 7.161 5.110 -5.450 1.00 46.63 ? 49 ASP B OD2 1 ATOM 268 N N . ARG A 1 36 ? 7.398 2.082 -1.956 1.00 35.59 ? 50 ARG B N 1 ATOM 269 C CA . ARG A 1 36 ? 6.795 0.753 -2.049 1.00 34.12 ? 50 ARG B CA 1 ATOM 270 C C . ARG A 1 36 ? 7.515 -0.369 -1.321 1.00 30.76 ? 50 ARG B C 1 ATOM 271 O O . ARG A 1 36 ? 7.097 -1.513 -1.440 1.00 30.12 ? 50 ARG B O 1 ATOM 272 C CB . ARG A 1 36 ? 6.611 0.384 -3.524 1.00 36.55 ? 50 ARG B CB 1 ATOM 273 C CG . ARG A 1 36 ? 7.869 -0.107 -4.221 1.00 37.84 ? 50 ARG B CG 1 ATOM 274 C CD . ARG A 1 36 ? 7.697 -0.064 -5.733 0.92 38.49 ? 50 ARG B CD 1 ATOM 275 N NE . ARG A 1 36 ? 7.438 1.305 -6.173 1.00 41.71 ? 50 ARG B NE 1 ATOM 276 C CZ . ARG A 1 36 ? 7.053 1.668 -7.391 0.63 42.53 ? 50 ARG B CZ 1 ATOM 277 N NH1 . ARG A 1 36 ? 6.863 0.766 -8.347 0.98 44.76 ? 50 ARG B NH1 1 ATOM 278 N NH2 . ARG A 1 36 ? 6.857 2.953 -7.647 1.00 42.81 ? 50 ARG B NH2 1 ATOM 279 N N . TRP A 1 37 ? 8.550 -0.050 -0.542 1.00 30.49 ? 51 TRP B N 1 ATOM 280 C CA . TRP A 1 37 ? 9.268 -1.047 0.235 1.00 31.80 ? 51 TRP B CA 1 ATOM 281 C C . TRP A 1 37 ? 9.279 -0.699 1.715 1.00 30.88 ? 51 TRP B C 1 ATOM 282 O O . TRP A 1 37 ? 9.536 0.442 2.111 1.00 27.36 ? 51 TRP B O 1 ATOM 283 C CB . TRP A 1 37 ? 10.707 -1.207 -0.256 1.00 29.83 ? 51 TRP B CB 1 ATOM 284 C CG . TRP A 1 37 ? 10.800 -1.956 -1.549 1.00 31.31 ? 51 TRP B CG 1 ATOM 285 C CD1 . TRP A 1 37 ? 10.921 -1.421 -2.801 1.00 34.44 ? 51 TRP B CD1 1 ATOM 286 C CD2 . TRP A 1 37 ? 10.773 -3.379 -1.720 1.00 32.22 ? 51 TRP B CD2 1 ATOM 287 N NE1 . TRP A 1 37 ? 10.983 -2.431 -3.748 1.00 35.40 ? 51 TRP B NE1 1 ATOM 288 C CE2 . TRP A 1 37 ? 10.901 -3.641 -3.110 1.00 33.78 ? 51 TRP B CE2 1 ATOM 289 C CE3 . TRP A 1 37 ? 10.664 -4.457 -0.839 1.00 31.83 ? 51 TRP B CE3 1 ATOM 290 C CZ2 . TRP A 1 37 ? 10.913 -4.941 -3.634 1.00 34.76 ? 51 TRP B CZ2 1 ATOM 291 C CZ3 . TRP A 1 37 ? 10.689 -5.755 -1.359 1.00 34.44 ? 51 TRP B CZ3 1 ATOM 292 C CH2 . TRP A 1 37 ? 10.802 -5.981 -2.751 1.00 34.76 ? 51 TRP B CH2 1 ATOM 293 N N . VAL A 1 38 ? 9.013 -1.718 2.512 1.00 30.00 ? 52 VAL B N 1 ATOM 294 C CA . VAL A 1 38 ? 9.016 -1.607 3.958 1.00 29.35 ? 52 VAL B CA 1 ATOM 295 C C . VAL A 1 38 ? 9.962 -2.623 4.560 1.00 28.39 ? 52 VAL B C 1 ATOM 296 O O . VAL A 1 38 ? 9.998 -3.792 4.151 1.00 35.79 ? 52 VAL B O 1 ATOM 297 C CB . VAL A 1 38 ? 7.584 -1.785 4.503 1.00 28.96 ? 52 VAL B CB 1 ATOM 298 C CG1 . VAL A 1 38 ? 7.584 -1.886 6.022 1.00 26.06 ? 52 VAL B CG1 1 ATOM 299 C CG2 . VAL A 1 38 ? 6.748 -0.611 4.053 1.00 29.70 ? 52 VAL B CG2 1 ATOM 300 N N . LEU A 1 39 ? 10.720 -2.167 5.555 1.00 30.26 ? 53 LEU B N 1 ATOM 301 C CA . LEU A 1 39 ? 11.716 -2.984 6.224 1.00 31.26 ? 53 LEU B CA 1 ATOM 302 C C . LEU A 1 39 ? 11.231 -3.271 7.649 1.00 29.22 ? 53 LEU B C 1 ATOM 303 O O . LEU A 1 39 ? 10.655 -2.395 8.320 1.00 26.69 ? 53 LEU B O 1 ATOM 304 C CB . LEU A 1 39 ? 13.049 -2.234 6.221 1.00 31.15 ? 53 LEU B CB 1 ATOM 305 C CG . LEU A 1 39 ? 14.277 -2.890 6.833 1.00 35.92 ? 53 LEU B CG 1 ATOM 306 C CD1 . LEU A 1 39 ? 14.647 -4.179 6.106 1.00 33.91 ? 53 LEU B CD1 1 ATOM 307 C CD2 . LEU A 1 39 ? 15.429 -1.893 6.815 1.00 34.66 ? 53 LEU B CD2 1 ATOM 308 N N . THR A 1 40 ? 11.409 -4.512 8.087 1.00 27.50 ? 54 THR B N 1 ATOM 309 C CA . THR A 1 40 ? 11.016 -4.904 9.442 1.00 27.06 ? 54 THR B CA 1 ATOM 310 C C . THR A 1 40 ? 11.878 -6.084 9.894 1.00 29.13 ? 54 THR B C 1 ATOM 311 O O . THR A 1 40 ? 12.835 -6.460 9.217 1.00 25.92 ? 54 THR B O 1 ATOM 312 C CB . THR A 1 40 ? 9.503 -5.257 9.492 1.00 29.21 ? 54 THR B CB 1 ATOM 313 O OG1 . THR A 1 40 ? 9.039 -5.408 10.848 1.00 27.31 ? 54 THR B OG1 1 ATOM 314 C CG2 . THR A 1 40 ? 9.201 -6.508 8.701 1.00 30.59 ? 54 THR B CG2 1 ATOM 315 N N . ALA A 1 41 ? 11.538 -6.643 11.046 1.00 27.74 ? 55 ALA B N 1 ATOM 316 C CA . ALA A 1 41 ? 12.245 -7.786 11.595 1.00 29.78 ? 55 ALA B CA 1 ATOM 317 C C . ALA A 1 41 ? 11.555 -9.007 11.057 1.00 26.79 ? 55 ALA B C 1 ATOM 318 O O . ALA A 1 41 ? 10.344 -8.996 10.844 1.00 30.32 ? 55 ALA B O 1 ATOM 319 C CB . ALA A 1 41 ? 12.205 -7.770 13.118 1.00 29.00 ? 55 ALA B CB 1 ATOM 320 N N . ALA A 1 42 ? 12.320 -10.064 10.834 1.00 26.53 ? 56 ALA B N 1 ATOM 321 C CA . ALA A 1 42 ? 11.747 -11.336 10.446 1.00 29.54 ? 56 ALA B CA 1 ATOM 322 C C . ALA A 1 42 ? 10.819 -11.926 11.504 1.00 27.60 ? 56 ALA B C 1 ATOM 323 O O . ALA A 1 42 ? 9.801 -12.495 11.155 1.00 27.09 ? 56 ALA B O 1 ATOM 324 C CB . ALA A 1 42 ? 12.843 -12.333 10.113 1.00 28.51 ? 56 ALA B CB 1 ATOM 325 N N . HIS A 1 43 ? 11.164 -11.811 12.783 1.00 27.53 ? 57 HIS B N 1 ATOM 326 C CA . HIS A 1 43 ? 10.388 -12.502 13.816 1.00 29.73 ? 57 HIS B CA 1 ATOM 327 C C . HIS A 1 43 ? 8.969 -11.958 14.051 1.00 31.52 ? 57 HIS B C 1 ATOM 328 O O . HIS A 1 43 ? 8.125 -12.638 14.666 1.00 32.49 ? 57 HIS B O 1 ATOM 329 C CB . HIS A 1 43 ? 11.175 -12.646 15.130 1.00 29.71 ? 57 HIS B CB 1 ATOM 330 C CG . HIS A 1 43 ? 10.997 -11.524 16.102 1.00 28.90 ? 57 HIS B CG 1 ATOM 331 N ND1 . HIS A 1 43 ? 11.973 -10.578 16.326 1.00 28.79 ? 57 HIS B ND1 1 ATOM 332 C CD2 . HIS A 1 43 ? 9.986 -11.234 16.961 1.00 31.44 ? 57 HIS B CD2 1 ATOM 333 C CE1 . HIS A 1 43 ? 11.563 -9.746 17.265 1.00 27.87 ? 57 HIS B CE1 1 ATOM 334 N NE2 . HIS A 1 43 ? 10.351 -10.111 17.657 1.00 33.90 ? 57 HIS B NE2 1 ATOM 335 N N . CYS A 1 44 ? 8.734 -10.745 13.577 1.00 32.27 ? 58 CYS B N 1 ATOM 336 C CA A CYS A 1 44 ? 7.394 -10.170 13.446 0.53 37.18 ? 58 CYS B CA 1 ATOM 337 C CA B CYS A 1 44 ? 7.371 -10.208 13.539 0.47 34.96 ? 58 CYS B CA 1 ATOM 338 C C . CYS A 1 44 ? 6.469 -11.050 12.638 1.00 36.70 ? 58 CYS B C 1 ATOM 339 O O . CYS A 1 44 ? 5.278 -11.207 12.940 1.00 37.32 ? 58 CYS B O 1 ATOM 340 C CB A CYS A 1 44 ? 7.513 -8.853 12.694 0.53 40.29 ? 58 CYS B CB 1 ATOM 341 C CB B CYS A 1 44 ? 7.347 -8.754 13.064 0.47 34.88 ? 58 CYS B CB 1 ATOM 342 S SG A CYS A 1 44 ? 8.181 -7.569 13.738 0.53 47.27 ? 58 CYS B SG 1 ATOM 343 S SG B CYS A 1 44 ? 5.685 -8.025 13.112 0.47 36.11 ? 58 CYS B SG 1 ATOM 344 N N . LEU A 1 45 ? 7.044 -11.588 11.566 1.00 35.31 ? 59 LEU B N 1 ATOM 345 C CA . LEU A 1 45 ? 6.332 -12.348 10.547 1.00 35.66 ? 59 LEU B CA 1 ATOM 346 C C . LEU A 1 45 ? 6.491 -13.866 10.656 1.00 33.58 ? 59 LEU B C 1 ATOM 347 O O . LEU A 1 45 ? 5.584 -14.600 10.296 1.00 33.83 ? 59 LEU B O 1 ATOM 348 C CB . LEU A 1 45 ? 6.831 -11.899 9.177 1.00 36.68 ? 59 LEU B CB 1 ATOM 349 C CG . LEU A 1 45 ? 6.773 -10.383 8.907 1.00 38.32 ? 59 LEU B CG 1 ATOM 350 C CD1 . LEU A 1 45 ? 7.489 -10.005 7.618 1.00 37.15 ? 59 LEU B CD1 1 ATOM 351 C CD2 . LEU A 1 45 ? 5.333 -9.913 8.855 1.00 41.42 ? 59 LEU B CD2 1 ATOM 352 N N . LEU A 1 46 ? 7.656 -14.322 11.124 1.00 34.47 ? 60 LEU B N 1 ATOM 353 C CA . LEU A 1 46 ? 7.969 -15.750 11.246 1.00 33.56 ? 60 LEU B CA 1 ATOM 354 C C . LEU A 1 46 ? 8.604 -16.042 12.614 1.00 31.45 ? 60 LEU B C 1 ATOM 355 O O . LEU A 1 46 ? 9.772 -15.729 12.861 1.00 28.45 ? 60 LEU B O 1 ATOM 356 C CB . LEU A 1 46 ? 8.900 -16.203 10.123 1.00 35.97 ? 60 LEU B CB 1 ATOM 357 C CG . LEU A 1 46 ? 9.301 -17.687 10.135 1.00 38.48 ? 60 LEU B CG 1 ATOM 358 C CD1 . LEU A 1 46 ? 8.066 -18.578 10.144 1.00 40.30 ? 60 LEU B CD1 1 ATOM 359 C CD2 . LEU A 1 46 ? 10.204 -18.040 8.959 1.00 40.63 ? 60 LEU B CD2 1 ATOM 360 N N . TYR A 1 47 A 7.809 -16.621 13.506 1.00 32.95 ? 60 TYR B N 1 ATOM 361 C CA . TYR A 1 47 A 8.305 -17.103 14.787 1.00 33.38 ? 60 TYR B CA 1 ATOM 362 C C . TYR A 1 47 A 7.352 -18.206 15.243 1.00 36.09 ? 60 TYR B C 1 ATOM 363 O O . TYR A 1 47 A 6.388 -17.960 15.972 1.00 35.07 ? 60 TYR B O 1 ATOM 364 C CB . TYR A 1 47 A 8.474 -15.972 15.813 1.00 32.95 ? 60 TYR B CB 1 ATOM 365 C CG . TYR A 1 47 A 9.340 -16.402 16.989 1.00 33.24 ? 60 TYR B CG 1 ATOM 366 C CD1 . TYR A 1 47 A 10.720 -16.579 16.837 1.00 32.57 ? 60 TYR B CD1 1 ATOM 367 C CD2 . TYR A 1 47 A 8.774 -16.682 18.238 1.00 32.75 ? 60 TYR B CD2 1 ATOM 368 C CE1 . TYR A 1 47 A 11.513 -17.002 17.895 1.00 32.69 ? 60 TYR B CE1 1 ATOM 369 C CE2 . TYR A 1 47 A 9.561 -17.122 19.303 1.00 35.65 ? 60 TYR B CE2 1 ATOM 370 C CZ . TYR A 1 47 A 10.931 -17.279 19.126 1.00 34.90 ? 60 TYR B CZ 1 ATOM 371 O OH . TYR A 1 47 A 11.719 -17.711 20.179 1.00 37.57 ? 60 TYR B OH 1 ATOM 372 N N . PRO A 1 48 B 7.610 -19.447 14.783 1.00 38.75 ? 60 PRO B N 1 ATOM 373 C CA . PRO A 1 48 B 6.655 -20.526 14.990 1.00 39.69 ? 60 PRO B CA 1 ATOM 374 C C . PRO A 1 48 B 6.277 -20.834 16.449 1.00 41.19 ? 60 PRO B C 1 ATOM 375 O O . PRO A 1 48 B 5.135 -21.218 16.699 1.00 39.73 ? 60 PRO B O 1 ATOM 376 C CB . PRO A 1 48 B 7.347 -21.738 14.339 1.00 42.96 ? 60 PRO B CB 1 ATOM 377 C CG . PRO A 1 48 B 8.205 -21.126 13.283 1.00 41.45 ? 60 PRO B CG 1 ATOM 378 C CD . PRO A 1 48 B 8.718 -19.862 13.899 1.00 38.25 ? 60 PRO B CD 1 ATOM 379 N N . PRO A 1 49 C 7.211 -20.672 17.397 1.00 37.10 ? 60 PRO B N 1 ATOM 380 C CA . PRO A 1 49 C 6.811 -20.858 18.789 1.00 40.32 ? 60 PRO B CA 1 ATOM 381 C C . PRO A 1 49 C 5.684 -19.921 19.249 1.00 41.31 ? 60 PRO B C 1 ATOM 382 O O . PRO A 1 49 C 4.900 -20.303 20.111 1.00 44.71 ? 60 PRO B O 1 ATOM 383 C CB . PRO A 1 49 C 8.102 -20.592 19.568 1.00 39.27 ? 60 PRO B CB 1 ATOM 384 C CG . PRO A 1 49 C 9.194 -20.888 18.602 1.00 40.19 ? 60 PRO B CG 1 ATOM 385 C CD . PRO A 1 49 C 8.658 -20.434 17.271 1.00 38.84 ? 60 PRO B CD 1 ATOM 386 N N . TRP A 1 50 D 5.588 -18.726 18.673 1.00 39.37 ? 60 TRP B N 1 ATOM 387 C CA . TRP A 1 50 D 4.483 -17.815 18.982 1.00 39.95 ? 60 TRP B CA 1 ATOM 388 C C . TRP A 1 50 D 3.362 -17.842 17.917 1.00 43.07 ? 60 TRP B C 1 ATOM 389 O O . TRP A 1 50 D 2.537 -16.925 17.849 1.00 41.94 ? 60 TRP B O 1 ATOM 390 C CB . TRP A 1 50 D 5.004 -16.395 19.176 1.00 36.98 ? 60 TRP B CB 1 ATOM 391 C CG . TRP A 1 50 D 5.971 -16.216 20.317 1.00 34.73 ? 60 TRP B CG 1 ATOM 392 C CD1 . TRP A 1 50 D 6.358 -17.157 21.234 1.00 37.08 ? 60 TRP B CD1 1 ATOM 393 C CD2 . TRP A 1 50 D 6.645 -15.010 20.681 1.00 36.45 ? 60 TRP B CD2 1 ATOM 394 N NE1 . TRP A 1 50 D 7.241 -16.614 22.129 1.00 37.33 ? 60 TRP B NE1 1 ATOM 395 C CE2 . TRP A 1 50 D 7.428 -15.295 21.825 1.00 34.01 ? 60 TRP B CE2 1 ATOM 396 C CE3 . TRP A 1 50 D 6.670 -13.709 20.152 1.00 35.43 ? 60 TRP B CE3 1 ATOM 397 C CZ2 . TRP A 1 50 D 8.229 -14.329 22.443 1.00 37.47 ? 60 TRP B CZ2 1 ATOM 398 C CZ3 . TRP A 1 50 D 7.461 -12.754 20.771 1.00 34.27 ? 60 TRP B CZ3 1 ATOM 399 C CH2 . TRP A 1 50 D 8.236 -13.072 21.904 1.00 35.50 ? 60 TRP B CH2 1 ATOM 400 N N . ASP A 1 51 E 3.312 -18.902 17.114 1.00 45.51 ? 60 ASP B N 1 ATOM 401 C CA . ASP A 1 51 E 2.294 -19.046 16.068 1.00 54.87 ? 60 ASP B CA 1 ATOM 402 C C . ASP A 1 51 E 2.276 -17.880 15.100 1.00 51.03 ? 60 ASP B C 1 ATOM 403 O O . ASP A 1 51 E 1.219 -17.386 14.715 1.00 57.91 ? 60 ASP B O 1 ATOM 404 C CB . ASP A 1 51 E 0.900 -19.256 16.681 1.00 60.54 ? 60 ASP B CB 1 ATOM 405 C CG . ASP A 1 51 E 0.499 -20.701 16.699 1.00 66.64 ? 60 ASP B CG 1 ATOM 406 O OD1 . ASP A 1 51 E 1.252 -21.511 17.270 1.00 68.79 ? 60 ASP B OD1 1 ATOM 407 O OD2 . ASP A 1 51 E -0.565 -21.028 16.131 1.00 86.35 ? 60 ASP B OD2 1 ATOM 408 N N . LYS A 1 52 F 3.460 -17.430 14.719 1.00 49.42 ? 60 LYS B N 1 ATOM 409 C CA . LYS A 1 52 F 3.581 -16.394 13.714 1.00 46.39 ? 60 LYS B CA 1 ATOM 410 C C . LYS A 1 52 F 4.183 -17.034 12.479 1.00 44.59 ? 60 LYS B C 1 ATOM 411 O O . LYS A 1 52 F 5.334 -17.480 12.495 1.00 41.85 ? 60 LYS B O 1 ATOM 412 C CB . LYS A 1 52 F 4.456 -15.246 14.218 1.00 45.86 ? 60 LYS B CB 1 ATOM 413 C CG . LYS A 1 52 F 3.822 -14.428 15.333 1.00 51.90 ? 60 LYS B CG 1 ATOM 414 C CD . LYS A 1 52 F 4.832 -13.460 15.939 1.00 54.55 ? 60 LYS B CD 1 ATOM 415 C CE . LYS A 1 52 F 4.258 -12.748 17.158 1.00 59.68 ? 60 LYS B CE 1 ATOM 416 N NZ . LYS A 1 52 F 3.096 -11.868 16.834 1.00 58.04 ? 60 LYS B NZ 1 ATOM 417 N N . ASN A 1 53 G 3.368 -17.121 11.434 1.00 47.54 ? 60 ASN B N 1 ATOM 418 C CA . ASN A 1 53 G 3.831 -17.438 10.087 1.00 51.11 ? 60 ASN B CA 1 ATOM 419 C C . ASN A 1 53 G 2.867 -16.775 9.106 1.00 47.27 ? 60 ASN B C 1 ATOM 420 O O . ASN A 1 53 G 2.062 -17.431 8.457 1.00 48.11 ? 60 ASN B O 1 ATOM 421 C CB . ASN A 1 53 G 3.914 -18.953 9.861 1.00 59.13 ? 60 ASN B CB 1 ATOM 422 C CG . ASN A 1 53 G 4.682 -19.325 8.591 1.00 67.92 ? 60 ASN B CG 1 ATOM 423 O OD1 . ASN A 1 53 G 5.056 -18.462 7.786 1.00 63.99 ? 60 ASN B OD1 1 ATOM 424 N ND2 . ASN A 1 53 G 4.918 -20.636 8.410 1.00 74.20 ? 60 ASN B ND2 1 ATOM 425 N N . PHE A 1 54 H 2.951 -15.452 9.023 1.00 48.86 ? 60 PHE B N 1 ATOM 426 C CA . PHE A 1 54 H 1.971 -14.687 8.274 1.00 47.50 ? 60 PHE B CA 1 ATOM 427 C C . PHE A 1 54 H 2.295 -14.704 6.786 1.00 50.33 ? 60 PHE B C 1 ATOM 428 O O . PHE A 1 54 H 3.461 -14.724 6.391 1.00 49.95 ? 60 PHE B O 1 ATOM 429 C CB . PHE A 1 54 H 1.897 -13.250 8.781 1.00 42.46 ? 60 PHE B CB 1 ATOM 430 C CG . PHE A 1 54 H 1.419 -13.131 10.199 1.00 41.13 ? 60 PHE B CG 1 ATOM 431 C CD1 . PHE A 1 54 H 0.104 -13.435 10.529 1.00 46.21 ? 60 PHE B CD1 1 ATOM 432 C CD2 . PHE A 1 54 H 2.276 -12.693 11.203 1.00 41.07 ? 60 PHE B CD2 1 ATOM 433 C CE1 . PHE A 1 54 H -0.344 -13.322 11.837 1.00 46.17 ? 60 PHE B CE1 1 ATOM 434 C CE2 . PHE A 1 54 H 1.838 -12.584 12.513 1.00 41.22 ? 60 PHE B CE2 1 ATOM 435 C CZ . PHE A 1 54 H 0.525 -12.901 12.831 1.00 44.62 ? 60 PHE B CZ 1 ATOM 436 N N . THR A 1 55 I 1.242 -14.731 5.977 1.00 52.15 ? 60 THR B N 1 ATOM 437 C CA . THR A 1 55 I 1.361 -14.528 4.550 1.00 54.27 ? 60 THR B CA 1 ATOM 438 C C . THR A 1 55 I 1.009 -13.081 4.241 1.00 51.46 ? 60 THR B C 1 ATOM 439 O O . THR A 1 55 I 0.532 -12.340 5.100 1.00 47.77 ? 60 THR B O 1 ATOM 440 C CB . THR A 1 55 I 0.418 -15.454 3.775 1.00 56.88 ? 60 THR B CB 1 ATOM 441 O OG1 . THR A 1 55 I -0.927 -15.262 4.234 1.00 59.04 ? 60 THR B OG1 1 ATOM 442 C CG2 . THR A 1 55 I 0.819 -16.896 3.987 1.00 62.94 ? 60 THR B CG2 1 ATOM 443 N N . GLU A 1 56 ? 1.236 -12.705 2.994 1.00 50.08 ? 61 GLU B N 1 ATOM 444 C CA . GLU A 1 56 ? 0.946 -11.369 2.501 1.00 49.86 ? 61 GLU B CA 1 ATOM 445 C C . GLU A 1 56 ? -0.490 -10.967 2.858 1.00 49.53 ? 61 GLU B C 1 ATOM 446 O O . GLU A 1 56 ? -0.743 -9.831 3.247 1.00 46.94 ? 61 GLU B O 1 ATOM 447 C CB . GLU A 1 56 ? 1.143 -11.330 0.980 1.00 56.42 ? 61 GLU B CB 1 ATOM 448 C CG . GLU A 1 56 ? 2.588 -11.499 0.503 1.00 56.45 ? 61 GLU B CG 1 ATOM 449 C CD . GLU A 1 56 ? 3.178 -12.902 0.695 1.00 56.55 ? 61 GLU B CD 1 ATOM 450 O OE1 . GLU A 1 56 ? 2.423 -13.887 0.846 1.00 59.75 ? 61 GLU B OE1 1 ATOM 451 O OE2 . GLU A 1 56 ? 4.413 -13.029 0.684 1.00 51.07 ? 61 GLU B OE2 1 ATOM 452 N N . ASN A 1 57 ? -1.418 -11.914 2.746 1.00 49.70 ? 62 ASN B N 1 ATOM 453 C CA . ASN A 1 57 ? -2.841 -11.633 2.929 1.00 53.75 ? 62 ASN B CA 1 ATOM 454 C C . ASN A 1 57 ? -3.347 -11.461 4.365 1.00 52.31 ? 62 ASN B C 1 ATOM 455 O O . ASN A 1 57 ? -4.486 -11.044 4.560 1.00 49.26 ? 62 ASN B O 1 ATOM 456 C CB . ASN A 1 57 ? -3.675 -12.710 2.236 1.00 63.82 ? 62 ASN B CB 1 ATOM 457 C CG . ASN A 1 57 ? -3.878 -12.422 0.765 1.00 72.18 ? 62 ASN B CG 1 ATOM 458 O OD1 . ASN A 1 57 ? -2.929 -12.425 -0.021 1.00 79.11 ? 62 ASN B OD1 1 ATOM 459 N ND2 . ASN A 1 57 ? -5.122 -12.163 0.384 1.00 78.63 ? 62 ASN B ND2 1 ATOM 460 N N . ASP A 1 58 ? -2.528 -11.770 5.366 1.00 49.07 ? 63 ASP B N 1 ATOM 461 C CA . ASP A 1 58 ? -2.964 -11.661 6.760 1.00 47.71 ? 63 ASP B CA 1 ATOM 462 C C . ASP A 1 58 ? -2.777 -10.249 7.304 1.00 47.67 ? 63 ASP B C 1 ATOM 463 O O . ASP A 1 58 ? -3.330 -9.910 8.352 1.00 45.45 ? 63 ASP B O 1 ATOM 464 C CB . ASP A 1 58 ? -2.175 -12.636 7.644 1.00 47.32 ? 63 ASP B CB 1 ATOM 465 C CG . ASP A 1 58 ? -2.383 -14.091 7.252 1.00 52.48 ? 63 ASP B CG 1 ATOM 466 O OD1 . ASP A 1 58 ? -3.533 -14.465 6.921 1.00 49.63 ? 63 ASP B OD1 1 ATOM 467 O OD2 . ASP A 1 58 ? -1.394 -14.863 7.296 1.00 51.18 ? 63 ASP B OD2 1 ATOM 468 N N . LEU A 1 59 ? -1.999 -9.434 6.588 1.00 45.60 ? 64 LEU B N 1 ATOM 469 C CA . LEU A 1 59 ? -1.446 -8.206 7.141 1.00 44.44 ? 64 LEU B CA 1 ATOM 470 C C . LEU A 1 59 ? -1.755 -6.979 6.311 1.00 41.31 ? 64 LEU B C 1 ATOM 471 O O . LEU A 1 59 ? -1.982 -7.052 5.106 1.00 38.99 ? 64 LEU B O 1 ATOM 472 C CB . LEU A 1 59 ? 0.074 -8.315 7.215 1.00 46.04 ? 64 LEU B CB 1 ATOM 473 C CG . LEU A 1 59 ? 0.615 -9.596 7.827 1.00 51.17 ? 64 LEU B CG 1 ATOM 474 C CD1 . LEU A 1 59 ? 2.091 -9.754 7.507 1.00 54.95 ? 64 LEU B CD1 1 ATOM 475 C CD2 . LEU A 1 59 ? 0.377 -9.559 9.321 1.00 53.33 ? 64 LEU B CD2 1 ATOM 476 N N . LEU A 1 60 ? -1.723 -5.842 6.977 1.00 37.29 ? 65 LEU B N 1 ATOM 477 C CA . LEU A 1 60 ? -1.614 -4.571 6.275 1.00 40.85 ? 65 LEU B CA 1 ATOM 478 C C . LEU A 1 60 ? -0.607 -3.677 6.970 1.00 37.50 ? 65 LEU B C 1 ATOM 479 O O . LEU A 1 60 ? -0.203 -3.915 8.126 1.00 35.24 ? 65 LEU B O 1 ATOM 480 C CB . LEU A 1 60 ? -2.974 -3.899 6.142 1.00 45.24 ? 65 LEU B CB 1 ATOM 481 C CG . LEU A 1 60 ? -3.873 -3.912 7.375 1.00 49.12 ? 65 LEU B CG 1 ATOM 482 C CD1 . LEU A 1 60 ? -3.602 -2.678 8.218 1.00 51.61 ? 65 LEU B CD1 1 ATOM 483 C CD2 . LEU A 1 60 ? -5.338 -3.992 6.957 1.00 45.86 ? 65 LEU B CD2 1 ATOM 484 N N . VAL A 1 61 ? -0.181 -2.658 6.241 1.00 35.15 ? 66 VAL B N 1 ATOM 485 C CA . VAL A 1 61 ? 0.745 -1.681 6.767 1.00 37.61 ? 66 VAL B CA 1 ATOM 486 C C . VAL A 1 61 ? 0.000 -0.358 6.917 1.00 36.45 ? 66 VAL B C 1 ATOM 487 O O . VAL A 1 61 ? -0.810 0.035 6.056 1.00 30.99 ? 66 VAL B O 1 ATOM 488 C CB . VAL A 1 61 ? 2.011 -1.542 5.887 1.00 40.13 ? 66 VAL B CB 1 ATOM 489 C CG1 . VAL A 1 61 ? 2.602 -2.914 5.614 1.00 50.35 ? 66 VAL B CG1 1 ATOM 490 C CG2 . VAL A 1 61 ? 1.721 -0.839 4.578 1.00 44.36 ? 66 VAL B CG2 1 ATOM 491 N N . ARG A 1 62 ? 0.242 0.302 8.033 1.00 31.34 ? 67 ARG B N 1 ATOM 492 C CA . ARG A 1 62 ? -0.378 1.584 8.300 1.00 31.66 ? 67 ARG B CA 1 ATOM 493 C C . ARG A 1 62 ? 0.732 2.590 8.491 1.00 30.24 ? 67 ARG B C 1 ATOM 494 O O . ARG A 1 62 ? 1.597 2.435 9.354 1.00 27.89 ? 67 ARG B O 1 ATOM 495 C CB . ARG A 1 62 ? -1.276 1.505 9.531 1.00 33.41 ? 67 ARG B CB 1 ATOM 496 C CG . ARG A 1 62 ? -2.325 0.429 9.411 1.00 33.94 ? 67 ARG B CG 1 ATOM 497 C CD . ARG A 1 62 ? -3.114 0.250 10.686 1.00 34.74 ? 67 ARG B CD 1 ATOM 498 N NE . ARG A 1 62 ? -3.888 1.431 11.019 1.00 35.96 ? 67 ARG B NE 1 ATOM 499 C CZ . ARG A 1 62 ? -4.678 1.530 12.086 1.00 40.91 ? 67 ARG B CZ 1 ATOM 500 N NH1 . ARG A 1 62 ? -5.358 2.651 12.316 1.00 38.98 ? 67 ARG B NH1 1 ATOM 501 N NH2 . ARG A 1 62 ? -4.797 0.508 12.926 1.00 42.07 ? 67 ARG B NH2 1 ATOM 502 N N . ILE A 1 63 ? 0.697 3.634 7.678 1.00 29.35 ? 68 ILE B N 1 ATOM 503 C CA . ILE A 1 63 ? 1.828 4.539 7.535 1.00 28.92 ? 68 ILE B CA 1 ATOM 504 C C . ILE A 1 63 ? 1.351 5.955 7.814 1.00 28.46 ? 68 ILE B C 1 ATOM 505 O O . ILE A 1 63 ? 0.252 6.317 7.396 1.00 29.57 ? 68 ILE B O 1 ATOM 506 C CB . ILE A 1 63 ? 2.359 4.432 6.093 1.00 30.82 ? 68 ILE B CB 1 ATOM 507 C CG1 . ILE A 1 63 ? 2.517 2.954 5.704 1.00 31.40 ? 68 ILE B CG1 1 ATOM 508 C CG2 . ILE A 1 63 ? 3.678 5.160 5.939 1.00 30.42 ? 68 ILE B CG2 1 ATOM 509 C CD1 . ILE A 1 63 ? 2.775 2.734 4.223 1.00 36.05 ? 68 ILE B CD1 1 ATOM 510 N N . GLY A 1 64 ? 2.174 6.758 8.496 1.00 26.11 ? 69 GLY B N 1 ATOM 511 C CA . GLY A 1 64 ? 1.815 8.157 8.797 1.00 27.36 ? 69 GLY B CA 1 ATOM 512 C C . GLY A 1 64 ? 1.123 8.309 10.137 1.00 29.84 ? 69 GLY B C 1 ATOM 513 O O . GLY A 1 64 ? 0.489 9.336 10.419 1.00 31.26 ? 69 GLY B O 1 ATOM 514 N N . LYS A 1 65 ? 1.246 7.302 10.987 1.00 27.68 ? 70 LYS B N 1 ATOM 515 C CA . LYS A 1 65 ? 0.441 7.283 12.207 1.00 29.33 ? 70 LYS B CA 1 ATOM 516 C C . LYS A 1 65 ? 1.125 7.969 13.382 1.00 27.70 ? 70 LYS B C 1 ATOM 517 O O . LYS A 1 65 ? 2.354 8.078 13.453 1.00 25.90 ? 70 LYS B O 1 ATOM 518 C CB . LYS A 1 65 ? 0.078 5.838 12.601 1.00 28.07 ? 70 LYS B CB 1 ATOM 519 C CG . LYS A 1 65 ? -1.006 5.245 11.711 1.00 30.38 ? 70 LYS B CG 1 ATOM 520 C CD . LYS A 1 65 ? -1.543 3.925 12.248 1.00 33.45 ? 70 LYS B CD 1 ATOM 521 C CE . LYS A 1 65 ? -2.337 4.093 13.539 1.00 33.14 ? 70 LYS B CE 1 ATOM 522 N NZ . LYS A 1 65 ? -3.303 5.233 13.500 1.00 32.79 ? 70 LYS B NZ 1 ATOM 523 N N . HIS A 1 66 ? 0.299 8.387 14.321 1.00 26.18 ? 71 HIS B N 1 ATOM 524 C CA . HIS A 1 66 ? 0.749 8.912 15.584 1.00 28.00 ? 71 HIS B CA 1 ATOM 525 C C . HIS A 1 66 ? 0.048 8.144 16.707 1.00 27.30 ? 71 HIS B C 1 ATOM 526 O O . HIS A 1 66 ? 0.704 7.521 17.550 1.00 26.63 ? 71 HIS B O 1 ATOM 527 C CB . HIS A 1 66 ? 0.459 10.413 15.640 1.00 29.01 ? 71 HIS B CB 1 ATOM 528 C CG . HIS A 1 66 ? 1.003 11.085 16.858 1.00 32.24 ? 71 HIS B CG 1 ATOM 529 N ND1 . HIS A 1 66 ? 2.355 11.222 17.091 1.00 30.73 ? 71 HIS B ND1 1 ATOM 530 C CD2 . HIS A 1 66 ? 0.377 11.652 17.916 1.00 32.04 ? 71 HIS B CD2 1 ATOM 531 C CE1 . HIS A 1 66 ? 2.535 11.841 18.244 1.00 33.14 ? 71 HIS B CE1 1 ATOM 532 N NE2 . HIS A 1 66 ? 1.353 12.113 18.763 1.00 33.32 ? 71 HIS B NE2 1 ATOM 533 N N . SER A 1 67 ? -1.279 8.207 16.723 1.00 28.33 ? 72 SER B N 1 ATOM 534 C CA . SER A 1 67 ? -2.068 7.459 17.674 1.00 30.80 ? 72 SER B CA 1 ATOM 535 C C . SER A 1 67 ? -1.882 5.962 17.460 1.00 31.11 ? 72 SER B C 1 ATOM 536 O O . SER A 1 67 ? -1.841 5.495 16.327 1.00 30.70 ? 72 SER B O 1 ATOM 537 C CB . SER A 1 67 ? -3.532 7.802 17.521 1.00 32.02 ? 72 SER B CB 1 ATOM 538 O OG . SER A 1 67 ? -4.295 6.950 18.314 1.00 33.56 ? 72 SER B OG 1 ATOM 539 N N . ARG A 1 68 ? -1.736 5.220 18.551 1.00 29.36 ? 73 ARG B N 1 ATOM 540 C CA . ARG A 1 68 ? -1.638 3.761 18.460 1.00 31.95 ? 73 ARG B CA 1 ATOM 541 C C . ARG A 1 68 ? -2.959 3.148 18.024 1.00 34.39 ? 73 ARG B C 1 ATOM 542 O O . ARG A 1 68 ? -2.963 2.195 17.254 1.00 37.82 ? 73 ARG B O 1 ATOM 543 C CB . ARG A 1 68 ? -1.242 3.159 19.819 1.00 33.37 ? 73 ARG B CB 1 ATOM 544 C CG . ARG A 1 68 ? -1.133 1.634 19.838 1.00 35.12 ? 73 ARG B CG 1 ATOM 545 C CD . ARG A 1 68 ? -0.717 1.094 21.211 1.00 36.46 ? 73 ARG B CD 1 ATOM 546 N NE . ARG A 1 68 ? -1.659 1.414 22.294 1.00 40.64 ? 73 ARG B NE 1 ATOM 547 C CZ . ARG A 1 68 ? -2.693 0.665 22.685 1.00 43.13 ? 73 ARG B CZ 1 ATOM 548 N NH1 . ARG A 1 68 ? -2.977 -0.488 22.101 1.00 44.02 ? 73 ARG B NH1 1 ATOM 549 N NH2 . ARG A 1 68 ? -3.453 1.077 23.690 1.00 45.08 ? 73 ARG B NH2 1 ATOM 550 N N . THR A 1 69 ? -4.065 3.669 18.554 1.00 34.13 ? 74 THR B N 1 ATOM 551 C CA . THR A 1 69 ? -5.355 2.994 18.445 1.00 38.07 ? 74 THR B CA 1 ATOM 552 C C . THR A 1 69 ? -6.329 3.648 17.462 1.00 39.49 ? 74 THR B C 1 ATOM 553 O O . THR A 1 69 ? -7.115 2.940 16.839 1.00 39.10 ? 74 THR B O 1 ATOM 554 C CB . THR A 1 69 ? -6.041 2.905 19.810 1.00 39.91 ? 74 THR B CB 1 ATOM 555 O OG1 . THR A 1 69 ? -6.292 4.225 20.299 1.00 40.35 ? 74 THR B OG1 1 ATOM 556 C CG2 . THR A 1 69 ? -5.149 2.142 20.802 1.00 40.65 ? 74 THR B CG2 1 ATOM 557 N N . ARG A 1 70 ? -6.290 4.979 17.339 1.00 33.59 ? 75 ARG B N 1 ATOM 558 C CA . ARG A 1 70 ? -7.184 5.693 16.434 1.00 35.49 ? 75 ARG B CA 1 ATOM 559 C C . ARG A 1 70 ? -6.829 5.492 14.962 1.00 33.75 ? 75 ARG B C 1 ATOM 560 O O . ARG A 1 70 ? -5.659 5.524 14.595 1.00 32.55 ? 75 ARG B O 1 ATOM 561 C CB . ARG A 1 70 ? -7.166 7.204 16.726 1.00 38.93 ? 75 ARG B CB 1 ATOM 562 C CG . ARG A 1 70 ? -7.866 7.612 18.015 1.00 43.52 ? 75 ARG B CG 1 ATOM 563 C CD . ARG A 1 70 ? -9.361 7.505 17.858 1.00 47.11 ? 75 ARG B CD 1 ATOM 564 N NE . ARG A 1 70 ? -10.122 7.959 19.028 1.00 50.80 ? 75 ARG B NE 1 ATOM 565 C CZ . ARG A 1 70 ? -10.913 7.192 19.779 1.00 49.63 ? 75 ARG B CZ 1 ATOM 566 N NH1 . ARG A 1 70 ? -11.058 5.890 19.527 1.00 47.20 ? 75 ARG B NH1 1 ATOM 567 N NH2 . ARG A 1 70 ? -11.567 7.734 20.805 1.00 51.90 ? 75 ARG B NH2 1 ATOM 568 N N . TYR A 1 71 ? -7.853 5.301 14.130 1.00 34.71 ? 76 TYR B N 1 ATOM 569 C CA . TYR A 1 71 ? -7.711 5.498 12.690 1.00 35.14 ? 76 TYR B CA 1 ATOM 570 C C . TYR A 1 71 ? -7.661 6.988 12.417 1.00 34.20 ? 76 TYR B C 1 ATOM 571 O O . TYR A 1 71 ? -8.588 7.690 12.776 1.00 34.33 ? 76 TYR B O 1 ATOM 572 C CB . TYR A 1 71 ? -8.876 4.908 11.905 1.00 35.66 ? 76 TYR B CB 1 ATOM 573 C CG . TYR A 1 71 ? -8.754 5.174 10.419 1.00 36.61 ? 76 TYR B CG 1 ATOM 574 C CD1 . TYR A 1 71 ? -7.774 4.538 9.661 1.00 39.26 ? 76 TYR B CD1 1 ATOM 575 C CD2 . TYR A 1 71 ? -9.586 6.092 9.777 1.00 39.67 ? 76 TYR B CD2 1 ATOM 576 C CE1 . TYR A 1 71 ? -7.646 4.796 8.304 1.00 40.76 ? 76 TYR B CE1 1 ATOM 577 C CE2 . TYR A 1 71 ? -9.463 6.352 8.418 1.00 40.28 ? 76 TYR B CE2 1 ATOM 578 C CZ . TYR A 1 71 ? -8.486 5.691 7.691 1.00 41.38 ? 76 TYR B CZ 1 ATOM 579 O OH . TYR A 1 71 ? -8.331 5.919 6.355 1.00 43.47 ? 76 TYR B OH 1 ATOM 580 N N . GLU A 1 72 ? -6.594 7.444 11.761 1.00 31.79 ? 77 GLU B N 1 ATOM 581 C CA . GLU A 1 72 ? -6.331 8.871 11.570 1.00 33.40 ? 77 GLU B CA 1 ATOM 582 C C . GLU A 1 72 ? -6.604 9.290 10.123 1.00 32.94 ? 77 GLU B C 1 ATOM 583 O O . GLU A 1 72 ? -5.701 9.307 9.279 1.00 30.46 ? 77 GLU B O 1 ATOM 584 C CB . GLU A 1 72 ? -4.886 9.172 11.980 1.00 34.01 ? 77 GLU B CB 1 ATOM 585 C CG . GLU A 1 72 ? -4.664 9.046 13.491 1.00 34.00 ? 77 GLU B CG 1 ATOM 586 C CD . GLU A 1 72 ? -3.212 8.893 13.912 1.00 31.15 ? 77 GLU B CD 1 ATOM 587 O OE1 . GLU A 1 72 ? -2.753 9.675 14.770 1.00 32.60 ? 77 GLU B OE1 1 ATOM 588 O OE2 . GLU A 1 72 ? -2.514 7.970 13.456 1.00 32.67 ? 77 GLU B OE2 1 ATOM 589 N N . ARG A 1 73 A -7.858 9.618 9.861 1.00 36.14 ? 77 ARG B N 1 ATOM 590 C CA . ARG A 1 73 A -8.329 9.936 8.522 1.00 40.32 ? 77 ARG B CA 1 ATOM 591 C C . ARG A 1 73 A -7.575 11.140 7.937 1.00 42.06 ? 77 ARG B C 1 ATOM 592 O O . ARG A 1 73 A -7.335 12.128 8.631 1.00 39.63 ? 77 ARG B O 1 ATOM 593 C CB . ARG A 1 73 A -9.834 10.200 8.552 1.00 44.02 ? 77 ARG B CB 1 ATOM 594 C CG . ARG A 1 73 A -10.411 10.740 7.250 1.00 49.38 ? 77 ARG B CG 1 ATOM 595 C CD . ARG A 1 73 A -11.877 10.377 7.109 1.00 57.51 ? 77 ARG B CD 1 ATOM 596 N NE . ARG A 1 73 A -12.589 11.168 6.118 1.00 61.19 ? 77 ARG B NE 1 ATOM 597 C CZ . ARG A 1 73 A -13.850 10.946 5.749 1.00 69.56 ? 77 ARG B CZ 1 ATOM 598 N NH1 . ARG A 1 73 A -14.551 9.941 6.276 1.00 64.04 ? 77 ARG B NH1 1 ATOM 599 N NH2 . ARG A 1 73 A -14.414 11.732 4.837 1.00 75.52 ? 77 ARG B NH2 1 ATOM 600 N N . ASN A 1 74 ? -7.192 11.032 6.665 1.00 44.04 ? 78 ASN B N 1 ATOM 601 C CA . ASN A 1 74 ? -6.486 12.103 5.945 1.00 48.82 ? 78 ASN B CA 1 ATOM 602 C C . ASN A 1 74 ? -5.038 12.301 6.382 1.00 44.52 ? 78 ASN B C 1 ATOM 603 O O . ASN A 1 74 ? -4.384 13.242 5.929 1.00 47.00 ? 78 ASN B O 1 ATOM 604 C CB . ASN A 1 74 ? -7.222 13.449 6.054 1.00 53.03 ? 78 ASN B CB 1 ATOM 605 C CG . ASN A 1 74 ? -8.509 13.475 5.274 1.00 61.36 ? 78 ASN B CG 1 ATOM 606 O OD1 . ASN A 1 74 ? -8.577 12.966 4.158 1.00 76.37 ? 78 ASN B OD1 1 ATOM 607 N ND2 . ASN A 1 74 ? -9.536 14.093 5.847 1.00 61.15 ? 78 ASN B ND2 1 ATOM 608 N N . ILE A 1 75 ? -4.557 11.433 7.268 1.00 39.89 ? 79 ILE B N 1 ATOM 609 C CA . ILE A 1 75 ? -3.188 11.468 7.764 1.00 39.14 ? 79 ILE B CA 1 ATOM 610 C C . ILE A 1 75 ? -2.540 10.116 7.489 1.00 38.14 ? 79 ILE B C 1 ATOM 611 O O . ILE A 1 75 ? -1.520 10.029 6.784 1.00 35.20 ? 79 ILE B O 1 ATOM 612 C CB . ILE A 1 75 ? -3.160 11.802 9.269 1.00 43.37 ? 79 ILE B CB 1 ATOM 613 C CG1 . ILE A 1 75 ? -3.759 13.208 9.506 1.00 50.46 ? 79 ILE B CG1 1 ATOM 614 C CG2 . ILE A 1 75 ? -1.739 11.742 9.806 1.00 42.23 ? 79 ILE B CG2 1 ATOM 615 C CD1 . ILE A 1 75 ? -4.086 13.531 10.950 1.00 49.34 ? 79 ILE B CD1 1 ATOM 616 N N . GLU A 1 76 ? -3.129 9.047 8.020 1.00 34.12 ? 80 GLU B N 1 ATOM 617 C CA . GLU A 1 76 ? -2.545 7.734 7.782 1.00 34.10 ? 80 GLU B CA 1 ATOM 618 C C . GLU A 1 76 ? -2.969 7.166 6.457 1.00 32.29 ? 80 GLU B C 1 ATOM 619 O O . GLU A 1 76 ? -4.009 7.533 5.908 1.00 30.62 ? 80 GLU B O 1 ATOM 620 C CB . GLU A 1 76 ? -2.852 6.755 8.911 1.00 37.49 ? 80 GLU B CB 1 ATOM 621 C CG . GLU A 1 76 ? -4.236 6.155 8.922 1.00 38.37 ? 80 GLU B CG 1 ATOM 622 C CD . GLU A 1 76 ? -4.321 5.038 9.924 1.00 38.86 ? 80 GLU B CD 1 ATOM 623 O OE1 . GLU A 1 76 ? -3.967 3.886 9.572 1.00 35.45 ? 80 GLU B OE1 1 ATOM 624 O OE2 . GLU A 1 76 ? -4.722 5.326 11.071 1.00 38.57 ? 80 GLU B OE2 1 ATOM 625 N N . LYS A 1 77 ? -2.145 6.252 5.958 1.00 34.45 ? 81 LYS B N 1 ATOM 626 C CA . LYS A 1 77 ? -2.429 5.520 4.731 1.00 34.53 ? 81 LYS B CA 1 ATOM 627 C C . LYS A 1 77 ? -2.220 4.045 5.032 1.00 32.70 ? 81 LYS B C 1 ATOM 628 O O . LYS A 1 77 ? -1.289 3.672 5.748 1.00 30.13 ? 81 LYS B O 1 ATOM 629 C CB . LYS A 1 77 ? -1.484 5.924 3.603 1.00 36.59 ? 81 LYS B CB 1 ATOM 630 C CG . LYS A 1 77 ? -1.490 7.403 3.259 1.00 41.02 ? 81 LYS B CG 1 ATOM 631 C CD . LYS A 1 77 ? -2.765 7.822 2.575 1.00 48.51 ? 81 LYS B CD 1 ATOM 632 C CE . LYS A 1 77 ? -2.748 9.318 2.296 1.00 51.87 ? 81 LYS B CE 1 ATOM 633 N NZ . LYS A 1 77 ? -4.126 9.784 2.027 1.00 54.63 ? 81 LYS B NZ 1 ATOM 634 N N . ILE A 1 78 ? -3.086 3.218 4.475 1.00 35.01 ? 82 ILE B N 1 ATOM 635 C CA . ILE A 1 78 ? -3.052 1.771 4.687 1.00 35.69 ? 82 ILE B CA 1 ATOM 636 C C . ILE A 1 78 ? -2.769 1.134 3.352 1.00 35.41 ? 82 ILE B C 1 ATOM 637 O O . ILE A 1 78 ? -3.407 1.465 2.374 1.00 36.12 ? 82 ILE B O 1 ATOM 638 C CB . ILE A 1 78 ? -4.405 1.228 5.189 1.00 40.60 ? 82 ILE B CB 1 ATOM 639 C CG1 . ILE A 1 78 ? -4.673 1.692 6.618 1.00 40.48 ? 82 ILE B CG1 1 ATOM 640 C CG2 . ILE A 1 78 ? -4.424 -0.295 5.148 1.00 42.17 ? 82 ILE B CG2 1 ATOM 641 C CD1 . ILE A 1 78 ? -5.038 3.137 6.722 1.00 44.81 ? 82 ILE B CD1 1 ATOM 642 N N . SER A 1 79 ? -1.824 0.211 3.315 1.00 38.54 ? 83 SER B N 1 ATOM 643 C CA . SER A 1 79 ? -1.539 -0.546 2.107 1.00 39.21 ? 83 SER B CA 1 ATOM 644 C C . SER A 1 79 ? -1.526 -2.035 2.412 1.00 39.48 ? 83 SER B C 1 ATOM 645 O O . SER A 1 79 ? -1.240 -2.460 3.542 1.00 34.48 ? 83 SER B O 1 ATOM 646 C CB . SER A 1 79 ? -0.186 -0.130 1.517 1.00 40.46 ? 83 SER B CB 1 ATOM 647 O OG . SER A 1 79 ? 0.048 -0.815 0.288 0.40 42.23 ? 83 SER B OG 1 ATOM 648 N N . MET A 1 80 ? -1.842 -2.819 1.394 1.00 40.50 ? 84 MET B N 1 ATOM 649 C CA . MET A 1 80 ? -1.725 -4.272 1.459 1.00 44.35 ? 84 MET B CA 1 ATOM 650 C C . MET A 1 80 ? -0.342 -4.658 0.959 1.00 41.18 ? 84 MET B C 1 ATOM 651 O O . MET A 1 80 ? 0.357 -3.846 0.355 1.00 42.32 ? 84 MET B O 1 ATOM 652 C CB . MET A 1 80 ? -2.776 -4.935 0.573 1.00 52.32 ? 84 MET B CB 1 ATOM 653 C CG . MET A 1 80 ? -4.216 -4.544 0.863 1.00 61.36 ? 84 MET B CG 1 ATOM 654 S SD . MET A 1 80 ? -4.770 -4.987 2.519 1.00 77.94 ? 84 MET B SD 1 ATOM 655 C CE . MET A 1 80 ? -6.500 -4.518 2.417 1.00 81.36 ? 84 MET B CE 1 ATOM 656 N N . LEU A 1 81 ? 0.035 -5.910 1.174 1.00 38.54 ? 85 LEU B N 1 ATOM 657 C CA . LEU A 1 81 ? 1.330 -6.407 0.715 1.00 39.87 ? 85 LEU B CA 1 ATOM 658 C C . LEU A 1 81 ? 1.238 -7.249 -0.553 1.00 39.57 ? 85 LEU B C 1 ATOM 659 O O . LEU A 1 81 ? 0.350 -8.083 -0.697 1.00 39.51 ? 85 LEU B O 1 ATOM 660 C CB . LEU A 1 81 ? 1.979 -7.244 1.805 1.00 39.62 ? 85 LEU B CB 1 ATOM 661 C CG . LEU A 1 81 ? 2.057 -6.582 3.170 1.00 39.28 ? 85 LEU B CG 1 ATOM 662 C CD1 . LEU A 1 81 ? 2.638 -7.574 4.162 1.00 40.43 ? 85 LEU B CD1 1 ATOM 663 C CD2 . LEU A 1 81 ? 2.881 -5.307 3.105 1.00 42.90 ? 85 LEU B CD2 1 ATOM 664 N N . GLU A 1 82 ? 2.187 -7.036 -1.457 1.00 40.10 ? 86 GLU B N 1 ATOM 665 C CA . GLU A 1 82 ? 2.339 -7.872 -2.634 1.00 43.49 ? 86 GLU B CA 1 ATOM 666 C C . GLU A 1 82 ? 3.164 -9.106 -2.283 1.00 44.32 ? 86 GLU B C 1 ATOM 667 O O . GLU A 1 82 ? 2.843 -10.201 -2.716 1.00 40.37 ? 86 GLU B O 1 ATOM 668 C CB . GLU A 1 82 ? 3.040 -7.098 -3.755 1.00 48.70 ? 86 GLU B CB 1 ATOM 669 C CG . GLU A 1 82 ? 2.909 -7.726 -5.131 1.00 55.57 ? 86 GLU B CG 1 ATOM 670 C CD . GLU A 1 82 ? 1.690 -7.214 -5.883 1.00 69.04 ? 86 GLU B CD 1 ATOM 671 O OE1 . GLU A 1 82 ? 1.694 -6.029 -6.293 1.00 67.46 ? 86 GLU B OE1 1 ATOM 672 O OE2 . GLU A 1 82 ? 0.727 -7.994 -6.067 1.00 77.47 ? 86 GLU B OE2 1 ATOM 673 N N . LYS A 1 83 ? 4.239 -8.925 -1.511 1.00 44.17 ? 87 LYS B N 1 ATOM 674 C CA . LYS A 1 83 ? 5.139 -10.038 -1.187 1.00 44.88 ? 87 LYS B CA 1 ATOM 675 C C . LYS A 1 83 ? 5.964 -9.759 0.056 1.00 38.66 ? 87 LYS B C 1 ATOM 676 O O . LYS A 1 83 ? 6.333 -8.619 0.315 1.00 32.69 ? 87 LYS B O 1 ATOM 677 C CB . LYS A 1 83 ? 6.083 -10.330 -2.356 1.00 53.07 ? 87 LYS B CB 1 ATOM 678 C CG . LYS A 1 83 ? 6.890 -11.624 -2.233 1.00 62.60 ? 87 LYS B CG 1 ATOM 679 C CD . LYS A 1 83 ? 6.018 -12.874 -2.289 1.00 69.70 ? 87 LYS B CD 1 ATOM 680 C CE . LYS A 1 83 ? 6.721 -14.078 -1.682 1.00 75.87 ? 87 LYS B CE 1 ATOM 681 N NZ . LYS A 1 83 ? 7.958 -14.445 -2.430 1.00 81.09 ? 87 LYS B NZ 1 ATOM 682 N N . ILE A 1 84 ? 6.260 -10.830 0.794 1.00 39.61 ? 88 ILE B N 1 ATOM 683 C CA . ILE A 1 84 ? 7.091 -10.786 1.997 1.00 37.86 ? 88 ILE B CA 1 ATOM 684 C C . ILE A 1 84 ? 8.363 -11.568 1.722 1.00 38.25 ? 88 ILE B C 1 ATOM 685 O O . ILE A 1 84 ? 8.301 -12.657 1.179 1.00 41.17 ? 88 ILE B O 1 ATOM 686 C CB . ILE A 1 84 ? 6.370 -11.451 3.179 1.00 39.87 ? 88 ILE B CB 1 ATOM 687 C CG1 . ILE A 1 84 ? 5.222 -10.563 3.656 1.00 45.92 ? 88 ILE B CG1 1 ATOM 688 C CG2 . ILE A 1 84 ? 7.343 -11.723 4.324 1.00 41.86 ? 88 ILE B CG2 1 ATOM 689 C CD1 . ILE A 1 84 ? 4.182 -11.298 4.476 1.00 51.54 ? 88 ILE B CD1 1 ATOM 690 N N . TYR A 1 85 ? 9.508 -11.026 2.119 1.00 38.77 ? 89 TYR B N 1 ATOM 691 C CA . TYR A 1 85 ? 10.790 -11.726 1.964 1.00 38.41 ? 89 TYR B CA 1 ATOM 692 C C . TYR A 1 85 ? 11.492 -11.780 3.302 1.00 33.92 ? 89 TYR B C 1 ATOM 693 O O . TYR A 1 85 ? 11.725 -10.753 3.893 1.00 31.02 ? 89 TYR B O 1 ATOM 694 C CB . TYR A 1 85 ? 11.693 -10.986 0.984 1.00 40.21 ? 89 TYR B CB 1 ATOM 695 C CG . TYR A 1 85 ? 11.089 -10.801 -0.381 1.00 43.66 ? 89 TYR B CG 1 ATOM 696 C CD1 . TYR A 1 85 ? 10.264 -9.715 -0.654 1.00 46.92 ? 89 TYR B CD1 1 ATOM 697 C CD2 . TYR A 1 85 ? 11.350 -11.702 -1.400 1.00 50.13 ? 89 TYR B CD2 1 ATOM 698 C CE1 . TYR A 1 85 ? 9.706 -9.542 -1.907 1.00 49.98 ? 89 TYR B CE1 1 ATOM 699 C CE2 . TYR A 1 85 ? 10.796 -11.538 -2.657 1.00 54.26 ? 89 TYR B CE2 1 ATOM 700 C CZ . TYR A 1 85 ? 9.980 -10.454 -2.901 1.00 53.30 ? 89 TYR B CZ 1 ATOM 701 O OH . TYR A 1 85 ? 9.430 -10.292 -4.142 1.00 63.07 ? 89 TYR B OH 1 ATOM 702 N N . ILE A 1 86 ? 11.810 -12.978 3.777 1.00 35.08 ? 90 ILE B N 1 ATOM 703 C CA . ILE A 1 86 ? 12.605 -13.140 4.990 1.00 36.47 ? 90 ILE B CA 1 ATOM 704 C C . ILE A 1 86 ? 14.014 -13.535 4.564 1.00 34.00 ? 90 ILE B C 1 ATOM 705 O O . ILE A 1 86 ? 14.193 -14.203 3.563 1.00 37.48 ? 90 ILE B O 1 ATOM 706 C CB . ILE A 1 86 ? 11.963 -14.189 5.925 1.00 39.49 ? 90 ILE B CB 1 ATOM 707 C CG1 . ILE A 1 86 ? 10.598 -13.672 6.424 1.00 42.00 ? 90 ILE B CG1 1 ATOM 708 C CG2 . ILE A 1 86 ? 12.874 -14.510 7.106 1.00 39.99 ? 90 ILE B CG2 1 ATOM 709 C CD1 . ILE A 1 86 ? 9.538 -14.750 6.462 1.00 46.54 ? 90 ILE B CD1 1 ATOM 710 N N . HIS A 1 87 ? 15.017 -13.076 5.304 1.00 34.47 ? 91 HIS B N 1 ATOM 711 C CA . HIS A 1 87 ? 16.396 -13.450 5.026 1.00 33.99 ? 91 HIS B CA 1 ATOM 712 C C . HIS A 1 87 ? 16.491 -14.976 5.082 1.00 36.30 ? 91 HIS B C 1 ATOM 713 O O . HIS A 1 87 ? 15.985 -15.589 6.019 1.00 35.07 ? 91 HIS B O 1 ATOM 714 C CB . HIS A 1 87 ? 17.361 -12.815 6.041 1.00 33.36 ? 91 HIS B CB 1 ATOM 715 C CG . HIS A 1 87 ? 18.778 -12.762 5.560 1.00 32.91 ? 91 HIS B CG 1 ATOM 716 N ND1 . HIS A 1 87 ? 19.531 -13.890 5.361 1.00 33.94 ? 91 HIS B ND1 1 ATOM 717 C CD2 . HIS A 1 87 ? 19.569 -11.719 5.218 1.00 31.81 ? 91 HIS B CD2 1 ATOM 718 C CE1 . HIS A 1 87 ? 20.723 -13.556 4.907 1.00 34.73 ? 91 HIS B CE1 1 ATOM 719 N NE2 . HIS A 1 87 ? 20.773 -12.240 4.818 1.00 34.98 ? 91 HIS B NE2 1 ATOM 720 N N . PRO A 1 88 ? 17.127 -15.595 4.076 1.00 37.53 ? 92 PRO B N 1 ATOM 721 C CA . PRO A 1 88 ? 17.131 -17.055 4.039 1.00 41.25 ? 92 PRO B CA 1 ATOM 722 C C . PRO A 1 88 ? 17.933 -17.707 5.169 1.00 39.51 ? 92 PRO B C 1 ATOM 723 O O . PRO A 1 88 ? 17.721 -18.877 5.466 1.00 38.41 ? 92 PRO B O 1 ATOM 724 C CB . PRO A 1 88 ? 17.728 -17.387 2.660 1.00 42.53 ? 92 PRO B CB 1 ATOM 725 C CG . PRO A 1 88 ? 18.451 -16.155 2.236 1.00 42.35 ? 92 PRO B CG 1 ATOM 726 C CD . PRO A 1 88 ? 17.790 -14.992 2.905 1.00 39.84 ? 92 PRO B CD 1 ATOM 727 N N . ARG A 1 89 ? 18.849 -16.966 5.781 1.00 38.71 ? 93 ARG B N 1 ATOM 728 C CA . ARG A 1 89 ? 19.590 -17.457 6.940 1.00 39.69 ? 93 ARG B CA 1 ATOM 729 C C . ARG A 1 89 ? 19.077 -16.903 8.259 1.00 34.93 ? 93 ARG B C 1 ATOM 730 O O . ARG A 1 89 ? 19.767 -16.955 9.257 1.00 33.15 ? 93 ARG B O 1 ATOM 731 C CB . ARG A 1 89 ? 21.082 -17.166 6.779 1.00 45.55 ? 93 ARG B CB 1 ATOM 732 C CG . ARG A 1 89 ? 21.717 -17.828 5.562 1.00 55.66 ? 93 ARG B CG 1 ATOM 733 C CD . ARG A 1 89 ? 23.204 -17.496 5.474 1.00 66.82 ? 93 ARG B CD 1 ATOM 734 N NE . ARG A 1 89 ? 23.791 -17.922 4.202 1.00 89.22 ? 93 ARG B NE 1 ATOM 735 C CZ . ARG A 1 89 ? 23.691 -17.267 3.040 1.00 103.67 ? 93 ARG B CZ 1 ATOM 736 N NH1 . ARG A 1 89 ? 23.016 -16.118 2.946 1.00 102.67 ? 93 ARG B NH1 1 ATOM 737 N NH2 . ARG A 1 89 ? 24.271 -17.772 1.951 1.00 108.59 ? 93 ARG B NH2 1 ATOM 738 N N . TYR A 1 90 ? 17.867 -16.356 8.274 1.00 36.44 ? 94 TYR B N 1 ATOM 739 C CA . TYR A 1 90 ? 17.228 -15.963 9.521 1.00 32.34 ? 94 TYR B CA 1 ATOM 740 C C . TYR A 1 90 ? 17.190 -17.169 10.452 1.00 33.16 ? 94 TYR B C 1 ATOM 741 O O . TYR A 1 90 ? 16.733 -18.232 10.072 1.00 35.73 ? 94 TYR B O 1 ATOM 742 C CB . TYR A 1 90 ? 15.824 -15.438 9.241 1.00 32.36 ? 94 TYR B CB 1 ATOM 743 C CG . TYR A 1 90 ? 14.885 -15.340 10.435 1.00 30.79 ? 94 TYR B CG 1 ATOM 744 C CD1 . TYR A 1 90 ? 15.226 -14.615 11.570 1.00 30.99 ? 94 TYR B CD1 1 ATOM 745 C CD2 . TYR A 1 90 ? 13.648 -15.977 10.409 1.00 30.78 ? 94 TYR B CD2 1 ATOM 746 C CE1 . TYR A 1 90 ? 14.348 -14.509 12.649 1.00 30.00 ? 94 TYR B CE1 1 ATOM 747 C CE2 . TYR A 1 90 ? 12.772 -15.885 11.474 1.00 32.59 ? 94 TYR B CE2 1 ATOM 748 C CZ . TYR A 1 90 ? 13.123 -15.146 12.592 1.00 31.12 ? 94 TYR B CZ 1 ATOM 749 O OH . TYR A 1 90 ? 12.231 -15.068 13.635 1.00 32.57 ? 94 TYR B OH 1 ATOM 750 N N . ASN A 1 91 ? 17.718 -17.001 11.659 1.00 35.36 ? 95 ASN B N 1 ATOM 751 C CA . ASN A 1 91 ? 17.873 -18.085 12.609 1.00 38.24 ? 95 ASN B CA 1 ATOM 752 C C . ASN A 1 91 ? 16.971 -17.884 13.837 1.00 40.00 ? 95 ASN B C 1 ATOM 753 O O . ASN A 1 91 ? 17.417 -17.360 14.849 1.00 43.84 ? 95 ASN B O 1 ATOM 754 C CB . ASN A 1 91 ? 19.343 -18.151 13.035 1.00 40.24 ? 95 ASN B CB 1 ATOM 755 C CG . ASN A 1 91 ? 19.657 -19.365 13.894 1.00 46.89 ? 95 ASN B CG 1 ATOM 756 O OD1 . ASN A 1 91 ? 18.765 -20.115 14.306 1.00 50.70 ? 95 ASN B OD1 1 ATOM 757 N ND2 . ASN A 1 91 ? 20.940 -19.564 14.169 1.00 46.98 ? 95 ASN B ND2 1 ATOM 758 N N . TRP A 1 92 ? 15.712 -18.314 13.755 1.00 38.81 ? 96 TRP B N 1 ATOM 759 C CA . TRP A 1 92 ? 14.774 -18.108 14.877 1.00 37.71 ? 96 TRP B CA 1 ATOM 760 C C . TRP A 1 92 ? 14.937 -19.107 16.009 1.00 37.99 ? 96 TRP B C 1 ATOM 761 O O . TRP A 1 92 ? 14.452 -18.861 17.105 1.00 40.82 ? 96 TRP B O 1 ATOM 762 C CB . TRP A 1 92 ? 13.308 -18.095 14.423 1.00 36.89 ? 96 TRP B CB 1 ATOM 763 C CG . TRP A 1 92 ? 12.836 -19.333 13.771 1.00 38.29 ? 96 TRP B CG 1 ATOM 764 C CD1 . TRP A 1 92 ? 12.793 -19.577 12.429 1.00 38.31 ? 96 TRP B CD1 1 ATOM 765 C CD2 . TRP A 1 92 ? 12.319 -20.520 14.413 1.00 38.33 ? 96 TRP B CD2 1 ATOM 766 N NE1 . TRP A 1 92 ? 12.300 -20.836 12.200 1.00 38.86 ? 96 TRP B NE1 1 ATOM 767 C CE2 . TRP A 1 92 ? 12.000 -21.432 13.397 1.00 39.84 ? 96 TRP B CE2 1 ATOM 768 C CE3 . TRP A 1 92 ? 12.103 -20.892 15.744 1.00 39.34 ? 96 TRP B CE3 1 ATOM 769 C CZ2 . TRP A 1 92 ? 11.467 -22.706 13.666 1.00 43.73 ? 96 TRP B CZ2 1 ATOM 770 C CZ3 . TRP A 1 92 ? 11.574 -22.149 16.012 1.00 40.72 ? 96 TRP B CZ3 1 ATOM 771 C CH2 . TRP A 1 92 ? 11.266 -23.043 14.980 1.00 43.37 ? 96 TRP B CH2 1 ATOM 772 N N . ARG A 1 93 ? 15.606 -20.231 15.753 1.00 38.01 ? 97 ARG B N 1 ATOM 773 C CA . ARG A 1 93 ? 15.736 -21.275 16.759 1.00 38.93 ? 97 ARG B CA 1 ATOM 774 C C . ARG A 1 93 ? 16.719 -20.962 17.861 1.00 39.71 ? 97 ARG B C 1 ATOM 775 O O . ARG A 1 93 ? 16.548 -21.459 18.974 1.00 38.30 ? 97 ARG B O 1 ATOM 776 C CB . ARG A 1 93 ? 16.171 -22.590 16.123 1.00 42.57 ? 97 ARG B CB 1 ATOM 777 C CG . ARG A 1 93 ? 15.095 -23.290 15.331 1.00 45.34 ? 97 ARG B CG 1 ATOM 778 C CD . ARG A 1 93 ? 15.675 -24.555 14.732 1.00 49.85 ? 97 ARG B CD 1 ATOM 779 N NE . ARG A 1 93 ? 14.642 -25.534 14.449 1.00 55.26 ? 97 ARG B NE 1 ATOM 780 C CZ . ARG A 1 93 ? 13.804 -25.480 13.420 1.00 63.21 ? 97 ARG B CZ 1 ATOM 781 N NH1 . ARG A 1 93 ? 13.857 -24.478 12.543 1.00 68.56 ? 97 ARG B NH1 1 ATOM 782 N NH2 . ARG A 1 93 ? 12.901 -26.441 13.268 1.00 68.70 ? 97 ARG B NH2 1 ATOM 783 N N . GLU A 1 94 A 17.754 -20.176 17.550 1.00 40.60 ? 97 GLU B N 1 ATOM 784 C CA . GLU A 1 94 A 18.858 -19.911 18.485 1.00 42.08 ? 97 GLU B CA 1 ATOM 785 C C . GLU A 1 94 A 18.877 -18.481 19.002 1.00 39.08 ? 97 GLU B C 1 ATOM 786 O O . GLU A 1 94 A 18.638 -18.240 20.182 1.00 39.67 ? 97 GLU B O 1 ATOM 787 C CB . GLU A 1 94 A 20.229 -20.228 17.840 1.00 45.89 ? 97 GLU B CB 1 ATOM 788 C CG . GLU A 1 94 A 21.389 -20.195 18.846 1.00 52.33 ? 97 GLU B CG 1 ATOM 789 C CD . GLU A 1 94 A 22.798 -20.184 18.236 1.00 57.91 ? 97 GLU B CD 1 ATOM 790 O OE1 . GLU A 1 94 A 22.965 -20.164 16.989 1.00 54.76 ? 97 GLU B OE1 1 ATOM 791 O OE2 . GLU A 1 94 A 23.768 -20.186 19.032 1.00 56.97 ? 97 GLU B OE2 1 ATOM 792 N N . ASN A 1 95 ? 19.188 -17.531 18.127 1.00 35.89 ? 98 ASN B N 1 ATOM 793 C CA . ASN A 1 95 ? 19.558 -16.188 18.575 1.00 34.60 ? 98 ASN B CA 1 ATOM 794 C C . ASN A 1 95 ? 19.017 -15.035 17.743 1.00 31.98 ? 98 ASN B C 1 ATOM 795 O O . ASN A 1 95 ? 19.419 -13.890 17.950 1.00 35.46 ? 98 ASN B O 1 ATOM 796 C CB . ASN A 1 95 ? 21.088 -16.095 18.633 1.00 34.93 ? 98 ASN B CB 1 ATOM 797 C CG . ASN A 1 95 ? 21.741 -16.330 17.279 1.00 34.07 ? 98 ASN B CG 1 ATOM 798 O OD1 . ASN A 1 95 ? 21.062 -16.604 16.288 1.00 33.93 ? 98 ASN B OD1 1 ATOM 799 N ND2 . ASN A 1 95 ? 23.062 -16.246 17.238 1.00 35.70 ? 98 ASN B ND2 1 ATOM 800 N N . LEU A 1 96 ? 18.101 -15.332 16.818 1.00 31.52 ? 99 LEU B N 1 ATOM 801 C CA . LEU A 1 96 ? 17.530 -14.348 15.909 1.00 27.66 ? 99 LEU B CA 1 ATOM 802 C C . LEU A 1 96 ? 18.593 -13.692 15.026 1.00 27.11 ? 99 LEU B C 1 ATOM 803 O O . LEU A 1 96 ? 18.455 -12.533 14.623 1.00 27.77 ? 99 LEU B O 1 ATOM 804 C CB . LEU A 1 96 ? 16.707 -13.271 16.650 1.00 28.73 ? 99 LEU B CB 1 ATOM 805 C CG . LEU A 1 96 ? 15.494 -13.716 17.465 1.00 31.80 ? 99 LEU B CG 1 ATOM 806 C CD1 . LEU A 1 96 ? 14.840 -12.517 18.143 1.00 29.55 ? 99 LEU B CD1 1 ATOM 807 C CD2 . LEU A 1 96 ? 14.486 -14.440 16.588 1.00 34.79 ? 99 LEU B CD2 1 ATOM 808 N N . ASP A 1 97 ? 19.641 -14.432 14.704 1.00 28.39 ? 100 ASP B N 1 ATOM 809 C CA . ASP A 1 97 ? 20.626 -13.945 13.755 1.00 29.56 ? 100 ASP B CA 1 ATOM 810 C C . ASP A 1 97 ? 19.900 -13.595 12.461 1.00 27.85 ? 100 ASP B C 1 ATOM 811 O O . ASP A 1 97 ? 19.055 -14.356 12.002 1.00 27.04 ? 100 ASP B O 1 ATOM 812 C CB . ASP A 1 97 ? 21.691 -14.995 13.490 1.00 32.34 ? 100 ASP B CB 1 ATOM 813 C CG . ASP A 1 97 ? 22.890 -14.442 12.757 1.00 35.89 ? 100 ASP B CG 1 ATOM 814 O OD1 . ASP A 1 97 ? 23.126 -13.213 12.800 1.00 38.23 ? 100 ASP B OD1 1 ATOM 815 O OD2 . ASP A 1 97 ? 23.603 -15.250 12.151 1.00 40.32 ? 100 ASP B OD2 1 ATOM 816 N N . ARG A 1 98 ? 20.219 -12.427 11.913 1.00 26.33 ? 101 ARG B N 1 ATOM 817 C CA . ARG A 1 98 ? 19.611 -11.912 10.664 1.00 30.00 ? 101 ARG B CA 1 ATOM 818 C C . ARG A 1 98 ? 18.101 -11.738 10.730 1.00 29.43 ? 101 ARG B C 1 ATOM 819 O O . ARG A 1 98 ? 17.351 -12.218 9.864 1.00 31.07 ? 101 ARG B O 1 ATOM 820 C CB . ARG A 1 98 ? 19.997 -12.767 9.490 1.00 32.58 ? 101 ARG B CB 1 ATOM 821 C CG . ARG A 1 98 ? 21.498 -12.897 9.326 1.00 36.79 ? 101 ARG B CG 1 ATOM 822 C CD . ARG A 1 98 ? 21.783 -13.921 8.260 1.00 42.58 ? 101 ARG B CD 1 ATOM 823 N NE . ARG A 1 98 ? 23.194 -14.012 7.896 1.00 51.89 ? 101 ARG B NE 1 ATOM 824 C CZ . ARG A 1 98 ? 24.049 -14.949 8.308 1.00 54.11 ? 101 ARG B CZ 1 ATOM 825 N NH1 . ARG A 1 98 ? 23.680 -15.911 9.143 1.00 53.48 ? 101 ARG B NH1 1 ATOM 826 N NH2 . ARG A 1 98 ? 25.304 -14.916 7.875 1.00 62.79 ? 101 ARG B NH2 1 ATOM 827 N N . ASP A 1 99 ? 17.681 -11.036 11.775 1.00 27.92 ? 102 ASP B N 1 ATOM 828 C CA . ASP A 1 99 ? 16.285 -10.771 12.041 1.00 28.97 ? 102 ASP B CA 1 ATOM 829 C C . ASP A 1 99 ? 15.861 -9.634 11.112 1.00 26.61 ? 102 ASP B C 1 ATOM 830 O O . ASP A 1 99 ? 15.789 -8.474 11.520 1.00 27.71 ? 102 ASP B O 1 ATOM 831 C CB . ASP A 1 99 ? 16.096 -10.399 13.523 1.00 27.92 ? 102 ASP B CB 1 ATOM 832 C CG . ASP A 1 99 ? 14.633 -10.465 13.974 1.00 30.47 ? 102 ASP B CG 1 ATOM 833 O OD1 . ASP A 1 99 ? 13.749 -10.778 13.155 1.00 28.94 ? 102 ASP B OD1 1 ATOM 834 O OD2 . ASP A 1 99 ? 14.380 -10.238 15.167 1.00 26.55 ? 102 ASP B OD2 1 ATOM 835 N N . ILE A 1 100 ? 15.607 -9.976 9.850 1.00 29.43 ? 103 ILE B N 1 ATOM 836 C CA . ILE A 1 100 ? 15.304 -8.961 8.842 1.00 29.16 ? 103 ILE B CA 1 ATOM 837 C C . ILE A 1 100 ? 14.355 -9.488 7.779 1.00 27.37 ? 103 ILE B C 1 ATOM 838 O O . ILE A 1 100 ? 14.454 -10.634 7.371 1.00 28.11 ? 103 ILE B O 1 ATOM 839 C CB . ILE A 1 100 ? 16.598 -8.421 8.194 1.00 28.93 ? 103 ILE B CB 1 ATOM 840 C CG1 . ILE A 1 100 ? 16.309 -7.199 7.333 1.00 31.05 ? 103 ILE B CG1 1 ATOM 841 C CG2 . ILE A 1 100 ? 17.304 -9.473 7.357 1.00 30.23 ? 103 ILE B CG2 1 ATOM 842 C CD1 . ILE A 1 100 ? 17.542 -6.352 7.078 1.00 29.93 ? 103 ILE B CD1 1 ATOM 843 N N . ALA A 1 101 ? 13.417 -8.637 7.376 1.00 25.69 ? 104 ALA B N 1 ATOM 844 C CA . ALA A 1 101 ? 12.463 -8.950 6.333 1.00 26.58 ? 104 ALA B CA 1 ATOM 845 C C . ALA A 1 101 ? 12.072 -7.687 5.592 1.00 25.97 ? 104 ALA B C 1 ATOM 846 O O . ALA A 1 101 ? 12.073 -6.598 6.164 1.00 28.18 ? 104 ALA B O 1 ATOM 847 C CB . ALA A 1 101 ? 11.231 -9.625 6.916 1.00 28.50 ? 104 ALA B CB 1 ATOM 848 N N . LEU A 1 102 ? 11.785 -7.862 4.308 1.00 30.62 ? 105 LEU B N 1 ATOM 849 C CA . LEU A 1 102 ? 11.295 -6.825 3.428 1.00 31.41 ? 105 LEU B CA 1 ATOM 850 C C . LEU A 1 102 ? 9.876 -7.158 2.974 1.00 29.73 ? 105 LEU B C 1 ATOM 851 O O . LEU A 1 102 ? 9.522 -8.311 2.770 1.00 30.39 ? 105 LEU B O 1 ATOM 852 C CB . LEU A 1 102 ? 12.173 -6.709 2.182 1.00 31.25 ? 105 LEU B CB 1 ATOM 853 C CG . LEU A 1 102 ? 13.468 -5.924 2.326 1.00 32.04 ? 105 LEU B CG 1 ATOM 854 C CD1 . LEU A 1 102 ? 14.452 -6.320 1.226 1.00 35.35 ? 105 LEU B CD1 1 ATOM 855 C CD2 . LEU A 1 102 ? 13.173 -4.434 2.293 1.00 33.79 ? 105 LEU B CD2 1 ATOM 856 N N . MET A 1 103 ? 9.081 -6.117 2.821 1.00 29.80 ? 106 MET B N 1 ATOM 857 C CA . MET A 1 103 ? 7.712 -6.227 2.365 1.00 31.14 ? 106 MET B CA 1 ATOM 858 C C . MET A 1 103 ? 7.512 -5.254 1.219 1.00 30.96 ? 106 MET B C 1 ATOM 859 O O . MET A 1 103 ? 7.824 -4.057 1.338 1.00 27.90 ? 106 MET B O 1 ATOM 860 C CB . MET A 1 103 ? 6.751 -5.901 3.515 1.00 35.26 ? 106 MET B CB 1 ATOM 861 C CG . MET A 1 103 ? 7.002 -6.765 4.745 1.00 38.25 ? 106 MET B CG 1 ATOM 862 S SD . MET A 1 103 ? 5.844 -6.455 6.097 1.00 45.07 ? 106 MET B SD 1 ATOM 863 C CE . MET A 1 103 ? 6.440 -4.885 6.672 1.00 45.93 ? 106 MET B CE 1 ATOM 864 N N . LYS A 1 104 ? 7.017 -5.778 0.100 1.00 33.05 ? 107 LYS B N 1 ATOM 865 C CA . LYS A 1 104 ? 6.658 -4.957 -1.025 1.00 34.29 ? 107 LYS B CA 1 ATOM 866 C C . LYS A 1 104 ? 5.183 -4.620 -0.957 1.00 34.43 ? 107 LYS B C 1 ATOM 867 O O . LYS A 1 104 ? 4.344 -5.516 -0.866 1.00 32.32 ? 107 LYS B O 1 ATOM 868 C CB . LYS A 1 104 ? 6.930 -5.676 -2.338 1.00 37.68 ? 107 LYS B CB 1 ATOM 869 C CG . LYS A 1 104 ? 6.830 -4.725 -3.499 1.00 41.55 ? 107 LYS B CG 1 ATOM 870 C CD . LYS A 1 104 ? 7.097 -5.418 -4.803 1.00 47.07 ? 107 LYS B CD 1 ATOM 871 C CE . LYS A 1 104 ? 7.072 -4.430 -5.950 1.00 52.39 ? 107 LYS B CE 1 ATOM 872 N NZ . LYS A 1 104 ? 7.039 -5.177 -7.243 1.00 59.70 ? 107 LYS B NZ 1 ATOM 873 N N . LEU A 1 105 ? 4.876 -3.326 -1.052 1.00 33.63 ? 108 LEU B N 1 ATOM 874 C CA . LEU A 1 105 ? 3.496 -2.853 -0.983 1.00 35.48 ? 108 LEU B CA 1 ATOM 875 C C . LEU A 1 105 ? 2.799 -3.117 -2.290 1.00 37.40 ? 108 LEU B C 1 ATOM 876 O O . LEU A 1 105 ? 3.413 -3.050 -3.350 1.00 35.83 ? 108 LEU B O 1 ATOM 877 C CB . LEU A 1 105 ? 3.446 -1.350 -0.687 1.00 34.43 ? 108 LEU B CB 1 ATOM 878 C CG . LEU A 1 105 ? 4.136 -0.877 0.589 1.00 35.18 ? 108 LEU B CG 1 ATOM 879 C CD1 . LEU A 1 105 ? 3.858 0.595 0.833 1.00 36.38 ? 108 LEU B CD1 1 ATOM 880 C CD2 . LEU A 1 105 ? 3.697 -1.704 1.774 1.00 35.77 ? 108 LEU B CD2 1 ATOM 881 N N . LYS A 1 106 ? 1.508 -3.409 -2.208 1.00 41.39 ? 109 LYS B N 1 ATOM 882 C CA . LYS A 1 106 ? 0.716 -3.687 -3.404 1.00 46.03 ? 109 LYS B CA 1 ATOM 883 C C . LYS A 1 106 ? 0.650 -2.467 -4.317 1.00 49.76 ? 109 LYS B C 1 ATOM 884 O O . LYS A 1 106 ? 0.763 -2.600 -5.539 1.00 52.95 ? 109 LYS B O 1 ATOM 885 C CB . LYS A 1 106 ? -0.684 -4.154 -3.019 1.00 54.01 ? 109 LYS B CB 1 ATOM 886 C CG . LYS A 1 106 ? -1.348 -5.004 -4.082 1.00 63.47 ? 109 LYS B CG 1 ATOM 887 C CD . LYS A 1 106 ? -2.461 -5.863 -3.506 1.00 68.37 ? 109 LYS B CD 1 ATOM 888 C CE . LYS A 1 106 ? -1.913 -7.084 -2.792 1.00 69.64 ? 109 LYS B CE 1 ATOM 889 N NZ . LYS A 1 106 ? -2.978 -8.091 -2.548 1.00 74.93 ? 109 LYS B NZ 1 ATOM 890 N N . LYS A 1 107 ? 0.463 -1.284 -3.735 1.00 48.19 ? 110 LYS B N 1 ATOM 891 C CA . LYS A 1 107 ? 0.662 -0.036 -4.487 1.00 51.53 ? 110 LYS B CA 1 ATOM 892 C C . LYS A 1 107 ? 1.447 0.984 -3.686 1.00 45.07 ? 110 LYS B C 1 ATOM 893 O O . LYS A 1 107 ? 1.298 1.078 -2.465 1.00 42.84 ? 110 LYS B O 1 ATOM 894 C CB . LYS A 1 107 ? -0.656 0.565 -4.975 1.00 54.08 ? 110 LYS B CB 1 ATOM 895 C CG . LYS A 1 107 ? -1.806 0.512 -3.986 1.00 59.45 ? 110 LYS B CG 1 ATOM 896 C CD . LYS A 1 107 ? -2.830 1.598 -4.290 1.00 65.31 ? 110 LYS B CD 1 ATOM 897 C CE . LYS A 1 107 ? -3.486 1.415 -5.653 1.00 69.50 ? 110 LYS B CE 1 ATOM 898 N NZ . LYS A 1 107 ? -3.830 2.710 -6.307 1.00 71.99 ? 110 LYS B NZ 1 ATOM 899 N N . PRO A 1 108 ? 2.314 1.748 -4.367 1.00 46.68 ? 111 PRO B N 1 ATOM 900 C CA . PRO A 1 108 ? 3.080 2.761 -3.640 1.00 43.17 ? 111 PRO B CA 1 ATOM 901 C C . PRO A 1 108 ? 2.227 3.747 -2.842 1.00 39.73 ? 111 PRO B C 1 ATOM 902 O O . PRO A 1 108 ? 1.093 4.060 -3.215 1.00 35.79 ? 111 PRO B O 1 ATOM 903 C CB . PRO A 1 108 ? 3.830 3.497 -4.745 1.00 46.68 ? 111 PRO B CB 1 ATOM 904 C CG . PRO A 1 108 ? 4.009 2.463 -5.805 1.00 53.41 ? 111 PRO B CG 1 ATOM 905 C CD . PRO A 1 108 ? 2.784 1.592 -5.756 1.00 51.93 ? 111 PRO B CD 1 ATOM 906 N N . VAL A 1 109 ? 2.785 4.206 -1.735 1.00 37.76 ? 112 VAL B N 1 ATOM 907 C CA . VAL A 1 109 ? 2.121 5.190 -0.891 1.00 40.40 ? 112 VAL B CA 1 ATOM 908 C C . VAL A 1 109 ? 2.542 6.588 -1.362 1.00 36.65 ? 112 VAL B C 1 ATOM 909 O O . VAL A 1 109 ? 3.666 6.786 -1.813 1.00 36.90 ? 112 VAL B O 1 ATOM 910 C CB . VAL A 1 109 ? 2.464 4.961 0.600 1.00 44.43 ? 112 VAL B CB 1 ATOM 911 C CG1 . VAL A 1 109 ? 3.925 5.289 0.897 1.00 41.36 ? 112 VAL B CG1 1 ATOM 912 C CG2 . VAL A 1 109 ? 1.532 5.767 1.501 1.00 49.40 ? 112 VAL B CG2 1 ATOM 913 N N . ALA A 1 110 ? 1.622 7.535 -1.292 1.00 36.78 ? 113 ALA B N 1 ATOM 914 C CA . ALA A 1 110 ? 1.926 8.933 -1.543 1.00 37.76 ? 113 ALA B CA 1 ATOM 915 C C . ALA A 1 110 ? 2.637 9.522 -0.335 1.00 35.84 ? 113 ALA B C 1 ATOM 916 O O . ALA A 1 110 ? 2.206 9.308 0.795 1.00 36.74 ? 113 ALA B O 1 ATOM 917 C CB . ALA A 1 110 ? 0.642 9.695 -1.808 1.00 40.19 ? 113 ALA B CB 1 ATOM 918 N N . PHE A 1 111 ? 3.717 10.264 -0.562 1.00 33.88 ? 114 PHE B N 1 ATOM 919 C CA . PHE A 1 111 ? 4.402 10.945 0.541 1.00 34.21 ? 114 PHE B CA 1 ATOM 920 C C . PHE A 1 111 ? 3.597 12.172 0.976 1.00 33.44 ? 114 PHE B C 1 ATOM 921 O O . PHE A 1 111 ? 2.801 12.711 0.215 1.00 33.29 ? 114 PHE B O 1 ATOM 922 C CB . PHE A 1 111 ? 5.834 11.378 0.168 1.00 34.17 ? 114 PHE B CB 1 ATOM 923 C CG . PHE A 1 111 ? 6.742 10.249 -0.270 1.00 34.64 ? 114 PHE B CG 1 ATOM 924 C CD1 . PHE A 1 111 ? 6.568 8.948 0.190 1.00 34.51 ? 114 PHE B CD1 1 ATOM 925 C CD2 . PHE A 1 111 ? 7.808 10.511 -1.130 1.00 36.48 ? 114 PHE B CD2 1 ATOM 926 C CE1 . PHE A 1 111 ? 7.424 7.931 -0.221 1.00 36.07 ? 114 PHE B CE1 1 ATOM 927 C CE2 . PHE A 1 111 ? 8.661 9.502 -1.542 1.00 35.59 ? 114 PHE B CE2 1 ATOM 928 C CZ . PHE A 1 111 ? 8.471 8.213 -1.090 1.00 34.18 ? 114 PHE B CZ 1 ATOM 929 N N . SER A 1 112 ? 3.798 12.581 2.221 1.00 30.31 ? 115 SER B N 1 ATOM 930 C CA . SER A 1 112 ? 3.082 13.714 2.789 1.00 33.66 ? 115 SER B CA 1 ATOM 931 C C . SER A 1 112 ? 3.936 14.304 3.915 1.00 33.31 ? 115 SER B C 1 ATOM 932 O O . SER A 1 112 ? 5.058 13.833 4.182 1.00 32.21 ? 115 SER B O 1 ATOM 933 C CB . SER A 1 112 ? 1.719 13.234 3.327 1.00 32.82 ? 115 SER B CB 1 ATOM 934 O OG . SER A 1 112 ? 1.893 12.330 4.428 1.00 30.53 ? 115 SER B OG 1 ATOM 935 N N . ASP A 1 113 ? 3.395 15.299 4.609 1.00 32.97 ? 116 ASP B N 1 ATOM 936 C CA . ASP A 1 113 ? 4.044 15.808 5.814 1.00 32.54 ? 116 ASP B CA 1 ATOM 937 C C . ASP A 1 113 ? 4.291 14.686 6.826 1.00 30.57 ? 116 ASP B C 1 ATOM 938 O O . ASP A 1 113 ? 5.228 14.776 7.618 1.00 31.93 ? 116 ASP B O 1 ATOM 939 C CB . ASP A 1 113 ? 3.209 16.920 6.474 1.00 34.57 ? 116 ASP B CB 1 ATOM 940 C CG . ASP A 1 113 ? 3.226 18.238 5.695 1.00 43.34 ? 116 ASP B CG 1 ATOM 941 O OD1 . ASP A 1 113 ? 4.070 18.420 4.782 1.00 40.58 ? 116 ASP B OD1 1 ATOM 942 O OD2 . ASP A 1 113 ? 2.383 19.112 6.016 1.00 41.85 ? 116 ASP B OD2 1 ATOM 943 N N . TYR A 1 114 ? 3.462 13.636 6.793 1.00 28.98 ? 117 TYR B N 1 ATOM 944 C CA . TYR A 1 114 ? 3.478 12.576 7.796 1.00 28.99 ? 117 TYR B CA 1 ATOM 945 C C . TYR A 1 114 ? 4.133 11.272 7.326 1.00 29.53 ? 117 TYR B C 1 ATOM 946 O O . TYR A 1 114 ? 4.432 10.400 8.149 1.00 25.84 ? 117 TYR B O 1 ATOM 947 C CB . TYR A 1 114 ? 2.043 12.296 8.257 1.00 32.12 ? 117 TYR B CB 1 ATOM 948 C CG . TYR A 1 114 ? 1.285 13.576 8.540 1.00 34.24 ? 117 TYR B CG 1 ATOM 949 C CD1 . TYR A 1 114 ? 1.509 14.291 9.709 1.00 32.53 ? 117 TYR B CD1 1 ATOM 950 C CD2 . TYR A 1 114 ? 0.383 14.093 7.617 1.00 34.51 ? 117 TYR B CD2 1 ATOM 951 C CE1 . TYR A 1 114 ? 0.847 15.473 9.957 1.00 34.65 ? 117 TYR B CE1 1 ATOM 952 C CE2 . TYR A 1 114 ? -0.295 15.272 7.864 1.00 35.94 ? 117 TYR B CE2 1 ATOM 953 C CZ . TYR A 1 114 ? -0.064 15.957 9.033 1.00 37.19 ? 117 TYR B CZ 1 ATOM 954 O OH . TYR A 1 114 ? -0.720 17.146 9.266 1.00 38.55 ? 117 TYR B OH 1 ATOM 955 N N . ILE A 1 115 ? 4.360 11.166 6.014 1.00 26.97 ? 118 ILE B N 1 ATOM 956 C CA . ILE A 1 115 ? 4.859 9.962 5.387 1.00 27.99 ? 118 ILE B CA 1 ATOM 957 C C . ILE A 1 115 ? 6.077 10.299 4.502 1.00 26.51 ? 118 ILE B C 1 ATOM 958 O O . ILE A 1 115 ? 5.981 11.092 3.560 1.00 31.69 ? 118 ILE B O 1 ATOM 959 C CB . ILE A 1 115 ? 3.747 9.294 4.548 1.00 27.61 ? 118 ILE B CB 1 ATOM 960 C CG1 . ILE A 1 115 ? 2.570 8.884 5.462 1.00 27.61 ? 118 ILE B CG1 1 ATOM 961 C CG2 . ILE A 1 115 ? 4.282 8.068 3.838 1.00 27.07 ? 118 ILE B CG2 1 ATOM 962 C CD1 . ILE A 1 115 ? 1.342 8.392 4.739 1.00 28.70 ? 118 ILE B CD1 1 ATOM 963 N N . HIS A 1 116 ? 7.210 9.688 4.808 1.00 27.53 ? 119 HIS B N 1 ATOM 964 C CA . HIS A 1 116 ? 8.461 10.001 4.118 1.00 27.13 ? 119 HIS B CA 1 ATOM 965 C C . HIS A 1 116 ? 9.508 8.966 4.452 1.00 25.14 ? 119 HIS B C 1 ATOM 966 O O . HIS A 1 116 ? 9.649 8.595 5.606 1.00 25.08 ? 119 HIS B O 1 ATOM 967 C CB . HIS A 1 116 ? 8.967 11.391 4.522 1.00 28.77 ? 119 HIS B CB 1 ATOM 968 C CG . HIS A 1 116 ? 10.022 11.928 3.608 1.00 32.16 ? 119 HIS B CG 1 ATOM 969 N ND1 . HIS A 1 116 ? 9.718 12.609 2.453 1.00 34.92 ? 119 HIS B ND1 1 ATOM 970 C CD2 . HIS A 1 116 ? 11.372 11.864 3.665 1.00 33.76 ? 119 HIS B CD2 1 ATOM 971 C CE1 . HIS A 1 116 ? 10.838 12.952 1.838 1.00 35.27 ? 119 HIS B CE1 1 ATOM 972 N NE2 . HIS A 1 116 ? 11.856 12.505 2.551 1.00 36.13 ? 119 HIS B NE2 1 ATOM 973 N N . PRO A 1 117 ? 10.269 8.506 3.452 1.00 25.13 ? 120 PRO B N 1 ATOM 974 C CA . PRO A 1 117 ? 11.197 7.390 3.688 1.00 28.90 ? 120 PRO B CA 1 ATOM 975 C C . PRO A 1 117 ? 12.506 7.761 4.392 1.00 27.15 ? 120 PRO B C 1 ATOM 976 O O . PRO A 1 117 ? 13.024 8.878 4.214 1.00 27.91 ? 120 PRO B O 1 ATOM 977 C CB . PRO A 1 117 ? 11.492 6.886 2.272 1.00 29.14 ? 120 PRO B CB 1 ATOM 978 C CG . PRO A 1 117 ? 11.325 8.095 1.425 1.00 30.98 ? 120 PRO B CG 1 ATOM 979 C CD . PRO A 1 117 ? 10.179 8.846 2.022 1.00 27.64 ? 120 PRO B CD 1 ATOM 980 N N . VAL A 1 118 ? 13.028 6.818 5.177 1.00 24.94 ? 121 VAL B N 1 ATOM 981 C CA . VAL A 1 118 ? 14.364 6.939 5.773 1.00 26.27 ? 121 VAL B CA 1 ATOM 982 C C . VAL A 1 118 ? 15.441 6.466 4.801 1.00 27.94 ? 121 VAL B C 1 ATOM 983 O O . VAL A 1 118 ? 15.141 5.716 3.886 1.00 29.75 ? 121 VAL B O 1 ATOM 984 C CB . VAL A 1 118 ? 14.434 6.158 7.099 1.00 29.25 ? 121 VAL B CB 1 ATOM 985 C CG1 . VAL A 1 118 ? 14.478 4.636 6.855 1.00 28.13 ? 121 VAL B CG1 1 ATOM 986 C CG2 . VAL A 1 118 ? 15.604 6.653 7.943 1.00 29.39 ? 121 VAL B CG2 1 ATOM 987 N N . CYS A 1 119 ? 16.677 6.946 4.956 1.00 28.21 ? 122 CYS B N 1 ATOM 988 C CA . CYS A 1 119 ? 17.795 6.480 4.123 1.00 29.20 ? 122 CYS B CA 1 ATOM 989 C C . CYS A 1 119 ? 18.400 5.237 4.713 1.00 29.60 ? 122 CYS B C 1 ATOM 990 O O . CYS A 1 119 ? 18.378 5.039 5.928 1.00 25.73 ? 122 CYS B O 1 ATOM 991 C CB . CYS A 1 119 ? 18.918 7.500 4.055 1.00 30.62 ? 122 CYS B CB 1 ATOM 992 S SG . CYS A 1 119 ? 18.445 9.102 3.428 1.00 32.23 ? 122 CYS B SG 1 ATOM 993 N N . LEU A 1 120 ? 18.992 4.426 3.857 1.00 27.96 ? 123 LEU B N 1 ATOM 994 C CA . LEU A 1 120 ? 19.796 3.317 4.325 1.00 29.56 ? 123 LEU B CA 1 ATOM 995 C C . LEU A 1 120 ? 21.249 3.707 4.145 1.00 32.67 ? 123 LEU B C 1 ATOM 996 O O . LEU A 1 120 ? 21.601 4.361 3.156 1.00 28.46 ? 123 LEU B O 1 ATOM 997 C CB . LEU A 1 120 ? 19.475 2.025 3.563 1.00 32.15 ? 123 LEU B CB 1 ATOM 998 C CG . LEU A 1 120 ? 18.055 1.477 3.752 1.00 33.80 ? 123 LEU B CG 1 ATOM 999 C CD1 . LEU A 1 120 ? 17.908 0.180 2.985 1.00 37.45 ? 123 LEU B CD1 1 ATOM 1000 C CD2 . LEU A 1 120 ? 17.699 1.259 5.219 1.00 35.99 ? 123 LEU B CD2 1 ATOM 1001 N N . PRO A 1 121 ? 22.104 3.309 5.100 1.00 31.35 ? 124 PRO B N 1 ATOM 1002 C CA . PRO A 1 121 ? 23.495 3.730 5.049 1.00 35.08 ? 124 PRO B CA 1 ATOM 1003 C C . PRO A 1 121 ? 24.324 3.113 3.927 1.00 35.94 ? 124 PRO B C 1 ATOM 1004 O O . PRO A 1 121 ? 24.150 1.941 3.584 1.00 36.75 ? 124 PRO B O 1 ATOM 1005 C CB . PRO A 1 121 ? 24.045 3.255 6.389 1.00 35.66 ? 124 PRO B CB 1 ATOM 1006 C CG . PRO A 1 121 ? 23.232 2.066 6.731 1.00 34.98 ? 124 PRO B CG 1 ATOM 1007 C CD . PRO A 1 121 ? 21.850 2.388 6.218 1.00 33.87 ? 124 PRO B CD 1 ATOM 1008 N N . ASP A 1 122 ? 25.209 3.939 3.378 1.00 36.62 ? 125 ASP B N 1 ATOM 1009 C CA . ASP A 1 122 ? 26.372 3.504 2.612 1.00 37.75 ? 125 ASP B CA 1 ATOM 1010 C C . ASP A 1 122 ? 27.493 3.096 3.575 1.00 41.96 ? 125 ASP B C 1 ATOM 1011 O O . ASP A 1 122 ? 27.354 3.242 4.801 1.00 37.96 ? 125 ASP B O 1 ATOM 1012 C CB . ASP A 1 122 ? 26.865 4.638 1.711 1.00 42.81 ? 125 ASP B CB 1 ATOM 1013 C CG . ASP A 1 122 ? 27.165 5.910 2.486 1.00 45.39 ? 125 ASP B CG 1 ATOM 1014 O OD1 . ASP A 1 122 ? 26.211 6.553 2.994 1.00 49.75 ? 125 ASP B OD1 1 ATOM 1015 O OD2 . ASP A 1 122 ? 28.346 6.265 2.594 1.00 48.91 ? 125 ASP B OD2 1 ATOM 1016 N N . ARG A 1 123 ? 28.602 2.603 3.017 1.00 38.62 ? 126 ARG B N 1 ATOM 1017 C CA . ARG A 1 123 ? 29.726 2.130 3.816 1.00 43.96 ? 126 ARG B CA 1 ATOM 1018 C C . ARG A 1 123 ? 30.354 3.218 4.678 1.00 39.48 ? 126 ARG B C 1 ATOM 1019 O O . ARG A 1 123 ? 30.723 2.949 5.807 1.00 37.56 ? 126 ARG B O 1 ATOM 1020 C CB . ARG A 1 123 ? 30.815 1.514 2.921 1.00 46.54 ? 126 ARG B CB 1 ATOM 1021 C CG . ARG A 1 123 ? 31.786 0.638 3.694 1.00 54.83 ? 126 ARG B CG 1 ATOM 1022 C CD . ARG A 1 123 ? 32.825 -0.011 2.795 1.00 60.88 ? 126 ARG B CD 1 ATOM 1023 N NE . ARG A 1 123 ? 32.214 -0.745 1.681 1.00 70.73 ? 126 ARG B NE 1 ATOM 1024 C CZ . ARG A 1 123 ? 31.708 -1.980 1.749 1.00 73.07 ? 126 ARG B CZ 1 ATOM 1025 N NH1 . ARG A 1 123 ? 31.180 -2.531 0.659 1.00 75.23 ? 126 ARG B NH1 1 ATOM 1026 N NH2 . ARG A 1 123 ? 31.725 -2.674 2.888 1.00 68.55 ? 126 ARG B NH2 1 ATOM 1027 N N . GLU A 1 124 ? 30.500 4.426 4.134 1.00 42.35 ? 127 GLU B N 1 ATOM 1028 C CA . GLU A 1 124 ? 31.201 5.490 4.852 1.00 44.20 ? 127 GLU B CA 1 ATOM 1029 C C . GLU A 1 124 ? 30.343 5.964 5.993 1.00 39.41 ? 127 GLU B C 1 ATOM 1030 O O . GLU A 1 124 ? 30.837 6.214 7.079 1.00 39.64 ? 127 GLU B O 1 ATOM 1031 C CB . GLU A 1 124 ? 31.568 6.655 3.945 1.00 48.61 ? 127 GLU B CB 1 ATOM 1032 C CG . GLU A 1 124 ? 32.832 7.373 4.398 1.00 59.49 ? 127 GLU B CG 1 ATOM 1033 C CD . GLU A 1 124 ? 33.073 8.681 3.657 1.00 70.45 ? 127 GLU B CD 1 ATOM 1034 O OE1 . GLU A 1 124 ? 32.125 9.488 3.544 1.00 79.05 ? 127 GLU B OE1 1 ATOM 1035 O OE2 . GLU A 1 124 ? 34.211 8.917 3.193 1.00 67.14 ? 127 GLU B OE2 1 ATOM 1036 N N . THR A 1 125 ? 29.049 6.058 5.747 1.00 36.59 ? 128 THR B N 1 ATOM 1037 C CA . THR A 1 125 ? 28.112 6.468 6.781 1.00 35.48 ? 128 THR B CA 1 ATOM 1038 C C . THR A 1 125 ? 28.045 5.419 7.897 1.00 35.26 ? 128 THR B C 1 ATOM 1039 O O . THR A 1 125 ? 28.056 5.775 9.080 1.00 37.79 ? 128 THR B O 1 ATOM 1040 C CB . THR A 1 125 ? 26.731 6.796 6.152 1.00 36.92 ? 128 THR B CB 1 ATOM 1041 O OG1 . THR A 1 125 ? 26.894 7.881 5.238 1.00 37.16 ? 128 THR B OG1 1 ATOM 1042 C CG2 . THR A 1 125 ? 25.688 7.177 7.195 1.00 38.10 ? 128 THR B CG2 1 ATOM 1043 N N . ALA A 1 126 ? 28.032 4.134 7.539 1.00 34.35 ? 129 ALA B N 1 ATOM 1044 C CA . ALA A 1 126 ? 28.056 3.052 8.531 1.00 33.33 ? 129 ALA B CA 1 ATOM 1045 C C . ALA A 1 126 ? 29.307 3.093 9.405 1.00 33.47 ? 129 ALA B C 1 ATOM 1046 O O . ALA A 1 126 ? 29.220 2.983 10.636 1.00 32.87 ? 129 ALA B O 1 ATOM 1047 C CB . ALA A 1 126 ? 27.936 1.683 7.858 1.00 33.49 ? 129 ALA B CB 1 ATOM 1048 N N . ALA A 1 127 A 30.462 3.229 8.763 1.00 31.27 ? 129 ALA B N 1 ATOM 1049 C CA . ALA A 1 127 A 31.733 3.278 9.470 1.00 33.31 ? 129 ALA B CA 1 ATOM 1050 C C . ALA A 1 127 A 31.764 4.480 10.418 1.00 35.28 ? 129 ALA B C 1 ATOM 1051 O O . ALA A 1 127 A 32.259 4.381 11.538 1.00 34.78 ? 129 ALA B O 1 ATOM 1052 C CB . ALA A 1 127 A 32.906 3.363 8.481 1.00 35.41 ? 129 ALA B CB 1 ATOM 1053 N N . SER A 1 128 B 31.229 5.604 9.950 1.00 33.70 ? 129 SER B N 1 ATOM 1054 C CA . SER A 1 128 B 31.336 6.878 10.639 1.00 35.99 ? 129 SER B CA 1 ATOM 1055 C C . SER A 1 128 B 30.410 6.975 11.833 1.00 35.08 ? 129 SER B C 1 ATOM 1056 O O . SER A 1 128 B 30.789 7.497 12.872 1.00 32.00 ? 129 SER B O 1 ATOM 1057 C CB . SER A 1 128 B 30.982 8.001 9.674 1.00 37.39 ? 129 SER B CB 1 ATOM 1058 O OG . SER A 1 128 B 31.972 8.087 8.666 1.00 45.58 ? 129 SER B OG 1 ATOM 1059 N N . LEU A 1 129 C 29.189 6.488 11.669 1.00 32.51 ? 129 LEU B N 1 ATOM 1060 C CA . LEU A 1 129 C 28.153 6.716 12.654 1.00 34.39 ? 129 LEU B CA 1 ATOM 1061 C C . LEU A 1 129 C 27.980 5.549 13.610 1.00 33.14 ? 129 LEU B C 1 ATOM 1062 O O . LEU A 1 129 C 27.520 5.740 14.734 1.00 33.15 ? 129 LEU B O 1 ATOM 1063 C CB . LEU A 1 129 C 26.822 7.004 11.963 1.00 33.60 ? 129 LEU B CB 1 ATOM 1064 C CG . LEU A 1 129 C 26.684 8.244 11.102 1.00 35.77 ? 129 LEU B CG 1 ATOM 1065 C CD1 . LEU A 1 129 C 25.218 8.422 10.746 1.00 37.62 ? 129 LEU B CD1 1 ATOM 1066 C CD2 . LEU A 1 129 C 27.255 9.498 11.756 1.00 36.77 ? 129 LEU B CD2 1 ATOM 1067 N N . LEU A 1 130 ? 28.306 4.337 13.178 1.00 32.00 ? 130 LEU B N 1 ATOM 1068 C CA . LEU A 1 130 ? 28.049 3.190 14.038 1.00 34.23 ? 130 LEU B CA 1 ATOM 1069 C C . LEU A 1 130 ? 29.282 2.927 14.909 1.00 34.92 ? 130 LEU B C 1 ATOM 1070 O O . LEU A 1 130 ? 30.069 2.004 14.682 1.00 38.75 ? 130 LEU B O 1 ATOM 1071 C CB . LEU A 1 130 ? 27.594 1.971 13.221 1.00 37.80 ? 130 LEU B CB 1 ATOM 1072 C CG . LEU A 1 130 ? 26.738 0.952 13.967 1.00 39.60 ? 130 LEU B CG 1 ATOM 1073 C CD1 . LEU A 1 130 ? 25.377 1.507 14.350 1.00 37.58 ? 130 LEU B CD1 1 ATOM 1074 C CD2 . LEU A 1 130 ? 26.573 -0.302 13.123 1.00 49.26 ? 130 LEU B CD2 1 ATOM 1075 N N . GLN A 1 131 ? 29.444 3.797 15.903 1.00 29.69 ? 131 GLN B N 1 ATOM 1076 C CA . GLN A 1 131 ? 30.550 3.741 16.820 1.00 30.96 ? 131 GLN B CA 1 ATOM 1077 C C . GLN A 1 131 ? 30.032 3.826 18.247 1.00 31.20 ? 131 GLN B C 1 ATOM 1078 O O . GLN A 1 131 ? 29.040 4.507 18.534 1.00 28.31 ? 131 GLN B O 1 ATOM 1079 C CB . GLN A 1 131 ? 31.533 4.881 16.543 1.00 34.00 ? 131 GLN B CB 1 ATOM 1080 C CG . GLN A 1 131 ? 31.918 5.014 15.078 1.00 36.23 ? 131 GLN B CG 1 ATOM 1081 C CD . GLN A 1 131 ? 33.243 5.715 14.860 1.00 37.97 ? 131 GLN B CD 1 ATOM 1082 O OE1 . GLN A 1 131 ? 34.266 5.305 15.409 1.00 41.01 ? 131 GLN B OE1 1 ATOM 1083 N NE2 . GLN A 1 131 ? 33.238 6.768 14.052 1.00 37.97 ? 131 GLN B NE2 1 ATOM 1084 N N . ALA A 1 132 ? 30.731 3.144 19.140 1.00 33.52 ? 132 ALA B N 1 ATOM 1085 C CA . ALA A 1 132 ? 30.357 3.114 20.531 1.00 36.05 ? 132 ALA B CA 1 ATOM 1086 C C . ALA A 1 132 ? 30.352 4.520 21.114 1.00 32.67 ? 132 ALA B C 1 ATOM 1087 O O . ALA A 1 132 ? 31.292 5.305 20.913 1.00 34.71 ? 132 ALA B O 1 ATOM 1088 C CB . ALA A 1 132 ? 31.309 2.235 21.307 1.00 39.07 ? 132 ALA B CB 1 ATOM 1089 N N . GLY A 1 133 ? 29.290 4.824 21.844 1.00 29.45 ? 133 GLY B N 1 ATOM 1090 C CA . GLY A 1 133 ? 29.154 6.125 22.472 1.00 33.69 ? 133 GLY B CA 1 ATOM 1091 C C . GLY A 1 133 ? 28.292 7.088 21.686 1.00 32.20 ? 133 GLY B C 1 ATOM 1092 O O . GLY A 1 133 ? 27.750 8.017 22.265 1.00 35.32 ? 133 GLY B O 1 ATOM 1093 N N . TYR A 1 134 ? 28.176 6.883 20.371 1.00 31.02 ? 134 TYR B N 1 ATOM 1094 C CA . TYR A 1 134 ? 27.288 7.691 19.537 1.00 29.32 ? 134 TYR B CA 1 ATOM 1095 C C . TYR A 1 134 ? 25.849 7.251 19.768 1.00 29.85 ? 134 TYR B C 1 ATOM 1096 O O . TYR A 1 134 ? 25.570 6.065 19.940 1.00 27.37 ? 134 TYR B O 1 ATOM 1097 C CB . TYR A 1 134 ? 27.629 7.535 18.058 1.00 27.58 ? 134 TYR B CB 1 ATOM 1098 C CG . TYR A 1 134 ? 28.949 8.153 17.638 1.00 28.52 ? 134 TYR B CG 1 ATOM 1099 C CD1 . TYR A 1 134 ? 29.804 8.748 18.553 1.00 30.65 ? 134 TYR B CD1 1 ATOM 1100 C CD2 . TYR A 1 134 ? 29.353 8.107 16.311 1.00 29.99 ? 134 TYR B CD2 1 ATOM 1101 C CE1 . TYR A 1 134 ? 31.011 9.313 18.158 1.00 33.44 ? 134 TYR B CE1 1 ATOM 1102 C CE2 . TYR A 1 134 ? 30.562 8.663 15.905 1.00 31.80 ? 134 TYR B CE2 1 ATOM 1103 C CZ . TYR A 1 134 ? 31.379 9.268 16.824 1.00 32.65 ? 134 TYR B CZ 1 ATOM 1104 O OH . TYR A 1 134 ? 32.567 9.811 16.415 1.00 35.00 ? 134 TYR B OH 1 ATOM 1105 N N . LYS A 1 135 ? 24.937 8.214 19.753 1.00 26.45 ? 135 LYS B N 1 ATOM 1106 C CA . LYS A 1 135 ? 23.532 7.928 20.034 1.00 25.94 ? 135 LYS B CA 1 ATOM 1107 C C . LYS A 1 135 ? 22.698 7.845 18.772 1.00 25.85 ? 135 LYS B C 1 ATOM 1108 O O . LYS A 1 135 ? 22.909 8.592 17.847 1.00 28.71 ? 135 LYS B O 1 ATOM 1109 C CB . LYS A 1 135 ? 22.951 8.992 20.950 1.00 25.48 ? 135 LYS B CB 1 ATOM 1110 C CG . LYS A 1 135 ? 23.487 8.891 22.363 1.00 27.87 ? 135 LYS B CG 1 ATOM 1111 C CD . LYS A 1 135 ? 23.058 10.085 23.182 1.00 27.32 ? 135 LYS B CD 1 ATOM 1112 C CE . LYS A 1 135 ? 23.563 9.959 24.598 1.00 28.58 ? 135 LYS B CE 1 ATOM 1113 N NZ . LYS A 1 135 ? 23.123 11.141 25.369 1.00 30.23 ? 135 LYS B NZ 1 ATOM 1114 N N . GLY A 1 136 ? 21.762 6.904 18.754 1.00 24.83 ? 136 GLY B N 1 ATOM 1115 C CA . GLY A 1 136 ? 20.731 6.877 17.738 1.00 25.17 ? 136 GLY B CA 1 ATOM 1116 C C . GLY A 1 136 ? 19.378 6.891 18.400 1.00 26.33 ? 136 GLY B C 1 ATOM 1117 O O . GLY A 1 136 ? 19.264 7.016 19.621 1.00 23.05 ? 136 GLY B O 1 ATOM 1118 N N . ARG A 1 137 ? 18.344 6.772 17.590 1.00 26.08 ? 137 ARG B N 1 ATOM 1119 C CA . ARG A 1 137 ? 16.990 6.939 18.076 1.00 28.75 ? 137 ARG B CA 1 ATOM 1120 C C . ARG A 1 137 ? 16.110 5.767 17.679 1.00 26.68 ? 137 ARG B C 1 ATOM 1121 O O . ARG A 1 137 ? 16.170 5.280 16.542 1.00 24.85 ? 137 ARG B O 1 ATOM 1122 C CB . ARG A 1 137 ? 16.437 8.237 17.507 1.00 30.59 ? 137 ARG B CB 1 ATOM 1123 C CG . ARG A 1 137 ? 14.945 8.440 17.701 1.00 30.53 ? 137 ARG B CG 1 ATOM 1124 C CD . ARG A 1 137 ? 14.522 9.748 17.044 1.00 34.62 ? 137 ARG B CD 1 ATOM 1125 N NE . ARG A 1 137 ? 14.952 10.926 17.799 1.00 29.83 ? 137 ARG B NE 1 ATOM 1126 C CZ . ARG A 1 137 ? 14.863 12.174 17.355 1.00 29.49 ? 137 ARG B CZ 1 ATOM 1127 N NH1 . ARG A 1 137 ? 14.385 12.426 16.140 1.00 30.31 ? 137 ARG B NH1 1 ATOM 1128 N NH2 . ARG A 1 137 ? 15.259 13.175 18.130 1.00 27.32 ? 137 ARG B NH2 1 ATOM 1129 N N . VAL A 1 138 ? 15.275 5.351 18.621 1.00 23.41 ? 138 VAL B N 1 ATOM 1130 C CA . VAL A 1 138 ? 14.379 4.223 18.459 1.00 25.58 ? 138 VAL B CA 1 ATOM 1131 C C . VAL A 1 138 ? 12.956 4.704 18.738 1.00 26.98 ? 138 VAL B C 1 ATOM 1132 O O . VAL A 1 138 ? 12.723 5.481 19.669 1.00 25.23 ? 138 VAL B O 1 ATOM 1133 C CB . VAL A 1 138 ? 14.750 3.062 19.412 1.00 26.35 ? 138 VAL B CB 1 ATOM 1134 C CG1 . VAL A 1 138 ? 13.908 1.833 19.111 1.00 30.83 ? 138 VAL B CG1 1 ATOM 1135 C CG2 . VAL A 1 138 ? 16.221 2.730 19.268 0.70 30.27 ? 138 VAL B CG2 1 ATOM 1136 N N . THR A 1 139 ? 12.028 4.256 17.897 1.00 25.72 ? 139 THR B N 1 ATOM 1137 C CA . THR A 1 139 ? 10.619 4.632 17.956 1.00 25.16 ? 139 THR B CA 1 ATOM 1138 C C . THR A 1 139 ? 9.707 3.404 17.903 1.00 25.30 ? 139 THR B C 1 ATOM 1139 O O . THR A 1 139 ? 10.040 2.397 17.256 1.00 24.98 ? 139 THR B O 1 ATOM 1140 C CB . THR A 1 139 ? 10.247 5.493 16.737 1.00 29.58 ? 139 THR B CB 1 ATOM 1141 O OG1 . THR A 1 139 ? 10.879 4.934 15.580 1.00 27.41 ? 139 THR B OG1 1 ATOM 1142 C CG2 . THR A 1 139 ? 10.700 6.946 16.915 1.00 29.91 ? 139 THR B CG2 1 ATOM 1143 N N . GLY A 1 140 ? 8.556 3.484 18.581 1.00 23.84 ? 140 GLY B N 1 ATOM 1144 C CA . GLY A 1 140 ? 7.573 2.424 18.509 1.00 21.46 ? 140 GLY B CA 1 ATOM 1145 C C . GLY A 1 140 ? 6.371 2.603 19.413 1.00 24.69 ? 140 GLY B C 1 ATOM 1146 O O . GLY A 1 140 ? 6.311 3.546 20.222 1.00 25.61 ? 140 GLY B O 1 ATOM 1147 N N . TRP A 1 141 ? 5.402 1.705 19.224 1.00 25.68 ? 141 TRP B N 1 ATOM 1148 C CA . TRP A 1 141 ? 4.152 1.668 19.997 1.00 27.67 ? 141 TRP B CA 1 ATOM 1149 C C . TRP A 1 141 ? 4.117 0.489 20.962 1.00 27.68 ? 141 TRP B C 1 ATOM 1150 O O . TRP A 1 141 ? 3.044 0.123 21.475 1.00 29.69 ? 141 TRP B O 1 ATOM 1151 C CB . TRP A 1 141 ? 2.944 1.551 19.058 1.00 29.19 ? 141 TRP B CB 1 ATOM 1152 C CG . TRP A 1 141 ? 2.640 2.771 18.241 1.00 31.37 ? 141 TRP B CG 1 ATOM 1153 C CD1 . TRP A 1 141 ? 1.981 3.893 18.653 1.00 31.86 ? 141 TRP B CD1 1 ATOM 1154 C CD2 . TRP A 1 141 ? 2.955 2.974 16.859 1.00 28.85 ? 141 TRP B CD2 1 ATOM 1155 N NE1 . TRP A 1 141 ? 1.872 4.781 17.616 1.00 30.26 ? 141 TRP B NE1 1 ATOM 1156 C CE2 . TRP A 1 141 ? 2.476 4.250 16.508 1.00 30.06 ? 141 TRP B CE2 1 ATOM 1157 C CE3 . TRP A 1 141 ? 3.612 2.206 15.890 1.00 32.93 ? 141 TRP B CE3 1 ATOM 1158 C CZ2 . TRP A 1 141 ? 2.607 4.766 15.229 1.00 32.89 ? 141 TRP B CZ2 1 ATOM 1159 C CZ3 . TRP A 1 141 ? 3.760 2.733 14.612 1.00 34.70 ? 141 TRP B CZ3 1 ATOM 1160 C CH2 . TRP A 1 141 ? 3.260 4.000 14.296 1.00 34.07 ? 141 TRP B CH2 1 ATOM 1161 N N . GLY A 1 142 ? 5.277 -0.107 21.209 1.00 28.85 ? 142 GLY B N 1 ATOM 1162 C CA . GLY A 1 142 ? 5.376 -1.272 22.060 1.00 27.40 ? 142 GLY B CA 1 ATOM 1163 C C . GLY A 1 142 ? 5.244 -0.896 23.513 1.00 28.91 ? 142 GLY B C 1 ATOM 1164 O O . GLY A 1 142 ? 4.961 0.253 23.860 1.00 25.45 ? 142 GLY B O 1 ATOM 1165 N N . ASN A 1 143 ? 5.482 -1.874 24.362 1.00 26.61 ? 143 ASN B N 1 ATOM 1166 C CA . ASN A 1 143 ? 5.238 -1.708 25.782 1.00 32.12 ? 143 ASN B CA 1 ATOM 1167 C C . ASN A 1 143 ? 6.063 -0.575 26.411 1.00 32.79 ? 143 ASN B C 1 ATOM 1168 O O . ASN A 1 143 ? 7.221 -0.330 26.030 1.00 28.87 ? 143 ASN B O 1 ATOM 1169 C CB . ASN A 1 143 ? 5.464 -3.029 26.513 1.00 33.88 ? 143 ASN B CB 1 ATOM 1170 C CG . ASN A 1 143 ? 4.438 -4.080 26.147 1.00 36.25 ? 143 ASN B CG 1 ATOM 1171 O OD1 . ASN A 1 143 ? 3.393 -3.776 25.583 1.00 41.49 ? 143 ASN B OD1 1 ATOM 1172 N ND2 . ASN A 1 143 ? 4.725 -5.316 26.484 1.00 37.44 ? 143 ASN B ND2 1 ATOM 1173 N N . LEU A 1 144 ? 5.422 0.114 27.357 1.00 29.88 ? 144 LEU B N 1 ATOM 1174 C CA . LEU A 1 144 ? 6.037 1.171 28.148 1.00 31.05 ? 144 LEU B CA 1 ATOM 1175 C C . LEU A 1 144 ? 6.824 0.600 29.310 1.00 34.73 ? 144 LEU B C 1 ATOM 1176 O O . LEU A 1 144 ? 7.601 1.314 29.937 1.00 35.24 ? 144 LEU B O 1 ATOM 1177 C CB . LEU A 1 144 ? 4.970 2.091 28.720 1.00 33.34 ? 144 LEU B CB 1 ATOM 1178 C CG . LEU A 1 144 ? 4.199 2.901 27.680 1.00 35.22 ? 144 LEU B CG 1 ATOM 1179 C CD1 . LEU A 1 144 ? 3.096 3.685 28.368 1.00 34.56 ? 144 LEU B CD1 1 ATOM 1180 C CD2 . LEU A 1 144 ? 5.129 3.818 26.898 1.00 34.99 ? 144 LEU B CD2 1 ATOM 1181 N N . LYS A 1 145 ? 6.651 -0.682 29.673 1.00 33.96 ? 145 LYS B N 1 ATOM 1182 C CA . LYS A 1 145 ? 7.305 -1.352 30.781 1.00 41.09 ? 145 LYS B CA 1 ATOM 1183 C C . LYS A 1 145 ? 7.280 -2.850 30.495 1.00 38.58 ? 145 LYS B C 1 ATOM 1184 O O . LYS A 1 145 ? 6.631 -3.278 29.550 1.00 35.77 ? 145 LYS B O 1 ATOM 1185 C CB . LYS A 1 145 ? 6.568 -1.018 32.082 1.00 48.65 ? 145 LYS B CB 1 ATOM 1186 C CG . LYS A 1 145 ? 5.120 -1.493 32.167 1.00 72.12 ? 145 LYS B CG 1 ATOM 1187 C CD . LYS A 1 145 ? 4.450 -1.199 33.512 1.00 83.50 ? 145 LYS B CD 1 ATOM 1188 C CE . LYS A 1 145 ? 2.958 -1.512 33.483 1.00 91.35 ? 145 LYS B CE 1 ATOM 1189 N NZ . LYS A 1 145 ? 2.678 -2.949 33.195 1.00 87.79 ? 145 LYS B NZ 1 ATOM 1190 N N . GLU A 1 146 ? 7.896 -3.640 31.257 1.00 39.70 ? 146 GLU B N 1 ATOM 1191 C CA . GLU A 1 146 ? 7.746 -5.100 31.204 1.00 39.51 ? 146 GLU B CA 1 ATOM 1192 C C . GLU A 1 146 ? 6.360 -5.490 31.698 1.00 42.84 ? 146 GLU B C 1 ATOM 1193 O O . GLU A 1 146 ? 5.928 -5.016 32.743 1.00 43.30 ? 146 GLU B O 1 ATOM 1194 C CB . GLU A 1 146 ? 8.795 -5.785 32.078 1.00 41.81 ? 146 GLU B CB 1 ATOM 1195 C CG . GLU A 1 146 ? 10.236 -5.572 31.636 1.00 40.04 ? 146 GLU B CG 1 ATOM 1196 C CD . GLU A 1 146 ? 11.240 -6.308 32.513 1.00 38.01 ? 146 GLU B CD 1 ATOM 1197 O OE1 . GLU A 1 146 ? 12.448 -5.975 32.477 1.00 36.03 ? 146 GLU B OE1 1 ATOM 1198 O OE2 . GLU A 1 146 ? 10.831 -7.230 33.240 1.00 45.95 ? 146 GLU B OE2 1 ATOM 1199 N N . THR A 1 147 ? 5.670 -6.334 30.937 1.00 51.28 ? 147 THR B N 1 ATOM 1200 C CA . THR A 1 147 ? 4.351 -6.869 31.319 1.00 67.87 ? 147 THR B CA 1 ATOM 1201 C C . THR A 1 147 ? 4.358 -8.401 31.273 1.00 68.85 ? 147 THR B C 1 ATOM 1202 O O . THR A 1 147 ? 5.314 -9.049 31.707 1.00 72.41 ? 147 THR B O 1 ATOM 1203 C CB . THR A 1 147 ? 3.234 -6.354 30.380 1.00 75.98 ? 147 THR B CB 1 ATOM 1204 O OG1 . THR A 1 147 ? 3.111 -4.929 30.496 1.00 68.32 ? 147 THR B OG1 1 ATOM 1205 C CG2 . THR A 1 147 ? 1.887 -7.007 30.714 1.00 82.17 ? 147 THR B CG2 1 ATOM 1206 N N . GLY A 1 155 ? 0.869 0.201 30.424 1.00 50.40 ? 150 GLY B N 1 ATOM 1207 C CA . GLY A 1 155 ? 1.266 -0.897 29.534 1.00 47.53 ? 150 GLY B CA 1 ATOM 1208 C C . GLY A 1 155 ? 1.628 -0.460 28.126 1.00 38.09 ? 150 GLY B C 1 ATOM 1209 O O . GLY A 1 155 ? 2.788 -0.502 27.736 1.00 38.37 ? 150 GLY B O 1 ATOM 1210 N N . GLN A 1 156 ? 0.628 -0.054 27.358 1.00 38.74 ? 151 GLN B N 1 ATOM 1211 C CA . GLN A 1 156 ? 0.809 0.343 25.955 1.00 39.67 ? 151 GLN B CA 1 ATOM 1212 C C . GLN A 1 156 ? 0.540 1.860 25.844 1.00 35.36 ? 151 GLN B C 1 ATOM 1213 O O . GLN A 1 156 ? -0.340 2.371 26.522 1.00 33.90 ? 151 GLN B O 1 ATOM 1214 C CB . GLN A 1 156 ? -0.158 -0.456 25.088 1.00 45.47 ? 151 GLN B CB 1 ATOM 1215 C CG . GLN A 1 156 ? -0.269 -1.929 25.492 1.00 57.42 ? 151 GLN B CG 1 ATOM 1216 C CD . GLN A 1 156 ? -1.682 -2.482 25.390 1.00 68.97 ? 151 GLN B CD 1 ATOM 1217 O OE1 . GLN A 1 156 ? -2.292 -2.871 26.393 1.00 77.17 ? 151 GLN B OE1 1 ATOM 1218 N NE2 . GLN A 1 156 ? -2.207 -2.522 24.176 1.00 75.65 ? 151 GLN B NE2 1 ATOM 1219 N N . PRO A 1 157 ? 1.301 2.589 25.004 1.00 30.99 ? 152 PRO B N 1 ATOM 1220 C CA . PRO A 1 157 ? 1.119 4.068 24.925 1.00 30.68 ? 152 PRO B CA 1 ATOM 1221 C C . PRO A 1 157 ? -0.052 4.530 24.043 1.00 31.44 ? 152 PRO B C 1 ATOM 1222 O O . PRO A 1 157 ? -0.442 3.829 23.117 1.00 32.19 ? 152 PRO B O 1 ATOM 1223 C CB . PRO A 1 157 ? 2.425 4.532 24.275 1.00 28.46 ? 152 PRO B CB 1 ATOM 1224 C CG . PRO A 1 157 ? 2.815 3.390 23.377 1.00 28.67 ? 152 PRO B CG 1 ATOM 1225 C CD . PRO A 1 157 ? 2.410 2.139 24.143 1.00 29.33 ? 152 PRO B CD 1 ATOM 1226 N N . SER A 1 158 ? -0.564 5.733 24.279 1.00 32.43 ? 153 SER B N 1 ATOM 1227 C CA . SER A 1 158 ? -1.581 6.286 23.388 1.00 34.84 ? 153 SER B CA 1 ATOM 1228 C C . SER A 1 158 ? -0.988 6.714 22.037 1.00 30.45 ? 153 SER B C 1 ATOM 1229 O O . SER A 1 158 ? -1.686 6.662 21.024 1.00 29.70 ? 153 SER B O 1 ATOM 1230 C CB . SER A 1 158 ? -2.350 7.437 24.056 1.00 42.31 ? 153 SER B CB 1 ATOM 1231 O OG . SER A 1 158 ? -1.451 8.361 24.638 1.00 49.54 ? 153 SER B OG 1 ATOM 1232 N N . VAL A 1 159 ? 0.284 7.124 22.015 1.00 27.10 ? 154 VAL B N 1 ATOM 1233 C CA . VAL A 1 159 ? 0.904 7.652 20.793 1.00 25.86 ? 154 VAL B CA 1 ATOM 1234 C C . VAL A 1 159 ? 2.324 7.142 20.654 1.00 24.90 ? 154 VAL B C 1 ATOM 1235 O O . VAL A 1 159 ? 2.950 6.718 21.626 1.00 23.87 ? 154 VAL B O 1 ATOM 1236 C CB . VAL A 1 159 ? 0.917 9.212 20.743 1.00 26.30 ? 154 VAL B CB 1 ATOM 1237 C CG1 . VAL A 1 159 ? -0.484 9.790 20.962 1.00 28.20 ? 154 VAL B CG1 1 ATOM 1238 C CG2 . VAL A 1 159 ? 1.865 9.798 21.779 1.00 27.15 ? 154 VAL B CG2 1 ATOM 1239 N N . LEU A 1 160 ? 2.826 7.225 19.432 1.00 23.80 ? 155 LEU B N 1 ATOM 1240 C CA . LEU A 1 160 ? 4.171 6.797 19.111 1.00 24.79 ? 155 LEU B CA 1 ATOM 1241 C C . LEU A 1 160 ? 5.194 7.323 20.144 1.00 25.50 ? 155 LEU B C 1 ATOM 1242 O O . LEU A 1 160 ? 5.152 8.506 20.544 1.00 25.82 ? 155 LEU B O 1 ATOM 1243 C CB . LEU A 1 160 ? 4.526 7.259 17.696 1.00 23.89 ? 155 LEU B CB 1 ATOM 1244 C CG . LEU A 1 160 ? 5.905 6.818 17.217 1.00 25.94 ? 155 LEU B CG 1 ATOM 1245 C CD1 . LEU A 1 160 ? 5.972 5.311 17.087 1.00 25.74 ? 155 LEU B CD1 1 ATOM 1246 C CD2 . LEU A 1 160 ? 6.225 7.494 15.891 1.00 27.98 ? 155 LEU B CD2 1 ATOM 1247 N N . GLN A 1 161 ? 6.085 6.439 20.582 1.00 24.19 ? 156 GLN B N 1 ATOM 1248 C CA . GLN A 1 161 ? 7.116 6.793 21.541 1.00 24.16 ? 156 GLN B CA 1 ATOM 1249 C C . GLN A 1 161 ? 8.480 6.888 20.868 1.00 25.19 ? 156 GLN B C 1 ATOM 1250 O O . GLN A 1 161 ? 8.713 6.249 19.846 1.00 25.08 ? 156 GLN B O 1 ATOM 1251 C CB . GLN A 1 161 ? 7.165 5.786 22.676 1.00 24.16 ? 156 GLN B CB 1 ATOM 1252 C CG . GLN A 1 161 ? 5.892 5.710 23.490 1.00 26.34 ? 156 GLN B CG 1 ATOM 1253 C CD . GLN A 1 161 ? 5.587 6.981 24.270 1.00 28.38 ? 156 GLN B CD 1 ATOM 1254 O OE1 . GLN A 1 161 ? 6.250 7.300 25.259 1.00 28.47 ? 156 GLN B OE1 1 ATOM 1255 N NE2 . GLN A 1 161 ? 4.549 7.690 23.851 1.00 31.75 ? 156 GLN B NE2 1 ATOM 1256 N N . VAL A 1 162 ? 9.369 7.670 21.482 1.00 26.49 ? 157 VAL B N 1 ATOM 1257 C CA . VAL A 1 162 ? 10.726 7.917 20.969 1.00 24.73 ? 157 VAL B CA 1 ATOM 1258 C C . VAL A 1 162 ? 11.720 7.910 22.138 1.00 26.69 ? 157 VAL B C 1 ATOM 1259 O O . VAL A 1 162 ? 11.409 8.378 23.241 1.00 24.99 ? 157 VAL B O 1 ATOM 1260 C CB . VAL A 1 162 ? 10.824 9.255 20.174 1.00 27.00 ? 157 VAL B CB 1 ATOM 1261 C CG1 . VAL A 1 162 ? 10.457 10.462 21.011 1.00 29.22 ? 157 VAL B CG1 1 ATOM 1262 C CG2 . VAL A 1 162 ? 12.215 9.446 19.583 1.00 30.34 ? 157 VAL B CG2 1 ATOM 1263 N N . VAL A 1 163 ? 12.909 7.362 21.889 1.00 24.11 ? 158 VAL B N 1 ATOM 1264 C CA . VAL A 1 163 ? 14.001 7.384 22.853 1.00 26.43 ? 158 VAL B CA 1 ATOM 1265 C C . VAL A 1 163 ? 15.346 7.415 22.111 1.00 27.64 ? 158 VAL B C 1 ATOM 1266 O O . VAL A 1 163 ? 15.471 6.862 21.005 1.00 26.27 ? 158 VAL B O 1 ATOM 1267 C CB . VAL A 1 163 ? 13.926 6.189 23.826 1.00 30.24 ? 158 VAL B CB 1 ATOM 1268 C CG1 . VAL A 1 163 ? 14.326 4.877 23.161 1.00 30.46 ? 158 VAL B CG1 1 ATOM 1269 C CG2 . VAL A 1 163 ? 14.775 6.445 25.068 1.00 33.80 ? 158 VAL B CG2 1 ATOM 1270 N N . ASN A 1 164 ? 16.322 8.100 22.693 1.00 25.16 ? 159 ASN B N 1 ATOM 1271 C CA . ASN A 1 164 ? 17.679 8.153 22.125 1.00 25.67 ? 159 ASN B CA 1 ATOM 1272 C C . ASN A 1 164 ? 18.612 7.327 22.998 1.00 26.77 ? 159 ASN B C 1 ATOM 1273 O O . ASN A 1 164 ? 18.537 7.407 24.229 1.00 26.39 ? 159 ASN B O 1 ATOM 1274 C CB . ASN A 1 164 ? 18.200 9.586 22.082 1.00 25.95 ? 159 ASN B CB 1 ATOM 1275 C CG . ASN A 1 164 ? 17.357 10.502 21.229 1.00 24.95 ? 159 ASN B CG 1 ATOM 1276 O OD1 . ASN A 1 164 ? 16.720 10.075 20.296 1.00 26.26 ? 159 ASN B OD1 1 ATOM 1277 N ND2 . ASN A 1 164 ? 17.405 11.795 21.533 1.00 28.16 ? 159 ASN B ND2 1 ATOM 1278 N N . LEU A 1 165 ? 19.495 6.544 22.376 1.00 23.55 ? 160 LEU B N 1 ATOM 1279 C CA . LEU A 1 165 ? 20.295 5.584 23.110 1.00 24.80 ? 160 LEU B CA 1 ATOM 1280 C C . LEU A 1 165 ? 21.702 5.447 22.512 1.00 25.30 ? 160 LEU B C 1 ATOM 1281 O O . LEU A 1 165 ? 21.861 5.463 21.287 1.00 23.50 ? 160 LEU B O 1 ATOM 1282 C CB . LEU A 1 165 ? 19.612 4.224 23.123 1.00 26.11 ? 160 LEU B CB 1 ATOM 1283 C CG . LEU A 1 165 ? 18.248 4.161 23.848 1.00 27.56 ? 160 LEU B CG 1 ATOM 1284 C CD1 . LEU A 1 165 ? 17.607 2.834 23.543 1.00 29.77 ? 160 LEU B CD1 1 ATOM 1285 C CD2 . LEU A 1 165 ? 18.387 4.343 25.352 1.00 27.35 ? 160 LEU B CD2 1 ATOM 1286 N N . PRO A 1 166 ? 22.720 5.308 23.376 1.00 23.02 ? 161 PRO B N 1 ATOM 1287 C CA . PRO A 1 166 ? 24.088 5.185 22.884 1.00 22.81 ? 161 PRO B CA 1 ATOM 1288 C C . PRO A 1 166 ? 24.380 3.752 22.447 1.00 26.31 ? 161 PRO B C 1 ATOM 1289 O O . PRO A 1 166 ? 23.886 2.809 23.062 1.00 26.65 ? 161 PRO B O 1 ATOM 1290 C CB . PRO A 1 166 ? 24.937 5.543 24.105 1.00 23.84 ? 161 PRO B CB 1 ATOM 1291 C CG . PRO A 1 166 ? 24.108 5.136 25.258 1.00 23.11 ? 161 PRO B CG 1 ATOM 1292 C CD . PRO A 1 166 ? 22.672 5.306 24.849 1.00 22.90 ? 161 PRO B CD 1 ATOM 1293 N N . ILE A 1 167 ? 25.155 3.623 21.369 1.00 28.80 ? 162 ILE B N 1 ATOM 1294 C CA . ILE A 1 167 ? 25.700 2.362 20.908 1.00 26.81 ? 162 ILE B CA 1 ATOM 1295 C C . ILE A 1 167 ? 26.733 1.898 21.906 1.00 29.68 ? 162 ILE B C 1 ATOM 1296 O O . ILE A 1 167 ? 27.506 2.706 22.448 1.00 30.09 ? 162 ILE B O 1 ATOM 1297 C CB . ILE A 1 167 ? 26.349 2.513 19.510 1.00 28.70 ? 162 ILE B CB 1 ATOM 1298 C CG1 . ILE A 1 167 ? 25.266 2.801 18.466 1.00 31.27 ? 162 ILE B CG1 1 ATOM 1299 C CG2 . ILE A 1 167 ? 27.092 1.239 19.108 1.00 30.81 ? 162 ILE B CG2 1 ATOM 1300 C CD1 . ILE A 1 167 ? 25.776 3.502 17.225 1.00 32.18 ? 162 ILE B CD1 1 ATOM 1301 N N . VAL A 1 168 ? 26.742 0.590 22.143 1.00 28.84 ? 163 VAL B N 1 ATOM 1302 C CA . VAL A 1 168 ? 27.590 -0.004 23.157 1.00 31.17 ? 163 VAL B CA 1 ATOM 1303 C C . VAL A 1 168 ? 28.632 -0.900 22.478 1.00 32.39 ? 163 VAL B C 1 ATOM 1304 O O . VAL A 1 168 ? 28.349 -1.513 21.452 1.00 33.91 ? 163 VAL B O 1 ATOM 1305 C CB . VAL A 1 168 ? 26.730 -0.804 24.163 1.00 32.59 ? 163 VAL B CB 1 ATOM 1306 C CG1 . VAL A 1 168 ? 27.599 -1.582 25.134 1.00 33.61 ? 163 VAL B CG1 1 ATOM 1307 C CG2 . VAL A 1 168 ? 25.802 0.142 24.922 1.00 34.01 ? 163 VAL B CG2 1 ATOM 1308 N N . GLU A 1 169 ? 29.813 -0.971 23.080 1.00 32.79 ? 164 GLU B N 1 ATOM 1309 C CA . GLU A 1 169 ? 30.964 -1.718 22.559 1.00 36.89 ? 164 GLU B CA 1 ATOM 1310 C C . GLU A 1 169 ? 30.668 -3.205 22.583 1.00 35.99 ? 164 GLU B C 1 ATOM 1311 O O . GLU A 1 169 ? 29.992 -3.699 23.492 1.00 32.73 ? 164 GLU B O 1 ATOM 1312 C CB . GLU A 1 169 ? 32.221 -1.488 23.422 1.00 42.68 ? 164 GLU B CB 1 ATOM 1313 C CG . GLU A 1 169 ? 32.459 -0.061 23.875 1.00 50.86 ? 164 GLU B CG 1 ATOM 1314 C CD . GLU A 1 169 ? 31.820 0.243 25.214 1.00 54.62 ? 164 GLU B CD 1 ATOM 1315 O OE1 . GLU A 1 169 ? 32.436 -0.101 26.248 1.00 61.17 ? 164 GLU B OE1 1 ATOM 1316 O OE2 . GLU A 1 169 ? 30.707 0.827 25.226 1.00 44.58 ? 164 GLU B OE2 1 ATOM 1317 N N . ARG A 1 170 ? 31.210 -3.924 21.610 1.00 38.74 ? 165 ARG B N 1 ATOM 1318 C CA . ARG A 1 170 ? 30.879 -5.339 21.444 1.00 40.84 ? 165 ARG B CA 1 ATOM 1319 C C . ARG A 1 170 ? 31.191 -6.190 22.679 1.00 38.53 ? 165 ARG B C 1 ATOM 1320 O O . ARG A 1 170 ? 30.394 -7.043 23.036 1.00 39.73 ? 165 ARG B O 1 ATOM 1321 C CB . ARG A 1 170 ? 31.547 -5.923 20.185 1.00 47.03 ? 165 ARG B CB 1 ATOM 1322 C CG . ARG A 1 170 ? 30.977 -7.289 19.786 1.00 56.24 ? 165 ARG B CG 1 ATOM 1323 C CD . ARG A 1 170 ? 31.202 -7.638 18.316 1.00 60.68 ? 165 ARG B CD 1 ATOM 1324 N NE . ARG A 1 170 ? 30.415 -6.805 17.402 1.00 58.19 ? 165 ARG B NE 1 ATOM 1325 C CZ . ARG A 1 170 ? 29.166 -7.050 16.993 1.00 60.28 ? 165 ARG B CZ 1 ATOM 1326 N NH1 . ARG A 1 170 ? 28.495 -8.120 17.405 1.00 54.45 ? 165 ARG B NH1 1 ATOM 1327 N NH2 . ARG A 1 170 ? 28.569 -6.196 16.161 1.00 63.81 ? 165 ARG B NH2 1 ATOM 1328 N N . PRO A 1 171 ? 32.349 -5.968 23.335 1.00 40.40 ? 166 PRO B N 1 ATOM 1329 C CA . PRO A 1 171 ? 32.645 -6.762 24.525 1.00 42.17 ? 166 PRO B CA 1 ATOM 1330 C C . PRO A 1 171 ? 31.609 -6.598 25.630 1.00 39.27 ? 166 PRO B C 1 ATOM 1331 O O . PRO A 1 171 ? 31.318 -7.560 26.343 1.00 36.58 ? 166 PRO B O 1 ATOM 1332 C CB . PRO A 1 171 ? 34.004 -6.221 24.973 1.00 44.90 ? 166 PRO B CB 1 ATOM 1333 C CG . PRO A 1 171 ? 34.637 -5.749 23.712 1.00 44.51 ? 166 PRO B CG 1 ATOM 1334 C CD . PRO A 1 171 ? 33.501 -5.128 22.959 1.00 42.33 ? 166 PRO B CD 1 ATOM 1335 N N . VAL A 1 172 ? 31.069 -5.390 25.771 1.00 37.44 ? 167 VAL B N 1 ATOM 1336 C CA . VAL A 1 172 ? 30.088 -5.121 26.814 1.00 37.99 ? 167 VAL B CA 1 ATOM 1337 C C . VAL A 1 172 ? 28.771 -5.794 26.447 1.00 36.84 ? 167 VAL B C 1 ATOM 1338 O O . VAL A 1 172 ? 28.118 -6.396 27.305 1.00 37.71 ? 167 VAL B O 1 ATOM 1339 C CB . VAL A 1 172 ? 29.910 -3.608 27.068 1.00 36.86 ? 167 VAL B CB 1 ATOM 1340 C CG1 . VAL A 1 172 ? 28.719 -3.342 27.992 1.00 38.56 ? 167 VAL B CG1 1 ATOM 1341 C CG2 . VAL A 1 172 ? 31.175 -3.029 27.692 1.00 38.61 ? 167 VAL B CG2 1 ATOM 1342 N N . CYS A 1 173 ? 28.399 -5.703 25.169 1.00 33.86 ? 168 CYS B N 1 ATOM 1343 C CA . CYS A 1 173 ? 27.206 -6.374 24.645 1.00 33.55 ? 168 CYS B CA 1 ATOM 1344 C C . CYS A 1 173 ? 27.337 -7.878 24.890 1.00 34.69 ? 168 CYS B C 1 ATOM 1345 O O . CYS A 1 173 ? 26.414 -8.525 25.398 1.00 31.48 ? 168 CYS B O 1 ATOM 1346 C CB . CYS A 1 173 ? 27.009 -6.080 23.127 1.00 33.02 ? 168 CYS B CB 1 ATOM 1347 S SG . CYS A 1 173 ? 26.702 -4.347 22.627 1.00 36.67 ? 168 CYS B SG 1 ATOM 1348 N N . LYS A 1 174 ? 28.506 -8.431 24.564 1.00 35.95 ? 169 LYS B N 1 ATOM 1349 C CA . LYS A 1 174 ? 28.728 -9.874 24.680 1.00 36.23 ? 169 LYS B CA 1 ATOM 1350 C C . LYS A 1 174 ? 28.611 -10.361 26.110 1.00 39.64 ? 169 LYS B C 1 ATOM 1351 O O . LYS A 1 174 ? 27.933 -11.347 26.381 1.00 38.19 ? 169 LYS B O 1 ATOM 1352 C CB . LYS A 1 174 ? 30.094 -10.264 24.131 1.00 39.46 ? 169 LYS B CB 1 ATOM 1353 C CG . LYS A 1 174 ? 30.439 -11.707 24.400 1.00 44.11 ? 169 LYS B CG 1 ATOM 1354 C CD . LYS A 1 174 ? 31.681 -12.153 23.653 1.00 53.97 ? 169 LYS B CD 1 ATOM 1355 C CE . LYS A 1 174 ? 32.390 -13.251 24.434 1.00 61.46 ? 169 LYS B CE 1 ATOM 1356 N NZ . LYS A 1 174 ? 31.952 -14.606 24.006 1.00 62.78 ? 169 LYS B NZ 1 ATOM 1357 N N . ASP A 1 175 ? 29.267 -9.663 27.024 1.00 38.59 ? 170 ASP B N 1 ATOM 1358 C CA . ASP A 1 175 ? 29.269 -10.059 28.432 1.00 43.46 ? 170 ASP B CA 1 ATOM 1359 C C . ASP A 1 175 ? 27.954 -9.806 29.185 1.00 39.77 ? 170 ASP B C 1 ATOM 1360 O O . ASP A 1 175 ? 27.781 -10.307 30.300 1.00 41.79 ? 170 ASP B O 1 ATOM 1361 C CB . ASP A 1 175 ? 30.448 -9.401 29.153 1.00 48.11 ? 170 ASP B CB 1 ATOM 1362 C CG . ASP A 1 175 ? 31.789 -10.005 28.744 1.00 59.24 ? 170 ASP B CG 1 ATOM 1363 O OD1 . ASP A 1 175 ? 31.803 -11.148 28.223 1.00 61.08 ? 170 ASP B OD1 1 ATOM 1364 O OD2 . ASP A 1 175 ? 32.833 -9.347 28.952 1.00 60.92 ? 170 ASP B OD2 1 ATOM 1365 N N . SER A 1 176 ? 27.026 -9.078 28.575 1.00 34.69 ? 171 SER B N 1 ATOM 1366 C CA . SER A 1 176 ? 25.748 -8.762 29.217 1.00 36.18 ? 171 SER B CA 1 ATOM 1367 C C . SER A 1 176 ? 24.695 -9.866 29.091 1.00 38.17 ? 171 SER B C 1 ATOM 1368 O O . SER A 1 176 ? 23.606 -9.740 29.640 1.00 37.84 ? 171 SER B O 1 ATOM 1369 C CB . SER A 1 176 ? 25.163 -7.497 28.609 1.00 30.70 ? 171 SER B CB 1 ATOM 1370 O OG . SER A 1 176 ? 24.674 -7.745 27.294 1.00 31.13 ? 171 SER B OG 1 ATOM 1371 N N . THR A 1 177 ? 25.009 -10.939 28.371 1.00 36.20 ? 172 THR B N 1 ATOM 1372 C CA . THR A 1 177 ? 24.005 -11.925 28.019 1.00 34.90 ? 172 THR B CA 1 ATOM 1373 C C . THR A 1 177 ? 24.673 -13.257 27.742 1.00 38.72 ? 172 THR B C 1 ATOM 1374 O O . THR A 1 177 ? 25.823 -13.303 27.312 1.00 35.98 ? 172 THR B O 1 ATOM 1375 C CB . THR A 1 177 ? 23.198 -11.480 26.767 1.00 35.09 ? 172 THR B CB 1 ATOM 1376 O OG1 . THR A 1 177 ? 22.174 -12.433 26.469 1.00 33.04 ? 172 THR B OG1 1 ATOM 1377 C CG2 . THR A 1 177 ? 24.114 -11.323 25.532 1.00 36.81 ? 172 THR B CG2 1 ATOM 1378 N N . ARG A 1 178 ? 23.934 -14.337 27.992 1.00 38.68 ? 173 ARG B N 1 ATOM 1379 C CA . ARG A 1 178 ? 24.381 -15.675 27.626 1.00 40.99 ? 173 ARG B CA 1 ATOM 1380 C C . ARG A 1 178 ? 23.890 -16.114 26.237 1.00 40.47 ? 173 ARG B C 1 ATOM 1381 O O . ARG A 1 178 ? 24.171 -17.235 25.809 1.00 46.58 ? 173 ARG B O 1 ATOM 1382 C CB . ARG A 1 178 ? 23.927 -16.682 28.687 1.00 46.77 ? 173 ARG B CB 1 ATOM 1383 C CG . ARG A 1 178 ? 24.479 -16.417 30.087 1.00 49.08 ? 173 ARG B CG 1 ATOM 1384 C CD . ARG A 1 178 ? 23.943 -17.458 31.051 1.00 54.02 ? 173 ARG B CD 1 ATOM 1385 N NE . ARG A 1 178 ? 24.630 -17.510 32.345 1.00 58.61 ? 173 ARG B NE 1 ATOM 1386 C CZ . ARG A 1 178 ? 24.227 -16.902 33.461 1.00 58.35 ? 173 ARG B CZ 1 ATOM 1387 N NH1 . ARG A 1 178 ? 23.140 -16.140 33.478 1.00 53.85 ? 173 ARG B NH1 1 ATOM 1388 N NH2 . ARG A 1 178 ? 24.934 -17.048 34.574 1.00 66.95 ? 173 ARG B NH2 1 ATOM 1389 N N . ILE A 1 179 ? 23.142 -15.259 25.544 1.00 36.10 ? 174 ILE B N 1 ATOM 1390 C CA . ILE A 1 179 ? 22.727 -15.554 24.182 1.00 36.59 ? 174 ILE B CA 1 ATOM 1391 C C . ILE A 1 179 ? 23.890 -15.225 23.239 1.00 38.62 ? 174 ILE B C 1 ATOM 1392 O O . ILE A 1 179 ? 24.603 -14.251 23.449 1.00 36.38 ? 174 ILE B O 1 ATOM 1393 C CB . ILE A 1 179 ? 21.436 -14.787 23.822 1.00 35.77 ? 174 ILE B CB 1 ATOM 1394 C CG1 . ILE A 1 179 ? 20.284 -15.317 24.689 1.00 36.55 ? 174 ILE B CG1 1 ATOM 1395 C CG2 . ILE A 1 179 ? 21.106 -14.928 22.337 1.00 32.36 ? 174 ILE B CG2 1 ATOM 1396 C CD1 . ILE A 1 179 ? 19.108 -14.393 24.804 1.00 36.90 ? 174 ILE B CD1 1 ATOM 1397 N N . ARG A 1 180 ? 24.092 -16.047 22.213 1.00 42.41 ? 175 ARG B N 1 ATOM 1398 C CA . ARG A 1 180 ? 25.239 -15.885 21.328 1.00 44.76 ? 175 ARG B CA 1 ATOM 1399 C C . ARG A 1 180 ? 24.974 -14.735 20.378 1.00 41.33 ? 175 ARG B C 1 ATOM 1400 O O . ARG A 1 180 ? 24.023 -14.768 19.602 1.00 44.16 ? 175 ARG B O 1 ATOM 1401 C CB . ARG A 1 180 ? 25.526 -17.170 20.559 1.00 48.34 ? 175 ARG B CB 1 ATOM 1402 C CG . ARG A 1 180 ? 26.791 -17.112 19.715 1.00 52.83 ? 175 ARG B CG 1 ATOM 1403 C CD . ARG A 1 180 ? 27.055 -18.452 19.052 1.00 61.95 ? 175 ARG B CD 1 ATOM 1404 N NE . ARG A 1 180 ? 26.043 -18.775 18.041 1.00 66.97 ? 175 ARG B NE 1 ATOM 1405 C CZ . ARG A 1 180 ? 26.012 -18.272 16.805 1.00 69.68 ? 175 ARG B CZ 1 ATOM 1406 N NH1 . ARG A 1 180 ? 26.942 -17.411 16.387 1.00 69.38 ? 175 ARG B NH1 1 ATOM 1407 N NH2 . ARG A 1 180 ? 25.042 -18.635 15.973 1.00 71.77 ? 175 ARG B NH2 1 ATOM 1408 N N . ILE A 1 181 ? 25.800 -13.698 20.454 1.00 38.77 ? 176 ILE B N 1 ATOM 1409 C CA . ILE A 1 181 ? 25.642 -12.555 19.562 1.00 38.64 ? 176 ILE B CA 1 ATOM 1410 C C . ILE A 1 181 ? 26.509 -12.763 18.334 1.00 40.66 ? 176 ILE B C 1 ATOM 1411 O O . ILE A 1 181 ? 27.509 -13.500 18.390 1.00 39.57 ? 176 ILE B O 1 ATOM 1412 C CB . ILE A 1 181 ? 25.977 -11.220 20.256 1.00 41.47 ? 176 ILE B CB 1 ATOM 1413 C CG1 . ILE A 1 181 ? 27.487 -11.049 20.444 1.00 45.55 ? 176 ILE B CG1 1 ATOM 1414 C CG2 . ILE A 1 181 ? 25.244 -11.131 21.591 1.00 41.26 ? 176 ILE B CG2 1 ATOM 1415 C CD1 . ILE A 1 181 ? 27.898 -9.634 20.811 1.00 50.03 ? 176 ILE B CD1 1 ATOM 1416 N N . THR A 1 182 ? 26.108 -12.141 17.225 1.00 34.84 ? 177 THR B N 1 ATOM 1417 C CA . THR A 1 182 ? 26.862 -12.233 15.973 1.00 36.86 ? 177 THR B CA 1 ATOM 1418 C C . THR A 1 182 ? 27.221 -10.850 15.455 1.00 35.34 ? 177 THR B C 1 ATOM 1419 O O . THR A 1 182 ? 26.745 -9.835 15.964 1.00 32.53 ? 177 THR B O 1 ATOM 1420 C CB . THR A 1 182 ? 26.041 -12.916 14.867 1.00 36.48 ? 177 THR B CB 1 ATOM 1421 O OG1 . THR A 1 182 ? 24.954 -12.059 14.492 1.00 34.86 ? 177 THR B OG1 1 ATOM 1422 C CG2 . THR A 1 182 ? 25.503 -14.259 15.336 1.00 36.91 ? 177 THR B CG2 1 ATOM 1423 N N . ASP A 1 183 ? 28.032 -10.819 14.401 1.00 37.11 ? 178 ASP B N 1 ATOM 1424 C CA . ASP A 1 183 ? 28.378 -9.568 13.740 1.00 37.45 ? 178 ASP B CA 1 ATOM 1425 C C . ASP A 1 183 ? 27.190 -8.907 13.050 1.00 34.33 ? 178 ASP B C 1 ATOM 1426 O O . ASP A 1 183 ? 27.292 -7.753 12.652 1.00 36.78 ? 178 ASP B O 1 ATOM 1427 C CB . ASP A 1 183 ? 29.497 -9.795 12.712 1.00 41.50 ? 178 ASP B CB 1 ATOM 1428 C CG . ASP A 1 183 ? 30.835 -10.091 13.354 1.00 50.10 ? 178 ASP B CG 1 ATOM 1429 O OD1 . ASP A 1 183 ? 31.077 -9.605 14.479 1.00 58.58 ? 178 ASP B OD1 1 ATOM 1430 O OD2 . ASP A 1 183 ? 31.655 -10.806 12.732 1.00 60.62 ? 178 ASP B OD2 1 ATOM 1431 N N . ASN A 1 184 ? 26.071 -9.620 12.906 1.00 33.52 ? 179 ASN B N 1 ATOM 1432 C CA . ASN A 1 184 ? 24.839 -9.042 12.336 1.00 32.14 ? 179 ASN B CA 1 ATOM 1433 C C . ASN A 1 184 ? 23.952 -8.348 13.342 1.00 30.92 ? 179 ASN B C 1 ATOM 1434 O O . ASN A 1 184 ? 22.817 -7.991 13.041 1.00 30.78 ? 179 ASN B O 1 ATOM 1435 C CB . ASN A 1 184 ? 24.047 -10.136 11.648 1.00 34.58 ? 179 ASN B CB 1 ATOM 1436 C CG . ASN A 1 184 ? 24.881 -10.867 10.630 1.00 36.39 ? 179 ASN B CG 1 ATOM 1437 O OD1 . ASN A 1 184 ? 25.488 -10.234 9.775 1.00 35.54 ? 179 ASN B OD1 1 ATOM 1438 N ND2 . ASN A 1 184 ? 24.960 -12.191 10.744 1.00 37.55 ? 179 ASN B ND2 1 ATOM 1439 N N . MET A 1 185 ? 24.471 -8.134 14.539 1.00 32.72 ? 180 MET B N 1 ATOM 1440 C CA . MET A 1 185 ? 23.709 -7.464 15.579 1.00 31.00 ? 180 MET B CA 1 ATOM 1441 C C . MET A 1 185 ? 24.590 -6.386 16.190 1.00 31.09 ? 180 MET B C 1 ATOM 1442 O O . MET A 1 185 ? 25.809 -6.527 16.214 1.00 31.95 ? 180 MET B O 1 ATOM 1443 C CB . MET A 1 185 ? 23.330 -8.439 16.692 1.00 30.22 ? 180 MET B CB 1 ATOM 1444 C CG . MET A 1 185 ? 22.718 -9.752 16.277 1.00 34.14 ? 180 MET B CG 1 ATOM 1445 S SD . MET A 1 185 ? 22.688 -10.845 17.711 1.00 33.05 ? 180 MET B SD 1 ATOM 1446 C CE . MET A 1 185 ? 22.089 -12.345 16.950 1.00 34.45 ? 180 MET B CE 1 ATOM 1447 N N . PHE A 1 186 ? 23.976 -5.328 16.699 1.00 29.19 ? 181 PHE B N 1 ATOM 1448 C CA . PHE A 1 186 ? 24.637 -4.461 17.654 1.00 30.91 ? 181 PHE B CA 1 ATOM 1449 C C . PHE A 1 186 ? 23.698 -4.222 18.822 1.00 30.02 ? 181 PHE B C 1 ATOM 1450 O O . PHE A 1 186 ? 22.499 -4.499 18.724 1.00 27.20 ? 181 PHE B O 1 ATOM 1451 C CB . PHE A 1 186 ? 25.088 -3.132 17.031 1.00 30.99 ? 181 PHE B CB 1 ATOM 1452 C CG . PHE A 1 186 ? 23.974 -2.260 16.517 1.00 28.38 ? 181 PHE B CG 1 ATOM 1453 C CD1 . PHE A 1 186 ? 23.544 -2.359 15.203 1.00 30.31 ? 181 PHE B CD1 1 ATOM 1454 C CD2 . PHE A 1 186 ? 23.379 -1.312 17.336 1.00 30.56 ? 181 PHE B CD2 1 ATOM 1455 C CE1 . PHE A 1 186 ? 22.526 -1.552 14.721 1.00 27.84 ? 181 PHE B CE1 1 ATOM 1456 C CE2 . PHE A 1 186 ? 22.362 -0.499 16.863 1.00 28.16 ? 181 PHE B CE2 1 ATOM 1457 C CZ . PHE A 1 186 ? 21.942 -0.612 15.544 1.00 27.74 ? 181 PHE B CZ 1 ATOM 1458 N N . CYS A 1 187 ? 24.259 -3.747 19.930 1.00 28.06 ? 182 CYS B N 1 ATOM 1459 C CA . CYS A 1 187 ? 23.449 -3.413 21.091 1.00 29.36 ? 182 CYS B CA 1 ATOM 1460 C C . CYS A 1 187 ? 23.609 -1.946 21.477 1.00 29.73 ? 182 CYS B C 1 ATOM 1461 O O . CYS A 1 187 ? 24.607 -1.297 21.151 1.00 27.86 ? 182 CYS B O 1 ATOM 1462 C CB . CYS A 1 187 ? 23.706 -4.380 22.255 1.00 31.69 ? 182 CYS B CB 1 ATOM 1463 S SG . CYS A 1 187 ? 24.899 -3.910 23.516 1.00 35.35 ? 182 CYS B SG 1 ATOM 1464 N N . ALA A 1 188 ? 22.575 -1.419 22.115 1.00 26.41 ? 183 ALA B N 1 ATOM 1465 C CA . ALA A 1 188 ? 22.515 -0.022 22.465 1.00 27.46 ? 183 ALA B CA 1 ATOM 1466 C C . ALA A 1 188 ? 21.783 0.158 23.796 1.00 27.04 ? 183 ALA B C 1 ATOM 1467 O O . ALA A 1 188 ? 20.941 -0.663 24.183 1.00 24.70 ? 183 ALA B O 1 ATOM 1468 C CB . ALA A 1 188 ? 21.797 0.748 21.375 1.00 28.26 ? 183 ALA B CB 1 ATOM 1469 N N . GLY A 1 189 ? 22.106 1.235 24.494 1.00 29.47 ? 184 GLY B N 1 ATOM 1470 C CA . GLY A 1 189 ? 21.511 1.490 25.796 1.00 27.22 ? 184 GLY B CA 1 ATOM 1471 C C . GLY A 1 189 ? 22.531 2.047 26.746 1.00 28.56 ? 184 GLY B C 1 ATOM 1472 O O . GLY A 1 189 ? 23.738 1.948 26.509 1.00 30.33 ? 184 GLY B O 1 ATOM 1473 N N . TYR A 1 190 A 22.049 2.654 27.820 1.00 27.36 ? 184 TYR B N 1 ATOM 1474 C CA . TYR A 1 190 A 22.953 3.248 28.790 1.00 29.77 ? 184 TYR B CA 1 ATOM 1475 C C . TYR A 1 190 A 23.529 2.187 29.708 1.00 30.72 ? 184 TYR B C 1 ATOM 1476 O O . TYR A 1 190 A 22.885 1.169 29.989 1.00 30.11 ? 184 TYR B O 1 ATOM 1477 C CB . TYR A 1 190 A 22.258 4.346 29.590 1.00 33.10 ? 184 TYR B CB 1 ATOM 1478 C CG . TYR A 1 190 A 21.974 5.592 28.770 1.00 33.61 ? 184 TYR B CG 1 ATOM 1479 C CD1 . TYR A 1 190 A 22.991 6.505 28.483 1.00 35.65 ? 184 TYR B CD1 1 ATOM 1480 C CD2 . TYR A 1 190 A 20.693 5.852 28.270 1.00 33.17 ? 184 TYR B CD2 1 ATOM 1481 C CE1 . TYR A 1 190 A 22.741 7.650 27.751 1.00 36.38 ? 184 TYR B CE1 1 ATOM 1482 C CE2 . TYR A 1 190 A 20.433 6.994 27.528 1.00 32.86 ? 184 TYR B CE2 1 ATOM 1483 C CZ . TYR A 1 190 A 21.465 7.886 27.271 1.00 33.09 ? 184 TYR B CZ 1 ATOM 1484 O OH . TYR A 1 190 A 21.224 9.017 26.546 1.00 36.18 ? 184 TYR B OH 1 ATOM 1485 N N . LYS A 1 191 ? 24.764 2.415 30.136 1.00 31.24 ? 185 LYS B N 1 ATOM 1486 C CA . LYS A 1 191 ? 25.399 1.593 31.150 1.00 34.06 ? 185 LYS B CA 1 ATOM 1487 C C . LYS A 1 191 ? 24.920 2.027 32.527 1.00 34.97 ? 185 LYS B C 1 ATOM 1488 O O . LYS A 1 191 ? 24.527 3.175 32.714 1.00 36.30 ? 185 LYS B O 1 ATOM 1489 C CB . LYS A 1 191 ? 26.919 1.715 31.055 1.00 37.30 ? 185 LYS B CB 1 ATOM 1490 C CG . LYS A 1 191 ? 27.484 1.209 29.735 1.00 38.28 ? 185 LYS B CG 1 ATOM 1491 C CD . LYS A 1 191 ? 28.954 1.543 29.597 1.00 45.87 ? 185 LYS B CD 1 ATOM 1492 C CE . LYS A 1 191 ? 29.490 1.180 28.221 1.00 47.13 ? 185 LYS B CE 1 ATOM 1493 N NZ . LYS A 1 191 ? 30.940 1.533 28.088 1.00 51.94 ? 185 LYS B NZ 1 ATOM 1494 N N . PRO A 1 192 ? 24.948 1.109 33.503 1.00 37.88 ? 186 PRO B N 1 ATOM 1495 C CA . PRO A 1 192 ? 24.576 1.437 34.890 1.00 42.01 ? 186 PRO B CA 1 ATOM 1496 C C . PRO A 1 192 ? 25.234 2.717 35.430 1.00 43.08 ? 186 PRO B C 1 ATOM 1497 O O . PRO A 1 192 ? 24.603 3.480 36.164 1.00 48.30 ? 186 PRO B O 1 ATOM 1498 C CB . PRO A 1 192 ? 25.078 0.225 35.675 1.00 43.17 ? 186 PRO B CB 1 ATOM 1499 C CG . PRO A 1 192 ? 25.023 -0.894 34.696 1.00 41.63 ? 186 PRO B CG 1 ATOM 1500 C CD . PRO A 1 192 ? 25.382 -0.290 33.368 1.00 37.90 ? 186 PRO B CD 1 ATOM 1501 N N . ASP A 1 193 A 26.488 2.949 35.063 1.00 45.54 ? 186 ASP B N 1 ATOM 1502 C CA . ASP A 1 193 A 27.209 4.128 35.545 1.00 48.19 ? 186 ASP B CA 1 ATOM 1503 C C . ASP A 1 193 A 26.822 5.440 34.861 1.00 46.14 ? 186 ASP B C 1 ATOM 1504 O O . ASP A 1 193 A 27.207 6.503 35.327 1.00 48.46 ? 186 ASP B O 1 ATOM 1505 C CB . ASP A 1 193 A 28.730 3.910 35.509 1.00 49.55 ? 186 ASP B CB 1 ATOM 1506 C CG . ASP A 1 193 A 29.306 3.781 34.104 1.00 53.02 ? 186 ASP B CG 1 ATOM 1507 O OD1 . ASP A 1 193 A 28.569 3.767 33.095 1.00 49.33 ? 186 ASP B OD1 1 ATOM 1508 O OD2 . ASP A 1 193 A 30.546 3.663 34.025 1.00 61.14 ? 186 ASP B OD2 1 ATOM 1509 N N . GLU A 1 194 B 26.033 5.374 33.795 1.00 45.52 ? 186 GLU B N 1 ATOM 1510 C CA . GLU A 1 194 B 25.618 6.574 33.078 1.00 43.95 ? 186 GLU B CA 1 ATOM 1511 C C . GLU A 1 194 B 24.332 7.222 33.600 1.00 45.10 ? 186 GLU B C 1 ATOM 1512 O O . GLU A 1 194 B 24.030 8.351 33.231 1.00 46.11 ? 186 GLU B O 1 ATOM 1513 C CB . GLU A 1 194 B 25.521 6.273 31.585 1.00 44.43 ? 186 GLU B CB 1 ATOM 1514 C CG . GLU A 1 194 B 26.876 5.903 30.998 1.00 45.02 ? 186 GLU B CG 1 ATOM 1515 C CD . GLU A 1 194 B 26.808 5.514 29.537 1.00 45.95 ? 186 GLU B CD 1 ATOM 1516 O OE1 . GLU A 1 194 B 26.029 4.611 29.207 1.00 35.49 ? 186 GLU B OE1 1 ATOM 1517 O OE2 . GLU A 1 194 B 27.549 6.095 28.719 1.00 54.65 ? 186 GLU B OE2 1 ATOM 1518 N N . GLY A 1 195 C 23.585 6.543 34.469 1.00 46.40 ? 186 GLY B N 1 ATOM 1519 C CA . GLY A 1 195 C 22.435 7.172 35.138 1.00 51.46 ? 186 GLY B CA 1 ATOM 1520 C C . GLY A 1 195 C 21.146 7.223 34.320 1.00 54.11 ? 186 GLY B C 1 ATOM 1521 O O . GLY A 1 195 C 20.080 6.808 34.792 1.00 57.88 ? 186 GLY B O 1 ATOM 1522 N N . LYS A 1 196 D 21.238 7.729 33.094 1.00 49.78 ? 186 LYS B N 1 ATOM 1523 C CA . LYS A 1 196 D 20.100 7.767 32.177 1.00 41.51 ? 186 LYS B CA 1 ATOM 1524 C C . LYS A 1 196 D 19.579 6.366 31.838 1.00 39.49 ? 186 LYS B C 1 ATOM 1525 O O . LYS A 1 196 D 20.277 5.366 32.009 1.00 33.91 ? 186 LYS B O 1 ATOM 1526 C CB . LYS A 1 196 D 20.484 8.497 30.895 1.00 43.36 ? 186 LYS B CB 1 ATOM 1527 C CG . LYS A 1 196 D 20.801 9.986 31.076 1.00 48.39 ? 186 LYS B CG 1 ATOM 1528 C CD . LYS A 1 196 D 20.732 10.684 29.723 1.00 51.08 ? 186 LYS B CD 1 ATOM 1529 C CE . LYS A 1 196 D 20.840 12.194 29.821 1.00 60.00 ? 186 LYS B CE 1 ATOM 1530 N NZ . LYS A 1 196 D 20.448 12.807 28.515 1.00 64.94 ? 186 LYS B NZ 1 ATOM 1531 N N . ARG A 1 197 ? 18.341 6.319 31.338 1.00 36.89 ? 187 ARG B N 1 ATOM 1532 C CA . ARG A 1 197 ? 17.641 5.073 31.060 1.00 32.67 ? 187 ARG B CA 1 ATOM 1533 C C . ARG A 1 197 ? 16.997 5.090 29.677 1.00 30.23 ? 187 ARG B C 1 ATOM 1534 O O . ARG A 1 197 ? 17.012 6.095 28.971 1.00 29.98 ? 187 ARG B O 1 ATOM 1535 C CB . ARG A 1 197 ? 16.541 4.854 32.093 1.00 32.81 ? 187 ARG B CB 1 ATOM 1536 C CG . ARG A 1 197 ? 16.987 5.027 33.535 1.00 34.63 ? 187 ARG B CG 1 ATOM 1537 C CD . ARG A 1 197 ? 16.115 4.215 34.468 1.00 36.59 ? 187 ARG B CD 1 ATOM 1538 N NE . ARG A 1 197 ? 16.341 2.788 34.244 1.00 36.29 ? 187 ARG B NE 1 ATOM 1539 C CZ . ARG A 1 197 ? 17.235 2.044 34.888 1.00 38.27 ? 187 ARG B CZ 1 ATOM 1540 N NH1 . ARG A 1 197 ? 17.992 2.556 35.856 1.00 39.64 ? 187 ARG B NH1 1 ATOM 1541 N NH2 . ARG A 1 197 ? 17.350 0.758 34.580 1.00 38.58 ? 187 ARG B NH2 1 ATOM 1542 N N . GLY A 1 198 ? 16.390 3.972 29.307 1.00 27.98 ? 188 GLY B N 1 ATOM 1543 C CA . GLY A 1 198 ? 15.650 3.896 28.057 1.00 27.38 ? 188 GLY B CA 1 ATOM 1544 C C . GLY A 1 198 ? 15.956 2.586 27.377 1.00 28.87 ? 188 GLY B C 1 ATOM 1545 O O . GLY A 1 198 ? 17.053 2.063 27.489 1.00 28.50 ? 188 GLY B O 1 ATOM 1546 N N . ASP A 1 199 ? 14.975 2.071 26.649 1.00 29.91 ? 189 ASP B N 1 ATOM 1547 C CA . ASP A 1 199 ? 15.115 0.821 25.929 1.00 29.52 ? 189 ASP B CA 1 ATOM 1548 C C . ASP A 1 199 ? 13.909 0.654 25.033 1.00 30.58 ? 189 ASP B C 1 ATOM 1549 O O . ASP A 1 199 ? 12.880 1.318 25.225 1.00 28.23 ? 189 ASP B O 1 ATOM 1550 C CB . ASP A 1 199 ? 15.202 -0.350 26.906 1.00 30.44 ? 189 ASP B CB 1 ATOM 1551 C CG . ASP A 1 199 ? 15.774 -1.624 26.274 1.00 29.15 ? 189 ASP B CG 1 ATOM 1552 O OD1 . ASP A 1 199 ? 16.136 -1.633 25.072 1.00 25.08 ? 189 ASP B OD1 1 ATOM 1553 O OD2 . ASP A 1 199 ? 15.839 -2.623 27.018 1.00 27.79 ? 189 ASP B OD2 1 ATOM 1554 N N . ALA A 1 200 ? 14.058 -0.192 24.021 1.00 32.12 ? 190 ALA B N 1 ATOM 1555 C CA . ALA A 1 200 ? 12.920 -0.726 23.307 1.00 28.69 ? 190 ALA B CA 1 ATOM 1556 C C . ALA A 1 200 ? 12.332 -1.885 24.127 1.00 28.76 ? 190 ALA B C 1 ATOM 1557 O O . ALA A 1 200 ? 12.858 -2.275 25.186 1.00 27.12 ? 190 ALA B O 1 ATOM 1558 C CB . ALA A 1 200 ? 13.317 -1.172 21.917 1.00 29.91 ? 190 ALA B CB 1 ATOM 1559 N N . CYS A 1 201 ? 11.212 -2.410 23.670 1.00 26.46 ? 191 CYS B N 1 ATOM 1560 C CA . CYS A 1 201 ? 10.528 -3.454 24.417 1.00 29.92 ? 191 CYS B CA 1 ATOM 1561 C C . CYS A 1 201 ? 9.658 -4.283 23.466 1.00 30.54 ? 191 CYS B C 1 ATOM 1562 O O . CYS A 1 201 ? 9.665 -4.075 22.227 1.00 31.18 ? 191 CYS B O 1 ATOM 1563 C CB . CYS A 1 201 ? 9.710 -2.801 25.546 1.00 34.34 ? 191 CYS B CB 1 ATOM 1564 S SG . CYS A 1 201 ? 9.264 -3.867 26.943 1.00 41.12 ? 191 CYS B SG 1 ATOM 1565 N N . GLU A 1 202 ? 8.905 -5.216 24.037 1.00 34.11 ? 192 GLU B N 1 ATOM 1566 C CA . GLU A 1 202 ? 8.027 -6.068 23.243 1.00 36.73 ? 192 GLU B CA 1 ATOM 1567 C C . GLU A 1 202 ? 6.969 -5.198 22.584 1.00 32.20 ? 192 GLU B C 1 ATOM 1568 O O . GLU A 1 202 ? 6.418 -4.301 23.220 1.00 31.30 ? 192 GLU B O 1 ATOM 1569 C CB . GLU A 1 202 ? 7.382 -7.179 24.097 1.00 43.60 ? 192 GLU B CB 1 ATOM 1570 C CG . GLU A 1 202 ? 7.282 -8.518 23.359 1.00 57.09 ? 192 GLU B CG 1 ATOM 1571 C CD . GLU A 1 202 ? 6.098 -9.370 23.792 1.00 64.70 ? 192 GLU B CD 1 ATOM 1572 O OE1 . GLU A 1 202 ? 5.868 -9.520 25.014 1.00 67.79 ? 192 GLU B OE1 1 ATOM 1573 O OE2 . GLU A 1 202 ? 5.392 -9.898 22.901 1.00 64.22 ? 192 GLU B OE2 1 ATOM 1574 N N . GLY A 1 203 ? 6.699 -5.460 21.307 1.00 29.01 ? 193 GLY B N 1 ATOM 1575 C CA . GLY A 1 203 ? 5.864 -4.577 20.489 1.00 32.59 ? 193 GLY B CA 1 ATOM 1576 C C . GLY A 1 203 ? 6.655 -3.586 19.641 1.00 29.83 ? 193 GLY B C 1 ATOM 1577 O O . GLY A 1 203 ? 6.148 -3.103 18.649 1.00 29.43 ? 193 GLY B O 1 ATOM 1578 N N . ASP A 1 204 ? 7.899 -3.296 20.014 1.00 24.46 ? 194 ASP B N 1 ATOM 1579 C CA . ASP A 1 204 ? 8.735 -2.387 19.236 1.00 26.79 ? 194 ASP B CA 1 ATOM 1580 C C . ASP A 1 204 ? 9.538 -3.088 18.143 1.00 26.13 ? 194 ASP B C 1 ATOM 1581 O O . ASP A 1 204 ? 10.144 -2.418 17.329 1.00 25.77 ? 194 ASP B O 1 ATOM 1582 C CB . ASP A 1 204 ? 9.711 -1.615 20.137 1.00 24.83 ? 194 ASP B CB 1 ATOM 1583 C CG . ASP A 1 204 ? 9.006 -0.715 21.132 1.00 26.01 ? 194 ASP B CG 1 ATOM 1584 O OD1 . ASP A 1 204 ? 8.034 -0.033 20.750 1.00 26.23 ? 194 ASP B OD1 1 ATOM 1585 O OD2 . ASP A 1 204 ? 9.452 -0.667 22.308 1.00 25.06 ? 194 ASP B OD2 1 ATOM 1586 N N . THR A 1 205 ? 9.539 -4.420 18.126 1.00 26.45 ? 195 THR B N 1 ATOM 1587 C CA . THR A 1 205 ? 10.307 -5.186 17.141 1.00 25.06 ? 195 THR B CA 1 ATOM 1588 C C . THR A 1 205 ? 9.984 -4.690 15.765 1.00 27.26 ? 195 THR B C 1 ATOM 1589 O O . THR A 1 205 ? 8.827 -4.370 15.501 1.00 23.40 ? 195 THR B O 1 ATOM 1590 C CB . THR A 1 205 ? 9.907 -6.671 17.206 1.00 29.10 ? 195 THR B CB 1 ATOM 1591 O OG1 . THR A 1 205 ? 10.556 -7.280 18.328 1.00 27.33 ? 195 THR B OG1 1 ATOM 1592 C CG2 . THR A 1 205 ? 10.285 -7.420 15.914 1.00 28.44 ? 195 THR B CG2 1 ATOM 1593 N N . GLY A 1 206 ? 10.991 -4.620 14.888 1.00 24.98 ? 196 GLY B N 1 ATOM 1594 C CA . GLY A 1 206 ? 10.772 -4.168 13.524 1.00 26.14 ? 196 GLY B CA 1 ATOM 1595 C C . GLY A 1 206 ? 10.924 -2.673 13.318 1.00 28.28 ? 196 GLY B C 1 ATOM 1596 O O . GLY A 1 206 ? 11.193 -2.228 12.206 1.00 29.14 ? 196 GLY B O 1 ATOM 1597 N N . GLY A 1 207 ? 10.757 -1.903 14.386 1.00 29.45 ? 197 GLY B N 1 ATOM 1598 C CA . GLY A 1 207 ? 10.922 -0.463 14.346 1.00 29.64 ? 197 GLY B CA 1 ATOM 1599 C C . GLY A 1 207 ? 12.377 -0.086 14.147 1.00 32.22 ? 197 GLY B C 1 ATOM 1600 O O . GLY A 1 207 ? 13.266 -0.861 14.483 1.00 28.74 ? 197 GLY B O 1 ATOM 1601 N N . PRO A 1 208 ? 12.624 1.115 13.602 1.00 28.73 ? 198 PRO B N 1 ATOM 1602 C CA . PRO A 1 208 ? 13.959 1.496 13.175 1.00 28.19 ? 198 PRO B CA 1 ATOM 1603 C C . PRO A 1 208 ? 14.811 2.132 14.279 1.00 28.36 ? 198 PRO B C 1 ATOM 1604 O O . PRO A 1 208 ? 14.285 2.852 15.122 1.00 25.73 ? 198 PRO B O 1 ATOM 1605 C CB . PRO A 1 208 ? 13.667 2.504 12.070 1.00 27.28 ? 198 PRO B CB 1 ATOM 1606 C CG . PRO A 1 208 ? 12.435 3.199 12.544 1.00 29.23 ? 198 PRO B CG 1 ATOM 1607 C CD . PRO A 1 208 ? 11.614 2.115 13.193 1.00 26.14 ? 198 PRO B CD 1 ATOM 1608 N N . PHE A 1 209 ? 16.115 1.843 14.248 1.00 26.06 ? 199 PHE B N 1 ATOM 1609 C CA . PHE A 1 209 ? 17.115 2.556 15.027 1.00 27.10 ? 199 PHE B CA 1 ATOM 1610 C C . PHE A 1 209 ? 17.812 3.470 14.024 1.00 23.40 ? 199 PHE B C 1 ATOM 1611 O O . PHE A 1 209 ? 18.547 3.002 13.135 1.00 24.97 ? 199 PHE B O 1 ATOM 1612 C CB . PHE A 1 209 ? 18.094 1.578 15.682 1.00 24.12 ? 199 PHE B CB 1 ATOM 1613 C CG . PHE A 1 209 ? 19.201 2.236 16.490 1.00 27.05 ? 199 PHE B CG 1 ATOM 1614 C CD1 . PHE A 1 209 ? 20.306 2.809 15.866 1.00 27.20 ? 199 PHE B CD1 1 ATOM 1615 C CD2 . PHE A 1 209 ? 19.163 2.219 17.884 1.00 26.44 ? 199 PHE B CD2 1 ATOM 1616 C CE1 . PHE A 1 209 ? 21.317 3.395 16.603 1.00 31.36 ? 199 PHE B CE1 1 ATOM 1617 C CE2 . PHE A 1 209 ? 20.169 2.809 18.630 1.00 29.27 ? 199 PHE B CE2 1 ATOM 1618 C CZ . PHE A 1 209 ? 21.256 3.389 17.987 1.00 29.68 ? 199 PHE B CZ 1 ATOM 1619 N N . VAL A 1 210 ? 17.556 4.769 14.157 1.00 21.71 ? 200 VAL B N 1 ATOM 1620 C CA . VAL A 1 210 ? 18.047 5.761 13.219 1.00 25.35 ? 200 VAL B CA 1 ATOM 1621 C C . VAL A 1 210 ? 19.069 6.687 13.844 1.00 24.19 ? 200 VAL B C 1 ATOM 1622 O O . VAL A 1 210 ? 19.119 6.879 15.066 1.00 29.24 ? 200 VAL B O 1 ATOM 1623 C CB . VAL A 1 210 ? 16.889 6.567 12.597 1.00 26.75 ? 200 VAL B CB 1 ATOM 1624 C CG1 . VAL A 1 210 ? 15.864 5.597 12.010 1.00 25.31 ? 200 VAL B CG1 1 ATOM 1625 C CG2 . VAL A 1 210 ? 16.213 7.474 13.622 1.00 29.05 ? 200 VAL B CG2 1 ATOM 1626 N N . MET A 1 211 ? 19.920 7.214 12.990 1.00 26.17 ? 201 MET B N 1 ATOM 1627 C CA . MET A 1 211 ? 20.938 8.172 13.371 1.00 27.89 ? 201 MET B CA 1 ATOM 1628 C C . MET A 1 211 ? 20.939 9.285 12.340 1.00 28.89 ? 201 MET B C 1 ATOM 1629 O O . MET A 1 211 ? 20.639 9.054 11.156 1.00 28.45 ? 201 MET B O 1 ATOM 1630 C CB . MET A 1 211 ? 22.321 7.511 13.412 1.00 29.04 ? 201 MET B CB 1 ATOM 1631 C CG . MET A 1 211 ? 22.422 6.334 14.360 1.00 29.00 ? 201 MET B CG 1 ATOM 1632 S SD . MET A 1 211 ? 24.087 5.645 14.557 1.00 29.07 ? 201 MET B SD 1 ATOM 1633 C CE . MET A 1 211 ? 24.903 7.036 15.326 1.00 32.00 ? 201 MET B CE 1 ATOM 1634 N N . LYS A 1 212 ? 21.260 10.494 12.786 1.00 27.45 ? 202 LYS B N 1 ATOM 1635 C CA . LYS A 1 212 ? 21.302 11.650 11.895 1.00 27.46 ? 202 LYS B CA 1 ATOM 1636 C C . LYS A 1 212 ? 22.727 11.952 11.526 1.00 28.99 ? 202 LYS B C 1 ATOM 1637 O O . LYS A 1 212 ? 23.555 12.165 12.419 1.00 29.07 ? 202 LYS B O 1 ATOM 1638 C CB . LYS A 1 212 ? 20.701 12.871 12.578 1.00 30.15 ? 202 LYS B CB 1 ATOM 1639 C CG . LYS A 1 212 ? 20.875 14.162 11.782 1.00 36.61 ? 202 LYS B CG 1 ATOM 1640 C CD . LYS A 1 212 ? 19.931 15.253 12.268 1.00 37.61 ? 202 LYS B CD 1 ATOM 1641 C CE . LYS A 1 212 ? 19.206 15.860 11.088 1.00 41.04 ? 202 LYS B CE 1 ATOM 1642 N NZ . LYS A 1 212 ? 18.597 17.170 11.411 1.00 43.04 ? 202 LYS B NZ 1 ATOM 1643 N N . SER A 1 213 ? 23.015 11.995 10.232 1.00 27.50 ? 203 SER B N 1 ATOM 1644 C CA . SER A 1 213 ? 24.360 12.311 9.771 1.00 29.63 ? 203 SER B CA 1 ATOM 1645 C C . SER A 1 213 ? 24.624 13.810 9.918 1.00 31.70 ? 203 SER B C 1 ATOM 1646 O O . SER A 1 213 ? 23.863 14.631 9.405 1.00 35.59 ? 203 SER B O 1 ATOM 1647 C CB . SER A 1 213 ? 24.574 11.877 8.311 1.00 33.89 ? 203 SER B CB 1 ATOM 1648 O OG . SER A 1 213 ? 25.782 12.417 7.769 1.00 35.59 ? 203 SER B OG 1 ATOM 1649 N N . PRO A 1 214 ? 25.713 14.171 10.619 1.00 33.48 ? 204 PRO B N 1 ATOM 1650 C CA . PRO A 1 214 ? 26.160 15.559 10.676 1.00 36.75 ? 204 PRO B CA 1 ATOM 1651 C C . PRO A 1 214 ? 26.813 16.024 9.376 1.00 38.24 ? 204 PRO B C 1 ATOM 1652 O O . PRO A 1 214 ? 27.142 17.198 9.251 1.00 43.60 ? 204 PRO B O 1 ATOM 1653 C CB . PRO A 1 214 ? 27.180 15.539 11.816 1.00 36.45 ? 204 PRO B CB 1 ATOM 1654 C CG . PRO A 1 214 ? 27.774 14.175 11.745 1.00 38.58 ? 204 PRO B CG 1 ATOM 1655 C CD . PRO A 1 214 ? 26.671 13.262 11.283 1.00 36.36 ? 204 PRO B CD 1 ATOM 1656 N N . PHE A 1 215 A 27.009 15.121 8.417 1.00 41.02 ? 204 PHE B N 1 ATOM 1657 C CA . PHE A 1 215 A 27.653 15.476 7.147 1.00 42.93 ? 204 PHE B CA 1 ATOM 1658 C C . PHE A 1 215 A 26.652 15.988 6.120 1.00 38.87 ? 204 PHE B C 1 ATOM 1659 O O . PHE A 1 215 A 26.951 16.917 5.388 1.00 41.11 ? 204 PHE B O 1 ATOM 1660 C CB . PHE A 1 215 A 28.442 14.283 6.607 1.00 48.03 ? 204 PHE B CB 1 ATOM 1661 C CG . PHE A 1 215 A 29.424 13.727 7.603 1.00 54.71 ? 204 PHE B CG 1 ATOM 1662 C CD1 . PHE A 1 215 A 30.594 14.416 7.899 1.00 64.24 ? 204 PHE B CD1 1 ATOM 1663 C CD2 . PHE A 1 215 A 29.158 12.546 8.282 1.00 57.88 ? 204 PHE B CD2 1 ATOM 1664 C CE1 . PHE A 1 215 A 31.490 13.924 8.834 1.00 68.78 ? 204 PHE B CE1 1 ATOM 1665 C CE2 . PHE A 1 215 A 30.047 12.049 9.221 1.00 60.13 ? 204 PHE B CE2 1 ATOM 1666 C CZ . PHE A 1 215 A 31.216 12.738 9.497 1.00 66.73 ? 204 PHE B CZ 1 ATOM 1667 N N . ASN A 1 216 B 25.453 15.414 6.093 1.00 36.96 ? 204 ASN B N 1 ATOM 1668 C CA . ASN A 1 216 B 24.405 15.881 5.187 1.00 35.25 ? 204 ASN B CA 1 ATOM 1669 C C . ASN A 1 216 B 23.028 16.112 5.827 1.00 31.64 ? 204 ASN B C 1 ATOM 1670 O O . ASN A 1 216 B 22.070 16.356 5.116 1.00 29.50 ? 204 ASN B O 1 ATOM 1671 C CB . ASN A 1 216 B 24.266 14.899 4.017 1.00 36.54 ? 204 ASN B CB 1 ATOM 1672 C CG . ASN A 1 216 B 23.837 13.506 4.464 1.00 35.98 ? 204 ASN B CG 1 ATOM 1673 O OD1 . ASN A 1 216 B 23.249 13.318 5.543 1.00 33.18 ? 204 ASN B OD1 1 ATOM 1674 N ND2 . ASN A 1 216 B 24.126 12.515 3.624 1.00 38.02 ? 204 ASN B ND2 1 ATOM 1675 N N . ASN A 1 217 ? 22.921 16.010 7.150 1.00 32.35 ? 205 ASN B N 1 ATOM 1676 C CA . ASN A 1 217 ? 21.668 16.293 7.862 1.00 33.24 ? 205 ASN B CA 1 ATOM 1677 C C . ASN A 1 217 ? 20.511 15.311 7.585 1.00 33.33 ? 205 ASN B C 1 ATOM 1678 O O . ASN A 1 217 ? 19.362 15.619 7.881 1.00 35.46 ? 205 ASN B O 1 ATOM 1679 C CB . ASN A 1 217 ? 21.212 17.730 7.560 1.00 36.92 ? 205 ASN B CB 1 ATOM 1680 C CG . ASN A 1 217 ? 20.436 18.366 8.708 1.00 43.05 ? 205 ASN B CG 1 ATOM 1681 O OD1 . ASN A 1 217 ? 20.762 18.180 9.877 1.00 48.71 ? 205 ASN B OD1 1 ATOM 1682 N ND2 . ASN A 1 217 ? 19.423 19.156 8.366 1.00 43.19 ? 205 ASN B ND2 1 ATOM 1683 N N . ARG A 1 218 ? 20.815 14.130 7.049 1.00 31.42 ? 206 ARG B N 1 ATOM 1684 C CA . ARG A 1 218 ? 19.802 13.123 6.756 1.00 31.80 ? 206 ARG B CA 1 ATOM 1685 C C . ARG A 1 218 ? 19.784 12.047 7.818 1.00 30.58 ? 206 ARG B C 1 ATOM 1686 O O . ARG A 1 218 ? 20.823 11.729 8.408 1.00 29.49 ? 206 ARG B O 1 ATOM 1687 C CB . ARG A 1 218 ? 20.062 12.447 5.408 1.00 33.16 ? 206 ARG B CB 1 ATOM 1688 C CG . ARG A 1 218 ? 19.732 13.312 4.203 1.00 34.87 ? 206 ARG B CG 1 ATOM 1689 C CD . ARG A 1 218 ? 20.320 12.698 2.945 1.00 37.07 ? 206 ARG B CD 1 ATOM 1690 N NE . ARG A 1 218 ? 20.259 13.574 1.773 1.00 38.72 ? 206 ARG B NE 1 ATOM 1691 C CZ . ARG A 1 218 ? 19.331 13.530 0.814 1.00 42.30 ? 206 ARG B CZ 1 ATOM 1692 N NH1 . ARG A 1 218 ? 18.313 12.672 0.872 1.00 39.39 ? 206 ARG B NH1 1 ATOM 1693 N NH2 . ARG A 1 218 ? 19.419 14.369 -0.217 1.00 46.33 ? 206 ARG B NH2 1 ATOM 1694 N N . TRP A 1 219 ? 18.598 11.477 8.028 1.00 26.73 ? 207 TRP B N 1 ATOM 1695 C CA . TRP A 1 219 ? 18.412 10.359 8.933 1.00 25.67 ? 207 TRP B CA 1 ATOM 1696 C C . TRP A 1 219 ? 18.645 9.053 8.202 1.00 26.47 ? 207 TRP B C 1 ATOM 1697 O O . TRP A 1 219 ? 18.134 8.851 7.098 1.00 27.57 ? 207 TRP B O 1 ATOM 1698 C CB . TRP A 1 219 ? 16.997 10.349 9.532 1.00 25.76 ? 207 TRP B CB 1 ATOM 1699 C CG . TRP A 1 219 ? 16.742 11.490 10.391 1.00 24.08 ? 207 TRP B CG 1 ATOM 1700 C CD1 . TRP A 1 219 ? 16.327 12.724 10.008 1.00 25.73 ? 207 TRP B CD1 1 ATOM 1701 C CD2 . TRP A 1 219 ? 16.913 11.544 11.809 1.00 25.81 ? 207 TRP B CD2 1 ATOM 1702 N NE1 . TRP A 1 219 ? 16.235 13.550 11.093 1.00 24.52 ? 207 TRP B NE1 1 ATOM 1703 C CE2 . TRP A 1 219 ? 16.584 12.849 12.216 1.00 24.02 ? 207 TRP B CE2 1 ATOM 1704 C CE3 . TRP A 1 219 ? 17.344 10.633 12.762 1.00 23.69 ? 207 TRP B CE3 1 ATOM 1705 C CZ2 . TRP A 1 219 ? 16.648 13.255 13.545 1.00 25.12 ? 207 TRP B CZ2 1 ATOM 1706 C CZ3 . TRP A 1 219 ? 17.395 11.033 14.093 1.00 25.40 ? 207 TRP B CZ3 1 ATOM 1707 C CH2 . TRP A 1 219 ? 17.039 12.327 14.468 1.00 26.80 ? 207 TRP B CH2 1 ATOM 1708 N N . TYR A 1 220 ? 19.414 8.177 8.835 1.00 24.87 ? 208 TYR B N 1 ATOM 1709 C CA . TYR A 1 220 ? 19.756 6.868 8.293 1.00 25.79 ? 208 TYR B CA 1 ATOM 1710 C C . TYR A 1 220 ? 19.339 5.773 9.233 1.00 26.09 ? 208 TYR B C 1 ATOM 1711 O O . TYR A 1 220 ? 19.584 5.851 10.453 1.00 27.05 ? 208 TYR B O 1 ATOM 1712 C CB . TYR A 1 220 ? 21.274 6.749 8.109 1.00 26.44 ? 208 TYR B CB 1 ATOM 1713 C CG . TYR A 1 220 ? 21.826 7.527 6.975 1.00 25.98 ? 208 TYR B CG 1 ATOM 1714 C CD1 . TYR A 1 220 ? 22.220 8.869 7.133 1.00 26.67 ? 208 TYR B CD1 1 ATOM 1715 C CD2 . TYR A 1 220 ? 22.012 6.925 5.739 1.00 29.84 ? 208 TYR B CD2 1 ATOM 1716 C CE1 . TYR A 1 220 ? 22.745 9.575 6.075 1.00 29.78 ? 208 TYR B CE1 1 ATOM 1717 C CE2 . TYR A 1 220 ? 22.546 7.614 4.682 1.00 30.52 ? 208 TYR B CE2 1 ATOM 1718 C CZ . TYR A 1 220 ? 22.909 8.943 4.849 1.00 34.09 ? 208 TYR B CZ 1 ATOM 1719 O OH . TYR A 1 220 ? 23.447 9.620 3.793 1.00 34.93 ? 208 TYR B OH 1 ATOM 1720 N N . GLN A 1 221 ? 18.759 4.714 8.682 1.00 28.73 ? 209 GLN B N 1 ATOM 1721 C CA . GLN A 1 221 ? 18.422 3.557 9.508 1.00 28.30 ? 209 GLN B CA 1 ATOM 1722 C C . GLN A 1 221 ? 19.583 2.598 9.651 1.00 27.59 ? 209 GLN B C 1 ATOM 1723 O O . GLN A 1 221 ? 19.927 1.894 8.713 1.00 29.52 ? 209 GLN B O 1 ATOM 1724 C CB . GLN A 1 221 ? 17.221 2.804 8.992 1.00 28.81 ? 209 GLN B CB 1 ATOM 1725 C CG . GLN A 1 221 ? 16.814 1.689 9.969 1.00 30.78 ? 209 GLN B CG 1 ATOM 1726 C CD . GLN A 1 221 ? 15.562 0.966 9.542 1.00 30.81 ? 209 GLN B CD 1 ATOM 1727 O OE1 . GLN A 1 221 ? 14.913 1.352 8.566 1.00 30.11 ? 209 GLN B OE1 1 ATOM 1728 N NE2 . GLN A 1 221 ? 15.222 -0.108 10.257 1.00 32.50 ? 209 GLN B NE2 1 ATOM 1729 N N . MET A 1 222 ? 20.147 2.539 10.854 1.00 26.39 ? 210 MET B N 1 ATOM 1730 C CA . MET A 1 222 ? 21.275 1.688 11.125 1.00 26.48 ? 210 MET B CA 1 ATOM 1731 C C . MET A 1 222 ? 20.853 0.326 11.672 1.00 26.48 ? 210 MET B C 1 ATOM 1732 O O . MET A 1 222 ? 21.563 -0.655 11.485 1.00 26.21 ? 210 MET B O 1 ATOM 1733 C CB . MET A 1 222 ? 22.199 2.357 12.131 1.00 29.09 ? 210 MET B CB 1 ATOM 1734 C CG . MET A 1 222 ? 22.652 3.752 11.768 1.00 32.20 ? 210 MET B CG 1 ATOM 1735 S SD . MET A 1 222 ? 23.272 3.974 10.090 1.00 35.39 ? 210 MET B SD 1 ATOM 1736 C CE . MET A 1 222 ? 24.656 2.859 10.009 1.00 38.09 ? 210 MET B CE 1 ATOM 1737 N N . GLY A 1 223 ? 19.729 0.272 12.384 1.00 22.91 ? 211 GLY B N 1 ATOM 1738 C CA . GLY A 1 223 ? 19.284 -0.968 12.973 1.00 24.18 ? 211 GLY B CA 1 ATOM 1739 C C . GLY A 1 223 ? 17.793 -1.212 12.981 1.00 24.01 ? 211 GLY B C 1 ATOM 1740 O O . GLY A 1 223 ? 16.996 -0.338 12.646 1.00 25.68 ? 211 GLY B O 1 ATOM 1741 N N . ILE A 1 224 ? 17.428 -2.436 13.341 1.00 23.41 ? 212 ILE B N 1 ATOM 1742 C CA . ILE A 1 224 ? 16.031 -2.832 13.475 1.00 24.72 ? 212 ILE B CA 1 ATOM 1743 C C . ILE A 1 224 ? 15.846 -3.418 14.867 1.00 23.70 ? 212 ILE B C 1 ATOM 1744 O O . ILE A 1 224 ? 16.594 -4.289 15.257 1.00 25.19 ? 212 ILE B O 1 ATOM 1745 C CB . ILE A 1 224 ? 15.650 -3.916 12.446 1.00 26.21 ? 212 ILE B CB 1 ATOM 1746 C CG1 . ILE A 1 224 ? 15.970 -3.450 11.022 1.00 26.61 ? 212 ILE B CG1 1 ATOM 1747 C CG2 . ILE A 1 224 ? 14.179 -4.321 12.617 1.00 27.15 ? 212 ILE B CG2 1 ATOM 1748 C CD1 . ILE A 1 224 ? 16.036 -4.577 10.022 1.00 29.26 ? 212 ILE B CD1 1 ATOM 1749 N N . VAL A 1 225 ? 14.825 -2.987 15.601 1.00 23.59 ? 213 VAL B N 1 ATOM 1750 C CA . VAL A 1 225 ? 14.596 -3.550 16.943 1.00 24.05 ? 213 VAL B CA 1 ATOM 1751 C C . VAL A 1 225 ? 14.416 -5.070 16.801 1.00 23.74 ? 213 VAL B C 1 ATOM 1752 O O . VAL A 1 225 ? 13.536 -5.513 16.057 1.00 25.89 ? 213 VAL B O 1 ATOM 1753 C CB . VAL A 1 225 ? 13.337 -2.955 17.621 1.00 23.68 ? 213 VAL B CB 1 ATOM 1754 C CG1 . VAL A 1 225 ? 13.059 -3.630 18.966 1.00 22.39 ? 213 VAL B CG1 1 ATOM 1755 C CG2 . VAL A 1 225 ? 13.472 -1.456 17.829 1.00 24.79 ? 213 VAL B CG2 1 ATOM 1756 N N . SER A 1 226 ? 15.256 -5.863 17.476 1.00 23.67 ? 214 SER B N 1 ATOM 1757 C CA . SER A 1 226 ? 15.225 -7.336 17.346 1.00 24.19 ? 214 SER B CA 1 ATOM 1758 C C . SER A 1 226 ? 14.932 -8.057 18.644 1.00 25.76 ? 214 SER B C 1 ATOM 1759 O O . SER A 1 226 ? 14.024 -8.852 18.692 1.00 26.85 ? 214 SER B O 1 ATOM 1760 C CB . SER A 1 226 ? 16.543 -7.882 16.787 1.00 25.96 ? 214 SER B CB 1 ATOM 1761 O OG . SER A 1 226 ? 16.463 -9.285 16.617 1.00 25.21 ? 214 SER B OG 1 ATOM 1762 N N . TRP A 1 227 ? 15.752 -7.851 19.674 1.00 26.26 ? 215 TRP B N 1 ATOM 1763 C CA . TRP A 1 227 ? 15.590 -8.624 20.906 1.00 25.00 ? 215 TRP B CA 1 ATOM 1764 C C . TRP A 1 227 ? 16.232 -7.982 22.132 1.00 25.86 ? 215 TRP B C 1 ATOM 1765 O O . TRP A 1 227 ? 16.999 -7.023 22.023 1.00 25.12 ? 215 TRP B O 1 ATOM 1766 C CB . TRP A 1 227 ? 16.119 -10.071 20.740 1.00 25.60 ? 215 TRP B CB 1 ATOM 1767 C CG . TRP A 1 227 ? 17.596 -10.253 20.432 1.00 25.80 ? 215 TRP B CG 1 ATOM 1768 C CD1 . TRP A 1 227 ? 18.191 -10.231 19.197 1.00 28.28 ? 215 TRP B CD1 1 ATOM 1769 C CD2 . TRP A 1 227 ? 18.653 -10.516 21.372 1.00 26.68 ? 215 TRP B CD2 1 ATOM 1770 N NE1 . TRP A 1 227 ? 19.554 -10.456 19.310 1.00 28.36 ? 215 TRP B NE1 1 ATOM 1771 C CE2 . TRP A 1 227 ? 19.859 -10.647 20.630 1.00 27.57 ? 215 TRP B CE2 1 ATOM 1772 C CE3 . TRP A 1 227 ? 18.700 -10.657 22.758 1.00 28.19 ? 215 TRP B CE3 1 ATOM 1773 C CZ2 . TRP A 1 227 ? 21.087 -10.881 21.236 1.00 29.32 ? 215 TRP B CZ2 1 ATOM 1774 C CZ3 . TRP A 1 227 ? 19.925 -10.916 23.362 1.00 29.04 ? 215 TRP B CZ3 1 ATOM 1775 C CH2 . TRP A 1 227 ? 21.104 -11.035 22.596 1.00 30.30 ? 215 TRP B CH2 1 ATOM 1776 N N . GLY A 1 228 ? 15.888 -8.530 23.295 1.00 24.47 ? 216 GLY B N 1 ATOM 1777 C CA . GLY A 1 228 ? 16.484 -8.132 24.554 1.00 26.53 ? 216 GLY B CA 1 ATOM 1778 C C . GLY A 1 228 ? 15.994 -9.029 25.647 1.00 28.86 ? 216 GLY B C 1 ATOM 1779 O O . GLY A 1 228 ? 15.173 -9.909 25.422 1.00 36.06 ? 216 GLY B O 1 ATOM 1780 N N . GLU A 1 229 ? 16.516 -8.846 26.840 1.00 31.19 ? 217 GLU B N 1 ATOM 1781 C CA . GLU A 1 229 ? 16.090 -9.662 27.957 1.00 33.70 ? 217 GLU B CA 1 ATOM 1782 C C . GLU A 1 229 ? 15.504 -8.729 28.984 1.00 36.24 ? 217 GLU B C 1 ATOM 1783 O O . GLU A 1 229 ? 16.233 -7.975 29.621 1.00 37.95 ? 217 GLU B O 1 ATOM 1784 C CB . GLU A 1 229 ? 17.269 -10.462 28.508 1.00 37.10 ? 217 GLU B CB 1 ATOM 1785 C CG . GLU A 1 229 ? 17.795 -11.513 27.521 1.00 37.84 ? 217 GLU B CG 1 ATOM 1786 C CD . GLU A 1 229 ? 19.100 -12.143 27.976 1.00 40.92 ? 217 GLU B CD 1 ATOM 1787 O OE1 . GLU A 1 229 ? 20.165 -11.532 27.773 1.00 38.52 ? 217 GLU B OE1 1 ATOM 1788 O OE2 . GLU A 1 229 ? 19.061 -13.258 28.531 1.00 46.92 ? 217 GLU B OE2 1 ATOM 1789 N N . GLY A 1 230 ? 14.176 -8.772 29.124 1.00 34.94 ? 219 GLY B N 1 ATOM 1790 C CA . GLY A 1 230 ? 13.443 -7.778 29.889 1.00 37.99 ? 219 GLY B CA 1 ATOM 1791 C C . GLY A 1 230 ? 13.495 -6.469 29.127 1.00 35.63 ? 219 GLY B C 1 ATOM 1792 O O . GLY A 1 230 ? 13.808 -6.458 27.935 1.00 33.33 ? 219 GLY B O 1 ATOM 1793 N N . CYS A 1 231 ? 13.211 -5.367 29.816 1.00 33.36 ? 220 CYS B N 1 ATOM 1794 C CA . CYS A 1 231 ? 13.215 -4.055 29.194 1.00 35.54 ? 220 CYS B CA 1 ATOM 1795 C C . CYS A 1 231 ? 13.787 -3.039 30.153 1.00 30.66 ? 220 CYS B C 1 ATOM 1796 O O . CYS A 1 231 ? 13.291 -2.910 31.256 1.00 29.36 ? 220 CYS B O 1 ATOM 1797 C CB . CYS A 1 231 ? 11.775 -3.651 28.780 1.00 38.77 ? 220 CYS B CB 1 ATOM 1798 S SG . CYS A 1 231 ? 11.022 -4.770 27.555 1.00 42.72 ? 220 CYS B SG 1 ATOM 1799 N N . ASP A 1 232 ? 14.826 -2.318 29.721 1.00 29.27 ? 221 ASP B N 1 ATOM 1800 C CA . ASP A 1 232 ? 15.441 -1.251 30.516 1.00 29.92 ? 221 ASP B CA 1 ATOM 1801 C C . ASP A 1 232 ? 16.034 -1.738 31.843 1.00 30.10 ? 221 ASP B C 1 ATOM 1802 O O . ASP A 1 232 ? 15.970 -1.045 32.854 1.00 30.28 ? 221 ASP B O 1 ATOM 1803 C CB . ASP A 1 232 ? 14.429 -0.123 30.773 1.00 34.29 ? 221 ASP B CB 1 ATOM 1804 C CG . ASP A 1 232 ? 15.091 1.160 31.260 1.00 34.74 ? 221 ASP B CG 1 ATOM 1805 O OD1 . ASP A 1 232 ? 16.172 1.534 30.722 1.00 34.41 ? 221 ASP B OD1 1 ATOM 1806 O OD2 . ASP A 1 232 ? 14.540 1.774 32.198 1.00 32.44 ? 221 ASP B OD2 1 ATOM 1807 N N . ARG A 1 233 A 16.604 -2.940 31.841 1.00 27.87 ? 221 ARG B N 1 ATOM 1808 C CA . ARG A 1 233 A 17.251 -3.463 33.032 1.00 29.73 ? 221 ARG B CA 1 ATOM 1809 C C . ARG A 1 233 A 18.687 -2.961 33.118 1.00 30.07 ? 221 ARG B C 1 ATOM 1810 O O . ARG A 1 233 A 19.379 -2.829 32.109 1.00 28.69 ? 221 ARG B O 1 ATOM 1811 C CB . ARG A 1 233 A 17.229 -4.999 33.035 1.00 30.69 ? 221 ARG B CB 1 ATOM 1812 C CG . ARG A 1 233 A 15.847 -5.542 33.354 1.00 32.07 ? 221 ARG B CG 1 ATOM 1813 C CD . ARG A 1 233 A 15.786 -7.062 33.361 1.00 33.24 ? 221 ARG B CD 1 ATOM 1814 N NE . ARG A 1 233 A 14.398 -7.516 33.539 1.00 33.00 ? 221 ARG B NE 1 ATOM 1815 C CZ . ARG A 1 233 A 14.016 -8.600 34.215 1.00 32.82 ? 221 ARG B CZ 1 ATOM 1816 N NH1 . ARG A 1 233 A 14.902 -9.386 34.830 1.00 35.53 ? 221 ARG B NH1 1 ATOM 1817 N NH2 . ARG A 1 233 A 12.729 -8.895 34.303 1.00 33.26 ? 221 ARG B NH2 1 ATOM 1818 N N . ASP A 1 234 ? 19.139 -2.706 34.334 1.00 29.99 ? 222 ASP B N 1 ATOM 1819 C CA . ASP A 1 234 ? 20.519 -2.319 34.550 1.00 33.14 ? 222 ASP B CA 1 ATOM 1820 C C . ASP A 1 234 ? 21.436 -3.440 34.088 1.00 34.16 ? 222 ASP B C 1 ATOM 1821 O O . ASP A 1 234 ? 21.210 -4.601 34.412 1.00 36.51 ? 222 ASP B O 1 ATOM 1822 C CB . ASP A 1 234 ? 20.764 -2.058 36.027 1.00 34.57 ? 222 ASP B CB 1 ATOM 1823 C CG . ASP A 1 234 ? 20.109 -0.767 36.519 1.00 38.44 ? 222 ASP B CG 1 ATOM 1824 O OD1 . ASP A 1 234 ? 19.833 0.156 35.718 1.00 36.50 ? 222 ASP B OD1 1 ATOM 1825 O OD2 . ASP A 1 234 ? 19.897 -0.666 37.739 1.00 40.82 ? 222 ASP B OD2 1 ATOM 1826 N N . GLY A 1 235 ? 22.474 -3.102 33.336 1.00 33.35 ? 223 GLY B N 1 ATOM 1827 C CA . GLY A 1 235 ? 23.463 -4.108 32.934 1.00 34.20 ? 223 GLY B CA 1 ATOM 1828 C C . GLY A 1 235 ? 23.026 -4.934 31.740 1.00 33.52 ? 223 GLY B C 1 ATOM 1829 O O . GLY A 1 235 ? 23.717 -5.885 31.344 1.00 32.49 ? 223 GLY B O 1 ATOM 1830 N N . LYS A 1 236 ? 21.875 -4.568 31.171 1.00 35.12 ? 224 LYS B N 1 ATOM 1831 C CA . LYS A 1 236 ? 21.309 -5.215 29.994 1.00 33.87 ? 224 LYS B CA 1 ATOM 1832 C C . LYS A 1 236 ? 21.109 -4.195 28.887 1.00 31.15 ? 224 LYS B C 1 ATOM 1833 O O . LYS A 1 236 ? 20.928 -3.000 29.157 1.00 30.98 ? 224 LYS B O 1 ATOM 1834 C CB . LYS A 1 236 ? 19.974 -5.872 30.361 1.00 36.39 ? 224 LYS B CB 1 ATOM 1835 C CG . LYS A 1 236 ? 20.120 -7.136 31.190 1.00 43.10 ? 224 LYS B CG 1 ATOM 1836 C CD . LYS A 1 236 ? 20.755 -8.224 30.339 1.00 49.59 ? 224 LYS B CD 1 ATOM 1837 C CE . LYS A 1 236 ? 20.653 -9.593 30.968 1.00 55.50 ? 224 LYS B CE 1 ATOM 1838 N NZ . LYS A 1 236 ? 21.226 -10.633 30.066 1.00 53.11 ? 224 LYS B NZ 1 ATOM 1839 N N . TYR A 1 237 ? 21.120 -4.676 27.646 1.00 27.45 ? 225 TYR B N 1 ATOM 1840 C CA . TYR A 1 237 ? 21.069 -3.814 26.468 1.00 27.68 ? 225 TYR B CA 1 ATOM 1841 C C . TYR A 1 237 ? 20.103 -4.377 25.438 1.00 27.51 ? 225 TYR B C 1 ATOM 1842 O O . TYR A 1 237 ? 19.859 -5.587 25.398 1.00 28.73 ? 225 TYR B O 1 ATOM 1843 C CB . TYR A 1 237 ? 22.493 -3.672 25.893 1.00 27.41 ? 225 TYR B CB 1 ATOM 1844 C CG . TYR A 1 237 ? 23.430 -3.175 26.971 1.00 29.68 ? 225 TYR B CG 1 ATOM 1845 C CD1 . TYR A 1 237 ? 23.593 -1.808 27.202 1.00 29.79 ? 225 TYR B CD1 1 ATOM 1846 C CD2 . TYR A 1 237 ? 24.102 -4.061 27.800 1.00 31.71 ? 225 TYR B CD2 1 ATOM 1847 C CE1 . TYR A 1 237 ? 24.431 -1.345 28.204 1.00 30.35 ? 225 TYR B CE1 1 ATOM 1848 C CE2 . TYR A 1 237 ? 24.931 -3.606 28.813 1.00 32.71 ? 225 TYR B CE2 1 ATOM 1849 C CZ . TYR A 1 237 ? 25.086 -2.244 29.003 1.00 32.81 ? 225 TYR B CZ 1 ATOM 1850 O OH . TYR A 1 237 ? 25.875 -1.781 30.006 1.00 34.03 ? 225 TYR B OH 1 ATOM 1851 N N . GLY A 1 238 ? 19.548 -3.491 24.623 1.00 23.43 ? 226 GLY B N 1 ATOM 1852 C CA . GLY A 1 238 ? 18.691 -3.887 23.523 1.00 25.72 ? 226 GLY B CA 1 ATOM 1853 C C . GLY A 1 238 ? 19.562 -4.293 22.355 1.00 25.28 ? 226 GLY B C 1 ATOM 1854 O O . GLY A 1 238 ? 20.612 -3.670 22.125 1.00 24.99 ? 226 GLY B O 1 ATOM 1855 N N . PHE A 1 239 ? 19.148 -5.337 21.640 1.00 23.43 ? 227 PHE B N 1 ATOM 1856 C CA . PHE A 1 239 ? 19.844 -5.758 20.416 1.00 25.44 ? 227 PHE B CA 1 ATOM 1857 C C . PHE A 1 239 ? 19.071 -5.422 19.155 1.00 25.29 ? 227 PHE B C 1 ATOM 1858 O O . PHE A 1 239 ? 17.850 -5.454 19.142 1.00 23.89 ? 227 PHE B O 1 ATOM 1859 C CB . PHE A 1 239 ? 20.180 -7.237 20.469 1.00 26.02 ? 227 PHE B CB 1 ATOM 1860 C CG . PHE A 1 239 ? 21.280 -7.533 21.433 1.00 27.00 ? 227 PHE B CG 1 ATOM 1861 C CD1 . PHE A 1 239 ? 21.034 -7.514 22.795 1.00 29.10 ? 227 PHE B CD1 1 ATOM 1862 C CD2 . PHE A 1 239 ? 22.575 -7.759 20.987 1.00 27.07 ? 227 PHE B CD2 1 ATOM 1863 C CE1 . PHE A 1 239 ? 22.056 -7.731 23.703 1.00 28.77 ? 227 PHE B CE1 1 ATOM 1864 C CE2 . PHE A 1 239 ? 23.598 -7.997 21.884 1.00 29.26 ? 227 PHE B CE2 1 ATOM 1865 C CZ . PHE A 1 239 ? 23.338 -7.983 23.241 1.00 29.45 ? 227 PHE B CZ 1 ATOM 1866 N N . TYR A 1 240 ? 19.830 -5.098 18.103 1.00 24.47 ? 228 TYR B N 1 ATOM 1867 C CA . TYR A 1 240 ? 19.322 -4.555 16.877 1.00 24.91 ? 228 TYR B CA 1 ATOM 1868 C C . TYR A 1 240 ? 19.981 -5.243 15.714 1.00 28.10 ? 228 TYR B C 1 ATOM 1869 O O . TYR A 1 240 ? 21.203 -5.524 15.728 1.00 25.47 ? 228 TYR B O 1 ATOM 1870 C CB . TYR A 1 240 ? 19.613 -3.026 16.787 1.00 24.47 ? 228 TYR B CB 1 ATOM 1871 C CG . TYR A 1 240 ? 18.949 -2.262 17.881 1.00 24.03 ? 228 TYR B CG 1 ATOM 1872 C CD1 . TYR A 1 240 ? 19.507 -2.232 19.147 1.00 27.99 ? 228 TYR B CD1 1 ATOM 1873 C CD2 . TYR A 1 240 ? 17.737 -1.606 17.681 1.00 24.22 ? 228 TYR B CD2 1 ATOM 1874 C CE1 . TYR A 1 240 ? 18.883 -1.562 20.176 1.00 28.79 ? 228 TYR B CE1 1 ATOM 1875 C CE2 . TYR A 1 240 ? 17.103 -0.921 18.715 1.00 25.49 ? 228 TYR B CE2 1 ATOM 1876 C CZ . TYR A 1 240 ? 17.700 -0.906 19.971 1.00 26.42 ? 228 TYR B CZ 1 ATOM 1877 O OH . TYR A 1 240 ? 17.107 -0.261 21.056 1.00 26.21 ? 228 TYR B OH 1 ATOM 1878 N N . THR A 1 241 ? 19.191 -5.485 14.681 1.00 25.98 ? 229 THR B N 1 ATOM 1879 C CA . THR A 1 241 ? 19.734 -6.077 13.472 1.00 29.05 ? 229 THR B CA 1 ATOM 1880 C C . THR A 1 241 ? 20.589 -5.022 12.790 1.00 26.69 ? 229 THR B C 1 ATOM 1881 O O . THR A 1 241 ? 20.161 -3.886 12.600 1.00 28.72 ? 229 THR B O 1 ATOM 1882 C CB . THR A 1 241 ? 18.613 -6.527 12.524 1.00 30.54 ? 229 THR B CB 1 ATOM 1883 O OG1 . THR A 1 241 ? 17.729 -7.415 13.227 1.00 31.13 ? 229 THR B OG1 1 ATOM 1884 C CG2 . THR A 1 241 ? 19.192 -7.214 11.291 1.00 28.69 ? 229 THR B CG2 1 ATOM 1885 N N . HIS A 1 242 ? 21.781 -5.428 12.401 1.00 29.47 ? 230 HIS B N 1 ATOM 1886 C CA . HIS A 1 242 ? 22.789 -4.543 11.878 1.00 28.71 ? 230 HIS B CA 1 ATOM 1887 C C . HIS A 1 242 ? 22.472 -4.378 10.406 1.00 28.88 ? 230 HIS B C 1 ATOM 1888 O O . HIS A 1 242 ? 22.850 -5.209 9.581 1.00 33.90 ? 230 HIS B O 1 ATOM 1889 C CB . HIS A 1 242 ? 24.137 -5.213 12.092 1.00 34.55 ? 230 HIS B CB 1 ATOM 1890 C CG . HIS A 1 242 ? 25.323 -4.331 11.873 1.00 36.15 ? 230 HIS B CG 1 ATOM 1891 N ND1 . HIS A 1 242 ? 25.455 -3.499 10.783 1.00 34.82 ? 230 HIS B ND1 1 ATOM 1892 C CD2 . HIS A 1 242 ? 26.468 -4.206 12.580 1.00 37.26 ? 230 HIS B CD2 1 ATOM 1893 C CE1 . HIS A 1 242 ? 26.616 -2.875 10.844 1.00 35.84 ? 230 HIS B CE1 1 ATOM 1894 N NE2 . HIS A 1 242 ? 27.255 -3.295 11.920 1.00 36.65 ? 230 HIS B NE2 1 ATOM 1895 N N . VAL A 1 243 ? 21.783 -3.297 10.073 1.00 27.61 ? 231 VAL B N 1 ATOM 1896 C CA . VAL A 1 243 ? 21.240 -3.109 8.713 1.00 28.64 ? 231 VAL B CA 1 ATOM 1897 C C . VAL A 1 243 ? 22.318 -3.080 7.634 1.00 28.24 ? 231 VAL B C 1 ATOM 1898 O O . VAL A 1 243 ? 22.186 -3.770 6.616 1.00 30.07 ? 231 VAL B O 1 ATOM 1899 C CB . VAL A 1 243 ? 20.350 -1.853 8.602 1.00 28.52 ? 231 VAL B CB 1 ATOM 1900 C CG1 . VAL A 1 243 ? 20.054 -1.509 7.145 1.00 32.26 ? 231 VAL B CG1 1 ATOM 1901 C CG2 . VAL A 1 243 ? 19.041 -2.064 9.351 1.00 29.65 ? 231 VAL B CG2 1 ATOM 1902 N N . PHE A 1 244 ? 23.382 -2.311 7.831 1.00 29.56 ? 232 PHE B N 1 ATOM 1903 C CA . PHE A 1 244 ? 24.401 -2.219 6.778 1.00 31.90 ? 232 PHE B CA 1 ATOM 1904 C C . PHE A 1 244 ? 25.027 -3.571 6.456 1.00 34.37 ? 232 PHE B C 1 ATOM 1905 O O . PHE A 1 244 ? 25.312 -3.853 5.300 1.00 33.08 ? 232 PHE B O 1 ATOM 1906 C CB . PHE A 1 244 ? 25.521 -1.238 7.115 1.00 32.63 ? 232 PHE B CB 1 ATOM 1907 C CG . PHE A 1 244 ? 26.551 -1.145 6.028 1.00 33.56 ? 232 PHE B CG 1 ATOM 1908 C CD1 . PHE A 1 244 ? 26.242 -0.525 4.828 1.00 37.87 ? 232 PHE B CD1 1 ATOM 1909 C CD2 . PHE A 1 244 ? 27.796 -1.743 6.165 1.00 35.52 ? 232 PHE B CD2 1 ATOM 1910 C CE1 . PHE A 1 244 ? 27.166 -0.466 3.800 1.00 37.29 ? 232 PHE B CE1 1 ATOM 1911 C CE2 . PHE A 1 244 ? 28.732 -1.692 5.136 1.00 38.33 ? 232 PHE B CE2 1 ATOM 1912 C CZ . PHE A 1 244 ? 28.417 -1.049 3.953 1.00 39.91 ? 232 PHE B CZ 1 ATOM 1913 N N . ARG A 1 245 ? 25.256 -4.394 7.479 1.00 34.83 ? 233 ARG B N 1 ATOM 1914 C CA . ARG A 1 245 ? 25.820 -5.738 7.280 1.00 41.49 ? 233 ARG B CA 1 ATOM 1915 C C . ARG A 1 245 ? 24.967 -6.607 6.335 1.00 36.87 ? 233 ARG B C 1 ATOM 1916 O O . ARG A 1 245 ? 25.493 -7.492 5.681 1.00 38.21 ? 233 ARG B O 1 ATOM 1917 C CB . ARG A 1 245 ? 25.973 -6.470 8.614 1.00 42.89 ? 233 ARG B CB 1 ATOM 1918 C CG . ARG A 1 245 ? 27.093 -5.961 9.517 1.00 48.84 ? 233 ARG B CG 1 ATOM 1919 C CD . ARG A 1 245 ? 28.399 -6.710 9.329 1.00 54.41 ? 233 ARG B CD 1 ATOM 1920 N NE . ARG A 1 245 ? 28.196 -8.153 9.403 1.00 58.77 ? 233 ARG B NE 1 ATOM 1921 C CZ . ARG A 1 245 ? 29.106 -9.064 9.072 1.00 60.66 ? 233 ARG B CZ 1 ATOM 1922 N NH1 . ARG A 1 245 ? 28.797 -10.355 9.165 1.00 57.78 ? 233 ARG B NH1 1 ATOM 1923 N NH2 . ARG A 1 245 ? 30.320 -8.696 8.658 1.00 60.19 ? 233 ARG B NH2 1 ATOM 1924 N N . LEU A 1 246 ? 23.659 -6.362 6.290 1.00 34.46 ? 234 LEU B N 1 ATOM 1925 C CA . LEU A 1 246 ? 22.744 -7.134 5.437 1.00 37.35 ? 234 LEU B CA 1 ATOM 1926 C C . LEU A 1 246 ? 22.293 -6.401 4.168 1.00 40.24 ? 234 LEU B C 1 ATOM 1927 O O . LEU A 1 246 ? 21.382 -6.860 3.479 1.00 37.47 ? 234 LEU B O 1 ATOM 1928 C CB . LEU A 1 246 ? 21.521 -7.562 6.262 1.00 40.73 ? 234 LEU B CB 1 ATOM 1929 C CG . LEU A 1 246 ? 21.904 -8.251 7.587 1.00 37.72 ? 234 LEU B CG 1 ATOM 1930 C CD1 . LEU A 1 246 ? 20.687 -8.550 8.445 1.00 41.10 ? 234 LEU B CD1 1 ATOM 1931 C CD2 . LEU A 1 246 ? 22.704 -9.514 7.323 1.00 45.27 ? 234 LEU B CD2 1 ATOM 1932 N N . LYS A 1 247 ? 22.938 -5.284 3.836 1.00 40.29 ? 235 LYS B N 1 ATOM 1933 C CA . LYS A 1 247 ? 22.492 -4.460 2.721 1.00 47.39 ? 235 LYS B CA 1 ATOM 1934 C C . LYS A 1 247 ? 22.634 -5.168 1.353 1.00 45.08 ? 235 LYS B C 1 ATOM 1935 O O . LYS A 1 247 ? 21.893 -4.856 0.427 1.00 48.91 ? 235 LYS B O 1 ATOM 1936 C CB . LYS A 1 247 ? 23.212 -3.104 2.717 1.00 50.92 ? 235 LYS B CB 1 ATOM 1937 C CG . LYS A 1 247 ? 22.633 -2.107 1.723 1.00 55.84 ? 235 LYS B CG 1 ATOM 1938 C CD . LYS A 1 247 ? 23.159 -0.696 1.940 1.00 58.44 ? 235 LYS B CD 1 ATOM 1939 C CE . LYS A 1 247 ? 22.749 0.223 0.797 1.00 56.50 ? 235 LYS B CE 1 ATOM 1940 N NZ . LYS A 1 247 ? 23.340 1.583 0.925 1.00 55.70 ? 235 LYS B NZ 1 ATOM 1941 N N . LYS A 1 248 ? 23.547 -6.122 1.230 1.00 45.18 ? 236 LYS B N 1 ATOM 1942 C CA . LYS A 1 248 ? 23.650 -6.890 -0.022 1.00 50.14 ? 236 LYS B CA 1 ATOM 1943 C C . LYS A 1 248 ? 22.402 -7.731 -0.264 1.00 49.40 ? 236 LYS B C 1 ATOM 1944 O O . LYS A 1 248 ? 21.905 -7.818 -1.389 1.00 47.52 ? 236 LYS B O 1 ATOM 1945 C CB . LYS A 1 248 ? 24.897 -7.772 -0.052 1.00 55.91 ? 236 LYS B CB 1 ATOM 1946 C CG . LYS A 1 248 ? 25.932 -7.305 -1.062 1.00 67.17 ? 236 LYS B CG 1 ATOM 1947 C CD . LYS A 1 248 ? 27.275 -8.001 -0.889 1.00 79.58 ? 236 LYS B CD 1 ATOM 1948 C CE . LYS A 1 248 ? 28.060 -7.444 0.293 1.00 83.51 ? 236 LYS B CE 1 ATOM 1949 N NZ . LYS A 1 248 ? 28.294 -5.974 0.189 1.00 86.64 ? 236 LYS B NZ 1 ATOM 1950 N N . TRP A 1 249 ? 21.905 -8.354 0.797 1.00 44.76 ? 237 TRP B N 1 ATOM 1951 C CA . TRP A 1 249 ? 20.653 -9.086 0.731 1.00 42.76 ? 237 TRP B CA 1 ATOM 1952 C C . TRP A 1 249 ? 19.503 -8.136 0.360 1.00 38.04 ? 237 TRP B C 1 ATOM 1953 O O . TRP A 1 249 ? 18.713 -8.427 -0.549 1.00 39.74 ? 237 TRP B O 1 ATOM 1954 C CB . TRP A 1 249 ? 20.341 -9.774 2.066 1.00 41.37 ? 237 TRP B CB 1 ATOM 1955 C CG . TRP A 1 249 ? 19.022 -10.434 2.010 1.00 40.23 ? 237 TRP B CG 1 ATOM 1956 C CD1 . TRP A 1 249 ? 18.708 -11.574 1.338 1.00 42.10 ? 237 TRP B CD1 1 ATOM 1957 C CD2 . TRP A 1 249 ? 17.812 -9.953 2.577 1.00 39.78 ? 237 TRP B CD2 1 ATOM 1958 N NE1 . TRP A 1 249 ? 17.375 -11.849 1.477 1.00 40.75 ? 237 TRP B NE1 1 ATOM 1959 C CE2 . TRP A 1 249 ? 16.799 -10.873 2.237 1.00 39.02 ? 237 TRP B CE2 1 ATOM 1960 C CE3 . TRP A 1 249 ? 17.483 -8.847 3.356 1.00 37.89 ? 237 TRP B CE3 1 ATOM 1961 C CZ2 . TRP A 1 249 ? 15.481 -10.722 2.657 1.00 40.78 ? 237 TRP B CZ2 1 ATOM 1962 C CZ3 . TRP A 1 249 ? 16.170 -8.698 3.769 1.00 39.92 ? 237 TRP B CZ3 1 ATOM 1963 C CH2 . TRP A 1 249 ? 15.186 -9.634 3.410 1.00 36.54 ? 237 TRP B CH2 1 ATOM 1964 N N . ILE A 1 250 ? 19.429 -6.998 1.046 1.00 34.06 ? 238 ILE B N 1 ATOM 1965 C CA . ILE A 1 250 ? 18.413 -5.978 0.744 1.00 34.30 ? 238 ILE B CA 1 ATOM 1966 C C . ILE A 1 250 ? 18.444 -5.602 -0.748 1.00 38.68 ? 238 ILE B C 1 ATOM 1967 O O . ILE A 1 250 ? 17.394 -5.580 -1.403 1.00 37.46 ? 238 ILE B O 1 ATOM 1968 C CB . ILE A 1 250 ? 18.579 -4.726 1.622 1.00 35.40 ? 238 ILE B CB 1 ATOM 1969 C CG1 . ILE A 1 250 ? 18.329 -5.082 3.106 1.00 33.99 ? 238 ILE B CG1 1 ATOM 1970 C CG2 . ILE A 1 250 ? 17.624 -3.624 1.176 1.00 34.78 ? 238 ILE B CG2 1 ATOM 1971 C CD1 . ILE A 1 250 ? 18.616 -3.963 4.068 1.00 31.86 ? 238 ILE B CD1 1 ATOM 1972 N N . GLN A 1 251 ? 19.646 -5.358 -1.275 1.00 39.79 ? 239 GLN B N 1 ATOM 1973 C CA . GLN A 1 251 ? 19.849 -4.984 -2.687 1.00 45.32 ? 239 GLN B CA 1 ATOM 1974 C C . GLN A 1 251 ? 19.404 -6.068 -3.652 1.00 46.72 ? 239 GLN B C 1 ATOM 1975 O O . GLN A 1 251 ? 18.778 -5.778 -4.677 1.00 45.09 ? 239 GLN B O 1 ATOM 1976 C CB . GLN A 1 251 ? 21.335 -4.686 -2.957 1.00 52.48 ? 239 GLN B CB 1 ATOM 1977 C CG . GLN A 1 251 ? 21.657 -4.409 -4.432 1.00 63.26 ? 239 GLN B CG 1 ATOM 1978 C CD . GLN A 1 251 ? 23.144 -4.437 -4.760 1.00 70.76 ? 239 GLN B CD 1 ATOM 1979 O OE1 . GLN A 1 251 ? 23.987 -4.654 -3.890 1.00 82.76 ? 239 GLN B OE1 1 ATOM 1980 N NE2 . GLN A 1 251 ? 23.468 -4.217 -6.028 1.00 72.73 ? 239 GLN B NE2 1 ATOM 1981 N N . LYS A 1 252 ? 19.798 -7.306 -3.354 1.00 45.88 ? 240 LYS B N 1 ATOM 1982 C CA . LYS A 1 252 ? 19.442 -8.462 -4.175 1.00 47.62 ? 240 LYS B CA 1 ATOM 1983 C C . LYS A 1 252 ? 17.925 -8.554 -4.315 1.00 43.42 ? 240 LYS B C 1 ATOM 1984 O O . LYS A 1 252 ? 17.398 -8.645 -5.425 1.00 42.30 ? 240 LYS B O 1 ATOM 1985 C CB . LYS A 1 252 ? 19.977 -9.762 -3.549 1.00 51.70 ? 240 LYS B CB 1 ATOM 1986 C CG . LYS A 1 252 ? 20.573 -10.746 -4.545 1.00 63.76 ? 240 LYS B CG 1 ATOM 1987 C CD . LYS A 1 252 ? 21.961 -10.299 -4.996 1.00 70.93 ? 240 LYS B CD 1 ATOM 1988 C CE . LYS A 1 252 ? 22.541 -11.235 -6.044 1.00 81.02 ? 240 LYS B CE 1 ATOM 1989 N NZ . LYS A 1 252 ? 23.907 -10.832 -6.488 1.00 84.32 ? 240 LYS B NZ 1 ATOM 1990 N N . VAL A 1 253 ? 17.237 -8.518 -3.174 1.00 38.99 ? 241 VAL B N 1 ATOM 1991 C CA . VAL A 1 253 ? 15.796 -8.712 -3.137 1.00 39.81 ? 241 VAL B CA 1 ATOM 1992 C C . VAL A 1 253 ? 15.116 -7.661 -3.993 1.00 40.47 ? 241 VAL B C 1 ATOM 1993 O O . VAL A 1 253 ? 14.328 -7.990 -4.877 1.00 42.50 ? 241 VAL B O 1 ATOM 1994 C CB . VAL A 1 253 ? 15.262 -8.691 -1.689 1.00 38.74 ? 241 VAL B CB 1 ATOM 1995 C CG1 . VAL A 1 253 ? 13.750 -8.507 -1.656 1.00 39.95 ? 241 VAL B CG1 1 ATOM 1996 C CG2 . VAL A 1 253 ? 15.651 -9.992 -0.993 1.00 39.16 ? 241 VAL B CG2 1 ATOM 1997 N N . ILE A 1 254 ? 15.466 -6.405 -3.738 1.00 41.92 ? 242 ILE B N 1 ATOM 1998 C CA . ILE A 1 254 ? 14.894 -5.263 -4.453 1.00 45.11 ? 242 ILE B CA 1 ATOM 1999 C C . ILE A 1 254 ? 15.224 -5.292 -5.941 1.00 49.27 ? 242 ILE B C 1 ATOM 2000 O O . ILE A 1 254 ? 14.331 -5.114 -6.761 1.00 49.54 ? 242 ILE B O 1 ATOM 2001 C CB . ILE A 1 254 ? 15.321 -3.932 -3.785 1.00 44.05 ? 242 ILE B CB 1 ATOM 2002 C CG1 . ILE A 1 254 ? 14.443 -3.700 -2.548 1.00 41.34 ? 242 ILE B CG1 1 ATOM 2003 C CG2 . ILE A 1 254 ? 15.207 -2.757 -4.749 1.00 47.02 ? 242 ILE B CG2 1 ATOM 2004 C CD1 . ILE A 1 254 ? 15.051 -2.796 -1.506 1.00 43.03 ? 242 ILE B CD1 1 ATOM 2005 N N . ASP A 1 255 ? 16.484 -5.531 -6.295 1.00 55.12 ? 243 ASP B N 1 ATOM 2006 C CA . ASP A 1 255 ? 16.862 -5.599 -7.714 1.00 62.43 ? 243 ASP B CA 1 ATOM 2007 C C . ASP A 1 255 ? 16.166 -6.741 -8.444 1.00 66.67 ? 243 ASP B C 1 ATOM 2008 O O . ASP A 1 255 ? 15.739 -6.580 -9.585 1.00 71.54 ? 243 ASP B O 1 ATOM 2009 C CB . ASP A 1 255 ? 18.378 -5.738 -7.882 1.00 71.31 ? 243 ASP B CB 1 ATOM 2010 C CG . ASP A 1 255 ? 19.123 -4.436 -7.624 1.00 79.39 ? 243 ASP B CG 1 ATOM 2011 O OD1 . ASP A 1 255 ? 18.521 -3.479 -7.077 1.00 91.97 ? 243 ASP B OD1 1 ATOM 2012 O OD2 . ASP A 1 255 ? 20.324 -4.373 -7.969 1.00 83.23 ? 243 ASP B OD2 1 ATOM 2013 N N . GLN A 1 256 ? 16.048 -7.891 -7.789 1.00 67.52 ? 244 GLN B N 1 ATOM 2014 C CA . GLN A 1 256 ? 15.496 -9.078 -8.440 1.00 75.90 ? 244 GLN B CA 1 ATOM 2015 C C . GLN A 1 256 ? 13.969 -9.118 -8.444 1.00 74.72 ? 244 GLN B C 1 ATOM 2016 O O . GLN A 1 256 ? 13.375 -9.775 -9.298 1.00 75.10 ? 244 GLN B O 1 ATOM 2017 C CB . GLN A 1 256 ? 16.081 -10.350 -7.814 1.00 80.47 ? 244 GLN B CB 1 ATOM 2018 C CG . GLN A 1 256 ? 17.569 -10.511 -8.117 1.00 86.70 ? 244 GLN B CG 1 ATOM 2019 C CD . GLN A 1 256 ? 18.183 -11.766 -7.523 1.00 92.34 ? 244 GLN B CD 1 ATOM 2020 O OE1 . GLN A 1 256 ? 17.700 -12.304 -6.526 1.00 99.30 ? 244 GLN B OE1 1 ATOM 2021 N NE2 . GLN A 1 256 ? 19.268 -12.233 -8.132 1.00 93.64 ? 244 GLN B NE2 1 ATOM 2022 N N . PHE A 1 257 ? 13.338 -8.414 -7.505 1.00 76.30 ? 245 PHE B N 1 ATOM 2023 C CA . PHE A 1 257 ? 11.877 -8.405 -7.389 1.00 78.77 ? 245 PHE B CA 1 ATOM 2024 C C . PHE A 1 257 ? 11.318 -6.987 -7.298 1.00 71.63 ? 245 PHE B C 1 ATOM 2025 O O . PHE A 1 257 ? 10.103 -6.802 -7.217 1.00 62.49 ? 245 PHE B O 1 ATOM 2026 C CB . PHE A 1 257 ? 11.437 -9.209 -6.160 1.00 81.41 ? 245 PHE B CB 1 ATOM 2027 C CG . PHE A 1 257 ? 11.645 -10.695 -6.291 1.00 93.58 ? 245 PHE B CG 1 ATOM 2028 C CD1 . PHE A 1 257 ? 10.915 -11.437 -7.223 1.00 101.10 ? 245 PHE B CD1 1 ATOM 2029 C CD2 . PHE A 1 257 ? 12.556 -11.360 -5.478 1.00 93.60 ? 245 PHE B CD2 1 ATOM 2030 C CE1 . PHE A 1 257 ? 11.097 -12.805 -7.345 1.00 99.49 ? 245 PHE B CE1 1 ATOM 2031 C CE2 . PHE A 1 257 ? 12.739 -12.730 -5.594 1.00 96.97 ? 245 PHE B CE2 1 ATOM 2032 C CZ . PHE A 1 257 ? 12.010 -13.453 -6.528 1.00 100.88 ? 245 PHE B CZ 1 ATOM 2033 N N . THR B 2 1 N 22.506 7.809 -5.311 1.00 101.96 ? 1 THR A N 1 ATOM 2034 C CA . THR B 2 1 N 21.490 6.771 -5.654 1.00 99.78 ? 1 THR A CA 1 ATOM 2035 C C . THR B 2 1 N 22.126 5.376 -5.755 1.00 92.71 ? 1 THR A C 1 ATOM 2036 O O . THR B 2 1 N 22.908 5.103 -6.668 1.00 105.00 ? 1 THR A O 1 ATOM 2037 C CB . THR B 2 1 N 20.737 7.122 -6.960 1.00 103.99 ? 1 THR A CB 1 ATOM 2038 O OG1 . THR B 2 1 N 19.751 6.117 -7.236 1.00 107.30 ? 1 THR A OG1 1 ATOM 2039 C CG2 . THR B 2 1 N 21.696 7.254 -8.157 1.00 108.43 ? 1 THR A CG2 1 ATOM 2040 N N . PHE B 2 2 M 21.792 4.506 -4.801 1.00 82.95 ? 1 PHE A N 1 ATOM 2041 C CA . PHE B 2 2 M 22.291 3.129 -4.769 1.00 84.23 ? 1 PHE A CA 1 ATOM 2042 C C . PHE B 2 2 M 21.345 2.162 -5.486 1.00 78.00 ? 1 PHE A C 1 ATOM 2043 O O . PHE B 2 2 M 21.767 1.424 -6.376 1.00 74.87 ? 1 PHE A O 1 ATOM 2044 C CB . PHE B 2 2 M 22.503 2.673 -3.321 1.00 84.75 ? 1 PHE A CB 1 ATOM 2045 C CG . PHE B 2 2 M 23.068 1.284 -3.198 1.00 96.55 ? 1 PHE A CG 1 ATOM 2046 C CD1 . PHE B 2 2 M 24.421 1.048 -3.409 1.00 103.74 ? 1 PHE A CD1 1 ATOM 2047 C CD2 . PHE B 2 2 M 22.247 0.208 -2.879 1.00 100.62 ? 1 PHE A CD2 1 ATOM 2048 C CE1 . PHE B 2 2 M 24.946 -0.230 -3.300 1.00 105.89 ? 1 PHE A CE1 1 ATOM 2049 C CE2 . PHE B 2 2 M 22.766 -1.073 -2.765 1.00 101.15 ? 1 PHE A CE2 1 ATOM 2050 C CZ . PHE B 2 2 M 24.117 -1.292 -2.975 1.00 105.22 ? 1 PHE A CZ 1 ATOM 2051 N N . PHE B 2 3 L 20.072 2.179 -5.097 1.00 69.81 ? 1 PHE A N 1 ATOM 2052 C CA . PHE B 2 3 L 19.061 1.280 -5.667 1.00 68.79 ? 1 PHE A CA 1 ATOM 2053 C C . PHE B 2 3 L 18.509 1.839 -6.970 1.00 69.01 ? 1 PHE A C 1 ATOM 2054 O O . PHE B 2 3 L 18.459 3.055 -7.158 1.00 66.27 ? 1 PHE A O 1 ATOM 2055 C CB . PHE B 2 3 L 17.894 1.079 -4.699 1.00 65.70 ? 1 PHE A CB 1 ATOM 2056 C CG . PHE B 2 3 L 18.305 0.559 -3.356 1.00 62.40 ? 1 PHE A CG 1 ATOM 2057 C CD1 . PHE B 2 3 L 18.418 -0.802 -3.132 1.00 64.26 ? 1 PHE A CD1 1 ATOM 2058 C CD2 . PHE B 2 3 L 18.586 1.432 -2.320 1.00 59.30 ? 1 PHE A CD2 1 ATOM 2059 C CE1 . PHE B 2 3 L 18.801 -1.283 -1.894 1.00 62.17 ? 1 PHE A CE1 1 ATOM 2060 C CE2 . PHE B 2 3 L 18.975 0.959 -1.079 1.00 56.13 ? 1 PHE A CE2 1 ATOM 2061 C CZ . PHE B 2 3 L 19.082 -0.400 -0.866 1.00 58.60 ? 1 PHE A CZ 1 ATOM 2062 N N . ASN B 2 4 K 18.093 0.941 -7.861 1.00 72.74 ? 1 ASN A N 1 ATOM 2063 C CA . ASN B 2 4 K 17.429 1.319 -9.105 1.00 70.93 ? 1 ASN A CA 1 ATOM 2064 C C . ASN B 2 4 K 15.961 1.645 -8.818 1.00 72.00 ? 1 ASN A C 1 ATOM 2065 O O . ASN B 2 4 K 15.234 0.795 -8.293 1.00 73.48 ? 1 ASN A O 1 ATOM 2066 C CB . ASN B 2 4 K 17.527 0.172 -10.107 1.00 73.07 ? 1 ASN A CB 1 ATOM 2067 C CG . ASN B 2 4 K 16.926 0.515 -11.457 1.00 75.54 ? 1 ASN A CG 1 ATOM 2068 O OD1 . ASN B 2 4 K 16.074 1.394 -11.569 1.00 71.36 ? 1 ASN A OD1 1 ATOM 2069 N ND2 . ASN B 2 4 K 17.366 -0.192 -12.493 1.00 77.67 ? 1 ASN A ND2 1 ATOM 2070 N N . PRO B 2 5 J 15.513 2.873 -9.162 1.00 70.27 ? 1 PRO A N 1 ATOM 2071 C CA . PRO B 2 5 J 14.139 3.261 -8.825 1.00 67.11 ? 1 PRO A CA 1 ATOM 2072 C C . PRO B 2 5 J 13.061 2.567 -9.665 1.00 67.54 ? 1 PRO A C 1 ATOM 2073 O O . PRO B 2 5 J 11.881 2.657 -9.318 1.00 63.96 ? 1 PRO A O 1 ATOM 2074 C CB . PRO B 2 5 J 14.129 4.778 -9.058 1.00 68.65 ? 1 PRO A CB 1 ATOM 2075 C CG . PRO B 2 5 J 15.206 5.024 -10.052 1.00 70.66 ? 1 PRO A CG 1 ATOM 2076 C CD . PRO B 2 5 J 16.242 3.953 -9.856 1.00 71.53 ? 1 PRO A CD 1 ATOM 2077 N N . ARG B 2 6 I 13.461 1.880 -10.740 1.00 67.85 ? 1 ARG A N 1 ATOM 2078 C CA . ARG B 2 6 I 12.542 1.035 -11.513 1.00 71.53 ? 1 ARG A CA 1 ATOM 2079 C C . ARG B 2 6 I 11.979 -0.125 -10.677 1.00 68.94 ? 1 ARG A C 1 ATOM 2080 O O . ARG B 2 6 I 10.874 -0.597 -10.938 1.00 69.61 ? 1 ARG A O 1 ATOM 2081 C CB . ARG B 2 6 I 13.228 0.472 -12.771 1.00 78.03 ? 1 ARG A CB 1 ATOM 2082 C CG . ARG B 2 6 I 13.798 1.526 -13.722 1.00 82.45 ? 1 ARG A CG 1 ATOM 2083 C CD . ARG B 2 6 I 13.710 1.098 -15.183 1.00 90.73 ? 1 ARG A CD 1 ATOM 2084 N NE . ARG B 2 6 I 12.422 1.469 -15.771 1.00 94.76 ? 1 ARG A NE 1 ATOM 2085 C CZ . ARG B 2 6 I 11.915 0.960 -16.892 1.00 101.37 ? 1 ARG A CZ 1 ATOM 2086 N NH1 . ARG B 2 6 I 12.570 0.033 -17.584 1.00 106.80 ? 1 ARG A NH1 1 ATOM 2087 N NH2 . ARG B 2 6 I 10.732 1.381 -17.325 1.00 105.53 ? 1 ARG A NH2 1 ATOM 2088 N N . THR B 2 7 H 12.752 -0.587 -9.694 1.00 66.24 ? 1 THR A N 1 ATOM 2089 C CA . THR B 2 7 H 12.325 -1.644 -8.769 1.00 63.87 ? 1 THR A CA 1 ATOM 2090 C C . THR B 2 7 H 12.181 -1.155 -7.325 1.00 58.85 ? 1 THR A C 1 ATOM 2091 O O . THR B 2 7 H 11.361 -1.675 -6.578 1.00 59.75 ? 1 THR A O 1 ATOM 2092 C CB . THR B 2 7 H 13.327 -2.804 -8.776 1.00 65.24 ? 1 THR A CB 1 ATOM 2093 O OG1 . THR B 2 7 H 14.631 -2.299 -8.470 1.00 64.93 ? 1 THR A OG1 1 ATOM 2094 C CG2 . THR B 2 7 H 13.349 -3.483 -10.134 1.00 69.53 ? 1 THR A CG2 1 ATOM 2095 N N . PHE B 2 8 G 12.995 -0.172 -6.936 1.00 55.70 ? 1 PHE A N 1 ATOM 2096 C CA . PHE B 2 8 G 12.933 0.443 -5.616 1.00 50.28 ? 1 PHE A CA 1 ATOM 2097 C C . PHE B 2 8 G 11.763 1.421 -5.498 1.00 47.89 ? 1 PHE A C 1 ATOM 2098 O O . PHE B 2 8 G 11.252 1.678 -4.400 1.00 41.27 ? 1 PHE A O 1 ATOM 2099 C CB . PHE B 2 8 G 14.250 1.187 -5.363 1.00 51.10 ? 1 PHE A CB 1 ATOM 2100 C CG . PHE B 2 8 G 14.509 1.529 -3.920 1.00 49.08 ? 1 PHE A CG 1 ATOM 2101 C CD1 . PHE B 2 8 G 14.568 0.540 -2.952 1.00 48.88 ? 1 PHE A CD1 1 ATOM 2102 C CD2 . PHE B 2 8 G 14.756 2.842 -3.537 1.00 47.01 ? 1 PHE A CD2 1 ATOM 2103 C CE1 . PHE B 2 8 G 14.835 0.855 -1.619 1.00 46.25 ? 1 PHE A CE1 1 ATOM 2104 C CE2 . PHE B 2 8 G 15.021 3.163 -2.206 1.00 46.89 ? 1 PHE A CE2 1 ATOM 2105 C CZ . PHE B 2 8 G 15.063 2.168 -1.246 1.00 44.37 ? 1 PHE A CZ 1 ATOM 2106 N N . GLY B 2 9 F 11.345 1.973 -6.634 1.00 49.48 ? 1 GLY A N 1 ATOM 2107 C CA . GLY B 2 9 F 10.376 3.057 -6.638 1.00 50.43 ? 1 GLY A CA 1 ATOM 2108 C C . GLY B 2 9 F 11.033 4.386 -6.327 1.00 50.23 ? 1 GLY A C 1 ATOM 2109 O O . GLY B 2 9 F 12.249 4.525 -6.407 1.00 51.97 ? 1 GLY A O 1 ATOM 2110 N N . SER B 2 10 E 10.223 5.378 -5.984 1.00 50.62 ? 1 SER A N 1 ATOM 2111 C CA . SER B 2 10 E 10.724 6.727 -5.795 1.00 51.32 ? 1 SER A CA 1 ATOM 2112 C C . SER B 2 10 E 11.009 6.964 -4.332 1.00 46.99 ? 1 SER A C 1 ATOM 2113 O O . SER B 2 10 E 10.558 6.198 -3.465 1.00 44.88 ? 1 SER A O 1 ATOM 2114 C CB . SER B 2 10 E 9.720 7.760 -6.329 1.00 54.66 ? 1 SER A CB 1 ATOM 2115 O OG . SER B 2 10 E 8.621 7.919 -5.450 1.00 57.61 ? 1 SER A OG 1 ATOM 2116 N N . GLY B 2 11 D 11.766 8.023 -4.062 1.00 45.47 ? 1 GLY A N 1 ATOM 2117 C CA . GLY B 2 11 D 12.006 8.474 -2.691 1.00 44.36 ? 1 GLY A CA 1 ATOM 2118 C C . GLY B 2 11 D 13.438 8.404 -2.185 1.00 46.05 ? 1 GLY A C 1 ATOM 2119 O O . GLY B 2 11 D 13.746 9.011 -1.153 1.00 45.98 ? 1 GLY A O 1 ATOM 2120 N N . GLU B 2 12 C 14.323 7.679 -2.876 1.00 46.65 ? 1 GLU A N 1 ATOM 2121 C CA . GLU B 2 12 C 15.707 7.582 -2.396 1.00 48.97 ? 1 GLU A CA 1 ATOM 2122 C C . GLU B 2 12 C 16.406 8.938 -2.371 1.00 44.51 ? 1 GLU A C 1 ATOM 2123 O O . GLU B 2 12 C 17.026 9.292 -1.366 1.00 38.19 ? 1 GLU A O 1 ATOM 2124 C CB . GLU B 2 12 C 16.559 6.617 -3.221 1.00 55.40 ? 1 GLU A CB 1 ATOM 2125 C CG . GLU B 2 12 C 17.906 6.340 -2.551 1.00 57.72 ? 1 GLU A CG 1 ATOM 2126 C CD . GLU B 2 12 C 18.833 5.429 -3.345 1.00 64.51 ? 1 GLU A CD 1 ATOM 2127 O OE1 . GLU B 2 12 C 18.428 4.881 -4.394 1.00 61.51 ? 1 GLU A OE1 1 ATOM 2128 O OE2 . GLU B 2 12 C 19.993 5.264 -2.903 1.00 68.25 ? 1 GLU A OE2 1 ATOM 2129 N N . ALA B 2 13 B 16.305 9.680 -3.477 1.00 45.12 ? 1 ALA A N 1 ATOM 2130 C CA . ALA B 2 13 B 16.973 10.984 -3.623 1.00 44.35 ? 1 ALA A CA 1 ATOM 2131 C C . ALA B 2 13 B 16.683 11.949 -2.468 1.00 41.47 ? 1 ALA A C 1 ATOM 2132 O O . ALA B 2 13 B 17.537 12.736 -2.093 1.00 39.48 ? 1 ALA A O 1 ATOM 2133 C CB . ALA B 2 13 B 16.602 11.630 -4.961 1.00 44.98 ? 1 ALA A CB 1 ATOM 2134 N N . ASP B 2 14 A 15.485 11.870 -1.899 1.00 39.84 ? 1 ASP A N 1 ATOM 2135 C CA . ASP B 2 14 A 15.059 12.812 -0.883 1.00 38.69 ? 1 ASP A CA 1 ATOM 2136 C C . ASP B 2 14 A 14.937 12.159 0.491 1.00 33.50 ? 1 ASP A C 1 ATOM 2137 O O . ASP B 2 14 A 14.379 12.747 1.426 1.00 30.06 ? 1 ASP A O 1 ATOM 2138 C CB . ASP B 2 14 A 13.719 13.400 -1.309 1.00 42.62 ? 1 ASP A CB 1 ATOM 2139 C CG . ASP B 2 14 A 13.399 14.711 -0.621 1.00 45.61 ? 1 ASP A CG 1 ATOM 2140 O OD1 . ASP B 2 14 A 14.314 15.533 -0.373 1.00 48.05 ? 1 ASP A OD1 1 ATOM 2141 O OD2 . ASP B 2 14 A 12.204 14.931 -0.344 1.00 49.32 ? 1 ASP A OD2 1 ATOM 2142 N N . CYS B 2 15 ? 15.487 10.955 0.616 1.00 31.01 ? 1 CYS A N 1 ATOM 2143 C CA . CYS B 2 15 ? 15.307 10.148 1.812 1.00 30.96 ? 1 CYS A CA 1 ATOM 2144 C C . CYS B 2 15 ? 15.878 10.855 3.009 1.00 26.24 ? 1 CYS A C 1 ATOM 2145 O O . CYS B 2 15 ? 16.814 11.650 2.899 1.00 27.16 ? 1 CYS A O 1 ATOM 2146 C CB . CYS B 2 15 ? 15.982 8.762 1.664 1.00 30.18 ? 1 CYS A CB 1 ATOM 2147 S SG . CYS B 2 15 ? 17.790 8.790 1.496 1.00 33.93 ? 1 CYS A SG 1 ATOM 2148 N N . GLY B 2 16 ? 15.292 10.564 4.162 1.00 26.51 ? 2 GLY A N 1 ATOM 2149 C CA . GLY B 2 16 ? 15.851 10.990 5.429 1.00 25.81 ? 2 GLY A CA 1 ATOM 2150 C C . GLY B 2 16 ? 15.688 12.464 5.768 1.00 24.90 ? 2 GLY A C 1 ATOM 2151 O O . GLY B 2 16 ? 16.191 12.894 6.797 1.00 29.06 ? 2 GLY A O 1 ATOM 2152 N N . LEU B 2 17 ? 14.991 13.230 4.930 1.00 25.19 ? 3 LEU A N 1 ATOM 2153 C CA . LEU B 2 17 ? 14.679 14.653 5.223 1.00 25.89 ? 3 LEU A CA 1 ATOM 2154 C C . LEU B 2 17 ? 13.195 14.841 5.554 1.00 27.92 ? 3 LEU A C 1 ATOM 2155 O O . LEU B 2 17 ? 12.322 14.670 4.695 1.00 30.73 ? 3 LEU A O 1 ATOM 2156 C CB . LEU B 2 17 ? 15.053 15.527 4.028 1.00 29.65 ? 3 LEU A CB 1 ATOM 2157 C CG . LEU B 2 17 ? 16.523 15.430 3.623 1.00 32.09 ? 3 LEU A CG 1 ATOM 2158 C CD1 . LEU B 2 17 ? 16.745 16.070 2.258 1.00 35.43 ? 3 LEU A CD1 1 ATOM 2159 C CD2 . LEU B 2 17 ? 17.419 16.062 4.673 1.00 34.98 ? 3 LEU A CD2 1 ATOM 2160 N N . ARG B 2 18 ? 12.900 15.212 6.794 1.00 24.76 ? 4 ARG A N 1 ATOM 2161 C CA . ARG B 2 18 ? 11.524 15.235 7.252 1.00 25.67 ? 4 ARG A CA 1 ATOM 2162 C C . ARG B 2 18 ? 10.804 16.506 6.842 1.00 27.61 ? 4 ARG A C 1 ATOM 2163 O O . ARG B 2 18 ? 11.332 17.608 7.010 1.00 26.08 ? 4 ARG A O 1 ATOM 2164 C CB . ARG B 2 18 ? 11.460 15.070 8.764 1.00 27.38 ? 4 ARG A CB 1 ATOM 2165 C CG . ARG B 2 18 ? 12.009 13.769 9.264 1.00 25.47 ? 4 ARG A CG 1 ATOM 2166 C CD . ARG B 2 18 ? 12.104 13.804 10.781 1.00 27.75 ? 4 ARG A CD 1 ATOM 2167 N NE . ARG B 2 18 ? 13.078 14.805 11.229 1.00 26.14 ? 4 ARG A NE 1 ATOM 2168 C CZ . ARG B 2 18 ? 13.360 15.075 12.507 1.00 27.81 ? 4 ARG A CZ 1 ATOM 2169 N NH1 . ARG B 2 18 ? 12.735 14.442 13.487 1.00 25.18 ? 4 ARG A NH1 1 ATOM 2170 N NH2 . ARG B 2 18 ? 14.258 16.009 12.807 1.00 29.43 ? 4 ARG A NH2 1 ATOM 2171 N N . PRO B 2 19 ? 9.580 16.366 6.293 1.00 28.56 ? 5 PRO A N 1 ATOM 2172 C CA . PRO B 2 19 ? 8.845 17.540 5.881 1.00 31.79 ? 5 PRO A CA 1 ATOM 2173 C C . PRO B 2 19 ? 8.628 18.568 6.994 1.00 30.79 ? 5 PRO A C 1 ATOM 2174 O O . PRO B 2 19 ? 8.755 19.754 6.747 1.00 30.89 ? 5 PRO A O 1 ATOM 2175 C CB . PRO B 2 19 ? 7.524 16.956 5.371 1.00 33.44 ? 5 PRO A CB 1 ATOM 2176 C CG . PRO B 2 19 ? 7.924 15.635 4.802 1.00 32.68 ? 5 PRO A CG 1 ATOM 2177 C CD . PRO B 2 19 ? 8.961 15.131 5.771 1.00 31.99 ? 5 PRO A CD 1 ATOM 2178 N N . LEU B 2 20 ? 8.332 18.119 8.205 1.00 30.12 ? 6 LEU A N 1 ATOM 2179 C CA . LEU B 2 20 ? 8.013 19.042 9.292 1.00 31.14 ? 6 LEU A CA 1 ATOM 2180 C C . LEU B 2 20 ? 9.240 19.545 10.083 1.00 28.20 ? 6 LEU A C 1 ATOM 2181 O O . LEU B 2 20 ? 9.114 20.421 10.949 1.00 27.14 ? 6 LEU A O 1 ATOM 2182 C CB . LEU B 2 20 ? 6.965 18.402 10.217 1.00 30.79 ? 6 LEU A CB 1 ATOM 2183 C CG . LEU B 2 20 ? 5.601 18.202 9.538 1.00 34.80 ? 6 LEU A CG 1 ATOM 2184 C CD1 . LEU B 2 20 ? 4.590 17.506 10.453 1.00 36.55 ? 6 LEU A CD1 1 ATOM 2185 C CD2 . LEU B 2 20 ? 5.029 19.531 9.056 1.00 39.07 ? 6 LEU A CD2 1 ATOM 2186 N N . PHE B 2 21 ? 10.419 19.019 9.773 1.00 28.20 ? 7 PHE A N 1 ATOM 2187 C CA . PHE B 2 21 ? 11.635 19.382 10.489 1.00 25.97 ? 7 PHE A CA 1 ATOM 2188 C C . PHE B 2 21 ? 12.715 19.880 9.523 1.00 25.52 ? 7 PHE A C 1 ATOM 2189 O O . PHE B 2 21 ? 12.757 21.093 9.233 1.00 25.60 ? 7 PHE A O 1 ATOM 2190 C CB . PHE B 2 21 ? 12.061 18.256 11.461 1.00 24.13 ? 7 PHE A CB 1 ATOM 2191 C CG . PHE B 2 21 ? 11.071 18.071 12.585 1.00 27.93 ? 7 PHE A CG 1 ATOM 2192 C CD1 . PHE B 2 21 ? 11.043 18.970 13.647 1.00 25.50 ? 7 PHE A CD1 1 ATOM 2193 C CD2 . PHE B 2 21 ? 10.084 17.089 12.517 1.00 26.60 ? 7 PHE A CD2 1 ATOM 2194 C CE1 . PHE B 2 21 ? 10.084 18.858 14.646 1.00 27.77 ? 7 PHE A CE1 1 ATOM 2195 C CE2 . PHE B 2 21 ? 9.141 16.965 13.524 1.00 28.44 ? 7 PHE A CE2 1 ATOM 2196 C CZ . PHE B 2 21 ? 9.138 17.847 14.587 1.00 27.99 ? 7 PHE A CZ 1 ATOM 2197 N N . GLU B 2 22 ? 13.558 19.002 8.996 1.00 27.30 ? 8 GLU A N 1 ATOM 2198 C CA . GLU B 2 22 ? 14.668 19.473 8.134 1.00 30.36 ? 8 GLU A CA 1 ATOM 2199 C C . GLU B 2 22 ? 14.149 20.392 7.058 1.00 31.68 ? 8 GLU A C 1 ATOM 2200 O O . GLU B 2 22 ? 14.732 21.448 6.792 1.00 33.31 ? 8 GLU A O 1 ATOM 2201 C CB . GLU B 2 22 ? 15.456 18.309 7.512 1.00 30.89 ? 8 GLU A CB 1 ATOM 2202 C CG . GLU B 2 22 ? 16.330 17.559 8.507 1.00 30.65 ? 8 GLU A CG 1 ATOM 2203 C CD . GLU B 2 22 ? 15.548 16.615 9.424 1.00 29.69 ? 8 GLU A CD 1 ATOM 2204 O OE1 . GLU B 2 22 ? 14.405 16.231 9.087 1.00 29.06 ? 8 GLU A OE1 1 ATOM 2205 O OE2 . GLU B 2 22 ? 16.065 16.282 10.512 1.00 29.19 ? 8 GLU A OE2 1 ATOM 2206 N N . LYS B 2 23 ? 13.022 20.011 6.451 1.00 32.85 ? 9 LYS A N 1 ATOM 2207 C CA . LYS B 2 23 ? 12.507 20.746 5.303 1.00 33.80 ? 9 LYS A CA 1 ATOM 2208 C C . LYS B 2 23 ? 11.961 22.123 5.699 1.00 34.16 ? 9 LYS A C 1 ATOM 2209 O O . LYS B 2 23 ? 11.867 23.000 4.872 1.00 35.84 ? 9 LYS A O 1 ATOM 2210 C CB . LYS B 2 23 ? 11.423 19.936 4.599 1.00 36.07 ? 9 LYS A CB 1 ATOM 2211 C CG . LYS B 2 23 ? 11.943 18.675 3.921 1.00 41.92 ? 9 LYS A CG 1 ATOM 2212 C CD . LYS B 2 23 ? 12.660 19.026 2.621 1.00 50.43 ? 9 LYS A CD 1 ATOM 2213 C CE . LYS B 2 23 ? 12.990 17.801 1.782 1.00 56.17 ? 9 LYS A CE 1 ATOM 2214 N NZ . LYS B 2 23 ? 11.803 16.918 1.602 1.00 62.68 ? 9 LYS A NZ 1 ATOM 2215 N N . LYS B 2 24 ? 11.593 22.292 6.963 1.00 37.62 ? 10 LYS A N 1 ATOM 2216 C CA . LYS B 2 24 ? 11.136 23.596 7.475 1.00 38.88 ? 10 LYS A CA 1 ATOM 2217 C C . LYS B 2 24 ? 12.231 24.316 8.273 1.00 36.20 ? 10 LYS A C 1 ATOM 2218 O O . LYS B 2 24 ? 11.960 25.324 8.910 1.00 34.59 ? 10 LYS A O 1 ATOM 2219 C CB . LYS B 2 24 ? 9.895 23.395 8.363 1.00 39.61 ? 10 LYS A CB 1 ATOM 2220 C CG . LYS B 2 24 ? 8.645 23.027 7.587 1.00 44.66 ? 10 LYS A CG 1 ATOM 2221 C CD . LYS B 2 24 ? 7.451 22.786 8.498 1.00 42.81 ? 10 LYS A CD 1 ATOM 2222 C CE . LYS B 2 24 ? 6.953 24.094 9.082 1.00 48.85 ? 10 LYS A CE 1 ATOM 2223 N NZ . LYS B 2 24 ? 5.581 23.961 9.637 1.00 52.13 ? 10 LYS A NZ 1 ATOM 2224 N N . SER B 2 25 ? 13.457 23.795 8.232 1.00 33.94 ? 11 SER A N 1 ATOM 2225 C CA . SER B 2 25 ? 14.557 24.276 9.048 1.00 34.22 ? 11 SER A CA 1 ATOM 2226 C C . SER B 2 25 ? 14.153 24.383 10.515 1.00 34.57 ? 11 SER A C 1 ATOM 2227 O O . SER B 2 25 ? 14.401 25.387 11.167 1.00 34.72 ? 11 SER A O 1 ATOM 2228 C CB . SER B 2 25 ? 15.064 25.619 8.529 1.00 38.60 ? 11 SER A CB 1 ATOM 2229 O OG . SER B 2 25 ? 15.505 25.468 7.203 1.00 40.74 ? 11 SER A OG 1 ATOM 2230 N N . LEU B 2 26 ? 13.505 23.343 11.011 1.00 30.29 ? 12 LEU A N 1 ATOM 2231 C CA . LEU B 2 26 ? 13.109 23.265 12.413 1.00 30.47 ? 12 LEU A CA 1 ATOM 2232 C C . LEU B 2 26 ? 13.794 22.067 13.003 1.00 29.97 ? 12 LEU A C 1 ATOM 2233 O O . LEU B 2 26 ? 13.884 21.012 12.357 1.00 29.99 ? 12 LEU A O 1 ATOM 2234 C CB . LEU B 2 26 ? 11.594 23.114 12.557 1.00 30.02 ? 12 LEU A CB 1 ATOM 2235 C CG . LEU B 2 26 ? 10.719 24.307 12.251 1.00 37.91 ? 12 LEU A CG 1 ATOM 2236 C CD1 . LEU B 2 26 ? 9.250 23.891 12.290 1.00 39.49 ? 12 LEU A CD1 1 ATOM 2237 C CD2 . LEU B 2 26 ? 10.999 25.448 13.231 1.00 40.61 ? 12 LEU A CD2 1 ATOM 2238 N N . GLU B 2 27 ? 14.280 22.239 14.228 1.00 31.22 ? 13 GLU A N 1 ATOM 2239 C CA . GLU B 2 27 ? 14.936 21.184 14.978 1.00 29.47 ? 13 GLU A CA 1 ATOM 2240 C C . GLU B 2 27 ? 13.895 20.494 15.858 1.00 28.23 ? 13 GLU A C 1 ATOM 2241 O O . GLU B 2 27 ? 13.022 21.161 16.422 1.00 28.62 ? 13 GLU A O 1 ATOM 2242 C CB . GLU B 2 27 ? 16.040 21.826 15.835 1.00 32.90 ? 13 GLU A CB 1 ATOM 2243 C CG . GLU B 2 27 ? 16.834 20.870 16.721 1.00 36.51 ? 13 GLU A CG 1 ATOM 2244 C CD . GLU B 2 27 ? 17.816 21.578 17.661 1.00 38.63 ? 13 GLU A CD 1 ATOM 2245 O OE1 . GLU B 2 27 ? 18.124 22.773 17.450 1.00 44.24 ? 13 GLU A OE1 1 ATOM 2246 O OE2 . GLU B 2 27 ? 18.301 20.935 18.614 1.00 37.69 ? 13 GLU A OE2 1 ATOM 2247 N N . ASP B 2 28 ? 13.967 19.171 15.988 1.00 29.22 ? 14 ASP A N 1 ATOM 2248 C CA . ASP B 2 28 ? 13.036 18.485 16.875 1.00 27.69 ? 14 ASP A CA 1 ATOM 2249 C C . ASP B 2 28 ? 13.567 18.551 18.304 1.00 31.32 ? 14 ASP A C 1 ATOM 2250 O O . ASP B 2 28 ? 14.694 18.976 18.537 1.00 30.68 ? 14 ASP A O 1 ATOM 2251 C CB . ASP B 2 28 ? 12.703 17.054 16.387 1.00 27.25 ? 14 ASP A CB 1 ATOM 2252 C CG . ASP B 2 28 ? 13.769 16.011 16.695 1.00 24.79 ? 14 ASP A CG 1 ATOM 2253 O OD1 . ASP B 2 28 ? 14.335 15.973 17.805 1.00 26.30 ? 14 ASP A OD1 1 ATOM 2254 O OD2 . ASP B 2 28 ? 13.998 15.150 15.817 1.00 26.13 ? 14 ASP A OD2 1 ATOM 2255 N N . LYS B 2 29 A 12.734 18.155 19.253 1.00 28.53 ? 14 LYS A N 1 ATOM 2256 C CA . LYS B 2 29 A 13.016 18.379 20.658 1.00 28.57 ? 14 LYS A CA 1 ATOM 2257 C C . LYS B 2 29 A 14.226 17.642 21.259 1.00 29.61 ? 14 LYS A C 1 ATOM 2258 O O . LYS B 2 29 A 14.676 18.021 22.345 1.00 30.08 ? 14 LYS A O 1 ATOM 2259 C CB . LYS B 2 29 A 11.750 18.130 21.504 1.00 31.57 ? 14 LYS A CB 1 ATOM 2260 C CG . LYS B 2 29 A 11.164 16.732 21.378 1.00 31.51 ? 14 LYS A CG 1 ATOM 2261 C CD . LYS B 2 29 A 9.990 16.523 22.309 1.00 33.76 ? 14 LYS A CD 1 ATOM 2262 C CE . LYS B 2 29 A 9.476 15.085 22.235 1.00 35.45 ? 14 LYS A CE 1 ATOM 2263 N NZ . LYS B 2 29 A 8.309 14.888 23.150 1.00 37.34 ? 14 LYS A NZ 1 ATOM 2264 N N . THR B 2 30 B 14.751 16.601 20.608 1.00 28.07 ? 14 THR A N 1 ATOM 2265 C CA . THR B 2 30 B 15.869 15.840 21.202 1.00 29.57 ? 14 THR A CA 1 ATOM 2266 C C . THR B 2 30 B 17.022 15.495 20.268 1.00 27.41 ? 14 THR A C 1 ATOM 2267 O O . THR B 2 30 B 17.965 14.829 20.686 1.00 27.43 ? 14 THR A O 1 ATOM 2268 C CB . THR B 2 30 B 15.386 14.510 21.844 1.00 29.47 ? 14 THR A CB 1 ATOM 2269 O OG1 . THR B 2 30 B 14.963 13.598 20.826 1.00 31.52 ? 14 THR A OG1 1 ATOM 2270 C CG2 . THR B 2 30 B 14.233 14.749 22.810 1.00 34.15 ? 14 THR A CG2 1 ATOM 2271 N N . GLU B 2 31 C 16.958 15.916 19.017 1.00 27.25 ? 14 GLU A N 1 ATOM 2272 C CA . GLU B 2 31 C 17.949 15.485 18.056 1.00 25.73 ? 14 GLU A CA 1 ATOM 2273 C C . GLU B 2 31 C 19.326 16.070 18.318 1.00 25.76 ? 14 GLU A C 1 ATOM 2274 O O . GLU B 2 31 C 20.297 15.543 17.839 1.00 24.56 ? 14 GLU A O 1 ATOM 2275 C CB . GLU B 2 31 C 17.494 15.801 16.625 1.00 27.62 ? 14 GLU A CB 1 ATOM 2276 C CG . GLU B 2 31 C 17.269 17.281 16.314 1.00 30.78 ? 14 GLU A CG 1 ATOM 2277 C CD . GLU B 2 31 C 17.093 17.531 14.826 1.00 34.28 ? 14 GLU A CD 1 ATOM 2278 O OE1 . GLU B 2 31 C 18.085 17.407 14.068 1.00 37.01 ? 14 GLU A OE1 1 ATOM 2279 O OE2 . GLU B 2 31 C 15.976 17.872 14.417 1.00 31.80 ? 14 GLU A OE2 1 ATOM 2280 N N . ARG B 2 32 D 19.396 17.171 19.058 1.00 30.56 ? 14 ARG A N 1 ATOM 2281 C CA . ARG B 2 32 D 20.665 17.741 19.526 1.00 30.22 ? 14 ARG A CA 1 ATOM 2282 C C . ARG B 2 32 D 21.444 16.768 20.406 1.00 31.28 ? 14 ARG A C 1 ATOM 2283 O O . ARG B 2 32 D 22.657 16.850 20.491 1.00 30.43 ? 14 ARG A O 1 ATOM 2284 C CB . ARG B 2 32 D 20.411 19.030 20.313 1.00 34.51 ? 14 ARG A CB 1 ATOM 2285 C CG . ARG B 2 32 D 21.645 19.903 20.473 1.00 33.61 ? 14 ARG A CG 1 ATOM 2286 C CD . ARG B 2 32 D 21.341 21.204 21.179 1.00 36.70 ? 14 ARG A CD 1 ATOM 2287 N NE . ARG B 2 32 D 20.412 22.027 20.421 1.00 34.13 ? 14 ARG A NE 1 ATOM 2288 C CZ . ARG B 2 32 D 20.116 23.285 20.736 1.00 38.04 ? 14 ARG A CZ 1 ATOM 2289 N NH1 . ARG B 2 32 D 20.671 23.872 21.798 1.00 38.26 ? 14 ARG A NH1 1 ATOM 2290 N NH2 . ARG B 2 32 D 19.259 23.959 19.986 1.00 36.00 ? 14 ARG A NH2 1 ATOM 2291 N N . GLU B 2 33 E 20.732 15.871 21.091 1.00 30.18 ? 14 GLU A N 1 ATOM 2292 C CA . GLU B 2 33 E 21.359 14.824 21.889 1.00 29.29 ? 14 GLU A CA 1 ATOM 2293 C C . GLU B 2 33 E 22.226 13.935 21.005 1.00 27.93 ? 14 GLU A C 1 ATOM 2294 O O . GLU B 2 33 E 23.339 13.543 21.370 1.00 29.25 ? 14 GLU A O 1 ATOM 2295 C CB . GLU B 2 33 E 20.285 13.948 22.558 1.00 29.09 ? 14 GLU A CB 1 ATOM 2296 C CG . GLU B 2 33 E 20.807 13.145 23.717 1.00 33.02 ? 14 GLU A CG 1 ATOM 2297 C CD . GLU B 2 33 E 19.722 12.392 24.463 1.00 32.82 ? 14 GLU A CD 1 ATOM 2298 O OE1 . GLU B 2 33 E 18.568 12.351 23.996 1.00 32.37 ? 14 GLU A OE1 1 ATOM 2299 O OE2 . GLU B 2 33 E 20.032 11.846 25.523 1.00 38.33 ? 14 GLU A OE2 1 ATOM 2300 N N . LEU B 2 34 F 21.698 13.638 19.830 1.00 27.03 ? 14 LEU A N 1 ATOM 2301 C CA . LEU B 2 34 F 22.376 12.790 18.880 1.00 28.58 ? 14 LEU A CA 1 ATOM 2302 C C . LEU B 2 34 F 23.612 13.497 18.360 1.00 29.97 ? 14 LEU A C 1 ATOM 2303 O O . LEU B 2 34 F 24.707 12.933 18.351 1.00 34.01 ? 14 LEU A O 1 ATOM 2304 C CB . LEU B 2 34 F 21.439 12.439 17.718 1.00 28.36 ? 14 LEU A CB 1 ATOM 2305 C CG . LEU B 2 34 F 20.096 11.799 18.103 1.00 29.74 ? 14 LEU A CG 1 ATOM 2306 C CD1 . LEU B 2 34 F 19.392 11.310 16.854 1.00 29.45 ? 14 LEU A CD1 1 ATOM 2307 C CD2 . LEU B 2 34 F 20.237 10.673 19.104 1.00 30.37 ? 14 LEU A CD2 1 ATOM 2308 N N . LEU B 2 35 G 23.435 14.749 17.958 1.00 32.04 ? 14 LEU A N 1 ATOM 2309 C CA . LEU B 2 35 G 24.548 15.553 17.432 1.00 34.13 ? 14 LEU A CA 1 ATOM 2310 C C . LEU B 2 35 G 25.642 15.738 18.471 1.00 32.65 ? 14 LEU A C 1 ATOM 2311 O O . LEU B 2 35 G 26.836 15.623 18.160 1.00 32.63 ? 14 LEU A O 1 ATOM 2312 C CB . LEU B 2 35 G 24.032 16.901 16.943 1.00 38.72 ? 14 LEU A CB 1 ATOM 2313 C CG . LEU B 2 35 G 23.107 16.741 15.732 1.00 43.82 ? 14 LEU A CG 1 ATOM 2314 C CD1 . LEU B 2 35 G 22.520 18.081 15.309 1.00 49.84 ? 14 LEU A CD1 1 ATOM 2315 C CD2 . LEU B 2 35 G 23.821 16.044 14.569 1.00 47.86 ? 14 LEU A CD2 1 ATOM 2316 N N . GLU B 2 36 H 25.240 15.977 19.716 1.00 30.63 ? 14 GLU A N 1 ATOM 2317 C CA . GLU B 2 36 H 26.219 16.157 20.789 1.00 32.84 ? 14 GLU A CA 1 ATOM 2318 C C . GLU B 2 36 H 27.006 14.899 21.127 1.00 31.85 ? 14 GLU A C 1 ATOM 2319 O O . GLU B 2 36 H 28.152 15.004 21.543 1.00 33.05 ? 14 GLU A O 1 ATOM 2320 C CB . GLU B 2 36 H 25.587 16.779 22.034 1.00 35.69 ? 14 GLU A CB 1 ATOM 2321 C CG . GLU B 2 36 H 25.378 18.270 21.836 1.00 40.85 ? 14 GLU A CG 1 ATOM 2322 C CD . GLU B 2 36 H 24.567 18.949 22.924 1.00 48.27 ? 14 GLU A CD 1 ATOM 2323 O OE1 . GLU B 2 36 H 24.392 20.186 22.814 1.00 51.95 ? 14 GLU A OE1 1 ATOM 2324 O OE2 . GLU B 2 36 H 24.107 18.269 23.870 1.00 47.53 ? 14 GLU A OE2 1 ATOM 2325 N N . SER B 2 37 I 26.411 13.723 20.902 1.00 29.84 ? 14 SER A N 1 ATOM 2326 C CA . SER B 2 37 I 27.096 12.456 21.115 1.00 29.70 ? 14 SER A CA 1 ATOM 2327 C C . SER B 2 37 I 28.307 12.270 20.194 1.00 32.32 ? 14 SER A C 1 ATOM 2328 O O . SER B 2 37 I 29.215 11.551 20.540 1.00 37.49 ? 14 SER A O 1 ATOM 2329 C CB . SER B 2 37 I 26.122 11.272 21.004 1.00 27.60 ? 14 SER A CB 1 ATOM 2330 O OG . SER B 2 37 I 25.743 10.977 19.665 1.00 26.06 ? 14 SER A OG 1 ATOM 2331 N N . TYR B 2 38 J 28.330 12.941 19.050 1.00 33.58 ? 14 TYR A N 1 ATOM 2332 C CA . TYR B 2 38 J 29.479 12.887 18.141 1.00 40.25 ? 14 TYR A CA 1 ATOM 2333 C C . TYR B 2 38 J 30.668 13.712 18.603 1.00 45.85 ? 14 TYR A C 1 ATOM 2334 O O . TYR B 2 38 J 31.815 13.403 18.273 1.00 47.22 ? 14 TYR A O 1 ATOM 2335 C CB . TYR B 2 38 J 29.084 13.361 16.750 1.00 41.20 ? 14 TYR A CB 1 ATOM 2336 C CG . TYR B 2 38 J 27.952 12.596 16.121 1.00 38.24 ? 14 TYR A CG 1 ATOM 2337 C CD1 . TYR B 2 38 J 27.885 11.204 16.183 1.00 39.61 ? 14 TYR A CD1 1 ATOM 2338 C CD2 . TYR B 2 38 J 26.964 13.262 15.424 1.00 37.63 ? 14 TYR A CD2 1 ATOM 2339 C CE1 . TYR B 2 38 J 26.843 10.512 15.581 1.00 41.22 ? 14 TYR A CE1 1 ATOM 2340 C CE2 . TYR B 2 38 J 25.933 12.587 14.810 1.00 38.24 ? 14 TYR A CE2 1 ATOM 2341 C CZ . TYR B 2 38 J 25.866 11.216 14.889 1.00 38.25 ? 14 TYR A CZ 1 ATOM 2342 O OH . TYR B 2 38 J 24.818 10.589 14.264 1.00 38.29 ? 14 TYR A OH 1 ATOM 2343 N N . ILE B 2 39 K 30.408 14.762 19.369 1.00 53.52 ? 14 ILE A N 1 ATOM 2344 C CA . ILE B 2 39 K 31.496 15.580 19.924 1.00 64.15 ? 14 ILE A CA 1 ATOM 2345 C C . ILE B 2 39 K 32.219 14.770 21.002 1.00 72.35 ? 14 ILE A C 1 ATOM 2346 O O . ILE B 2 39 K 33.435 14.878 21.172 1.00 75.37 ? 14 ILE A O 1 ATOM 2347 C CB . ILE B 2 39 K 30.968 16.910 20.499 1.00 66.14 ? 14 ILE A CB 1 ATOM 2348 C CG1 . ILE B 2 39 K 30.267 17.718 19.403 1.00 66.11 ? 14 ILE A CG1 1 ATOM 2349 C CG2 . ILE B 2 39 K 32.101 17.733 21.102 1.00 68.28 ? 14 ILE A CG2 1 ATOM 2350 C CD1 . ILE B 2 39 K 29.267 18.718 19.940 1.00 68.78 ? 14 ILE A CD1 1 ATOM 2351 N N . ASP B 2 40 L 31.455 13.937 21.702 1.00 89.57 ? 14 ASP A N 1 ATOM 2352 C CA . ASP B 2 40 L 31.991 13.029 22.711 1.00 107.17 ? 14 ASP A CA 1 ATOM 2353 C C . ASP B 2 40 L 32.639 11.815 22.043 1.00 105.89 ? 14 ASP A C 1 ATOM 2354 O O . ASP B 2 40 L 33.818 11.845 21.683 1.00 104.32 ? 14 ASP A O 1 ATOM 2355 C CB . ASP B 2 40 L 30.872 12.569 23.661 1.00 112.64 ? 14 ASP A CB 1 ATOM 2356 C CG . ASP B 2 40 L 30.098 13.735 24.275 1.00 112.25 ? 14 ASP A CG 1 ATOM 2357 O OD1 . ASP B 2 40 L 30.666 14.843 24.389 1.00 110.56 ? 14 ASP A OD1 1 ATOM 2358 O OD2 . ASP B 2 40 L 28.917 13.541 24.641 1.00 108.50 ? 14 ASP A OD2 1 HETATM 2359 N N . 0G6 C 3 . ? 13.454 -11.988 25.338 1.00 34.76 ? 301 0G6 B N 1 HETATM 2360 C CA . 0G6 C 3 . ? 13.816 -12.774 24.204 1.00 33.06 ? 301 0G6 B CA 1 HETATM 2361 C C . 0G6 C 3 . ? 13.528 -11.903 23.008 1.00 30.45 ? 301 0G6 B C 1 HETATM 2362 O O . 0G6 C 3 . ? 13.939 -10.712 22.885 1.00 30.04 ? 301 0G6 B O 1 HETATM 2363 C CB . 0G6 C 3 . ? 15.290 -13.158 24.219 1.00 33.05 ? 301 0G6 B CB 1 HETATM 2364 C CG . 0G6 C 3 . ? 15.728 -14.040 22.972 1.00 38.31 ? 301 0G6 B CG 1 HETATM 2365 C CD1 . 0G6 C 3 . ? 15.264 -15.335 22.809 1.00 45.95 ? 301 0G6 B CD1 1 HETATM 2366 C CD2 . 0G6 C 3 . ? 16.608 -13.517 22.014 1.00 36.45 ? 301 0G6 B CD2 1 HETATM 2367 C CE1 . 0G6 C 3 . ? 15.670 -16.093 21.687 1.00 49.44 ? 301 0G6 B CE1 1 HETATM 2368 C CE2 . 0G6 C 3 . ? 17.011 -14.268 20.908 1.00 37.69 ? 301 0G6 B CE2 1 HETATM 2369 C CZ . 0G6 C 3 . ? 16.548 -15.554 20.746 1.00 41.64 ? 301 0G6 B CZ 1 HETATM 2370 N N1 . 0G6 C 3 . ? 12.732 -12.447 21.941 1.00 31.16 ? 301 0G6 B N1 1 HETATM 2371 C CA1 . 0G6 C 3 . ? 12.423 -11.624 20.718 1.00 31.52 ? 301 0G6 B CA1 1 HETATM 2372 C C1 . 0G6 C 3 . ? 11.504 -10.468 21.097 1.00 30.47 ? 301 0G6 B C1 1 HETATM 2373 O O1 . 0G6 C 3 . ? 10.634 -10.568 21.967 1.00 32.36 ? 301 0G6 B O1 1 HETATM 2374 C CB1 . 0G6 C 3 . ? 11.790 -12.510 19.861 1.00 33.85 ? 301 0G6 B CB1 1 HETATM 2375 C CG1 . 0G6 C 3 . ? 11.921 -13.986 20.461 1.00 32.31 ? 301 0G6 B CG1 1 HETATM 2376 C CD . 0G6 C 3 . ? 12.083 -13.834 21.792 1.00 33.73 ? 301 0G6 B CD 1 HETATM 2377 N N2 . 0G6 C 3 . ? 11.655 -9.279 20.320 1.00 29.57 ? 301 0G6 B N2 1 HETATM 2378 C CA2 . 0G6 C 3 . ? 10.788 -8.129 20.498 1.00 27.70 ? 301 0G6 B CA2 1 HETATM 2379 C C2 . 0G6 C 3 . ? 9.920 -8.019 19.281 1.00 28.82 ? 301 0G6 B C2 1 HETATM 2380 O O2 . 0G6 C 3 . ? 8.700 -7.319 19.606 1.00 29.58 ? 301 0G6 B O2 1 HETATM 2381 C CB2 . 0G6 C 3 . ? 11.683 -6.922 20.741 1.00 27.20 ? 301 0G6 B CB2 1 HETATM 2382 C CG2 . 0G6 C 3 . ? 12.171 -6.981 22.200 1.00 29.03 ? 301 0G6 B CG2 1 HETATM 2383 C CD3 . 0G6 C 3 . ? 13.204 -5.876 22.389 1.00 31.67 ? 301 0G6 B CD3 1 HETATM 2384 N NE . 0G6 C 3 . ? 13.550 -5.876 23.782 1.00 31.49 ? 301 0G6 B NE 1 HETATM 2385 C CZ1 . 0G6 C 3 . ? 14.508 -4.931 24.317 1.00 27.87 ? 301 0G6 B CZ1 1 HETATM 2386 N NH1 . 0G6 C 3 . ? 15.175 -3.973 23.422 1.00 28.68 ? 301 0G6 B NH1 1 HETATM 2387 N NH2 . 0G6 C 3 . ? 14.807 -4.987 25.636 1.00 29.55 ? 301 0G6 B NH2 1 HETATM 2388 C C3 . 0G6 C 3 . ? 9.523 -9.393 18.644 1.00 29.50 ? 301 0G6 B C3 1 HETATM 2389 O O1 . MES D 4 . ? 29.675 -11.541 1.886 1.00 134.91 ? 302 MES B O1 1 HETATM 2390 C C2 . MES D 4 . ? 28.722 -11.010 0.962 1.00 134.41 ? 302 MES B C2 1 HETATM 2391 C C3 . MES D 4 . ? 27.321 -10.908 1.555 1.00 131.80 ? 302 MES B C3 1 HETATM 2392 N N4 . MES D 4 . ? 27.325 -11.517 2.836 1.00 131.36 ? 302 MES B N4 1 HETATM 2393 C C5 . MES D 4 . ? 28.235 -11.013 3.802 1.00 129.13 ? 302 MES B C5 1 HETATM 2394 C C6 . MES D 4 . ? 29.632 -10.945 3.188 1.00 130.03 ? 302 MES B C6 1 HETATM 2395 C C7 . MES D 4 . ? 26.534 -12.715 3.162 1.00 126.99 ? 302 MES B C7 1 HETATM 2396 C C8 . MES D 4 . ? 25.167 -12.808 2.441 1.00 120.09 ? 302 MES B C8 1 HETATM 2397 S S . MES D 4 . ? 24.086 -11.379 2.707 1.00 114.35 ? 302 MES B S 1 HETATM 2398 O O1S . MES D 4 . ? 24.799 -10.074 3.044 1.00 95.19 ? 302 MES B O1S 1 HETATM 2399 O O2S . MES D 4 . ? 23.238 -11.545 3.945 1.00 81.00 ? 302 MES B O2S 1 HETATM 2400 O O3S . MES D 4 . ? 23.221 -11.213 1.479 1.00 117.62 ? 302 MES B O3S 1 HETATM 2401 C C1 . GOL E 5 . ? 18.555 21.279 10.461 1.00 67.18 ? 303 GOL B C1 1 HETATM 2402 O O1 . GOL E 5 . ? 17.835 20.052 10.651 1.00 47.45 ? 303 GOL B O1 1 HETATM 2403 C C2 . GOL E 5 . ? 18.305 22.225 11.630 1.00 68.17 ? 303 GOL B C2 1 HETATM 2404 O O2 . GOL E 5 . ? 17.079 22.929 11.405 1.00 70.71 ? 303 GOL B O2 1 HETATM 2405 C C3 . GOL E 5 . ? 18.228 21.457 12.949 1.00 63.28 ? 303 GOL B C3 1 HETATM 2406 O O3 . GOL E 5 . ? 19.224 20.428 12.976 1.00 66.84 ? 303 GOL B O3 1 HETATM 2407 C C1 . GOL F 5 . ? 28.526 -2.067 17.048 1.00 62.59 ? 304 GOL B C1 1 HETATM 2408 O O1 . GOL F 5 . ? 28.937 -3.265 17.716 1.00 56.17 ? 304 GOL B O1 1 HETATM 2409 C C2 . GOL F 5 . ? 29.705 -1.117 16.974 1.00 67.31 ? 304 GOL B C2 1 HETATM 2410 O O2 . GOL F 5 . ? 30.144 -0.769 18.295 1.00 65.51 ? 304 GOL B O2 1 HETATM 2411 C C3 . GOL F 5 . ? 30.834 -1.796 16.211 1.00 66.30 ? 304 GOL B C3 1 HETATM 2412 O O3 . GOL F 5 . ? 31.672 -0.785 15.646 1.00 68.77 ? 304 GOL B O3 1 HETATM 2413 NA NA . NA G 6 . ? 19.832 -1.465 30.396 1.00 32.38 ? 305 NA B NA 1 HETATM 2414 C C1 . NAG H 7 . ? 5.635 -21.193 7.270 1.00 87.15 ? 306 NAG B C1 1 HETATM 2415 C C2 . NAG H 7 . ? 6.420 -22.505 7.464 1.00 90.27 ? 306 NAG B C2 1 HETATM 2416 C C3 . NAG H 7 . ? 6.683 -23.361 6.218 1.00 91.69 ? 306 NAG B C3 1 HETATM 2417 C C4 . NAG H 7 . ? 5.658 -23.118 5.126 1.00 96.27 ? 306 NAG B C4 1 HETATM 2418 C C5 . NAG H 7 . ? 5.593 -21.616 4.883 1.00 95.30 ? 306 NAG B C5 1 HETATM 2419 C C6 . NAG H 7 . ? 4.762 -21.278 3.650 1.00 94.23 ? 306 NAG B C6 1 HETATM 2420 C C7 . NAG H 7 . ? 8.159 -22.821 9.171 1.00 83.21 ? 306 NAG B C7 1 HETATM 2421 C C8 . NAG H 7 . ? 9.525 -22.409 9.644 1.00 76.82 ? 306 NAG B C8 1 HETATM 2422 N N2 . NAG H 7 . ? 7.713 -22.213 8.068 1.00 85.87 ? 306 NAG B N2 1 HETATM 2423 O O3 . NAG H 7 . ? 6.709 -24.732 6.563 1.00 87.96 ? 306 NAG B O3 1 HETATM 2424 O O4 . NAG H 7 . ? 6.040 -23.821 3.962 1.00 100.04 ? 306 NAG B O4 1 HETATM 2425 O O5 . NAG H 7 . ? 5.007 -20.997 6.010 1.00 91.86 ? 306 NAG B O5 1 HETATM 2426 O O6 . NAG H 7 . ? 4.700 -19.877 3.511 1.00 92.17 ? 306 NAG B O6 1 HETATM 2427 O O7 . NAG H 7 . ? 7.516 -23.670 9.796 1.00 81.30 ? 306 NAG B O7 1 HETATM 2428 O O . HOH I 8 . ? 5.702 18.886 14.303 1.00 29.22 ? 401 HOH B O 1 HETATM 2429 O O . HOH I 8 . ? 29.368 -13.191 13.700 1.00 51.80 ? 402 HOH B O 1 HETATM 2430 O O . HOH I 8 . ? -0.454 11.467 4.855 1.00 29.86 ? 403 HOH B O 1 HETATM 2431 O O . HOH I 8 . ? 4.893 7.300 9.347 1.00 26.14 ? 404 HOH B O 1 HETATM 2432 O O . HOH I 8 . ? 8.274 3.945 30.421 1.00 27.88 ? 405 HOH B O 1 HETATM 2433 O O . HOH I 8 . ? 20.661 -9.959 13.341 1.00 32.82 ? 406 HOH B O 1 HETATM 2434 O O . HOH I 8 . ? 18.749 -0.320 26.841 1.00 32.16 ? 407 HOH B O 1 HETATM 2435 O O . HOH I 8 . ? 5.945 -0.399 17.295 1.00 27.08 ? 408 HOH B O 1 HETATM 2436 O O . HOH I 8 . ? 6.319 10.414 13.349 1.00 28.88 ? 409 HOH B O 1 HETATM 2437 O O . HOH I 8 . ? 7.035 13.744 2.237 1.00 29.81 ? 410 HOH B O 1 HETATM 2438 O O . HOH I 8 . ? 4.541 8.301 11.866 1.00 29.68 ? 411 HOH B O 1 HETATM 2439 O O . HOH I 8 . ? 8.676 0.024 16.412 1.00 24.78 ? 412 HOH B O 1 HETATM 2440 O O . HOH I 8 . ? 7.792 15.162 8.930 1.00 26.71 ? 413 HOH B O 1 HETATM 2441 O O . HOH I 8 . ? 23.866 -0.641 10.169 1.00 27.22 ? 414 HOH B O 1 HETATM 2442 O O . HOH I 8 . ? 4.637 11.008 10.743 1.00 36.28 ? 415 HOH B O 1 HETATM 2443 O O . HOH I 8 . ? 2.700 4.578 10.829 1.00 25.47 ? 416 HOH B O 1 HETATM 2444 O O . HOH I 8 . ? 8.293 5.659 26.602 1.00 23.35 ? 417 HOH B O 1 HETATM 2445 O O . HOH I 8 . ? 33.154 -2.784 19.857 1.00 45.39 ? 418 HOH B O 1 HETATM 2446 O O . HOH I 8 . ? 26.245 3.123 27.031 1.00 29.76 ? 419 HOH B O 1 HETATM 2447 O O . HOH I 8 . ? -1.889 -7.445 2.731 1.00 34.52 ? 420 HOH B O 1 HETATM 2448 O O . HOH I 8 . ? 12.711 -1.424 10.238 1.00 24.61 ? 421 HOH B O 1 HETATM 2449 O O . HOH I 8 . ? 21.871 3.624 33.339 1.00 34.07 ? 422 HOH B O 1 HETATM 2450 O O . HOH I 8 . ? 21.943 -7.403 27.444 1.00 28.76 ? 423 HOH B O 1 HETATM 2451 O O . HOH I 8 . ? 13.592 5.755 15.279 1.00 33.97 ? 424 HOH B O 1 HETATM 2452 O O . HOH I 8 . ? 27.033 9.034 24.474 1.00 43.10 ? 425 HOH B O 1 HETATM 2453 O O . HOH I 8 . ? 26.609 10.665 5.852 1.00 33.49 ? 426 HOH B O 1 HETATM 2454 O O . HOH I 8 . ? 27.170 -3.131 19.649 1.00 34.84 ? 427 HOH B O 1 HETATM 2455 O O . HOH I 8 . ? 19.535 2.528 28.875 1.00 29.19 ? 428 HOH B O 1 HETATM 2456 O O . HOH I 8 . ? 6.386 -7.811 18.191 1.00 51.72 ? 429 HOH B O 1 HETATM 2457 O O . HOH I 8 . ? 25.979 -7.041 3.164 1.00 44.15 ? 430 HOH B O 1 HETATM 2458 O O . HOH I 8 . ? 12.481 10.718 24.178 1.00 36.73 ? 431 HOH B O 1 HETATM 2459 O O . HOH I 8 . ? 28.087 3.357 25.011 1.00 30.72 ? 432 HOH B O 1 HETATM 2460 O O . HOH I 8 . ? 16.514 -5.145 29.843 1.00 35.65 ? 433 HOH B O 1 HETATM 2461 O O . HOH I 8 . ? 16.155 -3.770 20.832 1.00 26.33 ? 434 HOH B O 1 HETATM 2462 O O . HOH I 8 . ? 12.782 7.828 13.707 1.00 26.88 ? 435 HOH B O 1 HETATM 2463 O O . HOH I 8 . ? 6.124 2.571 23.014 1.00 24.31 ? 436 HOH B O 1 HETATM 2464 O O . HOH I 8 . ? 22.331 -18.388 21.890 1.00 32.42 ? 437 HOH B O 1 HETATM 2465 O O . HOH I 8 . ? 18.059 -0.588 23.527 1.00 25.89 ? 438 HOH B O 1 HETATM 2466 O O . HOH I 8 . ? 13.174 10.675 14.002 1.00 34.72 ? 439 HOH B O 1 HETATM 2467 O O . HOH I 8 . ? -7.397 2.231 14.342 1.00 39.62 ? 440 HOH B O 1 HETATM 2468 O O . HOH I 8 . ? 28.429 -6.352 29.901 1.00 38.63 ? 441 HOH B O 1 HETATM 2469 O O . HOH I 8 . ? 27.014 -13.330 24.346 1.00 39.30 ? 442 HOH B O 1 HETATM 2470 O O . HOH I 8 . ? 3.208 12.011 12.975 1.00 41.75 ? 443 HOH B O 1 HETATM 2471 O O . HOH I 8 . ? 21.451 -14.506 29.121 1.00 42.39 ? 444 HOH B O 1 HETATM 2472 O O . HOH I 8 . ? -4.555 8.286 20.737 1.00 46.63 ? 445 HOH B O 1 HETATM 2473 O O . HOH I 8 . ? 4.089 17.595 18.062 1.00 30.62 ? 446 HOH B O 1 HETATM 2474 O O . HOH I 8 . ? 15.481 9.957 24.886 1.00 34.63 ? 447 HOH B O 1 HETATM 2475 O O . HOH I 8 . ? 22.049 -0.648 31.832 1.00 33.91 ? 448 HOH B O 1 HETATM 2476 O O . HOH I 8 . ? 0.198 -16.961 11.851 1.00 49.85 ? 449 HOH B O 1 HETATM 2477 O O . HOH I 8 . ? 20.514 1.218 33.400 1.00 35.31 ? 450 HOH B O 1 HETATM 2478 O O . HOH I 8 . ? 19.239 -9.982 15.685 1.00 31.65 ? 451 HOH B O 1 HETATM 2479 O O . HOH I 8 . ? 21.409 3.994 36.188 1.00 57.13 ? 452 HOH B O 1 HETATM 2480 O O . HOH I 8 . ? 1.229 -19.683 11.547 1.00 60.84 ? 453 HOH B O 1 HETATM 2481 O O . HOH I 8 . ? 1.754 -20.527 19.766 1.00 41.65 ? 454 HOH B O 1 HETATM 2482 O O . HOH I 8 . ? 12.790 -10.956 27.731 1.00 44.41 ? 455 HOH B O 1 HETATM 2483 O O . HOH I 8 . ? 32.693 2.185 12.739 1.00 37.91 ? 456 HOH B O 1 HETATM 2484 O O . HOH I 8 . ? 17.716 -4.567 27.646 1.00 42.57 ? 457 HOH B O 1 HETATM 2485 O O . HOH I 8 . ? -2.180 13.428 4.439 1.00 45.97 ? 458 HOH B O 1 HETATM 2486 O O . HOH I 8 . ? -4.372 11.161 16.261 1.00 40.22 ? 459 HOH B O 1 HETATM 2487 O O . HOH I 8 . ? 16.824 8.667 31.751 1.00 37.04 ? 460 HOH B O 1 HETATM 2488 O O . HOH I 8 . ? 2.284 14.234 22.848 1.00 40.36 ? 461 HOH B O 1 HETATM 2489 O O . HOH I 8 . ? 18.710 9.609 26.115 1.00 33.07 ? 462 HOH B O 1 HETATM 2490 O O . HOH I 8 . ? 18.016 -2.092 29.005 1.00 40.56 ? 463 HOH B O 1 HETATM 2491 O O . HOH I 8 . ? 20.959 -0.388 28.617 1.00 30.32 ? 464 HOH B O 1 HETATM 2492 O O . HOH I 8 . ? 18.969 0.555 31.160 1.00 31.84 ? 465 HOH B O 1 HETATM 2493 O O . HOH I 8 . ? 12.693 -7.690 25.578 1.00 38.32 ? 466 HOH B O 1 HETATM 2494 O O . HOH I 8 . ? 29.731 -6.304 12.835 1.00 48.03 ? 467 HOH B O 1 HETATM 2495 O O . HOH I 8 . ? 1.375 8.060 24.778 1.00 33.83 ? 468 HOH B O 1 HETATM 2496 O O . HOH I 8 . ? 27.111 -3.642 31.616 1.00 43.16 ? 469 HOH B O 1 HETATM 2497 O O . HOH I 8 . ? -0.596 1.548 -0.968 1.00 48.17 ? 470 HOH B O 1 HETATM 2498 O O . HOH I 8 . ? 0.831 16.725 3.796 1.00 43.61 ? 471 HOH B O 1 HETATM 2499 O O . HOH I 8 . ? 11.713 14.255 25.092 1.00 35.58 ? 472 HOH B O 1 HETATM 2500 O O . HOH I 8 . ? 11.995 16.866 25.287 1.00 33.45 ? 473 HOH B O 1 HETATM 2501 O O . HOH I 8 . ? 4.245 10.646 15.047 1.00 37.96 ? 474 HOH B O 1 HETATM 2502 O O . HOH I 8 . ? 0.597 11.576 12.232 1.00 43.95 ? 475 HOH B O 1 HETATM 2503 O O . HOH I 8 . ? 21.444 -15.866 31.521 1.00 44.21 ? 476 HOH B O 1 HETATM 2504 O O . HOH I 8 . ? 1.006 7.206 27.118 1.00 38.98 ? 477 HOH B O 1 HETATM 2505 O O . HOH I 8 . ? 24.197 8.150 1.692 1.00 46.97 ? 478 HOH B O 1 HETATM 2506 O O . HOH I 8 . ? 5.348 8.560 27.587 1.00 45.36 ? 479 HOH B O 1 HETATM 2507 O O . HOH I 8 . ? 15.762 4.998 1.293 1.00 43.14 ? 480 HOH B O 1 HETATM 2508 O O . HOH I 8 . ? 21.193 16.248 2.326 1.00 41.72 ? 481 HOH B O 1 HETATM 2509 O O . HOH I 8 . ? 18.547 4.781 1.107 1.00 31.21 ? 482 HOH B O 1 HETATM 2510 O O . HOH I 8 . ? 33.079 1.728 18.183 1.00 40.39 ? 483 HOH B O 1 HETATM 2511 O O . HOH I 8 . ? 1.468 -15.207 19.862 1.00 45.65 ? 484 HOH B O 1 HETATM 2512 O O . HOH I 8 . ? 9.871 -15.199 2.167 1.00 47.90 ? 485 HOH B O 1 HETATM 2513 O O . HOH I 8 . ? 21.011 -19.108 24.098 1.00 46.66 ? 486 HOH B O 1 HETATM 2514 O O . HOH I 8 . ? 30.846 0.851 33.239 1.00 56.05 ? 487 HOH B O 1 HETATM 2515 O O . HOH I 8 . ? -5.268 4.404 2.659 1.00 46.31 ? 488 HOH B O 1 HETATM 2516 O O . HOH I 8 . ? 5.915 -15.787 7.354 1.00 49.36 ? 489 HOH B O 1 HETATM 2517 O O . HOH I 8 . ? -3.588 -14.580 10.281 1.00 51.64 ? 490 HOH B O 1 HETATM 2518 O O . HOH I 8 . ? 18.949 5.167 36.648 1.00 57.35 ? 491 HOH B O 1 HETATM 2519 O O . HOH I 8 . ? 10.844 21.010 18.839 1.00 39.29 ? 492 HOH B O 1 HETATM 2520 O O . HOH I 8 . ? -6.989 10.385 16.455 1.00 52.08 ? 493 HOH B O 1 HETATM 2521 O O . HOH I 8 . ? 28.528 1.179 0.366 1.00 47.23 ? 494 HOH B O 1 HETATM 2522 O O . HOH I 8 . ? -1.248 -3.237 -7.500 1.00 47.40 ? 495 HOH B O 1 HETATM 2523 O O . HOH I 8 . ? 31.657 -16.966 23.103 1.00 58.12 ? 496 HOH B O 1 HETATM 2524 O O . HOH I 8 . ? 19.440 -14.209 32.755 1.00 39.39 ? 497 HOH B O 1 HETATM 2525 O O . HOH I 8 . ? 26.048 0.613 -0.123 1.00 55.60 ? 498 HOH B O 1 HETATM 2526 O O . HOH I 8 . ? 5.664 19.508 16.823 1.00 45.26 ? 499 HOH B O 1 HETATM 2527 O O . HOH I 8 . ? 22.154 -17.378 10.214 1.00 56.46 ? 500 HOH B O 1 HETATM 2528 O O . HOH I 8 . ? 32.352 11.530 13.557 1.00 57.45 ? 501 HOH B O 1 HETATM 2529 O O . HOH I 8 . ? 0.154 13.506 20.756 1.00 50.15 ? 502 HOH B O 1 HETATM 2530 O O . HOH I 8 . ? -4.088 5.300 21.217 1.00 45.23 ? 503 HOH B O 1 HETATM 2531 O O . HOH I 8 . ? 16.564 -14.546 29.102 1.00 46.43 ? 504 HOH B O 1 HETATM 2532 O O . HOH I 8 . ? -6.322 10.702 18.968 1.00 51.30 ? 505 HOH B O 1 HETATM 2533 O O . HOH I 8 . ? 24.361 -12.784 6.077 1.00 61.31 ? 506 HOH B O 1 HETATM 2534 O O . HOH I 8 . ? 9.263 -15.298 -0.518 1.00 68.92 ? 507 HOH B O 1 HETATM 2535 O O . HOH I 8 . ? 4.797 10.233 -3.292 1.00 53.33 ? 508 HOH B O 1 HETATM 2536 O O . HOH I 8 . ? 27.612 11.498 3.465 1.00 50.09 ? 509 HOH B O 1 HETATM 2537 O O . HOH I 8 . ? 4.828 -1.138 -7.785 1.00 51.02 ? 510 HOH B O 1 HETATM 2538 O O . HOH I 8 . ? -5.239 5.099 0.063 1.00 72.25 ? 511 HOH B O 1 HETATM 2539 O O . HOH I 8 . ? 33.655 13.797 13.755 1.00 58.26 ? 512 HOH B O 1 HETATM 2540 O O . HOH I 8 . ? 12.489 -3.452 33.925 1.00 47.43 ? 513 HOH B O 1 HETATM 2541 O O . HOH I 8 . ? 28.277 -14.345 22.406 1.00 52.74 ? 514 HOH B O 1 HETATM 2542 O O . HOH I 8 . ? 12.128 -15.284 2.320 1.00 48.99 ? 515 HOH B O 1 HETATM 2543 O O . HOH I 8 . ? 27.913 6.131 26.126 1.00 45.91 ? 516 HOH B O 1 HETATM 2544 O O . HOH I 8 . ? 10.683 -11.786 24.512 1.00 35.03 ? 517 HOH B O 1 HETATM 2545 O O . HOH I 8 . ? 27.955 -13.532 9.653 1.00 49.18 ? 518 HOH B O 1 HETATM 2546 O O . HOH I 8 . ? 17.249 8.735 28.457 1.00 38.95 ? 519 HOH B O 1 HETATM 2547 O O . HOH I 8 . ? 16.334 -21.330 12.861 1.00 45.52 ? 520 HOH B O 1 HETATM 2548 O O . HOH I 8 . ? 3.162 -22.645 18.001 1.00 47.21 ? 521 HOH B O 1 HETATM 2549 O O . HOH I 8 . ? 33.957 -0.143 20.188 1.00 48.49 ? 522 HOH B O 1 HETATM 2550 O O . HOH I 8 . ? 18.624 -7.242 26.968 1.00 45.34 ? 523 HOH B O 1 HETATM 2551 O O . HOH I 8 . ? 26.569 13.340 1.639 1.00 59.79 ? 524 HOH B O 1 HETATM 2552 O O . HOH J 8 . ? 7.500 20.719 13.109 1.00 30.80 ? 101 HOH A O 1 HETATM 2553 O O . HOH J 8 . ? 22.582 10.027 15.485 1.00 24.26 ? 102 HOH A O 1 HETATM 2554 O O . HOH J 8 . ? 15.811 18.999 12.061 1.00 29.48 ? 103 HOH A O 1 HETATM 2555 O O . HOH J 8 . ? 14.447 24.932 15.264 1.00 28.40 ? 104 HOH A O 1 HETATM 2556 O O . HOH J 8 . ? 16.659 25.198 16.911 1.00 36.70 ? 105 HOH A O 1 HETATM 2557 O O . HOH J 8 . ? 16.678 15.855 -1.259 1.00 46.97 ? 106 HOH A O 1 HETATM 2558 O O . HOH J 8 . ? 33.789 11.758 17.980 1.00 39.60 ? 107 HOH A O 1 HETATM 2559 O O . HOH J 8 . ? 24.337 13.398 23.971 1.00 31.98 ? 108 HOH A O 1 HETATM 2560 O O . HOH J 8 . ? 11.068 23.284 16.715 1.00 37.27 ? 109 HOH A O 1 HETATM 2561 O O . HOH J 8 . ? 7.757 20.970 4.546 1.00 40.35 ? 110 HOH A O 1 HETATM 2562 O O . HOH J 8 . ? 16.560 4.603 -6.257 1.00 54.35 ? 111 HOH A O 1 HETATM 2563 O O . HOH J 8 . ? 14.130 6.276 -5.575 1.00 42.06 ? 112 HOH A O 1 HETATM 2564 O O . HOH J 8 . ? 16.890 12.071 25.891 1.00 47.04 ? 113 HOH A O 1 HETATM 2565 O O . HOH J 8 . ? 22.411 23.450 23.777 1.00 42.43 ? 114 HOH A O 1 HETATM 2566 O O . HOH J 8 . ? 12.425 28.366 6.025 1.00 54.57 ? 115 HOH A O 1 HETATM 2567 O O . HOH J 8 . ? 10.455 13.340 -1.999 1.00 60.00 ? 116 HOH A O 1 HETATM 2568 O O . HOH J 8 . ? 15.089 27.063 13.245 1.00 43.50 ? 117 HOH A O 1 HETATM 2569 O O . HOH J 8 . ? 8.088 23.854 4.116 1.00 57.05 ? 118 HOH A O 1 HETATM 2570 O O . HOH J 8 . ? 10.174 27.997 6.919 1.00 63.68 ? 119 HOH A O 1 HETATM 2571 O O . HOH J 8 . ? 17.102 19.020 19.838 1.00 29.36 ? 120 HOH A O 1 HETATM 2572 O O . HOH J 8 . ? 13.417 25.834 5.557 1.00 66.23 ? 121 HOH A O 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 . ILE A 1 ? 0.3842 0.3791 0.3526 -0.0091 0.0449 0.0126 16 ILE B N 2 C CA . ILE A 1 ? 0.3409 0.3254 0.2947 -0.0060 0.0402 0.0069 16 ILE B CA 3 C C . ILE A 1 ? 0.3421 0.3208 0.2745 -0.0045 0.0458 0.0064 16 ILE B C 4 O O . ILE A 1 ? 0.3634 0.3473 0.2937 -0.0010 0.0560 0.0052 16 ILE B O 5 C CB . ILE A 1 ? 0.3689 0.3542 0.3297 -0.0017 0.0393 0.0006 16 ILE B CB 6 C CG1 . ILE A 1 ? 0.3356 0.3262 0.3135 -0.0027 0.0346 0.0014 16 ILE B CG1 7 C CG2 . ILE A 1 ? 0.3561 0.3300 0.3041 -0.0005 0.0335 -0.0044 16 ILE B CG2 8 C CD1 . ILE A 1 ? 0.3977 0.3840 0.3761 -0.0053 0.0268 0.0024 16 ILE B CD1 9 N N . VAL A 2 ? 0.3500 0.3182 0.2660 -0.0063 0.0390 0.0073 17 VAL B N 10 C CA . VAL A 2 ? 0.4180 0.3773 0.3076 -0.0050 0.0419 0.0066 17 VAL B CA 11 C C . VAL A 2 ? 0.4397 0.3884 0.3180 -0.0017 0.0355 -0.0026 17 VAL B C 12 O O . VAL A 2 ? 0.4162 0.3625 0.3038 -0.0034 0.0249 -0.0045 17 VAL B O 13 C CB . VAL A 2 ? 0.4295 0.3815 0.3055 -0.0094 0.0359 0.0140 17 VAL B CB 14 C CG1 . VAL A 2 ? 0.4976 0.4385 0.3410 -0.0078 0.0379 0.0131 17 VAL B CG1 15 C CG2 . VAL A 2 ? 0.4571 0.4166 0.3449 -0.0139 0.0411 0.0237 17 VAL B CG2 16 N N . GLU A 3 ? 0.4505 0.3929 0.3091 0.0028 0.0424 -0.0080 18 GLU B N 17 C CA . GLU A 3 ? 0.5068 0.4345 0.3497 0.0057 0.0358 -0.0176 18 GLU B CA 18 C C . GLU A 3 ? 0.4746 0.4035 0.3387 0.0065 0.0308 -0.0224 18 GLU B C 19 O O . GLU A 3 ? 0.4773 0.3958 0.3382 0.0046 0.0198 -0.0270 18 GLU B O 20 C CB . GLU A 3 ? 0.5306 0.4456 0.3543 0.0017 0.0221 -0.0171 18 GLU B CB 21 C CG . GLU A 3 ? 0.6144 0.5222 0.4070 0.0021 0.0264 -0.0138 18 GLU B CG 22 C CD . GLU A 3 ? 0.7116 0.6047 0.4723 0.0080 0.0309 -0.0235 18 GLU B CD 23 O OE1 . GLU A 3 ? 0.8216 0.7096 0.5536 0.0098 0.0385 -0.0211 18 GLU B OE1 24 O OE2 . GLU A 3 ? 0.6840 0.5690 0.4463 0.0110 0.0271 -0.0334 18 GLU B OE2 25 N N . GLY A 4 ? 0.4465 0.3882 0.3324 0.0085 0.0385 -0.0205 19 GLY B N 26 C CA . GLY A 4 ? 0.4595 0.4020 0.3633 0.0098 0.0351 -0.0235 19 GLY B CA 27 C C . GLY A 4 ? 0.4570 0.3954 0.3572 0.0177 0.0433 -0.0300 19 GLY B C 28 O O . GLY A 4 ? 0.4578 0.3872 0.3365 0.0222 0.0485 -0.0352 19 GLY B O 29 N N . SER A 5 ? 0.3945 0.3382 0.3140 0.0202 0.0443 -0.0298 20 SER B N 30 C CA . SER A 5 ? 0.4326 0.3744 0.3533 0.0292 0.0522 -0.0349 20 SER B CA 31 C C . SER A 5 ? 0.3742 0.3310 0.3212 0.0309 0.0547 -0.0298 20 SER B C 32 O O . SER A 5 ? 0.3494 0.3143 0.3093 0.0248 0.0492 -0.0238 20 SER B O 33 C CB . SER A 5 ? 0.5161 0.4364 0.4254 0.0320 0.0455 -0.0435 20 SER B CB 34 O OG . SER A 5 ? 0.5227 0.4396 0.4440 0.0257 0.0345 -0.0407 20 SER B OG 35 N N . ASP A 6 ? 0.3545 0.3145 0.3085 0.0400 0.0625 -0.0326 21 ASP B N 36 C CA . ASP A 6 ? 0.3554 0.3289 0.3346 0.0427 0.0629 -0.0279 21 ASP B CA 37 C C . ASP A 6 ? 0.3735 0.3383 0.3588 0.0393 0.0515 -0.0265 21 ASP B C 38 O O . ASP A 6 ? 0.3912 0.3378 0.3662 0.0401 0.0464 -0.0313 21 ASP B O 39 C CB . ASP A 6 ? 0.3523 0.3274 0.3379 0.0549 0.0716 -0.0322 21 ASP B CB 40 C CG . ASP A 6 ? 0.3614 0.3503 0.3456 0.0596 0.0862 -0.0321 21 ASP B CG 41 O OD1 . ASP A 6 ? 0.3703 0.3679 0.3499 0.0523 0.0891 -0.0272 21 ASP B OD1 42 O OD2 . ASP A 6 ? 0.4389 0.4302 0.4274 0.0710 0.0955 -0.0364 21 ASP B OD2 43 N N . ALA A 7 ? 0.3722 0.3488 0.3732 0.0353 0.0475 -0.0197 22 ALA B N 44 C CA . ALA A 7 ? 0.3827 0.3526 0.3886 0.0332 0.0389 -0.0170 22 ALA B CA 45 C C . ALA A 7 ? 0.3899 0.3526 0.4019 0.0419 0.0389 -0.0189 22 ALA B C 46 O O . ALA A 7 ? 0.4084 0.3794 0.4294 0.0500 0.0455 -0.0203 22 ALA B O 47 C CB . ALA A 7 ? 0.3777 0.3611 0.3956 0.0288 0.0353 -0.0101 22 ALA B CB 48 N N . GLU A 8 ? 0.3673 0.3152 0.3764 0.0404 0.0318 -0.0181 23 GLU B N 49 C CA . GLU A 8 ? 0.4027 0.3429 0.4198 0.0481 0.0295 -0.0173 23 GLU B CA 50 C C . GLU A 8 ? 0.3539 0.3088 0.3859 0.0482 0.0262 -0.0092 23 GLU B C 51 O O . GLU A 8 ? 0.3525 0.3171 0.3843 0.0407 0.0239 -0.0047 23 GLU B O 52 C CB . GLU A 8 ? 0.4564 0.3747 0.4658 0.0448 0.0221 -0.0170 23 GLU B CB 53 C CG . GLU A 8 ? 0.5273 0.4262 0.5220 0.0455 0.0221 -0.0261 23 GLU B CG 54 C CD . GLU A 8 ? 0.5933 0.4712 0.5841 0.0396 0.0132 -0.0243 23 GLU B CD 55 O OE1 . GLU A 8 ? 0.7002 0.5589 0.6901 0.0456 0.0102 -0.0272 23 GLU B OE1 56 O OE2 . GLU A 8 ? 0.6185 0.4997 0.6088 0.0289 0.0093 -0.0193 23 GLU B OE2 57 N N . ILE A 9 ? 0.3734 0.3287 0.4173 0.0571 0.0250 -0.0076 24 ILE B N 58 C CA . ILE A 9 ? 0.3955 0.3629 0.4523 0.0575 0.0190 0.0003 24 ILE B CA 59 C C . ILE A 9 ? 0.3996 0.3580 0.4466 0.0496 0.0113 0.0068 24 ILE B C 60 O O . ILE A 9 ? 0.4163 0.3566 0.4553 0.0486 0.0084 0.0078 24 ILE B O 61 C CB . ILE A 9 ? 0.4475 0.4165 0.5206 0.0696 0.0178 0.0014 24 ILE B CB 62 C CG1 . ILE A 9 ? 0.5479 0.5343 0.6342 0.0766 0.0281 -0.0035 24 ILE B CG1 63 C CG2 . ILE A 9 ? 0.4590 0.4356 0.5416 0.0690 0.0077 0.0105 24 ILE B CG2 64 C CD1 . ILE A 9 ? 0.6618 0.6601 0.7722 0.0888 0.0282 -0.0014 24 ILE B CD1 65 N N . GLY A 10 ? 0.3606 0.3310 0.4072 0.0436 0.0085 0.0109 25 GLY B N 66 C CA . GLY A 10 ? 0.3757 0.3400 0.4111 0.0371 0.0034 0.0169 25 GLY B CA 67 C C . GLY A 10 ? 0.3382 0.2959 0.3617 0.0292 0.0066 0.0155 25 GLY B C 68 O O . GLY A 10 ? 0.3589 0.3116 0.3743 0.0244 0.0046 0.0210 25 GLY B O 69 N N . MET A 11 ? 0.3328 0.2913 0.3555 0.0281 0.0118 0.0088 26 MET B N 70 C CA . MET A 11 ? 0.3592 0.3128 0.3736 0.0210 0.0134 0.0073 26 MET B CA 71 C C . MET A 11 ? 0.3588 0.3228 0.3699 0.0155 0.0138 0.0097 26 MET B C 72 O O . MET A 11 ? 0.3578 0.3199 0.3648 0.0101 0.0142 0.0117 26 MET B O 73 C CB . MET A 11 ? 0.3998 0.3519 0.4119 0.0221 0.0174 -0.0004 26 MET B CB 74 C CG . MET A 11 ? 0.4650 0.4103 0.4697 0.0156 0.0166 -0.0026 26 MET B CG 75 S SD . MET A 11 ? 0.4902 0.4331 0.4872 0.0182 0.0204 -0.0115 26 MET B SD 76 C CE . MET A 11 ? 0.5298 0.4525 0.5181 0.0139 0.0146 -0.0152 26 MET B CE 77 N N . SER A 12 ? 0.3471 0.3223 0.3615 0.0170 0.0136 0.0094 27 SER B N 78 C CA . SER A 12 ? 0.3673 0.3497 0.3775 0.0132 0.0135 0.0098 27 SER B CA 79 C C . SER A 12 ? 0.3586 0.3463 0.3697 0.0150 0.0086 0.0125 27 SER B C 80 O O . SER A 12 ? 0.3312 0.3268 0.3475 0.0148 0.0071 0.0106 27 SER B O 81 C CB . SER A 12 ? 0.3863 0.3741 0.3981 0.0113 0.0167 0.0052 27 SER B CB 82 O OG . SER A 12 ? 0.4568 0.4479 0.4642 0.0080 0.0163 0.0051 27 SER B OG 83 N N . PRO A 13 ? 0.3393 0.3217 0.3446 0.0162 0.0050 0.0178 28 PRO B N 84 C CA . PRO A 13 ? 0.3404 0.3259 0.3446 0.0184 -0.0022 0.0206 28 PRO B CA 85 C C . PRO A 13 ? 0.3287 0.3168 0.3222 0.0156 -0.0045 0.0188 28 PRO B C 86 O O . PRO A 13 ? 0.3516 0.3408 0.3418 0.0166 -0.0123 0.0201 28 PRO B O 87 C CB . PRO A 13 ? 0.3718 0.3476 0.3688 0.0202 -0.0050 0.0277 28 PRO B CB 88 C CG . PRO A 13 ? 0.3306 0.3002 0.3212 0.0162 0.0016 0.0290 28 PRO B CG 89 C CD . PRO A 13 ? 0.3359 0.3084 0.3357 0.0150 0.0064 0.0224 28 PRO B CD 90 N N . TRP A 14 ? 0.2973 0.2853 0.2852 0.0127 0.0013 0.0157 29 TRP B N 91 C CA . TRP A 14 ? 0.3171 0.3055 0.2950 0.0114 0.0000 0.0122 29 TRP B CA 92 C C . TRP A 14 ? 0.3376 0.3308 0.3254 0.0094 -0.0013 0.0073 29 TRP B C 93 O O . TRP A 14 ? 0.3242 0.3152 0.3054 0.0083 -0.0036 0.0036 29 TRP B O 94 C CB . TRP A 14 ? 0.3169 0.3032 0.2852 0.0107 0.0074 0.0122 29 TRP B CB 95 C CG . TRP A 14 ? 0.3275 0.3152 0.3057 0.0089 0.0133 0.0133 29 TRP B CG 96 C CD1 . TRP A 14 ? 0.3229 0.3133 0.3101 0.0073 0.0152 0.0095 29 TRP B CD1 97 C CD2 . TRP A 14 ? 0.3588 0.3433 0.3377 0.0077 0.0163 0.0188 29 TRP B CD2 98 N NE1 . TRP A 14 ? 0.3393 0.3282 0.3316 0.0055 0.0183 0.0113 29 TRP B NE1 99 C CE2 . TRP A 14 ? 0.3446 0.3298 0.3335 0.0053 0.0189 0.0169 29 TRP B CE2 100 C CE3 . TRP A 14 ? 0.3781 0.3580 0.3494 0.0079 0.0162 0.0258 29 TRP B CE3 101 C CZ2 . TRP A 14 ? 0.3491 0.3301 0.3420 0.0025 0.0205 0.0208 29 TRP B CZ2 102 C CZ3 . TRP A 14 ? 0.3918 0.3677 0.3682 0.0049 0.0190 0.0309 29 TRP B CZ3 103 C CH2 . TRP A 14 ? 0.3537 0.3300 0.3416 0.0020 0.0206 0.0280 29 TRP B CH2 104 N N . GLN A 15 ? 0.3140 0.3122 0.3162 0.0092 0.0006 0.0073 30 GLN B N 105 C CA . GLN A 15 ? 0.3499 0.3533 0.3617 0.0065 0.0008 0.0048 30 GLN B CA 106 C C . GLN A 15 ? 0.3244 0.3320 0.3423 0.0049 -0.0077 0.0050 30 GLN B C 107 O O . GLN A 15 ? 0.3663 0.3784 0.3918 0.0070 -0.0126 0.0079 30 GLN B O 108 C CB . GLN A 15 ? 0.3952 0.4039 0.4189 0.0077 0.0060 0.0054 30 GLN B CB 109 C CG . GLN A 15 ? 0.3998 0.4120 0.4282 0.0045 0.0097 0.0040 30 GLN B CG 110 C CD . GLN A 15 ? 0.4811 0.4867 0.4993 0.0031 0.0134 0.0020 30 GLN B CD 111 O OE1 . GLN A 15 ? 0.6595 0.6603 0.6716 0.0047 0.0150 0.0018 30 GLN B OE1 112 N NE2 . GLN A 15 ? 0.4185 0.4238 0.4366 0.0000 0.0138 0.0015 30 GLN B NE2 113 N N . VAL A 16 ? 0.3162 0.3218 0.3328 0.0010 -0.0106 0.0023 31 VAL B N 114 C CA . VAL A 16 ? 0.3340 0.3424 0.3584 -0.0026 -0.0203 0.0023 31 VAL B CA 115 C C . VAL A 16 ? 0.2989 0.3135 0.3387 -0.0079 -0.0180 0.0034 31 VAL B C 116 O O . VAL A 16 ? 0.3170 0.3284 0.3533 -0.0088 -0.0110 0.0027 31 VAL B O 117 C CB . VAL A 16 ? 0.3666 0.3626 0.3726 -0.0032 -0.0280 -0.0022 31 VAL B CB 118 C CG1 . VAL A 16 ? 0.4012 0.3972 0.4144 -0.0083 -0.0407 -0.0031 31 VAL B CG1 119 C CG2 . VAL A 16 ? 0.3684 0.3590 0.3566 0.0019 -0.0285 -0.0018 31 VAL B CG2 120 N N . MET A 17 ? 0.3177 0.3422 0.3755 -0.0114 -0.0240 0.0064 32 MET B N 121 C CA . MET A 17 ? 0.3197 0.3513 0.3939 -0.0181 -0.0226 0.0093 32 MET B CA 122 C C . MET A 17 ? 0.3032 0.3282 0.3786 -0.0250 -0.0360 0.0078 32 MET B C 123 O O . MET A 17 ? 0.3247 0.3524 0.4050 -0.0256 -0.0472 0.0078 32 MET B O 124 C CB . MET A 17 ? 0.3110 0.3622 0.4099 -0.0173 -0.0178 0.0148 32 MET B CB 125 C CG . MET A 17 ? 0.3569 0.4184 0.4734 -0.0241 -0.0124 0.0198 32 MET B CG 126 S SD . MET A 17 ? 0.3393 0.4280 0.4889 -0.0223 -0.0056 0.0266 32 MET B SD 127 C CE . MET A 17 ? 0.3932 0.4808 0.5302 -0.0113 0.0103 0.0240 32 MET B CE 128 N N . LEU A 18 ? 0.3082 0.3221 0.3776 -0.0298 -0.0366 0.0062 33 LEU B N 129 C CA . LEU A 18 ? 0.3727 0.3784 0.4461 -0.0378 -0.0496 0.0050 33 LEU B CA 130 C C . LEU A 18 ? 0.3577 0.3792 0.4603 -0.0466 -0.0490 0.0132 33 LEU B C 131 O O . LEU A 18 ? 0.3456 0.3746 0.4557 -0.0479 -0.0368 0.0185 33 LEU B O 132 C CB . LEU A 18 ? 0.4316 0.4161 0.4865 -0.0384 -0.0509 -0.0002 33 LEU B CB 133 C CG . LEU A 18 ? 0.5382 0.5099 0.5665 -0.0290 -0.0484 -0.0077 33 LEU B CG 134 C CD1 . LEU A 18 ? 0.5836 0.5337 0.5966 -0.0289 -0.0531 -0.0140 33 LEU B CD1 135 C CD2 . LEU A 18 ? 0.5994 0.5717 0.6179 -0.0248 -0.0550 -0.0107 33 LEU B CD2 136 N N . PHE A 19 ? 0.3183 0.3454 0.4368 -0.0527 -0.0623 0.0147 34 PHE B N 137 C CA . PHE A 19 ? 0.3761 0.4242 0.5288 -0.0611 -0.0622 0.0238 34 PHE B CA 138 C C . PHE A 19 ? 0.3901 0.4292 0.5523 -0.0734 -0.0794 0.0240 34 PHE B C 139 O O . PHE A 19 ? 0.4259 0.4522 0.5768 -0.0737 -0.0957 0.0175 34 PHE B O 140 C CB . PHE A 19 ? 0.3757 0.4455 0.5472 -0.0560 -0.0631 0.0269 34 PHE B CB 141 C CG . PHE A 19 ? 0.3678 0.4656 0.5758 -0.0598 -0.0544 0.0369 34 PHE B CG 142 C CD1 . PHE A 19 ? 0.3941 0.5016 0.6037 -0.0553 -0.0343 0.0405 34 PHE B CD1 143 C CD2 . PHE A 19 ? 0.4219 0.5368 0.6622 -0.0676 -0.0661 0.0425 34 PHE B CD2 144 C CE1 . PHE A 19 ? 0.4075 0.5414 0.6485 -0.0575 -0.0237 0.0495 34 PHE B CE1 145 C CE2 . PHE A 19 ? 0.4436 0.5878 0.7208 -0.0705 -0.0560 0.0526 34 PHE B CE2 146 C CZ . PHE A 19 ? 0.3796 0.5334 0.6562 -0.0650 -0.0336 0.0560 34 PHE B CZ 147 N N . ARG A 20 ? 0.3916 0.4361 0.5734 -0.0838 -0.0761 0.0319 35 ARG B N 148 C CA . ARG A 20 ? 0.4458 0.4817 0.6409 -0.0975 -0.0930 0.0335 35 ARG B CA 149 C C . ARG A 20 ? 0.4533 0.5148 0.6854 -0.1044 -0.1025 0.0404 35 ARG B C 150 O O . ARG A 20 ? 0.3972 0.4879 0.6555 -0.1026 -0.0896 0.0490 35 ARG B O 151 C CB . ARG A 20 ? 0.4854 0.5165 0.6879 -0.1069 -0.0855 0.0413 35 ARG B CB 152 C CG . ARG A 20 ? 0.5186 0.5308 0.7277 -0.1210 -0.1034 0.0417 35 ARG B CG 153 C CD . ARG A 20 ? 0.5480 0.5556 0.7632 -0.1295 -0.0938 0.0516 35 ARG B CD 154 N NE . ARG A 20 ? 0.6383 0.6243 0.8599 -0.1437 -0.1110 0.0528 35 ARG B NE 155 C CZ . ARG A 20 ? 0.6954 0.6656 0.9153 -0.1515 -0.1081 0.0596 35 ARG B CZ 156 N NH1 . ARG A 20 ? 0.6424 0.6169 0.8529 -0.1462 -0.0888 0.0660 35 ARG B NH1 157 N NH2 . ARG A 20 ? 0.7342 0.6821 0.9605 -0.1648 -0.1261 0.0601 35 ARG B NH2 158 N N . LYS A 21 ? 0.4898 0.5400 0.7237 -0.1117 -0.1253 0.0360 36 LYS B N 159 C CA . LYS A 21 ? 0.5398 0.6130 0.8099 -0.1191 -0.1390 0.0421 36 LYS B CA 160 C C . LYS A 21 ? 0.5818 0.6780 0.8964 -0.1339 -0.1354 0.0562 36 LYS B C 161 O O . LYS A 21 ? 0.5737 0.7040 0.9258 -0.1348 -0.1310 0.0655 36 LYS B O 162 C CB . LYS A 21 ? 0.5717 0.6226 0.8281 -0.1243 -0.1669 0.0330 36 LYS B CB 163 C CG . LYS A 21 ? 0.5929 0.6257 0.8086 -0.1104 -0.1719 0.0209 36 LYS B CG 164 C CD . LYS A 21 ? 0.6456 0.6638 0.8534 -0.1157 -0.2006 0.0140 36 LYS B CD 165 C CE . LYS A 21 ? 0.6838 0.6763 0.8420 -0.1030 -0.2050 0.0011 36 LYS B CE 166 N NZ . LYS A 21 ? 0.7354 0.7083 0.8788 -0.1085 -0.2338 -0.0069 36 LYS B NZ 167 N N . SER A 22 A 0.6286 0.7065 0.9404 -0.1455 -0.1374 0.0585 36 SER B N 168 C CA . SER A 22 A 0.6411 0.7383 0.9945 -0.1620 -0.1350 0.0734 36 SER B CA 169 C C . SER A 22 A 0.6215 0.6953 0.9603 -0.1695 -0.1280 0.0768 36 SER B C 170 O O . SER A 22 A 0.6401 0.6783 0.9540 -0.1730 -0.1430 0.0680 36 SER B O 171 C CB . SER A 22 A 0.7191 0.8200 1.1022 -0.1770 -0.1617 0.0755 36 SER B CB 172 O OG . SER A 22 A 0.7940 0.8546 1.1451 -0.1800 -0.1842 0.0623 36 SER B OG 173 N N . PRO A 23 ? 0.6538 0.7457 1.0048 -0.1705 -0.1049 0.0890 37 PRO B N 174 C CA . PRO A 23 ? 0.6384 0.7693 1.0123 -0.1631 -0.0840 0.0973 37 PRO B CA 175 C C . PRO A 23 ? 0.6029 0.7311 0.9464 -0.1428 -0.0755 0.0855 37 PRO B C 176 O O . PRO A 23 ? 0.6187 0.7172 0.9224 -0.1352 -0.0775 0.0748 37 PRO B O 177 C CB . PRO A 23 ? 0.6607 0.7967 1.0367 -0.1682 -0.0625 0.1099 37 PRO B CB 178 C CG . PRO A 23 ? 0.6758 0.7705 1.0139 -0.1693 -0.0687 0.1035 37 PRO B CG 179 C CD . PRO A 23 ? 0.6597 0.7296 0.9937 -0.1759 -0.0968 0.0937 37 PRO B CD 180 N N . GLN A 24 ? 0.5956 0.7544 0.9595 -0.1341 -0.0667 0.0880 38 GLN B N 181 C CA . GLN A 24 ? 0.5385 0.6954 0.8770 -0.1156 -0.0586 0.0784 38 GLN B CA 182 C C . GLN A 24 ? 0.5923 0.7424 0.9052 -0.1077 -0.0362 0.0784 38 GLN B C 183 O O . GLN A 24 ? 0.5485 0.7190 0.8778 -0.1091 -0.0178 0.0884 38 GLN B O 184 C CB . GLN A 24 ? 0.5472 0.7378 0.9172 -0.1082 -0.0552 0.0820 38 GLN B CB 185 C CG . GLN A 24 ? 0.5702 0.7669 0.9631 -0.1144 -0.0802 0.0813 38 GLN B CG 186 C CD . GLN A 24 ? 0.6082 0.8317 1.0239 -0.1031 -0.0798 0.0824 38 GLN B CD 187 O OE1 . GLN A 24 ? 0.5888 0.8468 1.0497 -0.1059 -0.0750 0.0928 38 GLN B OE1 188 N NE2 . GLN A 24 ? 0.5637 0.7718 0.9496 -0.0899 -0.0848 0.0724 38 GLN B NE2 189 N N . GLU A 25 ? 0.4669 0.5887 0.7394 -0.0997 -0.0378 0.0677 39 GLU B N 190 C CA . GLU A 25 ? 0.4887 0.6026 0.7361 -0.0925 -0.0198 0.0671 39 GLU B CA 191 C C . GLU A 25 ? 0.4544 0.5464 0.6654 -0.0804 -0.0220 0.0546 39 GLU B C 192 O O . GLU A 25 ? 0.3702 0.4441 0.5673 -0.0801 -0.0374 0.0465 39 GLU B O 193 C CB . GLU A 25 ? 0.5474 0.6480 0.7899 -0.1035 -0.0170 0.0743 39 GLU B CB 194 C CG . GLU A 25 ? 0.6184 0.6862 0.8406 -0.1085 -0.0341 0.0676 39 GLU B CG 195 C CD . GLU A 25 ? 0.7147 0.7690 0.9368 -0.1203 -0.0332 0.0765 39 GLU B CD 196 O OE1 . GLU A 25 ? 0.7571 0.7866 0.9509 -0.1164 -0.0329 0.0723 39 GLU B OE1 197 O OE2 . GLU A 25 ? 0.7612 0.8299 1.0128 -0.1335 -0.0328 0.0886 39 GLU B OE2 198 N N . LEU A 26 ? 0.4463 0.5403 0.6417 -0.0706 -0.0062 0.0533 40 LEU B N 199 C CA . LEU A 26 ? 0.4399 0.5150 0.6035 -0.0606 -0.0062 0.0434 40 LEU B CA 200 C C . LEU A 26 ? 0.4400 0.4905 0.5832 -0.0650 -0.0112 0.0414 40 LEU B C 201 O O . LEU A 26 ? 0.4560 0.5050 0.6006 -0.0710 -0.0050 0.0485 40 LEU B O 202 C CB . LEU A 26 ? 0.4761 0.5591 0.6308 -0.0510 0.0108 0.0433 40 LEU B CB 203 C CG . LEU A 26 ? 0.5408 0.6066 0.6654 -0.0421 0.0134 0.0354 40 LEU B CG 204 C CD1 . LEU A 26 ? 0.6018 0.6553 0.7150 -0.0383 0.0011 0.0274 40 LEU B CD1 205 C CD2 . LEU A 26 ? 0.6072 0.6835 0.7294 -0.0330 0.0270 0.0346 40 LEU B CD2 206 N N . LEU A 27 ? 0.4317 0.4630 0.5561 -0.0614 -0.0221 0.0324 41 LEU B N 207 C CA . LEU A 27 ? 0.4447 0.4518 0.5505 -0.0632 -0.0271 0.0292 41 LEU B CA 208 C C . LEU A 27 ? 0.4522 0.4498 0.5344 -0.0533 -0.0196 0.0242 41 LEU B C 209 O O . LEU A 27 ? 0.4633 0.4514 0.5366 -0.0542 -0.0156 0.0269 41 LEU B O 210 C CB . LEU A 27 ? 0.5020 0.4922 0.6015 -0.0650 -0.0440 0.0216 41 LEU B CB 211 C CG . LEU A 27 ? 0.5355 0.5275 0.6569 -0.0778 -0.0560 0.0263 41 LEU B CG 212 C CD1 . LEU A 27 ? 0.5655 0.5396 0.6756 -0.0779 -0.0739 0.0165 41 LEU B CD1 213 C CD2 . LEU A 27 ? 0.5565 0.5400 0.6845 -0.0877 -0.0547 0.0344 41 LEU B CD2 214 N N . CYS A 28 ? 0.4008 0.4011 0.4740 -0.0445 -0.0186 0.0177 42 CYS B N 215 C CA A CYS A 28 ? 0.4316 0.4228 0.4847 -0.0360 -0.0142 0.0123 42 CYS B CA 216 C CA B CYS A 28 ? 0.3832 0.3770 0.4378 -0.0361 -0.0122 0.0135 42 CYS B CA 217 C C . CYS A 28 ? 0.3670 0.3664 0.4164 -0.0285 -0.0111 0.0088 42 CYS B C 218 O O . CYS A 28 ? 0.3330 0.3421 0.3929 -0.0288 -0.0147 0.0094 42 CYS B O 219 C CB A CYS A 28 ? 0.4715 0.4429 0.5103 -0.0342 -0.0230 0.0056 42 CYS B CB 220 C CB B CYS A 28 ? 0.3694 0.3432 0.4091 -0.0345 -0.0180 0.0087 42 CYS B CB 221 S SG A CYS A 28 ? 0.5711 0.5245 0.6037 -0.0368 -0.0247 0.0074 42 CYS B SG 222 S SG B CYS A 28 ? 0.3602 0.3221 0.3911 -0.0322 -0.0302 -0.0003 42 CYS B SG 223 N N . GLY A 29 ? 0.3106 0.3047 0.3458 -0.0221 -0.0062 0.0054 43 GLY B N 224 C CA . GLY A 29 ? 0.3240 0.3204 0.3523 -0.0156 -0.0046 0.0021 43 GLY B CA 225 C C . GLY A 29 ? 0.3096 0.2947 0.3245 -0.0125 -0.0106 -0.0035 43 GLY B C 226 O O . GLY A 29 ? 0.3110 0.2851 0.3213 -0.0142 -0.0158 -0.0062 43 GLY B O 227 N N . ALA A 30 ? 0.3402 0.3270 0.3480 -0.0077 -0.0093 -0.0051 44 ALA B N 228 C CA . ALA A 30 ? 0.3236 0.3015 0.3158 -0.0036 -0.0126 -0.0098 44 ALA B CA 229 C C . ALA A 30 ? 0.3364 0.3193 0.3235 0.0007 -0.0078 -0.0080 44 ALA B C 230 O O . ALA A 30 ? 0.2991 0.2901 0.2956 0.0004 -0.0043 -0.0042 44 ALA B O 231 C CB . ALA A 30 ? 0.3639 0.3362 0.3535 -0.0063 -0.0238 -0.0124 44 ALA B CB 232 N N . SER A 31 ? 0.3214 0.2986 0.2930 0.0049 -0.0071 -0.0106 45 SER B N 233 C CA . SER A 31 ? 0.3538 0.3346 0.3204 0.0078 -0.0026 -0.0071 45 SER B CA 234 C C . SER A 31 ? 0.3483 0.3231 0.2974 0.0103 -0.0075 -0.0081 45 SER B C 235 O O . SER A 31 ? 0.3547 0.3207 0.2903 0.0119 -0.0113 -0.0136 45 SER B O 236 C CB . SER A 31 ? 0.3758 0.3582 0.3410 0.0101 0.0066 -0.0066 45 SER B CB 237 O OG . SER A 31 ? 0.4398 0.4164 0.3935 0.0138 0.0081 -0.0112 45 SER B OG 238 N N . LEU A 32 ? 0.3272 0.3048 0.2746 0.0111 -0.0079 -0.0028 46 LEU B N 239 C CA . LEU A 32 ? 0.3496 0.3209 0.2774 0.0136 -0.0127 -0.0019 46 LEU B CA 240 C C . LEU A 32 ? 0.3629 0.3325 0.2757 0.0170 -0.0024 0.0000 46 LEU B C 241 O O . LEU A 32 ? 0.3664 0.3415 0.2879 0.0163 0.0051 0.0055 46 LEU B O 242 C CB . LEU A 32 ? 0.3687 0.3435 0.3033 0.0132 -0.0186 0.0047 46 LEU B CB 243 C CG . LEU A 32 ? 0.4132 0.3809 0.3278 0.0152 -0.0275 0.0067 46 LEU B CG 244 C CD1 . LEU A 32 ? 0.4091 0.3724 0.3199 0.0134 -0.0409 0.0009 46 LEU B CD1 245 C CD2 . LEU A 32 ? 0.4692 0.4398 0.3915 0.0162 -0.0312 0.0151 46 LEU B CD2 246 N N . ILE A 33 ? 0.3752 0.3372 0.2658 0.0207 -0.0018 -0.0045 47 ILE B N 247 C CA . ILE A 33 ? 0.3892 0.3521 0.2659 0.0247 0.0106 -0.0021 47 ILE B CA 248 C C . ILE A 33 ? 0.4369 0.3930 0.2864 0.0273 0.0093 0.0016 47 ILE B C 249 O O . ILE A 33 ? 0.4667 0.4252 0.3047 0.0299 0.0207 0.0064 47 ILE B O 250 C CB . ILE A 33 ? 0.4063 0.3678 0.2792 0.0292 0.0176 -0.0099 47 ILE B CB 251 C CG1 . ILE A 33 ? 0.4279 0.3752 0.2818 0.0322 0.0086 -0.0200 47 ILE B CG1 252 C CG2 . ILE A 33 ? 0.4042 0.3731 0.3034 0.0265 0.0198 -0.0107 47 ILE B CG2 253 C CD1 . ILE A 33 ? 0.4396 0.3819 0.2866 0.0389 0.0154 -0.0286 47 ILE B CD1 254 N N . SER A 34 ? 0.4228 0.3712 0.2626 0.0264 -0.0048 0.0003 48 SER B N 255 C CA . SER A 34 ? 0.4625 0.4034 0.2762 0.0283 -0.0094 0.0052 48 SER B CA 256 C C . SER A 34 ? 0.4761 0.4140 0.2959 0.0254 -0.0276 0.0055 48 SER B C 257 O O . SER A 34 ? 0.4764 0.4208 0.3231 0.0219 -0.0328 0.0033 48 SER B O 258 C CB . SER A 34 ? 0.5010 0.4309 0.2800 0.0341 -0.0061 -0.0016 48 SER B CB 259 O OG . SER A 34 ? 0.4911 0.4101 0.2620 0.0344 -0.0195 -0.0128 48 SER B OG 260 N N . ASP A 35 ? 0.5102 0.4396 0.3065 0.0269 -0.0371 0.0091 49 ASP B N 261 C CA . ASP A 35 ? 0.5451 0.4734 0.3491 0.0245 -0.0563 0.0103 49 ASP B CA 262 C C . ASP A 35 ? 0.5496 0.4726 0.3542 0.0223 -0.0690 -0.0010 49 ASP B C 263 O O . ASP A 35 ? 0.5481 0.4747 0.3694 0.0188 -0.0845 -0.0004 49 ASP B O 264 C CB . ASP A 35 ? 0.6108 0.5300 0.3873 0.0269 -0.0653 0.0179 49 ASP B CB 265 C CG . ASP A 35 ? 0.6600 0.5639 0.3920 0.0307 -0.0654 0.0121 49 ASP B CG 266 O OD1 . ASP A 35 ? 0.6604 0.5607 0.3841 0.0325 -0.0576 0.0017 49 ASP B OD1 267 O OD2 . ASP A 35 ? 0.7246 0.6190 0.4282 0.0328 -0.0732 0.0179 49 ASP B OD2 268 N N . ARG A 36 ? 0.5499 0.4644 0.3380 0.0244 -0.0629 -0.0108 50 ARG B N 269 C CA . ARG A 36 ? 0.5356 0.4402 0.3205 0.0220 -0.0764 -0.0218 50 ARG B CA 270 C C . ARG A 36 ? 0.4914 0.3935 0.2839 0.0224 -0.0676 -0.0307 50 ARG B C 271 O O . ARG A 36 ? 0.4887 0.3791 0.2766 0.0204 -0.0787 -0.0399 50 ARG B O 272 C CB . ARG A 36 ? 0.5868 0.4725 0.3295 0.0253 -0.0880 -0.0273 50 ARG B CB 273 C CG . ARG A 36 ? 0.6192 0.4925 0.3261 0.0332 -0.0741 -0.0344 50 ARG B CG 274 C CD . ARG A 36 ? 0.6489 0.5047 0.3088 0.0375 -0.0832 -0.0368 50 ARG B CD 275 N NE . ARG A 36 ? 0.6889 0.5514 0.3445 0.0370 -0.0840 -0.0226 50 ARG B NE 276 C CZ . ARG A 36 ? 0.7155 0.5656 0.3348 0.0392 -0.0949 -0.0198 50 ARG B CZ 277 N NH1 . ARG A 36 ? 0.7636 0.5929 0.3443 0.0421 -0.1066 -0.0314 50 ARG B NH1 278 N NH2 . ARG A 36 ? 0.7166 0.5732 0.3367 0.0387 -0.0950 -0.0052 50 ARG B NH2 279 N N . TRP A 37 ? 0.4801 0.3924 0.2859 0.0246 -0.0496 -0.0275 51 TRP B N 280 C CA . TRP A 37 ? 0.4938 0.4049 0.3096 0.0256 -0.0418 -0.0344 51 TRP B CA 281 C C . TRP A 37 ? 0.4649 0.3917 0.3167 0.0210 -0.0356 -0.0285 51 TRP B C 282 O O . TRP A 37 ? 0.4124 0.3513 0.2758 0.0207 -0.0275 -0.0200 51 TRP B O 283 C CB . TRP A 37 ? 0.4769 0.3845 0.2720 0.0340 -0.0258 -0.0377 51 TRP B CB 284 C CG . TRP A 37 ? 0.5148 0.4033 0.2716 0.0402 -0.0303 -0.0474 51 TRP B CG 285 C CD1 . TRP A 37 ? 0.5675 0.4497 0.2911 0.0447 -0.0290 -0.0457 51 TRP B CD1 286 C CD2 . TRP A 37 ? 0.5363 0.4068 0.2810 0.0429 -0.0373 -0.0608 51 TRP B CD2 287 N NE1 . TRP A 37 ? 0.5982 0.4596 0.2872 0.0507 -0.0342 -0.0583 51 TRP B NE1 288 C CE2 . TRP A 37 ? 0.5761 0.4292 0.2781 0.0498 -0.0397 -0.0682 51 TRP B CE2 289 C CE3 . TRP A 37 ? 0.5268 0.3921 0.2907 0.0402 -0.0421 -0.0669 51 TRP B CE3 290 C CZ2 . TRP A 37 ? 0.6044 0.4339 0.2825 0.0546 -0.0472 -0.0832 51 TRP B CZ2 291 C CZ3 . TRP A 37 ? 0.5747 0.4166 0.3173 0.0443 -0.0497 -0.0805 51 TRP B CZ3 292 C CH2 . TRP A 37 ? 0.5991 0.4228 0.2990 0.0517 -0.0526 -0.0893 51 TRP B CH2 293 N N . VAL A 38 ? 0.4496 0.3739 0.3164 0.0175 -0.0398 -0.0332 52 VAL B N 294 C CA . VAL A 38 ? 0.4275 0.3640 0.3238 0.0134 -0.0344 -0.0287 52 VAL B CA 295 C C . VAL A 38 ? 0.4165 0.3477 0.3146 0.0158 -0.0278 -0.0339 52 VAL B C 296 O O . VAL A 38 ? 0.5192 0.4354 0.4054 0.0174 -0.0337 -0.0420 52 VAL B O 297 C CB . VAL A 38 ? 0.4139 0.3552 0.3312 0.0055 -0.0462 -0.0261 52 VAL B CB 298 C CG1 . VAL A 38 ? 0.3652 0.3168 0.3082 0.0016 -0.0397 -0.0223 52 VAL B CG1 299 C CG2 . VAL A 38 ? 0.4192 0.3691 0.3400 0.0048 -0.0513 -0.0196 52 VAL B CG2 300 N N . LEU A 39 ? 0.4314 0.3737 0.3448 0.0163 -0.0168 -0.0292 53 LEU B N 301 C CA . LEU A 39 ? 0.4434 0.3831 0.3614 0.0193 -0.0107 -0.0322 53 LEU B CA 302 C C . LEU A 39 ? 0.4086 0.3530 0.3485 0.0127 -0.0131 -0.0285 53 LEU B C 303 O O . LEU A 39 ? 0.3683 0.3240 0.3218 0.0083 -0.0121 -0.0222 53 LEU B O 304 C CB . LEU A 39 ? 0.4387 0.3881 0.3566 0.0246 0.0027 -0.0291 53 LEU B CB 305 C CG . LEU A 39 ? 0.4963 0.4469 0.4215 0.0292 0.0097 -0.0311 53 LEU B CG 306 C CD1 . LEU A 39 ? 0.4809 0.4167 0.3908 0.0365 0.0083 -0.0405 53 LEU B CD1 307 C CD2 . LEU A 39 ? 0.4738 0.4385 0.4044 0.0321 0.0216 -0.0257 53 LEU B CD2 308 N N . THR A 40 ? 0.3895 0.3238 0.3315 0.0126 -0.0163 -0.0322 54 THR B N 309 C CA . THR A 40 ? 0.3773 0.3143 0.3367 0.0063 -0.0178 -0.0275 54 THR B CA 310 C C . THR A 40 ? 0.4075 0.3333 0.3662 0.0098 -0.0176 -0.0306 54 THR B C 311 O O . THR A 40 ? 0.3728 0.2917 0.3204 0.0181 -0.0145 -0.0366 54 THR B O 312 C CB . THR A 40 ? 0.4024 0.3377 0.3698 -0.0023 -0.0281 -0.0258 54 THR B CB 313 O OG1 . THR A 40 ? 0.3704 0.3123 0.3550 -0.0088 -0.0266 -0.0190 54 THR B OG1 314 C CG2 . THR A 40 ? 0.4297 0.3460 0.3866 -0.0031 -0.0390 -0.0330 54 THR B CG2 315 N N . ALA A 41 ? 0.3863 0.3107 0.3569 0.0040 -0.0201 -0.0260 55 ALA B N 316 C CA . ALA A 41 ? 0.4160 0.3281 0.3872 0.0067 -0.0218 -0.0271 55 ALA B CA 317 C C . ALA A 41 ? 0.3865 0.2791 0.3523 0.0036 -0.0326 -0.0320 55 ALA B C 318 O O . ALA A 41 ? 0.4300 0.3227 0.3994 -0.0045 -0.0393 -0.0306 55 ALA B O 319 C CB . ALA A 41 ? 0.4001 0.3184 0.3835 0.0014 -0.0198 -0.0184 55 ALA B CB 320 N N . ALA A 42 ? 0.3914 0.2666 0.3500 0.0104 -0.0351 -0.0379 56 ALA B N 321 C CA . ALA A 42 ? 0.4392 0.2908 0.3923 0.0073 -0.0469 -0.0431 56 ALA B CA 322 C C . ALA A 42 ? 0.4109 0.2591 0.3787 -0.0052 -0.0536 -0.0339 56 ALA B C 323 O O . ALA A 42 ? 0.4076 0.2451 0.3767 -0.0136 -0.0640 -0.0349 56 ALA B O 324 C CB . ALA A 42 ? 0.4359 0.2683 0.3791 0.0190 -0.0474 -0.0513 56 ALA B CB 325 N N . HIS A 43 ? 0.4037 0.2605 0.3818 -0.0071 -0.0480 -0.0247 57 HIS B N 326 C CA . HIS A 43 ? 0.4296 0.2812 0.4189 -0.0184 -0.0528 -0.0149 57 HIS B CA 327 C C . HIS A 43 ? 0.4430 0.3100 0.4446 -0.0307 -0.0530 -0.0078 57 HIS B C 328 O O . HIS A 43 ? 0.4533 0.3158 0.4654 -0.0417 -0.0576 0.0001 57 HIS B O 329 C CB . HIS A 43 ? 0.4276 0.2809 0.4202 -0.0165 -0.0478 -0.0067 57 HIS B CB 330 C CG . HIS A 43 ? 0.4077 0.2840 0.4062 -0.0200 -0.0385 0.0017 57 HIS B CG 331 N ND1 . HIS A 43 ? 0.4029 0.2924 0.3986 -0.0121 -0.0308 0.0005 57 HIS B ND1 332 C CD2 . HIS A 43 ? 0.4335 0.3207 0.4402 -0.0302 -0.0354 0.0113 57 HIS B CD2 333 C CE1 . HIS A 43 ? 0.3850 0.2897 0.3843 -0.0172 -0.0246 0.0077 57 HIS B CE1 334 N NE2 . HIS A 43 ? 0.4595 0.3639 0.4649 -0.0273 -0.0262 0.0142 57 HIS B NE2 335 N N . CYS A 44 ? 0.4463 0.3318 0.4480 -0.0285 -0.0476 -0.0099 58 CYS B N 336 C CA A CYS A 44 ? 0.4994 0.3998 0.5133 -0.0372 -0.0490 -0.0057 58 CYS B CA 337 C CA B CYS A 44 ? 0.4709 0.3715 0.4858 -0.0377 -0.0488 -0.0050 58 CYS B CA 338 C C . CYS A 44 ? 0.4967 0.3838 0.5139 -0.0448 -0.0630 -0.0089 58 CYS B C 339 O O . CYS A 44 ? 0.4961 0.3911 0.5308 -0.0561 -0.0670 -0.0017 58 CYS B O 340 C CB A CYS A 44 ? 0.5357 0.4507 0.5444 -0.0305 -0.0441 -0.0102 58 CYS B CB 341 C CB B CYS A 44 ? 0.4642 0.3835 0.4775 -0.0324 -0.0422 -0.0072 58 CYS B CB 342 S SG A CYS A 44 ? 0.6172 0.5511 0.6279 -0.0256 -0.0294 -0.0049 58 CYS B SG 343 S SG B CYS A 44 ? 0.4662 0.4064 0.4996 -0.0414 -0.0432 -0.0005 58 CYS B SG 344 N N . LEU A 45 ? 0.4915 0.3587 0.4914 -0.0381 -0.0703 -0.0201 59 LEU B N 345 C CA . LEU A 45 ? 0.5030 0.3529 0.4988 -0.0432 -0.0858 -0.0269 59 LEU B CA 346 C C . LEU A 45 ? 0.4876 0.3082 0.4799 -0.0464 -0.0960 -0.0296 59 LEU B C 347 O O . LEU A 45 ? 0.4931 0.3011 0.4913 -0.0566 -0.1101 -0.0302 59 LEU B O 348 C CB . LEU A 45 ? 0.5255 0.3697 0.4985 -0.0325 -0.0873 -0.0391 59 LEU B CB 349 C CG . LEU A 45 ? 0.5379 0.4069 0.5111 -0.0284 -0.0783 -0.0367 59 LEU B CG 350 C CD1 . LEU A 45 ? 0.5341 0.3958 0.4815 -0.0171 -0.0773 -0.0472 59 LEU B CD1 351 C CD2 . LEU A 45 ? 0.5660 0.4504 0.5574 -0.0389 -0.0853 -0.0304 59 LEU B CD2 352 N N . LEU A 46 ? 0.5056 0.3147 0.4895 -0.0376 -0.0901 -0.0310 60 LEU B N 353 C CA . LEU A 46 ? 0.5057 0.2841 0.4851 -0.0379 -0.0995 -0.0338 60 LEU B CA 354 C C . LEU A 46 ? 0.4759 0.2557 0.4634 -0.0373 -0.0919 -0.0232 60 LEU B C 355 O O . LEU A 46 ? 0.4387 0.2229 0.4194 -0.0251 -0.0827 -0.0250 60 LEU B O 356 C CB . LEU A 46 ? 0.5519 0.3075 0.5073 -0.0234 -0.1027 -0.0501 60 LEU B CB 357 C CG . LEU A 46 ? 0.5980 0.3176 0.5466 -0.0208 -0.1129 -0.0555 60 LEU B CG 358 C CD1 . LEU A 46 ? 0.6240 0.3254 0.5820 -0.0376 -0.1298 -0.0522 60 LEU B CD1 359 C CD2 . LEU A 46 ? 0.6406 0.3393 0.5637 -0.0041 -0.1138 -0.0732 60 LEU B CD2 360 N N . TYR A 47 A 0.4907 0.2679 0.4934 -0.0511 -0.0961 -0.0110 60 TYR B N 361 C CA . TYR A 47 A 0.4963 0.2690 0.5031 -0.0520 -0.0919 0.0001 60 TYR B CA 362 C C . TYR A 47 A 0.5322 0.2881 0.5511 -0.0679 -0.1024 0.0099 60 TYR B C 363 O O . TYR A 47 A 0.5081 0.2815 0.5430 -0.0812 -0.0986 0.0230 60 TYR B O 364 C CB . TYR A 47 A 0.4790 0.2817 0.4913 -0.0512 -0.0769 0.0098 60 TYR B CB 365 C CG . TYR A 47 A 0.4861 0.2817 0.4953 -0.0476 -0.0736 0.0183 60 TYR B CG 366 C CD1 . TYR A 47 A 0.4844 0.2700 0.4832 -0.0328 -0.0733 0.0111 60 TYR B CD1 367 C CD2 . TYR A 47 A 0.4763 0.2749 0.4930 -0.0590 -0.0712 0.0341 60 TYR B CD2 368 C CE1 . TYR A 47 A 0.4887 0.2674 0.4858 -0.0292 -0.0727 0.0193 60 TYR B CE1 369 C CE2 . TYR A 47 A 0.5181 0.3077 0.5288 -0.0558 -0.0701 0.0426 60 TYR B CE2 370 C CZ . TYR A 47 A 0.5151 0.2945 0.5165 -0.0409 -0.0720 0.0350 60 TYR B CZ 371 O OH . TYR A 47 A 0.5534 0.3241 0.5501 -0.0374 -0.0730 0.0439 60 TYR B OH 372 N N . PRO A 48 B 0.5799 0.3008 0.5915 -0.0667 -0.1157 0.0034 60 PRO B N 373 C CA . PRO A 48 B 0.5945 0.2956 0.6180 -0.0832 -0.1286 0.0113 60 PRO B CA 374 C C . PRO A 48 B 0.6069 0.3141 0.6443 -0.0956 -0.1234 0.0322 60 PRO B C 375 O O . PRO A 48 B 0.5820 0.2908 0.6367 -0.1132 -0.1285 0.0429 60 PRO B O 376 C CB . PRO A 48 B 0.6551 0.3138 0.6635 -0.0749 -0.1422 -0.0009 60 PRO B CB 377 C CG . PRO A 48 B 0.6411 0.3030 0.6309 -0.0564 -0.1377 -0.0189 60 PRO B CG 378 C CD . PRO A 48 B 0.5876 0.2856 0.5801 -0.0497 -0.1198 -0.0130 60 PRO B CD 379 N N . PRO A 49 C 0.5562 0.2673 0.5862 -0.0869 -0.1138 0.0386 60 PRO B N 380 C CA . PRO A 49 C 0.5917 0.3100 0.6303 -0.0984 -0.1077 0.0590 60 PRO B CA 381 C C . PRO A 49 C 0.5871 0.3414 0.6410 -0.1101 -0.0961 0.0692 60 PRO B C 382 O O . PRO A 49 C 0.6249 0.3830 0.6907 -0.1246 -0.0935 0.0859 60 PRO B O 383 C CB . PRO A 49 C 0.5826 0.3024 0.6072 -0.0843 -0.0999 0.0608 60 PRO B CB 384 C CG . PRO A 49 C 0.6047 0.3050 0.6175 -0.0674 -0.1068 0.0434 60 PRO B CG 385 C CD . PRO A 49 C 0.5849 0.2919 0.5989 -0.0672 -0.1094 0.0289 60 PRO B CD 386 N N . TRP A 50 D 0.5539 0.3339 0.6082 -0.1035 -0.0888 0.0598 60 TRP B N 387 C CA . TRP A 50 D 0.5446 0.3581 0.6152 -0.1124 -0.0785 0.0676 60 TRP B CA 388 C C . TRP A 50 D 0.5768 0.3953 0.6645 -0.1217 -0.0883 0.0625 60 TRP B C 389 O O . TRP A 50 D 0.5478 0.3958 0.6499 -0.1250 -0.0813 0.0647 60 TRP B O 390 C CB . TRP A 50 D 0.5013 0.3407 0.5632 -0.1001 -0.0643 0.0628 60 TRP B CB 391 C CG . TRP A 50 D 0.4779 0.3169 0.5250 -0.0928 -0.0553 0.0688 60 TRP B CG 392 C CD1 . TRP A 50 D 0.5160 0.3362 0.5566 -0.0961 -0.0578 0.0796 60 TRP B CD1 393 C CD2 . TRP A 50 D 0.4969 0.3545 0.5336 -0.0818 -0.0440 0.0650 60 TRP B CD2 394 N NE1 . TRP A 50 D 0.5220 0.3484 0.5479 -0.0873 -0.0496 0.0823 60 TRP B NE1 395 C CE2 . TRP A 50 D 0.4731 0.3224 0.4969 -0.0790 -0.0411 0.0733 60 TRP B CE2 396 C CE3 . TRP A 50 D 0.4769 0.3556 0.5136 -0.0744 -0.0373 0.0559 60 TRP B CE3 397 C CZ2 . TRP A 50 D 0.5169 0.3786 0.5282 -0.0696 -0.0327 0.0716 60 TRP B CZ2 398 C CZ3 . TRP A 50 D 0.4623 0.3523 0.4874 -0.0654 -0.0281 0.0547 60 TRP B CZ3 399 C CH2 . TRP A 50 D 0.4848 0.3663 0.4975 -0.0632 -0.0264 0.0621 60 TRP B CH2 400 N N . ASP A 51 E 0.6180 0.4068 0.7046 -0.1257 -0.1057 0.0558 60 ASP B N 401 C CA . ASP A 51 E 0.7318 0.5206 0.8324 -0.1352 -0.1190 0.0502 60 ASP B CA 402 C C . ASP A 51 E 0.6783 0.4866 0.7738 -0.1252 -0.1168 0.0373 60 ASP B C 403 O O . ASP A 51 E 0.7524 0.5816 0.8663 -0.1331 -0.1193 0.0393 60 ASP B O 404 C CB . ASP A 51 E 0.7871 0.5941 0.9189 -0.1555 -0.1184 0.0677 60 ASP B CB 405 C CG . ASP A 51 E 0.8714 0.6480 1.0124 -0.1706 -0.1344 0.0740 60 ASP B CG 406 O OD1 . ASP A 51 E 0.9120 0.6621 1.0395 -0.1684 -0.1354 0.0778 60 ASP B OD1 407 O OD2 . ASP A 51 E 1.1133 0.8916 1.2758 -0.1850 -0.1473 0.0754 60 ASP B OD2 408 N N . LYS A 52 F 0.6680 0.4703 0.7396 -0.1078 -0.1119 0.0252 60 LYS B N 409 C CA . LYS A 52 F 0.6281 0.4439 0.6906 -0.0978 -0.1104 0.0131 60 LYS B CA 410 C C . LYS A 52 F 0.6229 0.4078 0.6634 -0.0896 -0.1237 -0.0037 60 LYS B C 411 O O . LYS A 52 F 0.6008 0.3660 0.6234 -0.0781 -0.1218 -0.0102 60 LYS B O 412 C CB . LYS A 52 F 0.6178 0.4538 0.6708 -0.0847 -0.0928 0.0132 60 LYS B CB 413 C CG . LYS A 52 F 0.6783 0.5450 0.7486 -0.0906 -0.0789 0.0270 60 LYS B CG 414 C CD . LYS A 52 F 0.7120 0.5912 0.7697 -0.0781 -0.0641 0.0264 60 LYS B CD 415 C CE . LYS A 52 F 0.7644 0.6689 0.8342 -0.0829 -0.0502 0.0390 60 LYS B CE 416 N NZ . LYS A 52 F 0.7291 0.6591 0.8169 -0.0870 -0.0474 0.0407 60 LYS B NZ 417 N N . ASN A 53 G 0.6611 0.4415 0.7036 -0.0956 -0.1378 -0.0106 60 ASN B N 418 C CA . ASN A 53 G 0.7235 0.4785 0.7402 -0.0862 -0.1493 -0.0286 60 ASN B CA 419 C C . ASN A 53 G 0.6691 0.4377 0.6894 -0.0909 -0.1584 -0.0326 60 ASN B C 420 O O . ASN A 53 G 0.6838 0.4367 0.7074 -0.1012 -0.1774 -0.0365 60 ASN B O 421 C CB . ASN A 53 G 0.8412 0.5552 0.8503 -0.0905 -0.1656 -0.0344 60 ASN B CB 422 C CG . ASN A 53 G 0.9735 0.6577 0.9493 -0.0762 -0.1736 -0.0550 60 ASN B CG 423 O OD1 . ASN A 53 G 0.9260 0.6210 0.8843 -0.0647 -0.1677 -0.0640 60 ASN B OD1 424 N ND2 . ASN A 53 G 1.0697 0.7143 1.0355 -0.0766 -0.1867 -0.0621 60 ASN B ND2 425 N N . PHE A 54 H 0.6796 0.4770 0.6997 -0.0837 -0.1461 -0.0311 60 PHE B N 426 C CA . PHE A 54 H 0.6538 0.4689 0.6819 -0.0882 -0.1536 -0.0314 60 PHE B CA 427 C C . PHE A 54 H 0.7071 0.5016 0.7034 -0.0793 -0.1651 -0.0479 60 PHE B C 428 O O . PHE A 54 H 0.7167 0.4965 0.6848 -0.0649 -0.1579 -0.0579 60 PHE B O 429 C CB . PHE A 54 H 0.5740 0.4253 0.6141 -0.0835 -0.1366 -0.0230 60 PHE B CB 430 C CG . PHE A 54 H 0.5402 0.4135 0.6092 -0.0920 -0.1251 -0.0073 60 PHE B CG 431 C CD1 . PHE A 54 H 0.5897 0.4761 0.6899 -0.1076 -0.1324 0.0030 60 PHE B CD1 432 C CD2 . PHE A 54 H 0.5378 0.4200 0.6028 -0.0844 -0.1067 -0.0026 60 PHE B CD2 433 C CE1 . PHE A 54 H 0.5739 0.4815 0.6988 -0.1147 -0.1194 0.0180 60 PHE B CE1 434 C CE2 . PHE A 54 H 0.5264 0.4270 0.6128 -0.0914 -0.0957 0.0113 60 PHE B CE2 435 C CZ . PHE A 54 H 0.5555 0.4690 0.6710 -0.1062 -0.1009 0.0217 60 PHE B CZ 436 N N . THR A 55 I 0.7288 0.5226 0.7302 -0.0881 -0.1832 -0.0501 60 THR B N 437 C CA . THR A 55 I 0.7710 0.5497 0.7411 -0.0805 -0.1945 -0.0640 60 THR B CA 438 C C . THR A 55 I 0.7236 0.5331 0.6985 -0.0764 -0.1882 -0.0588 60 THR B C 439 O O . THR A 55 I 0.6566 0.4970 0.6614 -0.0806 -0.1777 -0.0456 60 THR B O 440 C CB . THR A 55 I 0.8119 0.5676 0.7816 -0.0928 -0.2220 -0.0704 60 THR B CB 441 O OG1 . THR A 55 I 0.8170 0.5982 0.8281 -0.1093 -0.2302 -0.0567 60 THR B OG1 442 C CG2 . THR A 55 I 0.9035 0.6230 0.8649 -0.0958 -0.2296 -0.0770 60 THR B CG2 443 N N . GLU A 56 ? 0.7203 0.5190 0.6635 -0.0678 -0.1949 -0.0694 61 GLU B N 444 C CA . GLU A 56 ? 0.7103 0.5320 0.6521 -0.0630 -0.1918 -0.0653 61 GLU B CA 445 C C . GLU A 56 ? 0.6837 0.5321 0.6659 -0.0762 -0.2015 -0.0530 61 GLU B C 446 O O . GLU A 56 ? 0.6353 0.5127 0.6356 -0.0735 -0.1905 -0.0434 61 GLU B O 447 C CB . GLU A 56 ? 0.8147 0.6144 0.7144 -0.0554 -0.2043 -0.0785 61 GLU B CB 448 C CG . GLU A 56 ? 0.8357 0.6145 0.6946 -0.0396 -0.1910 -0.0901 61 GLU B CG 449 C CD . GLU A 56 ? 0.8508 0.5991 0.6988 -0.0386 -0.1934 -0.1003 61 GLU B CD 450 O OE1 . GLU A 56 ? 0.8918 0.6250 0.7532 -0.0508 -0.2112 -0.1017 61 GLU B OE1 451 O OE2 . GLU A 56 ? 0.7915 0.5303 0.6187 -0.0253 -0.1778 -0.1066 61 GLU B OE2 452 N N . ASN A 57 ? 0.6838 0.5223 0.6821 -0.0902 -0.2220 -0.0533 62 ASN B N 453 C CA . ASN A 57 ? 0.7129 0.5773 0.7521 -0.1033 -0.2339 -0.0420 62 ASN B CA 454 C C . ASN A 57 ? 0.6691 0.5645 0.7541 -0.1111 -0.2189 -0.0260 62 ASN B C 455 O O . ASN A 57 ? 0.6089 0.5320 0.7306 -0.1193 -0.2243 -0.0156 62 ASN B O 456 C CB . ASN A 57 ? 0.8466 0.6898 0.8885 -0.1170 -0.2633 -0.0477 62 ASN B CB 457 C CG . ASN A 57 ? 0.9679 0.7965 0.9783 -0.1126 -0.2835 -0.0582 62 ASN B CG 458 O OD1 . ASN A 57 ? 1.0797 0.8831 1.0428 -0.0998 -0.2812 -0.0712 62 ASN B OD1 459 N ND2 . ASN A 57 ? 1.0352 0.8806 1.0719 -0.1227 -0.3034 -0.0521 62 ASN B ND2 460 N N . ASP A 58 ? 0.6298 0.5216 0.7130 -0.1080 -0.2001 -0.0236 63 ASP B N 461 C CA . ASP A 58 ? 0.5913 0.5096 0.7120 -0.1151 -0.1851 -0.0086 63 ASP B CA 462 C C . ASP A 58 ? 0.5788 0.5265 0.7060 -0.1044 -0.1642 -0.0022 63 ASP B C 463 O O . ASP A 58 ? 0.5314 0.5056 0.6899 -0.1087 -0.1519 0.0099 63 ASP B O 464 C CB . ASP A 58 ? 0.5950 0.4944 0.7087 -0.1168 -0.1757 -0.0080 63 ASP B CB 465 C CG . ASP A 58 ? 0.6722 0.5398 0.7821 -0.1281 -0.1960 -0.0134 63 ASP B CG 466 O OD1 . ASP A 58 ? 0.6266 0.4986 0.7606 -0.1422 -0.2142 -0.0096 63 ASP B OD1 467 O OD2 . ASP A 58 ? 0.6741 0.5121 0.7586 -0.1227 -0.1942 -0.0212 63 ASP B OD2 468 N N . LEU A 59 ? 0.5646 0.5065 0.6616 -0.0905 -0.1601 -0.0104 64 LEU B N 469 C CA . LEU A 59 ? 0.5444 0.5046 0.6393 -0.0792 -0.1393 -0.0065 64 LEU B CA 470 C C . LEU A 59 ? 0.5021 0.4747 0.5928 -0.0717 -0.1428 -0.0069 64 LEU B C 471 O O . LEU A 59 ? 0.4822 0.4426 0.5568 -0.0714 -0.1599 -0.0133 64 LEU B O 472 C CB . LEU A 59 ? 0.5824 0.5230 0.6441 -0.0686 -0.1272 -0.0142 64 LEU B CB 473 C CG . LEU A 59 ? 0.6552 0.5762 0.7128 -0.0731 -0.1261 -0.0158 64 LEU B CG 474 C CD1 . LEU A 59 ? 0.7214 0.6213 0.7449 -0.0609 -0.1189 -0.0258 64 LEU B CD1 475 C CD2 . LEU A 59 ? 0.6676 0.6072 0.7514 -0.0784 -0.1119 -0.0037 64 LEU B CD2 476 N N . LEU A 60 ? 0.4398 0.4343 0.5425 -0.0652 -0.1267 -0.0003 65 LEU B N 477 C CA . LEU A 60 ? 0.4868 0.4875 0.5779 -0.0550 -0.1258 -0.0011 65 LEU B CA 478 C C . LEU A 60 ? 0.4465 0.4512 0.5270 -0.0451 -0.1046 -0.0001 65 LEU B C 479 O O . LEU A 60 ? 0.4144 0.4226 0.5022 -0.0461 -0.0907 0.0025 65 LEU B O 480 C CB . LEU A 60 ? 0.5234 0.5487 0.6467 -0.0577 -0.1343 0.0068 65 LEU B CB 481 C CG . LEU A 60 ? 0.5495 0.6015 0.7152 -0.0638 -0.1251 0.0170 65 LEU B CG 482 C CD1 . LEU A 60 ? 0.5739 0.6420 0.7451 -0.0535 -0.1046 0.0213 65 LEU B CD1 483 C CD2 . LEU A 60 ? 0.4904 0.5611 0.6908 -0.0717 -0.1423 0.0231 65 LEU B CD2 484 N N . VAL A 61 ? 0.4237 0.4261 0.4856 -0.0359 -0.1034 -0.0019 66 VAL B N 485 C CA . VAL A 61 ? 0.4569 0.4624 0.5097 -0.0273 -0.0859 -0.0008 66 VAL B CA 486 C C . VAL A 61 ? 0.4293 0.4541 0.5014 -0.0229 -0.0834 0.0062 66 VAL B C 487 O O . VAL A 61 ? 0.3570 0.3861 0.4342 -0.0224 -0.0966 0.0082 66 VAL B O 488 C CB . VAL A 61 ? 0.5074 0.4939 0.5235 -0.0202 -0.0836 -0.0074 66 VAL B CB 489 C CG1 . VAL A 61 ? 0.6492 0.6161 0.6476 -0.0230 -0.0880 -0.0154 66 VAL B CG1 490 C CG2 . VAL A 61 ? 0.5673 0.5502 0.5679 -0.0162 -0.0944 -0.0074 66 VAL B CG2 491 N N . ARG A 62 ? 0.3576 0.3926 0.4404 -0.0193 -0.0675 0.0095 67 ARG B N 492 C CA . ARG A 62 ? 0.3506 0.4013 0.4508 -0.0133 -0.0631 0.0149 67 ARG B CA 493 C C . ARG A 62 ? 0.3418 0.3843 0.4229 -0.0055 -0.0513 0.0135 67 ARG B C 494 O O . ARG A 62 ? 0.3158 0.3540 0.3897 -0.0055 -0.0394 0.0115 67 ARG B O 495 C CB . ARG A 62 ? 0.3553 0.4265 0.4878 -0.0160 -0.0549 0.0200 67 ARG B CB 496 C CG . ARG A 62 ? 0.3514 0.4319 0.5063 -0.0260 -0.0661 0.0229 67 ARG B CG 497 C CD . ARG A 62 ? 0.3441 0.4459 0.5301 -0.0295 -0.0548 0.0292 67 ARG B CD 498 N NE . ARG A 62 ? 0.3452 0.4672 0.5537 -0.0213 -0.0482 0.0337 67 ARG B NE 499 C CZ . ARG A 62 ? 0.3913 0.5353 0.6279 -0.0212 -0.0360 0.0394 67 ARG B CZ 500 N NH1 . ARG A 62 ? 0.3546 0.5157 0.6108 -0.0114 -0.0299 0.0421 67 ARG B NH1 501 N NH2 . ARG A 62 ? 0.4016 0.5502 0.6466 -0.0304 -0.0293 0.0427 67 ARG B NH2 502 N N . ILE A 63 ? 0.3338 0.3737 0.4075 0.0005 -0.0557 0.0155 68 ILE B N 503 C CA . ILE A 63 ? 0.3391 0.3679 0.3919 0.0061 -0.0477 0.0149 68 ILE B CA 504 C C . ILE A 63 ? 0.3265 0.3622 0.3926 0.0131 -0.0444 0.0196 68 ILE B C 505 O O . ILE A 63 ? 0.3322 0.3770 0.4144 0.0154 -0.0537 0.0235 68 ILE B O 506 C CB . ILE A 63 ? 0.3773 0.3915 0.4023 0.0067 -0.0566 0.0135 68 ILE B CB 507 C CG1 . ILE A 63 ? 0.3909 0.3973 0.4048 0.0009 -0.0631 0.0076 68 ILE B CG1 508 C CG2 . ILE A 63 ? 0.3827 0.3864 0.3868 0.0105 -0.0467 0.0138 68 ILE B CG2 509 C CD1 . ILE A 63 ? 0.4641 0.4562 0.4494 0.0020 -0.0737 0.0050 68 ILE B CD1 510 N N . GLY A 64 ? 0.3005 0.3309 0.3605 0.0167 -0.0327 0.0190 69 GLY B N 511 C CA . GLY A 64 ? 0.3124 0.3445 0.3825 0.0241 -0.0296 0.0223 69 GLY B CA 512 C C . GLY A 64 ? 0.3320 0.3771 0.4247 0.0268 -0.0205 0.0212 69 GLY B C 513 O O . GLY A 64 ? 0.3440 0.3933 0.4504 0.0344 -0.0187 0.0230 69 GLY B O 514 N N . LYS A 65 ? 0.3019 0.3523 0.3974 0.0214 -0.0141 0.0183 70 LYS B N 515 C CA . LYS A 65 ? 0.3111 0.3762 0.4273 0.0234 -0.0048 0.0184 70 LYS B CA 516 C C . LYS A 65 ? 0.2960 0.3537 0.4028 0.0275 0.0080 0.0147 70 LYS B C 517 O O . LYS A 65 ? 0.2849 0.3279 0.3711 0.0256 0.0099 0.0119 70 LYS B O 518 C CB . LYS A 65 ? 0.2889 0.3637 0.4140 0.0147 -0.0046 0.0190 70 LYS B CB 519 C CG . LYS A 65 ? 0.3080 0.3945 0.4516 0.0108 -0.0176 0.0229 70 LYS B CG 520 C CD . LYS A 65 ? 0.3384 0.4357 0.4967 0.0015 -0.0168 0.0249 70 LYS B CD 521 C CE . LYS A 65 ? 0.3205 0.4367 0.5018 0.0037 -0.0030 0.0282 70 LYS B CE 522 N NZ . LYS A 65 ? 0.3035 0.4349 0.5073 0.0135 -0.0013 0.0308 70 LYS B NZ 523 N N . HIS A 66 ? 0.2676 0.3366 0.3905 0.0332 0.0167 0.0145 71 HIS B N 524 C CA . HIS A 66 ? 0.2961 0.3586 0.4092 0.0373 0.0290 0.0100 71 HIS B CA 525 C C . HIS A 66 ? 0.2781 0.3565 0.4027 0.0356 0.0396 0.0109 71 HIS B C 526 O O . HIS A 66 ? 0.2763 0.3493 0.3863 0.0307 0.0456 0.0092 71 HIS B O 527 C CB . HIS A 66 ? 0.3098 0.3663 0.4262 0.0487 0.0308 0.0080 71 HIS B CB 528 C CG . HIS A 66 ? 0.3596 0.4041 0.4613 0.0534 0.0412 0.0016 71 HIS B CG 529 N ND1 . HIS A 66 ? 0.3546 0.3803 0.4326 0.0489 0.0401 -0.0021 71 HIS B ND1 530 C CD2 . HIS A 66 ? 0.3542 0.4025 0.4608 0.0625 0.0524 -0.0024 71 HIS B CD2 531 C CE1 . HIS A 66 ? 0.3916 0.4084 0.4593 0.0541 0.0483 -0.0082 71 HIS B CE1 532 N NE2 . HIS A 66 ? 0.3848 0.4139 0.4674 0.0629 0.0565 -0.0090 71 HIS B NE2 533 N N . SER A 67 ? 0.2754 0.3740 0.4271 0.0397 0.0420 0.0147 72 SER B N 534 C CA . SER A 67 ? 0.2954 0.4127 0.4623 0.0372 0.0529 0.0179 72 SER B CA 535 C C . SER A 67 ? 0.2986 0.4183 0.4651 0.0236 0.0472 0.0221 72 SER B C 536 O O . SER A 67 ? 0.2932 0.4106 0.4627 0.0179 0.0332 0.0238 72 SER B O 537 C CB . SER A 67 ? 0.2910 0.4327 0.4928 0.0436 0.0549 0.0224 72 SER B CB 538 O OG . SER A 67 ? 0.2977 0.4602 0.5172 0.0389 0.0653 0.0276 72 SER B OG 539 N N . ARG A 68 ? 0.2780 0.3997 0.4377 0.0187 0.0576 0.0234 73 ARG B N 540 C CA . ARG A 68 ? 0.3101 0.4327 0.4712 0.0059 0.0525 0.0282 73 ARG B CA 541 C C . ARG A 68 ? 0.3220 0.4673 0.5173 0.0004 0.0483 0.0357 73 ARG B C 542 O O . ARG A 68 ? 0.3650 0.5074 0.5647 -0.0092 0.0356 0.0380 73 ARG B O 543 C CB . ARG A 68 ? 0.3343 0.4534 0.4802 0.0023 0.0648 0.0297 73 ARG B CB 544 C CG . ARG A 68 ? 0.3567 0.4740 0.5036 -0.0107 0.0599 0.0356 73 ARG B CG 545 C CD . ARG A 68 ? 0.3813 0.4934 0.5106 -0.0138 0.0715 0.0384 73 ARG B CD 546 N NE . ARG A 68 ? 0.4247 0.5551 0.5642 -0.0100 0.0889 0.0430 73 ARG B NE 547 C CZ . ARG A 68 ? 0.4420 0.5921 0.6045 -0.0170 0.0960 0.0531 73 ARG B CZ 548 N NH1 . ARG A 68 ? 0.4471 0.5997 0.6258 -0.0294 0.0855 0.0598 73 ARG B NH1 549 N NH2 . ARG A 68 ? 0.4590 0.6261 0.6280 -0.0116 0.1144 0.0566 73 ARG B NH2 550 N N . THR A 69 ? 0.3030 0.4707 0.5231 0.0065 0.0591 0.0393 74 THR B N 551 C CA . THR A 69 ? 0.3317 0.5258 0.5891 -0.0002 0.0583 0.0484 74 THR B CA 552 C C . THR A 69 ? 0.3340 0.5447 0.6219 0.0054 0.0482 0.0501 74 THR B C 553 O O . THR A 69 ? 0.3152 0.5404 0.6301 -0.0035 0.0371 0.0564 74 THR B O 554 C CB . THR A 69 ? 0.3442 0.5582 0.6142 0.0014 0.0796 0.0541 74 THR B CB 555 O OG1 . THR A 69 ? 0.3478 0.5673 0.6179 0.0174 0.0922 0.0491 74 THR B OG1 556 C CG2 . THR A 69 ? 0.3692 0.5668 0.6087 -0.0053 0.0878 0.0544 74 THR B CG2 557 N N . ARG A 70 ? 0.2616 0.4691 0.5457 0.0196 0.0508 0.0449 75 ARG B N 558 C CA . ARG A 70 ? 0.2716 0.4932 0.5835 0.0267 0.0405 0.0470 75 ARG B CA 559 C C . ARG A 70 ? 0.2576 0.4645 0.5604 0.0212 0.0173 0.0460 75 ARG B C 560 O O . ARG A 70 ? 0.2627 0.4432 0.5308 0.0197 0.0122 0.0403 75 ARG B O 561 C CB . ARG A 70 ? 0.3183 0.5355 0.6254 0.0443 0.0492 0.0415 75 ARG B CB 562 C CG . ARG A 70 ? 0.3648 0.6011 0.6875 0.0540 0.0717 0.0420 75 ARG B CG 563 C CD . ARG A 70 ? 0.3814 0.6543 0.7543 0.0560 0.0725 0.0507 75 ARG B CD 564 N NE . ARG A 70 ? 0.4148 0.7096 0.8057 0.0675 0.0961 0.0515 75 ARG B NE 565 C CZ . ARG A 70 ? 0.3820 0.7052 0.7985 0.0618 0.1103 0.0596 75 ARG B CZ 566 N NH1 . ARG A 70 ? 0.3444 0.6763 0.7727 0.0433 0.1021 0.0681 75 ARG B NH1 567 N NH2 . ARG A 70 ? 0.4000 0.7423 0.8298 0.0747 0.1334 0.0595 75 ARG B NH2 568 N N . TYR A 71 ? 0.2532 0.4781 0.5874 0.0184 0.0032 0.0518 76 TYR B N 569 C CA . TYR A 71 ? 0.2657 0.4779 0.5914 0.0179 -0.0188 0.0507 76 TYR B CA 570 C C . TYR A 71 ? 0.2574 0.4635 0.5787 0.0334 -0.0183 0.0484 76 TYR B C 571 O O . TYR A 71 ? 0.2422 0.4688 0.5935 0.0435 -0.0120 0.0516 76 TYR B O 572 C CB . TYR A 71 ? 0.2536 0.4867 0.6146 0.0105 -0.0362 0.0577 76 TYR B CB 573 C CG . TYR A 71 ? 0.2750 0.4933 0.6225 0.0110 -0.0597 0.0565 76 TYR B CG 574 C CD1 . TYR A 71 ? 0.3303 0.5212 0.6402 0.0032 -0.0706 0.0513 76 TYR B CD1 575 C CD2 . TYR A 71 ? 0.3020 0.5328 0.6722 0.0206 -0.0703 0.0606 76 TYR B CD2 576 C CE1 . TYR A 71 ? 0.3598 0.5362 0.6526 0.0043 -0.0905 0.0502 76 TYR B CE1 577 C CE2 . TYR A 71 ? 0.3204 0.5360 0.6740 0.0211 -0.0921 0.0604 76 TYR B CE2 578 C CZ . TYR A 71 ? 0.3569 0.5451 0.6702 0.0126 -0.1016 0.0552 76 TYR B CZ 579 O OH . TYR A 71 ? 0.3959 0.5679 0.6877 0.0133 -0.1216 0.0549 76 TYR B OH 580 N N . GLU A 72 ? 0.2480 0.4263 0.5336 0.0353 -0.0248 0.0436 77 GLU B N 581 C CA . GLU A 72 ? 0.2757 0.4419 0.5514 0.0488 -0.0236 0.0416 77 GLU B CA 582 C C . GLU A 72 ? 0.2718 0.4324 0.5472 0.0507 -0.0447 0.0455 77 GLU B C 583 O O . GLU A 72 ? 0.2587 0.3965 0.5020 0.0473 -0.0536 0.0438 77 GLU B O 584 C CB . GLU A 72 ? 0.3055 0.4448 0.5421 0.0489 -0.0143 0.0349 77 GLU B CB 585 C CG . GLU A 72 ? 0.3047 0.4477 0.5394 0.0501 0.0060 0.0310 77 GLU B CG 586 C CD . GLU A 72 ? 0.2886 0.4080 0.4870 0.0456 0.0119 0.0252 77 GLU B CD 587 O OE1 . GLU A 72 ? 0.3141 0.4238 0.5006 0.0526 0.0233 0.0204 77 GLU B OE1 588 O OE2 . GLU A 72 ? 0.3163 0.4266 0.4983 0.0354 0.0054 0.0248 77 GLU B OE2 589 N N . ARG A 73 A 0.2929 0.4756 0.6046 0.0566 -0.0522 0.0513 77 ARG B N 590 C CA . ARG A 73 A 0.3450 0.5261 0.6610 0.0583 -0.0746 0.0565 77 ARG B CA 591 C C . ARG A 73 A 0.3857 0.5401 0.6724 0.0673 -0.0779 0.0558 77 ARG B C 592 O O . ARG A 73 A 0.3576 0.5055 0.6428 0.0779 -0.0647 0.0534 77 ARG B O 593 C CB . ARG A 73 A 0.3646 0.5774 0.7308 0.0651 -0.0801 0.0633 77 ARG B CB 594 C CG . ARG A 73 A 0.4303 0.6422 0.8038 0.0697 -0.1042 0.0696 77 ARG B CG 595 C CD . ARG A 73 A 0.5043 0.7513 0.9296 0.0690 -0.1155 0.0769 77 ARG B CD 596 N NE . ARG A 73 A 0.5445 0.7951 0.9852 0.0781 -0.1363 0.0838 77 ARG B NE 597 C CZ . ARG A 73 A 0.6256 0.9056 1.1116 0.0778 -0.1521 0.0913 77 ARG B CZ 598 N NH1 . ARG A 73 A 0.5341 0.8433 1.0557 0.0676 -0.1487 0.0933 77 ARG B NH1 599 N NH2 . ARG A 73 A 0.6975 0.9779 1.1941 0.0871 -0.1723 0.0979 77 ARG B NH2 600 N N . ASN A 74 ? 0.4246 0.5623 0.6864 0.0626 -0.0955 0.0580 78 ASN B N 601 C CA . ASN A 74 ? 0.5032 0.6155 0.7361 0.0690 -0.1003 0.0600 78 ASN B CA 602 C C . ASN A 74 ? 0.4682 0.5572 0.6660 0.0666 -0.0854 0.0543 78 ASN B C 603 O O . ASN A 74 ? 0.5139 0.5821 0.6898 0.0710 -0.0867 0.0566 78 ASN B O 604 C CB . ASN A 74 ? 0.5471 0.6640 0.8036 0.0844 -0.1014 0.0648 78 ASN B CB 605 C CG . ASN A 74 ? 0.6363 0.7718 0.9231 0.0881 -0.1213 0.0725 78 ASN B CG 606 O OD1 . ASN A 74 ? 0.8324 0.9634 1.1059 0.0807 -0.1404 0.0760 78 ASN B OD1 607 N ND2 . ASN A 74 ? 0.6131 0.7697 0.9408 0.1002 -0.1175 0.0751 78 ASN B ND2 608 N N . ILE A 75 ? 0.4095 0.5024 0.6038 0.0593 -0.0721 0.0480 79 ILE B N 609 C CA . ILE A 75 ? 0.4161 0.4902 0.5809 0.0561 -0.0591 0.0426 79 ILE B CA 610 C C . ILE A 75 ? 0.4109 0.4814 0.5570 0.0438 -0.0608 0.0392 79 ILE B C 611 O O . ILE A 75 ? 0.3898 0.4422 0.5052 0.0401 -0.0633 0.0384 79 ILE B O 612 C CB . ILE A 75 ? 0.4638 0.5435 0.6406 0.0610 -0.0406 0.0377 79 ILE B CB 613 C CG1 . ILE A 75 ? 0.5483 0.6276 0.7412 0.0752 -0.0388 0.0396 79 ILE B CG1 614 C CG2 . ILE A 75 ? 0.4651 0.5265 0.6130 0.0563 -0.0297 0.0322 79 ILE B CG2 615 C CD1 . ILE A 75 ? 0.5260 0.6142 0.7344 0.0826 -0.0215 0.0342 79 ILE B CD1 616 N N . GLU A 76 ? 0.3481 0.4354 0.5130 0.0379 -0.0592 0.0376 80 GLU B N 617 C CA . GLU A 76 ? 0.3555 0.4367 0.5032 0.0269 -0.0618 0.0339 80 GLU B CA 618 C C . GLU A 76 ? 0.3354 0.4142 0.4773 0.0223 -0.0814 0.0358 80 GLU B C 619 O O . GLU A 76 ? 0.3043 0.3937 0.4654 0.0254 -0.0941 0.0409 80 GLU B O 620 C CB . GLU A 76 ? 0.3878 0.4831 0.5534 0.0209 -0.0522 0.0319 80 GLU B CB 621 C CG . GLU A 76 ? 0.3798 0.4981 0.5802 0.0171 -0.0600 0.0362 80 GLU B CG 622 C CD . GLU A 76 ? 0.3792 0.5068 0.5904 0.0085 -0.0506 0.0354 80 GLU B CD 623 O OE1 . GLU A 76 ? 0.3432 0.4616 0.5420 -0.0013 -0.0577 0.0332 80 GLU B OE1 624 O OE2 . GLU A 76 ? 0.3643 0.5066 0.5944 0.0123 -0.0357 0.0370 80 GLU B OE2 625 N N . LYS A 77 ? 0.3767 0.4409 0.4915 0.0153 -0.0843 0.0313 81 LYS B N 626 C CA . LYS A 77 ? 0.3842 0.4416 0.4864 0.0101 -0.1028 0.0306 81 LYS B CA 627 C C . LYS A 77 ? 0.3626 0.4176 0.4623 0.0004 -0.1026 0.0248 81 LYS B C 628 O O . LYS A 77 ? 0.3359 0.3843 0.4247 -0.0010 -0.0887 0.0208 81 LYS B O 629 C CB . LYS A 77 ? 0.4306 0.4663 0.4932 0.0130 -0.1066 0.0298 81 LYS B CB 630 C CG . LYS A 77 ? 0.4888 0.5214 0.5485 0.0218 -0.1065 0.0366 81 LYS B CG 631 C CD . LYS A 77 ? 0.5746 0.6164 0.6520 0.0249 -0.1247 0.0429 81 LYS B CD 632 C CE . LYS A 77 ? 0.6199 0.6562 0.6948 0.0344 -0.1245 0.0503 81 LYS B CE 633 N NZ . LYS A 77 ? 0.6399 0.6910 0.7447 0.0394 -0.1397 0.0568 81 LYS B NZ 634 N N . ILE A 78 ? 0.3870 0.4462 0.4971 -0.0063 -0.1195 0.0247 82 ILE B N 635 C CA . ILE A 78 ? 0.3970 0.4518 0.5073 -0.0164 -0.1227 0.0199 82 ILE B CA 636 C C . ILE A 78 ? 0.4114 0.4449 0.4894 -0.0192 -0.1397 0.0140 82 ILE B C 637 O O . ILE A 78 ? 0.4214 0.4544 0.4967 -0.0181 -0.1567 0.0162 82 ILE B O 638 C CB . ILE A 78 ? 0.4374 0.5147 0.5904 -0.0241 -0.1300 0.0248 82 ILE B CB 639 C CG1 . ILE A 78 ? 0.4190 0.5173 0.6016 -0.0213 -0.1103 0.0298 82 ILE B CG1 640 C CG2 . ILE A 78 ? 0.4612 0.5290 0.6119 -0.0361 -0.1384 0.0204 82 ILE B CG2 641 C CD1 . ILE A 78 ? 0.4655 0.5762 0.6610 -0.0099 -0.1051 0.0346 82 ILE B CD1 642 N N . SER A 79 ? 0.4655 0.4806 0.5181 -0.0220 -0.1354 0.0063 83 SER B N 643 C CA . SER A 79 ? 0.4927 0.4852 0.5120 -0.0239 -0.1503 -0.0013 83 SER B CA 644 C C . SER A 79 ? 0.4986 0.4813 0.5202 -0.0329 -0.1547 -0.0077 83 SER B C 645 O O . SER A 79 ? 0.4282 0.4165 0.4655 -0.0358 -0.1413 -0.0068 83 SER B O 646 C CB . SER A 79 ? 0.5282 0.5028 0.5062 -0.0155 -0.1398 -0.0055 83 SER B CB 647 O OG . SER A 79 ? 0.5700 0.5223 0.5122 -0.0157 -0.1532 -0.0135 83 SER B OG 648 N N . MET A 80 ? 0.5230 0.4890 0.5270 -0.0374 -0.1747 -0.0141 84 MET B N 649 C CA . MET A 80 ? 0.5794 0.5281 0.5778 -0.0452 -0.1817 -0.0221 84 MET B CA 650 C C . MET A 80 ? 0.5627 0.4853 0.5166 -0.0375 -0.1733 -0.0325 84 MET B C 651 O O . MET A 80 ? 0.5874 0.5059 0.5145 -0.0279 -0.1658 -0.0331 84 MET B O 652 C CB . MET A 80 ? 0.6823 0.6230 0.6827 -0.0540 -0.2098 -0.0251 84 MET B CB 653 C CG . MET A 80 ? 0.7719 0.7408 0.8188 -0.0614 -0.2212 -0.0143 84 MET B CG 654 S SD . MET A 80 ? 0.9557 0.9501 1.0556 -0.0710 -0.2076 -0.0051 84 MET B SD 655 C CE . MET A 80 ? 0.9716 0.9982 1.1216 -0.0779 -0.2250 0.0062 84 MET B CE 656 N N . LEU A 81 ? 0.5375 0.4423 0.4844 -0.0415 -0.1747 -0.0402 85 LEU B N 657 C CA . LEU A 81 ? 0.5756 0.4560 0.4832 -0.0330 -0.1667 -0.0510 85 LEU B CA 658 C C . LEU A 81 ? 0.5932 0.4444 0.4659 -0.0332 -0.1861 -0.0635 85 LEU B C 659 O O . LEU A 81 ? 0.5919 0.4344 0.4751 -0.0434 -0.2060 -0.0663 85 LEU B O 660 C CB . LEU A 81 ? 0.5698 0.4463 0.4891 -0.0346 -0.1543 -0.0523 85 LEU B CB 661 C CG . LEU A 81 ? 0.5464 0.4485 0.4975 -0.0354 -0.1364 -0.0411 85 LEU B CG 662 C CD1 . LEU A 81 ? 0.5611 0.4552 0.5197 -0.0378 -0.1283 -0.0424 85 LEU B CD1 663 C CD2 . LEU A 81 ? 0.5928 0.5053 0.5320 -0.0248 -0.1200 -0.0380 85 LEU B CD2 664 N N . GLU A 82 ? 0.6193 0.4548 0.4497 -0.0218 -0.1796 -0.0710 86 GLU B N 665 C CA . GLU A 82 ? 0.6866 0.4904 0.4753 -0.0189 -0.1939 -0.0852 86 GLU B CA 666 C C . GLU A 82 ? 0.7074 0.4899 0.4868 -0.0161 -0.1875 -0.0959 86 GLU B C 667 O O . GLU A 82 ? 0.6704 0.4270 0.4363 -0.0202 -0.2049 -0.1067 86 GLU B O 668 C CB . GLU A 82 ? 0.7694 0.5664 0.5145 -0.0067 -0.1869 -0.0879 86 GLU B CB 669 C CG . GLU A 82 ? 0.8826 0.6484 0.5805 -0.0039 -0.2052 -0.1015 86 GLU B CG 670 C CD . GLU A 82 ? 1.0528 0.8216 0.7489 -0.0105 -0.2295 -0.0968 86 GLU B CD 671 O OE1 . GLU A 82 ? 1.0310 0.8132 0.7191 -0.0058 -0.2247 -0.0876 86 GLU B OE1 672 O OE2 . GLU A 82 ? 1.1608 0.9181 0.8648 -0.0207 -0.2546 -0.1019 86 GLU B OE2 673 N N . LYS A 83 ? 0.7000 0.4919 0.4864 -0.0089 -0.1639 -0.0931 87 LYS B N 674 C CA . LYS A 83 ? 0.7185 0.4907 0.4960 -0.0039 -0.1568 -0.1026 87 LYS B CA 675 C C . LYS A 83 ? 0.6249 0.4162 0.4280 -0.0009 -0.1349 -0.0944 87 LYS B C 676 O O . LYS A 83 ? 0.5391 0.3531 0.3498 0.0028 -0.1202 -0.0854 87 LYS B O 677 C CB . LYS A 83 ? 0.8467 0.5948 0.5752 0.0102 -0.1524 -0.1166 87 LYS B CB 678 C CG . LYS A 83 ? 0.9802 0.7022 0.6961 0.0170 -0.1493 -0.1293 87 LYS B CG 679 C CD . LYS A 83 ? 1.0784 0.7734 0.7963 0.0069 -0.1737 -0.1376 87 LYS B CD 680 C CE . LYS A 83 ? 1.1620 0.8368 0.8840 0.0110 -0.1694 -0.1449 87 LYS B CE 681 N NZ . LYS A 83 ? 1.2479 0.9024 0.9306 0.0298 -0.1571 -0.1593 87 LYS B NZ 682 N N . ILE A 84 ? 0.6371 0.4164 0.4515 -0.0026 -0.1344 -0.0976 88 ILE B N 683 C CA . ILE A 84 ? 0.6034 0.3960 0.4391 0.0003 -0.1165 -0.0909 88 ILE B CA 684 C C . ILE A 84 ? 0.6227 0.3950 0.4355 0.0135 -0.1080 -0.1021 88 ILE B C 685 O O . ILE A 84 ? 0.6755 0.4188 0.4700 0.0151 -0.1197 -0.1140 88 ILE B O 686 C CB . ILE A 84 ? 0.6167 0.4120 0.4861 -0.0126 -0.1234 -0.0835 88 ILE B CB 687 C CG1 . ILE A 84 ? 0.6747 0.4969 0.5729 -0.0237 -0.1264 -0.0707 88 ILE B CG1 688 C CG2 . ILE A 84 ? 0.6360 0.4356 0.5187 -0.0083 -0.1082 -0.0793 88 ILE B CG2 689 C CD1 . ILE A 84 ? 0.7356 0.5589 0.6640 -0.0385 -0.1372 -0.0639 88 ILE B CD1 690 N N . TYR A 85 ? 0.6234 0.4107 0.4392 0.0230 -0.0881 -0.0985 89 TYR B N 691 C CA . TYR A 85 ? 0.6286 0.4018 0.4293 0.0368 -0.0779 -0.1077 89 TYR B CA 692 C C . TYR A 85 ? 0.5576 0.3447 0.3866 0.0373 -0.0667 -0.0992 89 TYR B C 693 O O . TYR A 85 ? 0.5067 0.3196 0.3522 0.0356 -0.0558 -0.0886 89 TYR B O 694 C CB . TYR A 85 ? 0.6577 0.4375 0.4328 0.0498 -0.0634 -0.1114 89 TYR B CB 695 C CG . TYR A 85 ? 0.7168 0.4835 0.4584 0.0505 -0.0733 -0.1188 89 TYR B CG 696 C CD1 . TYR A 85 ? 0.7521 0.5345 0.4960 0.0425 -0.0781 -0.1099 89 TYR B CD1 697 C CD2 . TYR A 85 ? 0.8206 0.5577 0.5263 0.0601 -0.0783 -0.1347 89 TYR B CD2 698 C CE1 . TYR A 85 ? 0.8059 0.5755 0.5176 0.0432 -0.0891 -0.1158 89 TYR B CE1 699 C CE2 . TYR A 85 ? 0.8894 0.6125 0.5599 0.0608 -0.0887 -0.1418 89 TYR B CE2 700 C CZ . TYR A 85 ? 0.8704 0.6103 0.5443 0.0520 -0.0945 -0.1317 89 TYR B CZ 701 O OH . TYR A 85 ? 1.0110 0.7364 0.6489 0.0527 -0.1066 -0.1378 89 TYR B OH 702 N N . ILE A 86 ? 0.5772 0.3451 0.4104 0.0395 -0.0708 -0.1038 90 ILE B N 703 C CA . ILE A 86 ? 0.5840 0.3618 0.4400 0.0418 -0.0614 -0.0964 90 ILE B CA 704 C C . ILE A 86 ? 0.5594 0.3302 0.4024 0.0597 -0.0499 -0.1053 90 ILE B C 705 O O . ILE A 86 ? 0.6195 0.3674 0.4371 0.0688 -0.0531 -0.1188 90 ILE B O 706 C CB . ILE A 86 ? 0.6218 0.3841 0.4946 0.0314 -0.0742 -0.0926 90 ILE B CB 707 C CG1 . ILE A 86 ? 0.6429 0.4194 0.5337 0.0141 -0.0820 -0.0818 90 ILE B CG1 708 C CG2 . ILE A 86 ? 0.6205 0.3877 0.5112 0.0357 -0.0663 -0.0859 90 ILE B CG2 709 C CD1 . ILE A 86 ? 0.7064 0.4604 0.6013 0.0022 -0.1003 -0.0832 90 ILE B CD1 710 N N . HIS A 87 ? 0.5526 0.3441 0.4131 0.0652 -0.0362 -0.0979 91 HIS B N 711 C CA . HIS A 87 ? 0.5485 0.3384 0.4045 0.0823 -0.0245 -0.1045 91 HIS B CA 712 C C . HIS A 87 ? 0.5905 0.3478 0.4409 0.0883 -0.0345 -0.1140 91 HIS B C 713 O O . HIS A 87 ? 0.5732 0.3206 0.4387 0.0790 -0.0454 -0.1083 91 HIS B O 714 C CB . HIS A 87 ? 0.5226 0.3399 0.4051 0.0843 -0.0126 -0.0932 91 HIS B CB 715 C CG . HIS A 87 ? 0.5139 0.3411 0.3954 0.1012 0.0027 -0.0976 91 HIS B CG 716 N ND1 . HIS A 87 ? 0.5341 0.3436 0.4118 0.1158 0.0037 -0.1071 91 HIS B ND1 717 C CD2 . HIS A 87 ? 0.4899 0.3433 0.3754 0.1060 0.0182 -0.0933 91 HIS B CD2 718 C CE1 . HIS A 87 ? 0.5375 0.3643 0.4179 0.1296 0.0201 -0.1088 91 HIS B CE1 719 N NE2 . HIS A 87 ? 0.5298 0.3838 0.4154 0.1230 0.0291 -0.0998 91 HIS B NE2 720 N N . PRO A 88 ? 0.6197 0.3590 0.4474 0.1042 -0.0304 -0.1284 92 PRO B N 721 C CA . PRO A 88 ? 0.6815 0.3847 0.5011 0.1103 -0.0417 -0.1392 92 PRO B CA 722 C C . PRO A 88 ? 0.6511 0.3539 0.4962 0.1159 -0.0404 -0.1332 92 PRO B C 723 O O . PRO A 88 ? 0.6473 0.3200 0.4922 0.1160 -0.0531 -0.1374 92 PRO B O 724 C CB . PRO A 88 ? 0.7140 0.4011 0.5009 0.1286 -0.0343 -0.1567 92 PRO B CB 725 C CG . PRO A 88 ? 0.7004 0.4218 0.4871 0.1348 -0.0142 -0.1517 92 PRO B CG 726 C CD . PRO A 88 ? 0.6527 0.4019 0.4589 0.1169 -0.0155 -0.1355 92 PRO B CD 727 N N . ARG A 89 ? 0.6233 0.3577 0.4900 0.1201 -0.0266 -0.1233 93 ARG B N 728 C CA . ARG A 89 ? 0.6260 0.3635 0.5184 0.1241 -0.0271 -0.1155 93 ARG B CA 729 C C . ARG A 89 ? 0.5526 0.3075 0.4672 0.1068 -0.0322 -0.0984 93 ARG B C 730 O O . ARG A 89 ? 0.5196 0.2852 0.4548 0.1090 -0.0307 -0.0895 93 ARG B O 731 C CB . ARG A 89 ? 0.6893 0.4487 0.5928 0.1422 -0.0101 -0.1166 93 ARG B CB 732 C CG . ARG A 89 ? 0.8301 0.5724 0.7124 0.1626 -0.0025 -0.1337 93 ARG B CG 733 C CD . ARG A 89 ? 0.9564 0.7263 0.8562 0.1801 0.0162 -0.1326 93 ARG B CD 734 N NE . ARG A 89 ? 1.2512 1.0103 1.1283 0.2002 0.0281 -0.1488 93 ARG B NE 735 C CZ . ARG A 89 ? 1.4403 1.2068 1.2920 0.2027 0.0397 -0.1550 93 ARG B CZ 736 N NH1 . ARG A 89 ? 1.4229 1.2076 1.2703 0.1862 0.0401 -0.1461 93 ARG B NH1 737 N NH2 . ARG A 89 ? 1.5143 1.2686 1.3432 0.2228 0.0511 -0.1703 93 ARG B NH2 738 N N . TYR A 90 ? 0.5722 0.3305 0.4821 0.0901 -0.0381 -0.0938 94 TYR B N 739 C CA . TYR A 90 ? 0.5101 0.2807 0.4379 0.0741 -0.0430 -0.0789 94 TYR B CA 740 C C . TYR A 90 ? 0.5251 0.2729 0.4617 0.0720 -0.0541 -0.0745 94 TYR B C 741 O O . TYR A 90 ? 0.5715 0.2885 0.4977 0.0717 -0.0651 -0.0817 94 TYR B O 742 C CB . TYR A 90 ? 0.5118 0.2847 0.4332 0.0585 -0.0490 -0.0768 94 TYR B CB 743 C CG . TYR A 90 ? 0.4847 0.2633 0.4218 0.0416 -0.0555 -0.0632 94 TYR B CG 744 C CD1 . TYR A 90 ? 0.4744 0.2759 0.4273 0.0382 -0.0486 -0.0512 94 TYR B CD1 745 C CD2 . TYR A 90 ? 0.4911 0.2519 0.4266 0.0289 -0.0684 -0.0625 94 TYR B CD2 746 C CE1 . TYR A 90 ? 0.4565 0.2631 0.4202 0.0239 -0.0526 -0.0392 94 TYR B CE1 747 C CE2 . TYR A 90 ? 0.5063 0.2749 0.4570 0.0138 -0.0719 -0.0493 94 TYR B CE2 748 C CZ . TYR A 90 ? 0.4759 0.2673 0.4392 0.0120 -0.0630 -0.0379 94 TYR B CZ 749 O OH . TYR A 90 ? 0.4879 0.2865 0.4630 -0.0020 -0.0648 -0.0253 94 TYR B OH 750 N N . ASN A 91 ? 0.5426 0.3040 0.4970 0.0707 -0.0521 -0.0626 95 ASN B N 751 C CA . ASN A 91 ? 0.5831 0.3243 0.5455 0.0704 -0.0618 -0.0563 95 ASN B CA 752 C C . ASN A 91 ? 0.6007 0.3476 0.5715 0.0522 -0.0670 -0.0408 95 ASN B C 753 O O . ASN A 91 ? 0.6398 0.4049 0.6211 0.0506 -0.0632 -0.0303 95 ASN B O 754 C CB . ASN A 91 ? 0.6008 0.3521 0.5759 0.0858 -0.0562 -0.0546 95 ASN B CB 755 C CG . ASN A 91 ? 0.6909 0.4180 0.6728 0.0890 -0.0672 -0.0490 95 ASN B CG 756 O OD1 . ASN A 91 ? 0.7484 0.4519 0.7260 0.0776 -0.0785 -0.0442 95 ASN B OD1 757 N ND2 . ASN A 91 ? 0.6857 0.4191 0.6801 0.1042 -0.0644 -0.0485 95 ASN B ND2 758 N N . TRP A 92 ? 0.5924 0.3238 0.5584 0.0384 -0.0757 -0.0394 96 TRP B N 759 C CA . TRP A 92 ? 0.5729 0.3123 0.5475 0.0211 -0.0780 -0.0242 96 TRP B CA 760 C C . TRP A 92 ? 0.5810 0.3018 0.5608 0.0181 -0.0858 -0.0129 96 TRP B C 761 O O . TRP A 92 ? 0.6117 0.3424 0.5970 0.0066 -0.0848 0.0011 96 TRP B O 762 C CB . TRP A 92 ? 0.5643 0.3000 0.5371 0.0061 -0.0835 -0.0244 96 TRP B CB 763 C CG . TRP A 92 ? 0.5955 0.2972 0.5620 0.0038 -0.0970 -0.0317 96 TRP B CG 764 C CD1 . TRP A 92 ? 0.6054 0.2921 0.5581 0.0104 -0.1015 -0.0476 96 TRP B CD1 765 C CD2 . TRP A 92 ? 0.6032 0.2786 0.5748 -0.0063 -0.1088 -0.0234 96 TRP B CD2 766 N NE1 . TRP A 92 ? 0.6254 0.2769 0.5743 0.0053 -0.1164 -0.0511 96 TRP B NE1 767 C CE2 . TRP A 92 ? 0.6359 0.2800 0.5978 -0.0055 -0.1211 -0.0358 96 TRP B CE2 768 C CE3 . TRP A 92 ? 0.6130 0.2870 0.5947 -0.0162 -0.1103 -0.0062 96 TRP B CE3 769 C CZ2 . TRP A 92 ? 0.6953 0.3061 0.6601 -0.0151 -0.1358 -0.0316 96 TRP B CZ2 770 C CZ3 . TRP A 92 ? 0.6401 0.2828 0.6244 -0.0258 -0.1233 -0.0006 96 TRP B CZ3 771 C CH2 . TRP A 92 ? 0.6865 0.2977 0.6638 -0.0255 -0.1363 -0.0132 96 TRP B CH2 772 N N . ARG A 93 ? 0.5915 0.2845 0.5684 0.0289 -0.0934 -0.0188 97 ARG B N 773 C CA . ARG A 93 ? 0.6093 0.2799 0.5901 0.0263 -0.1027 -0.0076 97 ARG B CA 774 C C . ARG A 93 ? 0.6119 0.2974 0.5995 0.0326 -0.0990 0.0029 97 ARG B C 775 O O . ARG A 93 ? 0.5968 0.2725 0.5860 0.0250 -0.1049 0.0174 97 ARG B O 776 C CB . ARG A 93 ? 0.6696 0.3027 0.6453 0.0375 -0.1131 -0.0178 97 ARG B CB 777 C CG . ARG A 93 ? 0.7161 0.3224 0.6842 0.0278 -0.1232 -0.0251 97 ARG B CG 778 C CD . ARG A 93 ? 0.7889 0.3554 0.7496 0.0416 -0.1334 -0.0370 97 ARG B CD 779 N NE . ARG A 93 ? 0.8706 0.4024 0.8267 0.0285 -0.1483 -0.0382 97 ARG B NE 780 C CZ . ARG A 93 ? 0.9767 0.5014 0.9237 0.0217 -0.1530 -0.0497 97 ARG B CZ 781 N NH1 . ARG A 93 ? 1.0388 0.5882 0.9779 0.0274 -0.1430 -0.0606 97 ARG B NH1 782 N NH2 . ARG A 93 ? 1.0576 0.5492 1.0033 0.0084 -0.1690 -0.0494 97 ARG B NH2 783 N N . GLU A 94 A 0.6143 0.3225 0.6056 0.0461 -0.0902 -0.0038 97 GLU B N 784 C CA . GLU A 94 A 0.6257 0.3478 0.6256 0.0539 -0.0890 0.0043 97 GLU B CA 785 C C . GLU A 94 A 0.5752 0.3320 0.5776 0.0478 -0.0796 0.0098 97 GLU B C 786 O O . GLU A 94 A 0.5813 0.3437 0.5822 0.0385 -0.0814 0.0229 97 GLU B O 787 C CB . GLU A 94 A 0.6717 0.3927 0.6792 0.0755 -0.0876 -0.0062 97 GLU B CB 788 C CG . GLU A 94 A 0.7454 0.4771 0.7656 0.0838 -0.0906 0.0033 97 GLU B CG 789 C CD . GLU A 94 A 0.8075 0.5507 0.8420 0.1049 -0.0859 -0.0059 97 GLU B CD 790 O OE1 . GLU A 94 A 0.7680 0.5119 0.8005 0.1147 -0.0778 -0.0204 97 GLU B OE1 791 O OE2 . GLU A 94 A 0.7878 0.5409 0.8361 0.1120 -0.0901 0.0021 97 GLU B OE2 792 N N . ASN A 95 ? 0.5269 0.3053 0.5314 0.0535 -0.0697 -0.0001 98 ASN B N 793 C CA . ASN A 95 ? 0.4985 0.3080 0.5080 0.0513 -0.0618 0.0038 98 ASN B CA 794 C C . ASN A 95 ? 0.4601 0.2888 0.4662 0.0468 -0.0517 -0.0029 98 ASN B C 795 O O . ASN A 95 ? 0.4947 0.3472 0.5055 0.0464 -0.0452 -0.0013 98 ASN B O 796 C CB . ASN A 95 ? 0.4943 0.3157 0.5173 0.0663 -0.0610 0.0023 98 ASN B CB 797 C CG . ASN A 95 ? 0.4820 0.3032 0.5092 0.0812 -0.0549 -0.0114 98 ASN B CG 798 O OD1 . ASN A 95 ? 0.4881 0.2969 0.5043 0.0806 -0.0528 -0.0206 98 ASN B OD1 799 N ND2 . ASN A 95 ? 0.4928 0.3280 0.5357 0.0948 -0.0523 -0.0126 98 ASN B ND2 800 N N . LEU A 96 ? 0.4609 0.2778 0.4588 0.0431 -0.0519 -0.0101 99 LEU B N 801 C CA . LEU A 96 ? 0.4087 0.2404 0.4019 0.0396 -0.0443 -0.0164 99 LEU B CA 802 C C . LEU A 96 ? 0.3955 0.2432 0.3914 0.0522 -0.0352 -0.0246 99 LEU B C 803 O O . LEU A 96 ? 0.3976 0.2648 0.3928 0.0495 -0.0274 -0.0256 99 LEU B O 804 C CB . LEU A 96 ? 0.4159 0.2658 0.4100 0.0265 -0.0405 -0.0079 99 LEU B CB 805 C CG . LEU A 96 ? 0.4585 0.2989 0.4508 0.0127 -0.0457 0.0013 99 LEU B CG 806 C CD1 . LEU A 96 ? 0.4227 0.2842 0.4159 0.0036 -0.0390 0.0079 99 LEU B CD1 807 C CD2 . LEU A 96 ? 0.5032 0.3268 0.4918 0.0075 -0.0514 -0.0040 99 LEU B CD2 808 N N . ASP A 97 ? 0.4130 0.2528 0.4130 0.0663 -0.0355 -0.0299 100 ASP B N 809 C CA . ASP A 97 ? 0.4216 0.2766 0.4249 0.0789 -0.0251 -0.0376 100 ASP B CA 810 C C . ASP A 97 ? 0.4062 0.2587 0.3931 0.0774 -0.0203 -0.0468 100 ASP B C 811 O O . ASP A 97 ? 0.4081 0.2374 0.3818 0.0745 -0.0274 -0.0525 100 ASP B O 812 C CB . ASP A 97 ? 0.4588 0.3020 0.4680 0.0958 -0.0260 -0.0434 100 ASP B CB 813 C CG . ASP A 97 ? 0.4932 0.3587 0.5119 0.1093 -0.0131 -0.0483 100 ASP B CG 814 O OD1 . ASP A 97 ? 0.5114 0.4037 0.5375 0.1044 -0.0054 -0.0435 100 ASP B OD1 815 O OD2 . ASP A 97 ? 0.5521 0.4081 0.5718 0.1251 -0.0105 -0.0566 100 ASP B OD2 816 N N . ARG A 98 ? 0.3791 0.2546 0.3669 0.0784 -0.0096 -0.0474 101 ARG B N 817 C CA . ARG A 98 ? 0.4310 0.3069 0.4019 0.0772 -0.0047 -0.0545 101 ARG B CA 818 C C . ARG A 98 ? 0.4297 0.2974 0.3913 0.0627 -0.0126 -0.0525 101 ARG B C 819 O O . ARG A 98 ? 0.4615 0.3119 0.4071 0.0618 -0.0178 -0.0602 101 ARG B O 820 C CB . ARG A 98 ? 0.4742 0.3332 0.4305 0.0909 -0.0022 -0.0674 101 ARG B CB 821 C CG . ARG A 98 ? 0.5196 0.3906 0.4878 0.1070 0.0082 -0.0695 101 ARG B CG 822 C CD . ARG A 98 ? 0.6057 0.4550 0.5570 0.1220 0.0101 -0.0836 101 ARG B CD 823 N NE . ARG A 98 ? 0.7154 0.5787 0.6777 0.1396 0.0232 -0.0868 101 ARG B NE 824 C CZ . ARG A 98 ? 0.7409 0.5975 0.7176 0.1525 0.0216 -0.0886 101 ARG B CZ 825 N NH1 . ARG A 98 ? 0.7396 0.5728 0.7197 0.1495 0.0067 -0.0869 101 ARG B NH1 826 N NH2 . ARG A 98 ? 0.8408 0.7150 0.8300 0.1690 0.0354 -0.0913 101 ARG B NH2 827 N N . ASP A 99 ? 0.4026 0.2834 0.3749 0.0518 -0.0138 -0.0422 102 ASP B N 828 C CA . ASP A 99 ? 0.4175 0.2963 0.3871 0.0383 -0.0195 -0.0381 102 ASP B CA 829 C C . ASP A 99 ? 0.3857 0.2773 0.3479 0.0365 -0.0140 -0.0404 102 ASP B C 830 O O . ASP A 99 ? 0.3913 0.3012 0.3603 0.0319 -0.0089 -0.0342 102 ASP B O 831 C CB . ASP A 99 ? 0.3968 0.2854 0.3785 0.0297 -0.0204 -0.0268 102 ASP B CB 832 C CG . ASP A 99 ? 0.4303 0.3151 0.4123 0.0166 -0.0259 -0.0216 102 ASP B CG 833 O OD1 . ASP A 99 ? 0.4160 0.2916 0.3918 0.0131 -0.0308 -0.0263 102 ASP B OD1 834 O OD2 . ASP A 99 ? 0.3764 0.2675 0.3648 0.0100 -0.0256 -0.0127 102 ASP B OD2 835 N N . ILE A 100 ? 0.4306 0.3105 0.3771 0.0407 -0.0157 -0.0495 103 ILE B N 836 C CA . ILE A 100 ? 0.4275 0.3172 0.3633 0.0405 -0.0112 -0.0514 103 ILE B CA 837 C C . ILE A 100 ? 0.4168 0.2887 0.3345 0.0388 -0.0203 -0.0594 103 ILE B C 838 O O . ILE A 100 ? 0.4368 0.2872 0.3441 0.0437 -0.0262 -0.0678 103 ILE B O 839 C CB . ILE A 100 ? 0.4218 0.3234 0.3541 0.0518 0.0016 -0.0537 103 ILE B CB 840 C CG1 . ILE A 100 ? 0.4480 0.3613 0.3706 0.0498 0.0070 -0.0520 103 ILE B CG1 841 C CG2 . ILE A 100 ? 0.4480 0.3337 0.3669 0.0647 0.0034 -0.0645 103 ILE B CG2 842 C CD1 . ILE A 100 ? 0.4260 0.3578 0.3535 0.0564 0.0209 -0.0487 103 ILE B CD1 843 N N . ALA A 101 ? 0.3940 0.2737 0.3085 0.0317 -0.0229 -0.0567 104 ALA B N 844 C CA . ALA A 101 ? 0.4155 0.2810 0.3134 0.0290 -0.0335 -0.0632 104 ALA B CA 845 C C . ALA A 101 ? 0.4060 0.2848 0.2961 0.0278 -0.0308 -0.0603 104 ALA B C 846 O O . ALA A 101 ? 0.4228 0.3210 0.3268 0.0245 -0.0242 -0.0514 104 ALA B O 847 C CB . ALA A 101 ? 0.4387 0.2957 0.3485 0.0171 -0.0471 -0.0605 104 ALA B CB 848 N N . LEU A 102 ? 0.4773 0.3431 0.3431 0.0311 -0.0366 -0.0681 105 LEU B N 849 C CA . LEU A 102 ? 0.4889 0.3620 0.3424 0.0300 -0.0375 -0.0657 105 LEU B CA 850 C C . LEU A 102 ? 0.4725 0.3350 0.3221 0.0215 -0.0559 -0.0680 105 LEU B C 851 O O . LEU A 102 ? 0.4899 0.3323 0.3325 0.0198 -0.0674 -0.0760 105 LEU B O 852 C CB . LEU A 102 ? 0.4992 0.3657 0.3226 0.0414 -0.0292 -0.0724 105 LEU B CB 853 C CG . LEU A 102 ? 0.5018 0.3858 0.3300 0.0485 -0.0102 -0.0671 105 LEU B CG 854 C CD1 . LEU A 102 ? 0.5559 0.4307 0.3564 0.0615 -0.0005 -0.0757 105 LEU B CD1 855 C CD2 . LEU A 102 ? 0.5159 0.4178 0.3504 0.0434 -0.0066 -0.0560 105 LEU B CD2 856 N N . MET A 103 ? 0.4668 0.3428 0.3226 0.0163 -0.0593 -0.0606 106 MET B N 857 C CA . MET A 103 ? 0.4850 0.3564 0.3416 0.0083 -0.0771 -0.0608 106 MET B CA 858 C C . MET A 103 ? 0.4891 0.3627 0.3247 0.0117 -0.0794 -0.0595 106 MET B C 859 O O . MET A 103 ? 0.4434 0.3330 0.2839 0.0141 -0.0687 -0.0512 106 MET B O 860 C CB . MET A 103 ? 0.5193 0.4086 0.4119 -0.0019 -0.0799 -0.0508 106 MET B CB 861 C CG . MET A 103 ? 0.5512 0.4393 0.4629 -0.0055 -0.0758 -0.0496 106 MET B CG 862 S SD . MET A 103 ? 0.6176 0.5267 0.5681 -0.0171 -0.0768 -0.0376 106 MET B SD 863 C CE . MET A 103 ? 0.6192 0.5498 0.5761 -0.0113 -0.0597 -0.0301 106 MET B CE 864 N N . LYS A 104 ? 0.5302 0.3853 0.3403 0.0119 -0.0942 -0.0675 107 LYS B N 865 C CA . LYS A 104 ? 0.5537 0.4081 0.3412 0.0141 -0.1002 -0.0657 107 LYS B CA 866 C C . LYS A 104 ? 0.5453 0.4087 0.3540 0.0043 -0.1181 -0.0593 107 LYS B C 867 O O . LYS A 104 ? 0.5180 0.3731 0.3367 -0.0035 -0.1344 -0.0635 107 LYS B O 868 C CB . LYS A 104 ? 0.6201 0.4482 0.3635 0.0206 -0.1076 -0.0784 107 LYS B CB 869 C CG . LYS A 104 ? 0.6790 0.5066 0.3932 0.0247 -0.1097 -0.0750 107 LYS B CG 870 C CD . LYS A 104 ? 0.7743 0.5745 0.4395 0.0318 -0.1162 -0.0882 107 LYS B CD 871 C CE . LYS A 104 ? 0.8530 0.6524 0.4851 0.0363 -0.1167 -0.0830 107 LYS B CE 872 N NZ . LYS A 104 ? 0.9724 0.7422 0.5536 0.0418 -0.1283 -0.0969 107 LYS B NZ 873 N N . LEU A 105 ? 0.5273 0.4070 0.3433 0.0048 -0.1157 -0.0490 108 LEU B N 874 C CA . LEU A 105 ? 0.5388 0.4307 0.3786 -0.0024 -0.1312 -0.0417 108 LEU B CA 875 C C . LEU A 105 ? 0.5772 0.4532 0.3905 -0.0035 -0.1529 -0.0467 108 LEU B C 876 O O . LEU A 105 ? 0.5764 0.4364 0.3486 0.0036 -0.1519 -0.0517 108 LEU B O 877 C CB . LEU A 105 ? 0.5140 0.4256 0.3687 0.0003 -0.1218 -0.0296 108 LEU B CB 878 C CG . LEU A 105 ? 0.5107 0.4372 0.3889 0.0016 -0.1015 -0.0245 108 LEU B CG 879 C CD1 . LEU A 105 ? 0.5155 0.4578 0.4089 0.0037 -0.0965 -0.0135 108 LEU B CD1 880 C CD2 . LEU A 105 ? 0.5055 0.4390 0.4146 -0.0054 -0.1018 -0.0254 108 LEU B CD2 881 N N . LYS A 106 ? 0.6180 0.4994 0.4551 -0.0125 -0.1726 -0.0448 109 LYS B N 882 C CA . LYS A 106 ? 0.6890 0.5557 0.5042 -0.0152 -0.1976 -0.0493 109 LYS B CA 883 C C . LYS A 106 ? 0.7425 0.6118 0.5362 -0.0087 -0.2003 -0.0423 109 LYS B C 884 O O . LYS A 106 ? 0.8042 0.6529 0.5549 -0.0050 -0.2113 -0.0482 109 LYS B O 885 C CB . LYS A 106 ? 0.7735 0.6510 0.6278 -0.0274 -0.2180 -0.0462 109 LYS B CB 886 C CG . LYS A 106 ? 0.9080 0.7633 0.7402 -0.0329 -0.2462 -0.0554 109 LYS B CG 887 C CD . LYS A 106 ? 0.9540 0.8165 0.8274 -0.0472 -0.2633 -0.0543 109 LYS B CD 888 C CE . LYS A 106 ? 0.9734 0.8222 0.8503 -0.0512 -0.2552 -0.0620 109 LYS B CE 889 N NZ . LYS A 106 ? 1.0309 0.8781 0.9379 -0.0665 -0.2766 -0.0625 109 LYS B NZ 890 N N . LYS A 107 ? 0.7058 0.5980 0.5270 -0.0070 -0.1907 -0.0297 110 LYS B N 891 C CA . LYS A 107 ? 0.7551 0.6478 0.5549 0.0002 -0.1884 -0.0216 110 LYS B CA 892 C C . LYS A 107 ? 0.6636 0.5708 0.4780 0.0052 -0.1638 -0.0132 110 LYS B C 893 O O . LYS A 107 ? 0.6168 0.5412 0.4698 0.0024 -0.1544 -0.0099 110 LYS B O 894 C CB . LYS A 107 ? 0.7799 0.6810 0.5939 -0.0024 -0.2112 -0.0135 110 LYS B CB 895 C CG . LYS A 107 ? 0.8210 0.7463 0.6915 -0.0097 -0.2185 -0.0082 110 LYS B CG 896 C CD . LYS A 107 ? 0.8837 0.8239 0.7740 -0.0077 -0.2322 0.0035 110 LYS B CD 897 C CE . LYS A 107 ? 0.9509 0.8763 0.8136 -0.0091 -0.2607 0.0019 110 LYS B CE 898 N NZ . LYS A 107 ? 0.9835 0.9123 0.8393 -0.0022 -0.2683 0.0136 110 LYS B NZ 899 N N . PRO A 108 ? 0.6974 0.5967 0.4796 0.0123 -0.1532 -0.0094 111 PRO B N 900 C CA . PRO A 108 ? 0.6441 0.5555 0.4406 0.0157 -0.1317 -0.0011 111 PRO B CA 901 C C . PRO A 108 ? 0.5805 0.5111 0.4180 0.0144 -0.1340 0.0091 111 PRO B C 902 O O . PRO A 108 ? 0.5255 0.4604 0.3738 0.0134 -0.1521 0.0137 111 PRO B O 903 C CB . PRO A 108 ? 0.7061 0.6057 0.4618 0.0218 -0.1260 0.0039 111 PRO B CB 904 C CG . PRO A 108 ? 0.8121 0.6914 0.5260 0.0233 -0.1344 -0.0070 111 PRO B CG 905 C CD . PRO A 108 ? 0.7886 0.6663 0.5180 0.0170 -0.1578 -0.0136 111 PRO B CD 906 N N . VAL A 109 ? 0.5442 0.4860 0.4046 0.0151 -0.1159 0.0119 112 VAL B N 907 C CA . VAL A 109 ? 0.5603 0.5182 0.4566 0.0158 -0.1144 0.0201 112 VAL B CA 908 C C . VAL A 109 ? 0.5187 0.4721 0.4018 0.0211 -0.1093 0.0301 112 VAL B C 909 O O . VAL A 109 ? 0.5343 0.4777 0.3900 0.0229 -0.0981 0.0310 112 VAL B O 910 C CB . VAL A 109 ? 0.5979 0.5676 0.5227 0.0137 -0.0989 0.0173 112 VAL B CB 911 C CG1 . VAL A 109 ? 0.5655 0.5300 0.4760 0.0160 -0.0796 0.0171 112 VAL B CG1 912 C CG2 . VAL A 109 ? 0.6427 0.6291 0.6050 0.0148 -0.0991 0.0234 112 VAL B CG2 913 N N . ALA A 110 ? 0.5111 0.4719 0.4146 0.0237 -0.1179 0.0383 113 ALA B N 914 C CA . ALA A 110 ? 0.5272 0.4830 0.4246 0.0285 -0.1135 0.0487 113 ALA B CA 915 C C . ALA A 110 ? 0.4947 0.4559 0.4113 0.0291 -0.0946 0.0492 113 ALA B C 916 O O . ALA A 110 ? 0.4916 0.4656 0.4387 0.0284 -0.0907 0.0451 113 ALA B O 917 C CB . ALA A 110 ? 0.5499 0.5112 0.4660 0.0324 -0.1303 0.0566 113 ALA B CB 918 N N . PHE A 111 ? 0.4791 0.4306 0.3775 0.0300 -0.0832 0.0544 114 PHE B N 919 C CA . PHE A 111 ? 0.4766 0.4310 0.3923 0.0299 -0.0680 0.0553 114 PHE B CA 920 C C . PHE A 111 ? 0.4586 0.4145 0.3975 0.0347 -0.0728 0.0619 114 PHE B C 921 O O . PHE A 111 ? 0.4587 0.4109 0.3952 0.0385 -0.0861 0.0689 114 PHE B O 922 C CB . PHE A 111 ? 0.4868 0.4315 0.3799 0.0280 -0.0549 0.0598 114 PHE B CB 923 C CG . PHE A 111 ? 0.5006 0.4443 0.3713 0.0254 -0.0477 0.0534 114 PHE B CG 924 C CD1 . PHE A 111 ? 0.4945 0.4447 0.3719 0.0239 -0.0485 0.0422 114 PHE B CD1 925 C CD2 . PHE A 111 ? 0.5357 0.4715 0.3791 0.0249 -0.0389 0.0591 114 PHE B CD2 926 C CE1 . PHE A 111 ? 0.5223 0.4692 0.3790 0.0231 -0.0419 0.0357 114 PHE B CE1 927 C CE2 . PHE A 111 ? 0.5311 0.4666 0.3545 0.0246 -0.0306 0.0527 114 PHE B CE2 928 C CZ . PHE A 111 ? 0.5095 0.4496 0.3394 0.0243 -0.0325 0.0404 114 PHE B CZ 929 N N . SER A 112 ? 0.4101 0.3706 0.3709 0.0354 -0.0625 0.0590 115 SER B N 930 C CA . SER A 112 ? 0.4451 0.4057 0.4283 0.0415 -0.0649 0.0628 115 SER B CA 931 C C . SER A 112 ? 0.4396 0.3958 0.4302 0.0406 -0.0509 0.0600 115 SER B C 932 O O . SER A 112 ? 0.4297 0.3846 0.4096 0.0348 -0.0408 0.0565 115 SER B O 933 C CB . SER A 112 ? 0.4193 0.3969 0.4310 0.0450 -0.0717 0.0583 115 SER B CB 934 O OG . SER A 112 ? 0.3826 0.3713 0.4062 0.0412 -0.0616 0.0492 115 SER B OG 935 N N . ASP A 113 ? 0.4298 0.3836 0.4393 0.0469 -0.0509 0.0609 116 ASP B N 936 C CA . ASP A 113 ? 0.4236 0.3724 0.4404 0.0465 -0.0396 0.0560 116 ASP B CA 937 C C . ASP A 113 ? 0.3923 0.3540 0.4152 0.0425 -0.0308 0.0459 116 ASP B C 938 O O . ASP A 113 ? 0.4122 0.3691 0.4319 0.0389 -0.0219 0.0419 116 ASP B O 939 C CB . ASP A 113 ? 0.4442 0.3886 0.4805 0.0561 -0.0414 0.0558 116 ASP B CB 940 C CG . ASP A 113 ? 0.5639 0.4893 0.5937 0.0599 -0.0489 0.0661 116 ASP B CG 941 O OD1 . ASP A 113 ? 0.5396 0.4539 0.5483 0.0537 -0.0503 0.0742 116 ASP B OD1 942 O OD2 . ASP A 113 ? 0.5410 0.4621 0.5871 0.0697 -0.0529 0.0667 116 ASP B OD2 943 N N . TYR A 114 ? 0.3641 0.3413 0.3959 0.0424 -0.0344 0.0425 117 TYR B N 944 C CA . TYR A 114 ? 0.3575 0.3466 0.3976 0.0390 -0.0271 0.0345 117 TYR B CA 945 C C . TYR A 114 ? 0.3684 0.3599 0.3936 0.0315 -0.0269 0.0321 117 TYR B C 946 O O . TYR A 114 ? 0.3188 0.3161 0.3470 0.0279 -0.0205 0.0263 117 TYR B O 947 C CB . TYR A 114 ? 0.3832 0.3888 0.4484 0.0436 -0.0300 0.0329 117 TYR B CB 948 C CG . TYR A 114 ? 0.4054 0.4093 0.4864 0.0536 -0.0309 0.0354 117 TYR B CG 949 C CD1 . TYR A 114 ? 0.3842 0.3824 0.4696 0.0581 -0.0207 0.0307 117 TYR B CD1 950 C CD2 . TYR A 114 ? 0.4055 0.4110 0.4949 0.0592 -0.0430 0.0421 117 TYR B CD2 951 C CE1 . TYR A 114 ? 0.4083 0.4019 0.5065 0.0687 -0.0214 0.0316 117 TYR B CE1 952 C CE2 . TYR A 114 ? 0.4192 0.4219 0.5243 0.0699 -0.0442 0.0443 117 TYR B CE2 953 C CZ . TYR A 114 ? 0.4357 0.4321 0.5453 0.0750 -0.0328 0.0387 117 TYR B CZ 954 O OH . TYR A 114 ? 0.4501 0.4408 0.5738 0.0870 -0.0339 0.0397 117 TYR B OH 955 N N . ILE A 115 ? 0.3441 0.3293 0.3514 0.0301 -0.0340 0.0365 118 ILE B N 956 C CA . ILE A 115 ? 0.3626 0.3477 0.3533 0.0252 -0.0351 0.0333 118 ILE B CA 957 C C . ILE A 115 ? 0.3561 0.3295 0.3216 0.0236 -0.0311 0.0375 118 ILE B C 958 O O . ILE A 115 ? 0.4282 0.3938 0.3821 0.0257 -0.0364 0.0450 118 ILE B O 959 C CB . ILE A 115 ? 0.3559 0.3458 0.3474 0.0252 -0.0490 0.0335 118 ILE B CB 960 C CG1 . ILE A 115 ? 0.3409 0.3462 0.3620 0.0255 -0.0513 0.0307 118 ILE B CG1 961 C CG2 . ILE A 115 ? 0.3577 0.3429 0.3279 0.0210 -0.0510 0.0288 118 ILE B CG2 962 C CD1 . ILE A 115 ? 0.3493 0.3620 0.3793 0.0250 -0.0668 0.0322 118 ILE B CD1 963 N N . HIS A 116 ? 0.3715 0.3448 0.3296 0.0201 -0.0216 0.0335 119 HIS B N 964 C CA . HIS A 116 ? 0.3750 0.3414 0.3143 0.0185 -0.0147 0.0379 119 HIS B CA 965 C C . HIS A 116 ? 0.3498 0.3201 0.2853 0.0161 -0.0059 0.0317 119 HIS B C 966 O O . HIS A 116 ? 0.3422 0.3178 0.2927 0.0146 -0.0022 0.0266 119 HIS B O 967 C CB . HIS A 116 ? 0.3953 0.3562 0.3415 0.0179 -0.0098 0.0445 119 HIS B CB 968 C CG . HIS A 116 ? 0.4461 0.4005 0.3752 0.0156 -0.0043 0.0527 119 HIS B CG 969 N ND1 . HIS A 116 ? 0.4892 0.4351 0.4025 0.0171 -0.0096 0.0620 119 HIS B ND1 970 C CD2 . HIS A 116 ? 0.4667 0.4233 0.3928 0.0117 0.0065 0.0542 119 HIS B CD2 971 C CE1 . HIS A 116 ? 0.4991 0.4419 0.3990 0.0138 -0.0010 0.0693 119 HIS B CE1 972 N NE2 . HIS A 116 ? 0.5043 0.4548 0.4136 0.0105 0.0091 0.0646 119 HIS B NE2 973 N N . PRO A 117 ? 0.3576 0.3250 0.2723 0.0163 -0.0021 0.0323 120 PRO B N 974 C CA . PRO A 117 ? 0.4050 0.3762 0.3170 0.0160 0.0055 0.0255 120 PRO B CA 975 C C . PRO A 117 ? 0.3774 0.3539 0.3001 0.0137 0.0169 0.0277 120 PRO B C 976 O O . PRO A 117 ? 0.3872 0.3624 0.3109 0.0116 0.0211 0.0360 120 PRO B O 977 C CB . PRO A 117 ? 0.4192 0.3847 0.3031 0.0190 0.0061 0.0253 120 PRO B CB 978 C CG . PRO A 117 ? 0.4482 0.4083 0.3205 0.0190 0.0044 0.0358 120 PRO B CG 979 C CD . PRO A 117 ? 0.4000 0.3599 0.2904 0.0182 -0.0055 0.0384 120 PRO B CD 980 N N . VAL A 118 ? 0.3447 0.3264 0.2763 0.0134 0.0206 0.0210 121 VAL B N 981 C CA . VAL A 118 ? 0.3559 0.3442 0.2981 0.0115 0.0298 0.0225 121 VAL B CA 982 C C . VAL A 118 ? 0.3800 0.3718 0.3096 0.0144 0.0391 0.0234 121 VAL B C 983 O O . VAL A 118 ? 0.4108 0.3979 0.3217 0.0187 0.0379 0.0194 121 VAL B O 984 C CB . VAL A 118 ? 0.3874 0.3794 0.3445 0.0107 0.0285 0.0158 121 VAL B CB 985 C CG1 . VAL A 118 ? 0.3760 0.3671 0.3257 0.0143 0.0280 0.0083 121 VAL B CG1 986 C CG2 . VAL A 118 ? 0.3822 0.3802 0.3541 0.0075 0.0339 0.0186 121 VAL B CG2 987 N N . CYS A 119 ? 0.3774 0.3774 0.3171 0.0122 0.0482 0.0288 122 CYS B N 988 C CA . CYS A 119 ? 0.3900 0.3974 0.3221 0.0159 0.0598 0.0302 122 CYS B CA 989 C C . CYS A 119 ? 0.3899 0.4033 0.3314 0.0200 0.0622 0.0219 122 CYS B C 990 O O . CYS A 119 ? 0.3346 0.3496 0.2934 0.0174 0.0569 0.0188 122 CYS B O 991 C CB . CYS A 119 ? 0.4005 0.4177 0.3452 0.0110 0.0691 0.0410 122 CYS B CB 992 S SG . CYS A 119 ? 0.4264 0.4349 0.3631 0.0052 0.0669 0.0535 122 CYS B SG 993 N N . LEU A 120 ? 0.3726 0.3883 0.3014 0.0270 0.0704 0.0186 123 LEU B N 994 C CA . LEU A 120 ? 0.3871 0.4092 0.3268 0.0323 0.0744 0.0120 123 LEU B CA 995 C C . LEU A 120 ? 0.4155 0.4554 0.3704 0.0330 0.0881 0.0192 123 LEU B C 996 O O . LEU A 120 ? 0.3641 0.4085 0.3088 0.0328 0.0978 0.0266 123 LEU B O 997 C CB . LEU A 120 ? 0.4310 0.4424 0.3483 0.0413 0.0739 0.0015 123 LEU B CB 998 C CG . LEU A 120 ? 0.4609 0.4560 0.3672 0.0396 0.0591 -0.0056 123 LEU B CG 999 C CD1 . LEU A 120 ? 0.5186 0.5012 0.4032 0.0479 0.0579 -0.0164 123 LEU B CD1 1000 C CD2 . LEU A 120 ? 0.4810 0.4768 0.4095 0.0346 0.0505 -0.0069 123 LEU B CD2 1001 N N . PRO A 121 ? 0.3867 0.4376 0.3668 0.0333 0.0888 0.0182 124 PRO B N 1002 C CA . PRO A 121 ? 0.4200 0.4912 0.4217 0.0326 0.1003 0.0262 124 PRO B CA 1003 C C . PRO A 121 ? 0.4303 0.5113 0.4238 0.0430 0.1164 0.0252 124 PRO B C 1004 O O . PRO A 121 ? 0.4484 0.5212 0.4268 0.0534 0.1171 0.0148 124 PRO B O 1005 C CB . PRO A 121 ? 0.4162 0.4943 0.4446 0.0318 0.0935 0.0235 124 PRO B CB 1006 C CG . PRO A 121 ? 0.4171 0.4797 0.4323 0.0375 0.0847 0.0124 124 PRO B CG 1007 C CD . PRO A 121 ? 0.4173 0.4628 0.4069 0.0347 0.0788 0.0104 124 PRO B CD 1008 N N . ASP A 122 ? 0.4300 0.5278 0.4336 0.0400 0.1293 0.0365 125 ASP B N 1009 C CA . ASP A 122 ? 0.4362 0.5526 0.4454 0.0491 0.1478 0.0385 125 ASP B CA 1010 C C . ASP A 122 ? 0.4696 0.6061 0.5184 0.0506 0.1484 0.0390 125 ASP B C 1011 O O . ASP A 122 ? 0.4134 0.5475 0.4812 0.0434 0.1338 0.0385 125 ASP B O 1012 C CB . ASP A 122 ? 0.4967 0.6253 0.5045 0.0432 0.1618 0.0530 125 ASP B CB 1013 C CG . ASP A 122 ? 0.5170 0.6539 0.5539 0.0278 0.1556 0.0655 125 ASP B CG 1014 O OD1 . ASP A 122 ? 0.5803 0.6996 0.6102 0.0194 0.1406 0.0654 125 ASP B OD1 1015 O OD2 . ASP A 122 ? 0.5432 0.7040 0.6110 0.0242 0.1652 0.0750 125 ASP B OD2 1016 N N . ARG A 123 ? 0.4166 0.5733 0.4774 0.0605 0.1652 0.0403 126 ARG B N 1017 C CA . ARG A 123 ? 0.4639 0.6421 0.5643 0.0641 0.1660 0.0410 126 ARG B CA 1018 C C . ARG A 123 ? 0.3890 0.5845 0.5267 0.0492 0.1599 0.0537 126 ARG B C 1019 O O . ARG A 123 ? 0.3542 0.5548 0.5180 0.0473 0.1480 0.0522 126 ARG B O 1020 C CB . ARG A 123 ? 0.4868 0.6866 0.5949 0.0785 0.1880 0.0412 126 ARG B CB 1021 C CG . ARG A 123 ? 0.5740 0.7909 0.7183 0.0875 0.1867 0.0378 126 ARG B CG 1022 C CD . ARG A 123 ? 0.6406 0.8793 0.7934 0.1042 0.2098 0.0369 126 ARG B CD 1023 N NE . ARG A 123 ? 0.7879 1.0054 0.8943 0.1178 0.2193 0.0249 126 ARG B NE 1024 C CZ . ARG A 123 ? 0.8324 1.0262 0.9178 0.1304 0.2116 0.0089 126 ARG B CZ 1025 N NH1 . ARG A 123 ? 0.8810 1.0548 0.9227 0.1414 0.2196 -0.0017 126 ARG B NH1 1026 N NH2 . ARG A 123 ? 0.7701 0.9583 0.8761 0.1318 0.1952 0.0036 126 ARG B NH2 1027 N N . GLU A 124 ? 0.4224 0.6252 0.5615 0.0386 0.1673 0.0664 127 GLU B N 1028 C CA . GLU A 124 ? 0.4283 0.6471 0.6041 0.0237 0.1619 0.0789 127 GLU B CA 1029 C C . GLU A 124 ? 0.3763 0.5732 0.5481 0.0132 0.1393 0.0751 127 GLU B C 1030 O O . GLU A 124 ? 0.3673 0.5712 0.5677 0.0058 0.1274 0.0773 127 GLU B O 1031 C CB . GLU A 124 ? 0.4797 0.7097 0.6577 0.0143 0.1757 0.0945 127 GLU B CB 1032 C CG . GLU A 124 ? 0.5916 0.8504 0.8184 0.0031 0.1777 0.1084 127 GLU B CG 1033 C CD . GLU A 124 ? 0.7273 0.9925 0.9571 -0.0101 0.1877 0.1257 127 GLU B CD 1034 O OE1 . GLU A 124 ? 0.8533 1.0931 1.0571 -0.0184 0.1793 0.1274 127 GLU B OE1 1035 O OE2 . GLU A 124 ? 0.6651 0.9611 0.9249 -0.0125 0.2041 0.1385 127 GLU B OE2 1036 N N . THR A 125 ? 0.3614 0.5318 0.4971 0.0132 0.1333 0.0691 128 THR B N 1037 C CA . THR A 125 ? 0.3567 0.5059 0.4856 0.0054 0.1141 0.0646 128 THR B CA 1038 C C . THR A 125 ? 0.3528 0.4980 0.4887 0.0110 0.1022 0.0540 128 THR B C 1039 O O . THR A 125 ? 0.3817 0.5231 0.5312 0.0033 0.0882 0.0538 128 THR B O 1040 C CB . THR A 125 ? 0.3953 0.5205 0.4870 0.0053 0.1117 0.0617 128 THR B CB 1041 O OG1 . THR A 125 ? 0.3986 0.5269 0.4862 -0.0013 0.1208 0.0739 128 THR B OG1 1042 C CG2 . THR A 125 ? 0.4193 0.5241 0.5044 -0.0009 0.0940 0.0564 128 THR B CG2 1043 N N . ALA A 126 ? 0.3448 0.4897 0.4707 0.0243 0.1076 0.0455 129 ALA B N 1044 C CA . ALA A 126 ? 0.3309 0.4716 0.4639 0.0302 0.0971 0.0370 129 ALA B CA 1045 C C . ALA A 126 ? 0.3128 0.4745 0.4844 0.0276 0.0930 0.0424 129 ALA B C 1046 O O . ALA A 126 ? 0.3047 0.4601 0.4843 0.0235 0.0776 0.0402 129 ALA B O 1047 C CB . ALA A 126 ? 0.3400 0.4756 0.4568 0.0455 0.1043 0.0275 129 ALA B CB 1048 N N . ALA A 127 A 0.2684 0.4559 0.4639 0.0303 0.1068 0.0499 129 ALA B N 1049 C CA . ALA A 127 A 0.2720 0.4840 0.5095 0.0279 0.1032 0.0564 129 ALA B CA 1050 C C . ALA A 127 A 0.2933 0.5028 0.5445 0.0107 0.0882 0.0630 129 ALA B C 1051 O O . ALA A 127 A 0.2783 0.4925 0.5509 0.0072 0.0738 0.0632 129 ALA B O 1052 C CB . ALA A 127 A 0.2799 0.5230 0.5423 0.0327 0.1235 0.0651 129 ALA B CB 1053 N N . SER A 128 B 0.2811 0.4813 0.5182 0.0006 0.0908 0.0680 129 SER B N 1054 C CA . SER A 128 B 0.3068 0.5037 0.5568 -0.0156 0.0789 0.0747 129 SER B CA 1055 C C . SER A 128 B 0.3103 0.4809 0.5417 -0.0197 0.0597 0.0662 129 SER B C 1056 O O . SER A 128 B 0.2663 0.4360 0.5135 -0.0289 0.0450 0.0677 129 SER B O 1057 C CB . SER A 128 B 0.3304 0.5221 0.5681 -0.0235 0.0883 0.0829 129 SER B CB 1058 O OG . SER A 128 B 0.4185 0.6370 0.6764 -0.0222 0.1066 0.0935 129 SER B OG 1059 N N . LEU A 129 C 0.2961 0.4455 0.4935 -0.0130 0.0599 0.0573 129 LEU B N 1060 C CA . LEU A 129 C 0.3348 0.4599 0.5121 -0.0169 0.0454 0.0504 129 LEU B CA 1061 C C . LEU A 129 C 0.3223 0.4416 0.4951 -0.0099 0.0362 0.0422 129 LEU B C 1062 O O . LEU A 129 C 0.3302 0.4350 0.4946 -0.0143 0.0229 0.0383 129 LEU B O 1063 C CB . LEU A 129 C 0.3416 0.4477 0.4873 -0.0154 0.0500 0.0472 129 LEU B CB 1064 C CG . LEU A 129 C 0.3709 0.4749 0.5133 -0.0226 0.0563 0.0552 129 LEU B CG 1065 C CD1 . LEU A 129 C 0.4118 0.4944 0.5232 -0.0201 0.0554 0.0504 129 LEU B CD1 1066 C CD2 . LEU A 129 C 0.3772 0.4812 0.5388 -0.0358 0.0474 0.0619 129 LEU B CD2 1067 N N . LEU A 130 ? 0.3039 0.4321 0.4797 0.0015 0.0434 0.0395 130 LEU B N 1068 C CA . LEU A 130 ? 0.3375 0.4566 0.5066 0.0081 0.0343 0.0327 130 LEU B CA 1069 C C . LEU A 130 ? 0.3310 0.4658 0.5300 0.0078 0.0252 0.0364 130 LEU B C 1070 O O . LEU A 130 ? 0.3691 0.5182 0.5852 0.0174 0.0294 0.0368 130 LEU B O 1071 C CB . LEU A 130 ? 0.3897 0.5036 0.5428 0.0207 0.0435 0.0264 130 LEU B CB 1072 C CG . LEU A 130 ? 0.4252 0.5196 0.5598 0.0247 0.0342 0.0192 130 LEU B CG 1073 C CD1 . LEU A 130 ? 0.4141 0.4892 0.5246 0.0175 0.0288 0.0165 130 LEU B CD1 1074 C CD2 . LEU A 130 ? 0.5523 0.6425 0.6770 0.0370 0.0421 0.0134 130 LEU B CD2 1075 N N . GLN A 131 ? 0.2638 0.3952 0.4691 -0.0032 0.0119 0.0389 131 GLN B N 1076 C CA . GLN A 131 ? 0.2665 0.4109 0.4989 -0.0061 -0.0006 0.0428 131 GLN B CA 1077 C C . GLN A 131 ? 0.2825 0.4063 0.4968 -0.0113 -0.0187 0.0386 131 GLN B C 1078 O O . GLN A 131 ? 0.2609 0.3649 0.4500 -0.0171 -0.0211 0.0347 131 GLN B O 1079 C CB . GLN A 131 ? 0.2886 0.4523 0.5510 -0.0165 0.0001 0.0517 131 GLN B CB 1080 C CG . GLN A 131 ? 0.3063 0.4890 0.5815 -0.0130 0.0206 0.0574 131 GLN B CG 1081 C CD . GLN A 131 ? 0.3050 0.5159 0.6217 -0.0208 0.0224 0.0685 131 GLN B CD 1082 O OE1 . GLN A 131 ? 0.3267 0.5566 0.6747 -0.0194 0.0147 0.0718 131 GLN B OE1 1083 N NE2 . GLN A 131 ? 0.3029 0.5176 0.6221 -0.0294 0.0322 0.0755 131 GLN B NE2 1084 N N . ALA A 132 ? 0.3058 0.4348 0.5330 -0.0086 -0.0311 0.0396 132 ALA B N 1085 C CA . ALA A 132 ? 0.3506 0.4606 0.5586 -0.0125 -0.0483 0.0363 132 ALA B CA 1086 C C . ALA A 132 ? 0.3117 0.4136 0.5162 -0.0259 -0.0585 0.0364 132 ALA B C 1087 O O . ALA A 132 ? 0.3228 0.4404 0.5554 -0.0335 -0.0617 0.0420 132 ALA B O 1088 C CB . ALA A 132 ? 0.3795 0.4990 0.6060 -0.0077 -0.0614 0.0395 132 ALA B CB 1089 N N . GLY A 133 ? 0.2906 0.3674 0.4611 -0.0287 -0.0634 0.0302 133 GLY B N 1090 C CA . GLY A 133 ? 0.3520 0.4152 0.5129 -0.0396 -0.0734 0.0279 133 GLY B CA 1091 C C . GLY A 133 ? 0.3401 0.3941 0.4892 -0.0427 -0.0616 0.0259 133 GLY B C 1092 O O . GLY A 133 ? 0.3923 0.4270 0.5225 -0.0485 -0.0679 0.0212 133 GLY B O 1093 N N . TYR A 134 ? 0.3178 0.3842 0.4765 -0.0382 -0.0451 0.0291 134 TYR B N 1094 C CA . TYR A 134 ? 0.3037 0.3610 0.4494 -0.0399 -0.0341 0.0281 134 TYR B CA 1095 C C . TYR A 134 ? 0.3273 0.3663 0.4407 -0.0335 -0.0301 0.0210 134 TYR B C 1096 O O . TYR A 134 ? 0.2980 0.3377 0.4040 -0.0261 -0.0283 0.0190 134 TYR B O 1097 C CB . TYR A 134 ? 0.2699 0.3456 0.4323 -0.0366 -0.0183 0.0343 134 TYR B CB 1098 C CG . TYR A 134 ? 0.2635 0.3599 0.4601 -0.0439 -0.0182 0.0434 134 TYR B CG 1099 C CD1 . TYR A 134 ? 0.2840 0.3824 0.4982 -0.0535 -0.0339 0.0456 134 TYR B CD1 1100 C CD2 . TYR A 134 ? 0.2711 0.3858 0.4825 -0.0414 -0.0022 0.0501 134 TYR B CD2 1101 C CE1 . TYR A 134 ? 0.3003 0.4200 0.5503 -0.0616 -0.0341 0.0553 134 TYR B CE1 1102 C CE2 . TYR A 134 ? 0.2755 0.4121 0.5207 -0.0485 0.0001 0.0601 134 TYR B CE2 1103 C CZ . TYR A 134 ? 0.2779 0.4179 0.5446 -0.0591 -0.0159 0.0631 134 TYR B CZ 1104 O OH . TYR A 134 ? 0.2873 0.4510 0.5916 -0.0675 -0.0140 0.0741 134 TYR B OH 1105 N N . LYS A 135 ? 0.2952 0.3182 0.3917 -0.0365 -0.0287 0.0177 135 LYS B N 1106 C CA . LYS A 135 ? 0.3027 0.3105 0.3723 -0.0311 -0.0248 0.0115 135 LYS B CA 1107 C C . LYS A 135 ? 0.3022 0.3124 0.3677 -0.0266 -0.0117 0.0125 135 LYS B C 1108 O O . LYS A 135 ? 0.3340 0.3483 0.4085 -0.0294 -0.0067 0.0168 135 LYS B O 1109 C CB . LYS A 135 ? 0.3094 0.2972 0.3615 -0.0351 -0.0320 0.0059 135 LYS B CB 1110 C CG . LYS A 135 ? 0.3445 0.3249 0.3896 -0.0380 -0.0460 0.0028 135 LYS B CG 1111 C CD . LYS A 135 ? 0.3508 0.3095 0.3777 -0.0417 -0.0533 -0.0038 135 LYS B CD 1112 C CE . LYS A 135 ? 0.3741 0.3232 0.3886 -0.0443 -0.0681 -0.0077 135 LYS B CE 1113 N NZ . LYS A 135 ? 0.4102 0.3353 0.4032 -0.0469 -0.0747 -0.0159 135 LYS B NZ 1114 N N . GLY A 136 ? 0.2949 0.3020 0.3467 -0.0201 -0.0070 0.0093 136 GLY B N 1115 C CA . GLY A 136 ? 0.3023 0.3078 0.3461 -0.0163 0.0022 0.0089 136 GLY B CA 1116 C C . GLY A 136 ? 0.3272 0.3202 0.3530 -0.0143 0.0019 0.0039 136 GLY B C 1117 O O . GLY A 136 ? 0.2914 0.2761 0.3083 -0.0156 -0.0039 0.0007 136 GLY B O 1118 N N . ARG A 137 ? 0.3261 0.3185 0.3463 -0.0108 0.0082 0.0036 137 ARG B N 1119 C CA . ARG A 137 ? 0.3668 0.3508 0.3749 -0.0088 0.0093 0.0000 137 ARG B CA 1120 C C . ARG A 137 ? 0.3404 0.3281 0.3453 -0.0052 0.0131 -0.0003 137 ARG B C 1121 O O . ARG A 137 ? 0.3142 0.3072 0.3227 -0.0034 0.0158 0.0013 137 ARG B O 1122 C CB . ARG A 137 ? 0.3921 0.3705 0.3997 -0.0088 0.0111 0.0004 137 ARG B CB 1123 C CG . ARG A 137 ? 0.3954 0.3690 0.3955 -0.0048 0.0139 -0.0025 137 ARG B CG 1124 C CD . ARG A 137 ? 0.4488 0.4162 0.4504 -0.0039 0.0143 -0.0012 137 ARG B CD 1125 N NE . ARG A 137 ? 0.3930 0.3481 0.3922 -0.0061 0.0101 -0.0037 137 ARG B NE 1126 C CZ . ARG A 137 ? 0.3913 0.3369 0.3923 -0.0064 0.0086 -0.0021 137 ARG B CZ 1127 N NH1 . ARG A 137 ? 0.3995 0.3478 0.4043 -0.0045 0.0111 0.0029 137 ARG B NH1 1128 N NH2 . ARG A 137 ? 0.3698 0.3011 0.3673 -0.0088 0.0034 -0.0056 137 ARG B NH2 1129 N N . VAL A 138 ? 0.3029 0.2868 0.2999 -0.0044 0.0131 -0.0024 138 VAL B N 1130 C CA . VAL A 138 ? 0.3300 0.3164 0.3256 -0.0029 0.0154 -0.0020 138 VAL B CA 1131 C C . VAL A 138 ? 0.3489 0.3344 0.3416 -0.0016 0.0191 -0.0031 138 VAL B C 1132 O O . VAL A 138 ? 0.3304 0.3112 0.3170 -0.0010 0.0202 -0.0052 138 VAL B O 1133 C CB . VAL A 138 ? 0.3417 0.3262 0.3333 -0.0039 0.0127 -0.0010 138 VAL B CB 1134 C CG1 . VAL A 138 ? 0.3979 0.3834 0.3902 -0.0037 0.0141 0.0003 138 VAL B CG1 1135 C CG2 . VAL A 138 ? 0.3886 0.3754 0.3863 -0.0038 0.0085 0.0000 138 VAL B CG2 1136 N N . THR A 139 ? 0.3299 0.3200 0.3275 -0.0007 0.0206 -0.0020 139 THR B N 1137 C CA . THR A 139 ? 0.3205 0.3140 0.3215 0.0010 0.0239 -0.0019 139 THR B CA 1138 C C . THR A 139 ? 0.3188 0.3177 0.3247 -0.0009 0.0241 0.0003 139 THR B C 1139 O O . THR A 139 ? 0.3148 0.3128 0.3215 -0.0028 0.0204 0.0009 139 THR B O 1140 C CB . THR A 139 ? 0.3743 0.3692 0.3805 0.0034 0.0227 -0.0014 139 THR B CB 1141 O OG1 . THR A 139 ? 0.3468 0.3420 0.3524 0.0024 0.0196 -0.0003 139 THR B OG1 1142 C CG2 . THR A 139 ? 0.3815 0.3697 0.3850 0.0052 0.0230 -0.0027 139 THR B CG2 1143 N N . GLY A 140 ? 0.2971 0.3015 0.3072 -0.0005 0.0288 0.0015 140 GLY B N 1144 C CA . GLY A 140 ? 0.2617 0.2729 0.2808 -0.0039 0.0289 0.0050 140 GLY B CA 1145 C C . GLY A 140 ? 0.2973 0.3178 0.3231 -0.0034 0.0366 0.0075 140 GLY B C 1146 O O . GLY A 140 ? 0.3113 0.3309 0.3310 0.0010 0.0428 0.0052 140 GLY B O 1147 N N . TRP A 141 ? 0.3026 0.3317 0.3415 -0.0077 0.0362 0.0119 141 TRP B N 1148 C CA . TRP A 141 ? 0.3194 0.3619 0.3701 -0.0083 0.0448 0.0164 141 TRP B CA 1149 C C . TRP A 141 ? 0.3212 0.3627 0.3677 -0.0149 0.0484 0.0222 141 TRP B C 1150 O O . TRP A 141 ? 0.3382 0.3925 0.3975 -0.0181 0.0553 0.0283 141 TRP B O 1151 C CB . TRP A 141 ? 0.3263 0.3824 0.4005 -0.0099 0.0409 0.0192 141 TRP B CB 1152 C CG . TRP A 141 ? 0.3504 0.4100 0.4313 -0.0027 0.0384 0.0158 141 TRP B CG 1153 C CD1 . TRP A 141 ? 0.3515 0.4193 0.4397 0.0049 0.0460 0.0149 141 TRP B CD1 1154 C CD2 . TRP A 141 ? 0.3209 0.3746 0.4007 -0.0020 0.0275 0.0135 141 TRP B CD2 1155 N NE1 . TRP A 141 ? 0.3299 0.3965 0.4231 0.0100 0.0393 0.0128 141 TRP B NE1 1156 C CE2 . TRP A 141 ? 0.3324 0.3906 0.4193 0.0055 0.0282 0.0124 141 TRP B CE2 1157 C CE3 . TRP A 141 ? 0.3786 0.4224 0.4502 -0.0062 0.0177 0.0121 141 TRP B CE3 1158 C CZ2 . TRP A 141 ? 0.3703 0.4237 0.4557 0.0078 0.0189 0.0115 141 TRP B CZ2 1159 C CZ3 . TRP A 141 ? 0.4035 0.4432 0.4719 -0.0033 0.0099 0.0102 141 TRP B CZ3 1160 C CH2 . TRP A 141 ? 0.3916 0.4362 0.4665 0.0030 0.0103 0.0106 141 TRP B CH2 1161 N N . GLY A 142 ? 0.3462 0.3735 0.3766 -0.0171 0.0438 0.0213 142 GLY B N 1162 C CA . GLY A 142 ? 0.3313 0.3541 0.3557 -0.0232 0.0450 0.0277 142 GLY B CA 1163 C C . GLY A 142 ? 0.3545 0.3787 0.3652 -0.0213 0.0559 0.0301 142 GLY B C 1164 O O . GLY A 142 ? 0.3102 0.3393 0.3176 -0.0149 0.0632 0.0260 142 GLY B O 1165 N N . ASN A 143 ? 0.3310 0.3485 0.3314 -0.0265 0.0566 0.0367 143 ASN B N 1166 C CA . ASN A 143 ? 0.4059 0.4243 0.3901 -0.0257 0.0677 0.0408 143 ASN B CA 1167 C C . ASN A 143 ? 0.4250 0.4345 0.3864 -0.0180 0.0687 0.0326 143 ASN B C 1168 O O . ASN A 143 ? 0.3814 0.3798 0.3358 -0.0160 0.0585 0.0269 143 ASN B O 1169 C CB . ASN A 143 ? 0.4343 0.4440 0.4090 -0.0333 0.0660 0.0507 143 ASN B CB 1170 C CG . ASN A 143 ? 0.4540 0.4724 0.4510 -0.0423 0.0670 0.0601 143 ASN B CG 1171 O OD1 . ASN A 143 ? 0.5074 0.5422 0.5269 -0.0430 0.0713 0.0603 143 ASN B OD1 1172 N ND2 . ASN A 143 ? 0.4745 0.4815 0.4665 -0.0496 0.0619 0.0685 143 ASN B ND2 1173 N N . LEU A 144 ? 0.3898 0.4045 0.3408 -0.0136 0.0813 0.0321 144 LEU B N 1174 C CA . LEU A 144 ? 0.4168 0.4206 0.3425 -0.0066 0.0829 0.0240 144 LEU B CA 1175 C C . LEU A 144 ? 0.4777 0.4672 0.3746 -0.0094 0.0801 0.0277 144 LEU B C 1176 O O . LEU A 144 ? 0.4962 0.4728 0.3698 -0.0052 0.0763 0.0209 144 LEU B O 1177 C CB . LEU A 144 ? 0.4432 0.4567 0.3670 0.0007 0.0984 0.0210 144 LEU B CB 1178 C CG . LEU A 144 ? 0.4537 0.4801 0.4045 0.0058 0.1004 0.0166 144 LEU B CG 1179 C CD1 . LEU A 144 ? 0.4419 0.4790 0.3922 0.0144 0.1173 0.0145 144 LEU B CD1 1180 C CD2 . LEU A 144 ? 0.4553 0.4696 0.4046 0.0094 0.0884 0.0072 144 LEU B CD2 1181 N N . LYS A 145 ? 0.4681 0.4580 0.3644 -0.0166 0.0808 0.0390 145 LYS B N 1182 C CA . LYS A 145 ? 0.5721 0.5481 0.4410 -0.0196 0.0776 0.0451 145 LYS B CA 1183 C C . LYS A 145 ? 0.5365 0.5115 0.4180 -0.0285 0.0722 0.0567 145 LYS B C 1184 O O . LYS A 145 ? 0.4882 0.4736 0.3974 -0.0322 0.0727 0.0591 145 LYS B O 1185 C CB . LYS A 145 ? 0.6753 0.6533 0.5200 -0.0169 0.0935 0.0478 145 LYS B CB 1186 C CG . LYS A 145 ? 0.9604 0.9574 0.8222 -0.0204 0.1102 0.0578 145 LYS B CG 1187 C CD . LYS A 145 ? 1.1125 1.1124 0.9479 -0.0168 0.1285 0.0612 145 LYS B CD 1188 C CE . LYS A 145 ? 1.1954 1.2198 1.0556 -0.0196 0.1469 0.0709 145 LYS B CE 1189 N NZ . LYS A 145 ? 1.1423 1.1711 1.0222 -0.0326 0.1433 0.0863 145 LYS B NZ 1190 N N . GLU A 146 ? 0.5613 0.5232 0.4239 -0.0318 0.0666 0.0640 146 GLU B N 1191 C CA . GLU A 146 ? 0.5575 0.5153 0.4286 -0.0403 0.0629 0.0767 146 GLU B CA 1192 C C . GLU A 146 ? 0.5938 0.5641 0.4700 -0.0462 0.0791 0.0879 146 GLU B C 1193 O O . GLU A 146 ? 0.6056 0.5793 0.4604 -0.0438 0.0922 0.0902 146 GLU B O 1194 C CB . GLU A 146 ? 0.6015 0.5401 0.4471 -0.0414 0.0523 0.0829 146 GLU B CB 1195 C CG . GLU A 146 ? 0.5827 0.5110 0.4279 -0.0364 0.0354 0.0742 146 GLU B CG 1196 C CD . GLU A 146 ? 0.5701 0.4807 0.3934 -0.0371 0.0234 0.0816 146 GLU B CD 1197 O OE1 . GLU A 146 ? 0.5486 0.4526 0.3677 -0.0324 0.0104 0.0752 146 GLU B OE1 1198 O OE2 . GLU A 146 ? 0.6768 0.5807 0.4885 -0.0426 0.0264 0.0948 146 GLU B OE2 1199 N N . THR A 147 ? 0.6888 0.6664 0.5934 -0.0538 0.0784 0.0946 147 THR B N 1200 C CA . THR A 147 ? 0.8901 0.8816 0.8069 -0.0619 0.0925 0.1077 147 THR B CA 1201 C C . THR A 147 ? 0.9039 0.8837 0.8283 -0.0733 0.0843 0.1214 147 THR B C 1202 O O . THR A 147 ? 0.9626 0.9216 0.8671 -0.0739 0.0738 0.1252 147 THR B O 1203 C CB . THR A 147 ? 0.9736 0.9883 0.9248 -0.0618 0.0993 0.1034 147 THR B CB 1204 O OG1 . THR A 147 ? 0.8756 0.9002 0.8202 -0.0508 0.1081 0.0920 147 THR B OG1 1205 C CG2 . THR A 147 ? 1.0398 1.0718 1.0105 -0.0717 0.1125 0.1185 147 THR B CG2 1206 N N . GLY A 155 ? 0.6262 0.7008 0.5880 -0.0091 0.1503 0.0557 150 GLY B N 1207 C CA . GLY A 155 ? 0.5859 0.6559 0.5642 -0.0203 0.1342 0.0616 150 GLY B CA 1208 C C . GLY A 155 ? 0.4608 0.5286 0.4577 -0.0182 0.1192 0.0527 150 GLY B C 1209 O O . GLY A 155 ? 0.4746 0.5246 0.4588 -0.0185 0.1053 0.0471 150 GLY B O 1210 N N . GLN A 156 ? 0.4525 0.5394 0.4802 -0.0160 0.1222 0.0522 151 GLN B N 1211 C CA . GLN A 156 ? 0.4587 0.5447 0.5040 -0.0143 0.1084 0.0453 151 GLN B CA 1212 C C . GLN A 156 ? 0.4022 0.4926 0.4488 -0.0014 0.1139 0.0357 151 GLN B C 1213 O O . GLN A 156 ? 0.3775 0.4817 0.4289 0.0049 0.1291 0.0367 151 GLN B O 1214 C CB . GLN A 156 ? 0.5149 0.6176 0.5950 -0.0228 0.1040 0.0532 151 GLN B CB 1215 C CG . GLN A 156 ? 0.6662 0.7673 0.7483 -0.0357 0.1032 0.0650 151 GLN B CG 1216 C CD . GLN A 156 ? 0.7927 0.9184 0.9096 -0.0434 0.1093 0.0760 151 GLN B CD 1217 O OE1 . GLN A 156 ? 0.8922 1.0291 1.0109 -0.0473 0.1239 0.0862 151 GLN B OE1 1218 N NE2 . GLN A 156 ? 0.8650 0.9994 1.0098 -0.0460 0.0980 0.0746 151 GLN B NE2 1219 N N . PRO A 157 ? 0.3525 0.4304 0.3946 0.0029 0.1022 0.0268 152 PRO B N 1220 C CA . PRO A 157 ? 0.3490 0.4264 0.3904 0.0150 0.1060 0.0180 152 PRO B CA 1221 C C . PRO A 157 ? 0.3411 0.4379 0.4157 0.0193 0.1067 0.0195 152 PRO B C 1222 O O . PRO A 157 ? 0.3400 0.4464 0.4366 0.0122 0.0982 0.0250 152 PRO B O 1223 C CB . PRO A 157 ? 0.3327 0.3896 0.3592 0.0154 0.0920 0.0108 152 PRO B CB 1224 C CG . PRO A 157 ? 0.3326 0.3887 0.3679 0.0054 0.0801 0.0158 152 PRO B CG 1225 C CD . PRO A 157 ? 0.3385 0.4012 0.3746 -0.0023 0.0860 0.0246 152 PRO B CD 1226 N N . SER A 158 ? 0.3513 0.4519 0.4289 0.0314 0.1149 0.0138 153 SER B N 1227 C CA . SER A 158 ? 0.3656 0.4831 0.4751 0.0371 0.1131 0.0150 153 SER B CA 1228 C C . SER A 158 ? 0.3135 0.4188 0.4248 0.0365 0.0956 0.0116 153 SER B C 1229 O O . SER A 158 ? 0.2912 0.4092 0.4281 0.0357 0.0880 0.0156 153 SER B O 1230 C CB . SER A 158 ? 0.4563 0.5811 0.5700 0.0521 0.1277 0.0101 153 SER B CB 1231 O OG . SER A 158 ? 0.5671 0.6668 0.6484 0.0593 0.1286 -0.0004 153 SER B OG 1232 N N . VAL A 159 ? 0.2879 0.3694 0.3725 0.0364 0.0889 0.0052 154 VAL B N 1233 C CA . VAL A 159 ? 0.2763 0.3460 0.3602 0.0364 0.0749 0.0028 154 VAL B CA 1234 C C . VAL A 159 ? 0.2772 0.3296 0.3393 0.0285 0.0667 0.0013 154 VAL B C 1235 O O . VAL A 159 ? 0.2727 0.3176 0.3166 0.0255 0.0709 0.0001 154 VAL B O 1236 C CB . VAL A 159 ? 0.2868 0.3458 0.3669 0.0481 0.0756 -0.0038 154 VAL B CB 1237 C CG1 . VAL A 159 ? 0.2973 0.3738 0.4004 0.0588 0.0849 -0.0031 154 VAL B CG1 1238 C CG2 . VAL A 159 ? 0.3139 0.3525 0.3652 0.0508 0.0797 -0.0115 154 VAL B CG2 1239 N N . LEU A 160 ? 0.2648 0.3111 0.3286 0.0260 0.0552 0.0017 155 LEU B N 1240 C CA . LEU A 160 ? 0.2872 0.3199 0.3347 0.0198 0.0479 0.0005 155 LEU B CA 1241 C C . LEU A 160 ? 0.3084 0.3262 0.3345 0.0212 0.0510 -0.0046 155 LEU B C 1242 O O . LEU A 160 ? 0.3167 0.3269 0.3375 0.0280 0.0539 -0.0093 155 LEU B O 1243 C CB . LEU A 160 ? 0.2767 0.3043 0.3266 0.0201 0.0381 0.0010 155 LEU B CB 1244 C CG . LEU A 160 ? 0.3109 0.3277 0.3472 0.0147 0.0321 0.0004 155 LEU B CG 1245 C CD1 . LEU A 160 ? 0.3065 0.3276 0.3438 0.0081 0.0297 0.0028 155 LEU B CD1 1246 C CD2 . LEU A 160 ? 0.3385 0.3501 0.3744 0.0160 0.0253 0.0014 155 LEU B CD2 1247 N N . GLN A 161 ? 0.2974 0.3100 0.3116 0.0150 0.0491 -0.0039 156 GLN B N 1248 C CA . GLN A 161 ? 0.3082 0.3072 0.3027 0.0150 0.0490 -0.0080 156 GLN B CA 1249 C C . GLN A 161 ? 0.3257 0.3156 0.3160 0.0113 0.0398 -0.0087 156 GLN B C 1250 O O . GLN A 161 ? 0.3201 0.3143 0.3184 0.0081 0.0353 -0.0056 156 GLN B O 1251 C CB . GLN A 161 ? 0.3114 0.3114 0.2953 0.0114 0.0532 -0.0057 156 GLN B CB 1252 C CG . GLN A 161 ? 0.3346 0.3448 0.3212 0.0147 0.0650 -0.0040 156 GLN B CG 1253 C CD . GLN A 161 ? 0.3662 0.3702 0.3419 0.0236 0.0722 -0.0108 156 GLN B CD 1254 O OE1 . GLN A 161 ? 0.3795 0.3699 0.3321 0.0247 0.0725 -0.0155 156 GLN B OE1 1255 N NE2 . GLN A 161 ? 0.4004 0.4135 0.3923 0.0304 0.0773 -0.0118 156 GLN B NE2 1256 N N . VAL A 162 ? 0.3505 0.3280 0.3281 0.0118 0.0373 -0.0130 157 VAL B N 1257 C CA . VAL A 162 ? 0.3309 0.3015 0.3074 0.0079 0.0294 -0.0130 157 VAL B CA 1258 C C . VAL A 162 ? 0.3638 0.3248 0.3256 0.0053 0.0255 -0.0158 157 VAL B C 1259 O O . VAL A 162 ? 0.3495 0.3026 0.2975 0.0082 0.0282 -0.0203 157 VAL B O 1260 C CB . VAL A 162 ? 0.3600 0.3243 0.3417 0.0101 0.0268 -0.0142 157 VAL B CB 1261 C CG1 . VAL A 162 ? 0.3950 0.3472 0.3680 0.0151 0.0286 -0.0202 157 VAL B CG1 1262 C CG2 . VAL A 162 ? 0.4027 0.3634 0.3867 0.0049 0.0203 -0.0121 157 VAL B CG2 1263 N N . VAL A 163 ? 0.3298 0.2917 0.2944 0.0006 0.0191 -0.0133 158 VAL B N 1264 C CA . VAL A 163 ? 0.3653 0.3192 0.3196 -0.0024 0.0123 -0.0150 158 VAL B CA 1265 C C . VAL A 163 ? 0.3754 0.3326 0.3422 -0.0066 0.0054 -0.0123 158 VAL B C 1266 O O . VAL A 163 ? 0.3506 0.3174 0.3300 -0.0067 0.0074 -0.0084 158 VAL B O 1267 C CB . VAL A 163 ? 0.4168 0.3717 0.3604 -0.0032 0.0128 -0.0129 158 VAL B CB 1268 C CG1 . VAL A 163 ? 0.4128 0.3768 0.3679 -0.0052 0.0111 -0.0074 158 VAL B CG1 1269 C CG2 . VAL A 163 ? 0.4712 0.4148 0.3981 -0.0051 0.0051 -0.0158 158 VAL B CG2 1270 N N . ASN A 164 ? 0.3477 0.2970 0.3113 -0.0100 -0.0025 -0.0144 159 ASN B N 1271 C CA . ASN A 164 ? 0.3470 0.3022 0.3260 -0.0146 -0.0089 -0.0107 159 ASN B CA 1272 C C . ASN A 164 ? 0.3611 0.3179 0.3381 -0.0168 -0.0168 -0.0095 159 ASN B C 1273 O O . ASN A 164 ? 0.3657 0.3119 0.3252 -0.0171 -0.0218 -0.0130 159 ASN B O 1274 C CB . ASN A 164 ? 0.3525 0.2986 0.3347 -0.0186 -0.0143 -0.0125 159 ASN B CB 1275 C CG . ASN A 164 ? 0.3405 0.2826 0.3249 -0.0162 -0.0082 -0.0127 159 ASN B CG 1276 O OD1 . ASN A 164 ? 0.3524 0.3032 0.3421 -0.0129 -0.0010 -0.0097 159 ASN B OD1 1277 N ND2 . ASN A 164 ? 0.3876 0.3148 0.3677 -0.0179 -0.0128 -0.0163 159 ASN B ND2 1278 N N . LEU A 165 ? 0.3106 0.2799 0.3041 -0.0174 -0.0181 -0.0045 160 LEU B N 1279 C CA . LEU A 165 ? 0.3253 0.2974 0.3195 -0.0177 -0.0256 -0.0023 160 LEU B CA 1280 C C . LEU A 165 ? 0.3191 0.3047 0.3376 -0.0196 -0.0301 0.0021 160 LEU B C 1281 O O . LEU A 165 ? 0.2878 0.2839 0.3212 -0.0184 -0.0227 0.0047 160 LEU B O 1282 C CB . LEU A 165 ? 0.3435 0.3172 0.3315 -0.0133 -0.0204 -0.0005 160 LEU B CB 1283 C CG . LEU A 165 ? 0.3721 0.3362 0.3389 -0.0119 -0.0151 -0.0029 160 LEU B CG 1284 C CD1 . LEU A 165 ? 0.3986 0.3662 0.3661 -0.0094 -0.0098 0.0005 160 LEU B CD1 1285 C CD2 . LEU A 165 ? 0.3801 0.3326 0.3264 -0.0134 -0.0222 -0.0048 160 LEU B CD2 1286 N N . PRO A 166 ? 0.2886 0.2748 0.3112 -0.0223 -0.0421 0.0035 161 PRO B N 1287 C CA . PRO A 166 ? 0.2712 0.2737 0.3216 -0.0238 -0.0463 0.0085 161 PRO B CA 1288 C C . PRO A 166 ? 0.3085 0.3219 0.3693 -0.0168 -0.0425 0.0118 161 PRO B C 1289 O O . PRO A 166 ? 0.3205 0.3258 0.3664 -0.0131 -0.0441 0.0113 161 PRO B O 1290 C CB . PRO A 166 ? 0.2862 0.2837 0.3358 -0.0291 -0.0631 0.0083 161 PRO B CB 1291 C CG . PRO A 166 ? 0.2931 0.2735 0.3115 -0.0270 -0.0665 0.0045 161 PRO B CG 1292 C CD . PRO A 166 ? 0.2987 0.2712 0.3004 -0.0240 -0.0527 0.0008 161 PRO B CD 1293 N N . ILE A 167 ? 0.3262 0.3566 0.4114 -0.0147 -0.0366 0.0154 162 ILE B N 1294 C CA . ILE A 167 ? 0.2928 0.3342 0.3916 -0.0068 -0.0335 0.0179 162 ILE B CA 1295 C C . ILE A 167 ? 0.3238 0.3696 0.4343 -0.0067 -0.0476 0.0210 162 ILE B C 1296 O O . ILE A 167 ? 0.3237 0.3741 0.4454 -0.0134 -0.0580 0.0230 162 ILE B O 1297 C CB . ILE A 167 ? 0.3031 0.3628 0.4245 -0.0042 -0.0222 0.0206 162 ILE B CB 1298 C CG1 . ILE A 167 ? 0.3428 0.3962 0.4490 -0.0031 -0.0095 0.0178 162 ILE B CG1 1299 C CG2 . ILE A 167 ? 0.3205 0.3920 0.4580 0.0057 -0.0194 0.0222 162 ILE B CG2 1300 C CD1 . ILE A 167 ? 0.3446 0.4121 0.4658 -0.0042 0.0008 0.0215 162 ILE B CD1 1301 N N . VAL A 168 ? 0.3148 0.3580 0.4228 0.0008 -0.0495 0.0219 163 VAL B N 1302 C CA . VAL A 168 ? 0.3415 0.3859 0.4570 0.0023 -0.0643 0.0256 163 VAL B CA 1303 C C . VAL A 168 ? 0.3410 0.4033 0.4863 0.0116 -0.0618 0.0290 163 VAL B C 1304 O O . VAL A 168 ? 0.3588 0.4235 0.5061 0.0189 -0.0489 0.0269 163 VAL B O 1305 C CB . VAL A 168 ? 0.3763 0.3998 0.4621 0.0035 -0.0699 0.0251 163 VAL B CB 1306 C CG1 . VAL A 168 ? 0.3874 0.4104 0.4791 0.0064 -0.0857 0.0303 163 VAL B CG1 1307 C CG2 . VAL A 168 ? 0.4089 0.4170 0.4665 -0.0045 -0.0714 0.0216 163 VAL B CG2 1308 N N . GLU A 169 ? 0.3346 0.4088 0.5024 0.0118 -0.0750 0.0338 164 GLU B N 1309 C CA . GLU A 169 ? 0.3682 0.4632 0.5704 0.0214 -0.0738 0.0376 164 GLU B CA 1310 C C . GLU A 169 ? 0.3638 0.4471 0.5567 0.0330 -0.0730 0.0369 164 GLU B C 1311 O O . GLU A 169 ? 0.3384 0.4004 0.5050 0.0315 -0.0816 0.0370 164 GLU B O 1312 C CB . GLU A 169 ? 0.4281 0.5373 0.6564 0.0184 -0.0922 0.0437 164 GLU B CB 1313 C CG . GLU A 169 ? 0.5298 0.6419 0.7607 0.0043 -0.1010 0.0445 164 GLU B CG 1314 C CD . GLU A 169 ? 0.5978 0.6845 0.7932 -0.0032 -0.1164 0.0420 164 GLU B CD 1315 O OE1 . GLU A 169 ? 0.6805 0.7653 0.8783 -0.0033 -0.1353 0.0456 164 GLU B OE1 1316 O OE2 . GLU A 169 ? 0.4867 0.5556 0.6515 -0.0082 -0.1093 0.0365 164 GLU B OE2 1317 N N . ARG A 170 ? 0.3870 0.4834 0.6014 0.0446 -0.0628 0.0364 165 ARG B N 1318 C CA . ARG A 170 ? 0.4216 0.5035 0.6267 0.0562 -0.0608 0.0342 165 ARG B CA 1319 C C . ARG A 170 ? 0.3967 0.4673 0.5997 0.0592 -0.0793 0.0394 165 ARG B C 1320 O O . ARG A 170 ? 0.4280 0.4751 0.6066 0.0611 -0.0818 0.0388 165 ARG B O 1321 C CB . ARG A 170 ? 0.4867 0.5845 0.7157 0.0700 -0.0467 0.0316 165 ARG B CB 1322 C CG . ARG A 170 ? 0.6155 0.6926 0.8287 0.0814 -0.0424 0.0265 165 ARG B CG 1323 C CD . ARG A 170 ? 0.6659 0.7518 0.8878 0.0933 -0.0242 0.0201 165 ARG B CD 1324 N NE . ARG A 170 ? 0.6404 0.7260 0.8446 0.0861 -0.0104 0.0156 165 ARG B NE 1325 C CZ . ARG A 170 ? 0.6846 0.7479 0.8578 0.0836 -0.0061 0.0097 165 ARG B CZ 1326 N NH1 . ARG A 170 ? 0.6249 0.6633 0.7806 0.0863 -0.0136 0.0074 165 ARG B NH1 1327 N NH2 . ARG A 170 ? 0.7326 0.7986 0.8934 0.0775 0.0049 0.0069 165 ARG B NH2 1328 N N . PRO A 171 ? 0.4063 0.4934 0.6354 0.0591 -0.0931 0.0456 166 PRO B N 1329 C CA . PRO A 171 ? 0.4342 0.5092 0.6589 0.0620 -0.1125 0.0515 166 PRO B CA 1330 C C . PRO A 171 ? 0.4203 0.4687 0.6032 0.0514 -0.1215 0.0524 166 PRO B C 1331 O O . PRO A 171 ? 0.3985 0.4272 0.5640 0.0549 -0.1305 0.0563 166 PRO B O 1332 C CB . PRO A 171 ? 0.4484 0.5487 0.7088 0.0606 -0.1263 0.0575 166 PRO B CB 1333 C CG . PRO A 171 ? 0.4225 0.5516 0.7170 0.0643 -0.1097 0.0554 166 PRO B CG 1334 C CD . PRO A 171 ? 0.4076 0.5260 0.6748 0.0574 -0.0922 0.0485 166 PRO B CD 1335 N N . VAL A 172 ? 0.4028 0.4501 0.5696 0.0391 -0.1185 0.0492 167 VAL B N 1336 C CA . VAL A 172 ? 0.4309 0.4549 0.5577 0.0300 -0.1247 0.0492 167 VAL B CA 1337 C C . VAL A 172 ? 0.4312 0.4363 0.5322 0.0316 -0.1115 0.0463 167 VAL B C 1338 O O . VAL A 172 ? 0.4580 0.4427 0.5320 0.0299 -0.1171 0.0499 167 VAL B O 1339 C CB . VAL A 172 ? 0.4185 0.4454 0.5364 0.0178 -0.1255 0.0455 167 VAL B CB 1340 C CG1 . VAL A 172 ? 0.4629 0.4654 0.5369 0.0106 -0.1266 0.0437 167 VAL B CG1 1341 C CG2 . VAL A 172 ? 0.4286 0.4696 0.5687 0.0141 -0.1438 0.0494 167 VAL B CG2 1342 N N . CYS A 173 ? 0.3883 0.4004 0.4978 0.0344 -0.0945 0.0406 168 CYS B N 1343 C CA . CYS A 173 ? 0.3960 0.3922 0.4863 0.0359 -0.0830 0.0373 168 CYS B CA 1344 C C . CYS A 173 ? 0.4151 0.3977 0.5052 0.0446 -0.0894 0.0415 168 CYS B C 1345 O O . CYS A 173 ? 0.3893 0.3512 0.4555 0.0417 -0.0907 0.0441 168 CYS B O 1346 C CB . CYS A 173 ? 0.3818 0.3891 0.4836 0.0391 -0.0661 0.0305 168 CYS B CB 1347 S SG . CYS A 173 ? 0.4243 0.4440 0.5251 0.0292 -0.0569 0.0264 168 CYS B SG 1348 N N . LYS A 174 ? 0.4177 0.4120 0.5362 0.0553 -0.0936 0.0430 169 LYS B N 1349 C CA . LYS A 174 ? 0.4249 0.4052 0.5466 0.0657 -0.0999 0.0463 169 LYS B CA 1350 C C . LYS A 174 ? 0.4803 0.4427 0.5831 0.0619 -0.1164 0.0555 169 LYS B C 1351 O O . LYS A 174 ? 0.4756 0.4150 0.5605 0.0626 -0.1182 0.0588 169 LYS B O 1352 C CB . LYS A 174 ? 0.4471 0.4463 0.6060 0.0794 -0.1013 0.0462 169 LYS B CB 1353 C CG . LYS A 174 ? 0.5095 0.4930 0.6733 0.0915 -0.1106 0.0502 169 LYS B CG 1354 C CD . LYS A 174 ? 0.6153 0.6180 0.8171 0.1079 -0.1080 0.0481 169 LYS B CD 1355 C CE . LYS A 174 ? 0.7097 0.7025 0.9229 0.1185 -0.1253 0.0559 169 LYS B CE 1356 N NZ . LYS A 174 ? 0.7387 0.7046 0.9422 0.1292 -0.1227 0.0529 169 LYS B NZ 1357 N N . ASP A 175 ? 0.4631 0.4347 0.5685 0.0570 -0.1292 0.0602 170 ASP B N 1358 C CA . ASP A 175 ? 0.5373 0.4921 0.6217 0.0537 -0.1465 0.0695 170 ASP B CA 1359 C C . ASP A 175 ? 0.5113 0.4461 0.5539 0.0420 -0.1432 0.0711 170 ASP B C 1360 O O . ASP A 175 ? 0.5505 0.4677 0.5699 0.0395 -0.1547 0.0797 170 ASP B O 1361 C CB . ASP A 175 ? 0.5857 0.5564 0.6860 0.0525 -0.1635 0.0733 170 ASP B CB 1362 C CG . ASP A 175 ? 0.7067 0.6949 0.8491 0.0658 -0.1709 0.0760 170 ASP B CG 1363 O OD1 . ASP A 175 ? 0.7296 0.7099 0.8811 0.0772 -0.1667 0.0764 170 ASP B OD1 1364 O OD2 . ASP A 175 ? 0.7124 0.7221 0.8800 0.0650 -0.1812 0.0777 170 ASP B OD2 1365 N N . SER A 176 ? 0.4490 0.3867 0.4822 0.0356 -0.1272 0.0636 171 SER B N 1366 C CA . SER A 176 ? 0.4847 0.4075 0.4825 0.0256 -0.1215 0.0645 171 SER B CA 1367 C C . SER A 176 ? 0.5210 0.4250 0.5045 0.0253 -0.1145 0.0682 171 SER B C 1368 O O . SER A 176 ? 0.5291 0.4225 0.4862 0.0173 -0.1087 0.0707 171 SER B O 1369 C CB . SER A 176 ? 0.4119 0.3461 0.4084 0.0196 -0.1080 0.0554 171 SER B CB 1370 O OG . SER A 176 ? 0.4115 0.3501 0.4211 0.0228 -0.0937 0.0496 171 SER B OG 1371 N N . THR A 177 ? 0.4913 0.3912 0.4931 0.0340 -0.1147 0.0685 172 THR B N 1372 C CA . THR A 177 ? 0.4837 0.3659 0.4763 0.0329 -0.1080 0.0701 172 THR B CA 1373 C C . THR A 177 ? 0.5308 0.4014 0.5389 0.0438 -0.1163 0.0733 172 THR B C 1374 O O . THR A 177 ? 0.4837 0.3665 0.5167 0.0544 -0.1208 0.0701 172 THR B O 1375 C CB . THR A 177 ? 0.4816 0.3717 0.4798 0.0308 -0.0916 0.0597 172 THR B CB 1376 O OG1 . THR A 177 ? 0.4646 0.3367 0.4542 0.0280 -0.0872 0.0615 172 THR B OG1 1377 C CG2 . THR A 177 ? 0.4887 0.3948 0.5150 0.0410 -0.0877 0.0507 172 THR B CG2 1378 N N . ARG A 178 ? 0.5429 0.3897 0.5372 0.0413 -0.1179 0.0799 173 ARG B N 1379 C CA . ARG A 178 ? 0.5735 0.4036 0.5805 0.0517 -0.1249 0.0818 173 ARG B CA 1380 C C . ARG A 178 ? 0.5650 0.3905 0.5820 0.0555 -0.1142 0.0710 173 ARG B C 1381 O O . ARG A 178 ? 0.6452 0.4537 0.6711 0.0648 -0.1190 0.0701 173 ARG B O 1382 C CB . ARG A 178 ? 0.6625 0.4654 0.6490 0.0466 -0.1349 0.0963 173 ARG B CB 1383 C CG . ARG A 178 ? 0.6965 0.4996 0.6688 0.0443 -0.1481 0.1078 173 ARG B CG 1384 C CD . ARG A 178 ? 0.7763 0.5507 0.7255 0.0387 -0.1561 0.1234 173 ARG B CD 1385 N NE . ARG A 178 ? 0.8411 0.6100 0.7758 0.0395 -0.1724 0.1358 173 ARG B NE 1386 C CZ . ARG A 178 ? 0.8482 0.6166 0.7523 0.0294 -0.1732 0.1432 173 ARG B CZ 1387 N NH1 . ARG A 178 ? 0.7946 0.5699 0.6815 0.0183 -0.1574 0.1395 173 ARG B NH1 1388 N NH2 . ARG A 178 ? 0.9643 0.7252 0.8543 0.0313 -0.1904 0.1542 173 ARG B NH2 1389 N N . ILE A 179 ? 0.5065 0.3447 0.5204 0.0488 -0.1008 0.0626 174 ILE B N 1390 C CA . ILE A 179 ? 0.5114 0.3464 0.5325 0.0525 -0.0918 0.0515 174 ILE B CA 1391 C C . ILE A 179 ? 0.5234 0.3769 0.5671 0.0663 -0.0880 0.0416 174 ILE B C 1392 O O . ILE A 179 ? 0.4843 0.3606 0.5374 0.0670 -0.0870 0.0415 174 ILE B O 1393 C CB . ILE A 179 ? 0.5030 0.3442 0.5120 0.0401 -0.0804 0.0477 174 ILE B CB 1394 C CG1 . ILE A 179 ? 0.5249 0.3482 0.5157 0.0276 -0.0828 0.0585 174 ILE B CG1 1395 C CG2 . ILE A 179 ? 0.4579 0.2983 0.4732 0.0444 -0.0725 0.0353 174 ILE B CG2 1396 C CD1 . ILE A 179 ? 0.5292 0.3637 0.5092 0.0152 -0.0726 0.0585 174 ILE B CD1 1397 N N . ARG A 180 ? 0.5721 0.4151 0.6241 0.0771 -0.0858 0.0334 175 ARG B N 1398 C CA . ARG A 180 ? 0.5890 0.4492 0.6626 0.0921 -0.0805 0.0248 175 ARG B CA 1399 C C . ARG A 180 ? 0.5385 0.4199 0.6121 0.0884 -0.0662 0.0161 175 ARG B C 1400 O O . ARG A 180 ? 0.5818 0.4540 0.6422 0.0839 -0.0596 0.0095 175 ARG B O 1401 C CB . ARG A 180 ? 0.6396 0.4789 0.7184 0.1065 -0.0820 0.0178 175 ARG B CB 1402 C CG . ARG A 180 ? 0.6824 0.5402 0.7846 0.1244 -0.0751 0.0097 175 ARG B CG 1403 C CD . ARG A 180 ? 0.8053 0.6385 0.9099 0.1404 -0.0771 0.0020 175 ARG B CD 1404 N NE . ARG A 180 ? 0.8823 0.6956 0.9666 0.1374 -0.0708 -0.0089 175 ARG B NE 1405 C CZ . ARG A 180 ? 0.9138 0.7387 0.9950 0.1417 -0.0570 -0.0210 175 ARG B CZ 1406 N NH1 . ARG A 180 ? 0.8934 0.7509 0.9918 0.1490 -0.0458 -0.0231 175 ARG B NH1 1407 N NH2 . ARG A 180 ? 0.9543 0.7579 1.0148 0.1381 -0.0548 -0.0303 175 ARG B NH2 1408 N N . ILE A 181 ? 0.4919 0.4009 0.5804 0.0894 -0.0628 0.0170 176 ILE B N 1409 C CA . ILE A 181 ? 0.4833 0.4121 0.5727 0.0859 -0.0496 0.0105 176 ILE B CA 1410 C C . ILE A 181 ? 0.4999 0.4395 0.6055 0.1009 -0.0399 0.0019 176 ILE B C 1411 O O . ILE A 181 ? 0.4798 0.4205 0.6033 0.1143 -0.0437 0.0024 176 ILE B O 1412 C CB . ILE A 181 ? 0.5097 0.4608 0.6052 0.0770 -0.0505 0.0161 176 ILE B CB 1413 C CG1 . ILE A 181 ? 0.5448 0.5172 0.6687 0.0859 -0.0543 0.0191 176 ILE B CG1 1414 C CG2 . ILE A 181 ? 0.5173 0.4561 0.5944 0.0649 -0.0602 0.0243 176 ILE B CG2 1415 C CD1 . ILE A 181 ? 0.5909 0.5863 0.7237 0.0771 -0.0541 0.0225 176 ILE B CD1 1416 N N . THR A 182 ? 0.4260 0.3731 0.5247 0.0995 -0.0272 -0.0056 177 THR B N 1417 C CA . THR A 182 ? 0.4444 0.4026 0.5536 0.1133 -0.0149 -0.0138 177 THR B CA 1418 C C . THR A 182 ? 0.4127 0.3995 0.5306 0.1089 -0.0035 -0.0130 177 THR B C 1419 O O . THR A 182 ? 0.3763 0.3702 0.4894 0.0951 -0.0055 -0.0079 177 THR B O 1420 C CB . THR A 182 ? 0.4543 0.3902 0.5414 0.1174 -0.0097 -0.0248 177 THR B CB 1421 O OG1 . THR A 182 ? 0.4398 0.3762 0.5087 0.1042 -0.0055 -0.0259 177 THR B OG1 1422 C CG2 . THR A 182 ? 0.4741 0.3775 0.5506 0.1188 -0.0220 -0.0253 177 THR B CG2 1423 N N . ASP A 183 ? 0.4261 0.4280 0.5557 0.1210 0.0094 -0.0181 178 ASP B N 1424 C CA . ASP A 183 ? 0.4194 0.4471 0.5566 0.1170 0.0221 -0.0166 178 ASP B CA 1425 C C . ASP A 183 ? 0.3919 0.4106 0.5017 0.1069 0.0275 -0.0203 178 ASP B C 1426 O O . ASP A 183 ? 0.4160 0.4525 0.5290 0.1006 0.0356 -0.0172 178 ASP B O 1427 C CB . ASP A 183 ? 0.4589 0.5047 0.6133 0.1334 0.0369 -0.0207 178 ASP B CB 1428 C CG . ASP A 183 ? 0.5491 0.6146 0.7399 0.1424 0.0330 -0.0147 178 ASP B CG 1429 O OD1 . ASP A 183 ? 0.6485 0.7231 0.8542 0.1326 0.0208 -0.0055 178 ASP B OD1 1430 O OD2 . ASP A 183 ? 0.6755 0.7477 0.8803 0.1601 0.0418 -0.0194 178 ASP B OD2 1431 N N . ASN A 184 ? 0.3991 0.3905 0.4841 0.1051 0.0223 -0.0262 179 ASN B N 1432 C CA . ASN A 184 ? 0.3924 0.3751 0.4535 0.0950 0.0245 -0.0290 179 ASN B CA 1433 C C . ASN A 184 ? 0.3791 0.3599 0.4357 0.0792 0.0159 -0.0221 179 ASN B C 1434 O O . ASN A 184 ? 0.3859 0.3582 0.4253 0.0711 0.0155 -0.0238 179 ASN B O 1435 C CB . ASN A 184 ? 0.4400 0.3953 0.4787 0.0999 0.0220 -0.0387 179 ASN B CB 1436 C CG . ASN A 184 ? 0.4635 0.4170 0.5020 0.1174 0.0311 -0.0476 179 ASN B CG 1437 O OD1 . ASN A 184 ? 0.4458 0.4176 0.4868 0.1228 0.0447 -0.0488 179 ASN B OD1 1438 N ND2 . ASN A 184 ? 0.4863 0.4179 0.5223 0.1268 0.0244 -0.0533 179 ASN B ND2 1439 N N . MET A 185 ? 0.3941 0.3831 0.4660 0.0755 0.0088 -0.0145 180 MET B N 1440 C CA . MET A 185 ? 0.3751 0.3618 0.4408 0.0620 0.0015 -0.0086 180 MET B CA 1441 C C . MET A 185 ? 0.3635 0.3712 0.4466 0.0580 0.0010 -0.0022 180 MET B C 1442 O O . MET A 185 ? 0.3629 0.3844 0.4668 0.0652 0.0014 -0.0003 180 MET B O 1443 C CB . MET A 185 ? 0.3729 0.3418 0.4335 0.0600 -0.0103 -0.0052 180 MET B CB 1444 C CG . MET A 185 ? 0.4342 0.3799 0.4831 0.0645 -0.0131 -0.0102 180 MET B CG 1445 S SD . MET A 185 ? 0.4264 0.3542 0.4751 0.0629 -0.0271 -0.0026 180 MET B SD 1446 C CE . MET A 185 ? 0.4573 0.3566 0.4950 0.0687 -0.0298 -0.0097 180 MET B CE 1447 N N . PHE A 186 ? 0.3412 0.3509 0.4171 0.0467 -0.0007 0.0008 181 PHE B N 1448 C CA . PHE A 186 ? 0.3551 0.3765 0.4428 0.0409 -0.0066 0.0066 181 PHE B CA 1449 C C . PHE A 186 ? 0.3539 0.3623 0.4245 0.0316 -0.0145 0.0089 181 PHE B C 1450 O O . PHE A 186 ? 0.3282 0.3235 0.3816 0.0287 -0.0126 0.0068 181 PHE B O 1451 C CB . PHE A 186 ? 0.3467 0.3858 0.4449 0.0370 0.0009 0.0078 181 PHE B CB 1452 C CG . PHE A 186 ? 0.3212 0.3547 0.4024 0.0303 0.0066 0.0057 181 PHE B CG 1453 C CD1 . PHE A 186 ? 0.3488 0.3811 0.4218 0.0342 0.0165 0.0018 181 PHE B CD1 1454 C CD2 . PHE A 186 ? 0.3531 0.3821 0.4259 0.0208 0.0017 0.0075 181 PHE B CD2 1455 C CE1 . PHE A 186 ? 0.3238 0.3513 0.3825 0.0285 0.0200 0.0007 181 PHE B CE1 1456 C CE2 . PHE A 186 ? 0.3286 0.3530 0.3885 0.0161 0.0066 0.0058 181 PHE B CE2 1457 C CZ . PHE A 186 ? 0.3251 0.3495 0.3793 0.0198 0.0152 0.0030 181 PHE B CZ 1458 N N . CYS A 187 ? 0.3260 0.3384 0.4016 0.0273 -0.0234 0.0133 182 CYS B N 1459 C CA . CYS A 187 ? 0.3529 0.3535 0.4094 0.0193 -0.0296 0.0152 182 CYS B CA 1460 C C . CYS A 187 ? 0.3552 0.3625 0.4119 0.0119 -0.0311 0.0153 182 CYS B C 1461 O O . CYS A 187 ? 0.3205 0.3421 0.3961 0.0116 -0.0317 0.0163 182 CYS B O 1462 C CB . CYS A 187 ? 0.3875 0.3778 0.4389 0.0208 -0.0410 0.0199 182 CYS B CB 1463 S SG . CYS A 187 ? 0.4292 0.4256 0.4883 0.0183 -0.0559 0.0250 182 CYS B SG 1464 N N . ALA A 188 ? 0.3234 0.3201 0.3598 0.0060 -0.0310 0.0142 183 ALA B N 1465 C CA . ALA A 188 ? 0.3379 0.3356 0.3700 -0.0004 -0.0321 0.0126 183 ALA B CA 1466 C C . ALA A 188 ? 0.3452 0.3289 0.3531 -0.0044 -0.0370 0.0124 183 ALA B C 1467 O O . ALA A 188 ? 0.3234 0.2980 0.3171 -0.0035 -0.0348 0.0138 183 ALA B O 1468 C CB . ALA A 188 ? 0.3470 0.3476 0.3792 -0.0014 -0.0212 0.0094 183 ALA B CB 1469 N N . GLY A 189 ? 0.3786 0.3597 0.3812 -0.0091 -0.0433 0.0107 184 GLY B N 1470 C CA . GLY A 189 ? 0.3638 0.3306 0.3399 -0.0118 -0.0475 0.0095 184 GLY B CA 1471 C C . GLY A 189 ? 0.3826 0.3462 0.3563 -0.0154 -0.0622 0.0093 184 GLY B C 1472 O O . GLY A 189 ? 0.3941 0.3684 0.3901 -0.0156 -0.0704 0.0122 184 GLY B O 1473 N N . TYR A 190 A 0.3811 0.3304 0.3280 -0.0180 -0.0657 0.0058 184 TYR B N 1474 C CA . TYR A 190 A 0.4163 0.3588 0.3561 -0.0221 -0.0819 0.0044 184 TYR B CA 1475 C C . TYR A 190 A 0.4322 0.3713 0.3639 -0.0208 -0.0940 0.0103 184 TYR B C 1476 O O . TYR A 190 A 0.4306 0.3648 0.3488 -0.0175 -0.0886 0.0145 184 TYR B O 1477 C CB . TYR A 190 A 0.4739 0.3992 0.3843 -0.0244 -0.0817 -0.0033 184 TYR B CB 1478 C CG . TYR A 190 A 0.4765 0.4030 0.3976 -0.0262 -0.0748 -0.0089 184 TYR B CG 1479 C CD1 . TYR A 190 A 0.4951 0.4246 0.4350 -0.0318 -0.0851 -0.0102 184 TYR B CD1 1480 C CD2 . TYR A 190 A 0.4737 0.3986 0.3881 -0.0227 -0.0589 -0.0119 184 TYR B CD2 1481 C CE1 . TYR A 190 A 0.5018 0.4299 0.4504 -0.0340 -0.0795 -0.0139 184 TYR B CE1 1482 C CE2 . TYR A 190 A 0.4669 0.3911 0.3904 -0.0237 -0.0539 -0.0161 184 TYR B CE2 1483 C CZ . TYR A 190 A 0.4644 0.3889 0.4038 -0.0295 -0.0641 -0.0169 184 TYR B CZ 1484 O OH . TYR A 190 A 0.5017 0.4234 0.4495 -0.0311 -0.0599 -0.0197 184 TYR B OH 1485 N N . LYS A 191 ? 0.4342 0.3761 0.3766 -0.0237 -0.1113 0.0118 185 LYS B N 1486 C CA . LYS A 191 ? 0.4749 0.4115 0.4076 -0.0228 -0.1268 0.0175 185 LYS B CA 1487 C C . LYS A 191 ? 0.5084 0.4228 0.3974 -0.0254 -0.1339 0.0137 185 LYS B C 1488 O O . LYS A 191 ? 0.5335 0.4385 0.4074 -0.0286 -0.1319 0.0054 185 LYS B O 1489 C CB . LYS A 191 ? 0.5007 0.4514 0.4653 -0.0249 -0.1438 0.0207 185 LYS B CB 1490 C CG . LYS A 191 ? 0.4913 0.4652 0.4982 -0.0206 -0.1355 0.0247 185 LYS B CG 1491 C CD . LYS A 191 ? 0.5694 0.5612 0.6123 -0.0235 -0.1499 0.0280 185 LYS B CD 1492 C CE . LYS A 191 ? 0.5635 0.5798 0.6474 -0.0185 -0.1380 0.0313 185 LYS B CE 1493 N NZ . LYS A 191 ? 0.6039 0.6419 0.7275 -0.0215 -0.1504 0.0357 185 LYS B NZ 1494 N N . PRO A 192 ? 0.5561 0.4604 0.4226 -0.0235 -0.1421 0.0199 186 PRO B N 1495 C CA . PRO A 192 ? 0.6313 0.5135 0.4513 -0.0254 -0.1493 0.0171 186 PRO B CA 1496 C C . PRO A 192 ? 0.6508 0.5242 0.4620 -0.0309 -0.1655 0.0085 186 PRO B C 1497 O O . PRO A 192 ? 0.7354 0.5902 0.5096 -0.0318 -0.1636 0.0005 186 PRO B O 1498 C CB . PRO A 192 ? 0.6511 0.5283 0.4610 -0.0233 -0.1626 0.0278 186 PRO B CB 1499 C CG . PRO A 192 ? 0.6162 0.5080 0.4574 -0.0187 -0.1526 0.0353 186 PRO B CG 1500 C CD . PRO A 192 ? 0.5489 0.4601 0.4309 -0.0189 -0.1458 0.0301 186 PRO B CD 1501 N N . ASP A 193 A 0.6661 0.5525 0.5118 -0.0344 -0.1812 0.0100 186 ASP B N 1502 C CA . ASP A 193 A 0.7036 0.5818 0.5457 -0.0415 -0.1996 0.0028 186 ASP B CA 1503 C C . ASP A 193 A 0.6754 0.5522 0.5256 -0.0451 -0.1896 -0.0069 186 ASP B C 1504 O O . ASP A 193 A 0.7122 0.5761 0.5528 -0.0512 -0.2036 -0.0145 186 ASP B O 1505 C CB . ASP A 193 A 0.7034 0.5974 0.5820 -0.0451 -0.2221 0.0093 186 ASP B CB 1506 C CG . ASP A 193 A 0.7189 0.6422 0.6536 -0.0445 -0.2133 0.0141 186 ASP B CG 1507 O OD1 . ASP A 193 A 0.6662 0.5971 0.6111 -0.0412 -0.1908 0.0129 186 ASP B OD1 1508 O OD2 . ASP A 193 A 0.8048 0.7445 0.7739 -0.0471 -0.2297 0.0196 186 ASP B OD2 1509 N N . GLU A 194 B 0.6587 0.5463 0.5244 -0.0414 -0.1669 -0.0067 186 GLU B N 1510 C CA . GLU A 194 B 0.6367 0.5226 0.5106 -0.0440 -0.1571 -0.0143 186 GLU B CA 1511 C C . GLU A 194 B 0.6721 0.5362 0.5054 -0.0407 -0.1456 -0.0239 186 GLU B C 1512 O O . GLU A 194 B 0.6867 0.5437 0.5215 -0.0425 -0.1414 -0.0315 186 GLU B O 1513 C CB . GLU A 194 B 0.6222 0.5312 0.5348 -0.0418 -0.1406 -0.0091 186 GLU B CB 1514 C CG . GLU A 194 B 0.6078 0.5394 0.5635 -0.0446 -0.1506 -0.0012 186 GLU B CG 1515 C CD . GLU A 194 B 0.6012 0.5545 0.5902 -0.0410 -0.1334 0.0036 186 GLU B CD 1516 O OE1 . GLU A 194 B 0.4705 0.4257 0.4524 -0.0342 -0.1196 0.0057 186 GLU B OE1 1517 O OE2 . GLU A 194 B 0.6955 0.6637 0.7172 -0.0454 -0.1339 0.0057 186 GLU B OE2 1518 N N . GLY A 195 C 0.7041 0.5573 0.5016 -0.0356 -0.1402 -0.0232 186 GLY B N 1519 C CA . GLY A 195 C 0.7884 0.6214 0.5452 -0.0315 -0.1294 -0.0326 186 GLY B CA 1520 C C . GLY A 195 C 0.8170 0.6579 0.5810 -0.0259 -0.1043 -0.0335 186 GLY B C 1521 O O . GLY A 195 C 0.8746 0.7111 0.6134 -0.0205 -0.0901 -0.0331 186 GLY B O 1522 N N . LYS A 196 D 0.7464 0.5998 0.5452 -0.0276 -0.0991 -0.0337 186 LYS B N 1523 C CA . LYS A 196 D 0.6348 0.4976 0.4450 -0.0227 -0.0780 -0.0336 186 LYS B CA 1524 C C . LYS A 196 D 0.6013 0.4793 0.4197 -0.0196 -0.0665 -0.0239 186 LYS B C 1525 O O . LYS A 196 D 0.5265 0.4107 0.3513 -0.0212 -0.0748 -0.0163 186 LYS B O 1526 C CB . LYS A 196 D 0.6431 0.5161 0.4884 -0.0259 -0.0774 -0.0337 186 LYS B CB 1527 C CG . LYS A 196 D 0.7142 0.5701 0.5541 -0.0295 -0.0868 -0.0429 186 LYS B CG 1528 C CD . LYS A 196 D 0.7351 0.6002 0.6055 -0.0310 -0.0797 -0.0415 186 LYS B CD 1529 C CE . LYS A 196 D 0.8565 0.7018 0.7214 -0.0341 -0.0870 -0.0501 186 LYS B CE 1530 N NZ . LYS A 196 D 0.9087 0.7612 0.7977 -0.0337 -0.0766 -0.0476 186 LYS B NZ 1531 N N . ARG A 197 ? 0.5662 0.4495 0.3860 -0.0151 -0.0484 -0.0242 187 ARG B N 1532 C CA . ARG A 197 ? 0.5068 0.4018 0.3325 -0.0130 -0.0370 -0.0159 187 ARG B CA 1533 C C . ARG A 197 ? 0.4619 0.3714 0.3153 -0.0114 -0.0250 -0.0147 187 ARG B C 1534 O O . ARG A 197 ? 0.4543 0.3646 0.3202 -0.0113 -0.0240 -0.0196 187 ARG B O 1535 C CB . ARG A 197 ? 0.5222 0.4088 0.3158 -0.0094 -0.0263 -0.0163 187 ARG B CB 1536 C CG . ARG A 197 ? 0.5636 0.4320 0.3203 -0.0098 -0.0366 -0.0192 187 ARG B CG 1537 C CD . ARG A 197 ? 0.5988 0.4638 0.3275 -0.0075 -0.0258 -0.0134 187 ARG B CD 1538 N NE . ARG A 197 ? 0.5874 0.4617 0.3299 -0.0105 -0.0279 -0.0009 187 ARG B NE 1539 C CZ . ARG A 197 ? 0.6181 0.4858 0.3502 -0.0131 -0.0424 0.0056 187 ARG B CZ 1540 N NH1 . ARG A 197 ? 0.6495 0.5017 0.3551 -0.0139 -0.0572 0.0011 187 ARG B NH1 1541 N NH2 . ARG A 197 ? 0.6147 0.4895 0.3618 -0.0147 -0.0432 0.0166 187 ARG B NH2 1542 N N . GLY A 198 ? 0.4275 0.3467 0.2890 -0.0105 -0.0167 -0.0078 188 GLY B N 1543 C CA . GLY A 198 ? 0.4083 0.3398 0.2922 -0.0091 -0.0064 -0.0067 188 GLY B CA 1544 C C . GLY A 198 ? 0.4184 0.3590 0.3196 -0.0103 -0.0079 0.0005 188 GLY B C 1545 O O . GLY A 198 ? 0.4123 0.3524 0.3182 -0.0116 -0.0182 0.0034 188 GLY B O 1546 N N . ASP A 199 ? 0.4254 0.3737 0.3371 -0.0095 0.0016 0.0030 189 ASP B N 1547 C CA . ASP A 199 ? 0.4138 0.3675 0.3401 -0.0103 0.0004 0.0084 189 ASP B CA 1548 C C . ASP A 199 ? 0.4211 0.3823 0.3586 -0.0099 0.0098 0.0088 189 ASP B C 1549 O O . ASP A 199 ? 0.3920 0.3555 0.3253 -0.0090 0.0179 0.0068 189 ASP B O 1550 C CB . ASP A 199 ? 0.4321 0.3789 0.3456 -0.0119 -0.0030 0.0153 189 ASP B CB 1551 C CG . ASP A 199 ? 0.4107 0.3584 0.3387 -0.0117 -0.0086 0.0199 189 ASP B CG 1552 O OD1 . ASP A 199 ? 0.3507 0.3049 0.2971 -0.0097 -0.0089 0.0170 189 ASP B OD1 1553 O OD2 . ASP A 199 ? 0.3990 0.3392 0.3177 -0.0130 -0.0122 0.0265 189 ASP B OD2 1554 N N . ALA A 200 ? 0.4344 0.3994 0.3867 -0.0100 0.0080 0.0107 190 ALA B N 1555 C CA . ALA A 200 ? 0.3864 0.3562 0.3476 -0.0112 0.0136 0.0124 190 ALA B CA 1556 C C . ALA A 200 ? 0.3908 0.3563 0.3454 -0.0148 0.0149 0.0194 190 ALA B C 1557 O O . ALA A 200 ? 0.3771 0.3350 0.3184 -0.0157 0.0114 0.0231 190 ALA B O 1558 C CB . ALA A 200 ? 0.3964 0.3685 0.3714 -0.0097 0.0104 0.0105 190 ALA B CB 1559 N N . CYS A 201 ? 0.3572 0.3272 0.3210 -0.0177 0.0192 0.0221 191 CYS B N 1560 C CA . CYS A 201 ? 0.4033 0.3701 0.3634 -0.0228 0.0215 0.0304 191 CYS B CA 1561 C C . CYS A 201 ? 0.4045 0.3743 0.3814 -0.0269 0.0208 0.0326 191 CYS B C 1562 O O . CYS A 201 ? 0.4081 0.3808 0.3959 -0.0248 0.0177 0.0269 191 CYS B O 1563 C CB . CYS A 201 ? 0.4613 0.4332 0.4100 -0.0234 0.0318 0.0330 191 CYS B CB 1564 S SG . CYS A 201 ? 0.5542 0.5203 0.4881 -0.0293 0.0361 0.0451 191 CYS B SG 1565 N N . GLU A 202 ? 0.4501 0.4181 0.4279 -0.0333 0.0231 0.0412 192 GLU B N 1566 C CA . GLU A 202 ? 0.4773 0.4466 0.4719 -0.0392 0.0205 0.0441 192 GLU B CA 1567 C C . GLU A 202 ? 0.4096 0.3951 0.4186 -0.0388 0.0259 0.0407 192 GLU B C 1568 O O . GLU A 202 ? 0.3950 0.3918 0.4025 -0.0369 0.0357 0.0415 192 GLU B O 1569 C CB . GLU A 202 ? 0.5657 0.5306 0.5602 -0.0479 0.0225 0.0560 192 GLU B CB 1570 C CG . GLU A 202 ? 0.7372 0.6897 0.7424 -0.0535 0.0123 0.0583 192 GLU B CG 1571 C CD . GLU A 202 ? 0.8290 0.7838 0.8453 -0.0650 0.0152 0.0702 192 GLU B CD 1572 O OE1 . GLU A 202 ? 0.8708 0.8270 0.8780 -0.0688 0.0231 0.0804 192 GLU B OE1 1573 O OE2 . GLU A 202 ? 0.8171 0.7721 0.8510 -0.0708 0.0093 0.0697 192 GLU B OE2 1574 N N . GLY A 203 ? 0.3649 0.3505 0.3869 -0.0397 0.0189 0.0367 193 GLY B N 1575 C CA . GLY A 203 ? 0.4013 0.4008 0.4364 -0.0379 0.0207 0.0329 193 GLY B CA 1576 C C . GLY A 203 ? 0.3687 0.3669 0.3977 -0.0299 0.0182 0.0238 193 GLY B C 1577 O O . GLY A 203 ? 0.3586 0.3631 0.3965 -0.0284 0.0156 0.0205 193 GLY B O 1578 N N . ASP A 204 ? 0.3081 0.2985 0.3229 -0.0252 0.0182 0.0208 194 ASP B N 1579 C CA . ASP A 204 ? 0.3391 0.3289 0.3499 -0.0189 0.0164 0.0139 194 ASP B CA 1580 C C . ASP A 204 ? 0.3342 0.3150 0.3434 -0.0170 0.0089 0.0099 194 ASP B C 1581 O O . ASP A 204 ? 0.3302 0.3119 0.3372 -0.0124 0.0083 0.0053 194 ASP B O 1582 C CB . ASP A 204 ? 0.3189 0.3065 0.3181 -0.0152 0.0194 0.0126 194 ASP B CB 1583 C CG . ASP A 204 ? 0.3328 0.3267 0.3288 -0.0147 0.0274 0.0139 194 ASP B CG 1584 O OD1 . ASP A 204 ? 0.3294 0.3324 0.3346 -0.0134 0.0313 0.0131 194 ASP B OD1 1585 O OD2 . ASP A 204 ? 0.3266 0.3158 0.3098 -0.0146 0.0295 0.0154 194 ASP B OD2 1586 N N . THR A 205 ? 0.3414 0.3127 0.3511 -0.0203 0.0037 0.0118 195 THR B N 1587 C CA . THR A 205 ? 0.3286 0.2889 0.3348 -0.0169 -0.0027 0.0067 195 THR B CA 1588 C C . THR A 205 ? 0.3551 0.3185 0.3621 -0.0145 -0.0046 0.0013 195 THR B C 1589 O O . THR A 205 ? 0.3014 0.2719 0.3157 -0.0183 -0.0052 0.0027 195 THR B O 1590 C CB . THR A 205 ? 0.3833 0.3309 0.3917 -0.0219 -0.0092 0.0093 195 THR B CB 1591 O OG1 . THR A 205 ? 0.3647 0.3049 0.3687 -0.0223 -0.0092 0.0143 195 THR B OG1 1592 C CG2 . THR A 205 ? 0.3805 0.3153 0.3849 -0.0182 -0.0165 0.0017 195 THR B CG2 1593 N N . GLY A 206 ? 0.3300 0.2892 0.3299 -0.0081 -0.0052 -0.0043 196 GLY B N 1594 C CA . GLY A 206 ? 0.3458 0.3061 0.3415 -0.0054 -0.0068 -0.0090 196 GLY B CA 1595 C C . GLY A 206 ? 0.3691 0.3406 0.3647 -0.0028 -0.0012 -0.0081 196 GLY B C 1596 O O . GLY A 206 ? 0.3823 0.3538 0.3711 0.0009 -0.0010 -0.0111 196 GLY B O 1597 N N . GLY A 207 ? 0.3795 0.3587 0.3809 -0.0047 0.0033 -0.0041 197 GLY B N 1598 C CA . GLY A 207 ? 0.3793 0.3659 0.3810 -0.0026 0.0078 -0.0033 197 GLY B CA 1599 C C . GLY A 207 ? 0.4135 0.3996 0.4111 0.0012 0.0106 -0.0045 197 GLY B C 1600 O O . GLY A 207 ? 0.3708 0.3535 0.3677 0.0026 0.0101 -0.0052 197 GLY B O 1601 N N . PRO A 208 ? 0.3683 0.3584 0.3650 0.0028 0.0133 -0.0039 198 PRO B N 1602 C CA . PRO A 208 ? 0.3612 0.3531 0.3567 0.0055 0.0165 -0.0037 198 PRO B CA 1603 C C . PRO A 208 ? 0.3606 0.3553 0.3617 0.0039 0.0179 -0.0018 198 PRO B C 1604 O O . PRO A 208 ? 0.3272 0.3212 0.3291 0.0015 0.0175 -0.0010 198 PRO B O 1605 C CB . PRO A 208 ? 0.3506 0.3439 0.3420 0.0064 0.0179 -0.0022 198 PRO B CB 1606 C CG . PRO A 208 ? 0.3740 0.3677 0.3690 0.0043 0.0159 -0.0009 198 PRO B CG 1607 C CD . PRO A 208 ? 0.3342 0.3271 0.3321 0.0024 0.0130 -0.0024 198 PRO B CD 1608 N N . PHE A 209 ? 0.3291 0.3268 0.3342 0.0056 0.0190 -0.0014 199 PHE B N 1609 C CA . PHE A 209 ? 0.3386 0.3402 0.3509 0.0035 0.0185 0.0008 199 PHE B CA 1610 C C . PHE A 209 ? 0.2882 0.2959 0.3048 0.0036 0.0230 0.0036 199 PHE B C 1611 O O . PHE A 209 ? 0.3055 0.3188 0.3244 0.0071 0.0272 0.0040 199 PHE B O 1612 C CB . PHE A 209 ? 0.2983 0.3016 0.3165 0.0052 0.0158 0.0008 199 PHE B CB 1613 C CG . PHE A 209 ? 0.3307 0.3389 0.3582 0.0025 0.0126 0.0033 199 PHE B CG 1614 C CD1 . PHE A 209 ? 0.3251 0.3434 0.3648 0.0025 0.0155 0.0060 199 PHE B CD1 1615 C CD2 . PHE A 209 ? 0.3259 0.3289 0.3499 -0.0003 0.0063 0.0033 199 PHE B CD2 1616 C CE1 . PHE A 209 ? 0.3722 0.3957 0.4237 -0.0014 0.0107 0.0087 199 PHE B CE1 1617 C CE2 . PHE A 209 ? 0.3583 0.3642 0.3896 -0.0033 0.0008 0.0050 199 PHE B CE2 1618 C CZ . PHE A 209 ? 0.3548 0.3713 0.4017 -0.0043 0.0022 0.0077 199 PHE B CZ 1619 N N . VAL A 210 ? 0.2674 0.2732 0.2842 -0.0001 0.0226 0.0057 200 VAL B N 1620 C CA . VAL A 210 ? 0.3114 0.3206 0.3312 -0.0015 0.0265 0.0101 200 VAL B CA 1621 C C . VAL A 210 ? 0.2920 0.3038 0.3234 -0.0067 0.0244 0.0135 200 VAL B C 1622 O O . VAL A 210 ? 0.3569 0.3641 0.3898 -0.0093 0.0185 0.0112 200 VAL B O 1623 C CB . VAL A 210 ? 0.3342 0.3367 0.3453 -0.0014 0.0265 0.0111 200 VAL B CB 1624 C CG1 . VAL A 210 ? 0.3197 0.3203 0.3215 0.0026 0.0261 0.0078 200 VAL B CG1 1625 C CG2 . VAL A 210 ? 0.3659 0.3605 0.3772 -0.0037 0.0223 0.0097 200 VAL B CG2 1626 N N . MET A 211 ? 0.3121 0.3312 0.3511 -0.0085 0.0292 0.0191 201 MET B N 1627 C CA . MET A 211 ? 0.3278 0.3505 0.3813 -0.0152 0.0269 0.0239 201 MET B CA 1628 C C . MET A 211 ? 0.3411 0.3623 0.3941 -0.0186 0.0315 0.0310 201 MET B C 1629 O O . MET A 211 ? 0.3378 0.3614 0.3818 -0.0147 0.0386 0.0334 201 MET B O 1630 C CB . MET A 211 ? 0.3312 0.3699 0.4022 -0.0149 0.0290 0.0265 201 MET B CB 1631 C CG . MET A 211 ? 0.3302 0.3696 0.4019 -0.0110 0.0237 0.0210 201 MET B CG 1632 S SD . MET A 211 ? 0.3164 0.3750 0.4131 -0.0096 0.0237 0.0244 201 MET B SD 1633 C CE . MET A 211 ? 0.3473 0.4077 0.4610 -0.0211 0.0148 0.0294 201 MET B CE 1634 N N . LYS A 212 ? 0.3224 0.3375 0.3831 -0.0259 0.0266 0.0345 202 LYS B N 1635 C CA . LYS A 212 ? 0.3237 0.3347 0.3849 -0.0305 0.0297 0.0429 202 LYS B CA 1636 C C . LYS A 212 ? 0.3315 0.3571 0.4129 -0.0372 0.0340 0.0519 202 LYS B C 1637 O O . LYS A 212 ? 0.3258 0.3548 0.4238 -0.0432 0.0273 0.0519 202 LYS B O 1638 C CB . LYS A 212 ? 0.3655 0.3573 0.4230 -0.0344 0.0211 0.0412 202 LYS B CB 1639 C CG . LYS A 212 ? 0.4488 0.4333 0.5091 -0.0405 0.0222 0.0511 202 LYS B CG 1640 C CD . LYS A 212 ? 0.4719 0.4335 0.5236 -0.0404 0.0143 0.0479 202 LYS B CD 1641 C CE . LYS A 212 ? 0.5212 0.4752 0.5629 -0.0380 0.0178 0.0551 202 LYS B CE 1642 N NZ . LYS A 212 ? 0.5551 0.4863 0.5938 -0.0391 0.0102 0.0550 202 LYS B NZ 1643 N N . SER A 213 ? 0.3102 0.3445 0.3902 -0.0364 0.0448 0.0602 203 SER B N 1644 C CA . SER A 213 ? 0.3243 0.3759 0.4256 -0.0429 0.0518 0.0708 203 SER B CA 1645 C C . SER A 213 ? 0.3505 0.3919 0.4619 -0.0548 0.0461 0.0794 203 SER B C 1646 O O . SER A 213 ? 0.4100 0.4352 0.5069 -0.0559 0.0454 0.0830 203 SER B O 1647 C CB . SER A 213 ? 0.3770 0.4409 0.4699 -0.0376 0.0673 0.0772 203 SER B CB 1648 O OG . SER A 213 ? 0.3860 0.4666 0.4995 -0.0450 0.0763 0.0901 203 SER B OG 1649 N N . PRO A 214 ? 0.3616 0.4115 0.4989 -0.0640 0.0405 0.0828 204 PRO B N 1650 C CA . PRO A 214 ? 0.4014 0.4426 0.5523 -0.0772 0.0349 0.0923 204 PRO B CA 1651 C C . PRO A 214 ? 0.4127 0.4672 0.5729 -0.0827 0.0485 0.1086 204 PRO B C 1652 O O . PRO A 214 ? 0.4799 0.5261 0.6506 -0.0944 0.0451 0.1188 204 PRO B O 1653 C CB . PRO A 214 ? 0.3861 0.4359 0.5630 -0.0848 0.0240 0.0902 204 PRO B CB 1654 C CG . PRO A 214 ? 0.4012 0.4766 0.5879 -0.0767 0.0318 0.0878 204 PRO B CG 1655 C CD . PRO A 214 ? 0.3847 0.4542 0.5424 -0.0629 0.0391 0.0796 204 PRO B CD 1656 N N . PHE A 215 A 0.4434 0.5169 0.5984 -0.0744 0.0641 0.1112 204 PHE B N 1657 C CA . PHE A 215 A 0.4609 0.5489 0.6214 -0.0783 0.0799 0.1269 204 PHE B CA 1658 C C . PHE A 215 A 0.4260 0.4955 0.5553 -0.0754 0.0842 0.1317 204 PHE B C 1659 O O . PHE A 215 A 0.4542 0.5219 0.5859 -0.0839 0.0898 0.1467 204 PHE B O 1660 C CB . PHE A 215 A 0.5128 0.6301 0.6820 -0.0697 0.0955 0.1271 204 PHE B CB 1661 C CG . PHE A 215 A 0.5801 0.7167 0.7817 -0.0712 0.0901 0.1230 204 PHE B CG 1662 C CD1 . PHE A 215 A 0.6832 0.8358 0.9219 -0.0846 0.0882 0.1343 204 PHE B CD1 1663 C CD2 . PHE A 215 A 0.6220 0.7593 0.8179 -0.0602 0.0849 0.1085 204 PHE B CD2 1664 C CE1 . PHE A 215 A 0.7245 0.8949 0.9941 -0.0860 0.0806 0.1310 204 PHE B CE1 1665 C CE2 . PHE A 215 A 0.6356 0.7889 0.8602 -0.0613 0.0780 0.1056 204 PHE B CE2 1666 C CZ . PHE A 215 A 0.7012 0.8716 0.9628 -0.0738 0.0754 0.1166 204 PHE B CZ 1667 N N . ASN A 216 B 0.4159 0.4713 0.5173 -0.0642 0.0805 0.1200 204 ASN B N 1668 C CA . ASN A 216 B 0.4099 0.4470 0.4822 -0.0607 0.0812 0.1238 204 ASN B CA 1669 C C . ASN A 216 B 0.3778 0.3902 0.4343 -0.0561 0.0666 0.1129 204 ASN B C 1670 O O . ASN A 216 B 0.3627 0.3617 0.3966 -0.0514 0.0656 0.1147 204 ASN B O 1671 C CB . ASN A 216 B 0.4301 0.4780 0.4801 -0.0501 0.0950 0.1233 204 ASN B CB 1672 C CG . ASN A 216 B 0.4242 0.4762 0.4667 -0.0385 0.0927 0.1066 204 ASN B CG 1673 O OD1 . ASN A 216 B 0.3908 0.4333 0.4367 -0.0372 0.0802 0.0956 204 ASN B OD1 1674 N ND2 . ASN A 216 B 0.4497 0.5146 0.4803 -0.0299 0.1053 0.1048 204 ASN B ND2 1675 N N . ASN A 217 ? 0.3845 0.3920 0.4524 -0.0568 0.0555 0.1019 205 ASN B N 1676 C CA . ASN A 217 ? 0.4070 0.3931 0.4627 -0.0523 0.0435 0.0918 205 ASN B CA 1677 C C . ASN A 217 ? 0.4156 0.4007 0.4501 -0.0401 0.0442 0.0823 205 ASN B C 1678 O O . ASN A 217 ? 0.4511 0.4208 0.4755 -0.0357 0.0365 0.0769 205 ASN B O 1679 C CB . ASN A 217 ? 0.4625 0.4267 0.5136 -0.0574 0.0377 0.1003 205 ASN B CB 1680 C CG . ASN A 217 ? 0.5475 0.4900 0.5981 -0.0562 0.0243 0.0905 205 ASN B CG 1681 O OD1 . ASN A 217 ? 0.6157 0.5587 0.6764 -0.0581 0.0184 0.0815 205 ASN B OD1 1682 N ND2 . ASN A 217 ? 0.5600 0.4828 0.5982 -0.0524 0.0195 0.0925 205 ASN B ND2 1683 N N . ARG A 218 ? 0.3875 0.3890 0.4173 -0.0346 0.0530 0.0801 206 ARG B N 1684 C CA . ARG A 218 ? 0.3990 0.3991 0.4102 -0.0246 0.0524 0.0712 206 ARG B CA 1685 C C . ARG A 218 ? 0.3792 0.3853 0.3974 -0.0208 0.0490 0.0591 206 ARG B C 1686 O O . ARG A 218 ? 0.3560 0.3735 0.3909 -0.0238 0.0509 0.0585 206 ARG B O 1687 C CB . ARG A 218 ? 0.4181 0.4277 0.4140 -0.0198 0.0634 0.0752 206 ARG B CB 1688 C CG . ARG A 218 ? 0.4484 0.4491 0.4274 -0.0211 0.0659 0.0867 206 ARG B CG 1689 C CD . ARG A 218 ? 0.4776 0.4894 0.4413 -0.0173 0.0792 0.0914 206 ARG B CD 1690 N NE . ARG A 218 ? 0.5065 0.5114 0.4531 -0.0200 0.0836 0.1052 206 ARG B NE 1691 C CZ . ARG A 218 ? 0.5653 0.5587 0.4831 -0.0145 0.0804 0.1063 206 ARG B CZ 1692 N NH1 . ARG A 218 ? 0.5347 0.5225 0.4396 -0.0068 0.0720 0.0939 206 ARG B NH1 1693 N NH2 . ARG A 218 ? 0.6237 0.6108 0.5257 -0.0176 0.0848 0.1208 206 ARG B NH2 1694 N N . TRP A 219 ? 0.3368 0.3358 0.3431 -0.0146 0.0437 0.0507 207 TRP B N 1695 C CA . TRP A 219 ? 0.3210 0.3239 0.3303 -0.0109 0.0409 0.0404 207 TRP B CA 1696 C C . TRP A 219 ? 0.3308 0.3427 0.3322 -0.0050 0.0470 0.0373 207 TRP B C 1697 O O . TRP A 219 ? 0.3512 0.3603 0.3360 -0.0011 0.0493 0.0384 207 TRP B O 1698 C CB . TRP A 219 ? 0.3279 0.3202 0.3307 -0.0077 0.0332 0.0338 207 TRP B CB 1699 C CG . TRP A 219 ? 0.3079 0.2900 0.3170 -0.0111 0.0276 0.0340 207 TRP B CG 1700 C CD1 . TRP A 219 ? 0.3333 0.3043 0.3401 -0.0124 0.0251 0.0394 207 TRP B CD1 1701 C CD2 . TRP A 219 ? 0.3284 0.3075 0.3450 -0.0130 0.0232 0.0281 207 TRP B CD2 1702 N NE1 . TRP A 219 ? 0.3194 0.2799 0.3324 -0.0146 0.0197 0.0362 207 TRP B NE1 1703 C CE2 . TRP A 219 ? 0.3099 0.2753 0.3275 -0.0151 0.0186 0.0290 207 TRP B CE2 1704 C CE3 . TRP A 219 ? 0.2981 0.2833 0.3189 -0.0130 0.0222 0.0224 207 TRP B CE3 1705 C CZ2 . TRP A 219 ? 0.3258 0.2827 0.3460 -0.0168 0.0133 0.0230 207 TRP B CZ2 1706 C CZ3 . TRP A 219 ? 0.3214 0.2992 0.3445 -0.0152 0.0166 0.0178 207 TRP B CZ3 1707 C CH2 . TRP A 219 ? 0.3443 0.3079 0.3659 -0.0169 0.0125 0.0174 207 TRP B CH2 1708 N N . TYR A 220 ? 0.3040 0.3249 0.3160 -0.0039 0.0485 0.0331 208 TYR B N 1709 C CA . TYR A 220 ? 0.3152 0.3429 0.3217 0.0029 0.0540 0.0288 208 TYR B CA 1710 C C . TYR A 220 ? 0.3196 0.3442 0.3275 0.0059 0.0477 0.0201 208 TYR B C 1711 O O . TYR A 220 ? 0.3275 0.3527 0.3477 0.0026 0.0426 0.0189 208 TYR B O 1712 C CB . TYR A 220 ? 0.3130 0.3566 0.3349 0.0028 0.0628 0.0334 208 TYR B CB 1713 C CG . TYR A 220 ? 0.3060 0.3559 0.3254 0.0008 0.0727 0.0431 208 TYR B CG 1714 C CD1 . TYR A 220 ? 0.3102 0.3611 0.3420 -0.0084 0.0721 0.0527 208 TYR B CD1 1715 C CD2 . TYR A 220 ? 0.3588 0.4126 0.3625 0.0079 0.0830 0.0430 208 TYR B CD2 1716 C CE1 . TYR A 220 ? 0.3484 0.4050 0.3780 -0.0112 0.0820 0.0636 208 TYR B CE1 1717 C CE2 . TYR A 220 ? 0.3668 0.4270 0.3657 0.0062 0.0939 0.0531 208 TYR B CE2 1718 C CZ . TYR A 220 ? 0.4067 0.4690 0.4195 -0.0038 0.0937 0.0643 208 TYR B CZ 1719 O OH . TYR A 220 ? 0.4169 0.4854 0.4250 -0.0065 0.1051 0.0762 208 TYR B OH 1720 N N . GLN A 221 ? 0.3592 0.3791 0.3534 0.0117 0.0475 0.0143 209 GLN B N 1721 C CA . GLN A 221 ? 0.3544 0.3704 0.3503 0.0139 0.0419 0.0074 209 GLN B CA 1722 C C . GLN A 221 ? 0.3400 0.3635 0.3449 0.0187 0.0459 0.0053 209 GLN B C 1723 O O . GLN A 221 ? 0.3669 0.3912 0.3637 0.0253 0.0517 0.0026 209 GLN B O 1724 C CB . GLN A 221 ? 0.3695 0.3753 0.3498 0.0167 0.0374 0.0020 209 GLN B CB 1725 C CG . GLN A 221 ? 0.3948 0.3956 0.3790 0.0169 0.0312 -0.0032 209 GLN B CG 1726 C CD . GLN A 221 ? 0.4023 0.3933 0.3752 0.0173 0.0251 -0.0076 209 GLN B CD 1727 O OE1 . GLN A 221 ? 0.3981 0.3861 0.3599 0.0177 0.0239 -0.0072 209 GLN B OE1 1728 N NE2 . GLN A 221 ? 0.4244 0.4100 0.4003 0.0169 0.0202 -0.0110 209 GLN B NE2 1729 N N . MET A 222 ? 0.3183 0.3459 0.3386 0.0162 0.0421 0.0061 210 MET B N 1730 C CA . MET A 222 ? 0.3125 0.3483 0.3453 0.0210 0.0440 0.0051 210 MET B CA 1731 C C . MET A 222 ? 0.3175 0.3433 0.3455 0.0251 0.0379 -0.0009 210 MET B C 1732 O O . MET A 222 ? 0.3118 0.3399 0.3443 0.0324 0.0402 -0.0035 210 MET B O 1733 C CB . MET A 222 ? 0.3356 0.3812 0.3885 0.0157 0.0407 0.0101 210 MET B CB 1734 C CG . MET A 222 ? 0.3696 0.4231 0.4306 0.0094 0.0447 0.0171 210 MET B CG 1735 S SD . MET A 222 ? 0.4067 0.4716 0.4662 0.0134 0.0594 0.0218 210 MET B SD 1736 C CE . MET A 222 ? 0.4292 0.5110 0.5072 0.0222 0.0659 0.0209 210 MET B CE 1737 N N . GLY A 223 ? 0.2784 0.2935 0.2987 0.0207 0.0306 -0.0024 211 GLY B N 1738 C CA . GLY A 223 ? 0.2990 0.3041 0.3156 0.0225 0.0247 -0.0060 211 GLY B CA 1739 C C . GLY A 223 ? 0.3045 0.2986 0.3092 0.0191 0.0205 -0.0082 211 GLY B C 1740 O O . GLY A 223 ? 0.3271 0.3216 0.3270 0.0155 0.0212 -0.0070 211 GLY B O 1741 N N . ILE A 224 ? 0.3012 0.2854 0.3031 0.0202 0.0156 -0.0106 212 ILE B N 1742 C CA . ILE A 224 ? 0.3229 0.2981 0.3180 0.0156 0.0108 -0.0114 212 ILE B CA 1743 C C . ILE A 224 ? 0.3102 0.2811 0.3092 0.0119 0.0063 -0.0082 212 ILE B C 1744 O O . ILE A 224 ? 0.3296 0.2960 0.3314 0.0153 0.0038 -0.0081 212 ILE B O 1745 C CB . ILE A 224 ? 0.3486 0.3125 0.3346 0.0191 0.0080 -0.0171 212 ILE B CB 1746 C CG1 . ILE A 224 ? 0.3557 0.3223 0.3328 0.0241 0.0131 -0.0205 212 ILE B CG1 1747 C CG2 . ILE A 224 ? 0.3638 0.3203 0.3475 0.0125 0.0016 -0.0168 212 ILE B CG2 1748 C CD1 . ILE A 224 ? 0.3977 0.3515 0.3626 0.0304 0.0113 -0.0281 212 ILE B CD1 1749 N N . VAL A 225 ? 0.3087 0.2805 0.3071 0.0058 0.0055 -0.0051 213 VAL B N 1750 C CA . VAL A 225 ? 0.3161 0.2834 0.3145 0.0020 0.0026 -0.0009 213 VAL B CA 1751 C C . VAL A 225 ? 0.3165 0.2714 0.3138 0.0023 -0.0025 -0.0014 213 VAL B C 1752 O O . VAL A 225 ? 0.3459 0.2959 0.3419 0.0003 -0.0045 -0.0036 213 VAL B O 1753 C CB . VAL A 225 ? 0.3105 0.2814 0.3079 -0.0038 0.0049 0.0022 213 VAL B CB 1754 C CG1 . VAL A 225 ? 0.2968 0.2628 0.2911 -0.0077 0.0035 0.0075 213 VAL B CG1 1755 C CG2 . VAL A 225 ? 0.3219 0.3009 0.3192 -0.0033 0.0089 0.0017 213 VAL B CG2 1756 N N . SER A 226 ? 0.3176 0.2661 0.3156 0.0048 -0.0060 0.0007 214 SER B N 1757 C CA . SER A 226 ? 0.3296 0.2627 0.3266 0.0061 -0.0117 0.0003 214 SER B CA 1758 C C . SER A 226 ? 0.3530 0.2778 0.3482 0.0009 -0.0159 0.0081 214 SER B C 1759 O O . SER A 226 ? 0.3703 0.2854 0.3646 -0.0046 -0.0189 0.0106 214 SER B O 1760 C CB . SER A 226 ? 0.3522 0.2819 0.3523 0.0162 -0.0129 -0.0042 214 SER B CB 1761 O OG . SER A 226 ? 0.3494 0.2609 0.3474 0.0184 -0.0190 -0.0057 214 SER B OG 1762 N N . TRP A 227 ? 0.3586 0.2861 0.3530 0.0024 -0.0171 0.0125 215 TRP B N 1763 C CA . TRP A 227 ? 0.3479 0.2652 0.3368 -0.0018 -0.0216 0.0209 215 TRP B CA 1764 C C . TRP A 227 ? 0.3589 0.2817 0.3421 -0.0020 -0.0226 0.0256 215 TRP B C 1765 O O . TRP A 227 ? 0.3447 0.2784 0.3313 0.0015 -0.0214 0.0220 215 TRP B O 1766 C CB . TRP A 227 ? 0.3605 0.2605 0.3518 0.0027 -0.0294 0.0216 215 TRP B CB 1767 C CG . TRP A 227 ? 0.3602 0.2612 0.3587 0.0138 -0.0326 0.0178 215 TRP B CG 1768 C CD1 . TRP A 227 ? 0.3882 0.2929 0.3936 0.0223 -0.0299 0.0089 215 TRP B CD1 1769 C CD2 . TRP A 227 ? 0.3711 0.2707 0.3718 0.0180 -0.0390 0.0232 215 TRP B CD2 1770 N NE1 . TRP A 227 ? 0.3850 0.2929 0.3998 0.0319 -0.0326 0.0087 215 TRP B NE1 1771 C CE2 . TRP A 227 ? 0.3765 0.2813 0.3898 0.0293 -0.0395 0.0174 215 TRP B CE2 1772 C CE3 . TRP A 227 ? 0.3946 0.2893 0.3870 0.0136 -0.0446 0.0328 215 TRP B CE3 1773 C CZ2 . TRP A 227 ? 0.3947 0.3021 0.4170 0.0362 -0.0462 0.0211 215 TRP B CZ2 1774 C CZ3 . TRP A 227 ? 0.4039 0.2982 0.4012 0.0202 -0.0528 0.0363 215 TRP B CZ3 1775 C CH2 . TRP A 227 ? 0.4118 0.3132 0.4262 0.0314 -0.0541 0.0305 215 TRP B CH2 1776 N N . GLY A 228 ? 0.3475 0.2615 0.3209 -0.0069 -0.0253 0.0342 216 GLY B N 1777 C CA . GLY A 228 ? 0.3770 0.2914 0.3397 -0.0071 -0.0286 0.0392 216 GLY B CA 1778 C C . GLY A 228 ? 0.4151 0.3164 0.3649 -0.0124 -0.0314 0.0499 216 GLY B C 1779 O O . GLY A 228 ? 0.5084 0.4014 0.4603 -0.0169 -0.0302 0.0538 216 GLY B O 1780 N N . GLU A 229 ? 0.4504 0.3486 0.3861 -0.0126 -0.0360 0.0554 217 GLU B N 1781 C CA . GLU A 229 ? 0.4921 0.3771 0.4115 -0.0178 -0.0382 0.0672 217 GLU B CA 1782 C C . GLU A 229 ? 0.5292 0.4197 0.4282 -0.0223 -0.0308 0.0694 217 GLU B C 1783 O O . GLU A 229 ? 0.5540 0.4463 0.4417 -0.0195 -0.0353 0.0670 217 GLU B O 1784 C CB . GLU A 229 ? 0.5400 0.4128 0.4569 -0.0129 -0.0520 0.0730 217 GLU B CB 1785 C CG . GLU A 229 ? 0.5455 0.4103 0.4819 -0.0067 -0.0583 0.0706 217 GLU B CG 1786 C CD . GLU A 229 ? 0.5864 0.4428 0.5256 0.0009 -0.0722 0.0749 217 GLU B CD 1787 O OE1 . GLU A 229 ? 0.5485 0.4167 0.4984 0.0077 -0.0764 0.0691 217 GLU B OE1 1788 O OE2 . GLU A 229 ? 0.6708 0.5088 0.6031 -0.0001 -0.0794 0.0850 217 GLU B OE2 1789 N N . GLY A 230 ? 0.5130 0.4062 0.4081 -0.0289 -0.0195 0.0734 219 GLY B N 1790 C CA . GLY A 230 ? 0.5545 0.4558 0.4331 -0.0313 -0.0086 0.0731 219 GLY B CA 1791 C C . GLY A 230 ? 0.5167 0.4315 0.4056 -0.0271 -0.0045 0.0602 219 GLY B C 1792 O O . GLY A 230 ? 0.4792 0.3988 0.3885 -0.0242 -0.0074 0.0536 219 GLY B O 1793 N N . CYS A 231 ? 0.4918 0.4112 0.3647 -0.0262 0.0021 0.0566 220 CYS B N 1794 C CA . CYS A 231 ? 0.5133 0.4428 0.3942 -0.0225 0.0057 0.0453 220 CYS B CA 1795 C C . CYS A 231 ? 0.4606 0.3852 0.3192 -0.0199 0.0028 0.0407 220 CYS B C 1796 O O . CYS A 231 ? 0.4538 0.3735 0.2883 -0.0209 0.0085 0.0440 220 CYS B O 1797 C CB . CYS A 231 ? 0.5472 0.4884 0.4373 -0.0241 0.0199 0.0441 220 CYS B CB 1798 S SG . CYS A 231 ? 0.5867 0.5329 0.5038 -0.0285 0.0208 0.0483 220 CYS B SG 1799 N N . ASP A 232 ? 0.4401 0.3657 0.3064 -0.0168 -0.0061 0.0331 221 ASP B N 1800 C CA . ASP A 232 ? 0.4565 0.3761 0.3043 -0.0153 -0.0117 0.0272 221 ASP B CA 1801 C C . ASP A 232 ? 0.4720 0.3785 0.2934 -0.0164 -0.0214 0.0331 221 ASP B C 1802 O O . ASP A 232 ? 0.4862 0.3842 0.2801 -0.0159 -0.0216 0.0299 221 ASP B O 1803 C CB . ASP A 232 ? 0.5151 0.4364 0.3512 -0.0137 0.0007 0.0207 221 ASP B CB 1804 C CG . ASP A 232 ? 0.5282 0.4415 0.3501 -0.0117 -0.0063 0.0114 221 ASP B CG 1805 O OD1 . ASP A 232 ? 0.5186 0.4332 0.3555 -0.0123 -0.0177 0.0079 221 ASP B OD1 1806 O OD2 . ASP A 232 ? 0.5105 0.4160 0.3060 -0.0098 -0.0003 0.0078 221 ASP B OD2 1807 N N . ARG A 233 A 0.4426 0.3458 0.2706 -0.0172 -0.0300 0.0415 221 ARG B N 1808 C CA . ARG A 233 A 0.4784 0.3685 0.2827 -0.0179 -0.0417 0.0485 221 ARG B CA 1809 C C . ARG A 233 A 0.4811 0.3704 0.2910 -0.0160 -0.0592 0.0439 221 ARG B C 1810 O O . ARG A 233 A 0.4502 0.3499 0.2901 -0.0142 -0.0633 0.0400 221 ARG B O 1811 C CB . ARG A 233 A 0.4905 0.3753 0.3001 -0.0192 -0.0446 0.0606 221 ARG B CB 1812 C CG . ARG A 233 A 0.5125 0.3955 0.3105 -0.0233 -0.0295 0.0682 221 ARG B CG 1813 C CD . ARG A 233 A 0.5284 0.4029 0.3316 -0.0260 -0.0332 0.0810 221 ARG B CD 1814 N NE . ARG A 233 A 0.5266 0.4024 0.3248 -0.0318 -0.0179 0.0887 221 ARG B NE 1815 C CZ . ARG A 233 A 0.5322 0.3971 0.3178 -0.0368 -0.0172 0.1031 221 ARG B CZ 1816 N NH1 . ARG A 233 A 0.5758 0.4250 0.3492 -0.0359 -0.0319 0.1117 221 ARG B NH1 1817 N NH2 . ARG A 233 A 0.5360 0.4058 0.3218 -0.0430 -0.0021 0.1101 221 ARG B NH2 1818 N N . ASP A 234 ? 0.4939 0.3711 0.2747 -0.0168 -0.0697 0.0450 222 ASP B N 1819 C CA . ASP A 234 ? 0.5321 0.4083 0.3187 -0.0162 -0.0892 0.0422 222 ASP B CA 1820 C C . ASP A 234 ? 0.5344 0.4157 0.3478 -0.0138 -0.1001 0.0500 222 ASP B C 1821 O O . ASP A 234 ? 0.5691 0.4430 0.3752 -0.0133 -0.1006 0.0601 222 ASP B O 1822 C CB . ASP A 234 ? 0.5695 0.4287 0.3152 -0.0176 -0.1005 0.0434 222 ASP B CB 1823 C CG . ASP A 234 ? 0.6300 0.4821 0.3484 -0.0183 -0.0925 0.0326 222 ASP B CG 1824 O OD1 . ASP A 234 ? 0.5968 0.4573 0.3329 -0.0179 -0.0841 0.0231 222 ASP B OD1 1825 O OD2 . ASP A 234 ? 0.6793 0.5155 0.3561 -0.0185 -0.0952 0.0335 222 ASP B OD2 1826 N N . GLY A 235 ? 0.5094 0.4032 0.3544 -0.0121 -0.1085 0.0459 223 GLY B N 1827 C CA . GLY A 235 ? 0.5091 0.4091 0.3812 -0.0078 -0.1191 0.0524 223 GLY B CA 1828 C C . GLY A 235 ? 0.4901 0.3973 0.3863 -0.0042 -0.1064 0.0535 223 GLY B C 1829 O O . GLY A 235 ? 0.4691 0.3790 0.3864 0.0011 -0.1127 0.0582 223 GLY B O 1830 N N . LYS A 236 ? 0.5108 0.4200 0.4034 -0.0065 -0.0893 0.0488 224 LYS B N 1831 C CA . LYS A 236 ? 0.4869 0.4013 0.3987 -0.0042 -0.0775 0.0482 224 LYS B CA 1832 C C . LYS A 236 ? 0.4424 0.3704 0.3709 -0.0044 -0.0674 0.0388 224 LYS B C 1833 O O . LYS A 236 ? 0.4428 0.3725 0.3618 -0.0075 -0.0654 0.0333 224 LYS B O 1834 C CB . LYS A 236 ? 0.5290 0.4326 0.4211 -0.0078 -0.0675 0.0537 224 LYS B CB 1835 C CG . LYS A 236 ? 0.6230 0.5119 0.5026 -0.0076 -0.0761 0.0652 224 LYS B CG 1836 C CD . LYS A 236 ? 0.6966 0.5853 0.6023 -0.0018 -0.0815 0.0672 224 LYS B CD 1837 C CE . LYS A 236 ? 0.7808 0.6518 0.6762 -0.0019 -0.0882 0.0792 224 LYS B CE 1838 N NZ . LYS A 236 ? 0.7429 0.6114 0.6638 0.0054 -0.0928 0.0792 224 LYS B NZ 1839 N N . TYR A 237 ? 0.3855 0.3209 0.3366 -0.0007 -0.0614 0.0368 225 TYR B N 1840 C CA . TYR A 237 ? 0.3786 0.3269 0.3463 -0.0001 -0.0527 0.0293 225 TYR B CA 1841 C C . TYR A 237 ? 0.3750 0.3229 0.3475 0.0009 -0.0417 0.0277 225 TYR B C 1842 O O . TYR A 237 ? 0.3934 0.3328 0.3654 0.0026 -0.0428 0.0318 225 TYR B O 1843 C CB . TYR A 237 ? 0.3623 0.3234 0.3557 0.0043 -0.0592 0.0281 225 TYR B CB 1844 C CG . TYR A 237 ? 0.3921 0.3532 0.3822 0.0021 -0.0731 0.0304 225 TYR B CG 1845 C CD1 . TYR A 237 ? 0.3933 0.3580 0.3804 -0.0031 -0.0749 0.0260 225 TYR B CD1 1846 C CD2 . TYR A 237 ? 0.4205 0.3756 0.4086 0.0047 -0.0861 0.0370 225 TYR B CD2 1847 C CE1 . TYR A 237 ? 0.4027 0.3653 0.3853 -0.0061 -0.0900 0.0273 225 TYR B CE1 1848 C CE2 . TYR A 237 ? 0.4351 0.3893 0.4185 0.0022 -0.1013 0.0391 225 TYR B CE2 1849 C CZ . TYR A 237 ? 0.4362 0.3941 0.4165 -0.0035 -0.1033 0.0338 225 TYR B CZ 1850 O OH . TYR A 237 ? 0.4547 0.4097 0.4286 -0.0069 -0.1202 0.0350 225 TYR B OH 1851 N N . GLY A 238 ? 0.3194 0.2749 0.2961 -0.0005 -0.0326 0.0221 226 GLY B N 1852 C CA . GLY A 238 ? 0.3463 0.3025 0.3284 0.0003 -0.0240 0.0197 226 GLY B CA 1853 C C . GLY A 238 ? 0.3325 0.2951 0.3330 0.0066 -0.0242 0.0168 226 GLY B C 1854 O O . GLY A 238 ? 0.3214 0.2942 0.3339 0.0089 -0.0261 0.0154 226 GLY B O 1855 N N . PHE A 239 ? 0.3105 0.2666 0.3132 0.0093 -0.0223 0.0160 227 PHE B N 1856 C CA . PHE A 239 ? 0.3302 0.2904 0.3462 0.0168 -0.0202 0.0116 227 PHE B CA 1857 C C . PHE A 239 ? 0.3278 0.2905 0.3425 0.0165 -0.0122 0.0061 227 PHE B C 1858 O O . PHE A 239 ? 0.3149 0.2720 0.3209 0.0113 -0.0104 0.0062 227 PHE B O 1859 C CB . PHE A 239 ? 0.3407 0.2887 0.3591 0.0224 -0.0260 0.0132 227 PHE B CB 1860 C CG . PHE A 239 ? 0.3509 0.2996 0.3754 0.0256 -0.0349 0.0184 227 PHE B CG 1861 C CD1 . PHE A 239 ? 0.3839 0.3257 0.3960 0.0197 -0.0414 0.0251 227 PHE B CD1 1862 C CD2 . PHE A 239 ? 0.3428 0.3003 0.3855 0.0348 -0.0366 0.0169 227 PHE B CD2 1863 C CE1 . PHE A 239 ? 0.3784 0.3203 0.3944 0.0224 -0.0519 0.0303 227 PHE B CE1 1864 C CE2 . PHE A 239 ? 0.3668 0.3268 0.4182 0.0379 -0.0466 0.0223 227 PHE B CE2 1865 C CZ . PHE A 239 ? 0.3768 0.3281 0.4140 0.0314 -0.0554 0.0290 227 PHE B CZ 1866 N N . TYR A 240 ? 0.3112 0.2834 0.3352 0.0222 -0.0077 0.0022 228 TYR B N 1867 C CA . TYR A 240 ? 0.3164 0.2924 0.3375 0.0223 -0.0005 -0.0023 228 TYR B CA 1868 C C . TYR A 240 ? 0.3556 0.3315 0.3804 0.0315 0.0031 -0.0071 228 TYR B C 1869 O O . TYR A 240 ? 0.3160 0.2987 0.3530 0.0384 0.0034 -0.0067 228 TYR B O 1870 C CB . TYR A 240 ? 0.3049 0.2944 0.3303 0.0190 0.0038 -0.0010 228 TYR B CB 1871 C CG . TYR A 240 ? 0.3020 0.2897 0.3211 0.0116 0.0010 0.0018 228 TYR B CG 1872 C CD1 . TYR A 240 ? 0.3521 0.3391 0.3722 0.0096 -0.0052 0.0052 228 TYR B CD1 1873 C CD2 . TYR A 240 ? 0.3078 0.2937 0.3189 0.0074 0.0043 0.0008 228 TYR B CD2 1874 C CE1 . TYR A 240 ? 0.3669 0.3502 0.3768 0.0040 -0.0070 0.0066 228 TYR B CE1 1875 C CE2 . TYR A 240 ? 0.3266 0.3107 0.3313 0.0024 0.0034 0.0025 228 TYR B CE2 1876 C CZ . TYR A 240 ? 0.3398 0.3218 0.3421 0.0009 -0.0017 0.0050 228 TYR B CZ 1877 O OH . TYR A 240 ? 0.3421 0.3202 0.3335 -0.0029 -0.0021 0.0056 228 TYR B OH 1878 N N . THR A 241 ? 0.3346 0.3033 0.3490 0.0322 0.0058 -0.0120 229 THR B N 1879 C CA . THR A 241 ? 0.3751 0.3415 0.3873 0.0417 0.0103 -0.0182 229 THR B CA 1880 C C . THR A 241 ? 0.3370 0.3213 0.3559 0.0446 0.0196 -0.0173 229 THR B C 1881 O O . THR A 241 ? 0.3613 0.3526 0.3774 0.0384 0.0224 -0.0147 229 THR B O 1882 C CB . THR A 241 ? 0.4040 0.3565 0.4000 0.0408 0.0088 -0.0241 229 THR B CB 1883 O OG1 . THR A 241 ? 0.4175 0.3548 0.4105 0.0354 0.0000 -0.0231 229 THR B OG1 1884 C CG2 . THR A 241 ? 0.3852 0.3315 0.3735 0.0519 0.0132 -0.0322 229 THR B CG2 1885 N N . HIS A 242 ? 0.3665 0.3580 0.3951 0.0542 0.0246 -0.0189 230 HIS B N 1886 C CA . HIS A 242 ? 0.3464 0.3578 0.3868 0.0567 0.0342 -0.0159 230 HIS B CA 1887 C C . HIS A 242 ? 0.3548 0.3641 0.3784 0.0606 0.0433 -0.0206 230 HIS B C 1888 O O . HIS A 242 ? 0.4221 0.4266 0.4392 0.0713 0.0486 -0.0270 230 HIS B O 1889 C CB . HIS A 242 ? 0.4106 0.4316 0.4706 0.0666 0.0360 -0.0155 230 HIS B CB 1890 C CG . HIS A 242 ? 0.4156 0.4616 0.4966 0.0675 0.0445 -0.0098 230 HIS B CG 1891 N ND1 . HIS A 242 ? 0.3964 0.4532 0.4735 0.0671 0.0565 -0.0087 230 HIS B ND1 1892 C CD2 . HIS A 242 ? 0.4151 0.4780 0.5228 0.0686 0.0422 -0.0042 230 HIS B CD2 1893 C CE1 . HIS A 242 ? 0.3933 0.4732 0.4952 0.0670 0.0622 -0.0020 230 HIS B CE1 1894 N NE2 . HIS A 242 ? 0.3953 0.4800 0.5174 0.0680 0.0532 0.0004 230 HIS B NE2 1895 N N . VAL A 243 ? 0.3409 0.3524 0.3559 0.0526 0.0447 -0.0177 231 VAL B N 1896 C CA . VAL A 243 ? 0.3627 0.3687 0.3567 0.0549 0.0503 -0.0214 231 VAL B CA 1897 C C . VAL A 243 ? 0.3540 0.3712 0.3475 0.0643 0.0641 -0.0221 231 VAL B C 1898 O O . VAL A 243 ? 0.3873 0.3941 0.3612 0.0726 0.0681 -0.0296 231 VAL B O 1899 C CB . VAL A 243 ? 0.3630 0.3701 0.3503 0.0450 0.0486 -0.0164 231 VAL B CB 1900 C CG1 . VAL A 243 ? 0.4183 0.4225 0.3848 0.0479 0.0548 -0.0179 231 VAL B CG1 1901 C CG2 . VAL A 243 ? 0.3831 0.3776 0.3659 0.0381 0.0371 -0.0177 231 VAL B CG2 1902 N N . PHE A 244 ? 0.3570 0.3950 0.3713 0.0632 0.0716 -0.0145 232 PHE B N 1903 C CA . PHE A 244 ? 0.3813 0.4336 0.3972 0.0717 0.0873 -0.0134 232 PHE B CA 1904 C C . PHE A 244 ? 0.4138 0.4627 0.4293 0.0865 0.0920 -0.0220 232 PHE B C 1905 O O . PHE A 244 ? 0.4028 0.4515 0.4027 0.0963 0.1039 -0.0266 232 PHE B O 1906 C CB . PHE A 244 ? 0.3724 0.4502 0.4172 0.0670 0.0941 -0.0026 232 PHE B CB 1907 C CG . PHE A 244 ? 0.3770 0.4725 0.4258 0.0753 0.1123 0.0001 232 PHE B CG 1908 C CD1 . PHE A 244 ? 0.4397 0.5337 0.4657 0.0746 0.1223 0.0024 232 PHE B CD1 1909 C CD2 . PHE A 244 ? 0.3875 0.5008 0.4615 0.0850 0.1198 0.0003 232 PHE B CD2 1910 C CE1 . PHE A 244 ? 0.4268 0.5370 0.4531 0.0827 0.1412 0.0054 232 PHE B CE1 1911 C CE2 . PHE A 244 ? 0.4154 0.5472 0.4938 0.0939 0.1392 0.0029 232 PHE B CE2 1912 C CZ . PHE A 244 ? 0.4442 0.5745 0.4976 0.0925 0.1507 0.0056 232 PHE B CZ 1913 N N . ARG A 245 ? 0.4158 0.4608 0.4469 0.0890 0.0828 -0.0241 233 ARG B N 1914 C CA . ARG A 245 ? 0.5019 0.5402 0.5341 0.1040 0.0852 -0.0325 233 ARG B CA 1915 C C . ARG A 245 ? 0.4637 0.4755 0.4617 0.1107 0.0841 -0.0445 233 ARG B C 1916 O O . ARG A 245 ? 0.4847 0.4910 0.4760 0.1252 0.0912 -0.0529 233 ARG B O 1917 C CB . ARG A 245 ? 0.5153 0.5483 0.5660 0.1036 0.0719 -0.0316 233 ARG B CB 1918 C CG . ARG A 245 ? 0.5707 0.6285 0.6564 0.1014 0.0715 -0.0219 233 ARG B CG 1919 C CD . ARG A 245 ? 0.6292 0.7010 0.7372 0.1171 0.0793 -0.0235 233 ARG B CD 1920 N NE . ARG A 245 ? 0.6955 0.7440 0.7935 0.1285 0.0730 -0.0327 233 ARG B NE 1921 C CZ . ARG A 245 ? 0.7142 0.7663 0.8242 0.1458 0.0796 -0.0377 233 ARG B CZ 1922 N NH1 . ARG A 245 ? 0.6907 0.7161 0.7888 0.1550 0.0717 -0.0464 233 ARG B NH1 1923 N NH2 . ARG A 245 ? 0.6900 0.7719 0.8252 0.1540 0.0939 -0.0337 233 ARG B NH2 1924 N N . LEU A 246 ? 0.4455 0.4408 0.4230 0.1004 0.0743 -0.0457 234 LEU B N 1925 C CA . LEU A 246 ? 0.5013 0.4706 0.4472 0.1041 0.0695 -0.0567 234 LEU B CA 1926 C C . LEU A 246 ? 0.5469 0.5156 0.4663 0.1028 0.0763 -0.0576 234 LEU B C 1927 O O . LEU A 246 ? 0.5283 0.4753 0.4200 0.1031 0.0693 -0.0658 234 LEU B O 1928 C CB . LEU A 246 ? 0.5512 0.5018 0.4945 0.0936 0.0518 -0.0574 234 LEU B CB 1929 C CG . LEU A 246 ? 0.5058 0.4553 0.4721 0.0935 0.0442 -0.0546 234 LEU B CG 1930 C CD1 . LEU A 246 ? 0.5544 0.4886 0.5185 0.0817 0.0293 -0.0526 234 LEU B CD1 1931 C CD2 . LEU A 246 ? 0.6048 0.5437 0.5715 0.1091 0.0466 -0.0631 234 LEU B CD2 1932 N N . LYS A 247 ? 0.5375 0.5287 0.4646 0.1011 0.0890 -0.0488 235 LYS B N 1933 C CA . LYS A 247 ? 0.6360 0.6265 0.5381 0.0984 0.0946 -0.0467 235 LYS B CA 1934 C C . LYS A 247 ? 0.6223 0.5995 0.4910 0.1119 0.1031 -0.0576 235 LYS B C 1935 O O . LYS A 247 ? 0.6849 0.6505 0.5231 0.1098 0.1010 -0.0595 235 LYS B O 1936 C CB . LYS A 247 ? 0.6662 0.6827 0.5857 0.0926 0.1062 -0.0331 235 LYS B CB 1937 C CG . LYS A 247 ? 0.7374 0.7518 0.6324 0.0873 0.1094 -0.0279 235 LYS B CG 1938 C CD . LYS A 247 ? 0.7564 0.7924 0.6718 0.0780 0.1167 -0.0130 235 LYS B CD 1939 C CE . LYS A 247 ? 0.7416 0.7745 0.6305 0.0749 0.1220 -0.0068 235 LYS B CE 1940 N NZ . LYS A 247 ? 0.7187 0.7705 0.6272 0.0658 0.1297 0.0085 235 LYS B NZ 1941 N N . LYS A 248 ? 0.6221 0.5995 0.4951 0.1262 0.1116 -0.0652 236 LYS B N 1942 C CA . LYS A 248 ? 0.7022 0.6630 0.5400 0.1407 0.1193 -0.0781 236 LYS B CA 1943 C C . LYS A 248 ? 0.7141 0.6402 0.5226 0.1389 0.1007 -0.0904 236 LYS B C 1944 O O . LYS A 248 ? 0.7087 0.6179 0.4789 0.1423 0.1003 -0.0978 236 LYS B O 1945 C CB . LYS A 248 ? 0.7686 0.7363 0.6194 0.1585 0.1326 -0.0846 236 LYS B CB 1946 C CG . LYS A 248 ? 0.9063 0.8951 0.7506 0.1693 0.1576 -0.0816 236 LYS B CG 1947 C CD . LYS A 248 ? 1.0495 1.0544 0.9197 0.1862 0.1722 -0.0846 236 LYS B CD 1948 C CE . LYS A 248 ? 1.0714 1.1076 0.9941 0.1787 0.1726 -0.0703 236 LYS B CE 1949 N NZ . LYS A 248 ? 1.0978 1.1611 1.0331 0.1656 0.1815 -0.0538 236 LYS B NZ 1950 N N . TRP A 249 ? 0.6529 0.5682 0.4794 0.1328 0.0847 -0.0918 237 TRP B N 1951 C CA . TRP A 249 ? 0.6443 0.5295 0.4509 0.1273 0.0653 -0.1007 237 TRP B CA 1952 C C . TRP A 249 ? 0.5895 0.4742 0.3814 0.1137 0.0567 -0.0948 237 TRP B C 1953 O O . TRP A 249 ? 0.6290 0.4924 0.3884 0.1139 0.0481 -0.1032 237 TRP B O 1954 C CB . TRP A 249 ? 0.6202 0.4985 0.4532 0.1208 0.0513 -0.0991 237 TRP B CB 1955 C CG . TRP A 249 ? 0.6203 0.4710 0.4371 0.1128 0.0319 -0.1057 237 TRP B CG 1956 C CD1 . TRP A 249 ? 0.6629 0.4827 0.4542 0.1198 0.0236 -0.1203 237 TRP B CD1 1957 C CD2 . TRP A 249 ? 0.6116 0.4632 0.4367 0.0960 0.0183 -0.0981 237 TRP B CD2 1958 N NE1 . TRP A 249 ? 0.6535 0.4557 0.4391 0.1068 0.0043 -0.1213 237 TRP B NE1 1959 C CE2 . TRP A 249 ? 0.6175 0.4404 0.4248 0.0924 0.0016 -0.1075 237 TRP B CE2 1960 C CE3 . TRP A 249 ? 0.5732 0.4468 0.4198 0.0839 0.0185 -0.0847 237 TRP B CE3 1961 C CZ2 . TRP A 249 ? 0.6386 0.4581 0.4529 0.0770 -0.0138 -0.1025 237 TRP B CZ2 1962 C CZ3 . TRP A 249 ? 0.5992 0.4678 0.4499 0.0704 0.0043 -0.0809 237 TRP B CZ3 1963 C CH2 . TRP A 249 ? 0.5696 0.4131 0.4057 0.0669 -0.0112 -0.0892 237 TRP B CH2 1964 N N . ILE A 250 ? 0.5239 0.4309 0.3394 0.1027 0.0583 -0.0808 238 ILE B N 1965 C CA . ILE A 250 ? 0.5295 0.4383 0.3354 0.0911 0.0512 -0.0739 238 ILE B CA 1966 C C . ILE A 250 ? 0.5989 0.5026 0.3681 0.0972 0.0585 -0.0767 238 ILE B C 1967 O O . ILE A 250 ? 0.5971 0.4847 0.3416 0.0929 0.0460 -0.0802 238 ILE B O 1968 C CB . ILE A 250 ? 0.5255 0.4589 0.3608 0.0813 0.0552 -0.0591 238 ILE B CB 1969 C CG1 . ILE A 250 ? 0.4971 0.4322 0.3620 0.0743 0.0457 -0.0567 238 ILE B CG1 1970 C CG2 . ILE A 250 ? 0.5210 0.4555 0.3451 0.0721 0.0495 -0.0521 238 ILE B CG2 1971 C CD1 . ILE A 250 ? 0.4541 0.4104 0.3460 0.0661 0.0493 -0.0444 238 ILE B CD1 1972 N N . GLN A 251 ? 0.6097 0.5270 0.3753 0.1072 0.0782 -0.0749 239 GLN B N 1973 C CA . GLN A 251 ? 0.6929 0.6073 0.4218 0.1141 0.0891 -0.0761 239 GLN B CA 1974 C C . GLN A 251 ? 0.7344 0.6186 0.4221 0.1234 0.0819 -0.0929 239 GLN B C 1975 O O . GLN A 251 ? 0.7303 0.6015 0.3815 0.1226 0.0771 -0.0947 239 GLN B O 1976 C CB . GLN A 251 ? 0.7728 0.7102 0.5111 0.1240 0.1142 -0.0709 239 GLN B CB 1977 C CG . GLN A 251 ? 0.9237 0.8585 0.6213 0.1328 0.1290 -0.0720 239 GLN B CG 1978 C CD . GLN A 251 ? 1.0086 0.9651 0.7149 0.1456 0.1555 -0.0696 239 GLN B CD 1979 O OE1 . GLN A 251 ? 1.1414 1.1161 0.8869 0.1481 0.1619 -0.0671 239 GLN B OE1 1980 N NE2 . GLN A 251 ? 1.0462 1.0014 0.7157 0.1540 0.1711 -0.0699 239 GLN B NE2 1981 N N . LYS A 252 ? 0.7265 0.5984 0.4184 0.1330 0.0811 -0.1052 240 LYS B N 1982 C CA . LYS A 252 ? 0.7721 0.6112 0.4261 0.1427 0.0730 -0.1233 240 LYS B CA 1983 C C . LYS A 252 ? 0.7316 0.5487 0.3695 0.1301 0.0476 -0.1264 240 LYS B C 1984 O O . LYS A 252 ? 0.7380 0.5353 0.3341 0.1326 0.0411 -0.1341 240 LYS B O 1985 C CB . LYS A 252 ? 0.8222 0.6499 0.4921 0.1525 0.0720 -0.1342 240 LYS B CB 1986 C CG . LYS A 252 ? 0.9939 0.8001 0.6286 0.1722 0.0810 -0.1518 240 LYS B CG 1987 C CD . LYS A 252 ? 1.0750 0.9074 0.7125 0.1863 0.1102 -0.1475 240 LYS B CD 1988 C CE . LYS A 252 ? 1.2225 1.0341 0.8218 0.2079 0.1217 -0.1657 240 LYS B CE 1989 N NZ . LYS A 252 ? 1.2528 1.0933 0.8577 0.2225 0.1525 -0.1608 240 LYS B NZ 1990 N N . VAL A 253 ? 0.6626 0.4844 0.3343 0.1167 0.0335 -0.1198 241 VAL B N 1991 C CA . VAL A 253 ? 0.6807 0.4852 0.3469 0.1043 0.0094 -0.1218 241 VAL B CA 1992 C C . VAL A 253 ? 0.6952 0.5034 0.3391 0.0984 0.0053 -0.1153 241 VAL B C 1993 O O . VAL A 253 ? 0.7393 0.5250 0.3504 0.0977 -0.0093 -0.1237 241 VAL B O 1994 C CB . VAL A 253 ? 0.6490 0.4643 0.3586 0.0912 -0.0003 -0.1129 241 VAL B CB 1995 C CG1 . VAL A 253 ? 0.6664 0.4746 0.3770 0.0769 -0.0216 -0.1101 241 VAL B CG1 1996 C CG2 . VAL A 253 ? 0.6546 0.4558 0.3775 0.0961 -0.0032 -0.1212 241 VAL B CG2 1997 N N . ILE A 254 ? 0.6988 0.5338 0.3600 0.0945 0.0175 -0.1002 242 ILE B N 1998 C CA . ILE A 254 ? 0.7431 0.5834 0.3874 0.0889 0.0147 -0.0910 242 ILE B CA 1999 C C . ILE A 254 ? 0.8171 0.6437 0.4112 0.0995 0.0216 -0.0974 242 ILE B C 2000 O O . ILE A 254 ? 0.8353 0.6472 0.4000 0.0962 0.0071 -0.0991 242 ILE B O 2001 C CB . ILE A 254 ? 0.7095 0.5792 0.3849 0.0829 0.0270 -0.0736 242 ILE B CB 2002 C CG1 . ILE A 254 ? 0.6601 0.5376 0.3731 0.0702 0.0135 -0.0673 242 ILE B CG1 2003 C CG2 . ILE A 254 ? 0.7534 0.6277 0.4053 0.0817 0.0313 -0.0636 242 ILE B CG2 2004 C CD1 . ILE A 254 ? 0.6612 0.5635 0.4103 0.0658 0.0250 -0.0548 242 ILE B CD1 2005 N N . ASP A 255 ? 0.8930 0.7246 0.4768 0.1125 0.0433 -0.1010 243 ASP B N 2006 C CA . ASP A 255 ? 1.0070 0.8257 0.5395 0.1241 0.0531 -0.1076 243 ASP B CA 2007 C C . ASP A 255 ? 1.0860 0.8686 0.5786 0.1291 0.0352 -0.1267 243 ASP B C 2008 O O . ASP A 255 ? 1.1685 0.9345 0.6151 0.1313 0.0292 -0.1303 243 ASP B O 2009 C CB . ASP A 255 ? 1.1141 0.9475 0.6479 0.1384 0.0818 -0.1083 243 ASP B CB 2010 C CG . ASP A 255 ? 1.1966 1.0636 0.7563 0.1338 0.1007 -0.0885 243 ASP B CG 2011 O OD1 . ASP A 255 ? 1.3445 1.2227 0.9272 0.1197 0.0913 -0.0751 243 ASP B OD1 2012 O OD2 . ASP A 255 ? 1.2406 1.1228 0.7988 0.1444 0.1252 -0.0865 243 ASP B OD2 2013 N N . GLN A 256 ? 1.0961 0.8646 0.6048 0.1303 0.0253 -0.1386 244 GLN B N 2014 C CA . GLN A 256 ? 1.2269 0.9578 0.6991 0.1353 0.0081 -0.1582 244 GLN B CA 2015 C C . GLN A 256 ? 1.2178 0.9333 0.6881 0.1201 -0.0227 -0.1585 244 GLN B C 2016 O O . GLN A 256 ? 1.2462 0.9306 0.6768 0.1220 -0.0395 -0.1724 244 GLN B O 2017 C CB . GLN A 256 ? 1.2834 1.0024 0.7718 0.1441 0.0107 -0.1709 244 GLN B CB 2018 C CG . GLN A 256 ? 1.3613 1.0903 0.8424 0.1631 0.0398 -0.1749 244 GLN B CG 2019 C CD . GLN A 256 ? 1.4313 1.1478 0.9292 0.1739 0.0420 -0.1873 244 GLN B CD 2020 O OE1 . GLN A 256 ? 1.5109 1.2216 1.0404 0.1647 0.0262 -0.1868 244 GLN B OE1 2021 N NE2 . GLN A 256 ? 1.4561 1.1689 0.9331 0.1941 0.0625 -0.1977 244 GLN B NE2 2022 N N . PHE A 257 ? 1.2165 0.9534 0.7293 0.1052 -0.0303 -0.1435 245 PHE B N 2023 C CA . PHE A 257 ? 1.2479 0.9765 0.7685 0.0905 -0.0581 -0.1417 245 PHE B CA 2024 C C . PHE A 257 ? 1.1442 0.8969 0.6804 0.0807 -0.0596 -0.1236 245 PHE B C 2025 O O . PHE A 257 ? 1.0256 0.7767 0.5721 0.0691 -0.0811 -0.1198 245 PHE B O 2026 C CB . PHE A 257 ? 1.2678 0.9950 0.8303 0.0816 -0.0694 -0.1431 245 PHE B CB 2027 C CG . PHE A 257 ? 1.4377 1.1337 0.9842 0.0885 -0.0763 -0.1614 245 PHE B CG 2028 C CD1 . PHE A 257 ? 1.5566 1.2189 1.0658 0.0880 -0.0978 -0.1759 245 PHE B CD1 2029 C CD2 . PHE A 257 ? 1.4299 1.1281 0.9986 0.0955 -0.0631 -0.1643 245 PHE B CD2 2030 C CE1 . PHE A 257 ? 1.5524 1.1820 1.0459 0.0944 -0.1053 -0.1936 245 PHE B CE1 2031 C CE2 . PHE A 257 ? 1.4876 1.1544 1.0422 0.1027 -0.0702 -0.1810 245 PHE B CE2 2032 C CZ . PHE A 257 ? 1.5616 1.1931 1.0782 0.1022 -0.0911 -0.1960 245 PHE B CZ 2033 N N . THR B 1 N 1.3923 1.4182 1.0635 0.1057 0.1938 -0.0592 1 THR A N 2034 C CA . THR B 1 N 1.3956 1.3703 1.0252 0.1194 0.1647 -0.0784 1 THR A CA 2035 C C . THR B 1 N 1.3076 1.2812 0.9338 0.1483 0.1704 -0.1048 1 THR A C 2036 O O . THR B 1 N 1.4707 1.4554 1.0633 0.1667 0.1968 -0.1152 1 THR A O 2037 C CB . THR B 1 N 1.4876 1.4233 1.0400 0.1178 0.1585 -0.0761 1 THR A CB 2038 O OG1 . THR B 1 N 1.5570 1.4447 1.0754 0.1283 0.1263 -0.0953 1 THR A OG1 2039 C CG2 . THR B 1 N 1.5556 1.5055 1.0589 0.1296 0.1956 -0.0778 1 THR A CG2 2040 N N . PHE B 2 M 1.1780 1.1366 0.8371 0.1531 0.1461 -0.1151 1 PHE A N 2041 C CA . PHE B 2 M 1.1995 1.1456 0.8552 0.1813 0.1444 -0.1401 1 PHE A CA 2042 C C . PHE B 2 M 1.1624 1.0444 0.7571 0.1914 0.1175 -0.1596 1 PHE A C 2043 O O . PHE B 2 M 1.1442 1.0083 0.6922 0.2169 0.1267 -0.1807 1 PHE A O 2044 C CB . PHE B 2 M 1.1809 1.1387 0.9005 0.1805 0.1311 -0.1391 1 PHE A CB 2045 C CG . PHE B 2 M 1.3363 1.2777 1.0545 0.2110 0.1269 -0.1632 1 PHE A CG 2046 C CD1 . PHE B 2 M 1.4078 1.3907 1.1430 0.2366 0.1554 -0.1736 1 PHE A CD1 2047 C CD2 . PHE B 2 M 1.4125 1.2967 1.1138 0.2142 0.0940 -0.1753 1 PHE A CD2 2048 C CE1 . PHE B 2 M 1.4418 1.4067 1.1749 0.2692 0.1497 -0.1971 1 PHE A CE1 2049 C CE2 . PHE B 2 M 1.4294 1.2891 1.1247 0.2432 0.0874 -0.1972 1 PHE A CE2 2050 C CZ . PHE B 2 M 1.4631 1.3617 1.1732 0.2729 0.1146 -0.2089 1 PHE A CZ 2051 N N . PHE B 3 L 1.0690 0.9182 0.6652 0.1714 0.0844 -0.1532 1 PHE A N 2052 C CA . PHE B 3 L 1.0924 0.8815 0.6399 0.1747 0.0528 -0.1701 1 PHE A CA 2053 C C . PHE B 3 L 1.1232 0.8925 0.6063 0.1716 0.0505 -0.1694 1 PHE A C 2054 O O . PHE B 3 L 1.0791 0.8743 0.5645 0.1571 0.0631 -0.1490 1 PHE A O 2055 C CB . PHE B 3 L 1.0478 0.8177 0.6306 0.1519 0.0190 -0.1621 1 PHE A CB 2056 C CG . PHE B 3 L 0.9832 0.7655 0.6221 0.1521 0.0179 -0.1599 1 PHE A CG 2057 C CD1 . PHE B 3 L 1.0227 0.7661 0.6529 0.1671 0.0028 -0.1784 1 PHE A CD1 2058 C CD2 . PHE B 3 L 0.9105 0.7373 0.6054 0.1382 0.0300 -0.1393 1 PHE A CD2 2059 C CE1 . PHE B 3 L 0.9791 0.7284 0.6547 0.1681 -0.0001 -0.1746 1 PHE A CE1 2060 C CE2 . PHE B 3 L 0.8527 0.6876 0.5925 0.1394 0.0271 -0.1369 1 PHE A CE2 2061 C CZ . PHE B 3 L 0.9002 0.6965 0.6299 0.1545 0.0122 -0.1537 1 PHE A CZ 2062 N N . ASN B 4 K 1.2081 0.9259 0.6298 0.1854 0.0318 -0.1918 1 ASN A N 2063 C CA . ASN B 4 K 1.2183 0.9063 0.5703 0.1834 0.0209 -0.1937 1 ASN A CA 2064 C C . ASN B 4 K 1.2322 0.9028 0.6006 0.1568 -0.0183 -0.1824 1 ASN A C 2065 O O . ASN B 4 K 1.2528 0.8970 0.6421 0.1493 -0.0490 -0.1915 1 ASN A O 2066 C CB . ASN B 4 K 1.2873 0.9229 0.5661 0.2093 0.0117 -0.2249 1 ASN A CB 2067 C CG . ASN B 4 K 1.3580 0.9585 0.5538 0.2104 -0.0002 -0.2289 1 ASN A CG 2068 O OD1 . ASN B 4 K 1.3038 0.9069 0.5006 0.1890 -0.0167 -0.2104 1 ASN A OD1 2069 N ND2 . ASN B 4 K 1.4221 0.9871 0.5421 0.2379 0.0067 -0.2543 1 ASN A ND2 2070 N N . PRO B 5 J 1.2080 0.8936 0.5682 0.1425 -0.0176 -0.1620 1 PRO A N 2071 C CA . PRO B 5 J 1.1616 0.8407 0.5475 0.1202 -0.0533 -0.1509 1 PRO A CA 2072 C C . PRO B 5 J 1.2006 0.8286 0.5370 0.1202 -0.0947 -0.1684 1 PRO A C 2073 O O . PRO B 5 J 1.1453 0.7714 0.5132 0.1020 -0.1274 -0.1627 1 PRO A O 2074 C CB . PRO B 5 J 1.1735 0.8782 0.5566 0.1108 -0.0393 -0.1259 1 PRO A CB 2075 C CG . PRO B 5 J 1.2194 0.9233 0.5422 0.1272 -0.0057 -0.1278 1 PRO A CG 2076 C CD . PRO B 5 J 1.2269 0.9357 0.5552 0.1461 0.0157 -0.1474 1 PRO A CD 2077 N N . ARG B 6 I 1.2425 0.8314 0.5041 0.1407 -0.0936 -0.1902 1 ARG A N 2078 C CA . ARG B 6 I 1.3248 0.8575 0.5355 0.1420 -0.1359 -0.2116 1 ARG A CA 2079 C C . ARG B 6 I 1.2829 0.7967 0.5399 0.1309 -0.1646 -0.2239 1 ARG A C 2080 O O . ARG B 6 I 1.3049 0.7864 0.5535 0.1181 -0.2072 -0.2329 1 ARG A O 2081 C CB . ARG B 6 I 1.4527 0.9438 0.5682 0.1701 -0.1252 -0.2354 1 ARG A CB 2082 C CG . ARG B 6 I 1.5242 1.0277 0.5808 0.1802 -0.0949 -0.2231 1 ARG A CG 2083 C CD . ARG B 6 I 1.6849 1.1314 0.6312 0.1999 -0.1075 -0.2452 1 ARG A CD 2084 N NE . ARG B 6 I 1.7565 1.1727 0.6713 0.1860 -0.1537 -0.2412 1 ARG A NE 2085 C CZ . ARG B 6 I 1.8891 1.2461 0.7165 0.1966 -0.1854 -0.2626 1 ARG A CZ 2086 N NH1 . ARG B 6 I 1.9950 1.3117 0.7510 0.2226 -0.1751 -0.2912 1 ARG A NH1 2087 N NH2 . ARG B 6 I 1.9538 1.2913 0.7646 0.1828 -0.2300 -0.2565 1 ARG A NH2 2088 N N . THR B 7 H 1.2267 0.7592 0.5310 0.1351 -0.1423 -0.2237 1 THR A N 2089 C CA . THR B 7 H 1.1880 0.7018 0.5368 0.1231 -0.1650 -0.2306 1 THR A CA 2090 C C . THR B 7 H 1.0787 0.6419 0.5154 0.1027 -0.1548 -0.2062 1 THR A C 2091 O O . THR B 7 H 1.0787 0.6344 0.5571 0.0819 -0.1791 -0.2033 1 THR A O 2092 C CB . THR B 7 H 1.2251 0.7060 0.5477 0.1486 -0.1532 -0.2534 1 THR A CB 2093 O OG1 . THR B 7 H 1.2004 0.7263 0.5404 0.1668 -0.1077 -0.2456 1 THR A OG1 2094 C CG2 . THR B 7 H 1.3295 0.7511 0.5612 0.1698 -0.1683 -0.2822 1 THR A CG2 2095 N N . PHE B 8 G 1.0140 0.6263 0.4762 0.1078 -0.1187 -0.1891 1 PHE A N 2096 C CA . PHE B 8 G 0.9051 0.5634 0.4421 0.0910 -0.1074 -0.1667 1 PHE A CA 2097 C C . PHE B 8 G 0.8582 0.5391 0.4223 0.0692 -0.1241 -0.1489 1 PHE A C 2098 O O . PHE B 8 G 0.7453 0.4532 0.3696 0.0518 -0.1271 -0.1345 1 PHE A O 2099 C CB . PHE B 8 G 0.8976 0.5969 0.4472 0.1042 -0.0659 -0.1566 1 PHE A CB 2100 C CG . PHE B 8 G 0.8359 0.5735 0.4553 0.0932 -0.0534 -0.1398 1 PHE A CG 2101 C CD1 . PHE B 8 G 0.8275 0.5525 0.4772 0.0916 -0.0617 -0.1446 1 PHE A CD1 2102 C CD2 . PHE B 8 G 0.7855 0.5666 0.4340 0.0853 -0.0338 -0.1191 1 PHE A CD2 2103 C CE1 . PHE B 8 G 0.7648 0.5217 0.4707 0.0828 -0.0507 -0.1292 1 PHE A CE1 2104 C CE2 . PHE B 8 G 0.7543 0.5667 0.4608 0.0765 -0.0239 -0.1056 1 PHE A CE2 2105 C CZ . PHE B 8 G 0.7169 0.5182 0.4509 0.0758 -0.0321 -0.1107 1 PHE A CZ 2106 N N . GLY B 9 F 0.8981 0.5671 0.4149 0.0723 -0.1350 -0.1503 1 GLY A N 2107 C CA . GLY B 9 F 0.8953 0.5873 0.4334 0.0581 -0.1489 -0.1332 1 GLY A CA 2108 C C . GLY B 9 F 0.8747 0.6048 0.4291 0.0602 -0.1174 -0.1125 1 GLY A C 2109 O O . GLY B 9 F 0.8991 0.6375 0.4378 0.0723 -0.0854 -0.1119 1 GLY A O 2110 N N . SER B 10 E 0.8607 0.6144 0.4481 0.0485 -0.1274 -0.0959 1 SER A N 2111 C CA . SER B 10 E 0.8583 0.6380 0.4538 0.0493 -0.1035 -0.0763 1 SER A CA 2112 C C . SER B 10 E 0.7691 0.5840 0.4323 0.0409 -0.0865 -0.0657 1 SER A C 2113 O O . SER B 10 E 0.7265 0.5473 0.4313 0.0326 -0.0967 -0.0705 1 SER A O 2114 C CB . SER B 10 E 0.9051 0.6828 0.4890 0.0462 -0.1258 -0.0650 1 SER A CB 2115 O OG . SER B 10 E 0.9138 0.7154 0.5597 0.0347 -0.1455 -0.0598 1 SER A OG 2116 N N . GLY B 11 D 0.7407 0.5757 0.4111 0.0415 -0.0614 -0.0507 1 GLY A N 2117 C CA . GLY B 11 D 0.6969 0.5628 0.4257 0.0338 -0.0479 -0.0398 1 GLY A CA 2118 C C . GLY B 11 D 0.7089 0.5912 0.4495 0.0377 -0.0173 -0.0385 1 GLY A C 2119 O O . GLY B 11 D 0.6870 0.5925 0.4677 0.0314 -0.0064 -0.0280 1 GLY A O 2120 N N . GLU B 12 C 0.7310 0.6030 0.4385 0.0492 -0.0041 -0.0503 1 GLU A N 2121 C CA . GLU B 12 C 0.7462 0.6416 0.4730 0.0548 0.0241 -0.0501 1 GLU A CA 2122 C C . GLU B 12 C 0.6795 0.5985 0.4132 0.0477 0.0458 -0.0321 1 GLU A C 2123 O O . GLU B 12 C 0.5763 0.5213 0.3535 0.0422 0.0573 -0.0249 1 GLU A O 2124 C CB . GLU B 12 C 0.8433 0.7279 0.5336 0.0725 0.0368 -0.0672 1 GLU A CB 2125 C CG . GLU B 12 C 0.8512 0.7662 0.5756 0.0806 0.0614 -0.0694 1 GLU A CG 2126 C CD . GLU B 12 C 0.9493 0.8598 0.6420 0.1029 0.0774 -0.0877 1 GLU A CD 2127 O OE1 . GLU B 12 C 0.9407 0.8176 0.5790 0.1129 0.0685 -0.1011 1 GLU A OE1 2128 O OE2 . GLU B 12 C 0.9760 0.9180 0.6992 0.1122 0.0984 -0.0898 1 GLU A OE2 2129 N N . ALA B 13 B 0.7070 0.6128 0.3946 0.0469 0.0493 -0.0245 1 ALA A N 2130 C CA . ALA B 13 B 0.6933 0.6133 0.3783 0.0373 0.0697 -0.0054 1 ALA A CA 2131 C C . ALA B 13 B 0.6372 0.5695 0.3692 0.0239 0.0631 0.0087 1 ALA A C 2132 O O . ALA B 13 B 0.5991 0.5503 0.3508 0.0147 0.0811 0.0206 1 ALA A O 2133 C CB . ALA B 13 B 0.7323 0.6242 0.3526 0.0373 0.0670 0.0027 1 ALA A CB 2134 N N . ASP B 14 A 0.6135 0.5360 0.3641 0.0227 0.0374 0.0065 1 ASP A N 2135 C CA . ASP B 14 A 0.5844 0.5145 0.3713 0.0139 0.0302 0.0177 1 ASP A CA 2136 C C . ASP B 14 A 0.4960 0.4438 0.3329 0.0133 0.0261 0.0105 1 ASP A C 2137 O O . ASP B 14 A 0.4413 0.3942 0.3067 0.0088 0.0179 0.0161 1 ASP A O 2138 C CB . ASP B 14 A 0.6471 0.5560 0.4162 0.0151 0.0056 0.0224 1 ASP A CB 2139 C CG . ASP B 14 A 0.6784 0.5869 0.4676 0.0097 0.0011 0.0359 1 ASP A CG 2140 O OD1 . ASP B 14 A 0.7075 0.6187 0.4996 0.0018 0.0176 0.0468 1 ASP A OD1 2141 O OD2 . ASP B 14 A 0.7218 0.6273 0.5248 0.0136 -0.0201 0.0350 1 ASP A OD2 2142 N N . CYS B 15 ? 0.4602 0.4145 0.3035 0.0193 0.0322 -0.0020 1 CYS A N 2143 C CA . CYS B 15 ? 0.4445 0.4071 0.3249 0.0191 0.0259 -0.0084 1 CYS A CA 2144 C C . CYS B 15 ? 0.3666 0.3483 0.2822 0.0130 0.0347 0.0002 1 CYS A C 2145 O O . CYS B 15 ? 0.3741 0.3671 0.2907 0.0094 0.0493 0.0078 1 CYS A O 2146 C CB . CYS B 15 ? 0.4375 0.3968 0.3125 0.0292 0.0307 -0.0229 1 CYS A CB 2147 S SG . CYS B 15 ? 0.4754 0.4591 0.3548 0.0372 0.0586 -0.0242 1 CYS A SG 2148 N N . GLY B 16 ? 0.3599 0.3444 0.3029 0.0104 0.0254 -0.0006 2 GLY A N 2149 C CA . GLY B 16 ? 0.3368 0.3351 0.3086 0.0066 0.0311 0.0044 2 GLY A CA 2150 C C . GLY B 16 ? 0.3232 0.3227 0.3000 0.0002 0.0313 0.0151 2 GLY A C 2151 O O . GLY B 16 ? 0.3669 0.3741 0.3631 -0.0031 0.0342 0.0181 2 GLY A O 2152 N N . LEU B 17 ? 0.3377 0.3253 0.2941 -0.0005 0.0256 0.0203 3 LEU A N 2153 C CA . LEU B 17 ? 0.3490 0.3288 0.3058 -0.0040 0.0220 0.0299 3 LEU A CA 2154 C C . LEU B 17 ? 0.3735 0.3497 0.3377 0.0013 0.0068 0.0286 3 LEU A C 2155 O O . LEU B 17 ? 0.4155 0.3858 0.3662 0.0054 -0.0041 0.0271 3 LEU A O 2156 C CB . LEU B 17 ? 0.4118 0.3773 0.3376 -0.0076 0.0262 0.0392 3 LEU A CB 2157 C CG . LEU B 17 ? 0.4399 0.4170 0.3622 -0.0142 0.0454 0.0419 3 LEU A CG 2158 C CD1 . LEU B 17 ? 0.5005 0.4623 0.3835 -0.0184 0.0521 0.0519 3 LEU A CD1 2159 C CD2 . LEU B 17 ? 0.4635 0.4517 0.4141 -0.0234 0.0513 0.0463 3 LEU A CD2 2160 N N . ARG B 18 ? 0.3244 0.3062 0.3103 0.0023 0.0058 0.0284 4 ARG A N 2161 C CA . ARG B 18 ? 0.3285 0.3174 0.3293 0.0085 -0.0041 0.0257 4 ARG A CA 2162 C C . ARG B 18 ? 0.3605 0.3368 0.3516 0.0161 -0.0142 0.0304 4 ARG A C 2163 O O . ARG B 18 ? 0.3507 0.3096 0.3307 0.0158 -0.0125 0.0359 4 ARG A O 2164 C CB . ARG B 18 ? 0.3393 0.3392 0.3618 0.0086 0.0015 0.0230 4 ARG A CB 2165 C CG . ARG B 18 ? 0.3099 0.3176 0.3403 0.0031 0.0078 0.0192 4 ARG A CG 2166 C CD . ARG B 18 ? 0.3337 0.3454 0.3752 0.0033 0.0130 0.0188 4 ARG A CD 2167 N NE . ARG B 18 ? 0.3191 0.3205 0.3538 0.0033 0.0153 0.0208 4 ARG A NE 2168 C CZ . ARG B 18 ? 0.3406 0.3390 0.3769 0.0044 0.0171 0.0195 4 ARG A CZ 2169 N NH1 . ARG B 18 ? 0.3034 0.3087 0.3447 0.0064 0.0201 0.0177 4 ARG A NH1 2170 N NH2 . ARG B 18 ? 0.3671 0.3536 0.3975 0.0021 0.0153 0.0206 4 ARG A NH2 2171 N N . PRO B 19 ? 0.3687 0.3519 0.3645 0.0229 -0.0274 0.0282 5 PRO A N 2172 C CA . PRO B 19 ? 0.4168 0.3872 0.4039 0.0341 -0.0405 0.0322 5 PRO A CA 2173 C C . PRO B 19 ? 0.4012 0.3684 0.4004 0.0431 -0.0385 0.0318 5 PRO A C 2174 O O . PRO B 19 ? 0.4183 0.3579 0.3974 0.0490 -0.0448 0.0373 5 PRO A O 2175 C CB . PRO B 19 ? 0.4256 0.4158 0.4293 0.0400 -0.0559 0.0271 5 PRO A CB 2176 C CG . PRO B 19 ? 0.4173 0.4108 0.4135 0.0285 -0.0536 0.0234 5 PRO A CG 2177 C CD . PRO B 19 ? 0.4049 0.4021 0.4086 0.0199 -0.0344 0.0224 5 PRO A CD 2178 N N . LEU B 20 ? 0.3759 0.3664 0.4023 0.0441 -0.0298 0.0257 6 LEU A N 2179 C CA . LEU B 20 ? 0.3873 0.3749 0.4210 0.0559 -0.0275 0.0226 6 LEU A CA 2180 C C . LEU B 20 ? 0.3631 0.3275 0.3808 0.0492 -0.0189 0.0238 6 LEU A C 2181 O O . LEU B 20 ? 0.3550 0.3068 0.3694 0.0591 -0.0191 0.0200 6 LEU A O 2182 C CB . LEU B 20 ? 0.3589 0.3844 0.4266 0.0616 -0.0210 0.0158 6 LEU A CB 2183 C CG . LEU B 20 ? 0.3924 0.4452 0.4847 0.0700 -0.0330 0.0138 6 LEU A CG 2184 C CD1 . LEU B 20 ? 0.3863 0.4839 0.5183 0.0708 -0.0231 0.0090 6 LEU A CD1 2185 C CD2 . LEU B 20 ? 0.4544 0.4911 0.5388 0.0904 -0.0482 0.0138 6 LEU A CD2 2186 N N . PHE B 21 ? 0.3680 0.3272 0.3763 0.0335 -0.0127 0.0278 7 PHE A N 2187 C CA . PHE B 21 ? 0.3472 0.2917 0.3478 0.0248 -0.0070 0.0287 7 PHE A CA 2188 C C . PHE B 21 ? 0.3543 0.2789 0.3364 0.0124 -0.0073 0.0377 7 PHE A C 2189 O O . PHE B 21 ? 0.3711 0.2662 0.3353 0.0132 -0.0148 0.0432 7 PHE A O 2190 C CB . PHE B 21 ? 0.3122 0.2772 0.3275 0.0193 0.0025 0.0240 7 PHE A CB 2191 C CG . PHE B 21 ? 0.3519 0.3305 0.3786 0.0296 0.0056 0.0178 7 PHE A CG 2192 C CD1 . PHE B 21 ? 0.3291 0.2929 0.3470 0.0380 0.0052 0.0132 7 PHE A CD1 2193 C CD2 . PHE B 21 ? 0.3204 0.3253 0.3650 0.0310 0.0089 0.0163 7 PHE A CD2 2194 C CE1 . PHE B 21 ? 0.3506 0.3290 0.3754 0.0496 0.0117 0.0073 7 PHE A CE1 2195 C CE2 . PHE B 21 ? 0.3337 0.3562 0.3908 0.0388 0.0155 0.0124 7 PHE A CE2 2196 C CZ . PHE B 21 ? 0.3354 0.3464 0.3817 0.0492 0.0187 0.0078 7 PHE A CZ 2197 N N . GLU B 22 ? 0.3713 0.3101 0.3558 0.0016 0.0011 0.0397 8 GLU A N 2198 C CA . GLU B 22 ? 0.4188 0.3460 0.3886 -0.0116 0.0059 0.0489 8 GLU A CA 2199 C C . GLU B 22 ? 0.4535 0.3541 0.3961 -0.0093 -0.0019 0.0577 8 GLU A C 2200 O O . GLU B 22 ? 0.4882 0.3630 0.4143 -0.0189 -0.0030 0.0674 8 GLU A O 2201 C CB . GLU B 22 ? 0.4162 0.3665 0.3909 -0.0178 0.0176 0.0479 8 GLU A CB 2202 C CG . GLU B 22 ? 0.3981 0.3693 0.3971 -0.0210 0.0238 0.0417 8 GLU A CG 2203 C CD . GLU B 22 ? 0.3783 0.3597 0.3902 -0.0115 0.0201 0.0328 8 GLU A CD 2204 O OE1 . GLU B 22 ? 0.3712 0.3533 0.3797 -0.0045 0.0158 0.0305 8 GLU A OE1 2205 O OE2 . GLU B 22 ? 0.3652 0.3535 0.3904 -0.0123 0.0208 0.0290 8 GLU A OE2 2206 N N . LYS B 23 ? 0.4690 0.3732 0.4061 0.0025 -0.0097 0.0551 9 LYS A N 2207 C CA . LYS B 23 ? 0.4998 0.3779 0.4067 0.0068 -0.0203 0.0637 9 LYS A CA 2208 C C . LYS B 23 ? 0.5178 0.3642 0.4159 0.0160 -0.0338 0.0670 9 LYS A C 2209 O O . LYS B 23 ? 0.5606 0.3734 0.4278 0.0165 -0.0429 0.0775 9 LYS A O 2210 C CB . LYS B 23 ? 0.5238 0.4161 0.4306 0.0176 -0.0297 0.0583 9 LYS A CB 2211 C CG . LYS B 23 ? 0.5936 0.5033 0.4957 0.0103 -0.0199 0.0550 9 LYS A CG 2212 C CD . LYS B 23 ? 0.7225 0.6106 0.5831 0.0028 -0.0146 0.0657 9 LYS A CD 2213 C CE . LYS B 23 ? 0.7952 0.6962 0.6427 0.0014 -0.0069 0.0597 9 LYS A CE 2214 N NZ . LYS B 23 ? 0.8720 0.7822 0.7274 0.0114 -0.0233 0.0488 9 LYS A NZ 2215 N N . LYS B 24 ? 0.5516 0.4053 0.4723 0.0247 -0.0354 0.0577 10 LYS A N 2216 C CA . LYS B 24 ? 0.5818 0.4025 0.4928 0.0368 -0.0477 0.0573 10 LYS A CA 2217 C C . LYS B 24 ? 0.5578 0.3546 0.4632 0.0235 -0.0441 0.0590 10 LYS A C 2218 O O . LYS B 24 ? 0.5506 0.3167 0.4469 0.0333 -0.0543 0.0555 10 LYS A O 2219 C CB . LYS B 24 ? 0.5746 0.4190 0.5114 0.0587 -0.0515 0.0439 10 LYS A CB 2220 C CG . LYS B 24 ? 0.6289 0.4929 0.5750 0.0734 -0.0617 0.0424 10 LYS A CG 2221 C CD . LYS B 24 ? 0.5827 0.4809 0.5630 0.0924 -0.0615 0.0299 10 LYS A CD 2222 C CE . LYS B 24 ? 0.6705 0.5420 0.6433 0.1142 -0.0707 0.0251 10 LYS A CE 2223 N NZ . LYS B 24 ? 0.6876 0.5980 0.6951 0.1377 -0.0714 0.0138 10 LYS A NZ 2224 N N . SER B 25 ? 0.5221 0.3333 0.4340 0.0023 -0.0313 0.0632 11 SER A N 2225 C CA . SER B 25 ? 0.5282 0.3275 0.4443 -0.0129 -0.0294 0.0634 11 SER A CA 2226 C C . SER B 25 ? 0.5291 0.3282 0.4561 0.0005 -0.0343 0.0491 11 SER A C 2227 O O . SER B 25 ? 0.5466 0.3111 0.4614 -0.0004 -0.0440 0.0469 11 SER A O 2228 C CB . SER B 25 ? 0.6090 0.3599 0.4977 -0.0261 -0.0378 0.0766 11 SER A CB 2229 O OG . SER B 25 ? 0.6402 0.3933 0.5146 -0.0399 -0.0293 0.0910 11 SER A OG 2230 N N . LEU B 26 ? 0.4567 0.2916 0.4028 0.0125 -0.0276 0.0397 12 LEU A N 2231 C CA . LEU B 26 ? 0.4547 0.2949 0.4079 0.0249 -0.0275 0.0271 12 LEU A CA 2232 C C . LEU B 26 ? 0.4319 0.3039 0.4031 0.0152 -0.0172 0.0242 12 LEU A C 2233 O O . LEU B 26 ? 0.4186 0.3183 0.4027 0.0098 -0.0092 0.0276 12 LEU A O 2234 C CB . LEU B 26 ? 0.4416 0.2971 0.4019 0.0482 -0.0275 0.0200 12 LEU A CB 2235 C CG . LEU B 26 ? 0.5564 0.3821 0.5018 0.0668 -0.0402 0.0188 12 LEU A CG 2236 C CD1 . LEU B 26 ? 0.5584 0.4175 0.5244 0.0885 -0.0381 0.0120 12 LEU A CD1 2237 C CD2 . LEU B 26 ? 0.6115 0.3957 0.5360 0.0736 -0.0483 0.0114 12 LEU A CD2 2238 N N . GLU B 27 ? 0.4516 0.3150 0.4197 0.0146 -0.0196 0.0172 13 GLU A N 2239 C CA . GLU B 27 ? 0.4175 0.3044 0.3980 0.0083 -0.0138 0.0142 13 GLU A CA 2240 C C . GLU B 27 ? 0.3961 0.2992 0.3772 0.0236 -0.0066 0.0069 13 GLU A C 2241 O O . GLU B 27 ? 0.4092 0.2998 0.3783 0.0389 -0.0077 0.0003 13 GLU A O 2242 C CB . GLU B 27 ? 0.4706 0.3359 0.4436 -0.0014 -0.0242 0.0110 13 GLU A CB 2243 C CG . GLU B 27 ? 0.5068 0.3910 0.4895 -0.0061 -0.0237 0.0075 13 GLU A CG 2244 C CD . GLU B 27 ? 0.5441 0.4054 0.5184 -0.0141 -0.0390 0.0024 13 GLU A CD 2245 O OE1 . GLU B 27 ? 0.6275 0.4597 0.5935 -0.0223 -0.0495 0.0034 13 GLU A OE1 2246 O OE2 . GLU B 27 ? 0.5295 0.3988 0.5038 -0.0132 -0.0431 -0.0024 13 GLU A OE2 2247 N N . ASP B 28 ? 0.3955 0.3253 0.3894 0.0199 0.0016 0.0083 14 ASP A N 2248 C CA . ASP B 28 ? 0.3716 0.3157 0.3649 0.0297 0.0102 0.0043 14 ASP A CA 2249 C C . ASP B 28 ? 0.4287 0.3582 0.4030 0.0316 0.0078 -0.0012 14 ASP A C 2250 O O . ASP B 28 ? 0.4285 0.3409 0.3963 0.0241 -0.0029 -0.0023 14 ASP A O 2251 C CB . ASP B 28 ? 0.3511 0.3224 0.3619 0.0241 0.0181 0.0090 14 ASP A CB 2252 C CG . ASP B 28 ? 0.3187 0.2925 0.3308 0.0148 0.0174 0.0111 14 ASP A CG 2253 O OD1 . ASP B 28 ? 0.3456 0.3088 0.3448 0.0154 0.0145 0.0088 14 ASP A OD1 2254 O OD2 . ASP B 28 ? 0.3278 0.3130 0.3519 0.0088 0.0186 0.0144 14 ASP A OD2 2255 N N . LYS B 29 A 0.3941 0.3310 0.3590 0.0410 0.0175 -0.0043 14 LYS A N 2256 C CA . LYS B 29 A 0.4106 0.3282 0.3466 0.0469 0.0157 -0.0106 14 LYS A CA 2257 C C . LYS B 29 A 0.4290 0.3393 0.3567 0.0369 0.0072 -0.0083 14 LYS A C 2258 O O . LYS B 29 A 0.4519 0.3393 0.3517 0.0409 -0.0009 -0.0145 14 LYS A O 2259 C CB . LYS B 29 A 0.4479 0.3785 0.3730 0.0598 0.0327 -0.0133 14 LYS A CB 2260 C CG . LYS B 29 A 0.4311 0.3920 0.3741 0.0517 0.0465 -0.0040 14 LYS A CG 2261 C CD . LYS B 29 A 0.4574 0.4345 0.3908 0.0609 0.0660 -0.0048 14 LYS A CD 2262 C CE . LYS B 29 A 0.4647 0.4672 0.4151 0.0472 0.0782 0.0068 14 LYS A CE 2263 N NZ . LYS B 29 A 0.4834 0.5075 0.4278 0.0527 0.1010 0.0082 14 LYS A NZ 2264 N N . THR B 30 B 0.3967 0.3240 0.3457 0.0263 0.0071 -0.0009 14 THR A N 2265 C CA . THR B 30 B 0.4193 0.3413 0.3629 0.0210 -0.0026 0.0007 14 THR A CA 2266 C C . THR B 30 B 0.3784 0.3130 0.3500 0.0114 -0.0106 0.0037 14 THR A C 2267 O O . THR B 30 B 0.3779 0.3129 0.3513 0.0098 -0.0199 0.0043 14 THR A O 2268 C CB . THR B 30 B 0.4206 0.3467 0.3526 0.0222 0.0064 0.0065 14 THR A CB 2269 O OG1 . THR B 30 B 0.4318 0.3776 0.3883 0.0165 0.0146 0.0126 14 THR A OG1 2270 C CG2 . THR B 30 B 0.4905 0.4113 0.3957 0.0307 0.0197 0.0050 14 THR A CG2 2271 N N . GLU B 31 C 0.3660 0.3116 0.3579 0.0067 -0.0069 0.0056 14 GLU A N 2272 C CA . GLU B 31 C 0.3328 0.2954 0.3495 -0.0010 -0.0087 0.0086 14 GLU A CA 2273 C C . GLU B 31 C 0.3298 0.2919 0.3570 -0.0083 -0.0219 0.0066 14 GLU A C 2274 O O . GLU B 31 C 0.3003 0.2824 0.3506 -0.0124 -0.0233 0.0080 14 GLU A O 2275 C CB . GLU B 31 C 0.3499 0.3218 0.3779 -0.0043 -0.0003 0.0121 14 GLU A CB 2276 C CG . GLU B 31 C 0.3974 0.3536 0.4185 -0.0069 -0.0034 0.0124 14 GLU A CG 2277 C CD . GLU B 31 C 0.4372 0.3998 0.4654 -0.0113 0.0025 0.0180 14 GLU A CD 2278 O OE1 . GLU B 31 C 0.4633 0.4382 0.5047 -0.0206 0.0047 0.0218 14 GLU A OE1 2279 O OE2 . GLU B 31 C 0.4106 0.3670 0.4305 -0.0047 0.0047 0.0187 14 GLU A OE2 2280 N N . ARG B 32 D 0.4031 0.3434 0.4147 -0.0098 -0.0321 0.0024 14 ARG A N 2281 C CA . ARG B 32 D 0.3967 0.3337 0.4178 -0.0191 -0.0493 -0.0005 14 ARG A CA 2282 C C . ARG B 32 D 0.4064 0.3517 0.4304 -0.0146 -0.0604 -0.0028 14 ARG A C 2283 O O . ARG B 32 D 0.3830 0.3423 0.4311 -0.0221 -0.0739 -0.0040 14 ARG A O 2284 C CB . ARG B 32 D 0.4721 0.3735 0.4657 -0.0191 -0.0611 -0.0069 14 ARG A CB 2285 C CG . ARG B 32 D 0.4580 0.3531 0.4658 -0.0349 -0.0804 -0.0089 14 ARG A CG 2286 C CD . ARG B 32 D 0.5229 0.3735 0.4982 -0.0346 -0.0942 -0.0168 14 ARG A CD 2287 N NE . ARG B 32 D 0.5001 0.3324 0.4643 -0.0320 -0.0839 -0.0143 14 ARG A NE 2288 C CZ . ARG B 32 D 0.5727 0.3621 0.5104 -0.0309 -0.0952 -0.0205 14 ARG A CZ 2289 N NH1 . ARG B 32 D 0.5923 0.3514 0.5099 -0.0337 -0.1170 -0.0306 14 ARG A NH1 2290 N NH2 . ARG B 32 D 0.5553 0.3285 0.4841 -0.0256 -0.0871 -0.0175 14 ARG A NH2 2291 N N . GLU B 33 E 0.4037 0.3398 0.4033 -0.0027 -0.0558 -0.0027 14 GLU A N 2292 C CA . GLU B 33 E 0.3936 0.3306 0.3888 0.0036 -0.0669 -0.0028 14 GLU A CA 2293 C C . GLU B 33 E 0.3531 0.3213 0.3870 0.0029 -0.0657 -0.0001 14 GLU A C 2294 O O . GLU B 33 E 0.3604 0.3398 0.4111 0.0052 -0.0816 -0.0023 14 GLU A O 2295 C CB . GLU B 33 E 0.4081 0.3282 0.3689 0.0132 -0.0569 0.0006 14 GLU A CB 2296 C CG . GLU B 33 E 0.4710 0.3751 0.4084 0.0204 -0.0719 0.0013 14 GLU A CG 2297 C CD . GLU B 33 E 0.4888 0.3722 0.3861 0.0261 -0.0599 0.0074 14 GLU A CD 2298 O OE1 . GLU B 33 E 0.4810 0.3706 0.3784 0.0240 -0.0393 0.0108 14 GLU A OE1 2299 O OE2 . GLU B 33 E 0.5761 0.4380 0.4422 0.0318 -0.0719 0.0095 14 GLU A OE2 2300 N N . LEU B 34 F 0.3325 0.3148 0.3796 0.0016 -0.0479 0.0034 14 LEU A N 2301 C CA . LEU B 34 F 0.3332 0.3422 0.4103 0.0039 -0.0430 0.0042 14 LEU A CA 2302 C C . LEU B 34 F 0.3291 0.3665 0.4432 -0.0053 -0.0474 0.0027 14 LEU A C 2303 O O . LEU B 34 F 0.3627 0.4246 0.5050 -0.0007 -0.0548 0.0002 14 LEU A O 2304 C CB . LEU B 34 F 0.3300 0.3423 0.4053 0.0038 -0.0244 0.0070 14 LEU A CB 2305 C CG . LEU B 34 F 0.3641 0.3549 0.4110 0.0082 -0.0182 0.0097 14 LEU A CG 2306 C CD1 . LEU B 34 F 0.3563 0.3543 0.4083 0.0075 -0.0053 0.0110 14 LEU A CD1 2307 C CD2 . LEU B 34 F 0.3827 0.3577 0.4134 0.0160 -0.0271 0.0109 14 LEU A CD2 2308 N N . LEU B 35 G 0.3562 0.3901 0.4710 -0.0183 -0.0434 0.0047 14 LEU A N 2309 C CA . LEU B 35 G 0.3627 0.4218 0.5122 -0.0330 -0.0456 0.0062 14 LEU A CA 2310 C C . LEU B 35 G 0.3356 0.4021 0.5028 -0.0363 -0.0688 0.0016 14 LEU A C 2311 O O . LEU B 35 G 0.3080 0.4131 0.5187 -0.0415 -0.0720 0.0013 14 LEU A O 2312 C CB . LEU B 35 G 0.4314 0.4715 0.5683 -0.0471 -0.0404 0.0107 14 LEU A CB 2313 C CG . LEU B 35 G 0.5005 0.5392 0.6253 -0.0442 -0.0202 0.0158 14 LEU A CG 2314 C CD1 . LEU B 35 G 0.5912 0.6041 0.6983 -0.0547 -0.0186 0.0208 14 LEU A CD1 2315 C CD2 . LEU B 35 G 0.5302 0.6059 0.6822 -0.0446 -0.0054 0.0183 14 LEU A CD2 2316 N N . GLU B 36 H 0.3325 0.3647 0.4665 -0.0319 -0.0851 -0.0026 14 GLU A N 2317 C CA . GLU B 36 H 0.3574 0.3901 0.5004 -0.0340 -0.1121 -0.0081 14 GLU A CA 2318 C C . GLU B 36 H 0.3300 0.3867 0.4934 -0.0196 -0.1223 -0.0104 14 GLU A C 2319 O O . GLU B 36 H 0.3272 0.4061 0.5223 -0.0231 -0.1430 -0.0141 14 GLU A O 2320 C CB . GLU B 36 H 0.4261 0.4108 0.5192 -0.0312 -0.1272 -0.0134 14 GLU A CB 2321 C CG . GLU B 36 H 0.5009 0.4643 0.5867 -0.0472 -0.1289 -0.0143 14 GLU A CG 2322 C CD . GLU B 36 H 0.6303 0.5427 0.6609 -0.0403 -0.1389 -0.0217 14 GLU A CD 2323 O OE1 . GLU B 36 H 0.6888 0.5760 0.7092 -0.0507 -0.1433 -0.0240 14 GLU A OE1 2324 O OE2 . GLU B 36 H 0.6386 0.5337 0.6335 -0.0242 -0.1417 -0.0249 14 GLU A OE2 2325 N N . SER B 37 I 0.3112 0.3634 0.4591 -0.0037 -0.1095 -0.0082 14 SER A N 2326 C CA . SER B 37 I 0.2990 0.3669 0.4624 0.0130 -0.1190 -0.0101 14 SER A CA 2327 C C . SER B 37 I 0.2932 0.4164 0.5183 0.0126 -0.1153 -0.0123 14 SER A C 2328 O O . SER B 37 I 0.3436 0.4873 0.5935 0.0259 -0.1311 -0.0164 14 SER A O 2329 C CB . SER B 37 I 0.2916 0.3351 0.4218 0.0271 -0.1061 -0.0067 14 SER A CB 2330 O OG . SER B 37 I 0.2616 0.3221 0.4063 0.0263 -0.0820 -0.0050 14 SER A OG 2331 N N . TYR B 38 J 0.2931 0.4409 0.5420 -0.0017 -0.0946 -0.0093 14 TYR A N 2332 C CA . TYR B 38 J 0.3388 0.5442 0.6462 -0.0046 -0.0858 -0.0104 14 TYR A CA 2333 C C . TYR B 38 J 0.3838 0.6217 0.7366 -0.0201 -0.1050 -0.0119 14 TYR A C 2334 O O . TYR B 38 J 0.3642 0.6568 0.7732 -0.0169 -0.1058 -0.0147 14 TYR A O 2335 C CB . TYR B 38 J 0.3462 0.5631 0.6561 -0.0166 -0.0558 -0.0046 14 TYR A CB 2336 C CG . TYR B 38 J 0.3304 0.5207 0.6018 -0.0039 -0.0382 -0.0039 14 TYR A CG 2337 C CD1 . TYR B 38 J 0.3518 0.5375 0.6155 0.0193 -0.0397 -0.0093 14 TYR A CD1 2338 C CD2 . TYR B 38 J 0.3393 0.5076 0.5828 -0.0152 -0.0223 0.0021 14 TYR A CD2 2339 C CE1 . TYR B 38 J 0.3921 0.5518 0.6221 0.0274 -0.0260 -0.0089 14 TYR A CE1 2340 C CE2 . TYR B 38 J 0.3641 0.5118 0.5771 -0.0054 -0.0092 0.0022 14 TYR A CE2 2341 C CZ . TYR B 38 J 0.3677 0.5112 0.5745 0.0144 -0.0110 -0.0034 14 TYR A CZ 2342 O OH . TYR B 38 J 0.3856 0.5064 0.5630 0.0204 -0.0004 -0.0034 14 TYR A OH 2343 N N . ILE B 39 K 0.4991 0.7047 0.8296 -0.0365 -0.1214 -0.0109 14 ILE A N 2344 C CA . ILE B 39 K 0.6131 0.8416 0.9829 -0.0541 -0.1457 -0.0133 14 ILE A CA 2345 C C . ILE B 39 K 0.7099 0.9474 1.0915 -0.0354 -0.1766 -0.0212 14 ILE A C 2346 O O . ILE B 39 K 0.7135 0.9978 1.1524 -0.0410 -0.1945 -0.0246 14 ILE A O 2347 C CB . ILE B 39 K 0.6666 0.8466 0.9999 -0.0745 -0.1584 -0.0124 14 ILE A CB 2348 C CG1 . ILE B 39 K 0.6745 0.8423 0.9951 -0.0907 -0.1307 -0.0036 14 ILE A CG1 2349 C CG2 . ILE B 39 K 0.6744 0.8730 1.0470 -0.0950 -0.1881 -0.0158 14 ILE A CG2 2350 C CD1 . ILE B 39 K 0.7481 0.8525 1.0128 -0.0974 -0.1382 -0.0044 14 ILE A CD1 2351 N N . ASP B 40 L 0.9606 1.1540 1.2886 -0.0136 -0.1828 -0.0231 14 ASP A N 2352 C CA . ASP B 40 L 1.1858 1.3755 1.5107 0.0079 -0.2117 -0.0284 14 ASP A CA 2353 C C . ASP B 40 L 1.1405 1.3747 1.5081 0.0296 -0.2032 -0.0304 14 ASP A C 2354 O O . ASP B 40 L 1.0774 1.3728 1.5133 0.0286 -0.2086 -0.0341 14 ASP A O 2355 C CB . ASP B 40 L 1.3042 1.4261 1.5497 0.0212 -0.2173 -0.0269 14 ASP A CB 2356 C CG . ASP B 40 L 1.3304 1.4066 1.5278 0.0050 -0.2208 -0.0270 14 ASP A CG 2357 O OD1 . ASP B 40 L 1.2979 1.3846 1.5185 -0.0143 -0.2347 -0.0305 14 ASP A OD1 2358 O OD2 . ASP B 40 L 1.3183 1.3484 1.4557 0.0117 -0.2094 -0.0241 14 ASP A OD2 2359 N N . 0G6 C . ? 0.4982 0.3685 0.4540 -0.0300 -0.0313 0.0667 301 0G6 B N 2360 C CA . 0G6 C . ? 0.4764 0.3358 0.4439 -0.0252 -0.0382 0.0599 301 0G6 B CA 2361 C C . 0G6 C . ? 0.4354 0.3095 0.4120 -0.0228 -0.0326 0.0481 301 0G6 B C 2362 O O . 0G6 C . ? 0.4252 0.3151 0.4013 -0.0184 -0.0276 0.0423 301 0G6 B O 2363 C CB . 0G6 C . ? 0.4788 0.3299 0.4469 -0.0143 -0.0470 0.0575 301 0G6 B CB 2364 C CG . 0G6 C . ? 0.5462 0.3843 0.5253 -0.0065 -0.0529 0.0487 301 0G6 B CG 2365 C CD1 . 0G6 C . ? 0.6501 0.4656 0.6302 -0.0101 -0.0596 0.0522 301 0G6 B CD1 2366 C CD2 . 0G6 C . ? 0.5165 0.3648 0.5035 0.0042 -0.0511 0.0371 301 0G6 B CD2 2367 C CE1 . 0G6 C . ? 0.6970 0.4980 0.6836 -0.0018 -0.0650 0.0423 301 0G6 B CE1 2368 C CE2 . 0G6 C . ? 0.5341 0.3707 0.5273 0.0126 -0.0546 0.0283 301 0G6 B CE2 2369 C CZ . 0G6 C . ? 0.5927 0.4047 0.5846 0.0103 -0.0618 0.0299 301 0G6 B CZ 2370 N N1 . 0G6 C . ? 0.4435 0.3116 0.4288 -0.0263 -0.0343 0.0437 301 0G6 B N1 2371 C CA1 . 0G6 C . ? 0.4418 0.3225 0.4332 -0.0238 -0.0302 0.0329 301 0G6 B CA1 2372 C C1 . 0G6 C . ? 0.4217 0.3221 0.4140 -0.0295 -0.0209 0.0355 301 0G6 B C1 2373 O O1 . 0G6 C . ? 0.4448 0.3482 0.4367 -0.0378 -0.0171 0.0448 301 0G6 B O1 2374 C CB1 . 0G6 C . ? 0.4740 0.3419 0.4704 -0.0273 -0.0362 0.0300 301 0G6 B CB1 2375 C CG1 . 0G6 C . ? 0.4631 0.3068 0.4578 -0.0304 -0.0448 0.0378 301 0G6 B CG1 2376 C CD . 0G6 C . ? 0.4817 0.3292 0.4706 -0.0332 -0.0416 0.0486 301 0G6 B CD 2377 N N2 . 0G6 C . ? 0.4048 0.3197 0.3992 -0.0243 -0.0163 0.0269 301 0G6 B N2 2378 C CA2 . 0G6 C . ? 0.3746 0.3065 0.3714 -0.0277 -0.0082 0.0277 301 0G6 B CA2 2379 C C2 . 0G6 C . ? 0.3843 0.3204 0.3903 -0.0296 -0.0095 0.0227 301 0G6 B C2 2380 O O2 . 0G6 C . ? 0.3865 0.3376 0.3998 -0.0350 -0.0030 0.0268 301 0G6 B O2 2381 C CB2 . 0G6 C . ? 0.3671 0.3082 0.3582 -0.0211 -0.0042 0.0238 301 0G6 B CB2 2382 C CG2 . 0G6 C . ? 0.3950 0.3327 0.3755 -0.0219 -0.0038 0.0305 301 0G6 B CG2 2383 C CD3 . 0G6 C . ? 0.4277 0.3719 0.4037 -0.0161 -0.0031 0.0259 301 0G6 B CD3 2384 N NE . 0G6 C . ? 0.4311 0.3712 0.3942 -0.0174 -0.0042 0.0317 301 0G6 B NE 2385 C CZ1 . 0G6 C . ? 0.3864 0.3297 0.3428 -0.0139 -0.0061 0.0289 301 0G6 B CZ1 2386 N NH1 . 0G6 C . ? 0.3907 0.3425 0.3566 -0.0096 -0.0061 0.0214 301 0G6 B NH1 2387 N NH2 . 0G6 C . ? 0.4149 0.3521 0.3557 -0.0152 -0.0090 0.0341 301 0G6 B NH2 2388 C C3 . 0G6 C . ? 0.3968 0.3170 0.4071 -0.0340 -0.0187 0.0225 301 0G6 B C3 2389 O O1 . MES D . ? 1.7166 1.7208 1.6883 0.2262 0.1587 -0.0999 302 MES B O1 2390 C C2 . MES D . ? 1.7291 1.7188 1.6590 0.2178 0.1595 -0.1031 302 MES B C2 2391 C C3 . MES D . ? 1.7086 1.6742 1.6250 0.1987 0.1357 -0.1020 302 MES B C3 2392 N N4 . MES D . ? 1.6958 1.6557 1.6395 0.1956 0.1200 -0.0995 302 MES B N4 2393 C C5 . MES D . ? 1.6424 1.6339 1.6299 0.1926 0.1227 -0.0863 302 MES B C5 2394 C C6 . MES D . ? 1.6383 1.6582 1.6440 0.2095 0.1455 -0.0857 302 MES B C6 2395 C C7 . MES D . ? 1.6581 1.5801 1.5867 0.1966 0.1015 -0.1101 302 MES B C7 2396 C C8 . MES D . ? 1.5947 1.4865 1.4815 0.1881 0.0910 -0.1186 302 MES B C8 2397 S S . MES D . ? 1.5184 1.4231 1.4033 0.1634 0.0837 -0.1052 302 MES B S 2398 O O1S . MES D . ? 1.2542 1.1969 1.1658 0.1573 0.0958 -0.0901 302 MES B O1S 2399 O O2S . MES D . ? 1.0942 0.9894 0.9941 0.1482 0.0643 -0.0991 302 MES B O2S 2400 O O3S . MES D . ? 1.5796 1.4665 1.4229 0.1617 0.0828 -0.1132 302 MES B O3S 2401 C C1 . GOL E . ? 0.8795 0.7507 0.9225 -0.0538 -0.0046 0.0787 303 GOL B C1 2402 O O1 . GOL E . ? 0.6275 0.5137 0.6618 -0.0433 -0.0002 0.0687 303 GOL B O1 2403 C C2 . GOL E . ? 0.9004 0.7455 0.9442 -0.0541 -0.0161 0.0693 303 GOL B C2 2404 O O2 . GOL E . ? 0.9426 0.7679 0.9760 -0.0445 -0.0196 0.0680 303 GOL B O2 2405 C C3 . GOL E . ? 0.8373 0.6881 0.8791 -0.0498 -0.0183 0.0533 303 GOL B C3 2406 O O3 . GOL E . ? 0.8709 0.7468 0.9220 -0.0553 -0.0133 0.0550 303 GOL B O3 2407 C C1 . GOL F . ? 0.7048 0.7987 0.8744 0.0401 0.0006 0.0197 304 GOL B C1 2408 O O1 . GOL F . ? 0.6230 0.7124 0.7988 0.0482 -0.0084 0.0199 304 GOL B O1 2409 C C2 . GOL F . ? 0.7463 0.8650 0.9461 0.0355 0.0013 0.0262 304 GOL B C2 2410 O O2 . GOL F . ? 0.7203 0.8394 0.9292 0.0281 -0.0157 0.0301 304 GOL B O2 2411 C C3 . GOL F . ? 0.7171 0.8573 0.9446 0.0477 0.0107 0.0278 304 GOL B C3 2412 O O3 . GOL F . ? 0.7319 0.8967 0.9844 0.0426 0.0188 0.0341 304 GOL B O3 2413 NA NA . NA G . ? 0.4775 0.3965 0.3563 -0.0128 -0.0590 0.0271 305 NA B NA 2414 C C1 . NAG H . ? 1.2560 0.8666 1.1886 -0.0623 -0.1946 -0.0827 306 NAG B C1 2415 C C2 . NAG H . ? 1.3128 0.8829 1.2343 -0.0550 -0.2000 -0.0891 306 NAG B C2 2416 C C3 . NAG H . ? 1.3559 0.8825 1.2456 -0.0457 -0.2152 -0.1112 306 NAG B C3 2417 C C4 . NAG H . ? 1.4179 0.9419 1.2981 -0.0550 -0.2314 -0.1196 306 NAG B C4 2418 C C5 . NAG H . ? 1.3908 0.9581 1.2718 -0.0511 -0.2168 -0.1154 306 NAG B C5 2419 C C6 . NAG H . ? 1.3836 0.9479 1.2487 -0.0559 -0.2323 -0.1253 306 NAG B C6 2420 C C7 . NAG H . ? 1.2191 0.7925 1.1500 -0.0389 -0.1775 -0.0764 306 NAG B C7 2421 C C8 . NAG H . ? 1.1350 0.7220 1.0618 -0.0206 -0.1595 -0.0757 306 NAG B C8 2422 N N2 . NAG H . ? 1.2547 0.8354 1.1727 -0.0383 -0.1809 -0.0870 306 NAG B N2 2423 O O3 . NAG H . ? 1.3211 0.8079 1.2132 -0.0501 -0.2288 -0.1121 306 NAG B O3 2424 O O4 . NAG H . ? 1.4913 0.9744 1.3352 -0.0434 -0.2433 -0.1417 306 NAG B O4 2425 O O5 . NAG H . ? 1.3232 0.9269 1.2401 -0.0642 -0.2081 -0.0947 306 NAG B O5 2426 O O6 . NAG H . ? 1.3434 0.9471 1.2115 -0.0523 -0.2188 -0.1193 306 NAG B O6 2427 O O7 . NAG H . ? 1.1953 0.7522 1.1414 -0.0539 -0.1888 -0.0665 306 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 ILE 1 16 16 ILE ILE B . n A 1 2 VAL 2 17 17 VAL VAL B . n A 1 3 GLU 3 18 18 GLU GLU B . n A 1 4 GLY 4 19 19 GLY GLY B . n A 1 5 SER 5 20 20 SER SER B . n A 1 6 ASP 6 21 21 ASP ASP B . n A 1 7 ALA 7 22 22 ALA ALA B . n A 1 8 GLU 8 23 23 GLU GLU B . n A 1 9 ILE 9 24 24 ILE ILE B . n A 1 10 GLY 10 25 25 GLY GLY B . n A 1 11 MET 11 26 26 MET MET B . n A 1 12 SER 12 27 27 SER SER B . n A 1 13 PRO 13 28 28 PRO PRO B . n A 1 14 TRP 14 29 29 TRP TRP B . n A 1 15 GLN 15 30 30 GLN GLN B . n A 1 16 VAL 16 31 31 VAL VAL B . n A 1 17 MET 17 32 32 MET MET B . n A 1 18 LEU 18 33 33 LEU LEU B . n A 1 19 PHE 19 34 34 PHE PHE B . n A 1 20 ARG 20 35 35 ARG ARG B . n A 1 21 LYS 21 36 36 LYS LYS B . n A 1 22 SER 22 36 36 SER SER B A n A 1 23 PRO 23 37 37 PRO PRO B . n A 1 24 GLN 24 38 38 GLN GLN B . n A 1 25 GLU 25 39 39 GLU GLU B . n A 1 26 LEU 26 40 40 LEU LEU B . n A 1 27 LEU 27 41 41 LEU LEU B . n A 1 28 CYS 28 42 42 CYS CYS B . n A 1 29 GLY 29 43 43 GLY GLY B . n A 1 30 ALA 30 44 44 ALA ALA B . n A 1 31 SER 31 45 45 SER SER B . n A 1 32 LEU 32 46 46 LEU LEU B . n A 1 33 ILE 33 47 47 ILE ILE B . n A 1 34 SER 34 48 48 SER SER B . n A 1 35 ASP 35 49 49 ASP ASP B . n A 1 36 ARG 36 50 50 ARG ARG B . n A 1 37 TRP 37 51 51 TRP TRP B . n A 1 38 VAL 38 52 52 VAL VAL B . n A 1 39 LEU 39 53 53 LEU LEU B . n A 1 40 THR 40 54 54 THR THR B . n A 1 41 ALA 41 55 55 ALA ALA B . n A 1 42 ALA 42 56 56 ALA ALA B . n A 1 43 HIS 43 57 57 HIS HIS B . n A 1 44 CYS 44 58 58 CYS CYS B . n A 1 45 LEU 45 59 59 LEU LEU B . n A 1 46 LEU 46 60 60 LEU LEU B . n A 1 47 TYR 47 60 60 TYR TYR B A n A 1 48 PRO 48 60 60 PRO PRO B B n A 1 49 PRO 49 60 60 PRO PRO B C n A 1 50 TRP 50 60 60 TRP TRP B D n A 1 51 ASP 51 60 60 ASP ASP B E n A 1 52 LYS 52 60 60 LYS LYS B F n A 1 53 ASN 53 60 60 ASN ASN B G n A 1 54 PHE 54 60 60 PHE PHE B H n A 1 55 THR 55 60 60 THR THR B I n A 1 56 GLU 56 61 61 GLU GLU B . n A 1 57 ASN 57 62 62 ASN ASN B . n A 1 58 ASP 58 63 63 ASP ASP B . n A 1 59 LEU 59 64 64 LEU LEU B . n A 1 60 LEU 60 65 65 LEU LEU B . n A 1 61 VAL 61 66 66 VAL VAL B . n A 1 62 ARG 62 67 67 ARG ARG B . n A 1 63 ILE 63 68 68 ILE ILE B . n A 1 64 GLY 64 69 69 GLY GLY B . n A 1 65 LYS 65 70 70 LYS LYS B . n A 1 66 HIS 66 71 71 HIS HIS B . n A 1 67 SER 67 72 72 SER SER B . n A 1 68 ARG 68 73 73 ARG ARG B . n A 1 69 THR 69 74 74 THR THR B . n A 1 70 ARG 70 75 75 ARG ARG B . n A 1 71 TYR 71 76 76 TYR TYR B . n A 1 72 GLU 72 77 77 GLU GLU B . n A 1 73 ARG 73 77 77 ARG ARG B A n A 1 74 ASN 74 78 78 ASN ASN B . n A 1 75 ILE 75 79 79 ILE ILE B . n A 1 76 GLU 76 80 80 GLU GLU B . n A 1 77 LYS 77 81 81 LYS LYS B . n A 1 78 ILE 78 82 82 ILE ILE B . n A 1 79 SER 79 83 83 SER SER B . n A 1 80 MET 80 84 84 MET MET B . n A 1 81 LEU 81 85 85 LEU LEU B . n A 1 82 GLU 82 86 86 GLU GLU B . n A 1 83 LYS 83 87 87 LYS LYS B . n A 1 84 ILE 84 88 88 ILE ILE B . n A 1 85 TYR 85 89 89 TYR TYR B . n A 1 86 ILE 86 90 90 ILE ILE B . n A 1 87 HIS 87 91 91 HIS HIS B . n A 1 88 PRO 88 92 92 PRO PRO B . n A 1 89 ARG 89 93 93 ARG ARG B . n A 1 90 TYR 90 94 94 TYR TYR B . n A 1 91 ASN 91 95 95 ASN ASN B . n A 1 92 TRP 92 96 96 TRP TRP B . n A 1 93 ARG 93 97 97 ARG ARG B . n A 1 94 GLU 94 97 97 GLU GLU B A n A 1 95 ASN 95 98 98 ASN ASN B . n A 1 96 LEU 96 99 99 LEU LEU B . n A 1 97 ASP 97 100 100 ASP ASP B . n A 1 98 ARG 98 101 101 ARG ARG B . n A 1 99 ASP 99 102 102 ASP ASP B . n A 1 100 ILE 100 103 103 ILE ILE B . n A 1 101 ALA 101 104 104 ALA ALA B . n A 1 102 LEU 102 105 105 LEU LEU B . n A 1 103 MET 103 106 106 MET MET B . n A 1 104 LYS 104 107 107 LYS LYS B . n A 1 105 LEU 105 108 108 LEU LEU B . n A 1 106 LYS 106 109 109 LYS LYS B . n A 1 107 LYS 107 110 110 LYS LYS B . n A 1 108 PRO 108 111 111 PRO PRO B . n A 1 109 VAL 109 112 112 VAL VAL B . n A 1 110 ALA 110 113 113 ALA ALA B . n A 1 111 PHE 111 114 114 PHE PHE B . n A 1 112 SER 112 115 115 SER SER B . n A 1 113 ASP 113 116 116 ASP ASP B . n A 1 114 TYR 114 117 117 TYR TYR B . n A 1 115 ILE 115 118 118 ILE ILE B . n A 1 116 HIS 116 119 119 HIS HIS B . n A 1 117 PRO 117 120 120 PRO PRO B . n A 1 118 VAL 118 121 121 VAL VAL B . n A 1 119 CYS 119 122 122 CYS CYS B . n A 1 120 LEU 120 123 123 LEU LEU B . n A 1 121 PRO 121 124 124 PRO PRO B . n A 1 122 ASP 122 125 125 ASP ASP B . n A 1 123 ARG 123 126 126 ARG ARG B . n A 1 124 GLU 124 127 127 GLU GLU B . n A 1 125 THR 125 128 128 THR THR B . n A 1 126 ALA 126 129 129 ALA ALA B . n A 1 127 ALA 127 129 129 ALA ALA B A n A 1 128 SER 128 129 129 SER SER B B n A 1 129 LEU 129 129 129 LEU LEU B C n A 1 130 LEU 130 130 130 LEU LEU B . n A 1 131 GLN 131 131 131 GLN GLN B . n A 1 132 ALA 132 132 132 ALA ALA B . n A 1 133 GLY 133 133 133 GLY GLY B . n A 1 134 TYR 134 134 134 TYR TYR B . n A 1 135 LYS 135 135 135 LYS LYS B . n A 1 136 GLY 136 136 136 GLY GLY B . n A 1 137 ARG 137 137 137 ARG ARG B . n A 1 138 VAL 138 138 138 VAL VAL B . n A 1 139 THR 139 139 139 THR THR B . n A 1 140 GLY 140 140 140 GLY GLY B . n A 1 141 TRP 141 141 141 TRP TRP B . n A 1 142 GLY 142 142 142 GLY GLY B . n A 1 143 ASN 143 143 143 ASN ASN B . n A 1 144 LEU 144 144 144 LEU LEU B . n A 1 145 LYS 145 145 145 LYS LYS B . n A 1 146 GLU 146 146 146 GLU GLU B . n A 1 147 THR 147 147 147 THR THR B . n A 1 148 TRP 148 148 ? ? ? B . n A 1 149 THR 149 149 ? ? ? B . n A 1 150 ALA 150 149 ? ? ? B A n A 1 151 ASN 151 149 ? ? ? B B n A 1 152 VAL 152 149 ? ? ? B C n A 1 153 GLY 153 149 ? ? ? B D n A 1 154 LYS 154 149 ? ? ? B E n A 1 155 GLY 155 150 150 GLY GLY B . n A 1 156 GLN 156 151 151 GLN GLN B . n A 1 157 PRO 157 152 152 PRO PRO B . n A 1 158 SER 158 153 153 SER SER B . n A 1 159 VAL 159 154 154 VAL VAL B . n A 1 160 LEU 160 155 155 LEU LEU B . n A 1 161 GLN 161 156 156 GLN GLN B . n A 1 162 VAL 162 157 157 VAL VAL B . n A 1 163 VAL 163 158 158 VAL VAL B . n A 1 164 ASN 164 159 159 ASN ASN B . n A 1 165 LEU 165 160 160 LEU LEU B . n A 1 166 PRO 166 161 161 PRO PRO B . n A 1 167 ILE 167 162 162 ILE ILE B . n A 1 168 VAL 168 163 163 VAL VAL B . n A 1 169 GLU 169 164 164 GLU GLU B . n A 1 170 ARG 170 165 165 ARG ARG B . n A 1 171 PRO 171 166 166 PRO PRO B . n A 1 172 VAL 172 167 167 VAL VAL B . n A 1 173 CYS 173 168 168 CYS CYS B . n A 1 174 LYS 174 169 169 LYS LYS B . n A 1 175 ASP 175 170 170 ASP ASP B . n A 1 176 SER 176 171 171 SER SER B . n A 1 177 THR 177 172 172 THR THR B . n A 1 178 ARG 178 173 173 ARG ARG B . n A 1 179 ILE 179 174 174 ILE ILE B . n A 1 180 ARG 180 175 175 ARG ARG B . n A 1 181 ILE 181 176 176 ILE ILE B . n A 1 182 THR 182 177 177 THR THR B . n A 1 183 ASP 183 178 178 ASP ASP B . n A 1 184 ASN 184 179 179 ASN ASN B . n A 1 185 MET 185 180 180 MET MET B . n A 1 186 PHE 186 181 181 PHE PHE B . n A 1 187 CYS 187 182 182 CYS CYS B . n A 1 188 ALA 188 183 183 ALA ALA B . n A 1 189 GLY 189 184 184 GLY GLY B . n A 1 190 TYR 190 184 184 TYR TYR B A n A 1 191 LYS 191 185 185 LYS LYS B . n A 1 192 PRO 192 186 186 PRO PRO B . n A 1 193 ASP 193 186 186 ASP ASP B A n A 1 194 GLU 194 186 186 GLU GLU B B n A 1 195 GLY 195 186 186 GLY GLY B C n A 1 196 LYS 196 186 186 LYS LYS B D n A 1 197 ARG 197 187 187 ARG ARG B . n A 1 198 GLY 198 188 188 GLY GLY B . n A 1 199 ASP 199 189 189 ASP ASP B . n A 1 200 ALA 200 190 190 ALA ALA B . n A 1 201 CYS 201 191 191 CYS CYS B . n A 1 202 GLU 202 192 192 GLU GLU B . n A 1 203 GLY 203 193 193 GLY GLY B . n A 1 204 ASP 204 194 194 ASP ASP B . n A 1 205 THR 205 195 195 THR THR B . n A 1 206 GLY 206 196 196 GLY GLY B . n A 1 207 GLY 207 197 197 GLY GLY B . n A 1 208 PRO 208 198 198 PRO PRO B . n A 1 209 PHE 209 199 199 PHE PHE B . n A 1 210 VAL 210 200 200 VAL VAL B . n A 1 211 MET 211 201 201 MET MET B . n A 1 212 LYS 212 202 202 LYS LYS B . n A 1 213 SER 213 203 203 SER SER B . n A 1 214 PRO 214 204 204 PRO PRO B . n A 1 215 PHE 215 204 204 PHE PHE B A n A 1 216 ASN 216 204 204 ASN ASN B B n A 1 217 ASN 217 205 205 ASN ASN B . n A 1 218 ARG 218 206 206 ARG ARG B . n A 1 219 TRP 219 207 207 TRP TRP B . n A 1 220 TYR 220 208 208 TYR TYR B . n A 1 221 GLN 221 209 209 GLN GLN B . n A 1 222 MET 222 210 210 MET MET B . n A 1 223 GLY 223 211 211 GLY GLY B . n A 1 224 ILE 224 212 212 ILE ILE B . n A 1 225 VAL 225 213 213 VAL VAL B . n A 1 226 SER 226 214 214 SER SER B . n A 1 227 TRP 227 215 215 TRP TRP B . n A 1 228 GLY 228 216 216 GLY GLY B . n A 1 229 GLU 229 217 217 GLU GLU B . n A 1 230 GLY 230 219 219 GLY GLY B . n A 1 231 CYS 231 220 220 CYS CYS B . n A 1 232 ASP 232 221 221 ASP ASP B . n A 1 233 ARG 233 221 221 ARG ARG B A n A 1 234 ASP 234 222 222 ASP ASP B . n A 1 235 GLY 235 223 223 GLY GLY B . n A 1 236 LYS 236 224 224 LYS LYS B . n A 1 237 TYR 237 225 225 TYR TYR B . n A 1 238 GLY 238 226 226 GLY GLY B . n A 1 239 PHE 239 227 227 PHE PHE B . n A 1 240 TYR 240 228 228 TYR TYR B . n A 1 241 THR 241 229 229 THR THR B . n A 1 242 HIS 242 230 230 HIS HIS B . n A 1 243 VAL 243 231 231 VAL VAL B . n A 1 244 PHE 244 232 232 PHE PHE B . n A 1 245 ARG 245 233 233 ARG ARG B . n A 1 246 LEU 246 234 234 LEU LEU B . n A 1 247 LYS 247 235 235 LYS LYS B . n A 1 248 LYS 248 236 236 LYS LYS B . n A 1 249 TRP 249 237 237 TRP TRP B . n A 1 250 ILE 250 238 238 ILE ILE B . n A 1 251 GLN 251 239 239 GLN GLN B . n A 1 252 LYS 252 240 240 LYS LYS B . n A 1 253 VAL 253 241 241 VAL VAL B . n A 1 254 ILE 254 242 242 ILE ILE B . n A 1 255 ASP 255 243 243 ASP ASP B . n A 1 256 GLN 256 244 244 GLN GLN B . n A 1 257 PHE 257 245 245 PHE PHE B . n A 1 258 GLY 258 246 ? ? ? B . n A 1 259 GLU 259 247 ? ? ? B . n B 2 1 THR 1 1 1 THR THR A N n B 2 2 PHE 2 1 1 PHE PHE A M n B 2 3 PHE 3 1 1 PHE PHE A L n B 2 4 ASN 4 1 1 ASN ASN A K n B 2 5 PRO 5 1 1 PRO PRO A J n B 2 6 ARG 6 1 1 ARG ARG A I n B 2 7 THR 7 1 1 THR THR A H n B 2 8 PHE 8 1 1 PHE PHE A G n B 2 9 GLY 9 1 1 GLY GLY A F n B 2 10 SER 10 1 1 SER SER A E n B 2 11 GLY 11 1 1 GLY GLY A D n B 2 12 GLU 12 1 1 GLU GLU A C n B 2 13 ALA 13 1 1 ALA ALA A B n B 2 14 ASP 14 1 1 ASP ASP A A n B 2 15 CYS 15 1 1 CYS CYS A . n B 2 16 GLY 16 2 2 GLY GLY A . n B 2 17 LEU 17 3 3 LEU LEU A . n B 2 18 ARG 18 4 4 ARG ARG A . n B 2 19 PRO 19 5 5 PRO PRO A . n B 2 20 LEU 20 6 6 LEU LEU A . n B 2 21 PHE 21 7 7 PHE PHE A . n B 2 22 GLU 22 8 8 GLU GLU A . n B 2 23 LYS 23 9 9 LYS LYS A . n B 2 24 LYS 24 10 10 LYS LYS A . n B 2 25 SER 25 11 11 SER SER A . n B 2 26 LEU 26 12 12 LEU LEU A . n B 2 27 GLU 27 13 13 GLU GLU A . n B 2 28 ASP 28 14 14 ASP ASP A . n B 2 29 LYS 29 14 14 LYS LYS A A n B 2 30 THR 30 14 14 THR THR A B n B 2 31 GLU 31 14 14 GLU GLU A C n B 2 32 ARG 32 14 14 ARG ARG A D n B 2 33 GLU 33 14 14 GLU GLU A E n B 2 34 LEU 34 14 14 LEU LEU A F n B 2 35 LEU 35 14 14 LEU LEU A G n B 2 36 GLU 36 14 14 GLU GLU A H n B 2 37 SER 37 14 14 SER SER A I n B 2 38 TYR 38 14 14 TYR TYR A J n B 2 39 ILE 39 14 14 ILE ILE A K n B 2 40 ASP 40 14 14 ASP ASP A L n B 2 41 GLY 41 14 ? ? ? A M n B 2 42 ARG 42 15 ? ? ? A . n # _pdbx_molecule_features.prd_id PRD_000020 _pdbx_molecule_features.name D-Phe-Pro-Arg-CH2Cl _pdbx_molecule_features.type Peptide-like _pdbx_molecule_features.class Inhibitor _pdbx_molecule_features.details ? # _pdbx_molecule.instance_id 1 _pdbx_molecule.prd_id PRD_000020 _pdbx_molecule.asym_id C # _pdbx_struct_mod_residue.id 1 _pdbx_struct_mod_residue.label_asym_id A _pdbx_struct_mod_residue.label_comp_id ASN _pdbx_struct_mod_residue.label_seq_id 53 _pdbx_struct_mod_residue.auth_asym_id B _pdbx_struct_mod_residue.auth_comp_id ASN _pdbx_struct_mod_residue.auth_seq_id 60 _pdbx_struct_mod_residue.PDB_ins_code G _pdbx_struct_mod_residue.parent_comp_id ASN _pdbx_struct_mod_residue.details 'GLYCOSYLATION SITE' # _pdbx_struct_assembly.id 1 _pdbx_struct_assembly.details author_and_software_defined_assembly _pdbx_struct_assembly.method_details PISA _pdbx_struct_assembly.oligomeric_details dimeric _pdbx_struct_assembly.oligomeric_count 2 # _pdbx_struct_assembly_gen.assembly_id 1 _pdbx_struct_assembly_gen.oper_expression 1 _pdbx_struct_assembly_gen.asym_id_list A,B,C,D,E,F,G,H,I,J # 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)' 4360 ? 1 MORE -21 ? 1 'SSA (A^2)' 12880 ? # _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_struct_conn_angle.id _pdbx_struct_conn_angle.ptnr1_label_atom_id _pdbx_struct_conn_angle.ptnr1_label_alt_id _pdbx_struct_conn_angle.ptnr1_label_asym_id _pdbx_struct_conn_angle.ptnr1_label_comp_id _pdbx_struct_conn_angle.ptnr1_label_seq_id _pdbx_struct_conn_angle.ptnr1_auth_atom_id _pdbx_struct_conn_angle.ptnr1_auth_asym_id _pdbx_struct_conn_angle.ptnr1_auth_comp_id _pdbx_struct_conn_angle.ptnr1_auth_seq_id _pdbx_struct_conn_angle.ptnr1_PDB_ins_code _pdbx_struct_conn_angle.ptnr1_symmetry _pdbx_struct_conn_angle.ptnr2_label_atom_id _pdbx_struct_conn_angle.ptnr2_label_alt_id _pdbx_struct_conn_angle.ptnr2_label_asym_id _pdbx_struct_conn_angle.ptnr2_label_comp_id _pdbx_struct_conn_angle.ptnr2_label_seq_id _pdbx_struct_conn_angle.ptnr2_auth_atom_id _pdbx_struct_conn_angle.ptnr2_auth_asym_id _pdbx_struct_conn_angle.ptnr2_auth_comp_id _pdbx_struct_conn_angle.ptnr2_auth_seq_id _pdbx_struct_conn_angle.ptnr2_PDB_ins_code _pdbx_struct_conn_angle.ptnr2_symmetry _pdbx_struct_conn_angle.ptnr3_label_atom_id _pdbx_struct_conn_angle.ptnr3_label_alt_id _pdbx_struct_conn_angle.ptnr3_label_asym_id _pdbx_struct_conn_angle.ptnr3_label_comp_id _pdbx_struct_conn_angle.ptnr3_label_seq_id _pdbx_struct_conn_angle.ptnr3_auth_atom_id _pdbx_struct_conn_angle.ptnr3_auth_asym_id _pdbx_struct_conn_angle.ptnr3_auth_comp_id _pdbx_struct_conn_angle.ptnr3_auth_seq_id _pdbx_struct_conn_angle.ptnr3_PDB_ins_code _pdbx_struct_conn_angle.ptnr3_symmetry _pdbx_struct_conn_angle.value _pdbx_struct_conn_angle.value_esd 1 O ? A ARG 233 ? B ARG 221 A 1_555 NA ? G NA . ? B NA 305 ? 1_555 O ? A LYS 236 ? B LYS 224 ? 1_555 96.0 ? 2 O ? A ARG 233 ? B ARG 221 A 1_555 NA ? G NA . ? B NA 305 ? 1_555 O ? I HOH . ? B HOH 465 ? 1_555 101.7 ? 3 O ? A LYS 236 ? B LYS 224 ? 1_555 NA ? G NA . ? B NA 305 ? 1_555 O ? I HOH . ? B HOH 465 ? 1_555 162.1 ? 4 O ? A ARG 233 ? B ARG 221 A 1_555 NA ? G NA . ? B NA 305 ? 1_555 O ? I HOH . ? B HOH 464 ? 1_555 161.9 ? 5 O ? A LYS 236 ? B LYS 224 ? 1_555 NA ? G NA . ? B NA 305 ? 1_555 O ? I HOH . ? B HOH 464 ? 1_555 70.5 ? 6 O ? I HOH . ? B HOH 465 ? 1_555 NA ? G NA . ? B NA 305 ? 1_555 O ? I HOH . ? B HOH 464 ? 1_555 91.6 ? 7 O ? A ARG 233 ? B ARG 221 A 1_555 NA ? G NA . ? B NA 305 ? 1_555 O ? I HOH . ? B HOH 463 ? 1_555 97.6 ? 8 O ? A LYS 236 ? B LYS 224 ? 1_555 NA ? G NA . ? B NA 305 ? 1_555 O ? I HOH . ? B HOH 463 ? 1_555 82.5 ? 9 O ? I HOH . ? B HOH 465 ? 1_555 NA ? G NA . ? B NA 305 ? 1_555 O ? I HOH . ? B HOH 463 ? 1_555 97.9 ? 10 O ? I HOH . ? B HOH 464 ? 1_555 NA ? G NA . ? B NA 305 ? 1_555 O ? I HOH . ? B HOH 463 ? 1_555 92.5 ? 11 O ? A ARG 233 ? B ARG 221 A 1_555 NA ? G NA . ? B NA 305 ? 1_555 O ? I HOH . ? B HOH 448 ? 1_555 86.8 ? 12 O ? A LYS 236 ? B LYS 224 ? 1_555 NA ? G NA . ? B NA 305 ? 1_555 O ? I HOH . ? B HOH 448 ? 1_555 95.6 ? 13 O ? I HOH . ? B HOH 465 ? 1_555 NA ? G NA . ? B NA 305 ? 1_555 O ? I HOH . ? B HOH 448 ? 1_555 82.5 ? 14 O ? I HOH . ? B HOH 464 ? 1_555 NA ? G NA . ? B NA 305 ? 1_555 O ? I HOH . ? B HOH 448 ? 1_555 82.8 ? 15 O ? I HOH . ? B HOH 463 ? 1_555 NA ? G NA . ? B NA 305 ? 1_555 O ? I HOH . ? B HOH 448 ? 1_555 175.3 ? # _pdbx_audit_revision_history.ordinal 1 _pdbx_audit_revision_history.data_content_type 'Structure model' _pdbx_audit_revision_history.major_revision 1 _pdbx_audit_revision_history.minor_revision 0 _pdbx_audit_revision_history.revision_date 2015-03-11 # _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_refine_tls.pdbx_refine_id _pdbx_refine_tls.id _pdbx_refine_tls.details _pdbx_refine_tls.method _pdbx_refine_tls.origin_x _pdbx_refine_tls.origin_y _pdbx_refine_tls.origin_z _pdbx_refine_tls.T[1][1] _pdbx_refine_tls.T[2][2] _pdbx_refine_tls.T[3][3] _pdbx_refine_tls.T[1][2] _pdbx_refine_tls.T[1][3] _pdbx_refine_tls.T[2][3] _pdbx_refine_tls.L[1][1] _pdbx_refine_tls.L[2][2] _pdbx_refine_tls.L[3][3] _pdbx_refine_tls.L[1][2] _pdbx_refine_tls.L[1][3] _pdbx_refine_tls.L[2][3] _pdbx_refine_tls.S[1][1] _pdbx_refine_tls.S[1][2] _pdbx_refine_tls.S[1][3] _pdbx_refine_tls.S[2][1] _pdbx_refine_tls.S[2][2] _pdbx_refine_tls.S[2][3] _pdbx_refine_tls.S[3][1] _pdbx_refine_tls.S[3][2] _pdbx_refine_tls.S[3][3] 'X-RAY DIFFRACTION' 1 ? refined 16.6380 12.9070 7.5840 0.0448 0.0579 0.0555 0.0012 0.0317 0.0188 2.6302 4.6190 4.7642 -0.3909 1.2917 0.1828 0.0129 0.3551 0.0171 -0.4206 0.0087 -0.1660 -0.0873 0.2654 -0.0215 'X-RAY DIFFRACTION' 2 ? refined 12.8220 -2.0050 13.2350 0.0359 0.0066 0.0277 0.0032 -0.0000 -0.0095 1.8654 2.6468 1.9595 -0.2501 0.6172 -0.4986 0.1096 0.1021 -0.1623 -0.1444 -0.0354 0.0380 0.2019 0.0019 -0.0741 # loop_ _pdbx_refine_tls_group.pdbx_refine_id _pdbx_refine_tls_group.id _pdbx_refine_tls_group.refine_tls_id _pdbx_refine_tls_group.beg_auth_asym_id _pdbx_refine_tls_group.beg_auth_seq_id _pdbx_refine_tls_group.end_auth_asym_id _pdbx_refine_tls_group.end_auth_seq_id _pdbx_refine_tls_group.selection_details _pdbx_refine_tls_group.beg_label_asym_id _pdbx_refine_tls_group.beg_label_seq_id _pdbx_refine_tls_group.end_label_asym_id _pdbx_refine_tls_group.end_label_seq_id _pdbx_refine_tls_group.selection 'X-RAY DIFFRACTION' 1 1 A 1 A 14 ? . . . . ? 'X-RAY DIFFRACTION' 2 2 B 16 B 245 ? . . . . ? 'X-RAY DIFFRACTION' 3 2 B 301 B 306 ? . . . . ? # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal CrystalClear 'data collection' . ? 1 MOLREP phasing 'from ccp4' ? 2 REFMAC refinement 5.8.0073 ? 3 HKL-2000 'data reduction' . ? 4 HKL-2000 'data scaling' . ? 5 # loop_ _pdbx_validate_torsion.id _pdbx_validate_torsion.PDB_model_num _pdbx_validate_torsion.auth_comp_id _pdbx_validate_torsion.auth_asym_id _pdbx_validate_torsion.auth_seq_id _pdbx_validate_torsion.PDB_ins_code _pdbx_validate_torsion.label_alt_id _pdbx_validate_torsion.phi _pdbx_validate_torsion.psi 1 1 CYS B 42 ? ? -174.25 -175.82 2 1 TYR B 60 A ? -155.08 86.09 3 1 ASN B 60 G ? -151.33 71.87 4 1 HIS B 71 ? ? -126.89 -60.03 5 1 ILE B 79 ? ? -123.57 -58.45 6 1 PHE A 7 ? ? -125.00 -89.76 # 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 B TRP 148 ? A TRP 148 2 1 Y 1 B THR 149 ? A THR 149 3 1 Y 1 B ALA 149 A A ALA 150 4 1 Y 1 B ASN 149 B A ASN 151 5 1 Y 1 B VAL 149 C A VAL 152 6 1 Y 1 B GLY 149 D A GLY 153 7 1 Y 1 B LYS 149 E A LYS 154 8 1 Y 1 B GLY 246 ? A GLY 258 9 1 Y 1 B GLU 247 ? A GLU 259 10 1 Y 1 A GLY 14 M B GLY 41 11 1 Y 1 A ARG 15 ? B ARG 42 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 3 'D-phenylalanyl-N-[(2S,3S)-6-{[amino(iminio)methyl]amino}-1-chloro-2-hydroxyhexan-3-yl]-L-prolinamide' 0G6 4 '2-(N-MORPHOLINO)-ETHANESULFONIC ACID' MES 5 GLYCEROL GOL 6 'SODIUM ION' NA 7 N-ACETYL-D-GLUCOSAMINE NAG 8 water HOH # loop_ _pdbx_nonpoly_scheme.asym_id _pdbx_nonpoly_scheme.entity_id _pdbx_nonpoly_scheme.mon_id _pdbx_nonpoly_scheme.ndb_seq_num _pdbx_nonpoly_scheme.pdb_seq_num _pdbx_nonpoly_scheme.auth_seq_num _pdbx_nonpoly_scheme.pdb_mon_id _pdbx_nonpoly_scheme.auth_mon_id _pdbx_nonpoly_scheme.pdb_strand_id _pdbx_nonpoly_scheme.pdb_ins_code C 3 0G6 1 301 301 0G6 0G6 B . D 4 MES 1 302 302 MES MES B . E 5 GOL 1 303 303 GOL GOL B . F 5 GOL 1 304 304 GOL GOL B . G 6 NA 1 305 401 NA NA B . H 7 NAG 1 306 701 NAG NAG B . I 8 HOH 1 401 1 HOH HOH B . I 8 HOH 2 402 2 HOH HOH B . I 8 HOH 3 403 3 HOH HOH B . I 8 HOH 4 404 4 HOH HOH B . I 8 HOH 5 405 5 HOH HOH B . I 8 HOH 6 406 6 HOH HOH B . I 8 HOH 7 407 7 HOH HOH B . I 8 HOH 8 408 8 HOH HOH B . I 8 HOH 9 409 9 HOH HOH B . I 8 HOH 10 410 10 HOH HOH B . I 8 HOH 11 411 11 HOH HOH B . I 8 HOH 12 412 12 HOH HOH B . I 8 HOH 13 413 13 HOH HOH B . I 8 HOH 14 414 14 HOH HOH B . I 8 HOH 15 415 15 HOH HOH B . I 8 HOH 16 416 16 HOH HOH B . I 8 HOH 17 417 17 HOH HOH B . I 8 HOH 18 418 18 HOH HOH B . I 8 HOH 19 419 19 HOH HOH B . I 8 HOH 20 420 22 HOH HOH B . I 8 HOH 21 421 23 HOH HOH B . I 8 HOH 22 422 24 HOH HOH B . I 8 HOH 23 423 25 HOH HOH B . I 8 HOH 24 424 27 HOH HOH B . I 8 HOH 25 425 28 HOH HOH B . I 8 HOH 26 426 29 HOH HOH B . I 8 HOH 27 427 30 HOH HOH B . I 8 HOH 28 428 31 HOH HOH B . I 8 HOH 29 429 33 HOH HOH B . I 8 HOH 30 430 35 HOH HOH B . I 8 HOH 31 431 36 HOH HOH B . I 8 HOH 32 432 37 HOH HOH B . I 8 HOH 33 433 39 HOH HOH B . I 8 HOH 34 434 40 HOH HOH B . I 8 HOH 35 435 41 HOH HOH B . I 8 HOH 36 436 42 HOH HOH B . I 8 HOH 37 437 43 HOH HOH B . I 8 HOH 38 438 46 HOH HOH B . I 8 HOH 39 439 47 HOH HOH B . I 8 HOH 40 440 48 HOH HOH B . I 8 HOH 41 441 51 HOH HOH B . I 8 HOH 42 442 52 HOH HOH B . I 8 HOH 43 443 54 HOH HOH B . I 8 HOH 44 444 55 HOH HOH B . I 8 HOH 45 445 56 HOH HOH B . I 8 HOH 46 446 57 HOH HOH B . I 8 HOH 47 447 58 HOH HOH B . I 8 HOH 48 448 59 HOH HOH B . I 8 HOH 49 449 60 HOH HOH B . I 8 HOH 50 450 61 HOH HOH B . I 8 HOH 51 451 62 HOH HOH B . I 8 HOH 52 452 63 HOH HOH B . I 8 HOH 53 453 64 HOH HOH B . I 8 HOH 54 454 65 HOH HOH B . I 8 HOH 55 455 66 HOH HOH B . I 8 HOH 56 456 67 HOH HOH B . I 8 HOH 57 457 69 HOH HOH B . I 8 HOH 58 458 70 HOH HOH B . I 8 HOH 59 459 71 HOH HOH B . I 8 HOH 60 460 72 HOH HOH B . I 8 HOH 61 461 73 HOH HOH B . I 8 HOH 62 462 74 HOH HOH B . I 8 HOH 63 463 75 HOH HOH B . I 8 HOH 64 464 76 HOH HOH B . I 8 HOH 65 465 77 HOH HOH B . I 8 HOH 66 466 78 HOH HOH B . I 8 HOH 67 467 79 HOH HOH B . I 8 HOH 68 468 80 HOH HOH B . I 8 HOH 69 469 81 HOH HOH B . I 8 HOH 70 470 84 HOH HOH B . I 8 HOH 71 471 85 HOH HOH B . I 8 HOH 72 472 86 HOH HOH B . I 8 HOH 73 473 87 HOH HOH B . I 8 HOH 74 474 88 HOH HOH B . I 8 HOH 75 475 89 HOH HOH B . I 8 HOH 76 476 90 HOH HOH B . I 8 HOH 77 477 91 HOH HOH B . I 8 HOH 78 478 92 HOH HOH B . I 8 HOH 79 479 93 HOH HOH B . I 8 HOH 80 480 94 HOH HOH B . I 8 HOH 81 481 95 HOH HOH B . I 8 HOH 82 482 96 HOH HOH B . I 8 HOH 83 483 97 HOH HOH B . I 8 HOH 84 484 98 HOH HOH B . I 8 HOH 85 485 99 HOH HOH B . I 8 HOH 86 486 100 HOH HOH B . I 8 HOH 87 487 101 HOH HOH B . I 8 HOH 88 488 102 HOH HOH B . I 8 HOH 89 489 103 HOH HOH B . I 8 HOH 90 490 104 HOH HOH B . I 8 HOH 91 491 105 HOH HOH B . I 8 HOH 92 492 106 HOH HOH B . I 8 HOH 93 493 107 HOH HOH B . I 8 HOH 94 494 108 HOH HOH B . I 8 HOH 95 495 109 HOH HOH B . I 8 HOH 96 496 112 HOH HOH B . I 8 HOH 97 497 113 HOH HOH B . I 8 HOH 98 498 114 HOH HOH B . I 8 HOH 99 499 115 HOH HOH B . I 8 HOH 100 500 116 HOH HOH B . I 8 HOH 101 501 117 HOH HOH B . I 8 HOH 102 502 118 HOH HOH B . I 8 HOH 103 503 119 HOH HOH B . I 8 HOH 104 504 120 HOH HOH B . I 8 HOH 105 505 121 HOH HOH B . I 8 HOH 106 506 122 HOH HOH B . I 8 HOH 107 507 123 HOH HOH B . I 8 HOH 108 508 124 HOH HOH B . I 8 HOH 109 509 125 HOH HOH B . I 8 HOH 110 510 126 HOH HOH B . I 8 HOH 111 511 127 HOH HOH B . I 8 HOH 112 512 128 HOH HOH B . I 8 HOH 113 513 130 HOH HOH B . I 8 HOH 114 514 133 HOH HOH B . I 8 HOH 115 515 134 HOH HOH B . I 8 HOH 116 516 135 HOH HOH B . I 8 HOH 117 517 137 HOH HOH B . I 8 HOH 118 518 138 HOH HOH B . I 8 HOH 119 519 139 HOH HOH B . I 8 HOH 120 520 140 HOH HOH B . I 8 HOH 121 521 141 HOH HOH B . I 8 HOH 122 522 142 HOH HOH B . I 8 HOH 123 523 144 HOH HOH B . I 8 HOH 124 524 145 HOH HOH B . J 8 HOH 1 101 20 HOH HOH A . J 8 HOH 2 102 21 HOH HOH A . J 8 HOH 3 103 26 HOH HOH A . J 8 HOH 4 104 32 HOH HOH A . J 8 HOH 5 105 34 HOH HOH A . J 8 HOH 6 106 38 HOH HOH A . J 8 HOH 7 107 44 HOH HOH A . J 8 HOH 8 108 45 HOH HOH A . J 8 HOH 9 109 49 HOH HOH A . J 8 HOH 10 110 50 HOH HOH A . J 8 HOH 11 111 53 HOH HOH A . J 8 HOH 12 112 68 HOH HOH A . J 8 HOH 13 113 82 HOH HOH A . J 8 HOH 14 114 83 HOH HOH A . J 8 HOH 15 115 110 HOH HOH A . J 8 HOH 16 116 111 HOH HOH A . J 8 HOH 17 117 129 HOH HOH A . J 8 HOH 18 118 131 HOH HOH A . J 8 HOH 19 119 132 HOH HOH A . J 8 HOH 20 120 136 HOH HOH A . J 8 HOH 21 121 143 HOH HOH A . #