data_4AYY # _entry.id 4AYY # _audit_conform.dict_name mmcif_pdbx.dic _audit_conform.dict_version 5.280 _audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic # loop_ _database_2.database_id _database_2.database_code PDB 4AYY PDBE EBI-53011 WWPDB D_1290053011 # loop_ _pdbx_database_related.db_name _pdbx_database_related.db_id _pdbx_database_related.content_type _pdbx_database_related.details PDB 4AYV unspecified 'HUMAN THROMBIN - INHIBITOR COMPLEX' PDB 4AZ2 unspecified 'HUMAN THROMBIN - INHIBITOR COMPLEX' # _pdbx_database_status.status_code REL _pdbx_database_status.entry_id 4AYY _pdbx_database_status.deposit_site PDBE _pdbx_database_status.process_site PDBE _pdbx_database_status.SG_entry . _pdbx_database_status.recvd_initial_deposition_date 2012-06-22 _pdbx_database_status.pdb_format_compatible Y _pdbx_database_status.status_code_sf ? _pdbx_database_status.status_code_mr ? _pdbx_database_status.status_code_cs ? _pdbx_database_status.methods_development_category ? # loop_ _audit_author.name _audit_author.pdbx_ordinal 'Banner, D.W.' 1 ;D'Arcy, A. ; 2 'Winkler, F.K.' 3 'Hilpert, K.' 4 # _citation.id primary _citation.title 'Design and Synthesis of Potent and Highly Selective Thrombin Inhibitors.' _citation.journal_abbrev J.Med.Chem. _citation.journal_volume 37 _citation.page_first 3889 _citation.page_last ? _citation.year 1994 _citation.journal_id_ASTM JMCMAR _citation.country US _citation.journal_id_ISSN 0022-2623 _citation.journal_id_CSD 0151 _citation.book_publisher ? _citation.pdbx_database_id_PubMed 7966150 _citation.pdbx_database_id_DOI 10.1021/JM00049A008 # loop_ _citation_author.citation_id _citation_author.name _citation_author.ordinal primary 'Hilpert, K.' 1 primary 'Ackermann, J.' 2 primary 'Banner, D.W.' 3 primary 'Gast, A.' 4 primary 'Gubernator, K.' 5 primary 'Hadvary, P.' 6 primary 'Labler, L.' 7 primary 'Muller, K.' 8 primary 'Schmid, G.' 9 primary 'Tschopp, T.B.' 10 # _cell.entry_id 4AYY _cell.length_a 90.800 _cell.length_b 90.800 _cell.length_c 132.500 _cell.angle_alpha 90.00 _cell.angle_beta 90.00 _cell.angle_gamma 90.00 _cell.Z_PDB 8 _cell.pdbx_unique_axis ? # _symmetry.entry_id 4AYY _symmetry.space_group_name_H-M 'P 43 21 2' _symmetry.pdbx_full_space_group_name_H-M ? _symmetry.cell_setting ? _symmetry.Int_Tables_number 96 # loop_ _entity.id _entity.type _entity.src_method _entity.pdbx_description _entity.formula_weight _entity.pdbx_number_of_molecules _entity.pdbx_ec _entity.pdbx_mutation _entity.pdbx_fragment _entity.details 1 polymer nat 'THROMBIN LIGHT CHAIN' 3489.881 1 3.4.21.5 ? 'LIGHT CHAIN, RESIDUES 332-361' ? 2 polymer nat 'THROMBIN HEAVY CHAIN' 29594.055 1 3.4.21.5 ? 'HEAVY CHAIN, RESIDUES 364-620' 'ASN B53 IS GLYCOSYLATED' 3 polymer syn "HIRUDIN-3A'" 1411.465 1 ? ? 'C-TERMINUS, RESIDUES 55-65' ? 4 non-polymer syn ;(R)-1-[(S)-3-[((S)-1-Carbamimidoyl-piperidin-3-ylmethyl)-carbamoyl]-2-(naphthalene-2-sulfonylamino)-propionyl]-4-methyl-piperidine-2-carboxylic acid ; 586.703 1 ? ? ? ? 5 non-polymer man N-ACETYL-D-GLUCOSAMINE 221.208 1 ? ? ? ? 6 non-polymer syn 'SODIUM ION' 22.990 1 ? ? ? ? 7 water nat water 18.015 70 ? ? ? ? # loop_ _entity_name_com.entity_id _entity_name_com.name 1 'COAGULATION FACTOR II' 2 'COAGULATION FACTOR II' 3 ;HIRUDIN, HIRUDIN IIIA' ; # 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 GEADCGLRPLFEKKSLEDKTERELLESYID GEADCGLRPLFEKKSLEDKTERELLESYID A ? 2 'polypeptide(L)' no no ;IVEGSDAEIGMSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPWDKNFTENDLLVRIGKHSRTRYERNIEKISM LEKIYIHPRYNWRENLDRDIALMKLKKPVAFSDYIHPVCLPDRETAASLLQAGYKGRVTGWGNLKETWTANVGKGQPSVL QVVNLPIVERPVCKDSTRIRITDNMFCAGYKPDEGKRGDACEGDSGGPFVMKSPFNNRWYQMGIVSWGEGCDRDGKYGFY THVFRLKKWIQKVIDQF ; ;IVEGSDAEIGMSPWQVMLFRKSPQELLCGASLISDRWVLTAAHCLLYPPWDKNFTENDLLVRIGKHSRTRYERNIEKISM LEKIYIHPRYNWRENLDRDIALMKLKKPVAFSDYIHPVCLPDRETAASLLQAGYKGRVTGWGNLKETWTANVGKGQPSVL QVVNLPIVERPVCKDSTRIRITDNMFCAGYKPDEGKRGDACEGDSGGPFVMKSPFNNRWYQMGIVSWGEGCDRDGKYGFY THVFRLKKWIQKVIDQF ; B ? 3 'polypeptide(L)' no no DFEEIPEEYLQ DFEEIPEEYLQ D ? # loop_ _entity_poly_seq.entity_id _entity_poly_seq.num _entity_poly_seq.mon_id _entity_poly_seq.hetero 1 1 GLY n 1 2 GLU n 1 3 ALA n 1 4 ASP n 1 5 CYS n 1 6 GLY n 1 7 LEU n 1 8 ARG n 1 9 PRO n 1 10 LEU n 1 11 PHE n 1 12 GLU n 1 13 LYS n 1 14 LYS n 1 15 SER n 1 16 LEU n 1 17 GLU n 1 18 ASP n 1 19 LYS n 1 20 THR n 1 21 GLU n 1 22 ARG n 1 23 GLU n 1 24 LEU n 1 25 LEU n 1 26 GLU n 1 27 SER n 1 28 TYR n 1 29 ILE n 1 30 ASP n 2 1 ILE n 2 2 VAL n 2 3 GLU n 2 4 GLY n 2 5 SER n 2 6 ASP n 2 7 ALA n 2 8 GLU n 2 9 ILE n 2 10 GLY n 2 11 MET n 2 12 SER n 2 13 PRO n 2 14 TRP n 2 15 GLN n 2 16 VAL n 2 17 MET n 2 18 LEU n 2 19 PHE n 2 20 ARG n 2 21 LYS n 2 22 SER n 2 23 PRO n 2 24 GLN n 2 25 GLU n 2 26 LEU n 2 27 LEU n 2 28 CYS n 2 29 GLY n 2 30 ALA n 2 31 SER n 2 32 LEU n 2 33 ILE n 2 34 SER n 2 35 ASP n 2 36 ARG n 2 37 TRP n 2 38 VAL n 2 39 LEU n 2 40 THR n 2 41 ALA n 2 42 ALA n 2 43 HIS n 2 44 CYS n 2 45 LEU n 2 46 LEU n 2 47 TYR n 2 48 PRO n 2 49 PRO n 2 50 TRP n 2 51 ASP n 2 52 LYS n 2 53 ASN n 2 54 PHE n 2 55 THR n 2 56 GLU n 2 57 ASN n 2 58 ASP n 2 59 LEU n 2 60 LEU n 2 61 VAL n 2 62 ARG n 2 63 ILE n 2 64 GLY n 2 65 LYS n 2 66 HIS n 2 67 SER n 2 68 ARG n 2 69 THR n 2 70 ARG n 2 71 TYR n 2 72 GLU n 2 73 ARG n 2 74 ASN n 2 75 ILE n 2 76 GLU n 2 77 LYS n 2 78 ILE n 2 79 SER n 2 80 MET n 2 81 LEU n 2 82 GLU n 2 83 LYS n 2 84 ILE n 2 85 TYR n 2 86 ILE n 2 87 HIS n 2 88 PRO n 2 89 ARG n 2 90 TYR n 2 91 ASN n 2 92 TRP n 2 93 ARG n 2 94 GLU n 2 95 ASN n 2 96 LEU n 2 97 ASP n 2 98 ARG n 2 99 ASP n 2 100 ILE n 2 101 ALA n 2 102 LEU n 2 103 MET n 2 104 LYS n 2 105 LEU n 2 106 LYS n 2 107 LYS n 2 108 PRO n 2 109 VAL n 2 110 ALA n 2 111 PHE n 2 112 SER n 2 113 ASP n 2 114 TYR n 2 115 ILE n 2 116 HIS n 2 117 PRO n 2 118 VAL n 2 119 CYS n 2 120 LEU n 2 121 PRO n 2 122 ASP n 2 123 ARG n 2 124 GLU n 2 125 THR n 2 126 ALA n 2 127 ALA n 2 128 SER n 2 129 LEU n 2 130 LEU n 2 131 GLN n 2 132 ALA n 2 133 GLY n 2 134 TYR n 2 135 LYS n 2 136 GLY n 2 137 ARG n 2 138 VAL n 2 139 THR n 2 140 GLY n 2 141 TRP n 2 142 GLY n 2 143 ASN n 2 144 LEU n 2 145 LYS n 2 146 GLU n 2 147 THR n 2 148 TRP n 2 149 THR n 2 150 ALA n 2 151 ASN n 2 152 VAL n 2 153 GLY n 2 154 LYS n 2 155 GLY n 2 156 GLN n 2 157 PRO n 2 158 SER n 2 159 VAL n 2 160 LEU n 2 161 GLN n 2 162 VAL n 2 163 VAL n 2 164 ASN n 2 165 LEU n 2 166 PRO n 2 167 ILE n 2 168 VAL n 2 169 GLU n 2 170 ARG n 2 171 PRO n 2 172 VAL n 2 173 CYS n 2 174 LYS n 2 175 ASP n 2 176 SER n 2 177 THR n 2 178 ARG n 2 179 ILE n 2 180 ARG n 2 181 ILE n 2 182 THR n 2 183 ASP n 2 184 ASN n 2 185 MET n 2 186 PHE n 2 187 CYS n 2 188 ALA n 2 189 GLY n 2 190 TYR n 2 191 LYS n 2 192 PRO n 2 193 ASP n 2 194 GLU n 2 195 GLY n 2 196 LYS n 2 197 ARG n 2 198 GLY n 2 199 ASP n 2 200 ALA n 2 201 CYS n 2 202 GLU n 2 203 GLY n 2 204 ASP n 2 205 SER n 2 206 GLY n 2 207 GLY n 2 208 PRO n 2 209 PHE n 2 210 VAL n 2 211 MET n 2 212 LYS n 2 213 SER n 2 214 PRO n 2 215 PHE n 2 216 ASN n 2 217 ASN n 2 218 ARG n 2 219 TRP n 2 220 TYR n 2 221 GLN n 2 222 MET n 2 223 GLY n 2 224 ILE n 2 225 VAL n 2 226 SER n 2 227 TRP n 2 228 GLY n 2 229 GLU n 2 230 GLY n 2 231 CYS n 2 232 ASP n 2 233 ARG n 2 234 ASP n 2 235 GLY n 2 236 LYS n 2 237 TYR n 2 238 GLY n 2 239 PHE n 2 240 TYR n 2 241 THR n 2 242 HIS n 2 243 VAL n 2 244 PHE n 2 245 ARG n 2 246 LEU n 2 247 LYS n 2 248 LYS n 2 249 TRP n 2 250 ILE n 2 251 GLN n 2 252 LYS n 2 253 VAL n 2 254 ILE n 2 255 ASP n 2 256 GLN n 2 257 PHE n 3 1 ASP n 3 2 PHE n 3 3 GLU n 3 4 GLU n 3 5 ILE n 3 6 PRO n 3 7 GLU n 3 8 GLU n 3 9 TYR n 3 10 LEU n 3 11 GLN n # loop_ _entity_src_nat.entity_id _entity_src_nat.pdbx_src_id _entity_src_nat.pdbx_alt_source_flag _entity_src_nat.pdbx_beg_seq_num _entity_src_nat.pdbx_end_seq_num _entity_src_nat.common_name _entity_src_nat.pdbx_organism_scientific _entity_src_nat.pdbx_ncbi_taxonomy_id _entity_src_nat.genus _entity_src_nat.species _entity_src_nat.strain _entity_src_nat.tissue _entity_src_nat.tissue_fraction _entity_src_nat.pdbx_secretion _entity_src_nat.pdbx_fragment _entity_src_nat.pdbx_variant _entity_src_nat.pdbx_cell_line _entity_src_nat.pdbx_atcc _entity_src_nat.pdbx_cellular_location _entity_src_nat.pdbx_organ _entity_src_nat.pdbx_organelle _entity_src_nat.pdbx_cell _entity_src_nat.pdbx_plasmid_name _entity_src_nat.pdbx_plasmid_details _entity_src_nat.details 1 1 sample ? ? HUMAN 'HOMO SAPIENS' 9606 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 2 1 sample ? ? HUMAN 'HOMO SAPIENS' 9606 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? # _pdbx_entity_src_syn.entity_id 3 _pdbx_entity_src_syn.pdbx_src_id 1 _pdbx_entity_src_syn.pdbx_alt_source_flag sample _pdbx_entity_src_syn.pdbx_beg_seq_num ? _pdbx_entity_src_syn.pdbx_end_seq_num ? _pdbx_entity_src_syn.organism_scientific 'HIRUDO MEDICINALIS' _pdbx_entity_src_syn.organism_common_name 'MEDICINAL LEECH' _pdbx_entity_src_syn.ncbi_taxonomy_id 6421 _pdbx_entity_src_syn.details ? # loop_ _struct_ref.id _struct_ref.db_name _struct_ref.db_code _struct_ref.entity_id _struct_ref.pdbx_seq_one_letter_code _struct_ref.pdbx_align_begin _struct_ref.pdbx_db_accession _struct_ref.pdbx_db_isoform 1 UNP THRB_HUMAN 1 ? ? P00734 ? 2 UNP THRB_HUMAN 2 ? ? P00734 ? 3 UNP HIR2B_HIRME 3 ? ? P28506 ? # 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 4AYY A 1 ? 30 ? P00734 332 ? 361 ? 5 34 2 2 4AYY B 1 ? 257 ? P00734 364 ? 620 ? 1 257 3 3 4AYY D 1 ? 11 ? P28506 55 ? 65 ? 1 11 # 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 9MX non-polymer . ;(R)-1-[(S)-3-[((S)-1-Carbamimidoyl-piperidin-3-ylmethyl)-carbamoyl]-2-(naphthalene-2-sulfonylamino)-propionyl]-4-methyl-piperidine-2-carboxylic acid ; ? 'C28 H38 N6 O6 S' 586.703 ALA 'L-peptide linking' y ALANINE ? 'C3 H7 N O2' 89.093 ARG 'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1' 175.209 ASN 'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3' 132.118 ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4' 133.103 CYS 'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S' 121.158 GLN 'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3' 146.144 GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4' 147.129 GLY 'peptide linking' y GLYCINE ? 'C2 H5 N O2' 75.067 HIS 'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1' 156.162 HOH non-polymer . WATER ? 'H2 O' 18.015 ILE 'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2' 131.173 LEU 'L-peptide linking' y LEUCINE ? 'C6 H13 N O2' 131.173 LYS 'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1' 147.195 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 4AYY _exptl.method 'X-RAY DIFFRACTION' _exptl.crystals_number 1 # _exptl_crystal.id 1 _exptl_crystal.density_meas ? _exptl_crystal.density_Matthews 4.14 _exptl_crystal.density_percent_sol 70.3 _exptl_crystal.description 'SOME DATA PROCESSING INFORMATION HAS BEEN LOST.' _exptl_crystal.preparation ? # _diffrn.id 1 _diffrn.ambient_temp 15 _diffrn.ambient_temp_details ? _diffrn.crystal_id 1 # _diffrn_detector.diffrn_id 1 _diffrn_detector.detector 'AREA DETECTOR' _diffrn_detector.type 'MULTIWIRE XENTRONICS' _diffrn_detector.pdbx_collection_date 1993-10-15 _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 'NI FILTER' _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 'ELLIOTT GX-21' _diffrn_source.pdbx_synchrotron_site ? _diffrn_source.pdbx_synchrotron_beamline ? _diffrn_source.pdbx_wavelength 1.5418 _diffrn_source.pdbx_wavelength_list 1.5418 # _reflns.pdbx_diffrn_id 1 _reflns.pdbx_ordinal 1 _reflns.entry_id 4AYY _reflns.observed_criterion_sigma_I 0.0 _reflns.observed_criterion_sigma_F ? _reflns.d_resolution_low 50.00 _reflns.d_resolution_high 2.60 _reflns.number_obs 16836 _reflns.number_all ? _reflns.percent_possible_obs 99.9 _reflns.pdbx_Rmerge_I_obs 0.04 _reflns.pdbx_Rsym_value ? _reflns.pdbx_netI_over_sigmaI ? _reflns.B_iso_Wilson_estimate ? _reflns.pdbx_redundancy 2.49 # _reflns_shell.pdbx_diffrn_id 1 _reflns_shell.pdbx_ordinal 1 _reflns_shell.d_res_high 2.60 _reflns_shell.d_res_low 2.70 _reflns_shell.percent_possible_all 68.9 _reflns_shell.Rmerge_I_obs ? _reflns_shell.pdbx_Rsym_value ? _reflns_shell.meanI_over_sigI_obs ? _reflns_shell.pdbx_redundancy ? # _refine.pdbx_refine_id 'X-RAY DIFFRACTION' _refine.entry_id 4AYY _refine.pdbx_diffrn_id 1 _refine.pdbx_TLS_residual_ADP_flag ? _refine.ls_number_reflns_obs 15541 _refine.ls_number_reflns_all ? _refine.pdbx_ls_sigma_I ? _refine.pdbx_ls_sigma_F . _refine.pdbx_data_cutoff_high_absF ? _refine.pdbx_data_cutoff_low_absF ? _refine.pdbx_data_cutoff_high_rms_absF ? _refine.ls_d_res_low 24.75 _refine.ls_d_res_high 2.60 _refine.ls_percent_reflns_obs 92.69 _refine.ls_R_factor_obs 0.14917 _refine.ls_R_factor_all ? _refine.ls_R_factor_R_work 0.14674 _refine.ls_R_factor_R_free 0.19663 _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 842 _refine.ls_number_parameters ? _refine.ls_number_restraints ? _refine.occupancy_min ? _refine.occupancy_max ? _refine.correlation_coeff_Fo_to_Fc 0.965 _refine.correlation_coeff_Fo_to_Fc_free 0.936 _refine.B_iso_mean 38.516 _refine.aniso_B[1][1] ? _refine.aniso_B[2][2] ? _refine.aniso_B[3][3] ? _refine.aniso_B[1][2] ? _refine.aniso_B[1][3] ? _refine.aniso_B[2][3] ? _refine.solvent_model_details ? _refine.solvent_model_param_ksol ? _refine.solvent_model_param_bsol ? _refine.pdbx_solvent_vdw_probe_radii ? _refine.pdbx_solvent_ion_probe_radii ? _refine.pdbx_solvent_shrinkage_radii ? _refine.pdbx_ls_cross_valid_method THROUGHOUT _refine.details ;HYDROGENS GENERATED AT RIDING POSITIONS IN REFMAC BUT NOT OUTPUT. RESIDUES B153 AND B154 HAVE ELECTRON DENSITY WHICH IS HARD TO FIT WITH THE PUBLISHED THROMBIN SEQUENCE. ; _refine.pdbx_starting_model 'IN HOUSE STRUCTURES' _refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' _refine.pdbx_isotropic_thermal_model ? _refine.pdbx_stereochemistry_target_values 'MAXIMUM LIKELIHOOD' _refine.pdbx_stereochem_target_val_spec_case ? _refine.pdbx_R_Free_selection_details RANDOM _refine.pdbx_overall_ESU_R 0.278 _refine.pdbx_overall_ESU_R_Free 0.217 _refine.overall_SU_ML 0.134 _refine.pdbx_overall_phase_error ? _refine.overall_SU_B 6.300 _refine.overall_SU_R_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? _refine.pdbx_overall_SU_R_Blow_DPI ? _refine.pdbx_overall_SU_R_free_Blow_DPI ? # _refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_hist.cycle_id LAST _refine_hist.pdbx_number_atoms_protein 2424 _refine_hist.pdbx_number_atoms_nucleic_acid 0 _refine_hist.pdbx_number_atoms_ligand 56 _refine_hist.number_atoms_solvent 70 _refine_hist.number_atoms_total 2550 _refine_hist.d_res_high 2.60 _refine_hist.d_res_low 24.75 # loop_ _refine_ls_restr.type _refine_ls_restr.dev_ideal _refine_ls_restr.dev_ideal_target _refine_ls_restr.weight _refine_ls_restr.number _refine_ls_restr.pdbx_refine_id _refine_ls_restr.pdbx_restraint_function r_bond_refined_d 0.009 0.019 ? 2568 'X-RAY DIFFRACTION' ? r_bond_other_d ? ? ? ? 'X-RAY DIFFRACTION' ? r_angle_refined_deg 1.363 1.985 ? 3478 'X-RAY DIFFRACTION' ? r_angle_other_deg ? ? ? ? 'X-RAY DIFFRACTION' ? r_dihedral_angle_1_deg 6.010 5.000 ? 299 'X-RAY DIFFRACTION' ? r_dihedral_angle_2_deg 36.670 23.577 ? 123 'X-RAY DIFFRACTION' ? r_dihedral_angle_3_deg 16.486 15.000 ? 448 'X-RAY DIFFRACTION' ? r_dihedral_angle_4_deg 15.919 15.000 ? 21 'X-RAY DIFFRACTION' ? r_chiral_restr 0.094 0.200 ? 358 'X-RAY DIFFRACTION' ? r_gen_planes_refined 0.005 0.021 ? 1968 'X-RAY DIFFRACTION' ? r_gen_planes_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbd_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbd_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbtor_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_nbtor_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_xyhbond_nbd_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_xyhbond_nbd_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_metal_ion_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_metal_ion_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_vdw_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_vdw_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_hbond_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_hbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_metal_ion_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_symmetry_metal_ion_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcbond_it ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcangle_it ? ? ? ? 'X-RAY DIFFRACTION' ? r_mcangle_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_scbond_it ? ? ? ? 'X-RAY DIFFRACTION' ? r_scbond_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_scangle_it ? ? ? ? 'X-RAY DIFFRACTION' ? r_scangle_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_long_range_B_refined ? ? ? ? 'X-RAY DIFFRACTION' ? r_long_range_B_other ? ? ? ? 'X-RAY DIFFRACTION' ? r_rigid_bond_restr ? ? ? ? 'X-RAY DIFFRACTION' ? r_sphericity_free ? ? ? ? 'X-RAY DIFFRACTION' ? r_sphericity_bonded ? ? ? ? 'X-RAY DIFFRACTION' ? # _refine_ls_shell.pdbx_refine_id 'X-RAY DIFFRACTION' _refine_ls_shell.pdbx_total_number_of_bins_used 20 _refine_ls_shell.d_res_high 2.600 _refine_ls_shell.d_res_low 2.668 _refine_ls_shell.number_reflns_R_work 651 _refine_ls_shell.R_factor_R_work 0.210 _refine_ls_shell.percent_reflns_obs 53.83 _refine_ls_shell.R_factor_R_free 0.301 _refine_ls_shell.R_factor_R_free_error ? _refine_ls_shell.percent_reflns_R_free ? _refine_ls_shell.number_reflns_R_free 37 _refine_ls_shell.number_reflns_all ? _refine_ls_shell.R_factor_all ? # _struct.entry_id 4AYY _struct.title 'Human thrombin - inhibitor complex' _struct.pdbx_descriptor ;THROMBIN LIGHT CHAIN (E.C.3.4.21.5), THROMBIN HEAVY CHAIN (E.C.3.4.21.5), HIRUDIN-3A' ; _struct.pdbx_model_details ? _struct.pdbx_CASP_flag ? _struct.pdbx_model_type_details ? # _struct_keywords.entry_id 4AYY _struct_keywords.pdbx_keywords HYDROLASE/INHIBITOR _struct_keywords.text '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 6 ? G N N 7 ? H N N 7 ? I N N 7 ? # 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 PHE A 11 ? SER A 15 ? PHE A 15 SER A 19 5 ? 5 HELX_P HELX_P2 2 THR A 20 ? SER A 27 ? THR A 24 SER A 31 1 ? 8 HELX_P HELX_P3 3 TYR A 28 ? ASP A 30 ? TYR A 32 ASP A 34 5 ? 3 HELX_P HELX_P4 4 ALA B 41 ? CYS B 44 ? ALA B 41 CYS B 44 5 ? 4 HELX_P HELX_P5 5 PRO B 48 ? ASP B 51 ? PRO B 48 ASP B 51 5 ? 4 HELX_P HELX_P6 6 ASP B 122 ? LEU B 130 ? ASP B 122 LEU B 130 1 ? 9 HELX_P HELX_P7 7 GLU B 169 ? SER B 176 ? GLU B 169 SER B 176 1 ? 8 HELX_P HELX_P8 8 LYS B 191 ? GLY B 195 ? LYS B 191 GLY B 195 5 ? 5 HELX_P HELX_P9 9 LEU B 246 ? PHE B 257 ? LEU B 246 PHE B 257 1 ? 12 HELX_P HELX_P10 10 PRO C 6 ? LEU C 10 ? PRO D 6 LEU D 10 5 ? 5 # _struct_conf_type.id HELX_P _struct_conf_type.criteria ? _struct_conf_type.reference ? # loop_ _struct_conn.id _struct_conn.conn_type_id _struct_conn.pdbx_leaving_atom_flag _struct_conn.pdbx_PDB_id _struct_conn.ptnr1_label_asym_id _struct_conn.ptnr1_label_comp_id _struct_conn.ptnr1_label_seq_id _struct_conn.ptnr1_label_atom_id _struct_conn.pdbx_ptnr1_label_alt_id _struct_conn.pdbx_ptnr1_PDB_ins_code _struct_conn.pdbx_ptnr1_standard_comp_id _struct_conn.ptnr1_symmetry _struct_conn.ptnr2_label_asym_id _struct_conn.ptnr2_label_comp_id _struct_conn.ptnr2_label_seq_id _struct_conn.ptnr2_label_atom_id _struct_conn.pdbx_ptnr2_label_alt_id _struct_conn.pdbx_ptnr2_PDB_ins_code _struct_conn.ptnr1_auth_asym_id _struct_conn.ptnr1_auth_comp_id _struct_conn.ptnr1_auth_seq_id _struct_conn.ptnr2_auth_asym_id _struct_conn.ptnr2_auth_comp_id _struct_conn.ptnr2_auth_seq_id _struct_conn.ptnr2_symmetry _struct_conn.pdbx_ptnr3_label_atom_id _struct_conn.pdbx_ptnr3_label_seq_id _struct_conn.pdbx_ptnr3_label_comp_id _struct_conn.pdbx_ptnr3_label_asym_id _struct_conn.pdbx_ptnr3_label_alt_id _struct_conn.pdbx_ptnr3_PDB_ins_code _struct_conn.details _struct_conn.pdbx_dist_value _struct_conn.pdbx_value_order disulf1 disulf ? ? A CYS 5 SG ? ? ? 1_555 B CYS 119 SG ? ? A CYS 9 B CYS 119 1_555 ? ? ? ? ? ? ? 2.051 ? disulf2 disulf ? ? B CYS 28 SG ? ? ? 1_555 B CYS 44 SG ? ? B CYS 28 B CYS 44 1_555 ? ? ? ? ? ? ? 2.038 ? disulf3 disulf ? ? B CYS 173 SG ? ? ? 1_555 B CYS 187 SG ? ? B CYS 173 B CYS 187 1_555 ? ? ? ? ? ? ? 2.047 ? disulf4 disulf ? ? B CYS 201 SG ? ? ? 1_555 B CYS 231 SG ? ? B CYS 201 B CYS 231 1_555 ? ? ? ? ? ? ? 2.049 ? covale1 covale ? ? B ASN 53 ND2 ? ? ? 1_555 E NAG . C1 ? ? B ASN 53 B NAG 1259 1_555 ? ? ? ? ? ? ? 1.451 ? metalc1 metalc ? ? F NA . NA ? ? ? 1_555 H HOH . O ? ? B NA 1260 B HOH 2054 1_555 ? ? ? ? ? ? ? 2.234 ? metalc2 metalc ? ? F NA . NA ? ? ? 1_555 H HOH . O ? ? B NA 1260 B HOH 2061 1_555 ? ? ? ? ? ? ? 2.081 ? metalc3 metalc ? ? F NA . NA ? ? ? 1_555 H HOH . O ? ? B NA 1260 B HOH 2050 1_555 ? ? ? ? ? ? ? 3.110 ? metalc4 metalc ? ? F NA . NA ? ? ? 1_555 B LYS 236 O ? ? B NA 1260 B LYS 236 1_555 ? ? ? ? ? ? ? 2.385 ? metalc5 metalc ? ? F NA . NA ? ? ? 1_555 H HOH . O ? ? B NA 1260 B HOH 2049 1_555 ? ? ? ? ? ? ? 2.429 ? metalc6 metalc ? ? F NA . NA ? ? ? 1_555 B ARG 233 O ? ? B NA 1260 B ARG 233 1_555 ? ? ? ? ? ? ? 2.514 ? # 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 B _struct_mon_prot_cis.label_alt_id . _struct_mon_prot_cis.pdbx_PDB_ins_code ? _struct_mon_prot_cis.auth_comp_id SER _struct_mon_prot_cis.auth_seq_id 22 _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 B _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 23 _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 -7.30 # loop_ _struct_sheet.id _struct_sheet.type _struct_sheet.number_strands _struct_sheet.details BA ? 7 ? BB ? 7 ? BC ? 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 BA 1 2 ? anti-parallel BA 2 3 ? anti-parallel BA 3 4 ? anti-parallel BA 4 5 ? anti-parallel BA 5 6 ? anti-parallel BA 6 7 ? anti-parallel BB 1 2 ? anti-parallel BB 2 3 ? anti-parallel BB 3 4 ? anti-parallel BB 4 5 ? anti-parallel BB 5 6 ? anti-parallel BB 6 7 ? anti-parallel BC 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 BA 1 SER B 5 ? ASP B 6 ? SER B 5 ASP B 6 BA 2 GLN B 161 ? PRO B 166 ? GLN B 161 PRO B 166 BA 3 LYS B 135 ? GLY B 140 ? LYS B 135 GLY B 140 BA 4 PRO B 208 ? LYS B 212 ? PRO B 208 LYS B 212 BA 5 TRP B 219 ? TRP B 227 ? TRP B 219 TRP B 227 BA 6 GLY B 238 ? HIS B 242 ? GLY B 238 HIS B 242 BA 7 MET B 185 ? ALA B 188 ? MET B 185 ALA B 188 BB 1 GLN B 15 ? ARG B 20 ? GLN B 15 ARG B 20 BB 2 GLU B 25 ? LEU B 32 ? GLU B 25 LEU B 32 BB 3 TRP B 37 ? THR B 40 ? TRP B 37 THR B 40 BB 4 ALA B 101 ? LEU B 105 ? ALA B 101 LEU B 105 BB 5 LYS B 77 ? ILE B 86 ? LYS B 77 ILE B 86 BB 6 LEU B 59 ? ILE B 63 ? LEU B 59 ILE B 63 BB 7 GLN B 15 ? ARG B 20 ? GLN B 15 ARG B 20 BC 1 LEU B 46 ? TYR B 47 ? LEU B 46 TYR B 47 BC 2 LYS B 52 ? ASN B 53 ? LYS B 52 ASN B 53 # 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 BA 1 2 N SER B 5 ? N SER B 5 O VAL B 162 ? O VAL B 162 BA 2 3 N LEU B 165 ? N LEU B 165 O GLY B 136 ? O GLY B 136 BA 3 4 N THR B 139 ? N THR B 139 O PRO B 208 ? O PRO B 208 BA 4 5 N MET B 211 ? N MET B 211 O TYR B 220 ? O TYR B 220 BA 5 6 N SER B 226 ? N SER B 226 O PHE B 239 ? O PHE B 239 BA 6 7 N TYR B 240 ? N TYR B 240 O PHE B 186 ? O PHE B 186 BB 1 2 N ARG B 20 ? N ARG B 20 O GLU B 25 ? O GLU B 25 BB 2 3 N SER B 31 ? N SER B 31 O LEU B 39 ? O LEU B 39 BB 3 4 N THR B 40 ? N THR B 40 O ALA B 101 ? O ALA B 101 BB 4 5 O LYS B 104 ? O LYS B 104 N GLU B 82 ? N GLU B 82 BB 5 6 N LEU B 81 ? N LEU B 81 O LEU B 59 ? O LEU B 59 BB 6 7 N ARG B 62 ? N ARG B 62 O MET B 17 ? O MET B 17 BC 1 2 N TYR B 47 ? N TYR B 47 O LYS B 52 ? O LYS B 52 # 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 ? ? ? ? 17 'BINDING SITE FOR RESIDUE 9MX B 1258' AC2 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE NA B 1260' AC3 Software ? ? ? ? 1 'BINDING SITE FOR MONO-SACCHARIDE NAG B1259 BOUND TO ASN B 53' AC4 Software ? ? ? ? 18 ;BINDING SITE FOR CHAIN D OF HIRUDIN-3A' ; # 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 17 HIS B 43 ? HIS B 43 . ? 1_555 ? 2 AC1 17 TYR B 47 ? TYR B 47 . ? 1_555 ? 3 AC1 17 TRP B 50 ? TRP B 50 . ? 1_555 ? 4 AC1 17 LEU B 96 ? LEU B 96 . ? 1_555 ? 5 AC1 17 ASP B 199 ? ASP B 199 . ? 1_555 ? 6 AC1 17 ALA B 200 ? ALA B 200 . ? 1_555 ? 7 AC1 17 GLU B 202 ? GLU B 202 . ? 1_555 ? 8 AC1 17 SER B 205 ? SER B 205 . ? 1_555 ? 9 AC1 17 VAL B 225 ? VAL B 225 . ? 1_555 ? 10 AC1 17 SER B 226 ? SER B 226 . ? 1_555 ? 11 AC1 17 TRP B 227 ? TRP B 227 . ? 1_555 ? 12 AC1 17 GLY B 228 ? GLY B 228 . ? 1_555 ? 13 AC1 17 GLU B 229 ? GLU B 229 . ? 1_555 ? 14 AC1 17 GLY B 230 ? GLY B 230 . ? 1_555 ? 15 AC1 17 GLY B 238 ? GLY B 238 . ? 1_555 ? 16 AC1 17 HOH H . ? HOH B 2053 . ? 1_555 ? 17 AC1 17 HOH H . ? HOH B 2057 . ? 1_555 ? 18 AC2 5 ARG B 233 ? ARG B 233 . ? 1_555 ? 19 AC2 5 LYS B 236 ? LYS B 236 . ? 1_555 ? 20 AC2 5 HOH H . ? HOH B 2049 . ? 1_555 ? 21 AC2 5 HOH H . ? HOH B 2054 . ? 1_555 ? 22 AC2 5 HOH H . ? HOH B 2061 . ? 1_555 ? 23 AC3 1 ASN B 53 ? ASN B 53 . ? 1_555 ? 24 AC4 18 PHE B 19 ? PHE B 19 . ? 1_555 ? 25 AC4 18 LYS B 21 ? LYS B 21 . ? 1_555 ? 26 AC4 18 LEU B 60 ? LEU B 60 . ? 1_555 ? 27 AC4 18 ARG B 68 ? ARG B 68 . ? 1_555 ? 28 AC4 18 THR B 69 ? THR B 69 . ? 1_555 ? 29 AC4 18 ARG B 70 ? ARG B 70 . ? 7_555 ? 30 AC4 18 ARG B 70 ? ARG B 70 . ? 1_555 ? 31 AC4 18 TYR B 71 ? TYR B 71 . ? 1_555 ? 32 AC4 18 HIS B 87 ? HIS B 87 . ? 3_544 ? 33 AC4 18 PRO B 88 ? PRO B 88 . ? 3_544 ? 34 AC4 18 LYS B 248 ? LYS B 248 . ? 3_544 ? 35 AC4 18 GLN B 251 ? GLN B 251 . ? 3_544 ? 36 AC4 18 LYS B 252 ? LYS B 252 . ? 3_544 ? 37 AC4 18 GLN B 256 ? GLN B 256 . ? 3_544 ? 38 AC4 18 HOH H . ? HOH B 2019 . ? 1_555 ? 39 AC4 18 HOH H . ? HOH B 2024 . ? 1_555 ? 40 AC4 18 HOH I . ? HOH D 2001 . ? 1_555 ? 41 AC4 18 HOH I . ? HOH D 2002 . ? 1_555 ? # _database_PDB_matrix.entry_id 4AYY _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 4AYY _atom_sites.fract_transf_matrix[1][1] 0.011013 _atom_sites.fract_transf_matrix[1][2] 0.000000 _atom_sites.fract_transf_matrix[1][3] 0.000000 _atom_sites.fract_transf_matrix[2][1] 0.000000 _atom_sites.fract_transf_matrix[2][2] 0.011013 _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] 0.007547 _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 . GLY A 1 1 ? 68.167 27.399 13.782 1.00 54.83 ? 5 GLY A N 1 ATOM 2 C CA . GLY A 1 1 ? 67.631 27.229 15.164 1.00 57.00 ? 5 GLY A CA 1 ATOM 3 C C . GLY A 1 1 ? 66.244 26.606 15.168 1.00 58.11 ? 5 GLY A C 1 ATOM 4 O O . GLY A 1 1 ? 65.836 25.944 14.203 1.00 56.77 ? 5 GLY A O 1 ATOM 5 N N . GLU A 1 2 ? 65.527 26.819 16.267 1.00 58.43 ? 6 GLU A N 1 ATOM 6 C CA . GLU A 1 2 ? 64.161 26.334 16.428 1.00 59.22 ? 6 GLU A CA 1 ATOM 7 C C . GLU A 1 2 ? 63.220 27.016 15.446 1.00 58.51 ? 6 GLU A C 1 ATOM 8 O O . GLU A 1 2 ? 63.286 28.231 15.264 1.00 58.20 ? 6 GLU A O 1 ATOM 9 C CB . GLU A 1 2 ? 63.678 26.583 17.852 1.00 62.23 ? 6 GLU A CB 1 ATOM 10 C CG . GLU A 1 2 ? 64.168 25.515 18.829 1.00 73.50 ? 6 GLU A CG 1 ATOM 11 C CD . GLU A 1 2 ? 63.793 25.828 20.270 1.00 78.69 ? 6 GLU A CD 1 ATOM 12 O OE1 . GLU A 1 2 ? 63.496 27.008 20.578 1.00 78.72 ? 6 GLU A OE1 1 ATOM 13 O OE2 . GLU A 1 2 ? 63.802 24.875 21.089 1.00 81.80 ? 6 GLU A OE2 1 ATOM 14 N N . ALA A 1 3 ? 62.350 26.232 14.810 1.00 55.91 ? 7 ALA A N 1 ATOM 15 C CA . ALA A 1 3 ? 61.359 26.781 13.892 1.00 51.32 ? 7 ALA A CA 1 ATOM 16 C C . ALA A 1 3 ? 60.466 27.791 14.615 1.00 50.15 ? 7 ALA A C 1 ATOM 17 O O . ALA A 1 3 ? 60.063 27.583 15.767 1.00 50.38 ? 7 ALA A O 1 ATOM 18 C CB . ALA A 1 3 ? 60.533 25.671 13.251 1.00 47.75 ? 7 ALA A CB 1 ATOM 19 N N . ASP A 1 4 ? 60.215 28.904 13.934 1.00 49.99 ? 8 ASP A N 1 ATOM 20 C CA . ASP A 1 4 ? 59.273 29.934 14.356 1.00 47.52 ? 8 ASP A CA 1 ATOM 21 C C . ASP A 1 4 ? 57.878 29.326 14.637 1.00 44.67 ? 8 ASP A C 1 ATOM 22 O O . ASP A 1 4 ? 57.424 28.430 13.900 1.00 49.06 ? 8 ASP A O 1 ATOM 23 C CB . ASP A 1 4 ? 59.184 30.951 13.232 1.00 49.76 ? 8 ASP A CB 1 ATOM 24 C CG . ASP A 1 4 ? 58.669 32.278 13.689 1.00 56.12 ? 8 ASP A CG 1 ATOM 25 O OD1 . ASP A 1 4 ? 58.458 32.509 14.884 1.00 62.74 ? 8 ASP A OD1 1 ATOM 26 O OD2 . ASP A 1 4 ? 58.466 33.177 12.735 1.00 58.18 ? 8 ASP A OD2 1 ATOM 27 N N . CYS A 1 5 ? 57.218 29.774 15.704 1.00 34.16 ? 9 CYS A N 1 ATOM 28 C CA . CYS A 1 5 ? 55.922 29.233 16.079 1.00 29.01 ? 9 CYS A CA 1 ATOM 29 C C . CYS A 1 5 ? 55.167 30.174 16.987 1.00 28.97 ? 9 CYS A C 1 ATOM 30 O O . CYS A 1 5 ? 55.776 30.921 17.737 1.00 30.63 ? 9 CYS A O 1 ATOM 31 C CB . CYS A 1 5 ? 56.045 27.851 16.731 1.00 25.88 ? 9 CYS A CB 1 ATOM 32 S SG . CYS A 1 5 ? 56.863 27.708 18.342 1.00 23.83 ? 9 CYS A SG 1 ATOM 33 N N . GLY A 1 6 ? 53.839 30.137 16.919 1.00 27.36 ? 10 GLY A N 1 ATOM 34 C CA . GLY A 1 6 ? 53.001 30.862 17.860 1.00 25.46 ? 10 GLY A CA 1 ATOM 35 C C . GLY A 1 6 ? 53.061 32.368 17.714 1.00 25.95 ? 10 GLY A C 1 ATOM 36 O O . GLY A 1 6 ? 52.559 33.072 18.560 1.00 25.64 ? 10 GLY A O 1 ATOM 37 N N . LEU A 1 7 ? 53.700 32.858 16.655 1.00 28.00 ? 11 LEU A N 1 ATOM 38 C CA . LEU A 1 7 ? 53.670 34.273 16.302 1.00 28.89 ? 11 LEU A CA 1 ATOM 39 C C . LEU A 1 7 ? 52.898 34.464 14.996 1.00 30.32 ? 11 LEU A C 1 ATOM 40 O O . LEU A 1 7 ? 53.381 34.103 13.913 1.00 35.28 ? 11 LEU A O 1 ATOM 41 C CB . LEU A 1 7 ? 55.089 34.816 16.138 1.00 29.52 ? 11 LEU A CB 1 ATOM 42 C CG . LEU A 1 7 ? 55.974 35.082 17.360 1.00 31.47 ? 11 LEU A CG 1 ATOM 43 C CD1 . LEU A 1 7 ? 57.241 35.766 16.859 1.00 30.79 ? 11 LEU A CD1 1 ATOM 44 C CD2 . LEU A 1 7 ? 55.286 35.937 18.426 1.00 31.14 ? 11 LEU A CD2 1 ATOM 45 N N . ARG A 1 8 ? 51.709 35.037 15.086 1.00 28.00 ? 12 ARG A N 1 ATOM 46 C CA . ARG A 1 8 ? 50.802 35.070 13.943 1.00 27.64 ? 12 ARG A CA 1 ATOM 47 C C . ARG A 1 8 ? 51.187 36.156 12.932 1.00 28.66 ? 12 ARG A C 1 ATOM 48 O O . ARG A 1 8 ? 51.324 37.330 13.301 1.00 29.54 ? 12 ARG A O 1 ATOM 49 C CB . ARG A 1 8 ? 49.369 35.306 14.421 1.00 26.38 ? 12 ARG A CB 1 ATOM 50 C CG . ARG A 1 8 ? 48.857 34.255 15.379 1.00 25.96 ? 12 ARG A CG 1 ATOM 51 C CD . ARG A 1 8 ? 47.533 34.677 15.976 1.00 25.49 ? 12 ARG A CD 1 ATOM 52 N NE . ARG A 1 8 ? 47.720 35.760 16.926 1.00 25.15 ? 12 ARG A NE 1 ATOM 53 C CZ . ARG A 1 8 ? 46.748 36.356 17.607 1.00 24.26 ? 12 ARG A CZ 1 ATOM 54 N NH1 . ARG A 1 8 ? 45.484 35.968 17.462 1.00 23.64 ? 12 ARG A NH1 1 ATOM 55 N NH2 . ARG A 1 8 ? 47.054 37.344 18.443 1.00 23.30 ? 12 ARG A NH2 1 ATOM 56 N N . PRO A 1 9 ? 51.326 35.780 11.647 1.00 28.03 ? 13 PRO A N 1 ATOM 57 C CA . PRO A 1 9 ? 51.698 36.752 10.610 1.00 27.72 ? 13 PRO A CA 1 ATOM 58 C C . PRO A 1 9 ? 50.820 38.006 10.571 1.00 28.79 ? 13 PRO A C 1 ATOM 59 O O . PRO A 1 9 ? 51.330 39.085 10.297 1.00 31.12 ? 13 PRO A O 1 ATOM 60 C CB . PRO A 1 9 ? 51.559 35.959 9.317 1.00 26.52 ? 13 PRO A CB 1 ATOM 61 C CG . PRO A 1 9 ? 51.814 34.546 9.728 1.00 27.35 ? 13 PRO A CG 1 ATOM 62 C CD . PRO A 1 9 ? 51.206 34.416 11.102 1.00 27.87 ? 13 PRO A CD 1 ATOM 63 N N . LEU A 1 10 ? 49.531 37.888 10.869 1.00 29.30 ? 14 LEU A N 1 ATOM 64 C CA . LEU A 1 10 ? 48.643 39.058 10.786 1.00 29.40 ? 14 LEU A CA 1 ATOM 65 C C . LEU A 1 10 ? 48.454 39.787 12.117 1.00 29.12 ? 14 LEU A C 1 ATOM 66 O O . LEU A 1 10 ? 47.745 40.793 12.171 1.00 29.82 ? 14 LEU A O 1 ATOM 67 C CB . LEU A 1 10 ? 47.276 38.693 10.176 1.00 29.01 ? 14 LEU A CB 1 ATOM 68 C CG . LEU A 1 10 ? 47.214 38.223 8.706 1.00 31.41 ? 14 LEU A CG 1 ATOM 69 C CD1 . LEU A 1 10 ? 45.776 37.929 8.311 1.00 31.02 ? 14 LEU A CD1 1 ATOM 70 C CD2 . LEU A 1 10 ? 47.835 39.210 7.719 1.00 29.59 ? 14 LEU A CD2 1 ATOM 71 N N . PHE A 1 11 ? 49.058 39.287 13.192 1.00 28.27 ? 15 PHE A N 1 ATOM 72 C CA . PHE A 1 11 ? 48.930 39.968 14.484 1.00 28.64 ? 15 PHE A CA 1 ATOM 73 C C . PHE A 1 11 ? 50.272 40.317 15.130 1.00 30.37 ? 15 PHE A C 1 ATOM 74 O O . PHE A 1 11 ? 50.780 41.418 14.886 1.00 31.97 ? 15 PHE A O 1 ATOM 75 C CB . PHE A 1 11 ? 47.968 39.228 15.413 1.00 27.81 ? 15 PHE A CB 1 ATOM 76 C CG . PHE A 1 11 ? 46.560 39.192 14.887 1.00 27.92 ? 15 PHE A CG 1 ATOM 77 C CD1 . PHE A 1 11 ? 46.151 38.183 14.014 1.00 26.24 ? 15 PHE A CD1 1 ATOM 78 C CD2 . PHE A 1 11 ? 45.644 40.203 15.221 1.00 28.02 ? 15 PHE A CD2 1 ATOM 79 C CE1 . PHE A 1 11 ? 44.858 38.170 13.504 1.00 26.29 ? 15 PHE A CE1 1 ATOM 80 C CE2 . PHE A 1 11 ? 44.339 40.180 14.718 1.00 26.06 ? 15 PHE A CE2 1 ATOM 81 C CZ . PHE A 1 11 ? 43.950 39.162 13.866 1.00 26.00 ? 15 PHE A CZ 1 ATOM 82 N N . GLU A 1 12 ? 50.854 39.403 15.914 1.00 30.50 ? 16 GLU A N 1 ATOM 83 C CA . GLU A 1 12 ? 52.153 39.651 16.561 1.00 30.88 ? 16 GLU A CA 1 ATOM 84 C C . GLU A 1 12 ? 53.172 40.243 15.600 1.00 32.95 ? 16 GLU A C 1 ATOM 85 O O . GLU A 1 12 ? 53.831 41.217 15.937 1.00 32.56 ? 16 GLU A O 1 ATOM 86 C CB . GLU A 1 12 ? 52.730 38.392 17.210 1.00 29.10 ? 16 GLU A CB 1 ATOM 87 C CG . GLU A 1 12 ? 52.066 38.030 18.526 1.00 29.80 ? 16 GLU A CG 1 ATOM 88 C CD . GLU A 1 12 ? 50.683 37.394 18.359 1.00 29.73 ? 16 GLU A CD 1 ATOM 89 O OE1 . GLU A 1 12 ? 50.345 36.941 17.239 1.00 28.05 ? 16 GLU A OE1 1 ATOM 90 O OE2 . GLU A 1 12 ? 49.942 37.330 19.364 1.00 28.84 ? 16 GLU A OE2 1 ATOM 91 N N . LYS A 1 13 ? 53.272 39.678 14.399 1.00 36.00 ? 17 LYS A N 1 ATOM 92 C CA . LYS A 1 13 ? 54.262 40.114 13.406 1.00 37.52 ? 17 LYS A CA 1 ATOM 93 C C . LYS A 1 13 ? 54.035 41.502 12.809 1.00 39.01 ? 17 LYS A C 1 ATOM 94 O O . LYS A 1 13 ? 54.926 42.043 12.189 1.00 42.63 ? 17 LYS A O 1 ATOM 95 C CB . LYS A 1 13 ? 54.408 39.078 12.302 1.00 37.56 ? 17 LYS A CB 1 ATOM 96 C CG . LYS A 1 13 ? 55.434 38.034 12.670 1.00 42.34 ? 17 LYS A CG 1 ATOM 97 C CD . LYS A 1 13 ? 55.562 36.937 11.637 1.00 45.12 ? 17 LYS A CD 1 ATOM 98 C CE . LYS A 1 13 ? 56.545 35.895 12.148 1.00 47.28 ? 17 LYS A CE 1 ATOM 99 N NZ . LYS A 1 13 ? 56.037 34.524 11.868 1.00 47.58 ? 17 LYS A NZ 1 ATOM 100 N N . LYS A 1 14 ? 52.853 42.071 12.998 1.00 40.65 ? 18 LYS A N 1 ATOM 101 C CA . LYS A 1 14 ? 52.569 43.424 12.548 1.00 42.79 ? 18 LYS A CA 1 ATOM 102 C C . LYS A 1 14 ? 52.260 44.320 13.746 1.00 45.67 ? 18 LYS A C 1 ATOM 103 O O . LYS A 1 14 ? 51.692 45.407 13.587 1.00 47.03 ? 18 LYS A O 1 ATOM 104 C CB . LYS A 1 14 ? 51.369 43.418 11.599 1.00 45.11 ? 18 LYS A CB 1 ATOM 105 C CG . LYS A 1 14 ? 51.681 43.028 10.173 1.00 47.51 ? 18 LYS A CG 1 ATOM 106 C CD . LYS A 1 14 ? 50.438 42.450 9.520 1.00 53.14 ? 18 LYS A CD 1 ATOM 107 C CE . LYS A 1 14 ? 50.602 42.280 8.012 1.00 58.28 ? 18 LYS A CE 1 ATOM 108 N NZ . LYS A 1 14 ? 49.652 43.165 7.273 1.00 57.44 ? 18 LYS A NZ 1 ATOM 109 N N . SER A 1 15 ? 52.608 43.847 14.943 1.00 46.65 ? 19 SER A N 1 ATOM 110 C CA . SER A 1 15 ? 52.285 44.530 16.203 1.00 46.08 ? 19 SER A CA 1 ATOM 111 C C . SER A 1 15 ? 50.814 44.900 16.360 1.00 46.47 ? 19 SER A C 1 ATOM 112 O O . SER A 1 15 ? 50.496 45.905 16.985 1.00 48.60 ? 19 SER A O 1 ATOM 113 C CB . SER A 1 15 ? 53.141 45.785 16.370 1.00 45.78 ? 19 SER A CB 1 ATOM 114 O OG . SER A 1 15 ? 54.485 45.424 16.586 1.00 48.62 ? 19 SER A OG 1 ATOM 115 N N . LEU A 1 16 ? 49.916 44.106 15.785 1.00 46.37 ? 20 LEU A N 1 ATOM 116 C CA . LEU A 1 16 ? 48.483 44.324 15.992 1.00 43.62 ? 20 LEU A CA 1 ATOM 117 C C . LEU A 1 16 ? 47.977 43.324 17.013 1.00 40.88 ? 20 LEU A C 1 ATOM 118 O O . LEU A 1 16 ? 48.476 42.201 17.080 1.00 38.19 ? 20 LEU A O 1 ATOM 119 C CB . LEU A 1 16 ? 47.710 44.202 14.678 1.00 43.36 ? 20 LEU A CB 1 ATOM 120 C CG . LEU A 1 16 ? 48.108 45.222 13.601 1.00 47.54 ? 20 LEU A CG 1 ATOM 121 C CD1 . LEU A 1 16 ? 47.592 44.810 12.222 1.00 45.74 ? 20 LEU A CD1 1 ATOM 122 C CD2 . LEU A 1 16 ? 47.656 46.634 13.975 1.00 43.88 ? 20 LEU A CD2 1 ATOM 123 N N . GLU A 1 17 ? 47.009 43.726 17.826 1.00 39.42 ? 21 GLU A N 1 ATOM 124 C CA . GLU A 1 17 ? 46.421 42.770 18.751 1.00 42.88 ? 21 GLU A CA 1 ATOM 125 C C . GLU A 1 17 ? 44.967 42.383 18.415 1.00 39.47 ? 21 GLU A C 1 ATOM 126 O O . GLU A 1 17 ? 44.222 43.198 17.916 1.00 41.17 ? 21 GLU A O 1 ATOM 127 C CB . GLU A 1 17 ? 46.630 43.202 20.211 1.00 47.75 ? 21 GLU A CB 1 ATOM 128 C CG . GLU A 1 17 ? 45.745 44.305 20.769 1.00 55.82 ? 21 GLU A CG 1 ATOM 129 C CD . GLU A 1 17 ? 46.088 44.610 22.231 1.00 61.30 ? 21 GLU A CD 1 ATOM 130 O OE1 . GLU A 1 17 ? 47.304 44.748 22.532 1.00 60.33 ? 21 GLU A OE1 1 ATOM 131 O OE2 . GLU A 1 17 ? 45.154 44.692 23.078 1.00 60.12 ? 21 GLU A OE2 1 ATOM 132 N N . ASP A 1 18 ? 44.578 41.131 18.649 1.00 35.04 ? 22 ASP A N 1 ATOM 133 C CA . ASP A 1 18 ? 43.203 40.745 18.361 1.00 32.79 ? 22 ASP A CA 1 ATOM 134 C C . ASP A 1 18 ? 42.215 41.303 19.397 1.00 33.14 ? 22 ASP A C 1 ATOM 135 O O . ASP A 1 18 ? 42.626 41.798 20.438 1.00 33.81 ? 22 ASP A O 1 ATOM 136 C CB . ASP A 1 18 ? 43.053 39.242 18.056 1.00 29.69 ? 22 ASP A CB 1 ATOM 137 C CG . ASP A 1 18 ? 43.161 38.349 19.282 1.00 29.26 ? 22 ASP A CG 1 ATOM 138 O OD1 . ASP A 1 18 ? 42.429 38.508 20.261 1.00 30.14 ? 22 ASP A OD1 1 ATOM 139 O OD2 . ASP A 1 18 ? 44.038 37.358 19.205 1.00 27.03 ? 22 ASP A OD2 1 ATOM 140 N N . LYS A 1 19 ? 40.928 41.243 19.076 1.00 34.94 ? 23 LYS A N 1 ATOM 141 C CA . LYS A 1 19 ? 39.859 41.895 19.838 1.00 36.68 ? 23 LYS A CA 1 ATOM 142 C C . LYS A 1 19 ? 39.736 41.457 21.295 1.00 35.04 ? 23 LYS A C 1 ATOM 143 O O . LYS A 1 19 ? 39.242 42.208 22.108 1.00 32.17 ? 23 LYS A O 1 ATOM 144 C CB . LYS A 1 19 ? 38.497 41.668 19.154 1.00 41.45 ? 23 LYS A CB 1 ATOM 145 C CG . LYS A 1 19 ? 38.197 42.577 17.964 1.00 47.39 ? 23 LYS A CG 1 ATOM 146 C CD . LYS A 1 19 ? 36.942 42.103 17.219 1.00 50.97 ? 23 LYS A CD 1 ATOM 147 C CE . LYS A 1 19 ? 36.929 42.559 15.759 0.50 52.15 ? 23 LYS A CE 1 ATOM 148 N NZ . LYS A 1 19 ? 36.453 43.959 15.563 0.50 51.13 ? 23 LYS A NZ 1 ATOM 149 N N . THR A 1 20 ? 40.142 40.240 21.630 1.00 34.39 ? 24 THR A N 1 ATOM 150 C CA . THR A 1 20 ? 39.879 39.768 22.976 1.00 34.40 ? 24 THR A CA 1 ATOM 151 C C . THR A 1 20 ? 41.107 39.230 23.700 1.00 35.71 ? 24 THR A C 1 ATOM 152 O O . THR A 1 20 ? 40.971 38.688 24.805 1.00 36.91 ? 24 THR A O 1 ATOM 153 C CB . THR A 1 20 ? 38.736 38.713 23.025 1.00 35.62 ? 24 THR A CB 1 ATOM 154 O OG1 . THR A 1 20 ? 39.115 37.552 22.278 1.00 36.66 ? 24 THR A OG1 1 ATOM 155 C CG2 . THR A 1 20 ? 37.424 39.269 22.460 1.00 33.57 ? 24 THR A CG2 1 ATOM 156 N N . GLU A 1 21 ? 42.299 39.380 23.113 1.00 34.84 ? 25 GLU A N 1 ATOM 157 C CA . GLU A 1 21 ? 43.498 38.800 23.743 1.00 33.73 ? 25 GLU A CA 1 ATOM 158 C C . GLU A 1 21 ? 43.856 39.467 25.065 1.00 35.07 ? 25 GLU A C 1 ATOM 159 O O . GLU A 1 21 ? 44.369 38.798 25.970 1.00 36.00 ? 25 GLU A O 1 ATOM 160 C CB . GLU A 1 21 ? 44.708 38.734 22.807 1.00 30.87 ? 25 GLU A CB 1 ATOM 161 C CG . GLU A 1 21 ? 45.352 40.055 22.461 1.00 30.42 ? 25 GLU A CG 1 ATOM 162 C CD . GLU A 1 21 ? 46.580 39.872 21.592 1.00 31.39 ? 25 GLU A CD 1 ATOM 163 O OE1 . GLU A 1 21 ? 47.692 39.684 22.138 1.00 31.00 ? 25 GLU A OE1 1 ATOM 164 O OE2 . GLU A 1 21 ? 46.436 39.907 20.352 1.00 31.41 ? 25 GLU A OE2 1 ATOM 165 N N . ARG A 1 22 ? 43.563 40.764 25.182 1.00 35.53 ? 26 ARG A N 1 ATOM 166 C CA . ARG A 1 22 ? 43.785 41.476 26.433 1.00 38.03 ? 26 ARG A CA 1 ATOM 167 C C . ARG A 1 22 ? 43.086 40.804 27.619 1.00 36.59 ? 26 ARG A C 1 ATOM 168 O O . ARG A 1 22 ? 43.633 40.767 28.721 1.00 35.55 ? 26 ARG A O 1 ATOM 169 C CB . ARG A 1 22 ? 43.387 42.950 26.326 1.00 43.76 ? 26 ARG A CB 1 ATOM 170 C CG . ARG A 1 22 ? 43.975 43.772 27.461 1.00 53.61 ? 26 ARG A CG 1 ATOM 171 C CD . ARG A 1 22 ? 44.407 45.165 27.024 1.00 66.12 ? 26 ARG A CD 1 ATOM 172 N NE . ARG A 1 22 ? 45.609 45.631 27.739 1.00 72.70 ? 26 ARG A NE 1 ATOM 173 C CZ . ARG A 1 22 ? 45.662 45.995 29.026 1.00 71.06 ? 26 ARG A CZ 1 ATOM 174 N NH1 . ARG A 1 22 ? 44.588 45.953 29.804 1.00 66.66 ? 26 ARG A NH1 1 ATOM 175 N NH2 . ARG A 1 22 ? 46.813 46.401 29.547 1.00 74.24 ? 26 ARG A NH2 1 ATOM 176 N N . GLU A 1 23 ? 41.896 40.251 27.388 1.00 35.06 ? 27 GLU A N 1 ATOM 177 C CA . GLU A 1 23 ? 41.215 39.466 28.416 1.00 34.67 ? 27 GLU A CA 1 ATOM 178 C C . GLU A 1 23 ? 42.093 38.308 28.959 1.00 34.73 ? 27 GLU A C 1 ATOM 179 O O . GLU A 1 23 ? 42.102 38.053 30.173 1.00 34.52 ? 27 GLU A O 1 ATOM 180 C CB . GLU A 1 23 ? 39.854 38.969 27.919 1.00 34.35 ? 27 GLU A CB 1 ATOM 181 C CG . GLU A 1 23 ? 39.152 38.033 28.896 1.00 38.26 ? 27 GLU A CG 1 ATOM 182 C CD . GLU A 1 23 ? 37.847 37.427 28.378 1.00 40.00 ? 27 GLU A CD 1 ATOM 183 O OE1 . GLU A 1 23 ? 37.516 37.573 27.175 1.00 39.99 ? 27 GLU A OE1 1 ATOM 184 O OE2 . GLU A 1 23 ? 37.141 36.802 29.198 1.00 39.90 ? 27 GLU A OE2 1 ATOM 185 N N . LEU A 1 24 ? 42.837 37.632 28.075 1.00 32.73 ? 28 LEU A N 1 ATOM 186 C CA . LEU A 1 24 ? 43.730 36.547 28.488 1.00 31.36 ? 28 LEU A CA 1 ATOM 187 C C . LEU A 1 24 ? 44.893 37.046 29.355 1.00 30.79 ? 28 LEU A C 1 ATOM 188 O O . LEU A 1 24 ? 45.142 36.497 30.439 1.00 29.24 ? 28 LEU A O 1 ATOM 189 C CB . LEU A 1 24 ? 44.253 35.755 27.285 1.00 32.41 ? 28 LEU A CB 1 ATOM 190 C CG . LEU A 1 24 ? 43.285 35.020 26.329 1.00 34.34 ? 28 LEU A CG 1 ATOM 191 C CD1 . LEU A 1 24 ? 44.087 34.340 25.237 1.00 33.58 ? 28 LEU A CD1 1 ATOM 192 C CD2 . LEU A 1 24 ? 42.387 33.987 27.000 1.00 34.87 ? 28 LEU A CD2 1 ATOM 193 N N . LEU A 1 25 ? 45.582 38.084 28.881 1.00 30.06 ? 29 LEU A N 1 ATOM 194 C CA . LEU A 1 25 ? 46.707 38.702 29.602 1.00 31.58 ? 29 LEU A CA 1 ATOM 195 C C . LEU A 1 25 ? 46.331 39.231 31.002 1.00 33.00 ? 29 LEU A C 1 ATOM 196 O O . LEU A 1 25 ? 47.004 38.924 31.995 1.00 34.02 ? 29 LEU A O 1 ATOM 197 C CB . LEU A 1 25 ? 47.383 39.786 28.740 1.00 31.09 ? 29 LEU A CB 1 ATOM 198 C CG . LEU A 1 25 ? 47.920 39.287 27.373 1.00 32.10 ? 29 LEU A CG 1 ATOM 199 C CD1 . LEU A 1 25 ? 48.317 40.409 26.411 1.00 30.96 ? 29 LEU A CD1 1 ATOM 200 C CD2 . LEU A 1 25 ? 49.064 38.299 27.544 1.00 30.78 ? 29 LEU A CD2 1 ATOM 201 N N . GLU A 1 26 ? 45.236 39.979 31.087 1.00 34.39 ? 30 GLU A N 1 ATOM 202 C CA . GLU A 1 26 ? 44.722 40.452 32.365 1.00 36.45 ? 30 GLU A CA 1 ATOM 203 C C . GLU A 1 26 ? 44.460 39.346 33.367 1.00 36.08 ? 30 GLU A C 1 ATOM 204 O O . GLU A 1 26 ? 44.633 39.560 34.565 1.00 38.62 ? 30 GLU A O 1 ATOM 205 C CB . GLU A 1 26 ? 43.443 41.262 32.180 1.00 40.89 ? 30 GLU A CB 1 ATOM 206 C CG . GLU A 1 26 ? 43.675 42.755 32.074 1.00 47.01 ? 30 GLU A CG 1 ATOM 207 C CD . GLU A 1 26 ? 42.479 43.478 31.499 1.00 53.85 ? 30 GLU A CD 1 ATOM 208 O OE1 . GLU A 1 26 ? 41.326 43.093 31.806 1.00 57.03 ? 30 GLU A OE1 1 ATOM 209 O OE2 . GLU A 1 26 ? 42.692 44.432 30.726 1.00 59.64 ? 30 GLU A OE2 1 ATOM 210 N N . SER A 1 27 ? 44.039 38.172 32.898 1.00 34.33 ? 31 SER A N 1 ATOM 211 C CA . SER A 1 27 ? 43.761 37.068 33.813 1.00 34.08 ? 31 SER A CA 1 ATOM 212 C C . SER A 1 27 ? 45.006 36.649 34.607 1.00 35.72 ? 31 SER A C 1 ATOM 213 O O . SER A 1 27 ? 44.888 36.044 35.668 1.00 36.55 ? 31 SER A O 1 ATOM 214 C CB . SER A 1 27 ? 43.144 35.868 33.087 1.00 32.34 ? 31 SER A CB 1 ATOM 215 O OG . SER A 1 27 ? 44.122 35.077 32.441 1.00 33.22 ? 31 SER A OG 1 ATOM 216 N N . TYR A 1 28 ? 46.188 36.982 34.088 1.00 37.12 ? 32 TYR A N 1 ATOM 217 C CA . TYR A 1 28 ? 47.447 36.635 34.735 1.00 38.68 ? 32 TYR A CA 1 ATOM 218 C C . TYR A 1 28 ? 47.734 37.497 35.958 1.00 40.02 ? 32 TYR A C 1 ATOM 219 O O . TYR A 1 28 ? 48.445 37.077 36.868 1.00 39.91 ? 32 TYR A O 1 ATOM 220 C CB . TYR A 1 28 ? 48.611 36.794 33.762 1.00 38.45 ? 32 TYR A CB 1 ATOM 221 C CG . TYR A 1 28 ? 48.588 35.864 32.577 1.00 37.48 ? 32 TYR A CG 1 ATOM 222 C CD1 . TYR A 1 28 ? 48.230 34.523 32.714 1.00 36.42 ? 32 TYR A CD1 1 ATOM 223 C CD2 . TYR A 1 28 ? 48.959 36.325 31.314 1.00 37.79 ? 32 TYR A CD2 1 ATOM 224 C CE1 . TYR A 1 28 ? 48.210 33.680 31.619 1.00 36.42 ? 32 TYR A CE1 1 ATOM 225 C CE2 . TYR A 1 28 ? 48.954 35.483 30.217 1.00 37.22 ? 32 TYR A CE2 1 ATOM 226 C CZ . TYR A 1 28 ? 48.580 34.167 30.376 1.00 36.14 ? 32 TYR A CZ 1 ATOM 227 O OH . TYR A 1 28 ? 48.590 33.348 29.284 1.00 36.18 ? 32 TYR A OH 1 ATOM 228 N N . ILE A 1 29 ? 47.186 38.706 35.965 1.00 42.80 ? 33 ILE A N 1 ATOM 229 C CA . ILE A 1 29 ? 47.497 39.682 36.998 1.00 46.64 ? 33 ILE A CA 1 ATOM 230 C C . ILE A 1 29 ? 46.274 40.031 37.867 1.00 52.18 ? 33 ILE A C 1 ATOM 231 O O . ILE A 1 29 ? 45.918 41.189 37.993 1.00 58.49 ? 33 ILE A O 1 ATOM 232 C CB . ILE A 1 29 ? 48.172 40.934 36.377 1.00 45.20 ? 33 ILE A CB 1 ATOM 233 C CG1 . ILE A 1 29 ? 47.196 41.748 35.528 1.00 41.97 ? 33 ILE A CG1 1 ATOM 234 C CG2 . ILE A 1 29 ? 49.345 40.524 35.491 1.00 45.09 ? 33 ILE A CG2 1 ATOM 235 C CD1 . ILE A 1 29 ? 47.746 43.086 35.083 1.00 41.04 ? 33 ILE A CD1 1 ATOM 236 N N . ASP A 1 30 ? 45.643 39.018 38.464 1.00 61.05 ? 34 ASP A N 1 ATOM 237 C CA . ASP A 1 30 ? 44.517 39.223 39.393 1.00 69.30 ? 34 ASP A CA 1 ATOM 238 C C . ASP A 1 30 ? 44.735 38.701 40.825 1.00 72.64 ? 34 ASP A C 1 ATOM 239 O O . ASP A 1 30 ? 45.308 37.631 41.051 1.00 75.39 ? 34 ASP A O 1 ATOM 240 C CB . ASP A 1 30 ? 43.227 38.652 38.806 1.00 70.03 ? 34 ASP A CB 1 ATOM 241 C CG . ASP A 1 30 ? 42.592 39.587 37.807 1.00 72.85 ? 34 ASP A CG 1 ATOM 242 O OD1 . ASP A 1 30 ? 42.992 40.766 37.720 1.00 71.60 ? 34 ASP A OD1 1 ATOM 243 O OD2 . ASP A 1 30 ? 41.679 39.147 37.098 1.00 85.36 ? 34 ASP A OD2 1 ATOM 244 O OXT . ASP A 1 30 ? 44.336 39.350 41.794 0.010 72.32 ? 34 ASP A OXT 1 ATOM 245 N N . ILE B 2 1 ? 31.135 25.948 19.402 1.00 23.50 ? 1 ILE B N 1 ATOM 246 C CA . ILE B 2 1 ? 31.463 26.914 20.498 1.00 24.83 ? 1 ILE B CA 1 ATOM 247 C C . ILE B 2 1 ? 30.175 27.613 20.930 1.00 27.43 ? 1 ILE B C 1 ATOM 248 O O . ILE B 2 1 ? 29.488 28.246 20.116 1.00 28.32 ? 1 ILE B O 1 ATOM 249 C CB . ILE B 2 1 ? 32.510 28.007 20.088 1.00 24.14 ? 1 ILE B CB 1 ATOM 250 C CG1 . ILE B 2 1 ? 33.844 27.414 19.551 1.00 23.28 ? 1 ILE B CG1 1 ATOM 251 C CG2 . ILE B 2 1 ? 32.714 29.007 21.219 1.00 22.22 ? 1 ILE B CG2 1 ATOM 252 C CD1 . ILE B 2 1 ? 34.687 26.625 20.534 1.00 21.70 ? 1 ILE B CD1 1 ATOM 253 N N . VAL B 2 2 ? 29.859 27.490 22.218 1.00 28.98 ? 2 VAL B N 1 ATOM 254 C CA . VAL B 2 2 ? 28.719 28.159 22.809 1.00 28.87 ? 2 VAL B CA 1 ATOM 255 C C . VAL B 2 2 ? 29.168 29.488 23.410 1.00 30.69 ? 2 VAL B C 1 ATOM 256 O O . VAL B 2 2 ? 30.163 29.541 24.137 1.00 32.87 ? 2 VAL B O 1 ATOM 257 C CB . VAL B 2 2 ? 28.014 27.285 23.878 1.00 27.67 ? 2 VAL B CB 1 ATOM 258 C CG1 . VAL B 2 2 ? 26.705 27.933 24.291 1.00 26.36 ? 2 VAL B CG1 1 ATOM 259 C CG2 . VAL B 2 2 ? 27.736 25.883 23.355 1.00 25.27 ? 2 VAL B CG2 1 ATOM 260 N N . GLU B 2 3 ? 28.428 30.551 23.087 1.00 32.52 ? 3 GLU B N 1 ATOM 261 C CA . GLU B 2 3 ? 28.610 31.887 23.657 1.00 34.54 ? 3 GLU B CA 1 ATOM 262 C C . GLU B 2 3 ? 29.962 32.487 23.320 1.00 34.02 ? 3 GLU B C 1 ATOM 263 O O . GLU B 2 3 ? 30.526 33.252 24.093 1.00 36.96 ? 3 GLU B O 1 ATOM 264 C CB . GLU B 2 3 ? 28.364 31.880 25.176 1.00 39.16 ? 3 GLU B CB 1 ATOM 265 C CG . GLU B 2 3 ? 26.907 31.598 25.562 1.00 46.79 ? 3 GLU B CG 1 ATOM 266 C CD . GLU B 2 3 ? 26.032 32.837 25.468 1.00 49.55 ? 3 GLU B CD 1 ATOM 267 O OE1 . GLU B 2 3 ? 26.265 33.786 26.249 1.00 50.11 ? 3 GLU B OE1 1 ATOM 268 O OE2 . GLU B 2 3 ? 25.128 32.871 24.605 1.00 53.30 ? 3 GLU B OE2 1 ATOM 269 N N . GLY B 2 4 ? 30.481 32.138 22.155 1.00 32.58 ? 4 GLY B N 1 ATOM 270 C CA . GLY B 2 4 ? 31.730 32.706 21.674 1.00 31.74 ? 4 GLY B CA 1 ATOM 271 C C . GLY B 2 4 ? 31.408 33.824 20.715 1.00 30.95 ? 4 GLY B C 1 ATOM 272 O O . GLY B 2 4 ? 30.301 34.344 20.719 1.00 33.90 ? 4 GLY B O 1 ATOM 273 N N . SER B 2 5 ? 32.369 34.211 19.897 1.00 29.43 ? 5 SER B N 1 ATOM 274 C CA . SER B 2 5 ? 32.076 35.129 18.812 1.00 29.21 ? 5 SER B CA 1 ATOM 275 C C . SER B 2 5 ? 32.931 34.799 17.586 1.00 28.04 ? 5 SER B C 1 ATOM 276 O O . SER B 2 5 ? 33.776 33.906 17.637 1.00 28.28 ? 5 SER B O 1 ATOM 277 C CB . SER B 2 5 ? 32.248 36.582 19.264 1.00 28.26 ? 5 SER B CB 1 ATOM 278 O OG . SER B 2 5 ? 33.579 36.813 19.643 1.00 29.76 ? 5 SER B OG 1 ATOM 279 N N . ASP B 2 6 ? 32.688 35.511 16.492 1.00 26.71 ? 6 ASP B N 1 ATOM 280 C CA . ASP B 2 6 ? 33.371 35.270 15.232 1.00 27.57 ? 6 ASP B CA 1 ATOM 281 C C . ASP B 2 6 ? 34.860 35.545 15.364 1.00 27.15 ? 6 ASP B C 1 ATOM 282 O O . ASP B 2 6 ? 35.249 36.565 15.906 1.00 29.13 ? 6 ASP B O 1 ATOM 283 C CB . ASP B 2 6 ? 32.791 36.183 14.143 1.00 27.55 ? 6 ASP B CB 1 ATOM 284 C CG . ASP B 2 6 ? 31.362 35.820 13.751 1.00 28.05 ? 6 ASP B CG 1 ATOM 285 O OD1 . ASP B 2 6 ? 30.754 34.888 14.321 1.00 27.55 ? 6 ASP B OD1 1 ATOM 286 O OD2 . ASP B 2 6 ? 30.846 36.480 12.835 1.00 30.79 ? 6 ASP B OD2 1 ATOM 287 N N . ALA B 2 7 ? 35.695 34.641 14.885 1.00 25.96 ? 7 ALA B N 1 ATOM 288 C CA . ALA B 2 7 ? 37.107 34.915 14.873 1.00 26.82 ? 7 ALA B CA 1 ATOM 289 C C . ALA B 2 7 ? 37.374 36.020 13.863 1.00 28.72 ? 7 ALA B C 1 ATOM 290 O O . ALA B 2 7 ? 36.634 36.178 12.892 1.00 30.50 ? 7 ALA B O 1 ATOM 291 C CB . ALA B 2 7 ? 37.884 33.671 14.501 1.00 25.98 ? 7 ALA B CB 1 ATOM 292 N N . GLU B 2 8 ? 38.414 36.805 14.103 1.00 29.57 ? 8 GLU B N 1 ATOM 293 C CA . GLU B 2 8 ? 38.974 37.636 13.046 1.00 31.36 ? 8 GLU B CA 1 ATOM 294 C C . GLU B 2 8 ? 39.781 36.754 12.082 1.00 31.28 ? 8 GLU B C 1 ATOM 295 O O . GLU B 2 8 ? 40.250 35.664 12.453 1.00 29.75 ? 8 GLU B O 1 ATOM 296 C CB . GLU B 2 8 ? 39.864 38.711 13.642 1.00 32.32 ? 8 GLU B CB 1 ATOM 297 C CG . GLU B 2 8 ? 39.123 39.625 14.591 1.00 35.41 ? 8 GLU B CG 1 ATOM 298 C CD . GLU B 2 8 ? 40.075 40.466 15.403 1.00 38.06 ? 8 GLU B CD 1 ATOM 299 O OE1 . GLU B 2 8 ? 40.815 41.276 14.812 1.00 42.60 ? 8 GLU B OE1 1 ATOM 300 O OE2 . GLU B 2 8 ? 40.099 40.304 16.630 1.00 39.62 ? 8 GLU B OE2 1 ATOM 301 N N . ILE B 2 9 ? 39.923 37.224 10.848 1.00 31.21 ? 9 ILE B N 1 ATOM 302 C CA . ILE B 2 9 ? 40.698 36.534 9.829 1.00 33.74 ? 9 ILE B CA 1 ATOM 303 C C . ILE B 2 9 ? 42.138 36.374 10.322 1.00 31.99 ? 9 ILE B C 1 ATOM 304 O O . ILE B 2 9 ? 42.732 37.334 10.818 1.00 33.01 ? 9 ILE B O 1 ATOM 305 C CB . ILE B 2 9 ? 40.617 37.303 8.474 1.00 38.35 ? 9 ILE B CB 1 ATOM 306 C CG1 . ILE B 2 9 ? 39.296 36.967 7.766 1.00 42.83 ? 9 ILE B CG1 1 ATOM 307 C CG2 . ILE B 2 9 ? 41.765 36.932 7.549 1.00 39.32 ? 9 ILE B CG2 1 ATOM 308 C CD1 . ILE B 2 9 ? 38.818 37.999 6.760 1.00 45.22 ? 9 ILE B CD1 1 ATOM 309 N N . GLY B 2 10 ? 42.678 35.157 10.228 1.00 30.12 ? 10 GLY B N 1 ATOM 310 C CA . GLY B 2 10 ? 44.076 34.884 10.607 1.00 28.35 ? 10 GLY B CA 1 ATOM 311 C C . GLY B 2 10 ? 44.386 34.829 12.101 1.00 28.03 ? 10 GLY B C 1 ATOM 312 O O . GLY B 2 10 ? 45.552 34.784 12.493 1.00 28.90 ? 10 GLY B O 1 ATOM 313 N N . MET B 2 11 ? 43.343 34.819 12.925 1.00 27.27 ? 11 MET B N 1 ATOM 314 C CA . MET B 2 11 ? 43.443 34.827 14.378 1.00 26.67 ? 11 MET B CA 1 ATOM 315 C C . MET B 2 11 ? 43.958 33.500 14.939 1.00 26.22 ? 11 MET B C 1 ATOM 316 O O . MET B 2 11 ? 44.551 33.458 16.019 1.00 25.76 ? 11 MET B O 1 ATOM 317 C CB . MET B 2 11 ? 42.056 35.070 14.944 1.00 29.26 ? 11 MET B CB 1 ATOM 318 C CG . MET B 2 11 ? 42.013 35.525 16.380 1.00 33.15 ? 11 MET B CG 1 ATOM 319 S SD . MET B 2 11 ? 40.319 35.498 16.985 1.00 37.80 ? 11 MET B SD 1 ATOM 320 C CE . MET B 2 11 ? 40.254 37.070 17.830 1.00 35.39 ? 11 MET B CE 1 ATOM 321 N N . SER B 2 12 ? 43.689 32.418 14.219 1.00 24.97 ? 12 SER B N 1 ATOM 322 C CA . SER B 2 12 ? 44.081 31.088 14.625 1.00 24.66 ? 12 SER B CA 1 ATOM 323 C C . SER B 2 12 ? 44.718 30.371 13.459 1.00 24.21 ? 12 SER B C 1 ATOM 324 O O . SER B 2 12 ? 44.136 29.421 12.934 1.00 25.01 ? 12 SER B O 1 ATOM 325 C CB . SER B 2 12 ? 42.862 30.300 15.027 1.00 25.42 ? 12 SER B CB 1 ATOM 326 O OG . SER B 2 12 ? 42.964 29.960 16.367 1.00 30.07 ? 12 SER B OG 1 ATOM 327 N N . PRO B 2 13 ? 45.916 30.805 13.045 1.00 22.81 ? 13 PRO B N 1 ATOM 328 C CA . PRO B 2 13 ? 46.397 30.235 11.784 1.00 21.38 ? 13 PRO B CA 1 ATOM 329 C C . PRO B 2 13 ? 46.805 28.759 11.881 1.00 21.01 ? 13 PRO B C 1 ATOM 330 O O . PRO B 2 13 ? 47.105 28.163 10.855 1.00 21.57 ? 13 PRO B O 1 ATOM 331 C CB . PRO B 2 13 ? 47.572 31.139 11.404 1.00 21.20 ? 13 PRO B CB 1 ATOM 332 C CG . PRO B 2 13 ? 47.995 31.811 12.675 1.00 21.49 ? 13 PRO B CG 1 ATOM 333 C CD . PRO B 2 13 ? 46.885 31.725 13.678 1.00 21.49 ? 13 PRO B CD 1 ATOM 334 N N . TRP B 2 14 ? 46.787 28.175 13.088 1.00 20.08 ? 14 TRP B N 1 ATOM 335 C CA . TRP B 2 14 ? 47.116 26.749 13.300 1.00 19.42 ? 14 TRP B CA 1 ATOM 336 C C . TRP B 2 14 ? 45.869 25.852 13.376 1.00 19.78 ? 14 TRP B C 1 ATOM 337 O O . TRP B 2 14 ? 45.991 24.637 13.506 1.00 19.32 ? 14 TRP B O 1 ATOM 338 C CB . TRP B 2 14 ? 47.944 26.567 14.583 1.00 18.48 ? 14 TRP B CB 1 ATOM 339 C CG . TRP B 2 14 ? 47.424 27.425 15.668 1.00 18.43 ? 14 TRP B CG 1 ATOM 340 C CD1 . TRP B 2 14 ? 46.303 27.209 16.437 1.00 18.35 ? 14 TRP B CD1 1 ATOM 341 C CD2 . TRP B 2 14 ? 47.955 28.694 16.075 1.00 18.97 ? 14 TRP B CD2 1 ATOM 342 N NE1 . TRP B 2 14 ? 46.112 28.272 17.312 1.00 18.88 ? 14 TRP B NE1 1 ATOM 343 C CE2 . TRP B 2 14 ? 47.108 29.196 17.106 1.00 18.74 ? 14 TRP B CE2 1 ATOM 344 C CE3 . TRP B 2 14 ? 49.068 29.461 15.669 1.00 18.79 ? 14 TRP B CE3 1 ATOM 345 C CZ2 . TRP B 2 14 ? 47.346 30.418 17.736 1.00 18.29 ? 14 TRP B CZ2 1 ATOM 346 C CZ3 . TRP B 2 14 ? 49.309 30.675 16.308 1.00 18.83 ? 14 TRP B CZ3 1 ATOM 347 C CH2 . TRP B 2 14 ? 48.452 31.136 17.332 1.00 18.73 ? 14 TRP B CH2 1 ATOM 348 N N . GLN B 2 15 ? 44.681 26.446 13.316 1.00 20.61 ? 15 GLN B N 1 ATOM 349 C CA . GLN B 2 15 ? 43.424 25.692 13.338 1.00 22.04 ? 15 GLN B CA 1 ATOM 350 C C . GLN B 2 15 ? 43.310 24.844 12.084 1.00 22.58 ? 15 GLN B C 1 ATOM 351 O O . GLN B 2 15 ? 43.510 25.328 10.985 1.00 23.70 ? 15 GLN B O 1 ATOM 352 C CB . GLN B 2 15 ? 42.237 26.649 13.431 1.00 23.69 ? 15 GLN B CB 1 ATOM 353 C CG . GLN B 2 15 ? 40.861 26.010 13.505 1.00 24.85 ? 15 GLN B CG 1 ATOM 354 C CD . GLN B 2 15 ? 40.568 25.385 14.852 1.00 27.02 ? 15 GLN B CD 1 ATOM 355 O OE1 . GLN B 2 15 ? 39.966 24.298 14.939 1.00 29.16 ? 15 GLN B OE1 1 ATOM 356 N NE2 . GLN B 2 15 ? 40.986 26.053 15.912 1.00 26.70 ? 15 GLN B NE2 1 ATOM 357 N N . VAL B 2 16 ? 43.006 23.570 12.268 1.00 22.97 ? 16 VAL B N 1 ATOM 358 C CA . VAL B 2 16 ? 42.842 22.633 11.182 1.00 23.59 ? 16 VAL B CA 1 ATOM 359 C C . VAL B 2 16 ? 41.415 22.078 11.273 1.00 25.12 ? 16 VAL B C 1 ATOM 360 O O . VAL B 2 16 ? 40.881 21.935 12.376 1.00 26.73 ? 16 VAL B O 1 ATOM 361 C CB . VAL B 2 16 ? 43.884 21.501 11.316 1.00 23.24 ? 16 VAL B CB 1 ATOM 362 C CG1 . VAL B 2 16 ? 43.595 20.337 10.371 1.00 22.15 ? 16 VAL B CG1 1 ATOM 363 C CG2 . VAL B 2 16 ? 45.277 22.051 11.066 1.00 22.73 ? 16 VAL B CG2 1 ATOM 364 N N . MET B 2 17 ? 40.793 21.818 10.122 1.00 25.30 ? 17 MET B N 1 ATOM 365 C CA . MET B 2 17 ? 39.495 21.141 10.049 1.00 25.68 ? 17 MET B CA 1 ATOM 366 C C . MET B 2 17 ? 39.713 19.695 9.601 1.00 25.78 ? 17 MET B C 1 ATOM 367 O O . MET B 2 17 ? 40.406 19.446 8.611 1.00 25.06 ? 17 MET B O 1 ATOM 368 C CB . MET B 2 17 ? 38.567 21.860 9.054 1.00 25.89 ? 17 MET B CB 1 ATOM 369 C CG . MET B 2 17 ? 37.222 21.173 8.831 1.00 26.39 ? 17 MET B CG 1 ATOM 370 S SD . MET B 2 17 ? 36.107 21.996 7.655 1.00 27.83 ? 17 MET B SD 1 ATOM 371 C CE . MET B 2 17 ? 35.679 23.503 8.538 1.00 25.43 ? 17 MET B CE 1 ATOM 372 N N . LEU B 2 18 ? 39.138 18.745 10.336 1.00 27.17 ? 18 LEU B N 1 ATOM 373 C CA . LEU B 2 18 ? 39.113 17.347 9.894 1.00 28.86 ? 18 LEU B CA 1 ATOM 374 C C . LEU B 2 18 ? 37.837 17.095 9.130 1.00 28.28 ? 18 LEU B C 1 ATOM 375 O O . LEU B 2 18 ? 36.727 17.275 9.660 1.00 28.17 ? 18 LEU B O 1 ATOM 376 C CB . LEU B 2 18 ? 39.193 16.364 11.065 1.00 31.44 ? 18 LEU B CB 1 ATOM 377 C CG . LEU B 2 18 ? 40.510 16.278 11.821 1.00 34.11 ? 18 LEU B CG 1 ATOM 378 C CD1 . LEU B 2 18 ? 40.492 15.051 12.718 1.00 35.85 ? 18 LEU B CD1 1 ATOM 379 C CD2 . LEU B 2 18 ? 41.675 16.217 10.843 1.00 34.38 ? 18 LEU B CD2 1 ATOM 380 N N . PHE B 2 19 ? 38.007 16.641 7.900 1.00 27.21 ? 19 PHE B N 1 ATOM 381 C CA . PHE B 2 19 ? 36.908 16.578 6.958 1.00 28.09 ? 19 PHE B CA 1 ATOM 382 C C . PHE B 2 19 ? 36.750 15.176 6.370 1.00 28.19 ? 19 PHE B C 1 ATOM 383 O O . PHE B 2 19 ? 37.685 14.623 5.778 1.00 28.73 ? 19 PHE B O 1 ATOM 384 C CB . PHE B 2 19 ? 37.186 17.592 5.867 1.00 28.15 ? 19 PHE B CB 1 ATOM 385 C CG . PHE B 2 19 ? 36.023 17.881 4.979 1.00 28.10 ? 19 PHE B CG 1 ATOM 386 C CD1 . PHE B 2 19 ? 34.957 18.644 5.436 1.00 27.65 ? 19 PHE B CD1 1 ATOM 387 C CD2 . PHE B 2 19 ? 36.021 17.435 3.665 1.00 28.46 ? 19 PHE B CD2 1 ATOM 388 C CE1 . PHE B 2 19 ? 33.886 18.940 4.605 1.00 29.08 ? 19 PHE B CE1 1 ATOM 389 C CE2 . PHE B 2 19 ? 34.955 17.727 2.823 1.00 30.72 ? 19 PHE B CE2 1 ATOM 390 C CZ . PHE B 2 19 ? 33.881 18.483 3.292 1.00 29.53 ? 19 PHE B CZ 1 ATOM 391 N N . ARG B 2 20 ? 35.569 14.604 6.564 1.00 28.03 ? 20 ARG B N 1 ATOM 392 C CA . ARG B 2 20 ? 35.228 13.297 6.026 1.00 30.30 ? 20 ARG B CA 1 ATOM 393 C C . ARG B 2 20 ? 34.910 13.392 4.530 1.00 32.27 ? 20 ARG B C 1 ATOM 394 O O . ARG B 2 20 ? 34.237 14.338 4.090 1.00 31.75 ? 20 ARG B O 1 ATOM 395 C CB . ARG B 2 20 ? 34.035 12.753 6.784 1.00 32.37 ? 20 ARG B CB 1 ATOM 396 C CG . ARG B 2 20 ? 33.687 11.313 6.475 1.00 35.89 ? 20 ARG B CG 1 ATOM 397 C CD . ARG B 2 20 ? 32.462 10.954 7.289 1.00 37.82 ? 20 ARG B CD 1 ATOM 398 N NE . ARG B 2 20 ? 32.157 9.536 7.209 1.00 43.31 ? 20 ARG B NE 1 ATOM 399 C CZ . ARG B 2 20 ? 31.305 8.913 8.018 1.00 45.30 ? 20 ARG B CZ 1 ATOM 400 N NH1 . ARG B 2 20 ? 30.661 9.585 8.968 1.00 43.35 ? 20 ARG B NH1 1 ATOM 401 N NH2 . ARG B 2 20 ? 31.105 7.615 7.874 1.00 43.50 ? 20 ARG B NH2 1 ATOM 402 N N . LYS B 2 21 ? 35.412 12.433 3.752 1.00 32.77 ? 21 LYS B N 1 ATOM 403 C CA . LYS B 2 21 ? 35.197 12.431 2.307 1.00 36.50 ? 21 LYS B CA 1 ATOM 404 C C . LYS B 2 21 ? 33.764 12.107 1.874 1.00 39.85 ? 21 LYS B C 1 ATOM 405 O O . LYS B 2 21 ? 33.197 12.793 1.012 1.00 42.23 ? 21 LYS B O 1 ATOM 406 C CB . LYS B 2 21 ? 36.141 11.461 1.632 1.00 35.80 ? 21 LYS B CB 1 ATOM 407 C CG . LYS B 2 21 ? 37.559 11.948 1.584 1.00 35.45 ? 21 LYS B CG 1 ATOM 408 C CD . LYS B 2 21 ? 38.435 10.833 1.078 1.00 36.29 ? 21 LYS B CD 1 ATOM 409 C CE . LYS B 2 21 ? 39.828 11.347 0.804 1.00 38.29 ? 21 LYS B CE 1 ATOM 410 N NZ . LYS B 2 21 ? 40.513 10.389 -0.085 1.00 39.63 ? 21 LYS B NZ 1 ATOM 411 N N . SER B 2 22 ? 33.192 11.061 2.465 1.00 41.36 ? 22 SER B N 1 ATOM 412 C CA . SER B 2 22 ? 31.909 10.531 2.028 1.00 42.75 ? 22 SER B CA 1 ATOM 413 C C . SER B 2 22 ? 31.214 9.832 3.190 1.00 41.67 ? 22 SER B C 1 ATOM 414 O O . SER B 2 22 ? 31.731 8.851 3.704 1.00 41.82 ? 22 SER B O 1 ATOM 415 C CB . SER B 2 22 ? 32.124 9.546 0.868 1.00 44.84 ? 22 SER B CB 1 ATOM 416 O OG . SER B 2 22 ? 30.963 9.454 0.059 1.00 49.43 ? 22 SER B OG 1 ATOM 417 N N . PRO B 2 23 ? 30.069 10.368 3.655 1.00 42.65 ? 23 PRO B N 1 ATOM 418 C CA . PRO B 2 23 ? 29.490 11.653 3.252 1.00 43.37 ? 23 PRO B CA 1 ATOM 419 C C . PRO B 2 23 ? 30.377 12.839 3.676 1.00 44.78 ? 23 PRO B C 1 ATOM 420 O O . PRO B 2 23 ? 31.127 12.725 4.648 1.00 46.46 ? 23 PRO B O 1 ATOM 421 C CB . PRO B 2 23 ? 28.155 11.688 4.008 1.00 40.93 ? 23 PRO B CB 1 ATOM 422 C CG . PRO B 2 23 ? 28.333 10.780 5.171 1.00 39.92 ? 23 PRO B CG 1 ATOM 423 C CD . PRO B 2 23 ? 29.284 9.713 4.725 1.00 40.80 ? 23 PRO B CD 1 ATOM 424 N N . GLN B 2 24 ? 30.304 13.950 2.942 1.00 44.12 ? 24 GLN B N 1 ATOM 425 C CA . GLN B 2 24 ? 31.037 15.163 3.296 1.00 43.07 ? 24 GLN B CA 1 ATOM 426 C C . GLN B 2 24 ? 30.480 15.780 4.571 1.00 43.31 ? 24 GLN B C 1 ATOM 427 O O . GLN B 2 24 ? 29.335 16.231 4.597 1.00 43.58 ? 24 GLN B O 1 ATOM 428 C CB . GLN B 2 24 ? 30.993 16.169 2.161 1.00 43.21 ? 24 GLN B CB 1 ATOM 429 C CG . GLN B 2 24 ? 31.973 15.860 1.052 1.00 49.30 ? 24 GLN B CG 1 ATOM 430 C CD . GLN B 2 24 ? 31.698 16.662 -0.203 1.00 54.76 ? 24 GLN B CD 1 ATOM 431 O OE1 . GLN B 2 24 ? 32.300 17.717 -0.447 1.00 60.61 ? 24 GLN B OE1 1 ATOM 432 N NE2 . GLN B 2 24 ? 30.777 16.168 -1.007 1.00 57.95 ? 24 GLN B NE2 1 ATOM 433 N N . GLU B 2 25 ? 31.285 15.769 5.634 1.00 43.04 ? 25 GLU B N 1 ATOM 434 C CA . GLU B 2 25 ? 30.911 16.410 6.898 1.00 42.80 ? 25 GLU B CA 1 ATOM 435 C C . GLU B 2 25 ? 32.137 16.849 7.700 1.00 40.42 ? 25 GLU B C 1 ATOM 436 O O . GLU B 2 25 ? 33.237 16.329 7.495 1.00 40.54 ? 25 GLU B O 1 ATOM 437 C CB . GLU B 2 25 ? 30.004 15.499 7.736 1.00 44.79 ? 25 GLU B CB 1 ATOM 438 C CG . GLU B 2 25 ? 30.667 14.219 8.202 1.00 52.49 ? 25 GLU B CG 1 ATOM 439 C CD . GLU B 2 25 ? 29.721 13.289 8.944 1.00 58.04 ? 25 GLU B CD 1 ATOM 440 O OE1 . GLU B 2 25 ? 28.505 13.573 8.966 1.00 60.26 ? 25 GLU B OE1 1 ATOM 441 O OE2 . GLU B 2 25 ? 30.201 12.270 9.503 1.00 59.03 ? 25 GLU B OE2 1 ATOM 442 N N . LEU B 2 26 ? 31.943 17.826 8.589 1.00 36.52 ? 26 LEU B N 1 ATOM 443 C CA . LEU B 2 26 ? 32.963 18.230 9.543 1.00 32.88 ? 26 LEU B CA 1 ATOM 444 C C . LEU B 2 26 ? 33.058 17.156 10.613 1.00 32.03 ? 26 LEU B C 1 ATOM 445 O O . LEU B 2 26 ? 32.062 16.822 11.222 1.00 31.59 ? 26 LEU B O 1 ATOM 446 C CB . LEU B 2 26 ? 32.613 19.576 10.191 1.00 32.16 ? 26 LEU B CB 1 ATOM 447 C CG . LEU B 2 26 ? 33.368 19.883 11.500 1.00 31.00 ? 26 LEU B CG 1 ATOM 448 C CD1 . LEU B 2 26 ? 34.776 20.366 11.229 1.00 27.73 ? 26 LEU B CD1 1 ATOM 449 C CD2 . LEU B 2 26 ? 32.607 20.889 12.351 1.00 32.52 ? 26 LEU B CD2 1 ATOM 450 N N . LEU B 2 27 ? 34.251 16.620 10.847 1.00 31.64 ? 27 LEU B N 1 ATOM 451 C CA . LEU B 2 27 ? 34.420 15.588 11.863 1.00 30.46 ? 27 LEU B CA 1 ATOM 452 C C . LEU B 2 27 ? 34.848 16.146 13.212 1.00 28.96 ? 27 LEU B C 1 ATOM 453 O O . LEU B 2 27 ? 34.347 15.713 14.250 1.00 27.06 ? 27 LEU B O 1 ATOM 454 C CB . LEU B 2 27 ? 35.466 14.576 11.416 1.00 33.97 ? 27 LEU B CB 1 ATOM 455 C CG . LEU B 2 27 ? 35.088 13.382 10.549 1.00 37.53 ? 27 LEU B CG 1 ATOM 456 C CD1 . LEU B 2 27 ? 36.191 12.362 10.734 1.00 38.69 ? 27 LEU B CD1 1 ATOM 457 C CD2 . LEU B 2 27 ? 33.746 12.765 10.945 1.00 38.84 ? 27 LEU B CD2 1 ATOM 458 N N . CYS B 2 28 ? 35.782 17.106 13.178 1.00 27.77 ? 28 CYS B N 1 ATOM 459 C CA . CYS B 2 28 ? 36.580 17.524 14.339 1.00 25.21 ? 28 CYS B CA 1 ATOM 460 C C . CYS B 2 28 ? 37.506 18.694 14.000 1.00 24.80 ? 28 CYS B C 1 ATOM 461 O O . CYS B 2 28 ? 37.805 18.954 12.824 1.00 23.82 ? 28 CYS B O 1 ATOM 462 C CB . CYS B 2 28 ? 37.442 16.351 14.815 1.00 24.81 ? 28 CYS B CB 1 ATOM 463 S SG . CYS B 2 28 ? 36.682 15.312 16.101 1.00 25.89 ? 28 CYS B SG 1 ATOM 464 N N . GLY B 2 29 ? 37.979 19.382 15.038 1.00 24.38 ? 29 GLY B N 1 ATOM 465 C CA . GLY B 2 29 ? 39.095 20.322 14.912 1.00 22.49 ? 29 GLY B CA 1 ATOM 466 C C . GLY B 2 29 ? 40.422 19.600 15.089 1.00 23.47 ? 29 GLY B C 1 ATOM 467 O O . GLY B 2 29 ? 40.470 18.406 15.442 1.00 23.85 ? 29 GLY B O 1 ATOM 468 N N . ALA B 2 30 ? 41.503 20.328 14.846 1.00 23.02 ? 30 ALA B N 1 ATOM 469 C CA . ALA B 2 30 ? 42.853 19.840 15.039 1.00 22.67 ? 30 ALA B CA 1 ATOM 470 C C . ALA B 2 30 ? 43.764 21.069 15.040 1.00 23.96 ? 30 ALA B C 1 ATOM 471 O O . ALA B 2 30 ? 43.281 22.198 14.851 1.00 23.21 ? 30 ALA B O 1 ATOM 472 C CB . ALA B 2 30 ? 43.222 18.909 13.897 1.00 22.43 ? 30 ALA B CB 1 ATOM 473 N N . SER B 2 31 ? 45.071 20.867 15.233 1.00 23.61 ? 31 SER B N 1 ATOM 474 C CA . SER B 2 31 ? 46.019 21.987 15.153 1.00 23.47 ? 31 SER B CA 1 ATOM 475 C C . SER B 2 31 ? 47.304 21.616 14.433 1.00 23.16 ? 31 SER B C 1 ATOM 476 O O . SER B 2 31 ? 47.765 20.475 14.519 1.00 23.79 ? 31 SER B O 1 ATOM 477 C CB . SER B 2 31 ? 46.348 22.542 16.536 1.00 22.88 ? 31 SER B CB 1 ATOM 478 O OG . SER B 2 31 ? 46.878 21.505 17.326 1.00 24.79 ? 31 SER B OG 1 ATOM 479 N N . LEU B 2 32 ? 47.866 22.595 13.728 1.00 22.21 ? 32 LEU B N 1 ATOM 480 C CA . LEU B 2 32 ? 49.116 22.438 13.005 1.00 22.29 ? 32 LEU B CA 1 ATOM 481 C C . LEU B 2 32 ? 50.324 22.694 13.919 1.00 23.09 ? 32 LEU B C 1 ATOM 482 O O . LEU B 2 32 ? 50.452 23.777 14.488 1.00 23.35 ? 32 LEU B O 1 ATOM 483 C CB . LEU B 2 32 ? 49.120 23.412 11.835 1.00 21.76 ? 32 LEU B CB 1 ATOM 484 C CG . LEU B 2 32 ? 50.207 23.247 10.778 1.00 22.09 ? 32 LEU B CG 1 ATOM 485 C CD1 . LEU B 2 32 ? 50.036 21.953 9.983 1.00 21.23 ? 32 LEU B CD1 1 ATOM 486 C CD2 . LEU B 2 32 ? 50.216 24.470 9.863 1.00 22.11 ? 32 LEU B CD2 1 ATOM 487 N N . ILE B 2 33 ? 51.201 21.702 14.076 1.00 24.37 ? 33 ILE B N 1 ATOM 488 C CA . ILE B 2 33 ? 52.372 21.874 14.949 1.00 26.25 ? 33 ILE B CA 1 ATOM 489 C C . ILE B 2 33 ? 53.716 21.955 14.211 1.00 28.35 ? 33 ILE B C 1 ATOM 490 O O . ILE B 2 33 ? 54.709 22.409 14.775 1.00 30.49 ? 33 ILE B O 1 ATOM 491 C CB . ILE B 2 33 ? 52.432 20.846 16.100 1.00 25.29 ? 33 ILE B CB 1 ATOM 492 C CG1 . ILE B 2 33 ? 52.613 19.433 15.552 1.00 25.60 ? 33 ILE B CG1 1 ATOM 493 C CG2 . ILE B 2 33 ? 51.205 20.988 16.995 1.00 24.41 ? 33 ILE B CG2 1 ATOM 494 C CD1 . ILE B 2 33 ? 52.827 18.387 16.625 1.00 26.13 ? 33 ILE B CD1 1 ATOM 495 N N . SER B 2 34 ? 53.747 21.516 12.962 1.00 29.64 ? 34 SER B N 1 ATOM 496 C CA . SER B 2 34 ? 54.885 21.761 12.071 1.00 30.90 ? 34 SER B CA 1 ATOM 497 C C . SER B 2 34 ? 54.360 21.714 10.647 1.00 33.06 ? 34 SER B C 1 ATOM 498 O O . SER B 2 34 ? 53.143 21.723 10.433 1.00 35.99 ? 34 SER B O 1 ATOM 499 C CB . SER B 2 34 ? 55.995 20.734 12.283 1.00 30.05 ? 34 SER B CB 1 ATOM 500 O OG . SER B 2 34 ? 55.642 19.480 11.751 1.00 30.89 ? 34 SER B OG 1 ATOM 501 N N . ASP B 2 35 ? 55.245 21.657 9.664 1.00 33.62 ? 35 ASP B N 1 ATOM 502 C CA . ASP B 2 35 ? 54.776 21.596 8.276 1.00 33.18 ? 35 ASP B CA 1 ATOM 503 C C . ASP B 2 35 ? 54.232 20.218 7.839 1.00 31.48 ? 35 ASP B C 1 ATOM 504 O O . ASP B 2 35 ? 53.613 20.113 6.789 1.00 32.37 ? 35 ASP B O 1 ATOM 505 C CB . ASP B 2 35 ? 55.840 22.126 7.303 1.00 35.28 ? 35 ASP B CB 1 ATOM 506 C CG . ASP B 2 35 ? 57.069 21.210 7.178 1.00 37.58 ? 35 ASP B CG 1 ATOM 507 O OD1 . ASP B 2 35 ? 57.279 20.255 7.960 1.00 38.44 ? 35 ASP B OD1 1 ATOM 508 O OD2 . ASP B 2 35 ? 57.845 21.453 6.246 1.00 42.19 ? 35 ASP B OD2 1 ATOM 509 N N A ARG B 2 36 ? 54.443 19.174 8.634 0.50 30.33 ? 36 ARG B N 1 ATOM 510 N N B ARG B 2 36 ? 54.468 19.200 8.668 0.50 31.16 ? 36 ARG B N 1 ATOM 511 C CA A ARG B 2 36 ? 53.918 17.850 8.270 0.50 30.15 ? 36 ARG B CA 1 ATOM 512 C CA B ARG B 2 36 ? 54.126 17.809 8.356 0.50 31.57 ? 36 ARG B CA 1 ATOM 513 C C A ARG B 2 36 ? 53.169 17.119 9.377 0.50 29.24 ? 36 ARG B C 1 ATOM 514 C C B ARG B 2 36 ? 53.154 17.163 9.348 0.50 30.04 ? 36 ARG B C 1 ATOM 515 O O A ARG B 2 36 ? 52.750 15.982 9.181 0.50 29.26 ? 36 ARG B O 1 ATOM 516 O O B ARG B 2 36 ? 52.563 16.132 9.040 0.50 29.96 ? 36 ARG B O 1 ATOM 517 C CB A ARG B 2 36 ? 55.020 16.948 7.707 0.50 31.10 ? 36 ARG B CB 1 ATOM 518 C CB B ARG B 2 36 ? 55.397 16.947 8.305 0.50 33.61 ? 36 ARG B CB 1 ATOM 519 C CG A ARG B 2 36 ? 55.341 17.247 6.254 0.50 32.11 ? 36 ARG B CG 1 ATOM 520 C CG B ARG B 2 36 ? 56.261 17.159 7.075 0.50 36.48 ? 36 ARG B CG 1 ATOM 521 C CD A ARG B 2 36 ? 56.286 16.229 5.643 0.50 32.45 ? 36 ARG B CD 1 ATOM 522 C CD B ARG B 2 36 ? 57.391 16.141 6.998 0.50 38.96 ? 36 ARG B CD 1 ATOM 523 N NE A ARG B 2 36 ? 55.635 14.957 5.367 0.50 31.71 ? 36 ARG B NE 1 ATOM 524 N NE B ARG B 2 36 ? 58.562 16.549 7.770 0.50 39.62 ? 36 ARG B NE 1 ATOM 525 C CZ A ARG B 2 36 ? 56.259 13.941 4.789 0.50 32.21 ? 36 ARG B CZ 1 ATOM 526 C CZ B ARG B 2 36 ? 59.507 17.360 7.305 0.50 39.93 ? 36 ARG B CZ 1 ATOM 527 N NH1 A ARG B 2 36 ? 57.529 14.075 4.443 0.50 32.05 ? 36 ARG B NH1 1 ATOM 528 N NH1 B ARG B 2 36 ? 59.412 17.852 6.075 0.50 37.79 ? 36 ARG B NH1 1 ATOM 529 N NH2 A ARG B 2 36 ? 55.626 12.799 4.567 0.50 32.01 ? 36 ARG B NH2 1 ATOM 530 N NH2 B ARG B 2 36 ? 60.543 17.682 8.072 0.50 40.23 ? 36 ARG B NH2 1 ATOM 531 N N . TRP B 2 37 ? 52.999 17.756 10.531 1.00 27.95 ? 37 TRP B N 1 ATOM 532 C CA . TRP B 2 37 ? 52.290 17.107 11.627 1.00 26.05 ? 37 TRP B CA 1 ATOM 533 C C . TRP B 2 37 ? 51.090 17.866 12.150 1.00 24.38 ? 37 TRP B C 1 ATOM 534 O O . TRP B 2 37 ? 51.152 19.081 12.339 1.00 24.59 ? 37 TRP B O 1 ATOM 535 C CB . TRP B 2 37 ? 53.249 16.816 12.771 1.00 27.21 ? 37 TRP B CB 1 ATOM 536 C CG . TRP B 2 37 ? 54.286 15.801 12.411 1.00 28.32 ? 37 TRP B CG 1 ATOM 537 C CD1 . TRP B 2 37 ? 55.530 16.039 11.877 1.00 27.75 ? 37 TRP B CD1 1 ATOM 538 C CD2 . TRP B 2 37 ? 54.171 14.385 12.553 1.00 27.74 ? 37 TRP B CD2 1 ATOM 539 N NE1 . TRP B 2 37 ? 56.192 14.852 11.680 1.00 27.98 ? 37 TRP B NE1 1 ATOM 540 C CE2 . TRP B 2 37 ? 55.382 13.820 12.088 1.00 28.88 ? 37 TRP B CE2 1 ATOM 541 C CE3 . TRP B 2 37 ? 53.164 13.536 13.028 1.00 28.45 ? 37 TRP B CE3 1 ATOM 542 C CZ2 . TRP B 2 37 ? 55.615 12.430 12.090 1.00 28.79 ? 37 TRP B CZ2 1 ATOM 543 C CZ3 . TRP B 2 37 ? 53.392 12.148 13.024 1.00 28.75 ? 37 TRP B CZ3 1 ATOM 544 C CH2 . TRP B 2 37 ? 54.610 11.616 12.562 1.00 28.47 ? 37 TRP B CH2 1 ATOM 545 N N . VAL B 2 38 ? 50.008 17.129 12.393 1.00 22.30 ? 38 VAL B N 1 ATOM 546 C CA . VAL B 2 38 ? 48.769 17.689 12.915 1.00 21.70 ? 38 VAL B CA 1 ATOM 547 C C . VAL B 2 38 ? 48.407 16.973 14.201 1.00 21.55 ? 38 VAL B C 1 ATOM 548 O O . VAL B 2 38 ? 48.514 15.749 14.304 1.00 21.63 ? 38 VAL B O 1 ATOM 549 C CB . VAL B 2 38 ? 47.630 17.599 11.864 1.00 21.89 ? 38 VAL B CB 1 ATOM 550 C CG1 . VAL B 2 38 ? 46.266 17.931 12.456 1.00 20.17 ? 38 VAL B CG1 1 ATOM 551 C CG2 . VAL B 2 38 ? 47.934 18.514 10.680 1.00 21.38 ? 38 VAL B CG2 1 ATOM 552 N N . LEU B 2 39 ? 47.999 17.745 15.196 1.00 21.82 ? 39 LEU B N 1 ATOM 553 C CA . LEU B 2 39 ? 47.639 17.190 16.495 1.00 21.74 ? 39 LEU B CA 1 ATOM 554 C C . LEU B 2 39 ? 46.121 17.244 16.693 1.00 23.38 ? 39 LEU B C 1 ATOM 555 O O . LEU B 2 39 ? 45.491 18.294 16.444 1.00 25.22 ? 39 LEU B O 1 ATOM 556 C CB . LEU B 2 39 ? 48.365 17.965 17.586 1.00 20.61 ? 39 LEU B CB 1 ATOM 557 C CG . LEU B 2 39 ? 48.198 17.561 19.049 1.00 21.26 ? 39 LEU B CG 1 ATOM 558 C CD1 . LEU B 2 39 ? 48.702 16.136 19.300 1.00 19.88 ? 39 LEU B CD1 1 ATOM 559 C CD2 . LEU B 2 39 ? 48.891 18.594 19.948 1.00 20.33 ? 39 LEU B CD2 1 ATOM 560 N N . THR B 2 40 ? 45.531 16.121 17.116 1.00 22.79 ? 40 THR B N 1 ATOM 561 C CA . THR B 2 40 ? 44.088 16.059 17.366 1.00 22.83 ? 40 THR B CA 1 ATOM 562 C C . THR B 2 40 ? 43.742 15.151 18.560 1.00 22.86 ? 40 THR B C 1 ATOM 563 O O . THR B 2 40 ? 44.640 14.659 19.232 1.00 22.52 ? 40 THR B O 1 ATOM 564 C CB . THR B 2 40 ? 43.299 15.661 16.087 1.00 22.83 ? 40 THR B CB 1 ATOM 565 O OG1 . THR B 2 40 ? 41.906 15.878 16.319 1.00 23.84 ? 40 THR B OG1 1 ATOM 566 C CG2 . THR B 2 40 ? 43.499 14.198 15.731 1.00 22.15 ? 40 THR B CG2 1 ATOM 567 N N . ALA B 2 41 ? 42.449 14.960 18.840 1.00 23.14 ? 41 ALA B N 1 ATOM 568 C CA . ALA B 2 41 ? 42.000 14.010 19.870 1.00 23.80 ? 41 ALA B CA 1 ATOM 569 C C . ALA B 2 41 ? 41.898 12.606 19.280 1.00 26.44 ? 41 ALA B C 1 ATOM 570 O O . ALA B 2 41 ? 41.499 12.453 18.118 1.00 26.45 ? 41 ALA B O 1 ATOM 571 C CB . ALA B 2 41 ? 40.659 14.426 20.451 1.00 21.86 ? 41 ALA B CB 1 ATOM 572 N N . ALA B 2 42 ? 42.257 11.584 20.072 1.00 28.52 ? 42 ALA B N 1 ATOM 573 C CA . ALA B 2 42 ? 42.148 10.181 19.631 1.00 28.97 ? 42 ALA B CA 1 ATOM 574 C C . ALA B 2 42 ? 40.698 9.804 19.263 1.00 29.98 ? 42 ALA B C 1 ATOM 575 O O . ALA B 2 42 ? 40.452 9.123 18.249 1.00 30.77 ? 42 ALA B O 1 ATOM 576 C CB . ALA B 2 42 ? 42.697 9.230 20.687 1.00 27.40 ? 42 ALA B CB 1 ATOM 577 N N . HIS B 2 43 ? 39.748 10.280 20.062 1.00 28.83 ? 43 HIS B N 1 ATOM 578 C CA . HIS B 2 43 ? 38.359 9.892 19.899 1.00 30.42 ? 43 HIS B CA 1 ATOM 579 C C . HIS B 2 43 ? 37.704 10.448 18.617 1.00 31.58 ? 43 HIS B C 1 ATOM 580 O O . HIS B 2 43 ? 36.622 9.994 18.230 1.00 30.91 ? 43 HIS B O 1 ATOM 581 C CB . HIS B 2 43 ? 37.550 10.259 21.150 1.00 30.18 ? 43 HIS B CB 1 ATOM 582 C CG . HIS B 2 43 ? 37.038 11.662 21.146 1.00 31.30 ? 43 HIS B CG 1 ATOM 583 N ND1 . HIS B 2 43 ? 37.721 12.706 21.735 1.00 30.83 ? 43 HIS B ND1 1 ATOM 584 C CD2 . HIS B 2 43 ? 35.906 12.195 20.624 1.00 30.31 ? 43 HIS B CD2 1 ATOM 585 C CE1 . HIS B 2 43 ? 37.033 13.822 21.571 1.00 30.82 ? 43 HIS B CE1 1 ATOM 586 N NE2 . HIS B 2 43 ? 35.927 13.538 20.905 1.00 31.20 ? 43 HIS B NE2 1 ATOM 587 N N . CYS B 2 44 ? 38.359 11.417 17.968 1.00 30.49 ? 44 CYS B N 1 ATOM 588 C CA . CYS B 2 44 ? 37.961 11.857 16.629 1.00 29.01 ? 44 CYS B CA 1 ATOM 589 C C . CYS B 2 44 ? 38.138 10.766 15.571 1.00 30.80 ? 44 CYS B C 1 ATOM 590 O O . CYS B 2 44 ? 37.456 10.789 14.547 1.00 33.09 ? 44 CYS B O 1 ATOM 591 C CB . CYS B 2 44 ? 38.746 13.093 16.197 1.00 27.01 ? 44 CYS B CB 1 ATOM 592 S SG . CYS B 2 44 ? 38.298 14.581 17.104 1.00 26.62 ? 44 CYS B SG 1 ATOM 593 N N . LEU B 2 45 ? 39.040 9.815 15.809 1.00 31.27 ? 45 LEU B N 1 ATOM 594 C CA . LEU B 2 45 ? 39.379 8.809 14.798 1.00 31.89 ? 45 LEU B CA 1 ATOM 595 C C . LEU B 2 45 ? 38.936 7.395 15.187 1.00 34.32 ? 45 LEU B C 1 ATOM 596 O O . LEU B 2 45 ? 38.588 6.588 14.324 1.00 32.73 ? 45 LEU B O 1 ATOM 597 C CB . LEU B 2 45 ? 40.882 8.820 14.535 1.00 31.71 ? 45 LEU B CB 1 ATOM 598 C CG . LEU B 2 45 ? 41.478 10.193 14.190 1.00 33.14 ? 45 LEU B CG 1 ATOM 599 C CD1 . LEU B 2 45 ? 42.953 10.237 14.509 1.00 30.23 ? 45 LEU B CD1 1 ATOM 600 C CD2 . LEU B 2 45 ? 41.215 10.566 12.731 1.00 31.77 ? 45 LEU B CD2 1 ATOM 601 N N . LEU B 2 46 ? 38.958 7.113 16.487 1.00 36.09 ? 46 LEU B N 1 ATOM 602 C CA . LEU B 2 46 ? 38.734 5.777 17.011 1.00 38.12 ? 46 LEU B CA 1 ATOM 603 C C . LEU B 2 46 ? 37.878 5.835 18.258 1.00 40.15 ? 46 LEU B C 1 ATOM 604 O O . LEU B 2 46 ? 38.323 6.305 19.309 1.00 41.39 ? 46 LEU B O 1 ATOM 605 C CB . LEU B 2 46 ? 40.069 5.105 17.349 1.00 40.55 ? 46 LEU B CB 1 ATOM 606 C CG . LEU B 2 46 ? 40.038 3.666 17.902 1.00 42.92 ? 46 LEU B CG 1 ATOM 607 C CD1 . LEU B 2 46 ? 39.664 2.662 16.812 1.00 42.29 ? 46 LEU B CD1 1 ATOM 608 C CD2 . LEU B 2 46 ? 41.378 3.300 18.526 1.00 42.75 ? 46 LEU B CD2 1 ATOM 609 N N . TYR B 2 47 ? 36.641 5.378 18.131 1.00 43.79 ? 47 TYR B N 1 ATOM 610 C CA . TYR B 2 47 ? 35.778 5.165 19.285 1.00 51.76 ? 47 TYR B CA 1 ATOM 611 C C . TYR B 2 47 ? 34.874 3.958 19.010 1.00 56.08 ? 47 TYR B C 1 ATOM 612 O O . TYR B 2 47 ? 33.805 4.118 18.414 1.00 56.08 ? 47 TYR B O 1 ATOM 613 C CB . TYR B 2 47 ? 34.960 6.421 19.597 1.00 51.23 ? 47 TYR B CB 1 ATOM 614 C CG . TYR B 2 47 ? 34.186 6.345 20.885 1.00 55.32 ? 47 TYR B CG 1 ATOM 615 C CD1 . TYR B 2 47 ? 34.846 6.330 22.112 1.00 57.10 ? 47 TYR B CD1 1 ATOM 616 C CD2 . TYR B 2 47 ? 32.791 6.277 20.881 1.00 58.60 ? 47 TYR B CD2 1 ATOM 617 C CE1 . TYR B 2 47 ? 34.143 6.255 23.302 1.00 62.23 ? 47 TYR B CE1 1 ATOM 618 C CE2 . TYR B 2 47 ? 32.071 6.206 22.069 1.00 61.59 ? 47 TYR B CE2 1 ATOM 619 C CZ . TYR B 2 47 ? 32.757 6.197 23.279 1.00 63.97 ? 47 TYR B CZ 1 ATOM 620 O OH . TYR B 2 47 ? 32.071 6.128 24.471 1.00 64.21 ? 47 TYR B OH 1 ATOM 621 N N . PRO B 2 48 ? 35.313 2.744 19.423 1.00 58.55 ? 48 PRO B N 1 ATOM 622 C CA . PRO B 2 48 ? 34.563 1.506 19.122 1.00 60.97 ? 48 PRO B CA 1 ATOM 623 C C . PRO B 2 48 ? 33.100 1.427 19.624 1.00 63.61 ? 48 PRO B C 1 ATOM 624 O O . PRO B 2 48 ? 32.263 0.897 18.896 1.00 66.00 ? 48 PRO B O 1 ATOM 625 C CB . PRO B 2 48 ? 35.439 0.403 19.722 1.00 58.09 ? 48 PRO B CB 1 ATOM 626 C CG . PRO B 2 48 ? 36.815 0.982 19.703 1.00 57.83 ? 48 PRO B CG 1 ATOM 627 C CD . PRO B 2 48 ? 36.629 2.443 20.019 1.00 55.95 ? 48 PRO B CD 1 ATOM 628 N N . PRO B 2 49 ? 32.777 1.965 20.824 1.00 65.99 ? 49 PRO B N 1 ATOM 629 C CA . PRO B 2 49 ? 31.356 1.929 21.225 1.00 70.30 ? 49 PRO B CA 1 ATOM 630 C C . PRO B 2 49 ? 30.340 2.481 20.199 1.00 73.60 ? 49 PRO B C 1 ATOM 631 O O . PRO B 2 49 ? 29.171 2.094 20.248 1.00 80.95 ? 49 PRO B O 1 ATOM 632 C CB . PRO B 2 49 ? 31.328 2.766 22.509 1.00 69.47 ? 49 PRO B CB 1 ATOM 633 C CG . PRO B 2 49 ? 32.692 2.602 23.085 1.00 69.37 ? 49 PRO B CG 1 ATOM 634 C CD . PRO B 2 49 ? 33.632 2.481 21.913 1.00 67.86 ? 49 PRO B CD 1 ATOM 635 N N . TRP B 2 50 ? 30.764 3.376 19.303 1.00 69.11 ? 50 TRP B N 1 ATOM 636 C CA . TRP B 2 50 ? 29.905 3.829 18.196 1.00 63.13 ? 50 TRP B CA 1 ATOM 637 C C . TRP B 2 50 ? 30.486 3.442 16.845 1.00 62.42 ? 50 TRP B C 1 ATOM 638 O O . TRP B 2 50 ? 30.311 4.158 15.854 1.00 58.12 ? 50 TRP B O 1 ATOM 639 C CB . TRP B 2 50 ? 29.684 5.339 18.205 1.00 62.71 ? 50 TRP B CB 1 ATOM 640 C CG . TRP B 2 50 ? 29.139 5.911 19.454 1.00 66.86 ? 50 TRP B CG 1 ATOM 641 C CD1 . TRP B 2 50 ? 28.590 5.237 20.509 1.00 66.76 ? 50 TRP B CD1 1 ATOM 642 C CD2 . TRP B 2 50 ? 29.055 7.303 19.774 1.00 69.75 ? 50 TRP B CD2 1 ATOM 643 N NE1 . TRP B 2 50 ? 28.188 6.126 21.480 1.00 72.48 ? 50 TRP B NE1 1 ATOM 644 C CE2 . TRP B 2 50 ? 28.459 7.402 21.055 1.00 72.83 ? 50 TRP B CE2 1 ATOM 645 C CE3 . TRP B 2 50 ? 29.436 8.479 19.106 1.00 70.60 ? 50 TRP B CE3 1 ATOM 646 C CZ2 . TRP B 2 50 ? 28.232 8.636 21.690 1.00 74.70 ? 50 TRP B CZ2 1 ATOM 647 C CZ3 . TRP B 2 50 ? 29.208 9.708 19.731 1.00 75.66 ? 50 TRP B CZ3 1 ATOM 648 C CH2 . TRP B 2 50 ? 28.609 9.774 21.015 1.00 77.70 ? 50 TRP B CH2 1 ATOM 649 N N . ASP B 2 51 ? 31.201 2.320 16.821 1.00 64.40 ? 51 ASP B N 1 ATOM 650 C CA . ASP B 2 51 ? 31.785 1.766 15.597 1.00 68.23 ? 51 ASP B CA 1 ATOM 651 C C . ASP B 2 51 ? 32.524 2.789 14.709 1.00 65.39 ? 51 ASP B C 1 ATOM 652 O O . ASP B 2 51 ? 32.487 2.702 13.477 1.00 62.11 ? 51 ASP B O 1 ATOM 653 C CB . ASP B 2 51 ? 30.708 1.028 14.799 1.00 74.45 ? 51 ASP B CB 1 ATOM 654 C CG . ASP B 2 51 ? 31.070 -0.414 14.558 1.00 80.68 ? 51 ASP B CG 1 ATOM 655 O OD1 . ASP B 2 51 ? 31.955 -0.676 13.711 1.00 82.17 ? 51 ASP B OD1 1 ATOM 656 O OD2 . ASP B 2 51 ? 30.478 -1.286 15.232 1.00 83.06 ? 51 ASP B OD2 1 ATOM 657 N N . LYS B 2 52 ? 33.192 3.745 15.358 1.00 61.12 ? 52 LYS B N 1 ATOM 658 C CA . LYS B 2 52 ? 33.997 4.766 14.693 1.00 52.60 ? 52 LYS B CA 1 ATOM 659 C C . LYS B 2 52 ? 35.452 4.297 14.621 1.00 48.41 ? 52 LYS B C 1 ATOM 660 O O . LYS B 2 52 ? 36.090 4.041 15.645 1.00 48.19 ? 52 LYS B O 1 ATOM 661 C CB . LYS B 2 52 ? 33.881 6.089 15.455 1.00 54.96 ? 52 LYS B CB 1 ATOM 662 C CG . LYS B 2 52 ? 34.519 7.288 14.769 1.00 56.39 ? 52 LYS B CG 1 ATOM 663 C CD . LYS B 2 52 ? 34.723 8.455 15.727 1.00 56.19 ? 52 LYS B CD 1 ATOM 664 C CE . LYS B 2 52 ? 33.525 9.386 15.770 1.00 58.94 ? 52 LYS B CE 1 ATOM 665 N NZ . LYS B 2 52 ? 33.984 10.763 16.114 1.00 60.43 ? 52 LYS B NZ 1 ATOM 666 N N . ASN B 2 53 ? 35.959 4.153 13.406 1.00 44.74 ? 53 ASN B N 1 ATOM 667 C CA . ASN B 2 53 ? 37.313 3.699 13.187 1.00 46.19 ? 53 ASN B CA 1 ATOM 668 C C . ASN B 2 53 ? 37.794 4.226 11.835 1.00 45.62 ? 53 ASN B C 1 ATOM 669 O O . ASN B 2 53 ? 37.808 3.493 10.855 1.00 48.25 ? 53 ASN B O 1 ATOM 670 C CB . ASN B 2 53 ? 37.391 2.163 13.273 1.00 51.01 ? 53 ASN B CB 1 ATOM 671 C CG . ASN B 2 53 ? 38.815 1.627 13.161 1.00 60.47 ? 53 ASN B CG 1 ATOM 672 O OD1 . ASN B 2 53 ? 39.777 2.391 13.118 1.00 61.33 ? 53 ASN B OD1 1 ATOM 673 N ND2 . ASN B 2 53 ? 38.951 0.299 13.115 1.00 71.01 ? 53 ASN B ND2 1 ATOM 674 N N . PHE B 2 54 ? 38.188 5.500 11.793 1.00 43.49 ? 54 PHE B N 1 ATOM 675 C CA . PHE B 2 54 ? 38.616 6.151 10.547 1.00 41.94 ? 54 PHE B CA 1 ATOM 676 C C . PHE B 2 54 ? 40.066 5.860 10.153 1.00 43.16 ? 54 PHE B C 1 ATOM 677 O O . PHE B 2 54 ? 40.947 5.732 10.997 1.00 47.08 ? 54 PHE B O 1 ATOM 678 C CB . PHE B 2 54 ? 38.382 7.666 10.605 1.00 40.49 ? 54 PHE B CB 1 ATOM 679 C CG . PHE B 2 54 ? 36.931 8.063 10.688 1.00 41.05 ? 54 PHE B CG 1 ATOM 680 C CD1 . PHE B 2 54 ? 36.076 7.887 9.598 1.00 41.60 ? 54 PHE B CD1 1 ATOM 681 C CD2 . PHE B 2 54 ? 36.418 8.633 11.851 1.00 41.01 ? 54 PHE B CD2 1 ATOM 682 C CE1 . PHE B 2 54 ? 34.736 8.256 9.677 1.00 43.51 ? 54 PHE B CE1 1 ATOM 683 C CE2 . PHE B 2 54 ? 35.080 9.010 11.934 1.00 43.12 ? 54 PHE B CE2 1 ATOM 684 C CZ . PHE B 2 54 ? 34.235 8.822 10.847 1.00 43.65 ? 54 PHE B CZ 1 ATOM 685 N N . THR B 2 55 ? 40.286 5.824 8.846 1.00 42.83 ? 55 THR B N 1 ATOM 686 C CA . THR B 2 55 ? 41.523 5.417 8.197 1.00 41.62 ? 55 THR B CA 1 ATOM 687 C C . THR B 2 55 ? 42.121 6.616 7.461 1.00 40.29 ? 55 THR B C 1 ATOM 688 O O . THR B 2 55 ? 41.417 7.586 7.220 1.00 39.58 ? 55 THR B O 1 ATOM 689 C CB . THR B 2 55 ? 41.169 4.267 7.214 1.00 45.46 ? 55 THR B CB 1 ATOM 690 O OG1 . THR B 2 55 ? 41.524 3.030 7.818 1.00 50.84 ? 55 THR B OG1 1 ATOM 691 C CG2 . THR B 2 55 ? 41.843 4.368 5.829 1.00 45.42 ? 55 THR B CG2 1 ATOM 692 N N . GLU B 2 56 ? 43.404 6.538 7.105 1.00 40.22 ? 56 GLU B N 1 ATOM 693 C CA . GLU B 2 56 ? 44.101 7.559 6.302 1.00 42.45 ? 56 GLU B CA 1 ATOM 694 C C . GLU B 2 56 ? 43.360 7.979 5.033 1.00 42.42 ? 56 GLU B C 1 ATOM 695 O O . GLU B 2 56 ? 43.496 9.120 4.576 1.00 41.72 ? 56 GLU B O 1 ATOM 696 C CB . GLU B 2 56 ? 45.518 7.087 5.898 1.00 43.92 ? 56 GLU B CB 1 ATOM 697 C CG . GLU B 2 56 ? 46.534 6.975 7.022 1.00 48.77 ? 56 GLU B CG 1 ATOM 698 C CD . GLU B 2 56 ? 46.353 5.736 7.899 1.00 51.38 ? 56 GLU B CD 1 ATOM 699 O OE1 . GLU B 2 56 ? 45.480 4.903 7.585 1.00 50.82 ? 56 GLU B OE1 1 ATOM 700 O OE2 . GLU B 2 56 ? 47.088 5.593 8.909 1.00 52.07 ? 56 GLU B OE2 1 ATOM 701 N N . ASN B 2 57 ? 42.604 7.051 4.457 1.00 45.63 ? 57 ASN B N 1 ATOM 702 C CA . ASN B 2 57 ? 41.896 7.279 3.191 1.00 48.72 ? 57 ASN B CA 1 ATOM 703 C C . ASN B 2 57 ? 40.491 7.855 3.375 1.00 45.88 ? 57 ASN B C 1 ATOM 704 O O . ASN B 2 57 ? 39.890 8.359 2.425 1.00 46.08 ? 57 ASN B O 1 ATOM 705 C CB . ASN B 2 57 ? 41.838 5.987 2.362 1.00 55.42 ? 57 ASN B CB 1 ATOM 706 C CG . ASN B 2 57 ? 43.219 5.375 2.125 1.00 62.24 ? 57 ASN B CG 1 ATOM 707 O OD1 . ASN B 2 57 ? 44.120 6.026 1.579 1.00 61.76 ? 57 ASN B OD1 1 ATOM 708 N ND2 . ASN B 2 57 ? 43.388 4.112 2.533 1.00 60.66 ? 57 ASN B ND2 1 ATOM 709 N N . ASP B 2 58 ? 39.980 7.794 4.598 1.00 41.98 ? 58 ASP B N 1 ATOM 710 C CA . ASP B 2 58 ? 38.651 8.298 4.889 1.00 41.66 ? 58 ASP B CA 1 ATOM 711 C C . ASP B 2 58 ? 38.565 9.818 5.049 1.00 41.96 ? 58 ASP B C 1 ATOM 712 O O . ASP B 2 58 ? 37.461 10.365 5.099 1.00 43.35 ? 58 ASP B O 1 ATOM 713 C CB . ASP B 2 58 ? 38.127 7.630 6.155 1.00 42.73 ? 58 ASP B CB 1 ATOM 714 C CG . ASP B 2 58 ? 37.924 6.150 5.982 1.00 45.37 ? 58 ASP B CG 1 ATOM 715 O OD1 . ASP B 2 58 ? 37.730 5.699 4.831 1.00 47.36 ? 58 ASP B OD1 1 ATOM 716 O OD2 . ASP B 2 58 ? 37.948 5.430 6.998 1.00 47.82 ? 58 ASP B OD2 1 ATOM 717 N N . LEU B 2 59 ? 39.718 10.491 5.131 1.00 39.26 ? 59 LEU B N 1 ATOM 718 C CA . LEU B 2 59 ? 39.779 11.856 5.671 1.00 36.37 ? 59 LEU B CA 1 ATOM 719 C C . LEU B 2 59 ? 40.638 12.779 4.878 1.00 33.70 ? 59 LEU B C 1 ATOM 720 O O . LEU B 2 59 ? 41.656 12.386 4.307 1.00 31.88 ? 59 LEU B O 1 ATOM 721 C CB . LEU B 2 59 ? 40.361 11.867 7.091 1.00 37.79 ? 59 LEU B CB 1 ATOM 722 C CG . LEU B 2 59 ? 39.696 10.948 8.094 1.00 39.33 ? 59 LEU B CG 1 ATOM 723 C CD1 . LEU B 2 59 ? 40.620 10.684 9.256 1.00 39.01 ? 59 LEU B CD1 1 ATOM 724 C CD2 . LEU B 2 59 ? 38.400 11.591 8.537 1.00 40.39 ? 59 LEU B CD2 1 ATOM 725 N N . LEU B 2 60 ? 40.216 14.031 4.894 1.00 31.67 ? 60 LEU B N 1 ATOM 726 C CA . LEU B 2 60 ? 41.030 15.133 4.447 1.00 29.95 ? 60 LEU B CA 1 ATOM 727 C C . LEU B 2 60 ? 41.271 16.091 5.615 1.00 28.76 ? 60 LEU B C 1 ATOM 728 O O . LEU B 2 60 ? 40.475 16.183 6.564 1.00 28.83 ? 60 LEU B O 1 ATOM 729 C CB . LEU B 2 60 ? 40.353 15.844 3.280 1.00 29.82 ? 60 LEU B CB 1 ATOM 730 C CG . LEU B 2 60 ? 40.257 14.991 2.014 1.00 30.23 ? 60 LEU B CG 1 ATOM 731 C CD1 . LEU B 2 60 ? 39.194 15.583 1.108 1.00 31.27 ? 60 LEU B CD1 1 ATOM 732 C CD2 . LEU B 2 60 ? 41.601 14.897 1.303 1.00 29.10 ? 60 LEU B CD2 1 ATOM 733 N N . VAL B 2 61 ? 42.392 16.780 5.535 1.00 26.83 ? 61 VAL B N 1 ATOM 734 C CA . VAL B 2 61 ? 42.754 17.820 6.472 1.00 26.51 ? 61 VAL B CA 1 ATOM 735 C C . VAL B 2 61 ? 42.693 19.135 5.689 1.00 25.45 ? 61 VAL B C 1 ATOM 736 O O . VAL B 2 61 ? 43.270 19.240 4.591 1.00 25.78 ? 61 VAL B O 1 ATOM 737 C CB . VAL B 2 61 ? 44.159 17.499 7.032 1.00 28.35 ? 61 VAL B CB 1 ATOM 738 C CG1 . VAL B 2 61 ? 45.025 18.729 7.186 1.00 27.58 ? 61 VAL B CG1 1 ATOM 739 C CG2 . VAL B 2 61 ? 44.043 16.697 8.327 1.00 28.16 ? 61 VAL B CG2 1 ATOM 740 N N . ARG B 2 62 ? 41.946 20.110 6.209 1.00 23.35 ? 62 ARG B N 1 ATOM 741 C CA . ARG B 2 62 ? 41.844 21.430 5.573 1.00 22.12 ? 62 ARG B CA 1 ATOM 742 C C . ARG B 2 62 ? 42.417 22.541 6.491 1.00 22.36 ? 62 ARG B C 1 ATOM 743 O O . ARG B 2 62 ? 42.016 22.699 7.657 1.00 22.25 ? 62 ARG B O 1 ATOM 744 C CB . ARG B 2 62 ? 40.401 21.704 5.141 1.00 22.65 ? 62 ARG B CB 1 ATOM 745 C CG . ARG B 2 62 ? 39.836 20.642 4.194 1.00 23.41 ? 62 ARG B CG 1 ATOM 746 C CD . ARG B 2 62 ? 38.346 20.800 3.927 1.00 23.58 ? 62 ARG B CD 1 ATOM 747 N NE . ARG B 2 62 ? 38.067 22.034 3.182 1.00 25.01 ? 62 ARG B NE 1 ATOM 748 C CZ . ARG B 2 62 ? 36.869 22.396 2.710 1.00 24.52 ? 62 ARG B CZ 1 ATOM 749 N NH1 . ARG B 2 62 ? 35.807 21.619 2.891 1.00 23.54 ? 62 ARG B NH1 1 ATOM 750 N NH2 . ARG B 2 62 ? 36.734 23.554 2.068 1.00 24.82 ? 62 ARG B NH2 1 ATOM 751 N N . ILE B 2 63 ? 43.377 23.288 5.961 1.00 21.60 ? 63 ILE B N 1 ATOM 752 C CA . ILE B 2 63 ? 44.168 24.214 6.757 1.00 21.93 ? 63 ILE B CA 1 ATOM 753 C C . ILE B 2 63 ? 44.057 25.619 6.204 1.00 21.48 ? 63 ILE B C 1 ATOM 754 O O . ILE B 2 63 ? 44.019 25.801 4.991 1.00 21.83 ? 63 ILE B O 1 ATOM 755 C CB . ILE B 2 63 ? 45.658 23.803 6.757 1.00 23.26 ? 63 ILE B CB 1 ATOM 756 C CG1 . ILE B 2 63 ? 45.795 22.301 7.060 1.00 24.68 ? 63 ILE B CG1 1 ATOM 757 C CG2 . ILE B 2 63 ? 46.431 24.611 7.783 1.00 22.69 ? 63 ILE B CG2 1 ATOM 758 C CD1 . ILE B 2 63 ? 47.183 21.741 6.796 1.00 26.70 ? 63 ILE B CD1 1 ATOM 759 N N . GLY B 2 64 ? 44.025 26.613 7.081 1.00 20.83 ? 64 GLY B N 1 ATOM 760 C CA . GLY B 2 64 ? 43.923 28.008 6.641 1.00 21.73 ? 64 GLY B CA 1 ATOM 761 C C . GLY B 2 64 ? 42.494 28.542 6.502 1.00 22.48 ? 64 GLY B C 1 ATOM 762 O O . GLY B 2 64 ? 42.276 29.619 5.945 1.00 23.09 ? 64 GLY B O 1 ATOM 763 N N . LYS B 2 65 ? 41.518 27.801 7.017 1.00 21.70 ? 65 LYS B N 1 ATOM 764 C CA . LYS B 2 65 ? 40.124 28.118 6.784 1.00 22.26 ? 65 LYS B CA 1 ATOM 765 C C . LYS B 2 65 ? 39.554 29.190 7.729 1.00 23.11 ? 65 LYS B C 1 ATOM 766 O O . LYS B 2 65 ? 39.968 29.304 8.890 1.00 23.52 ? 65 LYS B O 1 ATOM 767 C CB . LYS B 2 65 ? 39.289 26.835 6.859 1.00 22.30 ? 65 LYS B CB 1 ATOM 768 C CG . LYS B 2 65 ? 39.432 25.950 5.630 1.00 21.63 ? 65 LYS B CG 1 ATOM 769 C CD . LYS B 2 65 ? 38.356 24.864 5.546 1.00 21.43 ? 65 LYS B CD 1 ATOM 770 C CE . LYS B 2 65 ? 36.962 25.417 5.314 1.00 20.82 ? 65 LYS B CE 1 ATOM 771 N NZ . LYS B 2 65 ? 36.928 26.439 4.238 1.00 19.97 ? 65 LYS B NZ 1 ATOM 772 N N . HIS B 2 66 ? 38.605 29.971 7.217 1.00 22.58 ? 66 HIS B N 1 ATOM 773 C CA . HIS B 2 66 ? 37.831 30.901 8.029 1.00 22.47 ? 66 HIS B CA 1 ATOM 774 C C . HIS B 2 66 ? 36.336 30.467 8.033 1.00 23.47 ? 66 HIS B C 1 ATOM 775 O O . HIS B 2 66 ? 35.751 30.218 9.094 1.00 23.82 ? 66 HIS B O 1 ATOM 776 C CB . HIS B 2 66 ? 38.003 32.351 7.528 1.00 21.87 ? 66 HIS B CB 1 ATOM 777 C CG . HIS B 2 66 ? 37.297 33.361 8.378 1.00 22.56 ? 66 HIS B CG 1 ATOM 778 N ND1 . HIS B 2 66 ? 37.642 33.598 9.695 1.00 23.58 ? 66 HIS B ND1 1 ATOM 779 C CD2 . HIS B 2 66 ? 36.244 34.167 8.116 1.00 22.66 ? 66 HIS B CD2 1 ATOM 780 C CE1 . HIS B 2 66 ? 36.829 34.504 10.207 1.00 23.57 ? 66 HIS B CE1 1 ATOM 781 N NE2 . HIS B 2 66 ? 35.970 34.865 9.270 1.00 24.14 ? 66 HIS B NE2 1 ATOM 782 N N . SER B 2 67 ? 35.734 30.378 6.845 1.00 23.21 ? 67 SER B N 1 ATOM 783 C CA . SER B 2 67 ? 34.354 29.925 6.683 1.00 22.75 ? 67 SER B CA 1 ATOM 784 C C . SER B 2 67 ? 34.250 28.428 6.974 1.00 23.88 ? 67 SER B C 1 ATOM 785 O O . SER B 2 67 ? 35.200 27.669 6.699 1.00 25.26 ? 67 SER B O 1 ATOM 786 C CB . SER B 2 67 ? 33.895 30.217 5.256 1.00 21.89 ? 67 SER B CB 1 ATOM 787 O OG . SER B 2 67 ? 32.818 29.394 4.886 1.00 21.89 ? 67 SER B OG 1 ATOM 788 N N . ARG B 2 68 ? 33.115 27.999 7.532 1.00 22.93 ? 68 ARG B N 1 ATOM 789 C CA . ARG B 2 68 ? 32.884 26.580 7.761 1.00 23.25 ? 68 ARG B CA 1 ATOM 790 C C . ARG B 2 68 ? 32.659 25.797 6.467 1.00 24.10 ? 68 ARG B C 1 ATOM 791 O O . ARG B 2 68 ? 33.169 24.675 6.313 1.00 24.82 ? 68 ARG B O 1 ATOM 792 C CB . ARG B 2 68 ? 31.718 26.347 8.706 1.00 23.56 ? 68 ARG B CB 1 ATOM 793 C CG . ARG B 2 68 ? 31.568 24.878 9.106 1.00 24.81 ? 68 ARG B CG 1 ATOM 794 C CD . ARG B 2 68 ? 30.419 24.660 10.086 1.00 25.68 ? 68 ARG B CD 1 ATOM 795 N NE . ARG B 2 68 ? 29.200 25.309 9.592 1.00 28.38 ? 68 ARG B NE 1 ATOM 796 C CZ . ARG B 2 68 ? 28.264 24.719 8.850 1.00 27.02 ? 68 ARG B CZ 1 ATOM 797 N NH1 . ARG B 2 68 ? 28.352 23.438 8.526 1.00 26.55 ? 68 ARG B NH1 1 ATOM 798 N NH2 . ARG B 2 68 ? 27.221 25.418 8.459 1.00 26.36 ? 68 ARG B NH2 1 ATOM 799 N N . THR B 2 69 ? 31.925 26.396 5.532 1.00 23.88 ? 69 THR B N 1 ATOM 800 C CA . THR B 2 69 ? 31.387 25.651 4.383 1.00 23.54 ? 69 THR B CA 1 ATOM 801 C C . THR B 2 69 ? 32.045 25.967 3.042 1.00 24.12 ? 69 THR B C 1 ATOM 802 O O . THR B 2 69 ? 32.085 25.111 2.154 1.00 23.85 ? 69 THR B O 1 ATOM 803 C CB . THR B 2 69 ? 29.867 25.849 4.259 1.00 22.80 ? 69 THR B CB 1 ATOM 804 O OG1 . THR B 2 69 ? 29.580 27.254 4.230 1.00 22.42 ? 69 THR B OG1 1 ATOM 805 C CG2 . THR B 2 69 ? 29.159 25.228 5.460 1.00 22.17 ? 69 THR B CG2 1 ATOM 806 N N . ARG B 2 70 ? 32.548 27.190 2.884 1.00 23.77 ? 70 ARG B N 1 ATOM 807 C CA . ARG B 2 70 ? 33.134 27.595 1.602 1.00 24.05 ? 70 ARG B CA 1 ATOM 808 C C . ARG B 2 70 ? 34.403 26.853 1.263 1.00 25.56 ? 70 ARG B C 1 ATOM 809 O O . ARG B 2 70 ? 35.122 26.377 2.144 1.00 26.45 ? 70 ARG B O 1 ATOM 810 C CB . ARG B 2 70 ? 33.420 29.088 1.569 1.00 22.93 ? 70 ARG B CB 1 ATOM 811 C CG . ARG B 2 70 ? 32.170 29.933 1.661 1.00 20.78 ? 70 ARG B CG 1 ATOM 812 C CD . ARG B 2 70 ? 32.559 31.374 1.744 1.00 19.24 ? 70 ARG B CD 1 ATOM 813 N NE . ARG B 2 70 ? 31.361 32.192 1.727 1.00 19.24 ? 70 ARG B NE 1 ATOM 814 C CZ . ARG B 2 70 ? 31.360 33.507 1.894 1.00 18.43 ? 70 ARG B CZ 1 ATOM 815 N NH1 . ARG B 2 70 ? 32.499 34.142 2.106 1.00 17.65 ? 70 ARG B NH1 1 ATOM 816 N NH2 . ARG B 2 70 ? 30.222 34.179 1.852 1.00 18.59 ? 70 ARG B NH2 1 ATOM 817 N N . TYR B 2 71 ? 34.658 26.734 -0.033 1.00 27.15 ? 71 TYR B N 1 ATOM 818 C CA . TYR B 2 71 ? 35.944 26.267 -0.500 1.00 27.71 ? 71 TYR B CA 1 ATOM 819 C C . TYR B 2 71 ? 36.735 27.531 -0.774 1.00 28.74 ? 71 TYR B C 1 ATOM 820 O O . TYR B 2 71 ? 36.493 28.240 -1.754 1.00 27.55 ? 71 TYR B O 1 ATOM 821 C CB . TYR B 2 71 ? 35.795 25.409 -1.750 1.00 27.41 ? 71 TYR B CB 1 ATOM 822 C CG . TYR B 2 71 ? 37.110 25.115 -2.417 1.00 28.07 ? 71 TYR B CG 1 ATOM 823 C CD1 . TYR B 2 71 ? 38.220 24.661 -1.670 1.00 26.98 ? 71 TYR B CD1 1 ATOM 824 C CD2 . TYR B 2 71 ? 37.255 25.278 -3.801 1.00 27.78 ? 71 TYR B CD2 1 ATOM 825 C CE1 . TYR B 2 71 ? 39.437 24.394 -2.291 1.00 27.08 ? 71 TYR B CE1 1 ATOM 826 C CE2 . TYR B 2 71 ? 38.460 25.009 -4.430 1.00 27.79 ? 71 TYR B CE2 1 ATOM 827 C CZ . TYR B 2 71 ? 39.545 24.574 -3.675 1.00 28.50 ? 71 TYR B CZ 1 ATOM 828 O OH . TYR B 2 71 ? 40.723 24.312 -4.320 1.00 29.10 ? 71 TYR B OH 1 ATOM 829 N N . GLU B 2 72 ? 37.646 27.845 0.140 1.00 30.22 ? 72 GLU B N 1 ATOM 830 C CA . GLU B 2 72 ? 38.311 29.140 0.122 1.00 30.15 ? 72 GLU B CA 1 ATOM 831 C C . GLU B 2 72 ? 39.564 29.025 -0.755 1.00 33.17 ? 72 GLU B C 1 ATOM 832 O O . GLU B 2 72 ? 40.694 28.896 -0.278 1.00 30.61 ? 72 GLU B O 1 ATOM 833 C CB . GLU B 2 72 ? 38.550 29.617 1.557 1.00 27.69 ? 72 GLU B CB 1 ATOM 834 C CG . GLU B 2 72 ? 37.255 29.800 2.337 1.00 26.39 ? 72 GLU B CG 1 ATOM 835 C CD . GLU B 2 72 ? 37.457 29.900 3.843 1.00 27.63 ? 72 GLU B CD 1 ATOM 836 O OE1 . GLU B 2 72 ? 38.017 28.959 4.465 1.00 26.97 ? 72 GLU B OE1 1 ATOM 837 O OE2 . GLU B 2 72 ? 37.038 30.924 4.423 1.00 27.52 ? 72 GLU B OE2 1 ATOM 838 N N . ARG B 2 73 ? 39.304 29.051 -2.061 1.00 38.78 ? 73 ARG B N 1 ATOM 839 C CA . ARG B 2 73 ? 40.262 28.747 -3.128 1.00 43.83 ? 73 ARG B CA 1 ATOM 840 C C . ARG B 2 73 ? 41.647 29.382 -2.963 1.00 43.32 ? 73 ARG B C 1 ATOM 841 O O . ARG B 2 73 ? 42.650 28.710 -3.122 1.00 42.43 ? 73 ARG B O 1 ATOM 842 C CB . ARG B 2 73 ? 39.649 29.137 -4.475 1.00 50.75 ? 73 ARG B CB 1 ATOM 843 C CG . ARG B 2 73 ? 40.422 28.734 -5.728 1.00 63.38 ? 73 ARG B CG 1 ATOM 844 C CD . ARG B 2 73 ? 39.716 29.251 -6.985 1.00 76.15 ? 73 ARG B CD 1 ATOM 845 N NE . ARG B 2 73 ? 38.602 28.387 -7.409 1.00 86.10 ? 73 ARG B NE 1 ATOM 846 C CZ . ARG B 2 73 ? 37.350 28.424 -6.934 1.00 88.12 ? 73 ARG B CZ 1 ATOM 847 N NH1 . ARG B 2 73 ? 36.987 29.289 -5.991 1.00 89.45 ? 73 ARG B NH1 1 ATOM 848 N NH2 . ARG B 2 73 ? 36.446 27.574 -7.404 1.00 87.87 ? 73 ARG B NH2 1 ATOM 849 N N . ASN B 2 74 ? 41.707 30.664 -2.639 1.00 46.94 ? 74 ASN B N 1 ATOM 850 C CA . ASN B 2 74 ? 43.004 31.351 -2.557 1.00 52.08 ? 74 ASN B CA 1 ATOM 851 C C . ASN B 2 74 ? 43.818 31.088 -1.287 1.00 49.43 ? 74 ASN B C 1 ATOM 852 O O . ASN B 2 74 ? 45.020 31.312 -1.265 1.00 51.00 ? 74 ASN B O 1 ATOM 853 C CB . ASN B 2 74 ? 42.815 32.864 -2.706 1.00 59.14 ? 74 ASN B CB 1 ATOM 854 C CG . ASN B 2 74 ? 42.030 33.245 -3.953 1.00 65.37 ? 74 ASN B CG 1 ATOM 855 O OD1 . ASN B 2 74 ? 42.291 32.748 -5.062 1.00 66.59 ? 74 ASN B OD1 1 ATOM 856 N ND2 . ASN B 2 74 ? 41.061 34.142 -3.778 1.00 66.57 ? 74 ASN B ND2 1 ATOM 857 N N . ILE B 2 75 ? 43.161 30.591 -0.247 1.00 45.53 ? 75 ILE B N 1 ATOM 858 C CA . ILE B 2 75 ? 43.667 30.702 1.109 1.00 40.77 ? 75 ILE B CA 1 ATOM 859 C C . ILE B 2 75 ? 43.898 29.356 1.789 1.00 37.50 ? 75 ILE B C 1 ATOM 860 O O . ILE B 2 75 ? 44.900 29.172 2.476 1.00 35.40 ? 75 ILE B O 1 ATOM 861 C CB . ILE B 2 75 ? 42.735 31.645 1.908 1.00 42.84 ? 75 ILE B CB 1 ATOM 862 C CG1 . ILE B 2 75 ? 43.153 33.094 1.648 1.00 46.05 ? 75 ILE B CG1 1 ATOM 863 C CG2 . ILE B 2 75 ? 42.711 31.328 3.388 1.00 41.72 ? 75 ILE B CG2 1 ATOM 864 C CD1 . ILE B 2 75 ? 41.997 34.076 1.682 1.00 54.03 ? 75 ILE B CD1 1 ATOM 865 N N . GLU B 2 76 ? 42.985 28.410 1.585 1.00 34.09 ? 76 GLU B N 1 ATOM 866 C CA . GLU B 2 76 ? 43.068 27.129 2.269 1.00 31.51 ? 76 GLU B CA 1 ATOM 867 C C . GLU B 2 76 ? 43.912 26.114 1.494 1.00 32.27 ? 76 GLU B C 1 ATOM 868 O O . GLU B 2 76 ? 44.059 26.216 0.282 1.00 32.43 ? 76 GLU B O 1 ATOM 869 C CB . GLU B 2 76 ? 41.671 26.589 2.598 1.00 29.38 ? 76 GLU B CB 1 ATOM 870 C CG . GLU B 2 76 ? 40.995 25.779 1.500 1.00 29.00 ? 76 GLU B CG 1 ATOM 871 C CD . GLU B 2 76 ? 39.669 25.186 1.944 1.00 29.30 ? 76 GLU B CD 1 ATOM 872 O OE1 . GLU B 2 76 ? 39.678 24.051 2.466 1.00 29.45 ? 76 GLU B OE1 1 ATOM 873 O OE2 . GLU B 2 76 ? 38.615 25.840 1.772 1.00 28.60 ? 76 GLU B OE2 1 ATOM 874 N N . LYS B 2 77 ? 44.488 25.159 2.215 1.00 33.40 ? 77 LYS B N 1 ATOM 875 C CA . LYS B 2 77 ? 45.232 24.071 1.620 1.00 34.02 ? 77 LYS B CA 1 ATOM 876 C C . LYS B 2 77 ? 44.593 22.793 2.082 1.00 32.84 ? 77 LYS B C 1 ATOM 877 O O . LYS B 2 77 ? 44.274 22.644 3.259 1.00 33.17 ? 77 LYS B O 1 ATOM 878 C CB . LYS B 2 77 ? 46.700 24.091 2.062 1.00 38.65 ? 77 LYS B CB 1 ATOM 879 C CG . LYS B 2 77 ? 47.502 25.263 1.519 1.00 45.57 ? 77 LYS B CG 1 ATOM 880 C CD . LYS B 2 77 ? 47.830 25.105 0.037 1.00 53.47 ? 77 LYS B CD 1 ATOM 881 C CE . LYS B 2 77 ? 48.369 26.402 -0.557 1.00 59.49 ? 77 LYS B CE 1 ATOM 882 N NZ . LYS B 2 77 ? 47.267 27.354 -0.891 1.00 61.54 ? 77 LYS B NZ 1 ATOM 883 N N . ILE B 2 78 ? 44.408 21.867 1.151 1.00 31.74 ? 78 ILE B N 1 ATOM 884 C CA . ILE B 2 78 ? 43.795 20.594 1.452 1.00 31.34 ? 78 ILE B CA 1 ATOM 885 C C . ILE B 2 78 ? 44.866 19.524 1.324 1.00 31.40 ? 78 ILE B C 1 ATOM 886 O O . ILE B 2 78 ? 45.547 19.473 0.309 1.00 32.79 ? 78 ILE B O 1 ATOM 887 C CB . ILE B 2 78 ? 42.622 20.304 0.494 1.00 31.02 ? 78 ILE B CB 1 ATOM 888 C CG1 . ILE B 2 78 ? 41.624 21.477 0.512 1.00 30.32 ? 78 ILE B CG1 1 ATOM 889 C CG2 . ILE B 2 78 ? 41.972 18.969 0.851 1.00 29.98 ? 78 ILE B CG2 1 ATOM 890 C CD1 . ILE B 2 78 ? 40.515 21.360 -0.514 1.00 30.23 ? 78 ILE B CD1 1 ATOM 891 N N . SER B 2 79 ? 45.020 18.686 2.348 1.00 29.74 ? 79 SER B N 1 ATOM 892 C CA . SER B 2 79 ? 46.080 17.676 2.354 1.00 30.23 ? 79 SER B CA 1 ATOM 893 C C . SER B 2 79 ? 45.529 16.301 2.643 1.00 31.93 ? 79 SER B C 1 ATOM 894 O O . SER B 2 79 ? 44.542 16.147 3.385 1.00 29.60 ? 79 SER B O 1 ATOM 895 C CB . SER B 2 79 ? 47.127 17.957 3.431 1.00 31.05 ? 79 SER B CB 1 ATOM 896 O OG . SER B 2 79 ? 47.627 19.273 3.365 1.00 33.68 ? 79 SER B OG 1 ATOM 897 N N . MET B 2 80 ? 46.205 15.297 2.091 1.00 34.16 ? 80 MET B N 1 ATOM 898 C CA . MET B 2 80 ? 45.880 13.918 2.395 1.00 36.17 ? 80 MET B CA 1 ATOM 899 C C . MET B 2 80 ? 46.775 13.429 3.529 1.00 34.48 ? 80 MET B C 1 ATOM 900 O O . MET B 2 80 ? 47.810 14.024 3.807 1.00 34.43 ? 80 MET B O 1 ATOM 901 C CB . MET B 2 80 ? 46.031 13.062 1.138 1.00 40.71 ? 80 MET B CB 1 ATOM 902 C CG . MET B 2 80 ? 45.086 13.468 0.010 1.00 44.90 ? 80 MET B CG 1 ATOM 903 S SD . MET B 2 80 ? 45.367 12.559 -1.521 1.00 46.67 ? 80 MET B SD 1 ATOM 904 C CE . MET B 2 80 ? 46.895 13.309 -2.106 1.00 45.69 ? 80 MET B CE 1 ATOM 905 N N . LEU B 2 81 ? 46.380 12.347 4.181 1.00 34.80 ? 81 LEU B N 1 ATOM 906 C CA . LEU B 2 81 ? 47.140 11.802 5.309 1.00 37.56 ? 81 LEU B CA 1 ATOM 907 C C . LEU B 2 81 ? 48.066 10.637 4.933 1.00 39.16 ? 81 LEU B C 1 ATOM 908 O O . LEU B 2 81 ? 47.664 9.720 4.237 1.00 40.61 ? 81 LEU B O 1 ATOM 909 C CB . LEU B 2 81 ? 46.180 11.361 6.420 1.00 36.67 ? 81 LEU B CB 1 ATOM 910 C CG . LEU B 2 81 ? 45.244 12.440 6.962 1.00 37.46 ? 81 LEU B CG 1 ATOM 911 C CD1 . LEU B 2 81 ? 44.283 11.835 7.968 1.00 39.22 ? 81 LEU B CD1 1 ATOM 912 C CD2 . LEU B 2 81 ? 46.063 13.558 7.595 1.00 39.84 ? 81 LEU B CD2 1 ATOM 913 N N . GLU B 2 82 ? 49.302 10.667 5.414 1.00 42.33 ? 82 GLU B N 1 ATOM 914 C CA . GLU B 2 82 ? 50.207 9.546 5.217 1.00 43.65 ? 82 GLU B CA 1 ATOM 915 C C . GLU B 2 82 ? 49.983 8.474 6.277 1.00 42.52 ? 82 GLU B C 1 ATOM 916 O O . GLU B 2 82 ? 49.973 7.298 5.955 1.00 45.77 ? 82 GLU B O 1 ATOM 917 C CB . GLU B 2 82 ? 51.669 10.002 5.188 1.00 46.49 ? 82 GLU B CB 1 ATOM 918 C CG . GLU B 2 82 ? 52.655 8.930 4.750 1.00 54.36 ? 82 GLU B CG 1 ATOM 919 C CD . GLU B 2 82 ? 54.099 9.287 5.095 1.00 63.15 ? 82 GLU B CD 1 ATOM 920 O OE1 . GLU B 2 82 ? 54.682 10.184 4.438 1.00 66.52 ? 82 GLU B OE1 1 ATOM 921 O OE2 . GLU B 2 82 ? 54.664 8.664 6.024 1.00 65.47 ? 82 GLU B OE2 1 ATOM 922 N N . LYS B 2 83 ? 49.779 8.872 7.528 1.00 40.91 ? 83 LYS B N 1 ATOM 923 C CA . LYS B 2 83 ? 49.753 7.914 8.628 1.00 41.23 ? 83 LYS B CA 1 ATOM 924 C C . LYS B 2 83 ? 49.173 8.542 9.901 1.00 38.48 ? 83 LYS B C 1 ATOM 925 O O . LYS B 2 83 ? 49.456 9.693 10.212 1.00 39.18 ? 83 LYS B O 1 ATOM 926 C CB . LYS B 2 83 ? 51.182 7.375 8.852 1.00 44.82 ? 83 LYS B CB 1 ATOM 927 C CG . LYS B 2 83 ? 51.370 6.290 9.904 1.00 51.09 ? 83 LYS B CG 1 ATOM 928 C CD . LYS B 2 83 ? 50.701 4.962 9.576 1.00 59.19 ? 83 LYS B CD 1 ATOM 929 C CE . LYS B 2 83 ? 50.844 4.008 10.760 1.00 65.54 ? 83 LYS B CE 1 ATOM 930 N NZ . LYS B 2 83 ? 49.733 3.020 10.841 1.00 69.61 ? 83 LYS B NZ 1 ATOM 931 N N . ILE B 2 84 ? 48.361 7.767 10.614 1.00 35.53 ? 84 ILE B N 1 ATOM 932 C CA . ILE B 2 84 ? 47.727 8.160 11.861 1.00 33.99 ? 84 ILE B CA 1 ATOM 933 C C . ILE B 2 84 ? 48.410 7.414 13.002 1.00 35.73 ? 84 ILE B C 1 ATOM 934 O O . ILE B 2 84 ? 48.706 6.228 12.867 1.00 38.40 ? 84 ILE B O 1 ATOM 935 C CB . ILE B 2 84 ? 46.231 7.768 11.833 1.00 34.35 ? 84 ILE B CB 1 ATOM 936 C CG1 . ILE B 2 84 ? 45.466 8.666 10.853 1.00 35.59 ? 84 ILE B CG1 1 ATOM 937 C CG2 . ILE B 2 84 ? 45.596 7.801 13.226 1.00 33.69 ? 84 ILE B CG2 1 ATOM 938 C CD1 . ILE B 2 84 ? 44.008 8.296 10.678 1.00 34.44 ? 84 ILE B CD1 1 ATOM 939 N N . TYR B 2 85 ? 48.661 8.104 14.117 1.00 35.27 ? 85 TYR B N 1 ATOM 940 C CA . TYR B 2 85 ? 49.227 7.490 15.323 1.00 33.84 ? 85 TYR B CA 1 ATOM 941 C C . TYR B 2 85 ? 48.376 7.814 16.524 1.00 34.03 ? 85 TYR B C 1 ATOM 942 O O . TYR B 2 85 ? 48.144 8.978 16.826 1.00 36.99 ? 85 TYR B O 1 ATOM 943 C CB . TYR B 2 85 ? 50.640 7.989 15.608 1.00 34.85 ? 85 TYR B CB 1 ATOM 944 C CG . TYR B 2 85 ? 51.615 7.782 14.487 1.00 35.58 ? 85 TYR B CG 1 ATOM 945 C CD1 . TYR B 2 85 ? 51.720 8.722 13.453 1.00 35.84 ? 85 TYR B CD1 1 ATOM 946 C CD2 . TYR B 2 85 ? 52.450 6.652 14.457 1.00 35.44 ? 85 TYR B CD2 1 ATOM 947 C CE1 . TYR B 2 85 ? 52.623 8.545 12.416 1.00 36.92 ? 85 TYR B CE1 1 ATOM 948 C CE2 . TYR B 2 85 ? 53.353 6.461 13.418 1.00 35.57 ? 85 TYR B CE2 1 ATOM 949 C CZ . TYR B 2 85 ? 53.434 7.411 12.405 1.00 37.56 ? 85 TYR B CZ 1 ATOM 950 O OH . TYR B 2 85 ? 54.315 7.245 11.363 1.00 42.14 ? 85 TYR B OH 1 ATOM 951 N N . ILE B 2 86 ? 47.939 6.780 17.224 1.00 33.50 ? 86 ILE B N 1 ATOM 952 C CA . ILE B 2 86 ? 47.091 6.934 18.383 1.00 34.18 ? 86 ILE B CA 1 ATOM 953 C C . ILE B 2 86 ? 47.862 6.489 19.615 1.00 35.43 ? 86 ILE B C 1 ATOM 954 O O . ILE B 2 86 ? 48.552 5.473 19.575 1.00 36.12 ? 86 ILE B O 1 ATOM 955 C CB . ILE B 2 86 ? 45.789 6.120 18.197 1.00 34.30 ? 86 ILE B CB 1 ATOM 956 C CG1 . ILE B 2 86 ? 45.003 6.697 17.005 1.00 32.17 ? 86 ILE B CG1 1 ATOM 957 C CG2 . ILE B 2 86 ? 44.969 6.047 19.502 1.00 32.81 ? 86 ILE B CG2 1 ATOM 958 C CD1 . ILE B 2 86 ? 43.690 6.003 16.721 1.00 34.71 ? 86 ILE B CD1 1 ATOM 959 N N . HIS B 2 87 ? 47.755 7.240 20.709 1.00 37.26 ? 87 HIS B N 1 ATOM 960 C CA . HIS B 2 87 ? 48.432 6.827 21.934 1.00 42.03 ? 87 HIS B CA 1 ATOM 961 C C . HIS B 2 87 ? 48.099 5.376 22.314 1.00 44.55 ? 87 HIS B C 1 ATOM 962 O O . HIS B 2 87 ? 46.931 4.990 22.389 1.00 43.69 ? 87 HIS B O 1 ATOM 963 C CB . HIS B 2 87 ? 48.150 7.758 23.104 1.00 43.03 ? 87 HIS B CB 1 ATOM 964 C CG . HIS B 2 87 ? 49.152 7.634 24.209 1.00 45.16 ? 87 HIS B CG 1 ATOM 965 N ND1 . HIS B 2 87 ? 49.154 6.579 25.096 1.00 46.26 ? 87 HIS B ND1 1 ATOM 966 C CD2 . HIS B 2 87 ? 50.207 8.412 24.546 1.00 45.08 ? 87 HIS B CD2 1 ATOM 967 C CE1 . HIS B 2 87 ? 50.155 6.723 25.946 1.00 46.17 ? 87 HIS B CE1 1 ATOM 968 N NE2 . HIS B 2 87 ? 50.805 7.830 25.637 1.00 47.55 ? 87 HIS B NE2 1 ATOM 969 N N . PRO B 2 88 ? 49.141 4.559 22.534 1.00 47.39 ? 88 PRO B N 1 ATOM 970 C CA . PRO B 2 88 ? 48.933 3.138 22.805 1.00 47.52 ? 88 PRO B CA 1 ATOM 971 C C . PRO B 2 88 ? 48.082 2.869 24.048 1.00 46.08 ? 88 PRO B C 1 ATOM 972 O O . PRO B 2 88 ? 47.441 1.831 24.125 1.00 47.47 ? 88 PRO B O 1 ATOM 973 C CB . PRO B 2 88 ? 50.360 2.607 22.990 1.00 46.33 ? 88 PRO B CB 1 ATOM 974 C CG . PRO B 2 88 ? 51.180 3.817 23.299 1.00 47.55 ? 88 PRO B CG 1 ATOM 975 C CD . PRO B 2 88 ? 50.573 4.894 22.469 1.00 45.46 ? 88 PRO B CD 1 ATOM 976 N N . ARG B 2 89 ? 48.059 3.797 24.998 1.00 46.40 ? 89 ARG B N 1 ATOM 977 C CA . ARG B 2 89 ? 47.288 3.592 26.232 1.00 45.87 ? 89 ARG B CA 1 ATOM 978 C C . ARG B 2 89 ? 46.068 4.504 26.339 1.00 42.09 ? 89 ARG B C 1 ATOM 979 O O . ARG B 2 89 ? 45.621 4.827 27.440 1.00 41.75 ? 89 ARG B O 1 ATOM 980 C CB . ARG B 2 89 ? 48.196 3.656 27.478 1.00 51.06 ? 89 ARG B CB 1 ATOM 981 C CG . ARG B 2 89 ? 49.231 2.522 27.512 1.00 57.77 ? 89 ARG B CG 1 ATOM 982 C CD . ARG B 2 89 ? 50.151 2.581 28.723 1.00 70.11 ? 89 ARG B CD 1 ATOM 983 N NE . ARG B 2 89 ? 49.444 2.175 29.940 1.00 83.05 ? 89 ARG B NE 1 ATOM 984 C CZ . ARG B 2 89 ? 49.599 2.736 31.138 1.00 85.77 ? 89 ARG B CZ 1 ATOM 985 N NH1 . ARG B 2 89 ? 50.445 3.747 31.314 1.00 87.67 ? 89 ARG B NH1 1 ATOM 986 N NH2 . ARG B 2 89 ? 48.887 2.288 32.165 1.00 87.80 ? 89 ARG B NH2 1 ATOM 987 N N . TYR B 2 90 ? 45.540 4.901 25.177 1.00 39.48 ? 90 TYR B N 1 ATOM 988 C CA . TYR B 2 90 ? 44.282 5.644 25.057 1.00 37.54 ? 90 TYR B CA 1 ATOM 989 C C . TYR B 2 90 ? 43.143 4.786 25.591 1.00 39.22 ? 90 TYR B C 1 ATOM 990 O O . TYR B 2 90 ? 42.864 3.718 25.062 1.00 42.74 ? 90 TYR B O 1 ATOM 991 C CB . TYR B 2 90 ? 44.042 6.025 23.580 1.00 34.47 ? 90 TYR B CB 1 ATOM 992 C CG . TYR B 2 90 ? 42.602 6.355 23.156 1.00 32.37 ? 90 TYR B CG 1 ATOM 993 C CD1 . TYR B 2 90 ? 41.844 7.319 23.835 1.00 31.95 ? 90 TYR B CD1 1 ATOM 994 C CD2 . TYR B 2 90 ? 42.016 5.717 22.053 1.00 31.67 ? 90 TYR B CD2 1 ATOM 995 C CE1 . TYR B 2 90 ? 40.549 7.634 23.438 1.00 31.24 ? 90 TYR B CE1 1 ATOM 996 C CE2 . TYR B 2 90 ? 40.721 6.020 21.646 1.00 31.02 ? 90 TYR B CE2 1 ATOM 997 C CZ . TYR B 2 90 ? 39.986 6.980 22.351 1.00 32.31 ? 90 TYR B CZ 1 ATOM 998 O OH . TYR B 2 90 ? 38.697 7.302 21.966 1.00 31.10 ? 90 TYR B OH 1 ATOM 999 N N . ASN B 2 91 ? 42.483 5.265 26.629 1.00 39.97 ? 91 ASN B N 1 ATOM 1000 C CA . ASN B 2 91 ? 41.453 4.508 27.311 1.00 43.74 ? 91 ASN B CA 1 ATOM 1001 C C . ASN B 2 91 ? 40.028 4.951 26.916 1.00 45.90 ? 91 ASN B C 1 ATOM 1002 O O . ASN B 2 91 ? 39.423 5.821 27.563 1.00 44.27 ? 91 ASN B O 1 ATOM 1003 C CB . ASN B 2 91 ? 41.697 4.629 28.825 1.00 47.91 ? 91 ASN B CB 1 ATOM 1004 C CG . ASN B 2 91 ? 40.767 3.769 29.663 1.00 50.40 ? 91 ASN B CG 1 ATOM 1005 O OD1 . ASN B 2 91 ? 39.935 3.014 29.158 1.00 52.92 ? 91 ASN B OD1 1 ATOM 1006 N ND2 . ASN B 2 91 ? 40.907 3.893 30.971 1.00 52.00 ? 91 ASN B ND2 1 ATOM 1007 N N . TRP B 2 92 ? 39.493 4.341 25.860 1.00 48.88 ? 92 TRP B N 1 ATOM 1008 C CA . TRP B 2 92 ? 38.129 4.648 25.402 1.00 53.71 ? 92 TRP B CA 1 ATOM 1009 C C . TRP B 2 92 ? 37.024 3.962 26.224 1.00 55.95 ? 92 TRP B C 1 ATOM 1010 O O . TRP B 2 92 ? 35.862 4.391 26.188 1.00 57.81 ? 92 TRP B O 1 ATOM 1011 C CB . TRP B 2 92 ? 37.964 4.343 23.905 1.00 55.93 ? 92 TRP B CB 1 ATOM 1012 C CG . TRP B 2 92 ? 38.334 2.938 23.490 1.00 59.08 ? 92 TRP B CG 1 ATOM 1013 C CD1 . TRP B 2 92 ? 39.523 2.526 22.945 1.00 59.67 ? 92 TRP B CD1 1 ATOM 1014 C CD2 . TRP B 2 92 ? 37.507 1.771 23.568 1.00 62.07 ? 92 TRP B CD2 1 ATOM 1015 N NE1 . TRP B 2 92 ? 39.488 1.177 22.688 1.00 61.71 ? 92 TRP B NE1 1 ATOM 1016 C CE2 . TRP B 2 92 ? 38.263 0.687 23.061 1.00 64.62 ? 92 TRP B CE2 1 ATOM 1017 C CE3 . TRP B 2 92 ? 36.201 1.532 24.026 1.00 66.13 ? 92 TRP B CE3 1 ATOM 1018 C CZ2 . TRP B 2 92 ? 37.756 -0.619 22.997 1.00 68.80 ? 92 TRP B CZ2 1 ATOM 1019 C CZ3 . TRP B 2 92 ? 35.694 0.229 23.963 1.00 69.07 ? 92 TRP B CZ3 1 ATOM 1020 C CH2 . TRP B 2 92 ? 36.472 -0.828 23.449 1.00 69.73 ? 92 TRP B CH2 1 ATOM 1021 N N . ARG B 2 93 ? 37.396 2.915 26.964 1.00 58.37 ? 93 ARG B N 1 ATOM 1022 C CA . ARG B 2 93 ? 36.456 2.133 27.777 1.00 61.63 ? 93 ARG B CA 1 ATOM 1023 C C . ARG B 2 93 ? 35.815 2.914 28.919 1.00 59.61 ? 93 ARG B C 1 ATOM 1024 O O . ARG B 2 93 ? 34.603 2.878 29.077 1.00 61.26 ? 93 ARG B O 1 ATOM 1025 C CB . ARG B 2 93 ? 37.127 0.873 28.329 1.00 68.51 ? 93 ARG B CB 1 ATOM 1026 C CG . ARG B 2 93 ? 37.282 -0.240 27.303 1.00 78.20 ? 93 ARG B CG 1 ATOM 1027 C CD . ARG B 2 93 ? 38.154 -1.376 27.840 1.00 86.36 ? 93 ARG B CD 1 ATOM 1028 N NE . ARG B 2 93 ? 38.297 -2.437 26.841 1.00 93.97 ? 93 ARG B NE 1 ATOM 1029 C CZ . ARG B 2 93 ? 39.356 -2.597 26.043 1.00 96.01 ? 93 ARG B CZ 1 ATOM 1030 N NH1 . ARG B 2 93 ? 40.405 -1.774 26.117 1.00 98.98 ? 93 ARG B NH1 1 ATOM 1031 N NH2 . ARG B 2 93 ? 39.371 -3.595 25.166 1.00 94.15 ? 93 ARG B NH2 1 ATOM 1032 N N . GLU B 2 94 ? 36.606 3.633 29.707 1.00 59.78 ? 94 GLU B N 1 ATOM 1033 C CA . GLU B 2 94 ? 36.026 4.284 30.884 1.00 60.28 ? 94 GLU B CA 1 ATOM 1034 C C . GLU B 2 94 ? 36.098 5.803 31.018 1.00 55.85 ? 94 GLU B C 1 ATOM 1035 O O . GLU B 2 94 ? 35.153 6.408 31.521 1.00 56.34 ? 94 GLU B O 1 ATOM 1036 C CB . GLU B 2 94 ? 36.495 3.615 32.181 1.00 66.69 ? 94 GLU B CB 1 ATOM 1037 C CG . GLU B 2 94 ? 37.943 3.176 32.184 1.00 72.22 ? 94 GLU B CG 1 ATOM 1038 C CD . GLU B 2 94 ? 38.519 3.104 33.585 1.00 79.42 ? 94 GLU B CD 1 ATOM 1039 O OE1 . GLU B 2 94 ? 38.118 3.922 34.458 1.00 76.99 ? 94 GLU B OE1 1 ATOM 1040 O OE2 . GLU B 2 94 ? 39.378 2.221 33.804 1.00 79.00 ? 94 GLU B OE2 1 ATOM 1041 N N . ASN B 2 95 ? 37.187 6.438 30.601 1.00 51.07 ? 95 ASN B N 1 ATOM 1042 C CA . ASN B 2 95 ? 37.289 7.884 30.848 1.00 46.45 ? 95 ASN B CA 1 ATOM 1043 C C . ASN B 2 95 ? 37.961 8.759 29.780 1.00 44.07 ? 95 ASN B C 1 ATOM 1044 O O . ASN B 2 95 ? 38.145 9.953 30.003 1.00 44.38 ? 95 ASN B O 1 ATOM 1045 C CB . ASN B 2 95 ? 37.932 8.136 32.217 1.00 42.84 ? 95 ASN B CB 1 ATOM 1046 C CG . ASN B 2 95 ? 39.321 7.541 32.325 1.00 42.31 ? 95 ASN B CG 1 ATOM 1047 O OD1 . ASN B 2 95 ? 39.813 6.852 31.411 1.00 38.64 ? 95 ASN B OD1 1 ATOM 1048 N ND2 . ASN B 2 95 ? 39.966 7.800 33.451 1.00 42.87 ? 95 ASN B ND2 1 ATOM 1049 N N . LEU B 2 96 ? 38.315 8.177 28.636 1.00 42.39 ? 96 LEU B N 1 ATOM 1050 C CA . LEU B 2 96 ? 39.000 8.912 27.552 1.00 42.71 ? 96 LEU B CA 1 ATOM 1051 C C . LEU B 2 96 ? 40.373 9.425 27.980 1.00 43.10 ? 96 LEU B C 1 ATOM 1052 O O . LEU B 2 96 ? 40.800 10.520 27.595 1.00 43.94 ? 96 LEU B O 1 ATOM 1053 C CB . LEU B 2 96 ? 38.133 10.057 26.994 1.00 41.67 ? 96 LEU B CB 1 ATOM 1054 C CG . LEU B 2 96 ? 37.020 9.711 26.002 1.00 40.90 ? 96 LEU B CG 1 ATOM 1055 C CD1 . LEU B 2 96 ? 36.336 10.991 25.562 1.00 40.11 ? 96 LEU B CD1 1 ATOM 1056 C CD2 . LEU B 2 96 ? 37.538 8.933 24.797 1.00 41.89 ? 96 LEU B CD2 1 ATOM 1057 N N . ASP B 2 97 ? 41.057 8.622 28.788 1.00 42.08 ? 97 ASP B N 1 ATOM 1058 C CA . ASP B 2 97 ? 42.369 8.972 29.289 1.00 39.49 ? 97 ASP B CA 1 ATOM 1059 C C . ASP B 2 97 ? 43.355 8.878 28.126 1.00 37.63 ? 97 ASP B C 1 ATOM 1060 O O . ASP B 2 97 ? 43.268 7.959 27.299 1.00 36.38 ? 97 ASP B O 1 ATOM 1061 C CB . ASP B 2 97 ? 42.741 8.049 30.462 1.00 41.13 ? 97 ASP B CB 1 ATOM 1062 C CG . ASP B 2 97 ? 44.070 8.405 31.103 1.00 40.78 ? 97 ASP B CG 1 ATOM 1063 O OD1 . ASP B 2 97 ? 44.289 9.587 31.445 1.00 38.90 ? 97 ASP B OD1 1 ATOM 1064 O OD2 . ASP B 2 97 ? 44.902 7.486 31.257 1.00 43.59 ? 97 ASP B OD2 1 ATOM 1065 N N . ARG B 2 98 ? 44.257 9.858 28.049 1.00 35.63 ? 98 ARG B N 1 ATOM 1066 C CA . ARG B 2 98 ? 45.221 9.979 26.947 1.00 35.18 ? 98 ARG B CA 1 ATOM 1067 C C . ARG B 2 98 ? 44.540 10.121 25.565 1.00 34.08 ? 98 ARG B C 1 ATOM 1068 O O . ARG B 2 98 ? 44.882 9.434 24.589 1.00 33.66 ? 98 ARG B O 1 ATOM 1069 C CB . ARG B 2 98 ? 46.256 8.846 26.985 1.00 38.98 ? 98 ARG B CB 1 ATOM 1070 C CG . ARG B 2 98 ? 47.000 8.767 28.311 1.00 43.09 ? 98 ARG B CG 1 ATOM 1071 C CD . ARG B 2 98 ? 47.911 7.559 28.368 1.00 49.07 ? 98 ARG B CD 1 ATOM 1072 N NE . ARG B 2 98 ? 47.753 6.837 29.632 1.00 54.77 ? 98 ARG B NE 1 ATOM 1073 C CZ . ARG B 2 98 ? 48.549 6.982 30.684 1.00 53.46 ? 98 ARG B CZ 1 ATOM 1074 N NH1 . ARG B 2 98 ? 49.579 7.824 30.645 1.00 52.68 ? 98 ARG B NH1 1 ATOM 1075 N NH2 . ARG B 2 98 ? 48.310 6.281 31.776 1.00 54.58 ? 98 ARG B NH2 1 ATOM 1076 N N . ASP B 2 99 ? 43.575 11.036 25.504 1.00 31.15 ? 99 ASP B N 1 ATOM 1077 C CA . ASP B 2 99 ? 42.829 11.311 24.295 1.00 28.35 ? 99 ASP B CA 1 ATOM 1078 C C . ASP B 2 99 ? 43.666 12.187 23.349 1.00 28.00 ? 99 ASP B C 1 ATOM 1079 O O . ASP B 2 99 ? 43.475 13.398 23.264 1.00 28.29 ? 99 ASP B O 1 ATOM 1080 C CB . ASP B 2 99 ? 41.507 11.984 24.658 1.00 26.13 ? 99 ASP B CB 1 ATOM 1081 C CG . ASP B 2 99 ? 40.544 12.047 23.501 1.00 25.69 ? 99 ASP B CG 1 ATOM 1082 O OD1 . ASP B 2 99 ? 40.728 11.342 22.471 1.00 25.02 ? 99 ASP B OD1 1 ATOM 1083 O OD2 . ASP B 2 99 ? 39.580 12.819 23.633 1.00 26.31 ? 99 ASP B OD2 1 ATOM 1084 N N . ILE B 2 100 ? 44.583 11.557 22.627 1.00 26.43 ? 100 ILE B N 1 ATOM 1085 C CA . ILE B 2 100 ? 45.538 12.288 21.813 1.00 26.69 ? 100 ILE B CA 1 ATOM 1086 C C . ILE B 2 100 ? 45.927 11.459 20.584 1.00 26.00 ? 100 ILE B C 1 ATOM 1087 O O . ILE B 2 100 ? 46.022 10.229 20.655 1.00 26.21 ? 100 ILE B O 1 ATOM 1088 C CB . ILE B 2 100 ? 46.792 12.672 22.661 1.00 26.62 ? 100 ILE B CB 1 ATOM 1089 C CG1 . ILE B 2 100 ? 47.673 13.707 21.943 1.00 26.26 ? 100 ILE B CG1 1 ATOM 1090 C CG2 . ILE B 2 100 ? 47.604 11.437 23.050 1.00 25.53 ? 100 ILE B CG2 1 ATOM 1091 C CD1 . ILE B 2 100 ? 48.692 14.397 22.837 1.00 25.29 ? 100 ILE B CD1 1 ATOM 1092 N N . ALA B 2 101 ? 46.160 12.131 19.465 1.00 24.81 ? 101 ALA B N 1 ATOM 1093 C CA . ALA B 2 101 ? 46.567 11.452 18.242 1.00 25.44 ? 101 ALA B CA 1 ATOM 1094 C C . ALA B 2 101 ? 47.376 12.396 17.403 1.00 25.38 ? 101 ALA B C 1 ATOM 1095 O O . ALA B 2 101 ? 47.138 13.602 17.431 1.00 26.39 ? 101 ALA B O 1 ATOM 1096 C CB . ALA B 2 101 ? 45.351 10.986 17.446 1.00 25.71 ? 101 ALA B CB 1 ATOM 1097 N N . LEU B 2 102 ? 48.322 11.835 16.654 1.00 25.27 ? 102 LEU B N 1 ATOM 1098 C CA . LEU B 2 102 ? 49.085 12.573 15.657 1.00 25.75 ? 102 LEU B CA 1 ATOM 1099 C C . LEU B 2 102 ? 48.766 12.097 14.229 1.00 25.75 ? 102 LEU B C 1 ATOM 1100 O O . LEU B 2 102 ? 48.398 10.937 14.016 1.00 24.41 ? 102 LEU B O 1 ATOM 1101 C CB . LEU B 2 102 ? 50.588 12.463 15.941 1.00 25.82 ? 102 LEU B CB 1 ATOM 1102 C CG . LEU B 2 102 ? 51.185 13.337 17.054 1.00 26.27 ? 102 LEU B CG 1 ATOM 1103 C CD1 . LEU B 2 102 ? 52.517 12.751 17.511 1.00 26.29 ? 102 LEU B CD1 1 ATOM 1104 C CD2 . LEU B 2 102 ? 51.356 14.793 16.618 1.00 25.64 ? 102 LEU B CD2 1 ATOM 1105 N N . MET B 2 103 ? 48.910 12.996 13.260 1.00 25.51 ? 103 MET B N 1 ATOM 1106 C CA . MET B 2 103 ? 48.673 12.664 11.868 1.00 26.91 ? 103 MET B CA 1 ATOM 1107 C C . MET B 2 103 ? 49.785 13.264 11.030 1.00 28.18 ? 103 MET B C 1 ATOM 1108 O O . MET B 2 103 ? 50.095 14.451 11.157 1.00 27.62 ? 103 MET B O 1 ATOM 1109 C CB . MET B 2 103 ? 47.332 13.220 11.374 1.00 28.22 ? 103 MET B CB 1 ATOM 1110 C CG . MET B 2 103 ? 46.090 12.765 12.130 1.00 31.35 ? 103 MET B CG 1 ATOM 1111 S SD . MET B 2 103 ? 44.668 13.779 11.642 1.00 35.32 ? 103 MET B SD 1 ATOM 1112 C CE . MET B 2 103 ? 43.384 12.609 11.984 1.00 34.87 ? 103 MET B CE 1 ATOM 1113 N N . LYS B 2 104 ? 50.369 12.455 10.153 1.00 29.09 ? 104 LYS B N 1 ATOM 1114 C CA . LYS B 2 104 ? 51.432 12.937 9.307 1.00 31.99 ? 104 LYS B CA 1 ATOM 1115 C C . LYS B 2 104 ? 50.868 13.237 7.932 1.00 33.35 ? 104 LYS B C 1 ATOM 1116 O O . LYS B 2 104 ? 50.211 12.393 7.330 1.00 35.50 ? 104 LYS B O 1 ATOM 1117 C CB . LYS B 2 104 ? 52.535 11.896 9.221 1.00 34.12 ? 104 LYS B CB 1 ATOM 1118 C CG . LYS B 2 104 ? 53.856 12.436 8.727 1.00 38.13 ? 104 LYS B CG 1 ATOM 1119 C CD . LYS B 2 104 ? 54.795 11.284 8.419 1.00 44.19 ? 104 LYS B CD 1 ATOM 1120 C CE . LYS B 2 104 ? 56.104 11.780 7.828 1.00 49.13 ? 104 LYS B CE 1 ATOM 1121 N NZ . LYS B 2 104 ? 56.895 10.619 7.338 1.00 55.63 ? 104 LYS B NZ 1 ATOM 1122 N N . LEU B 2 105 ? 51.108 14.444 7.443 1.00 33.36 ? 105 LEU B N 1 ATOM 1123 C CA . LEU B 2 105 ? 50.644 14.825 6.125 1.00 34.63 ? 105 LEU B CA 1 ATOM 1124 C C . LEU B 2 105 ? 51.482 14.133 5.066 1.00 38.52 ? 105 LEU B C 1 ATOM 1125 O O . LEU B 2 105 ? 52.678 13.900 5.268 1.00 40.11 ? 105 LEU B O 1 ATOM 1126 C CB . LEU B 2 105 ? 50.702 16.348 5.943 1.00 32.42 ? 105 LEU B CB 1 ATOM 1127 C CG . LEU B 2 105 ? 49.912 17.232 6.921 1.00 31.14 ? 105 LEU B CG 1 ATOM 1128 C CD1 . LEU B 2 105 ? 49.970 18.692 6.495 1.00 30.47 ? 105 LEU B CD1 1 ATOM 1129 C CD2 . LEU B 2 105 ? 48.473 16.771 7.042 1.00 31.07 ? 105 LEU B CD2 1 ATOM 1130 N N . LYS B 2 106 ? 50.849 13.817 3.936 1.00 42.46 ? 106 LYS B N 1 ATOM 1131 C CA . LYS B 2 106 ? 51.512 13.176 2.800 1.00 45.75 ? 106 LYS B CA 1 ATOM 1132 C C . LYS B 2 106 ? 52.604 14.066 2.183 1.00 46.99 ? 106 LYS B C 1 ATOM 1133 O O . LYS B 2 106 ? 53.668 13.575 1.834 1.00 50.13 ? 106 LYS B O 1 ATOM 1134 C CB . LYS B 2 106 ? 50.469 12.802 1.758 1.00 49.77 ? 106 LYS B CB 1 ATOM 1135 C CG . LYS B 2 106 ? 50.726 11.510 1.014 1.00 56.63 ? 106 LYS B CG 1 ATOM 1136 C CD . LYS B 2 106 ? 49.863 11.478 -0.246 1.00 67.44 ? 106 LYS B CD 1 ATOM 1137 C CE . LYS B 2 106 ? 50.151 10.272 -1.131 1.00 69.78 ? 106 LYS B CE 1 ATOM 1138 N NZ . LYS B 2 106 ? 49.822 9.004 -0.420 1.00 72.80 ? 106 LYS B NZ 1 ATOM 1139 N N . LYS B 2 107 ? 52.329 15.365 2.058 1.00 49.09 ? 107 LYS B N 1 ATOM 1140 C CA . LYS B 2 107 ? 53.295 16.382 1.607 1.00 48.65 ? 107 LYS B CA 1 ATOM 1141 C C . LYS B 2 107 ? 53.316 17.544 2.618 1.00 46.43 ? 107 LYS B C 1 ATOM 1142 O O . LYS B 2 107 ? 52.306 17.815 3.259 1.00 46.10 ? 107 LYS B O 1 ATOM 1143 C CB . LYS B 2 107 ? 52.885 16.941 0.242 1.00 53.60 ? 107 LYS B CB 1 ATOM 1144 C CG . LYS B 2 107 ? 53.160 16.053 -0.963 1.00 62.76 ? 107 LYS B CG 1 ATOM 1145 C CD . LYS B 2 107 ? 51.946 15.958 -1.900 1.00 73.39 ? 107 LYS B CD 1 ATOM 1146 C CE . LYS B 2 107 ? 51.313 17.312 -2.255 1.00 78.21 ? 107 LYS B CE 1 ATOM 1147 N NZ . LYS B 2 107 ? 52.151 18.125 -3.191 1.00 83.86 ? 107 LYS B NZ 1 ATOM 1148 N N . PRO B 2 108 ? 54.461 18.235 2.769 1.00 45.93 ? 108 PRO B N 1 ATOM 1149 C CA . PRO B 2 108 ? 54.512 19.420 3.656 1.00 44.06 ? 108 PRO B CA 1 ATOM 1150 C C . PRO B 2 108 ? 53.668 20.585 3.146 1.00 42.51 ? 108 PRO B C 1 ATOM 1151 O O . PRO B 2 108 ? 53.515 20.716 1.933 1.00 45.45 ? 108 PRO B O 1 ATOM 1152 C CB . PRO B 2 108 ? 56.004 19.805 3.650 1.00 46.44 ? 108 PRO B CB 1 ATOM 1153 C CG . PRO B 2 108 ? 56.603 19.083 2.479 1.00 45.37 ? 108 PRO B CG 1 ATOM 1154 C CD . PRO B 2 108 ? 55.804 17.828 2.311 1.00 44.44 ? 108 PRO B CD 1 ATOM 1155 N N . VAL B 2 109 ? 53.112 21.413 4.042 1.00 38.62 ? 109 VAL B N 1 ATOM 1156 C CA . VAL B 2 109 ? 52.362 22.602 3.596 1.00 36.10 ? 109 VAL B CA 1 ATOM 1157 C C . VAL B 2 109 ? 53.236 23.838 3.664 1.00 35.64 ? 109 VAL B C 1 ATOM 1158 O O . VAL B 2 109 ? 54.098 23.951 4.534 1.00 35.57 ? 109 VAL B O 1 ATOM 1159 C CB . VAL B 2 109 ? 51.019 22.864 4.344 1.00 36.15 ? 109 VAL B CB 1 ATOM 1160 C CG1 . VAL B 2 109 ? 50.062 21.710 4.150 1.00 39.03 ? 109 VAL B CG1 1 ATOM 1161 C CG2 . VAL B 2 109 ? 51.218 23.144 5.832 1.00 36.79 ? 109 VAL B CG2 1 ATOM 1162 N N . ALA B 2 110 ? 53.016 24.752 2.728 1.00 35.33 ? 110 ALA B N 1 ATOM 1163 C CA . ALA B 2 110 ? 53.680 26.050 2.747 1.00 35.20 ? 110 ALA B CA 1 ATOM 1164 C C . ALA B 2 110 ? 52.936 26.937 3.744 1.00 34.08 ? 110 ALA B C 1 ATOM 1165 O O . ALA B 2 110 ? 51.708 26.988 3.731 1.00 35.02 ? 110 ALA B O 1 ATOM 1166 C CB . ALA B 2 110 ? 53.679 26.682 1.360 1.00 33.26 ? 110 ALA B CB 1 ATOM 1167 N N . PHE B 2 111 ? 53.683 27.606 4.616 1.00 31.44 ? 111 PHE B N 1 ATOM 1168 C CA . PHE B 2 111 ? 53.108 28.552 5.539 1.00 30.92 ? 111 PHE B CA 1 ATOM 1169 C C . PHE B 2 111 ? 52.730 29.798 4.758 1.00 31.97 ? 111 PHE B C 1 ATOM 1170 O O . PHE B 2 111 ? 53.164 29.979 3.623 1.00 33.66 ? 111 PHE B O 1 ATOM 1171 C CB . PHE B 2 111 ? 54.074 28.867 6.683 1.00 29.99 ? 111 PHE B CB 1 ATOM 1172 C CG . PHE B 2 111 ? 54.460 27.662 7.501 1.00 31.59 ? 111 PHE B CG 1 ATOM 1173 C CD1 . PHE B 2 111 ? 53.593 26.583 7.643 1.00 32.24 ? 111 PHE B CD1 1 ATOM 1174 C CD2 . PHE B 2 111 ? 55.690 27.602 8.137 1.00 32.76 ? 111 PHE B CD2 1 ATOM 1175 C CE1 . PHE B 2 111 ? 53.948 25.469 8.402 1.00 33.54 ? 111 PHE B CE1 1 ATOM 1176 C CE2 . PHE B 2 111 ? 56.050 26.494 8.902 1.00 33.85 ? 111 PHE B CE2 1 ATOM 1177 C CZ . PHE B 2 111 ? 55.178 25.425 9.035 1.00 33.85 ? 111 PHE B CZ 1 ATOM 1178 N N . SER B 2 112 ? 51.892 30.637 5.350 1.00 31.43 ? 112 SER B N 1 ATOM 1179 C CA . SER B 2 112 ? 51.428 31.842 4.694 1.00 31.64 ? 112 SER B CA 1 ATOM 1180 C C . SER B 2 112 ? 50.861 32.701 5.804 1.00 31.55 ? 112 SER B C 1 ATOM 1181 O O . SER B 2 112 ? 51.074 32.394 6.974 1.00 33.57 ? 112 SER B O 1 ATOM 1182 C CB . SER B 2 112 ? 50.347 31.511 3.664 1.00 31.31 ? 112 SER B CB 1 ATOM 1183 O OG . SER B 2 112 ? 49.157 31.095 4.314 1.00 32.49 ? 112 SER B OG 1 ATOM 1184 N N . ASP B 2 113 ? 50.131 33.753 5.448 1.00 30.43 ? 113 ASP B N 1 ATOM 1185 C CA . ASP B 2 113 ? 49.512 34.611 6.443 1.00 31.25 ? 113 ASP B CA 1 ATOM 1186 C C . ASP B 2 113 ? 48.405 33.907 7.211 1.00 31.00 ? 113 ASP B C 1 ATOM 1187 O O . ASP B 2 113 ? 48.024 34.357 8.287 1.00 32.53 ? 113 ASP B O 1 ATOM 1188 C CB . ASP B 2 113 ? 48.945 35.869 5.787 1.00 32.13 ? 113 ASP B CB 1 ATOM 1189 C CG . ASP B 2 113 ? 50.021 36.845 5.340 1.00 34.90 ? 113 ASP B CG 1 ATOM 1190 O OD1 . ASP B 2 113 ? 51.236 36.640 5.618 1.00 35.84 ? 113 ASP B OD1 1 ATOM 1191 O OD2 . ASP B 2 113 ? 49.630 37.846 4.709 1.00 36.51 ? 113 ASP B OD2 1 ATOM 1192 N N . TYR B 2 114 ? 47.896 32.813 6.654 1.00 29.49 ? 114 TYR B N 1 ATOM 1193 C CA . TYR B 2 114 ? 46.717 32.144 7.185 1.00 30.14 ? 114 TYR B CA 1 ATOM 1194 C C . TYR B 2 114 ? 47.035 30.763 7.743 1.00 29.17 ? 114 TYR B C 1 ATOM 1195 O O . TYR B 2 114 ? 46.174 30.128 8.341 1.00 30.73 ? 114 TYR B O 1 ATOM 1196 C CB . TYR B 2 114 ? 45.634 32.042 6.097 1.00 31.56 ? 114 TYR B CB 1 ATOM 1197 C CG . TYR B 2 114 ? 45.377 33.363 5.442 1.00 33.68 ? 114 TYR B CG 1 ATOM 1198 C CD1 . TYR B 2 114 ? 44.533 34.309 6.044 1.00 34.55 ? 114 TYR B CD1 1 ATOM 1199 C CD2 . TYR B 2 114 ? 46.016 33.700 4.231 1.00 34.87 ? 114 TYR B CD2 1 ATOM 1200 C CE1 . TYR B 2 114 ? 44.321 35.544 5.452 1.00 36.11 ? 114 TYR B CE1 1 ATOM 1201 C CE2 . TYR B 2 114 ? 45.811 34.929 3.627 1.00 34.02 ? 114 TYR B CE2 1 ATOM 1202 C CZ . TYR B 2 114 ? 44.963 35.841 4.239 1.00 36.67 ? 114 TYR B CZ 1 ATOM 1203 O OH . TYR B 2 114 ? 44.761 37.057 3.655 1.00 37.78 ? 114 TYR B OH 1 ATOM 1204 N N . ILE B 2 115 ? 48.264 30.310 7.530 1.00 27.23 ? 115 ILE B N 1 ATOM 1205 C CA . ILE B 2 115 ? 48.710 29.001 7.957 1.00 27.25 ? 115 ILE B CA 1 ATOM 1206 C C . ILE B 2 115 ? 50.058 29.150 8.669 1.00 28.68 ? 115 ILE B C 1 ATOM 1207 O O . ILE B 2 115 ? 51.049 29.554 8.058 1.00 29.64 ? 115 ILE B O 1 ATOM 1208 C CB . ILE B 2 115 ? 48.856 28.054 6.747 1.00 27.20 ? 115 ILE B CB 1 ATOM 1209 C CG1 . ILE B 2 115 ? 47.521 27.949 5.970 1.00 26.12 ? 115 ILE B CG1 1 ATOM 1210 C CG2 . ILE B 2 115 ? 49.397 26.697 7.189 1.00 25.06 ? 115 ILE B CG2 1 ATOM 1211 C CD1 . ILE B 2 115 ? 47.624 27.243 4.630 1.00 23.72 ? 115 ILE B CD1 1 ATOM 1212 N N . HIS B 2 116 ? 50.081 28.832 9.963 1.00 29.14 ? 116 HIS B N 1 ATOM 1213 C CA . HIS B 2 116 ? 51.269 28.997 10.818 1.00 28.94 ? 116 HIS B CA 1 ATOM 1214 C C . HIS B 2 116 ? 51.128 28.087 12.051 1.00 26.41 ? 116 HIS B C 1 ATOM 1215 O O . HIS B 2 116 ? 50.037 27.989 12.623 1.00 27.09 ? 116 HIS B O 1 ATOM 1216 C CB . HIS B 2 116 ? 51.431 30.467 11.244 1.00 31.58 ? 116 HIS B CB 1 ATOM 1217 C CG . HIS B 2 116 ? 52.781 30.781 11.812 1.00 36.65 ? 116 HIS B CG 1 ATOM 1218 N ND1 . HIS B 2 116 ? 53.892 30.995 11.019 1.00 36.88 ? 116 HIS B ND1 1 ATOM 1219 C CD2 . HIS B 2 116 ? 53.208 30.889 13.095 1.00 39.45 ? 116 HIS B CD2 1 ATOM 1220 C CE1 . HIS B 2 116 ? 54.944 31.216 11.790 1.00 39.38 ? 116 HIS B CE1 1 ATOM 1221 N NE2 . HIS B 2 116 ? 54.556 31.167 13.054 1.00 41.11 ? 116 HIS B NE2 1 ATOM 1222 N N . PRO B 2 117 ? 52.212 27.406 12.461 1.00 23.77 ? 117 PRO B N 1 ATOM 1223 C CA . PRO B 2 117 ? 52.085 26.449 13.581 1.00 22.37 ? 117 PRO B CA 1 ATOM 1224 C C . PRO B 2 117 ? 52.074 27.107 14.960 1.00 22.22 ? 117 PRO B C 1 ATOM 1225 O O . PRO B 2 117 ? 52.532 28.247 15.120 1.00 23.87 ? 117 PRO B O 1 ATOM 1226 C CB . PRO B 2 117 ? 53.333 25.558 13.431 1.00 22.11 ? 117 PRO B CB 1 ATOM 1227 C CG . PRO B 2 117 ? 54.323 26.418 12.719 1.00 21.84 ? 117 PRO B CG 1 ATOM 1228 C CD . PRO B 2 117 ? 53.559 27.388 11.854 1.00 22.38 ? 117 PRO B CD 1 ATOM 1229 N N . VAL B 2 118 ? 51.554 26.382 15.942 1.00 21.25 ? 118 VAL B N 1 ATOM 1230 C CA . VAL B 2 118 ? 51.472 26.830 17.331 1.00 20.62 ? 118 VAL B CA 1 ATOM 1231 C C . VAL B 2 118 ? 52.670 26.197 18.070 1.00 21.77 ? 118 VAL B C 1 ATOM 1232 O O . VAL B 2 118 ? 53.183 25.172 17.638 1.00 23.56 ? 118 VAL B O 1 ATOM 1233 C CB . VAL B 2 118 ? 50.096 26.411 17.953 1.00 19.32 ? 118 VAL B CB 1 ATOM 1234 C CG1 . VAL B 2 118 ? 50.000 24.901 18.144 1.00 18.02 ? 118 VAL B CG1 1 ATOM 1235 C CG2 . VAL B 2 118 ? 49.809 27.144 19.258 1.00 18.41 ? 118 VAL B CG2 1 ATOM 1236 N N . CYS B 2 119 ? 53.129 26.788 19.164 1.00 21.56 ? 119 CYS B N 1 ATOM 1237 C CA . CYS B 2 119 ? 54.203 26.167 19.927 1.00 21.39 ? 119 CYS B CA 1 ATOM 1238 C C . CYS B 2 119 ? 53.614 25.158 20.885 1.00 22.24 ? 119 CYS B C 1 ATOM 1239 O O . CYS B 2 119 ? 52.506 25.352 21.406 1.00 22.17 ? 119 CYS B O 1 ATOM 1240 C CB . CYS B 2 119 ? 54.997 27.216 20.710 1.00 21.32 ? 119 CYS B CB 1 ATOM 1241 S SG . CYS B 2 119 ? 55.597 28.580 19.699 1.00 22.63 ? 119 CYS B SG 1 ATOM 1242 N N . LEU B 2 120 ? 54.357 24.082 21.120 1.00 23.80 ? 120 LEU B N 1 ATOM 1243 C CA . LEU B 2 120 ? 54.085 23.181 22.238 1.00 25.80 ? 120 LEU B CA 1 ATOM 1244 C C . LEU B 2 120 ? 54.874 23.689 23.458 1.00 27.05 ? 120 LEU B C 1 ATOM 1245 O O . LEU B 2 120 ? 55.927 24.303 23.295 1.00 27.86 ? 120 LEU B O 1 ATOM 1246 C CB . LEU B 2 120 ? 54.455 21.745 21.871 1.00 26.34 ? 120 LEU B CB 1 ATOM 1247 C CG . LEU B 2 120 ? 53.613 21.073 20.776 1.00 27.70 ? 120 LEU B CG 1 ATOM 1248 C CD1 . LEU B 2 120 ? 54.076 19.656 20.490 1.00 27.74 ? 120 LEU B CD1 1 ATOM 1249 C CD2 . LEU B 2 120 ? 52.134 21.048 21.134 1.00 28.22 ? 120 LEU B CD2 1 ATOM 1250 N N . PRO B 2 121 ? 54.357 23.484 24.679 1.00 28.00 ? 121 PRO B N 1 ATOM 1251 C CA . PRO B 2 121 ? 55.036 24.089 25.831 1.00 29.70 ? 121 PRO B CA 1 ATOM 1252 C C . PRO B 2 121 ? 56.229 23.279 26.366 1.00 32.88 ? 121 PRO B C 1 ATOM 1253 O O . PRO B 2 121 ? 56.234 22.042 26.303 1.00 35.00 ? 121 PRO B O 1 ATOM 1254 C CB . PRO B 2 121 ? 53.923 24.133 26.892 1.00 29.28 ? 121 PRO B CB 1 ATOM 1255 C CG . PRO B 2 121 ? 53.070 22.949 26.565 1.00 28.71 ? 121 PRO B CG 1 ATOM 1256 C CD . PRO B 2 121 ? 53.089 22.833 25.063 1.00 28.21 ? 121 PRO B CD 1 ATOM 1257 N N . ASP B 2 122 ? 57.227 23.979 26.900 1.00 35.11 ? 122 ASP B N 1 ATOM 1258 C CA . ASP B 2 122 ? 58.278 23.347 27.698 1.00 35.24 ? 122 ASP B CA 1 ATOM 1259 C C . ASP B 2 122 ? 57.820 23.283 29.160 1.00 36.00 ? 122 ASP B C 1 ATOM 1260 O O . ASP B 2 122 ? 56.723 23.754 29.502 1.00 34.03 ? 122 ASP B O 1 ATOM 1261 C CB . ASP B 2 122 ? 59.573 24.133 27.571 1.00 36.30 ? 122 ASP B CB 1 ATOM 1262 C CG . ASP B 2 122 ? 59.449 25.548 28.089 1.00 41.50 ? 122 ASP B CG 1 ATOM 1263 O OD1 . ASP B 2 122 ? 58.332 26.061 28.274 1.00 42.78 ? 122 ASP B OD1 1 ATOM 1264 O OD2 . ASP B 2 122 ? 60.487 26.176 28.328 1.00 50.51 ? 122 ASP B OD2 1 ATOM 1265 N N . ARG B 2 123 ? 58.660 22.705 30.015 1.00 36.98 ? 123 ARG B N 1 ATOM 1266 C CA . ARG B 2 123 ? 58.369 22.561 31.444 1.00 37.30 ? 123 ARG B CA 1 ATOM 1267 C C . ARG B 2 123 ? 58.070 23.892 32.168 1.00 37.17 ? 123 ARG B C 1 ATOM 1268 O O . ARG B 2 123 ? 57.135 23.962 32.975 1.00 36.48 ? 123 ARG B O 1 ATOM 1269 C CB . ARG B 2 123 ? 59.509 21.792 32.134 1.00 39.17 ? 123 ARG B CB 1 ATOM 1270 C CG . ARG B 2 123 ? 59.180 21.294 33.533 1.00 42.29 ? 123 ARG B CG 1 ATOM 1271 C CD . ARG B 2 123 ? 60.350 20.545 34.152 0.50 44.68 ? 123 ARG B CD 1 ATOM 1272 N NE . ARG B 2 123 ? 60.282 20.564 35.613 0.50 47.64 ? 123 ARG B NE 1 ATOM 1273 C CZ . ARG B 2 123 ? 60.733 19.591 36.403 0.50 47.46 ? 123 ARG B CZ 1 ATOM 1274 N NH1 . ARG B 2 123 ? 61.272 18.496 35.878 0.50 45.67 ? 123 ARG B NH1 1 ATOM 1275 N NH2 . ARG B 2 123 ? 60.630 19.708 37.721 0.50 45.79 ? 123 ARG B NH2 1 ATOM 1276 N N . GLU B 2 124 ? 58.834 24.945 31.866 1.00 37.53 ? 124 GLU B N 1 ATOM 1277 C CA . GLU B 2 124 ? 58.705 26.226 32.584 1.00 40.34 ? 124 GLU B CA 1 ATOM 1278 C C . GLU B 2 124 ? 57.409 26.935 32.218 1.00 38.07 ? 124 GLU B C 1 ATOM 1279 O O . GLU B 2 124 ? 56.717 27.465 33.085 1.00 37.75 ? 124 GLU B O 1 ATOM 1280 C CB . GLU B 2 124 ? 59.919 27.138 32.348 1.00 47.03 ? 124 GLU B CB 1 ATOM 1281 C CG . GLU B 2 124 ? 61.231 26.653 32.988 1.00 59.87 ? 124 GLU B CG 1 ATOM 1282 C CD . GLU B 2 124 ? 61.822 25.383 32.339 1.00 70.92 ? 124 GLU B CD 1 ATOM 1283 O OE1 . GLU B 2 124 ? 61.915 25.299 31.084 1.00 73.32 ? 124 GLU B OE1 1 ATOM 1284 O OE2 . GLU B 2 124 ? 62.204 24.451 33.090 1.00 74.96 ? 124 GLU B OE2 1 ATOM 1285 N N . THR B 2 125 ? 57.079 26.905 30.929 1.00 36.34 ? 125 THR B N 1 ATOM 1286 C CA . THR B 2 125 ? 55.830 27.439 30.408 1.00 33.53 ? 125 THR B CA 1 ATOM 1287 C C . THR B 2 125 ? 54.607 26.714 30.988 1.00 33.40 ? 125 THR B C 1 ATOM 1288 O O . THR B 2 125 ? 53.690 27.366 31.504 1.00 34.65 ? 125 THR B O 1 ATOM 1289 C CB . THR B 2 125 ? 55.836 27.417 28.877 1.00 32.92 ? 125 THR B CB 1 ATOM 1290 O OG1 . THR B 2 125 ? 56.896 28.262 28.414 1.00 32.57 ? 125 THR B OG1 1 ATOM 1291 C CG2 . THR B 2 125 ? 54.537 27.922 28.321 1.00 31.86 ? 125 THR B CG2 1 ATOM 1292 N N . ALA B 2 126 ? 54.604 25.385 30.942 1.00 30.78 ? 126 ALA B N 1 ATOM 1293 C CA . ALA B 2 126 ? 53.517 24.607 31.542 1.00 30.42 ? 126 ALA B CA 1 ATOM 1294 C C . ALA B 2 126 ? 53.299 24.935 33.020 1.00 32.55 ? 126 ALA B C 1 ATOM 1295 O O . ALA B 2 126 ? 52.162 25.133 33.445 1.00 34.26 ? 126 ALA B O 1 ATOM 1296 C CB . ALA B 2 126 ? 53.754 23.116 31.364 1.00 29.51 ? 126 ALA B CB 1 ATOM 1297 N N . ALA B 2 127 ? 54.379 24.989 33.803 1.00 33.31 ? 127 ALA B N 1 ATOM 1298 C CA . ALA B 2 127 ? 54.271 25.289 35.241 1.00 33.17 ? 127 ALA B CA 1 ATOM 1299 C C . ALA B 2 127 ? 53.791 26.714 35.536 1.00 32.73 ? 127 ALA B C 1 ATOM 1300 O O . ALA B 2 127 ? 53.021 26.918 36.466 1.00 34.24 ? 127 ALA B O 1 ATOM 1301 C CB . ALA B 2 127 ? 55.579 25.002 35.959 1.00 30.92 ? 127 ALA B CB 1 ATOM 1302 N N . SER B 2 128 ? 54.229 27.684 34.737 1.00 31.07 ? 128 SER B N 1 ATOM 1303 C CA . SER B 2 128 ? 53.789 29.066 34.889 1.00 31.33 ? 128 SER B CA 1 ATOM 1304 C C . SER B 2 128 ? 52.338 29.301 34.479 1.00 32.15 ? 128 SER B C 1 ATOM 1305 O O . SER B 2 128 ? 51.611 30.013 35.170 1.00 32.21 ? 128 SER B O 1 ATOM 1306 C CB . SER B 2 128 ? 54.633 29.988 34.022 1.00 31.94 ? 128 SER B CB 1 ATOM 1307 O OG . SER B 2 128 ? 55.983 29.925 34.381 1.00 33.45 ? 128 SER B OG 1 ATOM 1308 N N . LEU B 2 129 ? 51.937 28.741 33.331 1.00 30.83 ? 129 LEU B N 1 ATOM 1309 C CA . LEU B 2 129 ? 50.679 29.124 32.685 1.00 28.23 ? 129 LEU B CA 1 ATOM 1310 C C . LEU B 2 129 ? 49.492 28.275 33.108 1.00 28.47 ? 129 LEU B C 1 ATOM 1311 O O . LEU B 2 129 ? 48.365 28.770 33.170 1.00 27.80 ? 129 LEU B O 1 ATOM 1312 C CB . LEU B 2 129 ? 50.826 29.144 31.163 1.00 28.09 ? 129 LEU B CB 1 ATOM 1313 C CG . LEU B 2 129 ? 51.760 30.185 30.519 1.00 28.03 ? 129 LEU B CG 1 ATOM 1314 C CD1 . LEU B 2 129 ? 51.678 30.127 29.005 1.00 27.44 ? 129 LEU B CD1 1 ATOM 1315 C CD2 . LEU B 2 129 ? 51.470 31.605 30.999 1.00 27.96 ? 129 LEU B CD2 1 ATOM 1316 N N . LEU B 2 130 ? 49.737 27.010 33.428 1.00 28.63 ? 130 LEU B N 1 ATOM 1317 C CA . LEU B 2 130 ? 48.648 26.125 33.822 1.00 31.45 ? 130 LEU B CA 1 ATOM 1318 C C . LEU B 2 130 ? 48.236 26.234 35.266 1.00 31.95 ? 130 LEU B C 1 ATOM 1319 O O . LEU B 2 130 ? 48.491 25.314 36.039 1.00 32.50 ? 130 LEU B O 1 ATOM 1320 C CB . LEU B 2 130 ? 49.005 24.677 33.549 1.00 33.78 ? 130 LEU B CB 1 ATOM 1321 C CG . LEU B 2 130 ? 48.449 24.059 32.281 1.00 36.35 ? 130 LEU B CG 1 ATOM 1322 C CD1 . LEU B 2 130 ? 48.771 22.587 32.391 1.00 39.14 ? 130 LEU B CD1 1 ATOM 1323 C CD2 . LEU B 2 130 ? 46.946 24.258 32.138 1.00 36.42 ? 130 LEU B CD2 1 ATOM 1324 N N . GLN B 2 131 ? 47.579 27.337 35.620 1.00 33.23 ? 131 GLN B N 1 ATOM 1325 C CA . GLN B 2 131 ? 47.139 27.585 36.997 1.00 33.96 ? 131 GLN B CA 1 ATOM 1326 C C . GLN B 2 131 ? 45.684 28.018 37.016 1.00 33.84 ? 131 GLN B C 1 ATOM 1327 O O . GLN B 2 131 ? 45.263 28.833 36.183 1.00 35.25 ? 131 GLN B O 1 ATOM 1328 C CB . GLN B 2 131 ? 47.986 28.682 37.657 1.00 35.05 ? 131 GLN B CB 1 ATOM 1329 C CG . GLN B 2 131 ? 49.481 28.386 37.732 1.00 37.44 ? 131 GLN B CG 1 ATOM 1330 C CD . GLN B 2 131 ? 50.249 29.415 38.560 1.00 39.16 ? 131 GLN B CD 1 ATOM 1331 O OE1 . GLN B 2 131 ? 51.096 30.160 38.041 1.00 38.43 ? 131 GLN B OE1 1 ATOM 1332 N NE2 . GLN B 2 131 ? 49.949 29.467 39.851 1.00 39.40 ? 131 GLN B NE2 1 ATOM 1333 N N . ALA B 2 132 ? 44.927 27.486 37.976 1.00 31.91 ? 132 ALA B N 1 ATOM 1334 C CA . ALA B 2 132 ? 43.519 27.835 38.167 1.00 30.29 ? 132 ALA B CA 1 ATOM 1335 C C . ALA B 2 132 ? 43.302 29.343 38.115 1.00 31.26 ? 132 ALA B C 1 ATOM 1336 O O . ALA B 2 132 ? 44.060 30.098 38.713 1.00 33.53 ? 132 ALA B O 1 ATOM 1337 C CB . ALA B 2 132 ? 43.019 27.279 39.488 1.00 28.41 ? 132 ALA B CB 1 ATOM 1338 N N . GLY B 2 133 ? 42.282 29.789 37.389 1.00 31.33 ? 133 GLY B N 1 ATOM 1339 C CA . GLY B 2 133 ? 41.982 31.220 37.298 1.00 28.60 ? 133 GLY B CA 1 ATOM 1340 C C . GLY B 2 133 ? 42.574 31.904 36.085 1.00 29.70 ? 133 GLY B C 1 ATOM 1341 O O . GLY B 2 133 ? 42.071 32.936 35.649 1.00 30.13 ? 133 GLY B O 1 ATOM 1342 N N . TYR B 2 134 ? 43.651 31.349 35.532 1.00 30.86 ? 134 TYR B N 1 ATOM 1343 C CA . TYR B 2 134 ? 44.186 31.865 34.271 1.00 31.25 ? 134 TYR B CA 1 ATOM 1344 C C . TYR B 2 134 ? 43.283 31.412 33.095 1.00 29.92 ? 134 TYR B C 1 ATOM 1345 O O . TYR B 2 134 ? 42.699 30.318 33.131 1.00 27.62 ? 134 TYR B O 1 ATOM 1346 C CB . TYR B 2 134 ? 45.636 31.400 34.048 1.00 32.99 ? 134 TYR B CB 1 ATOM 1347 C CG . TYR B 2 134 ? 46.694 31.994 34.971 1.00 35.33 ? 134 TYR B CG 1 ATOM 1348 C CD1 . TYR B 2 134 ? 46.388 33.022 35.895 1.00 38.20 ? 134 TYR B CD1 1 ATOM 1349 C CD2 . TYR B 2 134 ? 48.006 31.514 34.939 1.00 35.29 ? 134 TYR B CD2 1 ATOM 1350 C CE1 . TYR B 2 134 ? 47.364 33.549 36.740 1.00 36.38 ? 134 TYR B CE1 1 ATOM 1351 C CE2 . TYR B 2 134 ? 48.983 32.034 35.775 1.00 36.73 ? 134 TYR B CE2 1 ATOM 1352 C CZ . TYR B 2 134 ? 48.659 33.051 36.667 1.00 38.53 ? 134 TYR B CZ 1 ATOM 1353 O OH . TYR B 2 134 ? 49.648 33.564 37.478 1.00 43.04 ? 134 TYR B OH 1 ATOM 1354 N N . LYS B 2 135 ? 43.195 32.254 32.066 1.00 27.80 ? 135 LYS B N 1 ATOM 1355 C CA . LYS B 2 135 ? 42.326 32.023 30.919 1.00 27.39 ? 135 LYS B CA 1 ATOM 1356 C C . LYS B 2 135 ? 43.075 31.573 29.660 1.00 28.08 ? 135 LYS B C 1 ATOM 1357 O O . LYS B 2 135 ? 44.085 32.168 29.279 1.00 29.90 ? 135 LYS B O 1 ATOM 1358 C CB . LYS B 2 135 ? 41.558 33.302 30.588 1.00 27.06 ? 135 LYS B CB 1 ATOM 1359 C CG . LYS B 2 135 ? 40.426 33.621 31.540 1.00 26.55 ? 135 LYS B CG 1 ATOM 1360 C CD . LYS B 2 135 ? 39.829 34.968 31.204 1.00 26.11 ? 135 LYS B CD 1 ATOM 1361 C CE . LYS B 2 135 ? 38.721 35.334 32.183 1.00 25.99 ? 135 LYS B CE 1 ATOM 1362 N NZ . LYS B 2 135 ? 38.077 36.603 31.752 1.00 25.44 ? 135 LYS B NZ 1 ATOM 1363 N N . GLY B 2 136 ? 42.563 30.524 29.021 1.00 26.79 ? 136 GLY B N 1 ATOM 1364 C CA . GLY B 2 136 ? 42.974 30.131 27.677 1.00 26.05 ? 136 GLY B CA 1 ATOM 1365 C C . GLY B 2 136 ? 41.870 30.352 26.644 1.00 27.27 ? 136 GLY B C 1 ATOM 1366 O O . GLY B 2 136 ? 40.764 30.836 26.960 1.00 26.73 ? 136 GLY B O 1 ATOM 1367 N N . ARG B 2 137 ? 42.164 29.980 25.404 1.00 26.00 ? 137 ARG B N 1 ATOM 1368 C CA . ARG B 2 137 ? 41.254 30.215 24.299 1.00 25.56 ? 137 ARG B CA 1 ATOM 1369 C C . ARG B 2 137 ? 40.953 28.936 23.519 1.00 26.09 ? 137 ARG B C 1 ATOM 1370 O O . ARG B 2 137 ? 41.867 28.154 23.212 1.00 27.49 ? 137 ARG B O 1 ATOM 1371 C CB . ARG B 2 137 ? 41.865 31.257 23.379 1.00 24.47 ? 137 ARG B CB 1 ATOM 1372 C CG . ARG B 2 137 ? 41.117 31.459 22.083 1.00 23.43 ? 137 ARG B CG 1 ATOM 1373 C CD . ARG B 2 137 ? 41.804 32.545 21.287 1.00 22.78 ? 137 ARG B CD 1 ATOM 1374 N NE . ARG B 2 137 ? 41.539 33.893 21.789 1.00 22.25 ? 137 ARG B NE 1 ATOM 1375 C CZ . ARG B 2 137 ? 42.148 34.980 21.313 1.00 23.06 ? 137 ARG B CZ 1 ATOM 1376 N NH1 . ARG B 2 137 ? 43.058 34.857 20.349 1.00 24.11 ? 137 ARG B NH1 1 ATOM 1377 N NH2 . ARG B 2 137 ? 41.864 36.186 21.788 1.00 21.72 ? 137 ARG B NH2 1 ATOM 1378 N N . VAL B 2 138 ? 39.677 28.725 23.199 1.00 25.24 ? 138 VAL B N 1 ATOM 1379 C CA . VAL B 2 138 ? 39.258 27.577 22.376 1.00 24.57 ? 138 VAL B CA 1 ATOM 1380 C C . VAL B 2 138 ? 38.655 28.090 21.074 1.00 24.25 ? 138 VAL B C 1 ATOM 1381 O O . VAL B 2 138 ? 37.932 29.094 21.088 1.00 26.40 ? 138 VAL B O 1 ATOM 1382 C CB . VAL B 2 138 ? 38.214 26.691 23.093 1.00 23.75 ? 138 VAL B CB 1 ATOM 1383 C CG1 . VAL B 2 138 ? 37.979 25.410 22.313 1.00 23.95 ? 138 VAL B CG1 1 ATOM 1384 C CG2 . VAL B 2 138 ? 38.682 26.339 24.488 1.00 24.55 ? 138 VAL B CG2 1 ATOM 1385 N N . THR B 2 139 ? 38.953 27.424 19.962 1.00 22.96 ? 139 THR B N 1 ATOM 1386 C CA . THR B 2 139 ? 38.358 27.777 18.670 1.00 22.78 ? 139 THR B CA 1 ATOM 1387 C C . THR B 2 139 ? 37.787 26.551 17.949 1.00 23.81 ? 139 THR B C 1 ATOM 1388 O O . THR B 2 139 ? 38.242 25.412 18.172 1.00 24.88 ? 139 THR B O 1 ATOM 1389 C CB . THR B 2 139 ? 39.364 28.506 17.751 1.00 22.23 ? 139 THR B CB 1 ATOM 1390 O OG1 . THR B 2 139 ? 40.575 27.767 17.708 1.00 22.07 ? 139 THR B OG1 1 ATOM 1391 C CG2 . THR B 2 139 ? 39.681 29.911 18.267 1.00 21.69 ? 139 THR B CG2 1 ATOM 1392 N N . GLY B 2 140 ? 36.779 26.774 17.104 1.00 22.78 ? 140 GLY B N 1 ATOM 1393 C CA . GLY B 2 140 ? 36.213 25.690 16.314 1.00 22.03 ? 140 GLY B CA 1 ATOM 1394 C C . GLY B 2 140 ? 34.958 26.037 15.529 1.00 23.29 ? 140 GLY B C 1 ATOM 1395 O O . GLY B 2 140 ? 34.396 27.130 15.653 1.00 23.77 ? 140 GLY B O 1 ATOM 1396 N N . TRP B 2 141 ? 34.516 25.091 14.712 1.00 22.98 ? 141 TRP B N 1 ATOM 1397 C CA . TRP B 2 141 ? 33.346 25.291 13.880 1.00 23.78 ? 141 TRP B CA 1 ATOM 1398 C C . TRP B 2 141 ? 32.193 24.409 14.395 1.00 25.72 ? 141 TRP B C 1 ATOM 1399 O O . TRP B 2 141 ? 31.215 24.172 13.678 1.00 26.40 ? 141 TRP B O 1 ATOM 1400 C CB . TRP B 2 141 ? 33.644 24.950 12.406 1.00 21.47 ? 141 TRP B CB 1 ATOM 1401 C CG . TRP B 2 141 ? 34.622 25.826 11.684 1.00 20.18 ? 141 TRP B CG 1 ATOM 1402 C CD1 . TRP B 2 141 ? 34.358 27.018 11.060 1.00 20.47 ? 141 TRP B CD1 1 ATOM 1403 C CD2 . TRP B 2 141 ? 36.017 25.549 11.438 1.00 19.65 ? 141 TRP B CD2 1 ATOM 1404 N NE1 . TRP B 2 141 ? 35.511 27.520 10.471 1.00 19.76 ? 141 TRP B NE1 1 ATOM 1405 C CE2 . TRP B 2 141 ? 36.537 26.634 10.681 1.00 19.29 ? 141 TRP B CE2 1 ATOM 1406 C CE3 . TRP B 2 141 ? 36.881 24.507 11.803 1.00 19.33 ? 141 TRP B CE3 1 ATOM 1407 C CZ2 . TRP B 2 141 ? 37.879 26.692 10.273 1.00 18.95 ? 141 TRP B CZ2 1 ATOM 1408 C CZ3 . TRP B 2 141 ? 38.231 24.571 11.391 1.00 19.40 ? 141 TRP B CZ3 1 ATOM 1409 C CH2 . TRP B 2 141 ? 38.705 25.650 10.631 1.00 18.99 ? 141 TRP B CH2 1 ATOM 1410 N N . GLY B 2 142 ? 32.308 23.918 15.629 1.00 26.60 ? 142 GLY B N 1 ATOM 1411 C CA . GLY B 2 142 ? 31.262 23.082 16.215 1.00 26.04 ? 142 GLY B CA 1 ATOM 1412 C C . GLY B 2 142 ? 29.992 23.845 16.565 1.00 26.83 ? 142 GLY B C 1 ATOM 1413 O O . GLY B 2 142 ? 29.922 25.068 16.398 1.00 25.49 ? 142 GLY B O 1 ATOM 1414 N N . ASN B 2 143 ? 29.004 23.111 17.086 1.00 27.82 ? 143 ASN B N 1 ATOM 1415 C CA . ASN B 2 143 ? 27.655 23.629 17.359 1.00 26.83 ? 143 ASN B CA 1 ATOM 1416 C C . ASN B 2 143 ? 27.625 24.815 18.315 1.00 27.39 ? 143 ASN B C 1 ATOM 1417 O O . ASN B 2 143 ? 28.464 24.918 19.223 1.00 29.55 ? 143 ASN B O 1 ATOM 1418 C CB . ASN B 2 143 ? 26.736 22.505 17.869 1.00 27.02 ? 143 ASN B CB 1 ATOM 1419 C CG . ASN B 2 143 ? 26.521 21.388 16.841 1.00 27.69 ? 143 ASN B CG 1 ATOM 1420 O OD1 . ASN B 2 143 ? 26.747 21.560 15.635 1.00 28.47 ? 143 ASN B OD1 1 ATOM 1421 N ND2 . ASN B 2 143 ? 26.065 20.241 17.317 1.00 27.12 ? 143 ASN B ND2 1 ATOM 1422 N N . LEU B 2 144 ? 26.652 25.700 18.090 1.00 27.03 ? 144 LEU B N 1 ATOM 1423 C CA . LEU B 2 144 ? 26.460 26.939 18.848 1.00 27.76 ? 144 LEU B CA 1 ATOM 1424 C C . LEU B 2 144 ? 25.592 26.791 20.117 1.00 29.44 ? 144 LEU B C 1 ATOM 1425 O O . LEU B 2 144 ? 25.528 27.712 20.946 1.00 28.58 ? 144 LEU B O 1 ATOM 1426 C CB . LEU B 2 144 ? 25.814 27.998 17.945 1.00 26.75 ? 144 LEU B CB 1 ATOM 1427 C CG . LEU B 2 144 ? 26.552 28.597 16.747 1.00 26.79 ? 144 LEU B CG 1 ATOM 1428 C CD1 . LEU B 2 144 ? 25.595 29.427 15.900 1.00 25.61 ? 144 LEU B CD1 1 ATOM 1429 C CD2 . LEU B 2 144 ? 27.724 29.448 17.218 1.00 26.20 ? 144 LEU B CD2 1 ATOM 1430 N N . LYS B 2 145 ? 24.901 25.658 20.237 1.00 30.38 ? 145 LYS B N 1 ATOM 1431 C CA . LYS B 2 145 ? 24.018 25.359 21.367 1.00 32.63 ? 145 LYS B CA 1 ATOM 1432 C C . LYS B 2 145 ? 24.048 23.855 21.526 1.00 33.47 ? 145 LYS B C 1 ATOM 1433 O O . LYS B 2 145 ? 24.371 23.132 20.579 1.00 35.38 ? 145 LYS B O 1 ATOM 1434 C CB . LYS B 2 145 ? 22.570 25.795 21.088 1.00 35.16 ? 145 LYS B CB 1 ATOM 1435 C CG . LYS B 2 145 ? 22.274 27.273 21.302 1.00 39.93 ? 145 LYS B CG 1 ATOM 1436 C CD . LYS B 2 145 ? 20.900 27.674 20.756 1.00 44.95 ? 145 LYS B CD 1 ATOM 1437 C CE . LYS B 2 145 ? 20.618 29.159 20.994 0.50 44.42 ? 145 LYS B CE 1 ATOM 1438 N NZ . LYS B 2 145 ? 19.475 29.704 20.202 0.50 42.36 ? 145 LYS B NZ 1 ATOM 1439 N N . GLU B 2 146 ? 23.710 23.367 22.711 1.00 35.32 ? 146 GLU B N 1 ATOM 1440 C CA . GLU B 2 146 ? 23.590 21.929 22.899 1.00 37.20 ? 146 GLU B CA 1 ATOM 1441 C C . GLU B 2 146 ? 22.462 21.369 22.034 1.00 37.77 ? 146 GLU B C 1 ATOM 1442 O O . GLU B 2 146 ? 22.597 20.323 21.394 1.00 36.91 ? 146 GLU B O 1 ATOM 1443 C CB . GLU B 2 146 ? 23.326 21.593 24.359 1.00 37.96 ? 146 GLU B CB 1 ATOM 1444 C CG . GLU B 2 146 ? 23.564 20.124 24.639 1.00 40.20 ? 146 GLU B CG 1 ATOM 1445 C CD . GLU B 2 146 ? 23.255 19.731 26.056 1.00 40.60 ? 146 GLU B CD 1 ATOM 1446 O OE1 . GLU B 2 146 ? 23.449 20.541 26.987 1.00 39.31 ? 146 GLU B OE1 1 ATOM 1447 O OE2 . GLU B 2 146 ? 22.829 18.578 26.216 1.00 45.68 ? 146 GLU B OE2 1 ATOM 1448 N N . THR B 2 147 ? 21.354 22.098 22.018 1.00 37.15 ? 147 THR B N 1 ATOM 1449 C CA . THR B 2 147 ? 20.171 21.667 21.330 1.00 36.66 ? 147 THR B CA 1 ATOM 1450 C C . THR B 2 147 ? 19.473 22.892 20.737 1.00 36.55 ? 147 THR B C 1 ATOM 1451 O O . THR B 2 147 ? 19.607 24.009 21.254 1.00 37.19 ? 147 THR B O 1 ATOM 1452 C CB . THR B 2 147 ? 19.274 20.840 22.290 1.00 38.65 ? 147 THR B CB 1 ATOM 1453 O OG1 . THR B 2 147 ? 18.478 19.937 21.531 1.00 44.49 ? 147 THR B OG1 1 ATOM 1454 C CG2 . THR B 2 147 ? 18.372 21.713 23.168 1.00 38.62 ? 147 THR B CG2 1 ATOM 1455 N N . TRP B 2 148 ? 18.763 22.693 19.631 1.00 35.35 ? 148 TRP B N 1 ATOM 1456 C CA . TRP B 2 148 ? 17.998 23.772 19.011 1.00 35.05 ? 148 TRP B CA 1 ATOM 1457 C C . TRP B 2 148 ? 16.804 23.185 18.250 1.00 34.09 ? 148 TRP B C 1 ATOM 1458 O O . TRP B 2 148 ? 16.757 21.977 17.998 1.00 34.05 ? 148 TRP B O 1 ATOM 1459 C CB . TRP B 2 148 ? 18.901 24.641 18.099 1.00 36.56 ? 148 TRP B CB 1 ATOM 1460 C CG . TRP B 2 148 ? 19.454 23.891 16.907 1.00 37.39 ? 148 TRP B CG 1 ATOM 1461 C CD1 . TRP B 2 148 ? 18.888 23.801 15.650 1.00 36.87 ? 148 TRP B CD1 1 ATOM 1462 C CD2 . TRP B 2 148 ? 20.657 23.105 16.863 1.00 35.55 ? 148 TRP B CD2 1 ATOM 1463 N NE1 . TRP B 2 148 ? 19.670 23.007 14.837 1.00 36.32 ? 148 TRP B NE1 1 ATOM 1464 C CE2 . TRP B 2 148 ? 20.759 22.568 15.549 1.00 36.06 ? 148 TRP B CE2 1 ATOM 1465 C CE3 . TRP B 2 148 ? 21.659 22.811 17.796 1.00 34.05 ? 148 TRP B CE3 1 ATOM 1466 C CZ2 . TRP B 2 148 ? 21.827 21.752 15.150 1.00 35.25 ? 148 TRP B CZ2 1 ATOM 1467 C CZ3 . TRP B 2 148 ? 22.716 21.994 17.407 1.00 35.66 ? 148 TRP B CZ3 1 ATOM 1468 C CH2 . TRP B 2 148 ? 22.794 21.475 16.088 1.00 36.79 ? 148 TRP B CH2 1 ATOM 1469 N N . THR B 2 149 ? 15.844 24.038 17.897 1.00 33.12 ? 149 THR B N 1 ATOM 1470 C CA . THR B 2 149 ? 14.640 23.618 17.160 1.00 32.45 ? 149 THR B CA 1 ATOM 1471 C C . THR B 2 149 ? 14.988 23.309 15.695 1.00 31.73 ? 149 THR B C 1 ATOM 1472 O O . THR B 2 149 ? 15.548 24.158 14.993 1.00 30.48 ? 149 THR B O 1 ATOM 1473 C CB . THR B 2 149 ? 13.548 24.717 17.226 1.00 32.23 ? 149 THR B CB 1 ATOM 1474 O OG1 . THR B 2 149 ? 13.222 24.973 18.592 1.00 32.70 ? 149 THR B OG1 1 ATOM 1475 C CG2 . THR B 2 149 ? 12.281 24.301 16.483 1.00 32.43 ? 149 THR B CG2 1 ATOM 1476 N N . ALA B 2 150 ? 14.645 22.106 15.239 1.00 30.58 ? 150 ALA B N 1 ATOM 1477 C CA . ALA B 2 150 ? 15.038 21.657 13.896 1.00 30.62 ? 150 ALA B CA 1 ATOM 1478 C C . ALA B 2 150 ? 14.528 22.590 12.788 1.00 31.40 ? 150 ALA B C 1 ATOM 1479 O O . ALA B 2 150 ? 13.380 23.048 12.832 1.00 31.16 ? 150 ALA B O 1 ATOM 1480 C CB . ALA B 2 150 ? 14.591 20.220 13.655 1.00 28.87 ? 150 ALA B CB 1 ATOM 1481 N N . ASN B 2 151 ? 15.404 22.886 11.821 1.00 31.70 ? 151 ASN B N 1 ATOM 1482 C CA . ASN B 2 151 ? 15.068 23.699 10.645 1.00 32.11 ? 151 ASN B CA 1 ATOM 1483 C C . ASN B 2 151 ? 14.632 25.124 10.928 1.00 34.78 ? 151 ASN B C 1 ATOM 1484 O O . ASN B 2 151 ? 14.046 25.760 10.070 1.00 38.28 ? 151 ASN B O 1 ATOM 1485 C CB . ASN B 2 151 ? 14.017 22.987 9.789 1.00 31.57 ? 151 ASN B CB 1 ATOM 1486 C CG . ASN B 2 151 ? 14.428 21.572 9.453 1.00 31.91 ? 151 ASN B CG 1 ATOM 1487 O OD1 . ASN B 2 151 ? 15.553 21.342 9.041 1.00 33.16 ? 151 ASN B OD1 1 ATOM 1488 N ND2 . ASN B 2 151 ? 13.531 20.615 9.651 1.00 32.07 ? 151 ASN B ND2 1 ATOM 1489 N N . VAL B 2 152 ? 14.906 25.619 12.129 1.00 38.76 ? 152 VAL B N 1 ATOM 1490 C CA . VAL B 2 152 ? 14.550 26.984 12.521 1.00 45.53 ? 152 VAL B CA 1 ATOM 1491 C C . VAL B 2 152 ? 15.778 27.614 13.178 1.00 51.75 ? 152 VAL B C 1 ATOM 1492 O O . VAL B 2 152 ? 16.408 28.498 12.591 1.00 53.63 ? 152 VAL B O 1 ATOM 1493 C CB . VAL B 2 152 ? 13.353 27.008 13.509 1.00 47.48 ? 152 VAL B CB 1 ATOM 1494 C CG1 . VAL B 2 152 ? 13.091 28.417 14.039 1.00 47.85 ? 152 VAL B CG1 1 ATOM 1495 C CG2 . VAL B 2 152 ? 12.104 26.435 12.865 1.00 47.39 ? 152 VAL B CG2 1 ATOM 1496 N N . GLY B 2 153 ? 16.120 27.127 14.380 1.00 54.68 ? 153 GLY B N 1 ATOM 1497 C CA . GLY B 2 153 ? 17.276 27.584 15.150 1.00 60.21 ? 153 GLY B CA 1 ATOM 1498 C C . GLY B 2 153 ? 18.601 27.581 14.394 1.00 67.31 ? 153 GLY B C 1 ATOM 1499 O O . GLY B 2 153 ? 18.687 27.074 13.257 1.00 64.73 ? 153 GLY B O 1 ATOM 1500 N N . LYS B 2 154 ? 19.630 28.145 15.042 1.00 69.48 ? 154 LYS B N 1 ATOM 1501 C CA . LYS B 2 154 ? 20.958 28.378 14.443 1.00 68.88 ? 154 LYS B CA 1 ATOM 1502 C C . LYS B 2 154 ? 21.771 27.103 14.096 1.00 65.80 ? 154 LYS B C 1 ATOM 1503 O O . LYS B 2 154 ? 21.965 26.775 12.903 1.00 58.87 ? 154 LYS B O 1 ATOM 1504 C CB . LYS B 2 154 ? 21.784 29.335 15.318 1.00 74.85 ? 154 LYS B CB 1 ATOM 1505 C CG . LYS B 2 154 ? 21.602 29.175 16.827 1.00 76.04 ? 154 LYS B CG 1 ATOM 1506 C CD . LYS B 2 154 ? 20.887 30.382 17.433 1.00 81.65 ? 154 LYS B CD 1 ATOM 1507 C CE . LYS B 2 154 ? 21.855 31.492 17.828 1.00 78.22 ? 154 LYS B CE 1 ATOM 1508 N NZ . LYS B 2 154 ? 21.143 32.653 18.436 1.00 78.10 ? 154 LYS B NZ 1 ATOM 1509 N N . GLY B 2 155 ? 22.238 26.395 15.130 1.00 56.68 ? 155 GLY B N 1 ATOM 1510 C CA . GLY B 2 155 ? 23.008 25.160 14.941 1.00 48.86 ? 155 GLY B CA 1 ATOM 1511 C C . GLY B 2 155 ? 24.500 25.370 14.731 1.00 44.06 ? 155 GLY B C 1 ATOM 1512 O O . GLY B 2 155 ? 25.266 25.386 15.686 1.00 42.69 ? 155 GLY B O 1 ATOM 1513 N N . GLN B 2 156 ? 24.899 25.526 13.472 1.00 40.37 ? 156 GLN B N 1 ATOM 1514 C CA . GLN B 2 156 ? 26.288 25.690 13.101 1.00 39.12 ? 156 GLN B CA 1 ATOM 1515 C C . GLN B 2 156 ? 26.611 27.109 12.688 1.00 36.13 ? 156 GLN B C 1 ATOM 1516 O O . GLN B 2 156 ? 25.806 27.756 12.023 1.00 33.72 ? 156 GLN B O 1 ATOM 1517 C CB . GLN B 2 156 ? 26.654 24.773 11.946 1.00 43.74 ? 156 GLN B CB 1 ATOM 1518 C CG . GLN B 2 156 ? 26.647 23.295 12.288 1.00 48.97 ? 156 GLN B CG 1 ATOM 1519 C CD . GLN B 2 156 ? 25.334 22.654 11.955 1.00 47.60 ? 156 GLN B CD 1 ATOM 1520 O OE1 . GLN B 2 156 ? 24.629 22.180 12.835 1.00 51.55 ? 156 GLN B OE1 1 ATOM 1521 N NE2 . GLN B 2 156 ? 24.982 22.659 10.677 1.00 48.75 ? 156 GLN B NE2 1 ATOM 1522 N N . PRO B 2 157 ? 27.820 27.582 13.056 1.00 33.43 ? 157 PRO B N 1 ATOM 1523 C CA . PRO B 2 157 ? 28.288 28.913 12.675 1.00 29.61 ? 157 PRO B CA 1 ATOM 1524 C C . PRO B 2 157 ? 28.650 28.935 11.199 1.00 27.34 ? 157 PRO B C 1 ATOM 1525 O O . PRO B 2 157 ? 28.896 27.887 10.586 1.00 27.04 ? 157 PRO B O 1 ATOM 1526 C CB . PRO B 2 157 ? 29.566 29.062 13.491 1.00 29.92 ? 157 PRO B CB 1 ATOM 1527 C CG . PRO B 2 157 ? 30.098 27.652 13.581 1.00 30.78 ? 157 PRO B CG 1 ATOM 1528 C CD . PRO B 2 157 ? 28.884 26.780 13.705 1.00 30.62 ? 157 PRO B CD 1 ATOM 1529 N N . SER B 2 158 ? 28.711 30.107 10.611 1.00 25.72 ? 158 SER B N 1 ATOM 1530 C CA . SER B 2 158 ? 29.186 30.130 9.243 1.00 26.97 ? 158 SER B CA 1 ATOM 1531 C C . SER B 2 158 ? 30.692 30.420 9.162 1.00 26.58 ? 158 SER B C 1 ATOM 1532 O O . SER B 2 158 ? 31.331 30.089 8.161 1.00 28.37 ? 158 SER B O 1 ATOM 1533 C CB . SER B 2 158 ? 28.366 31.090 8.394 1.00 25.85 ? 158 SER B CB 1 ATOM 1534 O OG . SER B 2 158 ? 28.628 32.392 8.809 1.00 26.75 ? 158 SER B OG 1 ATOM 1535 N N . VAL B 2 159 ? 31.239 31.050 10.204 1.00 24.28 ? 159 VAL B N 1 ATOM 1536 C CA . VAL B 2 159 ? 32.686 31.252 10.332 1.00 23.14 ? 159 VAL B CA 1 ATOM 1537 C C . VAL B 2 159 ? 33.206 30.709 11.672 1.00 22.21 ? 159 VAL B C 1 ATOM 1538 O O . VAL B 2 159 ? 32.425 30.518 12.609 1.00 22.28 ? 159 VAL B O 1 ATOM 1539 C CB . VAL B 2 159 ? 33.113 32.740 10.109 1.00 23.18 ? 159 VAL B CB 1 ATOM 1540 C CG1 . VAL B 2 159 ? 32.606 33.260 8.765 1.00 20.09 ? 159 VAL B CG1 1 ATOM 1541 C CG2 . VAL B 2 159 ? 32.667 33.641 11.262 1.00 22.04 ? 159 VAL B CG2 1 ATOM 1542 N N . LEU B 2 160 ? 34.514 30.440 11.732 1.00 21.36 ? 160 LEU B N 1 ATOM 1543 C CA . LEU B 2 160 ? 35.227 30.032 12.949 1.00 20.63 ? 160 LEU B CA 1 ATOM 1544 C C . LEU B 2 160 ? 34.831 30.841 14.180 1.00 21.38 ? 160 LEU B C 1 ATOM 1545 O O . LEU B 2 160 ? 34.743 32.083 14.126 1.00 21.28 ? 160 LEU B O 1 ATOM 1546 C CB . LEU B 2 160 ? 36.741 30.175 12.750 1.00 20.10 ? 160 LEU B CB 1 ATOM 1547 C CG . LEU B 2 160 ? 37.681 29.601 13.838 1.00 19.43 ? 160 LEU B CG 1 ATOM 1548 C CD1 . LEU B 2 160 ? 37.581 28.076 13.911 1.00 18.82 ? 160 LEU B CD1 1 ATOM 1549 C CD2 . LEU B 2 160 ? 39.123 30.046 13.624 1.00 18.20 ? 160 LEU B CD2 1 ATOM 1550 N N . GLN B 2 161 ? 34.603 30.130 15.287 1.00 21.22 ? 161 GLN B N 1 ATOM 1551 C CA . GLN B 2 161 ? 34.206 30.748 16.547 1.00 21.36 ? 161 GLN B CA 1 ATOM 1552 C C . GLN B 2 161 ? 35.333 30.698 17.582 1.00 23.45 ? 161 GLN B C 1 ATOM 1553 O O . GLN B 2 161 ? 36.214 29.818 17.523 1.00 23.70 ? 161 GLN B O 1 ATOM 1554 C CB . GLN B 2 161 ? 32.971 30.052 17.087 1.00 20.93 ? 161 GLN B CB 1 ATOM 1555 C CG . GLN B 2 161 ? 31.761 30.143 16.169 1.00 20.67 ? 161 GLN B CG 1 ATOM 1556 C CD . GLN B 2 161 ? 31.220 31.557 16.059 1.00 20.65 ? 161 GLN B CD 1 ATOM 1557 O OE1 . GLN B 2 161 ? 31.361 32.214 15.005 1.00 20.38 ? 161 GLN B OE1 1 ATOM 1558 N NE2 . GLN B 2 161 ? 30.624 32.053 17.153 1.00 19.11 ? 161 GLN B NE2 1 ATOM 1559 N N . VAL B 2 162 ? 35.293 31.634 18.533 1.00 24.18 ? 162 VAL B N 1 ATOM 1560 C CA . VAL B 2 162 ? 36.334 31.767 19.562 1.00 24.92 ? 162 VAL B CA 1 ATOM 1561 C C . VAL B 2 162 ? 35.706 32.060 20.925 1.00 24.99 ? 162 VAL B C 1 ATOM 1562 O O . VAL B 2 162 ? 34.724 32.786 21.020 1.00 25.51 ? 162 VAL B O 1 ATOM 1563 C CB . VAL B 2 162 ? 37.380 32.856 19.178 1.00 25.91 ? 162 VAL B CB 1 ATOM 1564 C CG1 . VAL B 2 162 ? 36.720 34.192 18.921 1.00 27.25 ? 162 VAL B CG1 1 ATOM 1565 C CG2 . VAL B 2 162 ? 38.426 33.046 20.257 1.00 26.48 ? 162 VAL B CG2 1 ATOM 1566 N N . VAL B 2 163 ? 36.260 31.467 21.976 1.00 25.01 ? 163 VAL B N 1 ATOM 1567 C CA . VAL B 2 163 ? 35.829 31.756 23.335 1.00 24.28 ? 163 VAL B CA 1 ATOM 1568 C C . VAL B 2 163 ? 37.008 31.629 24.314 1.00 25.77 ? 163 VAL B C 1 ATOM 1569 O O . VAL B 2 163 ? 37.862 30.734 24.163 1.00 26.66 ? 163 VAL B O 1 ATOM 1570 C CB . VAL B 2 163 ? 34.628 30.869 23.750 1.00 23.71 ? 163 VAL B CB 1 ATOM 1571 C CG1 . VAL B 2 163 ? 35.048 29.433 24.065 1.00 21.70 ? 163 VAL B CG1 1 ATOM 1572 C CG2 . VAL B 2 163 ? 33.882 31.493 24.925 1.00 23.93 ? 163 VAL B CG2 1 ATOM 1573 N N . ASN B 2 164 ? 37.049 32.527 25.305 1.00 26.09 ? 164 ASN B N 1 ATOM 1574 C CA . ASN B 2 164 ? 38.085 32.524 26.339 1.00 25.62 ? 164 ASN B CA 1 ATOM 1575 C C . ASN B 2 164 ? 37.555 31.965 27.663 1.00 27.14 ? 164 ASN B C 1 ATOM 1576 O O . ASN B 2 164 ? 36.557 32.454 28.198 1.00 29.37 ? 164 ASN B O 1 ATOM 1577 C CB . ASN B 2 164 ? 38.651 33.927 26.515 1.00 25.97 ? 164 ASN B CB 1 ATOM 1578 C CG . ASN B 2 164 ? 39.271 34.485 25.231 1.00 29.06 ? 164 ASN B CG 1 ATOM 1579 O OD1 . ASN B 2 164 ? 39.814 33.746 24.396 1.00 30.33 ? 164 ASN B OD1 1 ATOM 1580 N ND2 . ASN B 2 164 ? 39.218 35.804 25.080 1.00 30.49 ? 164 ASN B ND2 1 ATOM 1581 N N . LEU B 2 165 ? 38.208 30.929 28.184 1.00 27.45 ? 165 LEU B N 1 ATOM 1582 C CA . LEU B 2 165 ? 37.723 30.227 29.369 1.00 28.26 ? 165 LEU B CA 1 ATOM 1583 C C . LEU B 2 165 ? 38.815 30.085 30.436 1.00 30.89 ? 165 LEU B C 1 ATOM 1584 O O . LEU B 2 165 ? 39.966 29.828 30.106 1.00 31.68 ? 165 LEU B O 1 ATOM 1585 C CB . LEU B 2 165 ? 37.209 28.833 28.998 1.00 27.02 ? 165 LEU B CB 1 ATOM 1586 C CG . LEU B 2 165 ? 36.080 28.740 27.967 1.00 27.43 ? 165 LEU B CG 1 ATOM 1587 C CD1 . LEU B 2 165 ? 35.864 27.295 27.527 1.00 26.35 ? 165 LEU B CD1 1 ATOM 1588 C CD2 . LEU B 2 165 ? 34.789 29.381 28.484 1.00 27.84 ? 165 LEU B CD2 1 ATOM 1589 N N . PRO B 2 166 ? 38.451 30.242 31.724 1.00 32.16 ? 166 PRO B N 1 ATOM 1590 C CA . PRO B 2 166 ? 39.425 30.050 32.788 1.00 30.96 ? 166 PRO B CA 1 ATOM 1591 C C . PRO B 2 166 ? 39.606 28.588 33.159 1.00 29.35 ? 166 PRO B C 1 ATOM 1592 O O . PRO B 2 166 ? 38.634 27.830 33.172 1.00 28.31 ? 166 PRO B O 1 ATOM 1593 C CB . PRO B 2 166 ? 38.814 30.814 33.964 1.00 31.49 ? 166 PRO B CB 1 ATOM 1594 C CG . PRO B 2 166 ? 37.348 30.737 33.724 1.00 32.71 ? 166 PRO B CG 1 ATOM 1595 C CD . PRO B 2 166 ? 37.183 30.808 32.233 1.00 33.24 ? 166 PRO B CD 1 ATOM 1596 N N . ILE B 2 167 ? 40.859 28.222 33.440 1.00 28.40 ? 167 ILE B N 1 ATOM 1597 C CA . ILE B 2 167 ? 41.229 26.946 34.030 1.00 29.13 ? 167 ILE B CA 1 ATOM 1598 C C . ILE B 2 167 ? 40.656 26.880 35.451 1.00 31.26 ? 167 ILE B C 1 ATOM 1599 O O . ILE B 2 167 ? 40.660 27.868 36.200 1.00 31.27 ? 167 ILE B O 1 ATOM 1600 C CB . ILE B 2 167 ? 42.769 26.780 34.037 1.00 29.39 ? 167 ILE B CB 1 ATOM 1601 C CG1 . ILE B 2 167 ? 43.294 26.628 32.610 1.00 29.29 ? 167 ILE B CG1 1 ATOM 1602 C CG2 . ILE B 2 167 ? 43.209 25.579 34.863 1.00 28.56 ? 167 ILE B CG2 1 ATOM 1603 C CD1 . ILE B 2 167 ? 44.614 27.322 32.367 1.00 30.25 ? 167 ILE B CD1 1 ATOM 1604 N N . VAL B 2 168 ? 40.150 25.711 35.808 1.00 32.85 ? 168 VAL B N 1 ATOM 1605 C CA . VAL B 2 168 ? 39.392 25.531 37.029 1.00 34.59 ? 168 VAL B CA 1 ATOM 1606 C C . VAL B 2 168 ? 40.198 24.626 37.960 1.00 36.42 ? 168 VAL B C 1 ATOM 1607 O O . VAL B 2 168 ? 40.858 23.702 37.487 1.00 37.17 ? 168 VAL B O 1 ATOM 1608 C CB . VAL B 2 168 ? 38.004 24.926 36.673 1.00 33.85 ? 168 VAL B CB 1 ATOM 1609 C CG1 . VAL B 2 168 ? 37.272 24.398 37.899 1.00 33.32 ? 168 VAL B CG1 1 ATOM 1610 C CG2 . VAL B 2 168 ? 37.151 25.962 35.961 1.00 31.59 ? 168 VAL B CG2 1 ATOM 1611 N N . GLU B 2 169 ? 40.141 24.888 39.271 1.00 40.44 ? 169 GLU B N 1 ATOM 1612 C CA . GLU B 2 169 ? 40.826 24.057 40.294 1.00 40.58 ? 169 GLU B CA 1 ATOM 1613 C C . GLU B 2 169 ? 40.465 22.585 40.201 1.00 40.14 ? 169 GLU B C 1 ATOM 1614 O O . GLU B 2 169 ? 39.292 22.226 40.101 1.00 41.85 ? 169 GLU B O 1 ATOM 1615 C CB . GLU B 2 169 ? 40.503 24.531 41.708 1.00 42.05 ? 169 GLU B CB 1 ATOM 1616 C CG . GLU B 2 169 ? 40.869 25.971 42.001 1.00 49.00 ? 169 GLU B CG 1 ATOM 1617 C CD . GLU B 2 169 ? 39.756 26.944 41.662 1.00 55.16 ? 169 GLU B CD 1 ATOM 1618 O OE1 . GLU B 2 169 ? 38.717 26.517 41.114 1.00 57.75 ? 169 GLU B OE1 1 ATOM 1619 O OE2 . GLU B 2 169 ? 39.924 28.148 41.951 1.00 62.55 ? 169 GLU B OE2 1 ATOM 1620 N N . ARG B 2 170 ? 41.485 21.742 40.265 1.00 40.87 ? 170 ARG B N 1 ATOM 1621 C CA . ARG B 2 170 ? 41.330 20.294 40.199 1.00 43.11 ? 170 ARG B CA 1 ATOM 1622 C C . ARG B 2 170 ? 40.220 19.710 41.112 1.00 45.70 ? 170 ARG B C 1 ATOM 1623 O O . ARG B 2 170 ? 39.494 18.816 40.674 1.00 46.21 ? 170 ARG B O 1 ATOM 1624 C CB . ARG B 2 170 ? 42.686 19.602 40.410 1.00 42.85 ? 170 ARG B CB 1 ATOM 1625 C CG . ARG B 2 170 ? 42.645 18.088 40.275 1.00 49.75 ? 170 ARG B CG 1 ATOM 1626 C CD . ARG B 2 170 ? 43.999 17.507 39.893 1.00 55.75 ? 170 ARG B CD 1 ATOM 1627 N NE . ARG B 2 170 ? 44.503 18.140 38.674 1.00 64.23 ? 170 ARG B NE 1 ATOM 1628 C CZ . ARG B 2 170 ? 44.254 17.721 37.429 1.00 66.06 ? 170 ARG B CZ 1 ATOM 1629 N NH1 . ARG B 2 170 ? 43.506 16.637 37.203 1.00 63.37 ? 170 ARG B NH1 1 ATOM 1630 N NH2 . ARG B 2 170 ? 44.765 18.395 36.402 1.00 61.96 ? 170 ARG B NH2 1 ATOM 1631 N N . PRO B 2 171 ? 40.078 20.204 42.374 1.00 49.10 ? 171 PRO B N 1 ATOM 1632 C CA . PRO B 2 171 ? 38.983 19.656 43.213 1.00 47.39 ? 171 PRO B CA 1 ATOM 1633 C C . PRO B 2 171 ? 37.566 19.983 42.698 1.00 46.31 ? 171 PRO B C 1 ATOM 1634 O O . PRO B 2 171 ? 36.671 19.128 42.764 1.00 45.09 ? 171 PRO B O 1 ATOM 1635 C CB . PRO B 2 171 ? 39.228 20.304 44.588 1.00 47.10 ? 171 PRO B CB 1 ATOM 1636 C CG . PRO B 2 171 ? 40.678 20.663 44.585 1.00 47.29 ? 171 PRO B CG 1 ATOM 1637 C CD . PRO B 2 171 ? 40.980 21.067 43.170 1.00 46.87 ? 171 PRO B CD 1 ATOM 1638 N N . VAL B 2 172 ? 37.364 21.197 42.184 1.00 42.70 ? 172 VAL B N 1 ATOM 1639 C CA . VAL B 2 172 ? 36.085 21.539 41.553 1.00 40.13 ? 172 VAL B CA 1 ATOM 1640 C C . VAL B 2 172 ? 35.816 20.687 40.301 1.00 42.32 ? 172 VAL B C 1 ATOM 1641 O O . VAL B 2 172 ? 34.670 20.281 40.074 1.00 46.44 ? 172 VAL B O 1 ATOM 1642 C CB . VAL B 2 172 ? 35.983 23.035 41.216 1.00 38.02 ? 172 VAL B CB 1 ATOM 1643 C CG1 . VAL B 2 172 ? 34.606 23.380 40.667 1.00 36.27 ? 172 VAL B CG1 1 ATOM 1644 C CG2 . VAL B 2 172 ? 36.307 23.876 42.440 1.00 37.71 ? 172 VAL B CG2 1 ATOM 1645 N N . CYS B 2 173 ? 36.857 20.402 39.507 1.00 40.57 ? 173 CYS B N 1 ATOM 1646 C CA . CYS B 2 173 ? 36.718 19.490 38.363 1.00 41.42 ? 173 CYS B CA 1 ATOM 1647 C C . CYS B 2 173 ? 36.196 18.124 38.811 1.00 44.47 ? 173 CYS B C 1 ATOM 1648 O O . CYS B 2 173 ? 35.213 17.617 38.256 1.00 43.89 ? 173 CYS B O 1 ATOM 1649 C CB . CYS B 2 173 ? 38.035 19.312 37.580 1.00 39.13 ? 173 CYS B CB 1 ATOM 1650 S SG . CYS B 2 173 ? 38.755 20.798 36.839 1.00 38.08 ? 173 CYS B SG 1 ATOM 1651 N N . LYS B 2 174 ? 36.865 17.542 39.810 1.00 49.48 ? 174 LYS B N 1 ATOM 1652 C CA . LYS B 2 174 ? 36.509 16.236 40.368 1.00 52.56 ? 174 LYS B CA 1 ATOM 1653 C C . LYS B 2 174 ? 35.061 16.143 40.862 1.00 50.78 ? 174 LYS B C 1 ATOM 1654 O O . LYS B 2 174 ? 34.369 15.175 40.547 1.00 46.68 ? 174 LYS B O 1 ATOM 1655 C CB . LYS B 2 174 ? 37.485 15.840 41.478 1.00 56.90 ? 174 LYS B CB 1 ATOM 1656 C CG . LYS B 2 174 ? 38.404 14.696 41.093 1.00 65.62 ? 174 LYS B CG 1 ATOM 1657 C CD . LYS B 2 174 ? 39.821 14.904 41.612 1.00 76.01 ? 174 LYS B CD 1 ATOM 1658 C CE . LYS B 2 174 ? 40.780 13.823 41.117 1.00 78.96 ? 174 LYS B CE 1 ATOM 1659 N NZ . LYS B 2 174 ? 42.201 14.177 41.395 1.00 76.32 ? 174 LYS B NZ 1 ATOM 1660 N N . ASP B 2 175 ? 34.605 17.157 41.597 1.00 50.56 ? 175 ASP B N 1 ATOM 1661 C CA . ASP B 2 175 ? 33.260 17.151 42.190 1.00 55.41 ? 175 ASP B CA 1 ATOM 1662 C C . ASP B 2 175 ? 32.131 17.221 41.181 1.00 56.03 ? 175 ASP B C 1 ATOM 1663 O O . ASP B 2 175 ? 31.013 16.820 41.486 1.00 60.49 ? 175 ASP B O 1 ATOM 1664 C CB . ASP B 2 175 ? 33.083 18.308 43.178 1.00 60.51 ? 175 ASP B CB 1 ATOM 1665 C CG . ASP B 2 175 ? 33.754 18.050 44.515 1.00 65.87 ? 175 ASP B CG 1 ATOM 1666 O OD1 . ASP B 2 175 ? 34.188 16.903 44.780 1.00 65.92 ? 175 ASP B OD1 1 ATOM 1667 O OD2 . ASP B 2 175 ? 33.848 19.010 45.307 1.00 70.44 ? 175 ASP B OD2 1 ATOM 1668 N N . SER B 2 176 ? 32.426 17.729 39.987 1.00 55.82 ? 176 SER B N 1 ATOM 1669 C CA . SER B 2 176 ? 31.400 18.055 38.989 1.00 50.83 ? 176 SER B CA 1 ATOM 1670 C C . SER B 2 176 ? 30.960 16.876 38.095 1.00 47.73 ? 176 SER B C 1 ATOM 1671 O O . SER B 2 176 ? 30.005 17.007 37.329 1.00 48.19 ? 176 SER B O 1 ATOM 1672 C CB . SER B 2 176 ? 31.888 19.220 38.123 1.00 49.18 ? 176 SER B CB 1 ATOM 1673 O OG . SER B 2 176 ? 32.935 18.790 37.266 1.00 48.58 ? 176 SER B OG 1 ATOM 1674 N N . THR B 2 177 ? 31.645 15.740 38.190 1.00 43.59 ? 177 THR B N 1 ATOM 1675 C CA . THR B 2 177 ? 31.377 14.609 37.297 1.00 45.40 ? 177 THR B CA 1 ATOM 1676 C C . THR B 2 177 ? 31.607 13.292 38.018 1.00 47.73 ? 177 THR B C 1 ATOM 1677 O O . THR B 2 177 ? 32.436 13.207 38.917 1.00 50.40 ? 177 THR B O 1 ATOM 1678 C CB . THR B 2 177 ? 32.244 14.649 35.999 1.00 45.28 ? 177 THR B CB 1 ATOM 1679 O OG1 . THR B 2 177 ? 32.068 13.439 35.251 1.00 46.37 ? 177 THR B OG1 1 ATOM 1680 C CG2 . THR B 2 177 ? 33.743 14.806 36.310 1.00 42.87 ? 177 THR B CG2 1 ATOM 1681 N N . ARG B 2 178 ? 30.878 12.265 37.612 1.00 51.98 ? 178 ARG B N 1 ATOM 1682 C CA . ARG B 2 178 ? 31.021 10.947 38.210 1.00 56.47 ? 178 ARG B CA 1 ATOM 1683 C C . ARG B 2 178 ? 32.139 10.172 37.530 1.00 55.84 ? 178 ARG B C 1 ATOM 1684 O O . ARG B 2 178 ? 32.509 9.093 37.977 1.00 57.97 ? 178 ARG B O 1 ATOM 1685 C CB . ARG B 2 178 ? 29.698 10.175 38.137 1.00 63.26 ? 178 ARG B CB 1 ATOM 1686 C CG . ARG B 2 178 ? 28.514 10.995 38.622 1.00 73.40 ? 178 ARG B CG 1 ATOM 1687 C CD . ARG B 2 178 ? 27.398 10.148 39.211 1.00 84.61 ? 178 ARG B CD 1 ATOM 1688 N NE . ARG B 2 178 ? 26.870 10.798 40.415 1.00 93.00 ? 178 ARG B NE 1 ATOM 1689 C CZ . ARG B 2 178 ? 25.604 10.748 40.827 1.00 93.64 ? 178 ARG B CZ 1 ATOM 1690 N NH1 . ARG B 2 178 ? 24.689 10.079 40.136 1.00 95.77 ? 178 ARG B NH1 1 ATOM 1691 N NH2 . ARG B 2 178 ? 25.250 11.386 41.935 1.00 90.63 ? 178 ARG B NH2 1 ATOM 1692 N N . ILE B 2 179 ? 32.675 10.726 36.446 1.00 54.98 ? 179 ILE B N 1 ATOM 1693 C CA . ILE B 2 179 ? 33.727 10.056 35.680 1.00 52.73 ? 179 ILE B CA 1 ATOM 1694 C C . ILE B 2 179 ? 35.044 10.196 36.432 1.00 51.55 ? 179 ILE B C 1 ATOM 1695 O O . ILE B 2 179 ? 35.267 11.206 37.113 1.00 49.40 ? 179 ILE B O 1 ATOM 1696 C CB . ILE B 2 179 ? 33.798 10.599 34.226 1.00 53.47 ? 179 ILE B CB 1 ATOM 1697 C CG1 . ILE B 2 179 ? 32.660 10.002 33.390 1.00 51.47 ? 179 ILE B CG1 1 ATOM 1698 C CG2 . ILE B 2 179 ? 35.121 10.263 33.552 1.00 48.59 ? 179 ILE B CG2 1 ATOM 1699 C CD1 . ILE B 2 179 ? 31.948 11.024 32.535 1.00 55.12 ? 179 ILE B CD1 1 ATOM 1700 N N . ARG B 2 180 ? 35.883 9.161 36.338 1.00 52.85 ? 180 ARG B N 1 ATOM 1701 C CA . ARG B 2 180 ? 37.183 9.132 37.008 1.00 52.95 ? 180 ARG B CA 1 ATOM 1702 C C . ARG B 2 180 ? 38.197 9.942 36.201 1.00 52.91 ? 180 ARG B C 1 ATOM 1703 O O . ARG B 2 180 ? 38.700 9.479 35.168 1.00 54.87 ? 180 ARG B O 1 ATOM 1704 C CB . ARG B 2 180 ? 37.673 7.690 37.166 1.00 55.79 ? 180 ARG B CB 1 ATOM 1705 C CG . ARG B 2 180 ? 38.593 7.479 38.362 1.00 62.09 ? 180 ARG B CG 1 ATOM 1706 C CD . ARG B 2 180 ? 39.329 6.143 38.318 1.00 65.54 ? 180 ARG B CD 1 ATOM 1707 N NE . ARG B 2 180 ? 40.663 6.263 37.718 1.00 71.56 ? 180 ARG B NE 1 ATOM 1708 C CZ . ARG B 2 180 ? 41.045 5.672 36.585 1.00 75.27 ? 180 ARG B CZ 1 ATOM 1709 N NH1 . ARG B 2 180 ? 40.203 4.895 35.910 1.00 76.08 ? 180 ARG B NH1 1 ATOM 1710 N NH2 . ARG B 2 180 ? 42.279 5.855 36.123 1.00 73.55 ? 180 ARG B NH2 1 ATOM 1711 N N . ILE B 2 181 ? 38.492 11.150 36.667 1.00 48.51 ? 181 ILE B N 1 ATOM 1712 C CA . ILE B 2 181 ? 39.429 12.030 35.968 1.00 49.71 ? 181 ILE B CA 1 ATOM 1713 C C . ILE B 2 181 ? 40.885 11.760 36.374 1.00 48.37 ? 181 ILE B C 1 ATOM 1714 O O . ILE B 2 181 ? 41.174 11.549 37.548 1.00 53.67 ? 181 ILE B O 1 ATOM 1715 C CB . ILE B 2 181 ? 39.078 13.520 36.171 1.00 50.36 ? 181 ILE B CB 1 ATOM 1716 C CG1 . ILE B 2 181 ? 39.480 13.978 37.566 1.00 49.47 ? 181 ILE B CG1 1 ATOM 1717 C CG2 . ILE B 2 181 ? 37.595 13.774 35.894 1.00 47.78 ? 181 ILE B CG2 1 ATOM 1718 C CD1 . ILE B 2 181 ? 39.678 15.470 37.676 1.00 58.88 ? 181 ILE B CD1 1 ATOM 1719 N N . THR B 2 182 ? 41.791 11.762 35.401 1.00 44.18 ? 182 THR B N 1 ATOM 1720 C CA . THR B 2 182 ? 43.211 11.505 35.653 1.00 39.81 ? 182 THR B CA 1 ATOM 1721 C C . THR B 2 182 ? 44.040 12.775 35.576 1.00 40.16 ? 182 THR B C 1 ATOM 1722 O O . THR B 2 182 ? 43.511 13.870 35.345 1.00 39.45 ? 182 THR B O 1 ATOM 1723 C CB . THR B 2 182 ? 43.810 10.549 34.624 1.00 37.41 ? 182 THR B CB 1 ATOM 1724 O OG1 . THR B 2 182 ? 44.004 11.269 33.404 1.00 37.37 ? 182 THR B OG1 1 ATOM 1725 C CG2 . THR B 2 182 ? 42.910 9.347 34.394 1.00 35.21 ? 182 THR B CG2 1 ATOM 1726 N N . ASP B 2 183 ? 45.348 12.615 35.767 1.00 41.33 ? 183 ASP B N 1 ATOM 1727 C CA . ASP B 2 183 ? 46.287 13.737 35.719 1.00 43.23 ? 183 ASP B CA 1 ATOM 1728 C C . ASP B 2 183 ? 46.660 14.100 34.278 1.00 41.40 ? 183 ASP B C 1 ATOM 1729 O O . ASP B 2 183 ? 47.448 15.022 34.034 1.00 43.56 ? 183 ASP B O 1 ATOM 1730 C CB . ASP B 2 183 ? 47.536 13.418 36.549 1.00 47.67 ? 183 ASP B CB 1 ATOM 1731 C CG . ASP B 2 183 ? 47.261 13.448 38.042 1.00 54.71 ? 183 ASP B CG 1 ATOM 1732 O OD1 . ASP B 2 183 ? 46.543 14.367 38.504 1.00 56.82 ? 183 ASP B OD1 1 ATOM 1733 O OD2 . ASP B 2 183 ? 47.753 12.547 38.757 1.00 58.67 ? 183 ASP B OD2 1 ATOM 1734 N N . ASN B 2 184 ? 46.088 13.367 33.328 1.00 37.50 ? 184 ASN B N 1 ATOM 1735 C CA . ASN B 2 184 ? 46.245 13.673 31.918 1.00 33.86 ? 184 ASN B CA 1 ATOM 1736 C C . ASN B 2 184 ? 45.119 14.552 31.363 1.00 32.48 ? 184 ASN B C 1 ATOM 1737 O O . ASN B 2 184 ? 44.982 14.680 30.151 1.00 33.57 ? 184 ASN B O 1 ATOM 1738 C CB . ASN B 2 184 ? 46.363 12.383 31.119 1.00 33.87 ? 184 ASN B CB 1 ATOM 1739 C CG . ASN B 2 184 ? 47.534 11.521 31.567 1.00 33.87 ? 184 ASN B CG 1 ATOM 1740 O OD1 . ASN B 2 184 ? 48.633 12.021 31.830 1.00 33.45 ? 184 ASN B OD1 1 ATOM 1741 N ND2 . ASN B 2 184 ? 47.307 10.217 31.638 1.00 31.16 ? 184 ASN B ND2 1 ATOM 1742 N N . MET B 2 185 ? 44.337 15.159 32.260 1.00 30.72 ? 185 MET B N 1 ATOM 1743 C CA . MET B 2 185 ? 43.218 16.035 31.912 1.00 31.03 ? 185 MET B CA 1 ATOM 1744 C C . MET B 2 185 ? 43.236 17.258 32.778 1.00 31.33 ? 185 MET B C 1 ATOM 1745 O O . MET B 2 185 ? 43.691 17.187 33.913 1.00 35.10 ? 185 MET B O 1 ATOM 1746 C CB . MET B 2 185 ? 41.885 15.370 32.216 1.00 30.86 ? 185 MET B CB 1 ATOM 1747 C CG . MET B 2 185 ? 41.708 14.011 31.598 1.00 33.60 ? 185 MET B CG 1 ATOM 1748 S SD . MET B 2 185 ? 40.283 13.212 32.336 1.00 34.47 ? 185 MET B SD 1 ATOM 1749 C CE . MET B 2 185 ? 40.434 11.636 31.489 1.00 33.26 ? 185 MET B CE 1 ATOM 1750 N N . PHE B 2 186 ? 42.705 18.361 32.261 1.00 28.70 ? 186 PHE B N 1 ATOM 1751 C CA . PHE B 2 186 ? 42.268 19.475 33.098 1.00 27.84 ? 186 PHE B CA 1 ATOM 1752 C C . PHE B 2 186 ? 40.884 19.963 32.630 1.00 28.47 ? 186 PHE B C 1 ATOM 1753 O O . PHE B 2 186 ? 40.402 19.572 31.556 1.00 27.00 ? 186 PHE B O 1 ATOM 1754 C CB . PHE B 2 186 ? 43.314 20.610 33.124 1.00 26.77 ? 186 PHE B CB 1 ATOM 1755 C CG . PHE B 2 186 ? 43.545 21.290 31.787 1.00 26.95 ? 186 PHE B CG 1 ATOM 1756 C CD1 . PHE B 2 186 ? 44.458 20.776 30.871 1.00 27.04 ? 186 PHE B CD1 1 ATOM 1757 C CD2 . PHE B 2 186 ? 42.874 22.464 31.456 1.00 27.26 ? 186 PHE B CD2 1 ATOM 1758 C CE1 . PHE B 2 186 ? 44.684 21.411 29.653 1.00 27.26 ? 186 PHE B CE1 1 ATOM 1759 C CE2 . PHE B 2 186 ? 43.099 23.105 30.238 1.00 27.86 ? 186 PHE B CE2 1 ATOM 1760 C CZ . PHE B 2 186 ? 44.010 22.580 29.338 1.00 27.18 ? 186 PHE B CZ 1 ATOM 1761 N N . CYS B 2 187 ? 40.247 20.820 33.418 1.00 27.68 ? 187 CYS B N 1 ATOM 1762 C CA . CYS B 2 187 ? 38.931 21.291 33.051 1.00 28.19 ? 187 CYS B CA 1 ATOM 1763 C C . CYS B 2 187 ? 38.918 22.812 33.052 1.00 28.12 ? 187 CYS B C 1 ATOM 1764 O O . CYS B 2 187 ? 39.696 23.445 33.774 1.00 28.50 ? 187 CYS B O 1 ATOM 1765 C CB . CYS B 2 187 ? 37.834 20.655 33.935 1.00 30.03 ? 187 CYS B CB 1 ATOM 1766 S SG . CYS B 2 187 ? 37.379 21.485 35.488 1.00 34.65 ? 187 CYS B SG 1 ATOM 1767 N N . ALA B 2 188 ? 38.064 23.394 32.213 1.00 26.98 ? 188 ALA B N 1 ATOM 1768 C CA . ALA B 2 188 ? 37.965 24.848 32.101 1.00 27.42 ? 188 ALA B CA 1 ATOM 1769 C C . ALA B 2 188 ? 36.510 25.233 31.934 1.00 28.43 ? 188 ALA B C 1 ATOM 1770 O O . ALA B 2 188 ? 35.699 24.426 31.471 1.00 29.88 ? 188 ALA B O 1 ATOM 1771 C CB . ALA B 2 188 ? 38.788 25.356 30.922 1.00 25.99 ? 188 ALA B CB 1 ATOM 1772 N N . GLY B 2 189 ? 36.182 26.466 32.303 1.00 29.04 ? 189 GLY B N 1 ATOM 1773 C CA . GLY B 2 189 ? 34.823 26.986 32.162 1.00 29.56 ? 189 GLY B CA 1 ATOM 1774 C C . GLY B 2 189 ? 34.526 27.924 33.314 1.00 32.08 ? 189 GLY B C 1 ATOM 1775 O O . GLY B 2 189 ? 35.230 27.911 34.334 1.00 33.13 ? 189 GLY B O 1 ATOM 1776 N N . TYR B 2 190 ? 33.502 28.754 33.167 1.00 32.73 ? 190 TYR B N 1 ATOM 1777 C CA . TYR B 2 190 ? 33.096 29.602 34.273 1.00 35.21 ? 190 TYR B CA 1 ATOM 1778 C C . TYR B 2 190 ? 32.243 28.846 35.306 1.00 37.98 ? 190 TYR B C 1 ATOM 1779 O O . TYR B 2 190 ? 31.537 27.891 34.971 1.00 37.95 ? 190 TYR B O 1 ATOM 1780 C CB . TYR B 2 190 ? 32.370 30.833 33.774 1.00 34.37 ? 190 TYR B CB 1 ATOM 1781 C CG . TYR B 2 190 ? 33.214 31.751 32.928 1.00 35.50 ? 190 TYR B CG 1 ATOM 1782 C CD1 . TYR B 2 190 ? 34.052 32.702 33.521 1.00 34.97 ? 190 TYR B CD1 1 ATOM 1783 C CD2 . TYR B 2 190 ? 33.160 31.691 31.531 1.00 36.00 ? 190 TYR B CD2 1 ATOM 1784 C CE1 . TYR B 2 190 ? 34.813 33.568 32.758 1.00 35.12 ? 190 TYR B CE1 1 ATOM 1785 C CE2 . TYR B 2 190 ? 33.926 32.553 30.755 1.00 37.17 ? 190 TYR B CE2 1 ATOM 1786 C CZ . TYR B 2 190 ? 34.754 33.490 31.384 1.00 37.73 ? 190 TYR B CZ 1 ATOM 1787 O OH . TYR B 2 190 ? 35.519 34.350 30.630 1.00 40.37 ? 190 TYR B OH 1 ATOM 1788 N N . LYS B 2 191 ? 32.346 29.265 36.567 1.00 42.29 ? 191 LYS B N 1 ATOM 1789 C CA . LYS B 2 191 ? 31.549 28.700 37.656 1.00 45.19 ? 191 LYS B CA 1 ATOM 1790 C C . LYS B 2 191 ? 30.179 29.367 37.644 1.00 45.58 ? 191 LYS B C 1 ATOM 1791 O O . LYS B 2 191 ? 30.066 30.523 37.198 1.00 43.95 ? 191 LYS B O 1 ATOM 1792 C CB . LYS B 2 191 ? 32.245 28.935 38.993 1.00 45.75 ? 191 LYS B CB 1 ATOM 1793 C CG . LYS B 2 191 ? 33.465 28.069 39.202 1.00 46.89 ? 191 LYS B CG 1 ATOM 1794 C CD . LYS B 2 191 ? 34.442 28.749 40.140 1.00 49.93 ? 191 LYS B CD 1 ATOM 1795 C CE . LYS B 2 191 ? 35.791 28.055 40.097 1.00 51.36 ? 191 LYS B CE 1 ATOM 1796 N NZ . LYS B 2 191 ? 36.668 28.514 41.205 1.00 53.34 ? 191 LYS B NZ 1 ATOM 1797 N N . PRO B 2 192 ? 29.138 28.655 38.135 1.00 46.20 ? 192 PRO B N 1 ATOM 1798 C CA . PRO B 2 192 ? 27.751 29.145 38.060 1.00 47.23 ? 192 PRO B CA 1 ATOM 1799 C C . PRO B 2 192 ? 27.561 30.580 38.587 1.00 50.37 ? 192 PRO B C 1 ATOM 1800 O O . PRO B 2 192 ? 26.770 31.340 38.030 1.00 50.27 ? 192 PRO B O 1 ATOM 1801 C CB . PRO B 2 192 ? 26.977 28.134 38.906 1.00 46.79 ? 192 PRO B CB 1 ATOM 1802 C CG . PRO B 2 192 ? 27.786 26.887 38.844 1.00 46.36 ? 192 PRO B CG 1 ATOM 1803 C CD . PRO B 2 192 ? 29.217 27.344 38.806 1.00 46.20 ? 192 PRO B CD 1 ATOM 1804 N N . ASP B 2 193 ? 28.314 30.950 39.619 1.00 55.72 ? 193 ASP B N 1 ATOM 1805 C CA . ASP B 2 193 ? 28.217 32.278 40.232 1.00 61.76 ? 193 ASP B CA 1 ATOM 1806 C C . ASP B 2 193 ? 29.017 33.401 39.549 1.00 62.51 ? 193 ASP B C 1 ATOM 1807 O O . ASP B 2 193 ? 28.995 34.533 40.033 1.00 65.82 ? 193 ASP B O 1 ATOM 1808 C CB . ASP B 2 193 ? 28.588 32.211 41.733 1.00 68.74 ? 193 ASP B CB 1 ATOM 1809 C CG . ASP B 2 193 ? 29.957 31.554 41.984 1.00 78.22 ? 193 ASP B CG 1 ATOM 1810 O OD1 . ASP B 2 193 ? 30.028 30.303 42.000 1.00 79.76 ? 193 ASP B OD1 1 ATOM 1811 O OD2 . ASP B 2 193 ? 30.962 32.286 42.164 1.00 81.09 ? 193 ASP B OD2 1 ATOM 1812 N N . GLU B 2 194 ? 29.721 33.119 38.449 1.00 59.60 ? 194 GLU B N 1 ATOM 1813 C CA . GLU B 2 194 ? 30.571 34.157 37.828 1.00 56.50 ? 194 GLU B CA 1 ATOM 1814 C C . GLU B 2 194 ? 29.871 34.974 36.728 1.00 58.83 ? 194 GLU B C 1 ATOM 1815 O O . GLU B 2 194 ? 30.427 35.958 36.227 1.00 56.53 ? 194 GLU B O 1 ATOM 1816 C CB . GLU B 2 194 ? 31.895 33.589 37.310 1.00 53.24 ? 194 GLU B CB 1 ATOM 1817 C CG . GLU B 2 194 ? 32.557 32.578 38.222 1.00 54.56 ? 194 GLU B CG 1 ATOM 1818 C CD . GLU B 2 194 ? 34.006 32.309 37.852 1.00 55.26 ? 194 GLU B CD 1 ATOM 1819 O OE1 . GLU B 2 194 ? 34.895 33.009 38.367 1.00 58.20 ? 194 GLU B OE1 1 ATOM 1820 O OE2 . GLU B 2 194 ? 34.270 31.388 37.062 1.00 53.60 ? 194 GLU B OE2 1 ATOM 1821 N N . GLY B 2 195 ? 28.664 34.558 36.347 1.00 61.69 ? 195 GLY B N 1 ATOM 1822 C CA . GLY B 2 195 ? 27.847 35.320 35.396 1.00 66.06 ? 195 GLY B CA 1 ATOM 1823 C C . GLY B 2 195 ? 28.271 35.392 33.928 1.00 68.58 ? 195 GLY B C 1 ATOM 1824 O O . GLY B 2 195 ? 27.535 35.946 33.110 1.00 72.31 ? 195 GLY B O 1 ATOM 1825 N N . LYS B 2 196 ? 29.452 34.869 33.588 1.00 63.68 ? 196 LYS B N 1 ATOM 1826 C CA . LYS B 2 196 ? 29.829 34.667 32.184 1.00 54.41 ? 196 LYS B CA 1 ATOM 1827 C C . LYS B 2 196 ? 29.706 33.199 31.836 1.00 50.23 ? 196 LYS B C 1 ATOM 1828 O O . LYS B 2 196 ? 29.805 32.345 32.717 1.00 52.39 ? 196 LYS B O 1 ATOM 1829 C CB . LYS B 2 196 ? 31.236 35.167 31.899 1.00 56.77 ? 196 LYS B CB 1 ATOM 1830 C CG . LYS B 2 196 ? 31.381 36.660 32.076 1.00 61.25 ? 196 LYS B CG 1 ATOM 1831 C CD . LYS B 2 196 ? 32.629 37.161 31.386 1.00 67.18 ? 196 LYS B CD 1 ATOM 1832 C CE . LYS B 2 196 ? 33.016 38.522 31.942 1.00 72.77 ? 196 LYS B CE 1 ATOM 1833 N NZ . LYS B 2 196 ? 33.931 39.233 31.007 1.00 79.06 ? 196 LYS B NZ 1 ATOM 1834 N N . ARG B 2 197 ? 29.458 32.911 30.560 1.00 45.54 ? 197 ARG B N 1 ATOM 1835 C CA . ARG B 2 197 ? 29.267 31.529 30.080 1.00 41.43 ? 197 ARG B CA 1 ATOM 1836 C C . ARG B 2 197 ? 30.211 31.236 28.910 1.00 37.16 ? 197 ARG B C 1 ATOM 1837 O O . ARG B 2 197 ? 30.880 32.138 28.400 1.00 36.82 ? 197 ARG B O 1 ATOM 1838 C CB . ARG B 2 197 ? 27.815 31.290 29.618 1.00 41.96 ? 197 ARG B CB 1 ATOM 1839 C CG . ARG B 2 197 ? 26.737 31.927 30.478 1.00 40.90 ? 197 ARG B CG 1 ATOM 1840 C CD . ARG B 2 197 ? 25.364 31.341 30.183 1.00 40.93 ? 197 ARG B CD 1 ATOM 1841 N NE . ARG B 2 197 ? 25.364 29.883 30.252 1.00 39.81 ? 197 ARG B NE 1 ATOM 1842 C CZ . ARG B 2 197 ? 25.062 29.177 31.338 1.00 41.50 ? 197 ARG B CZ 1 ATOM 1843 N NH1 . ARG B 2 197 ? 24.723 29.787 32.465 1.00 40.48 ? 197 ARG B NH1 1 ATOM 1844 N NH2 . ARG B 2 197 ? 25.097 27.847 31.298 1.00 40.49 ? 197 ARG B NH2 1 ATOM 1845 N N . GLY B 2 198 ? 30.245 29.980 28.476 1.00 33.58 ? 198 GLY B N 1 ATOM 1846 C CA . GLY B 2 198 ? 31.016 29.598 27.304 1.00 29.79 ? 198 GLY B CA 1 ATOM 1847 C C . GLY B 2 198 ? 31.463 28.165 27.424 1.00 30.27 ? 198 GLY B C 1 ATOM 1848 O O . GLY B 2 198 ? 31.716 27.676 28.524 1.00 30.80 ? 198 GLY B O 1 ATOM 1849 N N . ASP B 2 199 ? 31.571 27.486 26.289 1.00 30.09 ? 199 ASP B N 1 ATOM 1850 C CA . ASP B 2 199 ? 32.026 26.093 26.260 1.00 28.28 ? 199 ASP B CA 1 ATOM 1851 C C . ASP B 2 199 ? 32.326 25.646 24.820 1.00 27.79 ? 199 ASP B C 1 ATOM 1852 O O . ASP B 2 199 ? 31.935 26.308 23.859 1.00 27.78 ? 199 ASP B O 1 ATOM 1853 C CB . ASP B 2 199 ? 30.962 25.190 26.898 1.00 26.87 ? 199 ASP B CB 1 ATOM 1854 C CG . ASP B 2 199 ? 31.497 23.827 27.291 1.00 28.25 ? 199 ASP B CG 1 ATOM 1855 O OD1 . ASP B 2 199 ? 32.737 23.616 27.306 1.00 27.88 ? 199 ASP B OD1 1 ATOM 1856 O OD2 . ASP B 2 199 ? 30.660 22.943 27.588 1.00 29.36 ? 199 ASP B OD2 1 ATOM 1857 N N . ALA B 2 200 ? 33.036 24.534 24.677 1.00 26.72 ? 200 ALA B N 1 ATOM 1858 C CA . ALA B 2 200 ? 33.136 23.855 23.396 1.00 27.27 ? 200 ALA B CA 1 ATOM 1859 C C . ALA B 2 200 ? 31.874 22.995 23.249 1.00 28.52 ? 200 ALA B C 1 ATOM 1860 O O . ALA B 2 200 ? 31.117 22.852 24.219 1.00 28.52 ? 200 ALA B O 1 ATOM 1861 C CB . ALA B 2 200 ? 34.393 22.996 23.355 1.00 26.42 ? 200 ALA B CB 1 ATOM 1862 N N . CYS B 2 201 ? 31.640 22.434 22.057 1.00 28.18 ? 201 CYS B N 1 ATOM 1863 C CA . CYS B 2 201 ? 30.447 21.616 21.796 1.00 28.51 ? 201 CYS B CA 1 ATOM 1864 C C . CYS B 2 201 ? 30.720 20.693 20.604 1.00 29.82 ? 201 CYS B C 1 ATOM 1865 O O . CYS B 2 201 ? 31.831 20.725 20.049 1.00 29.62 ? 201 CYS B O 1 ATOM 1866 C CB . CYS B 2 201 ? 29.235 22.529 21.550 1.00 29.62 ? 201 CYS B CB 1 ATOM 1867 S SG . CYS B 2 201 ? 27.618 21.767 21.847 1.00 31.89 ? 201 CYS B SG 1 ATOM 1868 N N A GLU B 2 202 ? 29.724 19.890 20.209 0.50 30.16 ? 202 GLU B N 1 ATOM 1869 N N B GLU B 2 202 ? 29.727 19.895 20.215 0.50 30.22 ? 202 GLU B N 1 ATOM 1870 C CA A GLU B 2 202 ? 29.883 18.900 19.121 0.50 31.30 ? 202 GLU B CA 1 ATOM 1871 C CA B GLU B 2 202 ? 29.887 18.915 19.137 0.50 31.51 ? 202 GLU B CA 1 ATOM 1872 C C A GLU B 2 202 ? 30.532 19.489 17.864 0.50 30.51 ? 202 GLU B C 1 ATOM 1873 C C B GLU B 2 202 ? 30.548 19.504 17.882 0.50 30.55 ? 202 GLU B C 1 ATOM 1874 O O A GLU B 2 202 ? 30.085 20.521 17.344 0.50 30.75 ? 202 GLU B O 1 ATOM 1875 O O B GLU B 2 202 ? 30.119 20.551 17.377 0.50 30.76 ? 202 GLU B O 1 ATOM 1876 C CB A GLU B 2 202 ? 28.551 18.205 18.773 0.50 33.27 ? 202 GLU B CB 1 ATOM 1877 C CB B GLU B 2 202 ? 28.537 18.294 18.786 0.50 33.31 ? 202 GLU B CB 1 ATOM 1878 C CG A GLU B 2 202 ? 28.567 17.471 17.429 0.50 36.85 ? 202 GLU B CG 1 ATOM 1879 C CG B GLU B 2 202 ? 28.633 17.165 17.778 0.50 36.98 ? 202 GLU B CG 1 ATOM 1880 C CD A GLU B 2 202 ? 27.563 16.323 17.331 0.50 40.17 ? 202 GLU B CD 1 ATOM 1881 C CD B GLU B 2 202 ? 29.343 15.944 18.337 0.50 39.57 ? 202 GLU B CD 1 ATOM 1882 O OE1 A GLU B 2 202 ? 26.944 15.958 18.354 0.50 41.24 ? 202 GLU B OE1 1 ATOM 1883 O OE1 B GLU B 2 202 ? 29.638 15.912 19.559 0.50 39.82 ? 202 GLU B OE1 1 ATOM 1884 O OE2 A GLU B 2 202 ? 27.399 15.767 16.221 0.50 41.82 ? 202 GLU B OE2 1 ATOM 1885 O OE2 B GLU B 2 202 ? 29.603 15.013 17.543 0.50 41.54 ? 202 GLU B OE2 1 ATOM 1886 N N . GLY B 2 203 ? 31.594 18.833 17.398 1.00 28.84 ? 203 GLY B N 1 ATOM 1887 C CA . GLY B 2 203 ? 32.380 19.321 16.268 1.00 26.52 ? 203 GLY B CA 1 ATOM 1888 C C . GLY B 2 203 ? 33.626 20.137 16.640 1.00 26.44 ? 203 GLY B C 1 ATOM 1889 O O . GLY B 2 203 ? 34.514 20.320 15.794 1.00 25.70 ? 203 GLY B O 1 ATOM 1890 N N . ASP B 2 204 ? 33.695 20.640 17.881 1.00 24.57 ? 204 ASP B N 1 ATOM 1891 C CA . ASP B 2 204 ? 34.871 21.364 18.362 1.00 24.26 ? 204 ASP B CA 1 ATOM 1892 C C . ASP B 2 204 ? 35.973 20.401 18.841 1.00 24.64 ? 204 ASP B C 1 ATOM 1893 O O . ASP B 2 204 ? 37.133 20.800 18.987 1.00 23.30 ? 204 ASP B O 1 ATOM 1894 C CB . ASP B 2 204 ? 34.505 22.314 19.499 1.00 24.50 ? 204 ASP B CB 1 ATOM 1895 C CG . ASP B 2 204 ? 33.636 23.496 19.047 1.00 26.98 ? 204 ASP B CG 1 ATOM 1896 O OD1 . ASP B 2 204 ? 33.906 24.093 17.979 1.00 26.43 ? 204 ASP B OD1 1 ATOM 1897 O OD2 . ASP B 2 204 ? 32.677 23.844 19.782 1.00 27.07 ? 204 ASP B OD2 1 ATOM 1898 N N . SER B 2 205 ? 35.597 19.142 19.097 1.00 24.92 ? 205 SER B N 1 ATOM 1899 C CA . SER B 2 205 ? 36.525 18.127 19.593 1.00 25.16 ? 205 SER B CA 1 ATOM 1900 C C . SER B 2 205 ? 37.789 18.098 18.768 1.00 23.74 ? 205 SER B C 1 ATOM 1901 O O . SER B 2 205 ? 37.733 18.265 17.545 1.00 22.55 ? 205 SER B O 1 ATOM 1902 C CB . SER B 2 205 ? 35.892 16.735 19.536 1.00 27.21 ? 205 SER B CB 1 ATOM 1903 O OG . SER B 2 205 ? 34.976 16.566 20.587 1.00 29.76 ? 205 SER B OG 1 ATOM 1904 N N . GLY B 2 206 ? 38.919 17.870 19.441 1.00 22.66 ? 206 GLY B N 1 ATOM 1905 C CA . GLY B 2 206 ? 40.207 17.766 18.769 1.00 22.16 ? 206 GLY B CA 1 ATOM 1906 C C . GLY B 2 206 ? 40.887 19.102 18.552 1.00 21.38 ? 206 GLY B C 1 ATOM 1907 O O . GLY B 2 206 ? 42.065 19.146 18.210 1.00 22.36 ? 206 GLY B O 1 ATOM 1908 N N . GLY B 2 207 ? 40.153 20.189 18.755 1.00 21.02 ? 207 GLY B N 1 ATOM 1909 C CA . GLY B 2 207 ? 40.698 21.544 18.581 1.00 22.35 ? 207 GLY B CA 1 ATOM 1910 C C . GLY B 2 207 ? 41.610 21.982 19.725 1.00 22.37 ? 207 GLY B C 1 ATOM 1911 O O . GLY B 2 207 ? 41.633 21.349 20.789 1.00 22.11 ? 207 GLY B O 1 ATOM 1912 N N . PRO B 2 208 ? 42.363 23.070 19.515 1.00 22.51 ? 208 PRO B N 1 ATOM 1913 C CA . PRO B 2 208 ? 43.356 23.522 20.506 1.00 22.65 ? 208 PRO B CA 1 ATOM 1914 C C . PRO B 2 208 ? 42.796 24.436 21.599 1.00 22.33 ? 208 PRO B C 1 ATOM 1915 O O . PRO B 2 208 ? 41.968 25.312 21.329 1.00 22.30 ? 208 PRO B O 1 ATOM 1916 C CB . PRO B 2 208 ? 44.359 24.306 19.655 1.00 22.17 ? 208 PRO B CB 1 ATOM 1917 C CG . PRO B 2 208 ? 43.536 24.853 18.516 1.00 22.43 ? 208 PRO B CG 1 ATOM 1918 C CD . PRO B 2 208 ? 42.375 23.903 18.293 1.00 22.76 ? 208 PRO B CD 1 ATOM 1919 N N . PHE B 2 209 ? 43.246 24.200 22.824 1.00 22.14 ? 209 PHE B N 1 ATOM 1920 C CA . PHE B 2 209 ? 43.118 25.151 23.908 1.00 23.24 ? 209 PHE B CA 1 ATOM 1921 C C . PHE B 2 209 ? 44.494 25.820 24.000 1.00 23.68 ? 209 PHE B C 1 ATOM 1922 O O . PHE B 2 209 ? 45.505 25.152 24.281 1.00 23.48 ? 209 PHE B O 1 ATOM 1923 C CB . PHE B 2 209 ? 42.775 24.407 25.189 1.00 24.45 ? 209 PHE B CB 1 ATOM 1924 C CG . PHE B 2 209 ? 42.646 25.288 26.398 1.00 26.31 ? 209 PHE B CG 1 ATOM 1925 C CD1 . PHE B 2 209 ? 43.779 25.717 27.095 1.00 27.73 ? 209 PHE B CD1 1 ATOM 1926 C CD2 . PHE B 2 209 ? 41.385 25.654 26.877 1.00 26.06 ? 209 PHE B CD2 1 ATOM 1927 C CE1 . PHE B 2 209 ? 43.649 26.520 28.228 1.00 27.81 ? 209 PHE B CE1 1 ATOM 1928 C CE2 . PHE B 2 209 ? 41.253 26.448 27.999 1.00 25.43 ? 209 PHE B CE2 1 ATOM 1929 C CZ . PHE B 2 209 ? 42.382 26.879 28.679 1.00 26.73 ? 209 PHE B CZ 1 ATOM 1930 N N . VAL B 2 210 ? 44.544 27.118 23.706 1.00 22.64 ? 210 VAL B N 1 ATOM 1931 C CA . VAL B 2 210 ? 45.816 27.812 23.610 1.00 23.84 ? 210 VAL B CA 1 ATOM 1932 C C . VAL B 2 210 ? 45.951 28.944 24.643 1.00 25.42 ? 210 VAL B C 1 ATOM 1933 O O . VAL B 2 210 ? 44.940 29.534 25.063 1.00 24.86 ? 210 VAL B O 1 ATOM 1934 C CB . VAL B 2 210 ? 46.103 28.359 22.175 1.00 23.37 ? 210 VAL B CB 1 ATOM 1935 C CG1 . VAL B 2 210 ? 46.064 27.237 21.147 1.00 22.99 ? 210 VAL B CG1 1 ATOM 1936 C CG2 . VAL B 2 210 ? 45.156 29.502 21.802 1.00 22.43 ? 210 VAL B CG2 1 ATOM 1937 N N . MET B 2 211 ? 47.199 29.239 25.035 1.00 25.39 ? 211 MET B N 1 ATOM 1938 C CA . MET B 2 211 ? 47.495 30.345 25.956 1.00 26.33 ? 211 MET B CA 1 ATOM 1939 C C . MET B 2 211 ? 48.645 31.203 25.421 1.00 26.76 ? 211 MET B C 1 ATOM 1940 O O . MET B 2 211 ? 49.555 30.694 24.763 1.00 27.99 ? 211 MET B O 1 ATOM 1941 C CB . MET B 2 211 ? 47.801 29.815 27.358 1.00 25.72 ? 211 MET B CB 1 ATOM 1942 C CG . MET B 2 211 ? 46.630 29.100 28.004 1.00 24.82 ? 211 MET B CG 1 ATOM 1943 S SD . MET B 2 211 ? 46.961 28.458 29.652 1.00 26.74 ? 211 MET B SD 1 ATOM 1944 C CE . MET B 2 211 ? 46.764 29.998 30.560 1.00 26.64 ? 211 MET B CE 1 ATOM 1945 N N . LYS B 2 212 ? 48.589 32.507 25.667 1.00 25.82 ? 212 LYS B N 1 ATOM 1946 C CA . LYS B 2 212 ? 49.653 33.398 25.199 1.00 26.10 ? 212 LYS B CA 1 ATOM 1947 C C . LYS B 2 212 ? 50.625 33.730 26.336 1.00 26.58 ? 212 LYS B C 1 ATOM 1948 O O . LYS B 2 212 ? 50.214 34.122 27.429 1.00 27.48 ? 212 LYS B O 1 ATOM 1949 C CB . LYS B 2 212 ? 49.068 34.686 24.614 1.00 24.97 ? 212 LYS B CB 1 ATOM 1950 C CG . LYS B 2 212 ? 50.139 35.592 24.026 1.00 25.19 ? 212 LYS B CG 1 ATOM 1951 C CD . LYS B 2 212 ? 49.593 36.874 23.433 1.00 24.34 ? 212 LYS B CD 1 ATOM 1952 C CE . LYS B 2 212 ? 50.652 37.489 22.546 1.00 25.19 ? 212 LYS B CE 1 ATOM 1953 N NZ . LYS B 2 212 ? 50.115 38.600 21.721 1.00 25.18 ? 212 LYS B NZ 1 ATOM 1954 N N . SER B 2 213 ? 51.911 33.570 26.088 1.00 27.63 ? 213 SER B N 1 ATOM 1955 C CA . SER B 2 213 ? 52.916 33.989 27.070 1.00 29.63 ? 213 SER B CA 1 ATOM 1956 C C . SER B 2 213 ? 53.225 35.476 26.945 1.00 30.12 ? 213 SER B C 1 ATOM 1957 O O . SER B 2 213 ? 53.591 35.941 25.861 1.00 30.79 ? 213 SER B O 1 ATOM 1958 C CB . SER B 2 213 ? 54.204 33.208 26.899 1.00 29.80 ? 213 SER B CB 1 ATOM 1959 O OG . SER B 2 213 ? 55.254 33.951 27.477 1.00 33.46 ? 213 SER B OG 1 ATOM 1960 N N . PRO B 2 214 ? 53.093 36.231 28.051 1.00 31.21 ? 214 PRO B N 1 ATOM 1961 C CA . PRO B 2 214 ? 53.335 37.685 27.974 1.00 31.49 ? 214 PRO B CA 1 ATOM 1962 C C . PRO B 2 214 ? 54.819 38.071 27.837 1.00 32.42 ? 214 PRO B C 1 ATOM 1963 O O . PRO B 2 214 ? 55.112 39.195 27.436 1.00 35.95 ? 214 PRO B O 1 ATOM 1964 C CB . PRO B 2 214 ? 52.741 38.223 29.280 1.00 30.43 ? 214 PRO B CB 1 ATOM 1965 C CG . PRO B 2 214 ? 52.752 37.069 30.216 1.00 32.11 ? 214 PRO B CG 1 ATOM 1966 C CD . PRO B 2 214 ? 52.749 35.788 29.414 1.00 31.93 ? 214 PRO B CD 1 ATOM 1967 N N . PHE B 2 215 ? 55.731 37.141 28.137 1.00 31.66 ? 215 PHE B N 1 ATOM 1968 C CA . PHE B 2 215 ? 57.173 37.411 28.100 1.00 30.39 ? 215 PHE B CA 1 ATOM 1969 C C . PHE B 2 215 ? 57.851 37.212 26.765 1.00 30.40 ? 215 PHE B C 1 ATOM 1970 O O . PHE B 2 215 ? 58.807 37.922 26.471 1.00 30.57 ? 215 PHE B O 1 ATOM 1971 C CB . PHE B 2 215 ? 57.915 36.669 29.212 1.00 29.15 ? 215 PHE B CB 1 ATOM 1972 C CG . PHE B 2 215 ? 57.410 37.015 30.569 1.00 29.48 ? 215 PHE B CG 1 ATOM 1973 C CD1 . PHE B 2 215 ? 57.170 38.356 30.906 1.00 30.05 ? 215 PHE B CD1 1 ATOM 1974 C CD2 . PHE B 2 215 ? 57.101 36.019 31.487 1.00 30.74 ? 215 PHE B CD2 1 ATOM 1975 C CE1 . PHE B 2 215 ? 56.660 38.695 32.149 1.00 30.78 ? 215 PHE B CE1 1 ATOM 1976 C CE2 . PHE B 2 215 ? 56.586 36.344 32.734 1.00 31.23 ? 215 PHE B CE2 1 ATOM 1977 C CZ . PHE B 2 215 ? 56.368 37.684 33.067 1.00 31.84 ? 215 PHE B CZ 1 ATOM 1978 N N . ASN B 2 216 ? 57.377 36.270 25.952 1.00 30.20 ? 216 ASN B N 1 ATOM 1979 C CA . ASN B 2 216 ? 57.925 36.142 24.594 1.00 28.50 ? 216 ASN B CA 1 ATOM 1980 C C . ASN B 2 216 ? 56.892 36.398 23.516 1.00 30.12 ? 216 ASN B C 1 ATOM 1981 O O . ASN B 2 216 ? 57.221 36.381 22.342 1.00 33.45 ? 216 ASN B O 1 ATOM 1982 C CB . ASN B 2 216 ? 58.688 34.822 24.378 1.00 26.53 ? 216 ASN B CB 1 ATOM 1983 C CG . ASN B 2 216 ? 57.802 33.599 24.504 1.00 26.22 ? 216 ASN B CG 1 ATOM 1984 O OD1 . ASN B 2 216 ? 56.588 33.702 24.547 1.00 27.53 ? 216 ASN B OD1 1 ATOM 1985 N ND2 . ASN B 2 216 ? 58.405 32.437 24.540 1.00 25.31 ? 216 ASN B ND2 1 ATOM 1986 N N . ASN B 2 217 ? 55.643 36.642 23.910 1.00 32.96 ? 217 ASN B N 1 ATOM 1987 C CA . ASN B 2 217 ? 54.564 36.925 22.944 1.00 34.69 ? 217 ASN B CA 1 ATOM 1988 C C . ASN B 2 217 ? 54.025 35.741 22.102 1.00 34.19 ? 217 ASN B C 1 ATOM 1989 O O . ASN B 2 217 ? 53.273 35.941 21.141 1.00 33.37 ? 217 ASN B O 1 ATOM 1990 C CB . ASN B 2 217 ? 54.960 38.080 22.026 1.00 38.67 ? 217 ASN B CB 1 ATOM 1991 C CG . ASN B 2 217 ? 54.179 39.331 22.330 1.00 47.15 ? 217 ASN B CG 1 ATOM 1992 O OD1 . ASN B 2 217 ? 54.471 40.032 23.303 1.00 52.41 ? 217 ASN B OD1 1 ATOM 1993 N ND2 . ASN B 2 217 ? 53.153 39.607 21.521 1.00 47.60 ? 217 ASN B ND2 1 ATOM 1994 N N . ARG B 2 218 ? 54.402 34.518 22.464 1.00 31.04 ? 218 ARG B N 1 ATOM 1995 C CA . ARG B 2 218 ? 54.030 33.360 21.680 1.00 29.87 ? 218 ARG B CA 1 ATOM 1996 C C . ARG B 2 218 ? 52.795 32.662 22.221 1.00 27.06 ? 218 ARG B C 1 ATOM 1997 O O . ARG B 2 218 ? 52.498 32.722 23.426 1.00 26.05 ? 218 ARG B O 1 ATOM 1998 C CB . ARG B 2 218 ? 55.195 32.371 21.596 1.00 31.37 ? 218 ARG B CB 1 ATOM 1999 C CG . ARG B 2 218 ? 56.316 32.839 20.695 1.00 33.83 ? 218 ARG B CG 1 ATOM 2000 C CD . ARG B 2 218 ? 57.527 31.920 20.789 1.00 36.41 ? 218 ARG B CD 1 ATOM 2001 N NE . ARG B 2 218 ? 58.690 32.626 20.264 1.00 41.07 ? 218 ARG B NE 1 ATOM 2002 C CZ . ARG B 2 218 ? 59.167 32.499 19.034 1.00 43.85 ? 218 ARG B CZ 1 ATOM 2003 N NH1 . ARG B 2 218 ? 58.623 31.651 18.166 1.00 49.42 ? 218 ARG B NH1 1 ATOM 2004 N NH2 . ARG B 2 218 ? 60.214 33.211 18.676 1.00 44.49 ? 218 ARG B NH2 1 ATOM 2005 N N . TRP B 2 219 ? 52.096 31.985 21.312 1.00 23.78 ? 219 TRP B N 1 ATOM 2006 C CA . TRP B 2 219 ? 50.966 31.140 21.663 1.00 21.64 ? 219 TRP B CA 1 ATOM 2007 C C . TRP B 2 219 ? 51.400 29.692 21.858 1.00 21.36 ? 219 TRP B C 1 ATOM 2008 O O . TRP B 2 219 ? 52.206 29.161 21.077 1.00 20.49 ? 219 TRP B O 1 ATOM 2009 C CB . TRP B 2 219 ? 49.904 31.230 20.590 1.00 20.87 ? 219 TRP B CB 1 ATOM 2010 C CG . TRP B 2 219 ? 49.293 32.574 20.478 1.00 20.27 ? 219 TRP B CG 1 ATOM 2011 C CD1 . TRP B 2 219 ? 49.733 33.615 19.708 1.00 20.23 ? 219 TRP B CD1 1 ATOM 2012 C CD2 . TRP B 2 219 ? 48.105 33.034 21.141 1.00 19.78 ? 219 TRP B CD2 1 ATOM 2013 N NE1 . TRP B 2 219 ? 48.885 34.699 19.845 1.00 20.53 ? 219 TRP B NE1 1 ATOM 2014 C CE2 . TRP B 2 219 ? 47.886 34.371 20.729 1.00 20.13 ? 219 TRP B CE2 1 ATOM 2015 C CE3 . TRP B 2 219 ? 47.213 32.452 22.055 1.00 19.46 ? 219 TRP B CE3 1 ATOM 2016 C CZ2 . TRP B 2 219 ? 46.808 35.132 21.202 1.00 19.88 ? 219 TRP B CZ2 1 ATOM 2017 C CZ3 . TRP B 2 219 ? 46.125 33.204 22.516 1.00 18.69 ? 219 TRP B CZ3 1 ATOM 2018 C CH2 . TRP B 2 219 ? 45.934 34.525 22.086 1.00 19.53 ? 219 TRP B CH2 1 ATOM 2019 N N . TYR B 2 220 ? 50.886 29.074 22.926 1.00 21.36 ? 220 TYR B N 1 ATOM 2020 C CA . TYR B 2 220 ? 51.194 27.695 23.257 1.00 21.92 ? 220 TYR B CA 1 ATOM 2021 C C . TYR B 2 220 ? 49.924 26.883 23.344 1.00 22.85 ? 220 TYR B C 1 ATOM 2022 O O . TYR B 2 220 ? 48.923 27.333 23.910 1.00 23.79 ? 220 TYR B O 1 ATOM 2023 C CB . TYR B 2 220 ? 51.922 27.603 24.591 1.00 22.54 ? 220 TYR B CB 1 ATOM 2024 C CG . TYR B 2 220 ? 53.307 28.157 24.532 1.00 23.85 ? 220 TYR B CG 1 ATOM 2025 C CD1 . TYR B 2 220 ? 53.540 29.525 24.742 1.00 24.17 ? 220 TYR B CD1 1 ATOM 2026 C CD2 . TYR B 2 220 ? 54.401 27.324 24.253 1.00 24.26 ? 220 TYR B CD2 1 ATOM 2027 C CE1 . TYR B 2 220 ? 54.822 30.046 24.673 1.00 24.98 ? 220 TYR B CE1 1 ATOM 2028 C CE2 . TYR B 2 220 ? 55.686 27.831 24.190 1.00 24.15 ? 220 TYR B CE2 1 ATOM 2029 C CZ . TYR B 2 220 ? 55.887 29.196 24.406 1.00 25.43 ? 220 TYR B CZ 1 ATOM 2030 O OH . TYR B 2 220 ? 57.155 29.726 24.338 1.00 27.00 ? 220 TYR B OH 1 ATOM 2031 N N . GLN B 2 221 ? 49.969 25.673 22.799 1.00 22.28 ? 221 GLN B N 1 ATOM 2032 C CA . GLN B 2 221 ? 48.862 24.774 22.954 1.00 21.69 ? 221 GLN B CA 1 ATOM 2033 C C . GLN B 2 221 ? 48.996 24.015 24.267 1.00 21.69 ? 221 GLN B C 1 ATOM 2034 O O . GLN B 2 221 ? 49.889 23.200 24.423 1.00 22.41 ? 221 GLN B O 1 ATOM 2035 C CB . GLN B 2 221 ? 48.781 23.817 21.778 1.00 21.05 ? 221 GLN B CB 1 ATOM 2036 C CG . GLN B 2 221 ? 47.549 22.957 21.904 1.00 21.46 ? 221 GLN B CG 1 ATOM 2037 C CD . GLN B 2 221 ? 47.198 22.175 20.668 1.00 21.75 ? 221 GLN B CD 1 ATOM 2038 O OE1 . GLN B 2 221 ? 46.180 21.494 20.658 1.00 24.12 ? 221 GLN B OE1 1 ATOM 2039 N NE2 . GLN B 2 221 ? 48.032 22.238 19.639 1.00 20.92 ? 221 GLN B NE2 1 ATOM 2040 N N . MET B 2 222 ? 48.097 24.270 25.205 1.00 22.60 ? 222 MET B N 1 ATOM 2041 C CA . MET B 2 222 ? 48.153 23.605 26.502 1.00 23.73 ? 222 MET B CA 1 ATOM 2042 C C . MET B 2 222 ? 47.194 22.428 26.573 1.00 25.32 ? 222 MET B C 1 ATOM 2043 O O . MET B 2 222 ? 47.399 21.522 27.386 1.00 25.80 ? 222 MET B O 1 ATOM 2044 C CB . MET B 2 222 ? 47.834 24.581 27.644 1.00 25.30 ? 222 MET B CB 1 ATOM 2045 C CG . MET B 2 222 ? 48.661 25.873 27.692 1.00 27.31 ? 222 MET B CG 1 ATOM 2046 S SD . MET B 2 222 ? 50.450 25.619 27.706 1.00 30.44 ? 222 MET B SD 1 ATOM 2047 C CE . MET B 2 222 ? 50.650 24.689 29.218 1.00 29.85 ? 222 MET B CE 1 ATOM 2048 N N . GLY B 2 223 ? 46.145 22.446 25.738 1.00 25.52 ? 223 GLY B N 1 ATOM 2049 C CA . GLY B 2 223 ? 45.114 21.412 25.750 1.00 24.25 ? 223 GLY B CA 1 ATOM 2050 C C . GLY B 2 223 ? 44.515 21.045 24.399 1.00 25.71 ? 223 GLY B C 1 ATOM 2051 O O . GLY B 2 223 ? 44.734 21.726 23.370 1.00 25.76 ? 223 GLY B O 1 ATOM 2052 N N . ILE B 2 224 ? 43.760 19.946 24.406 1.00 24.40 ? 224 ILE B N 1 ATOM 2053 C CA . ILE B 2 224 ? 43.000 19.485 23.253 1.00 23.32 ? 224 ILE B CA 1 ATOM 2054 C C . ILE B 2 224 ? 41.562 19.286 23.724 1.00 24.35 ? 224 ILE B C 1 ATOM 2055 O O . ILE B 2 224 ? 41.335 18.660 24.773 1.00 25.09 ? 224 ILE B O 1 ATOM 2056 C CB . ILE B 2 224 ? 43.555 18.151 22.718 1.00 23.21 ? 224 ILE B CB 1 ATOM 2057 C CG1 . ILE B 2 224 ? 45.039 18.293 22.331 1.00 22.56 ? 224 ILE B CG1 1 ATOM 2058 C CG2 . ILE B 2 224 ? 42.711 17.632 21.555 1.00 21.87 ? 224 ILE B CG2 1 ATOM 2059 C CD1 . ILE B 2 224 ? 45.734 16.984 22.014 1.00 21.56 ? 224 ILE B CD1 1 ATOM 2060 N N . VAL B 2 225 ? 40.591 19.829 22.984 1.00 23.64 ? 225 VAL B N 1 ATOM 2061 C CA . VAL B 2 225 ? 39.177 19.623 23.339 1.00 23.42 ? 225 VAL B CA 1 ATOM 2062 C C . VAL B 2 225 ? 38.883 18.116 23.323 1.00 23.93 ? 225 VAL B C 1 ATOM 2063 O O . VAL B 2 225 ? 39.033 17.442 22.287 1.00 22.81 ? 225 VAL B O 1 ATOM 2064 C CB . VAL B 2 225 ? 38.204 20.379 22.401 1.00 23.03 ? 225 VAL B CB 1 ATOM 2065 C CG1 . VAL B 2 225 ? 36.770 20.155 22.839 1.00 21.95 ? 225 VAL B CG1 1 ATOM 2066 C CG2 . VAL B 2 225 ? 38.526 21.863 22.353 1.00 22.30 ? 225 VAL B CG2 1 ATOM 2067 N N . SER B 2 226 ? 38.490 17.598 24.484 1.00 25.63 ? 226 SER B N 1 ATOM 2068 C CA . SER B 2 226 ? 38.349 16.159 24.681 1.00 27.86 ? 226 SER B CA 1 ATOM 2069 C C . SER B 2 226 ? 36.913 15.730 24.956 1.00 29.96 ? 226 SER B C 1 ATOM 2070 O O . SER B 2 226 ? 36.326 15.018 24.145 1.00 30.98 ? 226 SER B O 1 ATOM 2071 C CB . SER B 2 226 ? 39.257 15.666 25.808 1.00 27.32 ? 226 SER B CB 1 ATOM 2072 O OG . SER B 2 226 ? 39.223 14.257 25.884 1.00 26.20 ? 226 SER B OG 1 ATOM 2073 N N . TRP B 2 227 ? 36.351 16.135 26.094 1.00 30.65 ? 227 TRP B N 1 ATOM 2074 C CA . TRP B 2 227 ? 34.981 15.730 26.422 1.00 32.10 ? 227 TRP B CA 1 ATOM 2075 C C . TRP B 2 227 ? 34.303 16.668 27.414 1.00 32.95 ? 227 TRP B C 1 ATOM 2076 O O . TRP B 2 227 ? 34.941 17.533 28.027 1.00 32.76 ? 227 TRP B O 1 ATOM 2077 C CB . TRP B 2 227 ? 34.924 14.266 26.913 1.00 34.23 ? 227 TRP B CB 1 ATOM 2078 C CG . TRP B 2 227 ? 35.645 14.018 28.236 1.00 38.07 ? 227 TRP B CG 1 ATOM 2079 C CD1 . TRP B 2 227 ? 36.969 13.712 28.409 1.00 37.94 ? 227 TRP B CD1 1 ATOM 2080 C CD2 . TRP B 2 227 ? 35.072 14.061 29.554 1.00 39.94 ? 227 TRP B CD2 1 ATOM 2081 N NE1 . TRP B 2 227 ? 37.256 13.577 29.748 1.00 38.92 ? 227 TRP B NE1 1 ATOM 2082 C CE2 . TRP B 2 227 ? 36.111 13.779 30.472 1.00 41.60 ? 227 TRP B CE2 1 ATOM 2083 C CE3 . TRP B 2 227 ? 33.779 14.318 30.050 1.00 40.68 ? 227 TRP B CE3 1 ATOM 2084 C CZ2 . TRP B 2 227 ? 35.899 13.750 31.860 1.00 43.75 ? 227 TRP B CZ2 1 ATOM 2085 C CZ3 . TRP B 2 227 ? 33.568 14.283 31.428 1.00 40.66 ? 227 TRP B CZ3 1 ATOM 2086 C CH2 . TRP B 2 227 ? 34.622 14.005 32.314 1.00 43.10 ? 227 TRP B CH2 1 ATOM 2087 N N . GLY B 2 228 ? 32.997 16.481 27.552 1.00 33.64 ? 228 GLY B N 1 ATOM 2088 C CA . GLY B 2 228 ? 32.148 17.272 28.436 1.00 35.85 ? 228 GLY B CA 1 ATOM 2089 C C . GLY B 2 228 ? 30.779 16.618 28.495 1.00 38.48 ? 228 GLY B C 1 ATOM 2090 O O . GLY B 2 228 ? 30.483 15.703 27.714 1.00 37.71 ? 228 GLY B O 1 ATOM 2091 N N . GLU B 2 229 ? 29.944 17.065 29.429 1.00 39.88 ? 229 GLU B N 1 ATOM 2092 C CA . GLU B 2 229 ? 28.589 16.517 29.578 1.00 40.02 ? 229 GLU B CA 1 ATOM 2093 C C . GLU B 2 229 ? 27.593 17.585 29.128 1.00 38.61 ? 229 GLU B C 1 ATOM 2094 O O . GLU B 2 229 ? 27.274 18.518 29.876 1.00 37.17 ? 229 GLU B O 1 ATOM 2095 C CB . GLU B 2 229 ? 28.340 16.053 31.021 1.00 42.85 ? 229 GLU B CB 1 ATOM 2096 C CG . GLU B 2 229 ? 29.261 14.918 31.486 1.00 46.37 ? 229 GLU B CG 1 ATOM 2097 C CD . GLU B 2 229 ? 29.173 14.658 32.984 1.00 49.50 ? 229 GLU B CD 1 ATOM 2098 O OE1 . GLU B 2 229 ? 29.791 15.381 33.796 1.00 50.11 ? 229 GLU B OE1 1 ATOM 2099 O OE2 . GLU B 2 229 ? 28.468 13.716 33.362 1.00 54.41 ? 229 GLU B OE2 1 ATOM 2100 N N . GLY B 2 230 ? 27.143 17.466 27.879 1.00 37.73 ? 230 GLY B N 1 ATOM 2101 C CA . GLY B 2 230 ? 26.356 18.528 27.243 1.00 37.08 ? 230 GLY B CA 1 ATOM 2102 C C . GLY B 2 230 ? 27.261 19.696 26.879 1.00 35.86 ? 230 GLY B C 1 ATOM 2103 O O . GLY B 2 230 ? 28.470 19.524 26.753 1.00 35.36 ? 230 GLY B O 1 ATOM 2104 N N . CYS B 2 231 ? 26.686 20.884 26.705 1.00 33.65 ? 231 CYS B N 1 ATOM 2105 C CA . CYS B 2 231 ? 27.472 22.053 26.327 1.00 31.95 ? 231 CYS B CA 1 ATOM 2106 C C . CYS B 2 231 ? 26.978 23.212 27.133 1.00 31.84 ? 231 CYS B C 1 ATOM 2107 O O . CYS B 2 231 ? 25.795 23.482 27.131 1.00 33.89 ? 231 CYS B O 1 ATOM 2108 C CB . CYS B 2 231 ? 27.326 22.378 24.831 1.00 30.01 ? 231 CYS B CB 1 ATOM 2109 S SG . CYS B 2 231 ? 27.721 21.001 23.745 1.00 30.00 ? 231 CYS B SG 1 ATOM 2110 N N . ASP B 2 232 ? 27.889 23.886 27.825 1.00 33.08 ? 232 ASP B N 1 ATOM 2111 C CA . ASP B 2 232 ? 27.578 25.084 28.601 1.00 33.42 ? 232 ASP B CA 1 ATOM 2112 C C . ASP B 2 232 ? 26.547 24.870 29.733 1.00 33.81 ? 232 ASP B C 1 ATOM 2113 O O . ASP B 2 232 ? 25.812 25.795 30.084 1.00 33.76 ? 232 ASP B O 1 ATOM 2114 C CB . ASP B 2 232 ? 27.140 26.222 27.670 1.00 31.80 ? 232 ASP B CB 1 ATOM 2115 C CG . ASP B 2 232 ? 27.291 27.579 28.307 1.00 34.54 ? 232 ASP B CG 1 ATOM 2116 O OD1 . ASP B 2 232 ? 28.286 27.825 29.033 1.00 36.07 ? 232 ASP B OD1 1 ATOM 2117 O OD2 . ASP B 2 232 ? 26.409 28.420 28.091 1.00 37.41 ? 232 ASP B OD2 1 ATOM 2118 N N . ARG B 2 233 ? 26.500 23.671 30.316 1.00 32.65 ? 233 ARG B N 1 ATOM 2119 C CA . ARG B 2 233 ? 25.610 23.443 31.455 1.00 35.32 ? 233 ARG B CA 1 ATOM 2120 C C . ARG B 2 233 ? 26.161 24.080 32.730 1.00 38.36 ? 233 ARG B C 1 ATOM 2121 O O . ARG B 2 233 ? 27.378 24.106 32.931 1.00 42.19 ? 233 ARG B O 1 ATOM 2122 C CB . ARG B 2 233 ? 25.363 21.955 31.674 1.00 34.66 ? 233 ARG B CB 1 ATOM 2123 C CG . ARG B 2 233 ? 24.408 21.348 30.668 1.00 35.48 ? 233 ARG B CG 1 ATOM 2124 C CD . ARG B 2 233 ? 24.320 19.862 30.899 1.00 39.74 ? 233 ARG B CD 1 ATOM 2125 N NE . ARG B 2 233 ? 23.564 19.191 29.844 1.00 48.18 ? 233 ARG B NE 1 ATOM 2126 C CZ . ARG B 2 233 ? 23.445 17.867 29.732 1.00 52.81 ? 233 ARG B CZ 1 ATOM 2127 N NH1 . ARG B 2 233 ? 24.027 17.059 30.609 1.00 55.62 ? 233 ARG B NH1 1 ATOM 2128 N NH2 . ARG B 2 233 ? 22.755 17.336 28.736 1.00 53.19 ? 233 ARG B NH2 1 ATOM 2129 N N . ASP B 2 234 ? 25.274 24.598 33.581 1.00 40.01 ? 234 ASP B N 1 ATOM 2130 C CA . ASP B 2 234 ? 25.661 25.115 34.903 1.00 40.01 ? 234 ASP B CA 1 ATOM 2131 C C . ASP B 2 234 ? 26.207 24.016 35.804 1.00 39.32 ? 234 ASP B C 1 ATOM 2132 O O . ASP B 2 234 ? 25.667 22.913 35.833 1.00 38.59 ? 234 ASP B O 1 ATOM 2133 C CB . ASP B 2 234 ? 24.494 25.827 35.581 1.00 42.27 ? 234 ASP B CB 1 ATOM 2134 C CG . ASP B 2 234 ? 24.282 27.237 35.053 1.00 46.99 ? 234 ASP B CG 1 ATOM 2135 O OD1 . ASP B 2 234 ? 25.231 27.849 34.514 1.00 51.52 ? 234 ASP B OD1 1 ATOM 2136 O OD2 . ASP B 2 234 ? 23.158 27.748 35.177 1.00 51.51 ? 234 ASP B OD2 1 ATOM 2137 N N . GLY B 2 235 ? 27.301 24.323 36.509 1.00 38.99 ? 235 GLY B N 1 ATOM 2138 C CA . GLY B 2 235 ? 27.991 23.368 37.369 1.00 36.37 ? 235 GLY B CA 1 ATOM 2139 C C . GLY B 2 235 ? 28.722 22.289 36.599 1.00 38.72 ? 235 GLY B C 1 ATOM 2140 O O . GLY B 2 235 ? 29.161 21.298 37.177 1.00 40.81 ? 235 GLY B O 1 ATOM 2141 N N . LYS B 2 236 ? 28.857 22.476 35.288 1.00 39.71 ? 236 LYS B N 1 ATOM 2142 C CA . LYS B 2 236 ? 29.588 21.536 34.430 1.00 37.47 ? 236 LYS B CA 1 ATOM 2143 C C . LYS B 2 236 ? 30.800 22.216 33.747 1.00 35.20 ? 236 LYS B C 1 ATOM 2144 O O . LYS B 2 236 ? 30.812 23.446 33.557 1.00 32.05 ? 236 LYS B O 1 ATOM 2145 C CB . LYS B 2 236 ? 28.622 20.914 33.419 1.00 39.64 ? 236 LYS B CB 1 ATOM 2146 C CG . LYS B 2 236 ? 27.593 19.982 34.049 1.00 39.39 ? 236 LYS B CG 1 ATOM 2147 C CD . LYS B 2 236 ? 28.205 18.624 34.336 1.00 40.84 ? 236 LYS B CD 1 ATOM 2148 C CE . LYS B 2 236 ? 27.381 17.827 35.329 1.00 40.59 ? 236 LYS B CE 1 ATOM 2149 N NZ . LYS B 2 236 ? 27.889 16.424 35.358 1.00 40.57 ? 236 LYS B NZ 1 ATOM 2150 N N . TYR B 2 237 ? 31.831 21.432 33.424 1.00 33.85 ? 237 TYR B N 1 ATOM 2151 C CA . TYR B 2 237 ? 33.071 21.974 32.817 1.00 33.36 ? 237 TYR B CA 1 ATOM 2152 C C . TYR B 2 237 ? 33.551 21.101 31.681 1.00 31.65 ? 237 TYR B C 1 ATOM 2153 O O . TYR B 2 237 ? 33.398 19.874 31.724 1.00 32.69 ? 237 TYR B O 1 ATOM 2154 C CB . TYR B 2 237 ? 34.190 22.142 33.872 1.00 34.10 ? 237 TYR B CB 1 ATOM 2155 C CG . TYR B 2 237 ? 33.718 22.924 35.070 1.00 35.12 ? 237 TYR B CG 1 ATOM 2156 C CD1 . TYR B 2 237 ? 33.095 22.277 36.152 1.00 36.23 ? 237 TYR B CD1 1 ATOM 2157 C CD2 . TYR B 2 237 ? 33.819 24.307 35.101 1.00 34.07 ? 237 TYR B CD2 1 ATOM 2158 C CE1 . TYR B 2 237 ? 32.607 22.992 37.234 1.00 35.41 ? 237 TYR B CE1 1 ATOM 2159 C CE2 . TYR B 2 237 ? 33.343 25.030 36.187 1.00 36.16 ? 237 TYR B CE2 1 ATOM 2160 C CZ . TYR B 2 237 ? 32.739 24.364 37.251 1.00 36.67 ? 237 TYR B CZ 1 ATOM 2161 O OH . TYR B 2 237 ? 32.265 25.079 38.327 1.00 39.48 ? 237 TYR B OH 1 ATOM 2162 N N . GLY B 2 238 ? 34.124 21.720 30.655 1.00 29.91 ? 238 GLY B N 1 ATOM 2163 C CA . GLY B 2 238 ? 34.754 20.940 29.587 1.00 28.81 ? 238 GLY B CA 1 ATOM 2164 C C . GLY B 2 238 ? 36.088 20.396 30.065 1.00 28.68 ? 238 GLY B C 1 ATOM 2165 O O . GLY B 2 238 ? 36.746 20.997 30.903 1.00 28.80 ? 238 GLY B O 1 ATOM 2166 N N . PHE B 2 239 ? 36.482 19.251 29.532 1.00 29.34 ? 239 PHE B N 1 ATOM 2167 C CA . PHE B 2 239 ? 37.741 18.615 29.879 1.00 28.41 ? 239 PHE B CA 1 ATOM 2168 C C . PHE B 2 239 ? 38.676 18.558 28.682 1.00 28.38 ? 239 PHE B C 1 ATOM 2169 O O . PHE B 2 239 ? 38.250 18.406 27.531 1.00 29.80 ? 239 PHE B O 1 ATOM 2170 C CB . PHE B 2 239 ? 37.479 17.216 30.423 1.00 30.67 ? 239 PHE B CB 1 ATOM 2171 C CG . PHE B 2 239 ? 36.965 17.217 31.827 1.00 34.48 ? 239 PHE B CG 1 ATOM 2172 C CD1 . PHE B 2 239 ? 35.620 17.493 32.095 1.00 36.26 ? 239 PHE B CD1 1 ATOM 2173 C CD2 . PHE B 2 239 ? 37.830 16.986 32.896 1.00 33.91 ? 239 PHE B CD2 1 ATOM 2174 C CE1 . PHE B 2 239 ? 35.148 17.524 33.404 1.00 36.98 ? 239 PHE B CE1 1 ATOM 2175 C CE2 . PHE B 2 239 ? 37.357 17.015 34.203 1.00 36.23 ? 239 PHE B CE2 1 ATOM 2176 C CZ . PHE B 2 239 ? 36.018 17.284 34.456 1.00 35.82 ? 239 PHE B CZ 1 ATOM 2177 N N . TYR B 2 240 ? 39.964 18.677 28.964 1.00 27.43 ? 240 TYR B N 1 ATOM 2178 C CA . TYR B 2 240 ? 40.964 18.865 27.932 1.00 25.23 ? 240 TYR B CA 1 ATOM 2179 C C . TYR B 2 240 ? 42.124 17.923 28.184 1.00 26.06 ? 240 TYR B C 1 ATOM 2180 O O . TYR B 2 240 ? 42.561 17.762 29.327 1.00 27.16 ? 240 TYR B O 1 ATOM 2181 C CB . TYR B 2 240 ? 41.432 20.330 27.934 1.00 24.02 ? 240 TYR B CB 1 ATOM 2182 C CG . TYR B 2 240 ? 40.304 21.309 27.635 1.00 23.82 ? 240 TYR B CG 1 ATOM 2183 C CD1 . TYR B 2 240 ? 39.431 21.734 28.639 1.00 23.33 ? 240 TYR B CD1 1 ATOM 2184 C CD2 . TYR B 2 240 ? 40.095 21.784 26.338 1.00 23.93 ? 240 TYR B CD2 1 ATOM 2185 C CE1 . TYR B 2 240 ? 38.395 22.611 28.364 1.00 24.47 ? 240 TYR B CE1 1 ATOM 2186 C CE2 . TYR B 2 240 ? 39.065 22.666 26.050 1.00 24.19 ? 240 TYR B CE2 1 ATOM 2187 C CZ . TYR B 2 240 ? 38.213 23.070 27.066 1.00 25.36 ? 240 TYR B CZ 1 ATOM 2188 O OH . TYR B 2 240 ? 37.181 23.933 26.780 1.00 26.24 ? 240 TYR B OH 1 ATOM 2189 N N . THR B 2 241 ? 42.606 17.277 27.130 1.00 25.64 ? 241 THR B N 1 ATOM 2190 C CA . THR B 2 241 ? 43.859 16.556 27.202 1.00 26.34 ? 241 THR B CA 1 ATOM 2191 C C . THR B 2 241 ? 44.996 17.492 27.618 1.00 27.23 ? 241 THR B C 1 ATOM 2192 O O . THR B 2 241 ? 45.142 18.598 27.077 1.00 26.16 ? 241 THR B O 1 ATOM 2193 C CB . THR B 2 241 ? 44.209 15.967 25.845 1.00 26.99 ? 241 THR B CB 1 ATOM 2194 O OG1 . THR B 2 241 ? 43.069 15.269 25.342 1.00 27.08 ? 241 THR B OG1 1 ATOM 2195 C CG2 . THR B 2 241 ? 45.396 15.028 25.975 1.00 26.82 ? 241 THR B CG2 1 ATOM 2196 N N . HIS B 2 242 ? 45.784 17.038 28.595 1.00 28.16 ? 242 HIS B N 1 ATOM 2197 C CA . HIS B 2 242 ? 46.916 17.790 29.142 1.00 26.57 ? 242 HIS B CA 1 ATOM 2198 C C . HIS B 2 242 ? 48.146 17.636 28.229 1.00 25.64 ? 242 HIS B C 1 ATOM 2199 O O . HIS B 2 242 ? 48.923 16.688 28.373 1.00 24.88 ? 242 HIS B O 1 ATOM 2200 C CB . HIS B 2 242 ? 47.222 17.252 30.531 1.00 26.37 ? 242 HIS B CB 1 ATOM 2201 C CG . HIS B 2 242 ? 48.063 18.161 31.362 1.00 28.27 ? 242 HIS B CG 1 ATOM 2202 N ND1 . HIS B 2 242 ? 49.247 18.710 30.909 1.00 29.49 ? 242 HIS B ND1 1 ATOM 2203 C CD2 . HIS B 2 242 ? 47.905 18.601 32.630 1.00 28.19 ? 242 HIS B CD2 1 ATOM 2204 C CE1 . HIS B 2 242 ? 49.779 19.450 31.862 1.00 28.73 ? 242 HIS B CE1 1 ATOM 2205 N NE2 . HIS B 2 242 ? 48.984 19.402 32.917 1.00 29.52 ? 242 HIS B NE2 1 ATOM 2206 N N . VAL B 2 243 ? 48.327 18.559 27.291 1.00 24.64 ? 243 VAL B N 1 ATOM 2207 C CA . VAL B 2 243 ? 49.332 18.360 26.242 1.00 25.44 ? 243 VAL B CA 1 ATOM 2208 C C . VAL B 2 243 ? 50.744 18.130 26.796 1.00 27.32 ? 243 VAL B C 1 ATOM 2209 O O . VAL B 2 243 ? 51.428 17.209 26.370 1.00 27.72 ? 243 VAL B O 1 ATOM 2210 C CB . VAL B 2 243 ? 49.314 19.479 25.182 1.00 24.66 ? 243 VAL B CB 1 ATOM 2211 C CG1 . VAL B 2 243 ? 50.516 19.376 24.246 1.00 23.10 ? 243 VAL B CG1 1 ATOM 2212 C CG2 . VAL B 2 243 ? 48.009 19.416 24.398 1.00 24.86 ? 243 VAL B CG2 1 ATOM 2213 N N . PHE B 2 244 ? 51.165 18.945 27.761 1.00 28.58 ? 244 PHE B N 1 ATOM 2214 C CA . PHE B 2 244 ? 52.495 18.789 28.315 1.00 29.27 ? 244 PHE B CA 1 ATOM 2215 C C . PHE B 2 244 ? 52.781 17.397 28.924 1.00 31.38 ? 244 PHE B C 1 ATOM 2216 O O . PHE B 2 244 ? 53.845 16.833 28.666 1.00 30.86 ? 244 PHE B O 1 ATOM 2217 C CB . PHE B 2 244 ? 52.840 19.901 29.309 1.00 28.20 ? 244 PHE B CB 1 ATOM 2218 C CG . PHE B 2 244 ? 54.202 19.739 29.894 1.00 28.75 ? 244 PHE B CG 1 ATOM 2219 C CD1 . PHE B 2 244 ? 55.335 20.021 29.130 1.00 28.58 ? 244 PHE B CD1 1 ATOM 2220 C CD2 . PHE B 2 244 ? 54.368 19.216 31.178 1.00 29.54 ? 244 PHE B CD2 1 ATOM 2221 C CE1 . PHE B 2 244 ? 56.614 19.826 29.649 1.00 28.03 ? 244 PHE B CE1 1 ATOM 2222 C CE2 . PHE B 2 244 ? 55.643 19.014 31.702 1.00 29.22 ? 244 PHE B CE2 1 ATOM 2223 C CZ . PHE B 2 244 ? 56.767 19.324 30.935 1.00 28.12 ? 244 PHE B CZ 1 ATOM 2224 N N . ARG B 2 245 ? 51.851 16.856 29.725 1.00 32.16 ? 245 ARG B N 1 ATOM 2225 C CA . ARG B 2 245 ? 52.032 15.535 30.338 1.00 33.33 ? 245 ARG B CA 1 ATOM 2226 C C . ARG B 2 245 ? 52.245 14.428 29.296 1.00 32.96 ? 245 ARG B C 1 ATOM 2227 O O . ARG B 2 245 ? 52.742 13.353 29.626 1.00 35.61 ? 245 ARG B O 1 ATOM 2228 C CB . ARG B 2 245 ? 50.847 15.165 31.231 1.00 35.88 ? 245 ARG B CB 1 ATOM 2229 C CG . ARG B 2 245 ? 50.729 15.937 32.541 1.00 44.08 ? 245 ARG B CG 1 ATOM 2230 C CD . ARG B 2 245 ? 51.209 15.144 33.761 1.00 47.24 ? 245 ARG B CD 1 ATOM 2231 N NE . ARG B 2 245 ? 50.723 13.756 33.752 1.00 51.51 ? 245 ARG B NE 1 ATOM 2232 C CZ . ARG B 2 245 ? 50.828 12.894 34.771 1.00 52.15 ? 245 ARG B CZ 1 ATOM 2233 N NH1 . ARG B 2 245 ? 51.390 13.269 35.918 1.00 50.82 ? 245 ARG B NH1 1 ATOM 2234 N NH2 . ARG B 2 245 ? 50.360 11.652 34.649 1.00 48.22 ? 245 ARG B NH2 1 ATOM 2235 N N . LEU B 2 246 ? 51.880 14.688 28.044 1.00 31.18 ? 246 LEU B N 1 ATOM 2236 C CA . LEU B 2 246 ? 51.977 13.681 26.988 1.00 29.30 ? 246 LEU B CA 1 ATOM 2237 C C . LEU B 2 246 ? 53.009 14.038 25.936 1.00 28.49 ? 246 LEU B C 1 ATOM 2238 O O . LEU B 2 246 ? 53.140 13.352 24.913 1.00 28.00 ? 246 LEU B O 1 ATOM 2239 C CB . LEU B 2 246 ? 50.608 13.455 26.353 1.00 29.93 ? 246 LEU B CB 1 ATOM 2240 C CG . LEU B 2 246 ? 49.663 12.693 27.283 1.00 30.92 ? 246 LEU B CG 1 ATOM 2241 C CD1 . LEU B 2 246 ? 48.209 13.035 27.030 1.00 29.76 ? 246 LEU B CD1 1 ATOM 2242 C CD2 . LEU B 2 246 ? 49.900 11.195 27.138 1.00 31.37 ? 246 LEU B CD2 1 ATOM 2243 N N . LYS B 2 247 ? 53.776 15.090 26.211 1.00 27.84 ? 247 LYS B N 1 ATOM 2244 C CA . LYS B 2 247 ? 54.784 15.558 25.278 1.00 29.63 ? 247 LYS B CA 1 ATOM 2245 C C . LYS B 2 247 ? 55.841 14.498 24.955 1.00 29.00 ? 247 LYS B C 1 ATOM 2246 O O . LYS B 2 247 ? 56.356 14.480 23.834 1.00 29.47 ? 247 LYS B O 1 ATOM 2247 C CB . LYS B 2 247 ? 55.438 16.850 25.776 1.00 33.63 ? 247 LYS B CB 1 ATOM 2248 C CG . LYS B 2 247 ? 56.172 17.621 24.692 1.00 37.24 ? 247 LYS B CG 1 ATOM 2249 C CD . LYS B 2 247 ? 56.451 19.054 25.103 1.00 39.80 ? 247 LYS B CD 1 ATOM 2250 C CE . LYS B 2 247 ? 57.921 19.289 25.403 1.00 41.98 ? 247 LYS B CE 1 ATOM 2251 N NZ . LYS B 2 247 ? 58.301 18.895 26.781 1.00 49.18 ? 247 LYS B NZ 1 ATOM 2252 N N . LYS B 2 248 ? 56.159 13.620 25.909 1.00 28.15 ? 248 LYS B N 1 ATOM 2253 C CA . LYS B 2 248 ? 57.189 12.589 25.672 1.00 29.90 ? 248 LYS B CA 1 ATOM 2254 C C . LYS B 2 248 ? 56.779 11.594 24.593 1.00 29.75 ? 248 LYS B C 1 ATOM 2255 O O . LYS B 2 248 ? 57.613 11.206 23.755 1.00 30.10 ? 248 LYS B O 1 ATOM 2256 C CB . LYS B 2 248 ? 57.647 11.859 26.956 1.00 30.45 ? 248 LYS B CB 1 ATOM 2257 C CG . LYS B 2 248 ? 58.445 12.710 27.933 1.00 31.53 ? 248 LYS B CG 1 ATOM 2258 C CD . LYS B 2 248 ? 59.768 13.187 27.351 1.00 34.00 ? 248 LYS B CD 1 ATOM 2259 C CE . LYS B 2 248 ? 60.347 14.302 28.203 1.00 37.70 ? 248 LYS B CE 1 ATOM 2260 N NZ . LYS B 2 248 ? 61.636 14.741 27.600 1.00 45.61 ? 248 LYS B NZ 1 ATOM 2261 N N . TRP B 2 249 ? 55.503 11.201 24.603 1.00 29.20 ? 249 TRP B N 1 ATOM 2262 C CA . TRP B 2 249 ? 54.937 10.421 23.508 1.00 29.70 ? 249 TRP B CA 1 ATOM 2263 C C . TRP B 2 249 ? 55.055 11.138 22.136 1.00 30.42 ? 249 TRP B C 1 ATOM 2264 O O . TRP B 2 249 ? 55.520 10.547 21.153 1.00 29.50 ? 249 TRP B O 1 ATOM 2265 C CB . TRP B 2 249 ? 53.482 10.030 23.798 1.00 30.94 ? 249 TRP B CB 1 ATOM 2266 C CG . TRP B 2 249 ? 52.897 9.213 22.666 1.00 33.47 ? 249 TRP B CG 1 ATOM 2267 C CD1 . TRP B 2 249 ? 53.201 7.927 22.356 1.00 32.36 ? 249 TRP B CD1 1 ATOM 2268 C CD2 . TRP B 2 249 ? 51.944 9.649 21.677 1.00 34.09 ? 249 TRP B CD2 1 ATOM 2269 N NE1 . TRP B 2 249 ? 52.501 7.523 21.248 1.00 33.38 ? 249 TRP B NE1 1 ATOM 2270 C CE2 . TRP B 2 249 ? 51.714 8.554 20.811 1.00 34.76 ? 249 TRP B CE2 1 ATOM 2271 C CE3 . TRP B 2 249 ? 51.261 10.854 21.443 1.00 33.21 ? 249 TRP B CE3 1 ATOM 2272 C CZ2 . TRP B 2 249 ? 50.825 8.623 19.715 1.00 35.36 ? 249 TRP B CZ2 1 ATOM 2273 C CZ3 . TRP B 2 249 ? 50.375 10.926 20.355 1.00 33.82 ? 249 TRP B CZ3 1 ATOM 2274 C CH2 . TRP B 2 249 ? 50.169 9.813 19.505 1.00 34.64 ? 249 TRP B CH2 1 ATOM 2275 N N . ILE B 2 250 ? 54.644 12.409 22.079 1.00 30.35 ? 250 ILE B N 1 ATOM 2276 C CA . ILE B 2 250 ? 54.695 13.192 20.833 1.00 30.42 ? 250 ILE B CA 1 ATOM 2277 C C . ILE B 2 250 ? 56.124 13.155 20.299 1.00 31.94 ? 250 ILE B C 1 ATOM 2278 O O . ILE B 2 250 ? 56.381 12.966 19.096 1.00 32.63 ? 250 ILE B O 1 ATOM 2279 C CB . ILE B 2 250 ? 54.234 14.668 21.061 1.00 28.28 ? 250 ILE B CB 1 ATOM 2280 C CG1 . ILE B 2 250 ? 52.734 14.743 21.334 1.00 26.55 ? 250 ILE B CG1 1 ATOM 2281 C CG2 . ILE B 2 250 ? 54.584 15.577 19.885 1.00 26.57 ? 250 ILE B CG2 1 ATOM 2282 C CD1 . ILE B 2 250 ? 52.349 15.987 22.104 1.00 26.24 ? 250 ILE B CD1 1 ATOM 2283 N N . GLN B 2 251 ? 57.048 13.311 21.229 1.00 32.90 ? 251 GLN B N 1 ATOM 2284 C CA . GLN B 2 251 ? 58.445 13.409 20.926 1.00 35.86 ? 251 GLN B CA 1 ATOM 2285 C C . GLN B 2 251 ? 58.964 12.104 20.339 1.00 35.88 ? 251 GLN B C 1 ATOM 2286 O O . GLN B 2 251 ? 59.696 12.113 19.357 1.00 35.79 ? 251 GLN B O 1 ATOM 2287 C CB . GLN B 2 251 ? 59.157 13.726 22.212 1.00 39.10 ? 251 GLN B CB 1 ATOM 2288 C CG . GLN B 2 251 ? 60.575 14.181 22.039 1.00 43.53 ? 251 GLN B CG 1 ATOM 2289 C CD . GLN B 2 251 ? 61.182 14.493 23.374 1.00 45.58 ? 251 GLN B CD 1 ATOM 2290 O OE1 . GLN B 2 251 ? 62.212 13.909 23.738 1.00 47.04 ? 251 GLN B OE1 1 ATOM 2291 N NE2 . GLN B 2 251 ? 60.521 15.386 24.144 1.00 42.37 ? 251 GLN B NE2 1 ATOM 2292 N N . LYS B 2 252 ? 58.558 10.986 20.935 1.00 36.37 ? 252 LYS B N 1 ATOM 2293 C CA . LYS B 2 252 ? 58.899 9.671 20.424 1.00 36.13 ? 252 LYS B CA 1 ATOM 2294 C C . LYS B 2 252 ? 58.412 9.473 18.992 1.00 36.19 ? 252 LYS B C 1 ATOM 2295 O O . LYS B 2 252 ? 59.174 9.010 18.135 1.00 35.21 ? 252 LYS B O 1 ATOM 2296 C CB . LYS B 2 252 ? 58.325 8.597 21.333 1.00 37.60 ? 252 LYS B CB 1 ATOM 2297 C CG . LYS B 2 252 ? 58.563 7.193 20.840 1.00 42.11 ? 252 LYS B CG 1 ATOM 2298 C CD . LYS B 2 252 ? 58.525 6.214 21.996 1.00 49.64 ? 252 LYS B CD 1 ATOM 2299 C CE . LYS B 2 252 ? 58.375 4.776 21.507 1.00 56.01 ? 252 LYS B CE 1 ATOM 2300 N NZ . LYS B 2 252 ? 56.940 4.480 21.239 1.00 56.59 ? 252 LYS B NZ 1 ATOM 2301 N N . VAL B 2 253 ? 57.149 9.837 18.742 1.00 37.15 ? 253 VAL B N 1 ATOM 2302 C CA . VAL B 2 253 ? 56.502 9.585 17.444 1.00 37.25 ? 253 VAL B CA 1 ATOM 2303 C C . VAL B 2 253 ? 57.128 10.417 16.323 1.00 38.15 ? 253 VAL B C 1 ATOM 2304 O O . VAL B 2 253 ? 57.479 9.882 15.263 1.00 37.20 ? 253 VAL B O 1 ATOM 2305 C CB . VAL B 2 253 ? 54.961 9.742 17.498 1.00 35.85 ? 253 VAL B CB 1 ATOM 2306 C CG1 . VAL B 2 253 ? 54.353 9.727 16.100 1.00 32.92 ? 253 VAL B CG1 1 ATOM 2307 C CG2 . VAL B 2 253 ? 54.350 8.637 18.347 1.00 33.83 ? 253 VAL B CG2 1 ATOM 2308 N N . ILE B 2 254 ? 57.290 11.709 16.574 1.00 38.46 ? 254 ILE B N 1 ATOM 2309 C CA . ILE B 2 254 ? 57.941 12.597 15.616 1.00 42.72 ? 254 ILE B CA 1 ATOM 2310 C C . ILE B 2 254 ? 59.396 12.202 15.321 1.00 46.61 ? 254 ILE B C 1 ATOM 2311 O O . ILE B 2 254 ? 59.821 12.254 14.174 1.00 48.76 ? 254 ILE B O 1 ATOM 2312 C CB . ILE B 2 254 ? 57.782 14.076 16.041 1.00 41.21 ? 254 ILE B CB 1 ATOM 2313 C CG1 . ILE B 2 254 ? 56.373 14.544 15.668 1.00 42.24 ? 254 ILE B CG1 1 ATOM 2314 C CG2 . ILE B 2 254 ? 58.822 14.978 15.393 1.00 37.86 ? 254 ILE B CG2 1 ATOM 2315 C CD1 . ILE B 2 254 ? 55.947 15.840 16.330 1.00 43.03 ? 254 ILE B CD1 1 ATOM 2316 N N . ASP B 2 255 ? 60.142 11.787 16.342 1.00 53.60 ? 255 ASP B N 1 ATOM 2317 C CA . ASP B 2 255 ? 61.561 11.454 16.175 1.00 61.94 ? 255 ASP B CA 1 ATOM 2318 C C . ASP B 2 255 ? 61.777 10.177 15.373 1.00 62.94 ? 255 ASP B C 1 ATOM 2319 O O . ASP B 2 255 ? 62.636 10.125 14.499 1.00 61.22 ? 255 ASP B O 1 ATOM 2320 C CB . ASP B 2 255 ? 62.251 11.313 17.538 1.00 69.47 ? 255 ASP B CB 1 ATOM 2321 C CG . ASP B 2 255 ? 63.699 10.856 17.416 1.00 70.61 ? 255 ASP B CG 1 ATOM 2322 O OD1 . ASP B 2 255 ? 64.566 11.698 17.086 1.00 68.98 ? 255 ASP B OD1 1 ATOM 2323 O OD2 . ASP B 2 255 ? 63.958 9.652 17.641 1.00 72.35 ? 255 ASP B OD2 1 ATOM 2324 N N . GLN B 2 256 ? 61.005 9.148 15.695 1.00 69.17 ? 256 GLN B N 1 ATOM 2325 C CA . GLN B 2 256 ? 61.098 7.861 15.010 1.00 81.43 ? 256 GLN B CA 1 ATOM 2326 C C . GLN B 2 256 ? 60.525 7.857 13.589 1.00 82.71 ? 256 GLN B C 1 ATOM 2327 O O . GLN B 2 256 ? 60.941 7.043 12.764 1.00 83.33 ? 256 GLN B O 1 ATOM 2328 C CB . GLN B 2 256 ? 60.398 6.775 15.826 1.00 89.78 ? 256 GLN B CB 1 ATOM 2329 C CG . GLN B 2 256 ? 61.151 6.332 17.071 1.00 100.81 ? 256 GLN B CG 1 ATOM 2330 C CD . GLN B 2 256 ? 60.582 5.053 17.655 1.00 108.61 ? 256 GLN B CD 1 ATOM 2331 O OE1 . GLN B 2 256 ? 59.724 4.404 17.045 1.00 111.11 ? 256 GLN B OE1 1 ATOM 2332 N NE2 . GLN B 2 256 ? 61.056 4.680 18.842 1.00 106.51 ? 256 GLN B NE2 1 ATOM 2333 N N . PHE B 2 257 ? 59.577 8.753 13.305 1.00 83.37 ? 257 PHE B N 1 ATOM 2334 C CA . PHE B 2 257 ? 58.842 8.726 12.031 1.00 78.80 ? 257 PHE B CA 1 ATOM 2335 C C . PHE B 2 257 ? 58.918 10.014 11.191 1.00 77.57 ? 257 PHE B C 1 ATOM 2336 O O . PHE B 2 257 ? 58.179 10.172 10.219 1.00 75.53 ? 257 PHE B O 1 ATOM 2337 C CB . PHE B 2 257 ? 57.383 8.304 12.267 1.00 76.48 ? 257 PHE B CB 1 ATOM 2338 C CG . PHE B 2 257 ? 57.232 6.923 12.865 1.00 83.30 ? 257 PHE B CG 1 ATOM 2339 C CD1 . PHE B 2 257 ? 57.326 5.779 12.062 1.00 82.54 ? 257 PHE B CD1 1 ATOM 2340 C CD2 . PHE B 2 257 ? 56.979 6.760 14.233 1.00 84.81 ? 257 PHE B CD2 1 ATOM 2341 C CE1 . PHE B 2 257 ? 57.178 4.508 12.613 1.00 85.69 ? 257 PHE B CE1 1 ATOM 2342 C CE2 . PHE B 2 257 ? 56.830 5.489 14.790 1.00 85.16 ? 257 PHE B CE2 1 ATOM 2343 C CZ . PHE B 2 257 ? 56.930 4.363 13.979 1.00 86.86 ? 257 PHE B CZ 1 ATOM 2344 O OXT . PHE B 2 257 ? 59.717 10.930 11.421 1.00 74.21 ? 257 PHE B OXT 1 ATOM 2345 N N . ASP C 3 1 ? 25.759 21.227 2.962 0.010 51.41 ? 1 ASP D N 1 ATOM 2346 C CA . ASP C 3 1 ? 25.859 22.687 2.654 1.00 50.06 ? 1 ASP D CA 1 ATOM 2347 C C . ASP C 3 1 ? 27.300 23.145 2.353 1.00 42.61 ? 1 ASP D C 1 ATOM 2348 O O . ASP C 3 1 ? 27.582 24.335 2.238 1.00 41.79 ? 1 ASP D O 1 ATOM 2349 C CB . ASP C 3 1 ? 25.202 23.537 3.755 1.00 60.39 ? 1 ASP D CB 1 ATOM 2350 C CG . ASP C 3 1 ? 25.567 23.072 5.172 1.00 72.85 ? 1 ASP D CG 1 ATOM 2351 O OD1 . ASP C 3 1 ? 25.651 21.844 5.426 1.00 80.80 ? 1 ASP D OD1 1 ATOM 2352 O OD2 . ASP C 3 1 ? 25.754 23.949 6.045 1.00 75.27 ? 1 ASP D OD2 1 ATOM 2353 N N . PHE C 3 2 ? 28.197 22.187 2.187 1.00 36.02 ? 2 PHE D N 1 ATOM 2354 C CA . PHE C 3 2 ? 29.576 22.487 1.849 1.00 34.72 ? 2 PHE D CA 1 ATOM 2355 C C . PHE C 3 2 ? 29.704 22.801 0.373 1.00 32.83 ? 2 PHE D C 1 ATOM 2356 O O . PHE C 3 2 ? 29.119 22.111 -0.441 1.00 33.33 ? 2 PHE D O 1 ATOM 2357 C CB . PHE C 3 2 ? 30.483 21.315 2.243 1.00 34.18 ? 2 PHE D CB 1 ATOM 2358 C CG . PHE C 3 2 ? 30.644 21.165 3.730 1.00 35.46 ? 2 PHE D CG 1 ATOM 2359 C CD1 . PHE C 3 2 ? 29.738 20.413 4.471 1.00 36.34 ? 2 PHE D CD1 1 ATOM 2360 C CD2 . PHE C 3 2 ? 31.685 21.816 4.401 1.00 34.99 ? 2 PHE D CD2 1 ATOM 2361 C CE1 . PHE C 3 2 ? 29.873 20.304 5.852 1.00 38.79 ? 2 PHE D CE1 1 ATOM 2362 C CE2 . PHE C 3 2 ? 31.828 21.700 5.773 1.00 35.57 ? 2 PHE D CE2 1 ATOM 2363 C CZ . PHE C 3 2 ? 30.919 20.947 6.503 1.00 36.74 ? 2 PHE D CZ 1 ATOM 2364 N N . GLU C 3 3 ? 30.422 23.870 0.029 1.00 31.73 ? 3 GLU D N 1 ATOM 2365 C CA . GLU C 3 3 ? 30.785 24.128 -1.362 1.00 30.65 ? 3 GLU D CA 1 ATOM 2366 C C . GLU C 3 3 ? 31.635 22.951 -1.851 1.00 33.76 ? 3 GLU D C 1 ATOM 2367 O O . GLU C 3 3 ? 32.345 22.332 -1.067 1.00 34.46 ? 3 GLU D O 1 ATOM 2368 C CB . GLU C 3 3 ? 31.547 25.438 -1.487 1.00 27.65 ? 3 GLU D CB 1 ATOM 2369 C CG . GLU C 3 3 ? 30.672 26.675 -1.505 1.00 27.14 ? 3 GLU D CG 1 ATOM 2370 C CD . GLU C 3 3 ? 31.478 27.952 -1.698 1.00 28.81 ? 3 GLU D CD 1 ATOM 2371 O OE1 . GLU C 3 3 ? 32.724 27.889 -1.752 1.00 28.60 ? 3 GLU D OE1 1 ATOM 2372 O OE2 . GLU C 3 3 ? 30.877 29.043 -1.796 1.00 30.43 ? 3 GLU D OE2 1 ATOM 2373 N N . GLU C 3 4 ? 31.557 22.595 -3.124 1.00 38.72 ? 4 GLU D N 1 ATOM 2374 C CA . GLU C 3 4 ? 32.354 21.444 -3.527 1.00 42.62 ? 4 GLU D CA 1 ATOM 2375 C C . GLU C 3 4 ? 33.823 21.780 -3.760 1.00 38.72 ? 4 GLU D C 1 ATOM 2376 O O . GLU C 3 4 ? 34.181 22.885 -4.162 1.00 40.60 ? 4 GLU D O 1 ATOM 2377 C CB . GLU C 3 4 ? 31.721 20.629 -4.661 1.00 48.96 ? 4 GLU D CB 1 ATOM 2378 C CG . GLU C 3 4 ? 31.522 21.346 -5.978 1.00 58.38 ? 4 GLU D CG 1 ATOM 2379 C CD . GLU C 3 4 ? 31.099 20.382 -7.078 1.00 71.75 ? 4 GLU D CD 1 ATOM 2380 O OE1 . GLU C 3 4 ? 30.860 19.185 -6.772 1.00 74.81 ? 4 GLU D OE1 1 ATOM 2381 O OE2 . GLU C 3 4 ? 31.017 20.816 -8.249 1.00 74.32 ? 4 GLU D OE2 1 ATOM 2382 N N . ILE C 3 5 ? 34.661 20.811 -3.439 1.00 37.56 ? 5 ILE D N 1 ATOM 2383 C CA . ILE C 3 5 ? 36.095 20.930 -3.545 1.00 37.73 ? 5 ILE D CA 1 ATOM 2384 C C . ILE C 3 5 ? 36.494 20.097 -4.764 1.00 39.08 ? 5 ILE D C 1 ATOM 2385 O O . ILE C 3 5 ? 35.720 19.228 -5.180 1.00 40.85 ? 5 ILE D O 1 ATOM 2386 C CB . ILE C 3 5 ? 36.781 20.449 -2.244 1.00 36.46 ? 5 ILE D CB 1 ATOM 2387 C CG1 . ILE C 3 5 ? 36.278 19.069 -1.835 1.00 36.46 ? 5 ILE D CG1 1 ATOM 2388 C CG2 . ILE C 3 5 ? 36.487 21.409 -1.103 1.00 35.78 ? 5 ILE D CG2 1 ATOM 2389 C CD1 . ILE C 3 5 ? 37.303 18.260 -1.077 1.00 39.21 ? 5 ILE D CD1 1 ATOM 2390 N N . PRO C 3 6 ? 37.681 20.361 -5.358 1.00 39.96 ? 6 PRO D N 1 ATOM 2391 C CA . PRO C 3 6 ? 38.096 19.580 -6.535 1.00 39.56 ? 6 PRO D CA 1 ATOM 2392 C C . PRO C 3 6 ? 37.952 18.072 -6.303 1.00 40.70 ? 6 PRO D C 1 ATOM 2393 O O . PRO C 3 6 ? 38.278 17.583 -5.221 1.00 40.19 ? 6 PRO D O 1 ATOM 2394 C CB . PRO C 3 6 ? 39.567 19.971 -6.700 1.00 40.00 ? 6 PRO D CB 1 ATOM 2395 C CG . PRO C 3 6 ? 39.629 21.367 -6.172 1.00 39.65 ? 6 PRO D CG 1 ATOM 2396 C CD . PRO C 3 6 ? 38.705 21.357 -4.980 1.00 39.44 ? 6 PRO D CD 1 ATOM 2397 N N . GLU C 3 7 ? 37.457 17.346 -7.306 1.00 45.57 ? 7 GLU D N 1 ATOM 2398 C CA . GLU C 3 7 ? 37.125 15.915 -7.154 1.00 47.22 ? 7 GLU D CA 1 ATOM 2399 C C . GLU C 3 7 ? 38.346 14.992 -7.025 1.00 47.92 ? 7 GLU D C 1 ATOM 2400 O O . GLU C 3 7 ? 38.225 13.841 -6.574 1.00 47.54 ? 7 GLU D O 1 ATOM 2401 C CB . GLU C 3 7 ? 36.203 15.426 -8.275 1.00 49.89 ? 7 GLU D CB 1 ATOM 2402 C CG . GLU C 3 7 ? 35.065 16.369 -8.624 1.00 54.39 ? 7 GLU D CG 1 ATOM 2403 C CD . GLU C 3 7 ? 35.320 17.153 -9.907 1.00 58.75 ? 7 GLU D CD 1 ATOM 2404 O OE1 . GLU C 3 7 ? 36.476 17.533 -10.208 1.00 59.91 ? 7 GLU D OE1 1 ATOM 2405 O OE2 . GLU C 3 7 ? 34.340 17.383 -10.638 1.00 66.23 ? 7 GLU D OE2 1 ATOM 2406 N N . GLU C 3 8 ? 39.515 15.501 -7.409 1.00 47.28 ? 8 GLU D N 1 ATOM 2407 C CA . GLU C 3 8 ? 40.784 14.793 -7.229 1.00 49.19 ? 8 GLU D CA 1 ATOM 2408 C C . GLU C 3 8 ? 40.980 14.381 -5.768 1.00 49.63 ? 8 GLU D C 1 ATOM 2409 O O . GLU C 3 8 ? 41.482 13.292 -5.496 1.00 50.06 ? 8 GLU D O 1 ATOM 2410 C CB . GLU C 3 8 ? 41.959 15.669 -7.688 1.00 53.37 ? 8 GLU D CB 1 ATOM 2411 C CG . GLU C 3 8 ? 42.052 15.907 -9.193 1.00 60.92 ? 8 GLU D CG 1 ATOM 2412 C CD . GLU C 3 8 ? 40.870 16.679 -9.801 1.00 66.32 ? 8 GLU D CD 1 ATOM 2413 O OE1 . GLU C 3 8 ? 40.259 17.558 -9.137 1.00 64.25 ? 8 GLU D OE1 1 ATOM 2414 O OE2 . GLU C 3 8 ? 40.550 16.403 -10.979 1.00 69.22 ? 8 GLU D OE2 1 ATOM 2415 N N . TYR C 3 9 ? 40.566 15.247 -4.837 1.00 47.10 ? 9 TYR D N 1 ATOM 2416 C CA . TYR C 3 9 ? 40.728 14.995 -3.408 1.00 45.72 ? 9 TYR D CA 1 ATOM 2417 C C . TYR C 3 9 ? 39.722 14.005 -2.847 1.00 46.19 ? 9 TYR D C 1 ATOM 2418 O O . TYR C 3 9 ? 39.903 13.510 -1.739 1.00 46.67 ? 9 TYR D O 1 ATOM 2419 C CB . TYR C 3 9 ? 40.627 16.292 -2.598 1.00 46.28 ? 9 TYR D CB 1 ATOM 2420 C CG . TYR C 3 9 ? 41.673 17.335 -2.898 1.00 43.21 ? 9 TYR D CG 1 ATOM 2421 C CD1 . TYR C 3 9 ? 43.010 17.149 -2.527 1.00 43.14 ? 9 TYR D CD1 1 ATOM 2422 C CD2 . TYR C 3 9 ? 41.323 18.512 -3.551 1.00 43.66 ? 9 TYR D CD2 1 ATOM 2423 C CE1 . TYR C 3 9 ? 43.968 18.117 -2.804 1.00 42.83 ? 9 TYR D CE1 1 ATOM 2424 C CE2 . TYR C 3 9 ? 42.267 19.481 -3.837 1.00 44.18 ? 9 TYR D CE2 1 ATOM 2425 C CZ . TYR C 3 9 ? 43.584 19.278 -3.461 1.00 42.97 ? 9 TYR D CZ 1 ATOM 2426 O OH . TYR C 3 9 ? 44.496 20.252 -3.748 1.00 43.05 ? 9 TYR D OH 1 ATOM 2427 N N . LEU C 3 10 ? 38.672 13.716 -3.609 1.00 48.90 ? 10 LEU D N 1 ATOM 2428 C CA . LEU C 3 10 ? 37.531 12.939 -3.113 1.00 49.22 ? 10 LEU D CA 1 ATOM 2429 C C . LEU C 3 10 ? 37.285 11.589 -3.807 1.00 52.29 ? 10 LEU D C 1 ATOM 2430 O O . LEU C 3 10 ? 36.368 10.852 -3.421 1.00 49.98 ? 10 LEU D O 1 ATOM 2431 C CB . LEU C 3 10 ? 36.253 13.778 -3.249 1.00 46.11 ? 10 LEU D CB 1 ATOM 2432 C CG . LEU C 3 10 ? 35.916 14.885 -2.269 1.00 44.74 ? 10 LEU D CG 1 ATOM 2433 C CD1 . LEU C 3 10 ? 34.785 15.716 -2.851 1.00 42.85 ? 10 LEU D CD1 1 ATOM 2434 C CD2 . LEU C 3 10 ? 35.531 14.283 -0.922 1.00 45.39 ? 10 LEU D CD2 1 ATOM 2435 N N . GLN C 3 11 ? 38.062 11.277 -4.840 1.00 56.79 ? 11 GLN D N 1 ATOM 2436 C CA . GLN C 3 11 ? 37.744 10.119 -5.691 1.00 62.54 ? 11 GLN D CA 1 ATOM 2437 C C . GLN C 3 11 ? 38.068 8.775 -5.027 1.00 63.93 ? 11 GLN D C 1 ATOM 2438 O O . GLN C 3 11 ? 38.913 8.706 -4.133 1.00 67.50 ? 11 GLN D O 1 ATOM 2439 C CB . GLN C 3 11 ? 38.427 10.233 -7.053 1.00 61.85 ? 11 GLN D CB 1 ATOM 2440 C CG . GLN C 3 11 ? 39.937 10.251 -6.963 1.00 65.68 ? 11 GLN D CG 1 ATOM 2441 C CD . GLN C 3 11 ? 40.586 10.008 -8.299 1.00 70.29 ? 11 GLN D CD 1 ATOM 2442 O OE1 . GLN C 3 11 ? 40.369 10.757 -9.252 1.00 73.68 ? 11 GLN D OE1 1 ATOM 2443 N NE2 . GLN C 3 11 ? 41.388 8.950 -8.381 1.00 69.52 ? 11 GLN D NE2 1 ATOM 2444 O OXT . GLN C 3 11 ? 37.479 7.738 -5.354 1.00 61.75 ? 11 GLN D OXT 1 HETATM 2445 C C20 . 9MX D 4 . ? 29.564 17.730 23.491 1.00 49.20 ? 1258 9MX B C20 1 HETATM 2446 C C27 . 9MX D 4 . ? 30.953 18.384 23.624 1.00 48.58 ? 1258 9MX B C27 1 HETATM 2447 C C32 . 9MX D 4 . ? 31.389 18.368 25.091 1.00 49.04 ? 1258 9MX B C32 1 HETATM 2448 C C33 . 9MX D 4 . ? 31.996 17.688 22.753 1.00 47.30 ? 1258 9MX B C33 1 HETATM 2449 N N37 . 9MX D 4 . ? 32.674 18.993 25.352 1.00 49.96 ? 1258 9MX B N37 1 HETATM 2450 C C38 . 9MX D 4 . ? 33.413 18.087 23.116 1.00 45.15 ? 1258 9MX B C38 1 HETATM 2451 C C40 . 9MX D 4 . ? 33.467 19.201 24.153 1.00 46.59 ? 1258 9MX B C40 1 HETATM 2452 C C41 . 9MX D 4 . ? 32.585 20.097 26.313 1.00 53.54 ? 1258 9MX B C41 1 HETATM 2453 N N43 . 9MX D 4 . ? 31.267 20.312 26.837 1.00 53.16 ? 1258 9MX B N43 1 HETATM 2454 N N42 . 9MX D 4 . ? 33.630 20.803 26.666 1.00 58.11 ? 1258 9MX B N42 1 HETATM 2455 N N3 . 9MX D 4 . ? 29.470 13.437 26.614 1.00 84.76 ? 1258 9MX B N3 1 HETATM 2456 C C1 . 9MX D 4 . ? 29.673 13.340 25.193 1.00 76.75 ? 1258 9MX B C1 1 HETATM 2457 C C2 . 9MX D 4 . ? 31.143 13.746 24.833 1.00 78.10 ? 1258 9MX B C2 1 HETATM 2458 O O6 . 9MX D 4 . ? 31.737 14.635 25.480 1.00 73.76 ? 1258 9MX B O6 1 HETATM 2459 C C4 . 9MX D 4 . ? 28.626 14.090 24.303 1.00 66.52 ? 1258 9MX B C4 1 HETATM 2460 C C8 . 9MX D 4 . ? 28.661 15.622 24.347 1.00 58.34 ? 1258 9MX B C8 1 HETATM 2461 O O15 . 9MX D 4 . ? 27.917 16.247 25.143 1.00 56.19 ? 1258 9MX B O15 1 HETATM 2462 N N14 . 9MX D 4 . ? 29.503 16.297 23.493 1.00 51.45 ? 1258 9MX B N14 1 HETATM 2463 S S7 . 9MX D 4 . ? 29.159 12.207 27.645 1.00 88.18 ? 1258 9MX B S7 1 HETATM 2464 O O12 . 9MX D 4 . ? 28.827 12.787 28.898 1.00 82.63 ? 1258 9MX B O12 1 HETATM 2465 O O13 . 9MX D 4 . ? 28.217 11.352 27.033 1.00 89.58 ? 1258 9MX B O13 1 HETATM 2466 C C18 . 9MX D 4 . ? 30.772 10.093 27.260 1.00 79.79 ? 1258 9MX B C18 1 HETATM 2467 C C11 . 9MX D 4 . ? 30.584 11.324 27.861 1.00 83.03 ? 1258 9MX B C11 1 HETATM 2468 C C19 . 9MX D 4 . ? 31.607 11.841 28.706 1.00 78.93 ? 1258 9MX B C19 1 HETATM 2469 C C26 . 9MX D 4 . ? 32.770 11.152 28.924 1.00 78.02 ? 1258 9MX B C26 1 HETATM 2470 C C35 . 9MX D 4 . ? 34.173 9.151 28.515 1.00 76.50 ? 1258 9MX B C35 1 HETATM 2471 C C39 . 9MX D 4 . ? 34.336 7.929 27.900 1.00 81.66 ? 1258 9MX B C39 1 HETATM 2472 C C36 . 9MX D 4 . ? 33.331 7.382 27.060 1.00 81.73 ? 1258 9MX B C36 1 HETATM 2473 C C31 . 9MX D 4 . ? 32.168 8.083 26.847 1.00 84.35 ? 1258 9MX B C31 1 HETATM 2474 C C25 . 9MX D 4 . ? 31.965 9.353 27.465 1.00 82.47 ? 1258 9MX B C25 1 HETATM 2475 C C30 . 9MX D 4 . ? 32.979 9.891 28.308 1.00 79.05 ? 1258 9MX B C30 1 HETATM 2476 N N5 . 9MX D 4 . ? 31.781 13.084 23.800 1.00 79.76 ? 1258 9MX B N5 1 HETATM 2477 C C21 . 9MX D 4 . ? 31.025 12.410 22.761 1.00 82.86 ? 1258 9MX B C21 1 HETATM 2478 C C28 . 9MX D 4 . ? 31.549 10.983 22.504 1.00 82.17 ? 1258 9MX B C28 1 HETATM 2479 C C10 . 9MX D 4 . ? 33.065 10.909 22.334 1.00 81.00 ? 1258 9MX B C10 1 HETATM 2480 C C16 . 9MX D 4 . ? 33.823 11.788 23.320 1.00 77.80 ? 1258 9MX B C16 1 HETATM 2481 C C9 . 9MX D 4 . ? 33.194 13.171 23.497 1.00 78.24 ? 1258 9MX B C9 1 HETATM 2482 C C17 . 9MX D 4 . ? 30.937 13.214 21.466 1.00 87.64 ? 1258 9MX B C17 1 HETATM 2483 O O23 . 9MX D 4 . ? 31.135 12.468 20.338 1.00 89.81 ? 1258 9MX B O23 1 HETATM 2484 O O24 . 9MX D 4 . ? 30.718 14.430 21.334 1.00 85.72 ? 1258 9MX B O24 1 HETATM 2485 C C29 . 9MX D 4 . ? 33.529 9.470 22.458 1.00 79.46 ? 1258 9MX B C29 1 HETATM 2486 C C1 . NAG E 5 . ? 40.248 -0.341 12.993 1.00 80.80 ? 1259 NAG B C1 1 HETATM 2487 C C2 . NAG E 5 . ? 40.728 -1.567 13.800 1.00 84.97 ? 1259 NAG B C2 1 HETATM 2488 C C3 . NAG E 5 . ? 42.114 -2.094 13.398 1.00 88.75 ? 1259 NAG B C3 1 HETATM 2489 C C4 . NAG E 5 . ? 42.315 -2.090 11.885 1.00 91.02 ? 1259 NAG B C4 1 HETATM 2490 C C5 . NAG E 5 . ? 41.988 -0.683 11.387 1.00 87.40 ? 1259 NAG B C5 1 HETATM 2491 C C6 . NAG E 5 . ? 42.365 -0.478 9.919 1.00 84.85 ? 1259 NAG B C6 1 HETATM 2492 C C7 . NAG E 5 . ? 39.693 -1.400 16.010 1.00 77.54 ? 1259 NAG B C7 1 HETATM 2493 C C8 . NAG E 5 . ? 39.895 -1.124 17.476 1.00 74.10 ? 1259 NAG B C8 1 HETATM 2494 N N2 . NAG E 5 . ? 40.770 -1.307 15.231 1.00 78.66 ? 1259 NAG B N2 1 HETATM 2495 O O3 . NAG E 5 . ? 42.288 -3.401 13.893 1.00 89.42 ? 1259 NAG B O3 1 HETATM 2496 O O4 . NAG E 5 . ? 43.639 -2.468 11.554 1.00 96.31 ? 1259 NAG B O4 1 HETATM 2497 O O5 . NAG E 5 . ? 40.605 -0.448 11.617 1.00 82.36 ? 1259 NAG B O5 1 HETATM 2498 O O6 . NAG E 5 . ? 41.316 -0.899 9.077 1.00 81.61 ? 1259 NAG B O6 1 HETATM 2499 O O7 . NAG E 5 . ? 38.579 -1.693 15.577 1.00 74.79 ? 1259 NAG B O7 1 HETATM 2500 NA NA . NA F 6 . ? 29.607 25.114 32.352 1.00 36.54 ? 1260 NA B NA 1 HETATM 2501 O O . HOH G 7 . ? 69.975 28.747 13.791 1.00 44.43 ? 2001 HOH A O 1 HETATM 2502 O O . HOH G 7 . ? 70.579 26.122 12.754 1.00 37.49 ? 2002 HOH A O 1 HETATM 2503 O O . HOH G 7 . ? 48.929 40.204 19.355 1.00 37.08 ? 2003 HOH A O 1 HETATM 2504 O O . HOH G 7 . ? 47.938 35.264 11.001 1.00 27.02 ? 2004 HOH A O 1 HETATM 2505 O O . HOH G 7 . ? 45.340 41.842 11.226 1.00 37.43 ? 2005 HOH A O 1 HETATM 2506 O O . HOH G 7 . ? 40.210 38.230 32.146 1.00 34.35 ? 2006 HOH A O 1 HETATM 2507 O O . HOH G 7 . ? 46.453 33.241 27.894 1.00 31.24 ? 2007 HOH A O 1 HETATM 2508 O O . HOH H 7 . ? 31.551 27.156 16.808 1.00 23.39 ? 2001 HOH B O 1 HETATM 2509 O O . HOH H 7 . ? 29.704 30.940 19.486 1.00 25.98 ? 2002 HOH B O 1 HETATM 2510 O O . HOH H 7 . ? 26.341 30.182 21.371 1.00 31.08 ? 2003 HOH B O 1 HETATM 2511 O O . HOH H 7 . ? 40.369 32.634 10.225 1.00 31.64 ? 2004 HOH B O 1 HETATM 2512 O O . HOH H 7 . ? 42.243 31.678 11.853 1.00 28.20 ? 2005 HOH B O 1 HETATM 2513 O O . HOH H 7 . ? 44.217 32.738 18.823 1.00 36.85 ? 2006 HOH B O 1 HETATM 2514 O O . HOH H 7 . ? 42.442 29.296 10.360 1.00 22.40 ? 2007 HOH B O 1 HETATM 2515 O O . HOH H 7 . ? 43.890 29.791 18.799 1.00 23.54 ? 2008 HOH B O 1 HETATM 2516 O O . HOH H 7 . ? 44.689 27.374 9.783 1.00 18.47 ? 2009 HOH B O 1 HETATM 2517 O O . HOH H 7 . ? 41.596 25.307 8.784 1.00 16.38 ? 2010 HOH B O 1 HETATM 2518 O O . HOH H 7 . ? 37.938 22.825 17.156 1.00 20.51 ? 2011 HOH B O 1 HETATM 2519 O O . HOH H 7 . ? 33.366 7.400 6.238 1.00 38.33 ? 2012 HOH B O 1 HETATM 2520 O O . HOH H 7 . ? 28.278 13.936 0.431 1.00 27.24 ? 2013 HOH B O 1 HETATM 2521 O O . HOH H 7 . ? 32.557 38.747 0.665 1.00 36.07 ? 2014 HOH B O 1 HETATM 2522 O O . HOH H 7 . ? 44.611 20.132 18.654 1.00 18.67 ? 2015 HOH B O 1 HETATM 2523 O O . HOH H 7 . ? 55.250 23.882 16.872 1.00 34.85 ? 2016 HOH B O 1 HETATM 2524 O O . HOH H 7 . ? 58.930 15.241 10.616 1.00 52.23 ? 2017 HOH B O 1 HETATM 2525 O O . HOH H 7 . ? 43.870 11.537 3.275 1.00 39.46 ? 2018 HOH B O 1 HETATM 2526 O O . HOH H 7 . ? 33.864 23.244 1.160 1.00 22.01 ? 2019 HOH B O 1 HETATM 2527 O O . HOH H 7 . ? 29.365 21.643 10.239 1.00 42.71 ? 2020 HOH B O 1 HETATM 2528 O O . HOH H 7 . ? 35.585 32.857 3.471 1.00 29.56 ? 2021 HOH B O 1 HETATM 2529 O O . HOH H 7 . ? 31.679 36.893 2.218 1.00 34.81 ? 2022 HOH B O 1 HETATM 2530 O O . HOH H 7 . ? 47.388 29.999 2.691 1.00 36.22 ? 2023 HOH B O 1 HETATM 2531 O O . HOH H 7 . ? 45.120 22.320 -1.636 1.00 41.27 ? 2024 HOH B O 1 HETATM 2532 O O . HOH H 7 . ? 49.977 18.527 1.963 1.00 44.71 ? 2025 HOH B O 1 HETATM 2533 O O . HOH H 7 . ? 48.813 16.046 0.563 1.00 33.84 ? 2026 HOH B O 1 HETATM 2534 O O . HOH H 7 . ? 45.503 2.663 20.716 1.00 60.85 ? 2027 HOH B O 1 HETATM 2535 O O . HOH H 7 . ? 40.965 13.240 28.085 1.00 32.99 ? 2028 HOH B O 1 HETATM 2536 O O . HOH H 7 . ? 43.720 12.706 28.527 1.00 27.80 ? 2029 HOH B O 1 HETATM 2537 O O . HOH H 7 . ? 56.527 24.976 4.993 1.00 65.56 ? 2030 HOH B O 1 HETATM 2538 O O . HOH H 7 . ? 53.681 31.864 8.543 1.00 31.04 ? 2031 HOH B O 1 HETATM 2539 O O . HOH H 7 . ? 49.968 34.724 2.810 1.00 41.73 ? 2032 HOH B O 1 HETATM 2540 O O . HOH H 7 . ? 43.874 31.612 9.416 1.00 32.40 ? 2033 HOH B O 1 HETATM 2541 O O . HOH H 7 . ? 56.554 23.699 19.214 1.00 27.33 ? 2034 HOH B O 1 HETATM 2542 O O . HOH H 7 . ? 60.471 20.545 28.441 1.00 35.11 ? 2035 HOH B O 1 HETATM 2543 O O . HOH H 7 . ? 38.683 29.245 37.448 1.00 44.45 ? 2036 HOH B O 1 HETATM 2544 O O . HOH H 7 . ? 42.345 28.188 20.115 1.00 22.98 ? 2037 HOH B O 1 HETATM 2545 O O . HOH H 7 . ? 36.075 22.516 14.933 1.00 21.85 ? 2038 HOH B O 1 HETATM 2546 O O . HOH H 7 . ? 29.225 22.499 13.053 1.00 49.65 ? 2039 HOH B O 1 HETATM 2547 O O . HOH H 7 . ? 16.432 27.144 17.928 1.00 40.39 ? 2040 HOH B O 1 HETATM 2548 O O . HOH H 7 . ? 13.177 20.319 16.736 1.00 52.65 ? 2041 HOH B O 1 HETATM 2549 O O . HOH H 7 . ? 41.957 21.638 35.862 1.00 36.57 ? 2042 HOH B O 1 HETATM 2550 O O . HOH H 7 . ? 45.104 21.857 36.490 1.00 34.43 ? 2043 HOH B O 1 HETATM 2551 O O . HOH H 7 . ? 35.488 13.080 39.383 1.00 37.90 ? 2044 HOH B O 1 HETATM 2552 O O . HOH H 7 . ? 31.723 18.599 34.444 1.00 49.33 ? 2045 HOH B O 1 HETATM 2553 O O . HOH H 7 . ? 35.250 24.154 28.579 1.00 36.53 ? 2046 HOH B O 1 HETATM 2554 O O . HOH H 7 . ? 35.938 29.282 36.820 1.00 32.42 ? 2047 HOH B O 1 HETATM 2555 O O . HOH H 7 . ? 31.402 28.436 31.236 1.00 18.59 ? 2048 HOH B O 1 HETATM 2556 O O . HOH H 7 . ? 31.758 26.031 33.011 1.00 35.80 ? 2049 HOH B O 1 HETATM 2557 O O . HOH H 7 . ? 29.039 26.218 35.203 1.00 49.83 ? 2050 HOH B O 1 HETATM 2558 O O . HOH H 7 . ? 36.284 35.224 39.611 1.00 50.51 ? 2051 HOH B O 1 HETATM 2559 O O . HOH H 7 . ? 32.320 25.218 30.096 1.00 41.87 ? 2052 HOH B O 1 HETATM 2560 O O . HOH H 7 . ? 30.757 21.085 29.597 1.00 57.16 ? 2053 HOH B O 1 HETATM 2561 O O . HOH H 7 . ? 29.970 23.595 30.754 1.00 32.25 ? 2054 HOH B O 1 HETATM 2562 O O . HOH H 7 . ? 32.503 16.679 19.092 1.00 47.63 ? 2055 HOH B O 1 HETATM 2563 O O . HOH H 7 . ? 49.745 21.036 28.978 1.00 23.05 ? 2056 HOH B O 1 HETATM 2564 O O . HOH H 7 . ? 36.179 19.996 26.231 1.00 43.49 ? 2057 HOH B O 1 HETATM 2565 O O . HOH H 7 . ? 30.667 19.063 31.208 1.00 62.34 ? 2058 HOH B O 1 HETATM 2566 O O . HOH H 7 . ? 28.108 21.276 29.907 1.00 40.44 ? 2059 HOH B O 1 HETATM 2567 O O . HOH H 7 . ? 31.945 16.789 32.522 1.00 55.03 ? 2060 HOH B O 1 HETATM 2568 O O . HOH H 7 . ? 28.898 26.879 31.509 1.00 37.12 ? 2061 HOH B O 1 HETATM 2569 O O . HOH I 7 . ? 26.807 26.713 1.326 1.00 33.73 ? 2001 HOH D O 1 HETATM 2570 O O . HOH I 7 . ? 28.142 29.051 -1.784 1.00 25.99 ? 2002 HOH D O 1 # loop_ _pdbx_poly_seq_scheme.asym_id _pdbx_poly_seq_scheme.entity_id _pdbx_poly_seq_scheme.seq_id _pdbx_poly_seq_scheme.mon_id _pdbx_poly_seq_scheme.ndb_seq_num _pdbx_poly_seq_scheme.pdb_seq_num _pdbx_poly_seq_scheme.auth_seq_num _pdbx_poly_seq_scheme.pdb_mon_id _pdbx_poly_seq_scheme.auth_mon_id _pdbx_poly_seq_scheme.pdb_strand_id _pdbx_poly_seq_scheme.pdb_ins_code _pdbx_poly_seq_scheme.hetero A 1 1 GLY 1 5 5 GLY GLY A . n A 1 2 GLU 2 6 6 GLU GLU A . n A 1 3 ALA 3 7 7 ALA ALA A . n A 1 4 ASP 4 8 8 ASP ASP A . n A 1 5 CYS 5 9 9 CYS CYS A . n A 1 6 GLY 6 10 10 GLY GLY A . n A 1 7 LEU 7 11 11 LEU LEU A . n A 1 8 ARG 8 12 12 ARG ARG A . n A 1 9 PRO 9 13 13 PRO PRO A . n A 1 10 LEU 10 14 14 LEU LEU A . n A 1 11 PHE 11 15 15 PHE PHE A . n A 1 12 GLU 12 16 16 GLU GLU A . n A 1 13 LYS 13 17 17 LYS LYS A . n A 1 14 LYS 14 18 18 LYS LYS A . n A 1 15 SER 15 19 19 SER SER A . n A 1 16 LEU 16 20 20 LEU LEU A . n A 1 17 GLU 17 21 21 GLU GLU A . n A 1 18 ASP 18 22 22 ASP ASP A . n A 1 19 LYS 19 23 23 LYS LYS A . n A 1 20 THR 20 24 24 THR THR A . n A 1 21 GLU 21 25 25 GLU GLU A . n A 1 22 ARG 22 26 26 ARG ARG A . n A 1 23 GLU 23 27 27 GLU GLU A . n A 1 24 LEU 24 28 28 LEU LEU A . n A 1 25 LEU 25 29 29 LEU LEU A . n A 1 26 GLU 26 30 30 GLU GLU A . n A 1 27 SER 27 31 31 SER SER A . n A 1 28 TYR 28 32 32 TYR TYR A . n A 1 29 ILE 29 33 33 ILE ILE A . n A 1 30 ASP 30 34 34 ASP ASP A . n B 2 1 ILE 1 1 1 ILE ILE B . n B 2 2 VAL 2 2 2 VAL VAL B . n B 2 3 GLU 3 3 3 GLU GLU B . n B 2 4 GLY 4 4 4 GLY GLY B . n B 2 5 SER 5 5 5 SER SER B . n B 2 6 ASP 6 6 6 ASP ASP B . n B 2 7 ALA 7 7 7 ALA ALA B . n B 2 8 GLU 8 8 8 GLU GLU B . n B 2 9 ILE 9 9 9 ILE ILE B . n B 2 10 GLY 10 10 10 GLY GLY B . n B 2 11 MET 11 11 11 MET MET B . n B 2 12 SER 12 12 12 SER SER B . n B 2 13 PRO 13 13 13 PRO PRO B . n B 2 14 TRP 14 14 14 TRP TRP B . n B 2 15 GLN 15 15 15 GLN GLN B . n B 2 16 VAL 16 16 16 VAL VAL B . n B 2 17 MET 17 17 17 MET MET B . n B 2 18 LEU 18 18 18 LEU LEU B . n B 2 19 PHE 19 19 19 PHE PHE B . n B 2 20 ARG 20 20 20 ARG ARG B . n B 2 21 LYS 21 21 21 LYS LYS B . n B 2 22 SER 22 22 22 SER SER B . n B 2 23 PRO 23 23 23 PRO PRO B . n B 2 24 GLN 24 24 24 GLN GLN B . n B 2 25 GLU 25 25 25 GLU GLU B . n B 2 26 LEU 26 26 26 LEU LEU B . n B 2 27 LEU 27 27 27 LEU LEU B . n B 2 28 CYS 28 28 28 CYS CYS B . n B 2 29 GLY 29 29 29 GLY GLY B . n B 2 30 ALA 30 30 30 ALA ALA B . n B 2 31 SER 31 31 31 SER SER B . n B 2 32 LEU 32 32 32 LEU LEU B . n B 2 33 ILE 33 33 33 ILE ILE B . n B 2 34 SER 34 34 34 SER SER B . n B 2 35 ASP 35 35 35 ASP ASP B . n B 2 36 ARG 36 36 36 ARG ARG B . n B 2 37 TRP 37 37 37 TRP TRP B . n B 2 38 VAL 38 38 38 VAL VAL B . n B 2 39 LEU 39 39 39 LEU LEU B . n B 2 40 THR 40 40 40 THR THR B . n B 2 41 ALA 41 41 41 ALA ALA B . n B 2 42 ALA 42 42 42 ALA ALA B . n B 2 43 HIS 43 43 43 HIS HIS B . n B 2 44 CYS 44 44 44 CYS CYS B . n B 2 45 LEU 45 45 45 LEU LEU B . n B 2 46 LEU 46 46 46 LEU LEU B . n B 2 47 TYR 47 47 47 TYR TYR B . n B 2 48 PRO 48 48 48 PRO PRO B . n B 2 49 PRO 49 49 49 PRO PRO B . n B 2 50 TRP 50 50 50 TRP TRP B . n B 2 51 ASP 51 51 51 ASP ASP B . n B 2 52 LYS 52 52 52 LYS LYS B . n B 2 53 ASN 53 53 53 ASN ASN B . n B 2 54 PHE 54 54 54 PHE PHE B . n B 2 55 THR 55 55 55 THR THR B . n B 2 56 GLU 56 56 56 GLU GLU B . n B 2 57 ASN 57 57 57 ASN ASN B . n B 2 58 ASP 58 58 58 ASP ASP B . n B 2 59 LEU 59 59 59 LEU LEU B . n B 2 60 LEU 60 60 60 LEU LEU B . n B 2 61 VAL 61 61 61 VAL VAL B . n B 2 62 ARG 62 62 62 ARG ARG B . n B 2 63 ILE 63 63 63 ILE ILE B . n B 2 64 GLY 64 64 64 GLY GLY B . n B 2 65 LYS 65 65 65 LYS LYS B . n B 2 66 HIS 66 66 66 HIS HIS B . n B 2 67 SER 67 67 67 SER SER B . n B 2 68 ARG 68 68 68 ARG ARG B . n B 2 69 THR 69 69 69 THR THR B . n B 2 70 ARG 70 70 70 ARG ARG B . n B 2 71 TYR 71 71 71 TYR TYR B . n B 2 72 GLU 72 72 72 GLU GLU B . n B 2 73 ARG 73 73 73 ARG ARG B . n B 2 74 ASN 74 74 74 ASN ASN B . n B 2 75 ILE 75 75 75 ILE ILE B . n B 2 76 GLU 76 76 76 GLU GLU B . n B 2 77 LYS 77 77 77 LYS LYS B . n B 2 78 ILE 78 78 78 ILE ILE B . n B 2 79 SER 79 79 79 SER SER B . n B 2 80 MET 80 80 80 MET MET B . n B 2 81 LEU 81 81 81 LEU LEU B . n B 2 82 GLU 82 82 82 GLU GLU B . n B 2 83 LYS 83 83 83 LYS LYS B . n B 2 84 ILE 84 84 84 ILE ILE B . n B 2 85 TYR 85 85 85 TYR TYR B . n B 2 86 ILE 86 86 86 ILE ILE B . n B 2 87 HIS 87 87 87 HIS HIS B . n B 2 88 PRO 88 88 88 PRO PRO B . n B 2 89 ARG 89 89 89 ARG ARG B . n B 2 90 TYR 90 90 90 TYR TYR B . n B 2 91 ASN 91 91 91 ASN ASN B . n B 2 92 TRP 92 92 92 TRP TRP B . n B 2 93 ARG 93 93 93 ARG ARG B . n B 2 94 GLU 94 94 94 GLU GLU B . n B 2 95 ASN 95 95 95 ASN ASN B . n B 2 96 LEU 96 96 96 LEU LEU B . n B 2 97 ASP 97 97 97 ASP ASP B . n B 2 98 ARG 98 98 98 ARG ARG B . n B 2 99 ASP 99 99 99 ASP ASP B . n B 2 100 ILE 100 100 100 ILE ILE B . n B 2 101 ALA 101 101 101 ALA ALA B . n B 2 102 LEU 102 102 102 LEU LEU B . n B 2 103 MET 103 103 103 MET MET B . n B 2 104 LYS 104 104 104 LYS LYS B . n B 2 105 LEU 105 105 105 LEU LEU B . n B 2 106 LYS 106 106 106 LYS LYS B . n B 2 107 LYS 107 107 107 LYS LYS B . n B 2 108 PRO 108 108 108 PRO PRO B . n B 2 109 VAL 109 109 109 VAL VAL B . n B 2 110 ALA 110 110 110 ALA ALA B . n B 2 111 PHE 111 111 111 PHE PHE B . n B 2 112 SER 112 112 112 SER SER B . n B 2 113 ASP 113 113 113 ASP ASP B . n B 2 114 TYR 114 114 114 TYR TYR B . n B 2 115 ILE 115 115 115 ILE ILE B . n B 2 116 HIS 116 116 116 HIS HIS B . n B 2 117 PRO 117 117 117 PRO PRO B . n B 2 118 VAL 118 118 118 VAL VAL B . n B 2 119 CYS 119 119 119 CYS CYS B . n B 2 120 LEU 120 120 120 LEU LEU B . n B 2 121 PRO 121 121 121 PRO PRO B . n B 2 122 ASP 122 122 122 ASP ASP B . n B 2 123 ARG 123 123 123 ARG ARG B . n B 2 124 GLU 124 124 124 GLU GLU B . n B 2 125 THR 125 125 125 THR THR B . n B 2 126 ALA 126 126 126 ALA ALA B . n B 2 127 ALA 127 127 127 ALA ALA B . n B 2 128 SER 128 128 128 SER SER B . n B 2 129 LEU 129 129 129 LEU LEU B . n B 2 130 LEU 130 130 130 LEU LEU B . n B 2 131 GLN 131 131 131 GLN GLN B . n B 2 132 ALA 132 132 132 ALA ALA B . n B 2 133 GLY 133 133 133 GLY GLY B . n B 2 134 TYR 134 134 134 TYR TYR B . n B 2 135 LYS 135 135 135 LYS LYS B . n B 2 136 GLY 136 136 136 GLY GLY B . n B 2 137 ARG 137 137 137 ARG ARG B . n B 2 138 VAL 138 138 138 VAL VAL B . n B 2 139 THR 139 139 139 THR THR B . n B 2 140 GLY 140 140 140 GLY GLY B . n B 2 141 TRP 141 141 141 TRP TRP B . n B 2 142 GLY 142 142 142 GLY GLY B . n B 2 143 ASN 143 143 143 ASN ASN B . n B 2 144 LEU 144 144 144 LEU LEU B . n B 2 145 LYS 145 145 145 LYS LYS B . n B 2 146 GLU 146 146 146 GLU GLU B . n B 2 147 THR 147 147 147 THR THR B . n B 2 148 TRP 148 148 148 TRP TRP B . n B 2 149 THR 149 149 149 THR THR B . n B 2 150 ALA 150 150 150 ALA ALA B . n B 2 151 ASN 151 151 151 ASN ASN B . n B 2 152 VAL 152 152 152 VAL VAL B . n B 2 153 GLY 153 153 153 GLY GLY B . n B 2 154 LYS 154 154 154 LYS LYS B . n B 2 155 GLY 155 155 155 GLY GLY B . n B 2 156 GLN 156 156 156 GLN GLN B . n B 2 157 PRO 157 157 157 PRO PRO B . n B 2 158 SER 158 158 158 SER SER B . n B 2 159 VAL 159 159 159 VAL VAL B . n B 2 160 LEU 160 160 160 LEU LEU B . n B 2 161 GLN 161 161 161 GLN GLN B . n B 2 162 VAL 162 162 162 VAL VAL B . n B 2 163 VAL 163 163 163 VAL VAL B . n B 2 164 ASN 164 164 164 ASN ASN B . n B 2 165 LEU 165 165 165 LEU LEU B . n B 2 166 PRO 166 166 166 PRO PRO B . n B 2 167 ILE 167 167 167 ILE ILE B . n B 2 168 VAL 168 168 168 VAL VAL B . n B 2 169 GLU 169 169 169 GLU GLU B . n B 2 170 ARG 170 170 170 ARG ARG B . n B 2 171 PRO 171 171 171 PRO PRO B . n B 2 172 VAL 172 172 172 VAL VAL B . n B 2 173 CYS 173 173 173 CYS CYS B . n B 2 174 LYS 174 174 174 LYS LYS B . n B 2 175 ASP 175 175 175 ASP ASP B . n B 2 176 SER 176 176 176 SER SER B . n B 2 177 THR 177 177 177 THR THR B . n B 2 178 ARG 178 178 178 ARG ARG B . n B 2 179 ILE 179 179 179 ILE ILE B . n B 2 180 ARG 180 180 180 ARG ARG B . n B 2 181 ILE 181 181 181 ILE ILE B . n B 2 182 THR 182 182 182 THR THR B . n B 2 183 ASP 183 183 183 ASP ASP B . n B 2 184 ASN 184 184 184 ASN ASN B . n B 2 185 MET 185 185 185 MET MET B . n B 2 186 PHE 186 186 186 PHE PHE B . n B 2 187 CYS 187 187 187 CYS CYS B . n B 2 188 ALA 188 188 188 ALA ALA B . n B 2 189 GLY 189 189 189 GLY GLY B . n B 2 190 TYR 190 190 190 TYR TYR B . n B 2 191 LYS 191 191 191 LYS LYS B . n B 2 192 PRO 192 192 192 PRO PRO B . n B 2 193 ASP 193 193 193 ASP ASP B . n B 2 194 GLU 194 194 194 GLU GLU B . n B 2 195 GLY 195 195 195 GLY GLY B . n B 2 196 LYS 196 196 196 LYS LYS B . n B 2 197 ARG 197 197 197 ARG ARG B . n B 2 198 GLY 198 198 198 GLY GLY B . n B 2 199 ASP 199 199 199 ASP ASP B . n B 2 200 ALA 200 200 200 ALA ALA B . n B 2 201 CYS 201 201 201 CYS CYS B . n B 2 202 GLU 202 202 202 GLU GLU B . n B 2 203 GLY 203 203 203 GLY GLY B . n B 2 204 ASP 204 204 204 ASP ASP B . n B 2 205 SER 205 205 205 SER SER B . n B 2 206 GLY 206 206 206 GLY GLY B . n B 2 207 GLY 207 207 207 GLY GLY B . n B 2 208 PRO 208 208 208 PRO PRO B . n B 2 209 PHE 209 209 209 PHE PHE B . n B 2 210 VAL 210 210 210 VAL VAL B . n B 2 211 MET 211 211 211 MET MET B . n B 2 212 LYS 212 212 212 LYS LYS B . n B 2 213 SER 213 213 213 SER SER B . n B 2 214 PRO 214 214 214 PRO PRO B . n B 2 215 PHE 215 215 215 PHE PHE B . n B 2 216 ASN 216 216 216 ASN ASN B . n B 2 217 ASN 217 217 217 ASN ASN B . n B 2 218 ARG 218 218 218 ARG ARG B . n B 2 219 TRP 219 219 219 TRP TRP B . n B 2 220 TYR 220 220 220 TYR TYR B . n B 2 221 GLN 221 221 221 GLN GLN B . n B 2 222 MET 222 222 222 MET MET B . n B 2 223 GLY 223 223 223 GLY GLY B . n B 2 224 ILE 224 224 224 ILE ILE B . n B 2 225 VAL 225 225 225 VAL VAL B . n B 2 226 SER 226 226 226 SER SER B . n B 2 227 TRP 227 227 227 TRP TRP B . n B 2 228 GLY 228 228 228 GLY GLY B . n B 2 229 GLU 229 229 229 GLU GLU B . n B 2 230 GLY 230 230 230 GLY GLY B . n B 2 231 CYS 231 231 231 CYS CYS B . n B 2 232 ASP 232 232 232 ASP ASP B . n B 2 233 ARG 233 233 233 ARG ARG B . n B 2 234 ASP 234 234 234 ASP ASP B . n B 2 235 GLY 235 235 235 GLY GLY B . n B 2 236 LYS 236 236 236 LYS LYS B . n B 2 237 TYR 237 237 237 TYR TYR B . n B 2 238 GLY 238 238 238 GLY GLY B . n B 2 239 PHE 239 239 239 PHE PHE B . n B 2 240 TYR 240 240 240 TYR TYR B . n B 2 241 THR 241 241 241 THR THR B . n B 2 242 HIS 242 242 242 HIS HIS B . n B 2 243 VAL 243 243 243 VAL VAL B . n B 2 244 PHE 244 244 244 PHE PHE B . n B 2 245 ARG 245 245 245 ARG ARG B . n B 2 246 LEU 246 246 246 LEU LEU B . n B 2 247 LYS 247 247 247 LYS LYS B . n B 2 248 LYS 248 248 248 LYS LYS B . n B 2 249 TRP 249 249 249 TRP TRP B . n B 2 250 ILE 250 250 250 ILE ILE B . n B 2 251 GLN 251 251 251 GLN GLN B . n B 2 252 LYS 252 252 252 LYS LYS B . n B 2 253 VAL 253 253 253 VAL VAL B . n B 2 254 ILE 254 254 254 ILE ILE B . n B 2 255 ASP 255 255 255 ASP ASP B . n B 2 256 GLN 256 256 256 GLN GLN B . n B 2 257 PHE 257 257 257 PHE PHE B . n C 3 1 ASP 1 1 1 ASP ASP D . n C 3 2 PHE 2 2 2 PHE PHE D . n C 3 3 GLU 3 3 3 GLU GLU D . n C 3 4 GLU 4 4 4 GLU GLU D . n C 3 5 ILE 5 5 5 ILE ILE D . n C 3 6 PRO 6 6 6 PRO PRO D . n C 3 7 GLU 7 7 7 GLU GLU D . n C 3 8 GLU 8 8 8 GLU GLU D . n C 3 9 TYR 9 9 9 TYR TYR D . n C 3 10 LEU 10 10 10 LEU LEU D . n C 3 11 GLN 11 11 11 GLN GLN D . n # loop_ _pdbx_nonpoly_scheme.asym_id _pdbx_nonpoly_scheme.entity_id _pdbx_nonpoly_scheme.mon_id _pdbx_nonpoly_scheme.ndb_seq_num _pdbx_nonpoly_scheme.pdb_seq_num _pdbx_nonpoly_scheme.auth_seq_num _pdbx_nonpoly_scheme.pdb_mon_id _pdbx_nonpoly_scheme.auth_mon_id _pdbx_nonpoly_scheme.pdb_strand_id _pdbx_nonpoly_scheme.pdb_ins_code D 4 9MX 1 1258 1258 9MX 9MX B . E 5 NAG 1 1259 1259 NAG NAG B . F 6 NA 1 1260 1260 NA NA B . G 7 HOH 1 2001 2001 HOH HOH A . G 7 HOH 2 2002 2002 HOH HOH A . G 7 HOH 3 2003 2003 HOH HOH A . G 7 HOH 4 2004 2004 HOH HOH A . G 7 HOH 5 2005 2005 HOH HOH A . G 7 HOH 6 2006 2006 HOH HOH A . G 7 HOH 7 2007 2007 HOH HOH A . H 7 HOH 1 2001 2001 HOH HOH B . H 7 HOH 2 2002 2002 HOH HOH B . H 7 HOH 3 2003 2003 HOH HOH B . H 7 HOH 4 2004 2004 HOH HOH B . H 7 HOH 5 2005 2005 HOH HOH B . H 7 HOH 6 2006 2006 HOH HOH B . H 7 HOH 7 2007 2007 HOH HOH B . H 7 HOH 8 2008 2008 HOH HOH B . H 7 HOH 9 2009 2009 HOH HOH B . H 7 HOH 10 2010 2010 HOH HOH B . H 7 HOH 11 2011 2011 HOH HOH B . H 7 HOH 12 2012 2012 HOH HOH B . H 7 HOH 13 2013 2013 HOH HOH B . H 7 HOH 14 2014 2014 HOH HOH B . H 7 HOH 15 2015 2015 HOH HOH B . H 7 HOH 16 2016 2016 HOH HOH B . H 7 HOH 17 2017 2017 HOH HOH B . H 7 HOH 18 2018 2018 HOH HOH B . H 7 HOH 19 2019 2019 HOH HOH B . H 7 HOH 20 2020 2020 HOH HOH B . H 7 HOH 21 2021 2021 HOH HOH B . H 7 HOH 22 2022 2022 HOH HOH B . H 7 HOH 23 2023 2023 HOH HOH B . H 7 HOH 24 2024 2024 HOH HOH B . H 7 HOH 25 2025 2025 HOH HOH B . H 7 HOH 26 2026 2026 HOH HOH B . H 7 HOH 27 2027 2027 HOH HOH B . H 7 HOH 28 2028 2028 HOH HOH B . H 7 HOH 29 2029 2029 HOH HOH B . H 7 HOH 30 2030 2030 HOH HOH B . H 7 HOH 31 2031 2031 HOH HOH B . H 7 HOH 32 2032 2032 HOH HOH B . H 7 HOH 33 2033 2033 HOH HOH B . H 7 HOH 34 2034 2034 HOH HOH B . H 7 HOH 35 2035 2035 HOH HOH B . H 7 HOH 36 2036 2036 HOH HOH B . H 7 HOH 37 2037 2037 HOH HOH B . H 7 HOH 38 2038 2038 HOH HOH B . H 7 HOH 39 2039 2039 HOH HOH B . H 7 HOH 40 2040 2040 HOH HOH B . H 7 HOH 41 2041 2041 HOH HOH B . H 7 HOH 42 2042 2042 HOH HOH B . H 7 HOH 43 2043 2043 HOH HOH B . H 7 HOH 44 2044 2044 HOH HOH B . H 7 HOH 45 2045 2045 HOH HOH B . H 7 HOH 46 2046 2046 HOH HOH B . H 7 HOH 47 2047 2047 HOH HOH B . H 7 HOH 48 2048 2048 HOH HOH B . H 7 HOH 49 2049 2049 HOH HOH B . H 7 HOH 50 2050 2050 HOH HOH B . H 7 HOH 51 2051 2051 HOH HOH B . H 7 HOH 52 2052 2052 HOH HOH B . H 7 HOH 53 2053 2053 HOH HOH B . H 7 HOH 54 2054 2054 HOH HOH B . H 7 HOH 55 2055 2055 HOH HOH B . H 7 HOH 56 2056 2056 HOH HOH B . H 7 HOH 57 2057 2057 HOH HOH B . H 7 HOH 58 2058 2058 HOH HOH B . H 7 HOH 59 2059 2059 HOH HOH B . H 7 HOH 60 2060 2060 HOH HOH B . H 7 HOH 61 2061 2061 HOH HOH B . I 7 HOH 1 2001 2001 HOH HOH D . I 7 HOH 2 2002 2002 HOH HOH D . # _pdbx_struct_mod_residue.id 1 _pdbx_struct_mod_residue.label_asym_id B _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 53 _pdbx_struct_mod_residue.PDB_ins_code ? _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 trimeric _pdbx_struct_assembly.oligomeric_count 3 # _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 # 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)' 3700 ? 1 MORE -26.6 ? 1 'SSA (A^2)' 14370 ? # _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 ? H HOH . ? B HOH 2054 ? 1_555 NA ? F NA . ? B NA 1260 ? 1_555 O ? H HOH . ? B HOH 2061 ? 1_555 110.0 ? 2 O ? H HOH . ? B HOH 2054 ? 1_555 NA ? F NA . ? B NA 1260 ? 1_555 O ? H HOH . ? B HOH 2050 ? 1_555 157.9 ? 3 O ? H HOH . ? B HOH 2061 ? 1_555 NA ? F NA . ? B NA 1260 ? 1_555 O ? H HOH . ? B HOH 2050 ? 1_555 90.5 ? 4 O ? H HOH . ? B HOH 2054 ? 1_555 NA ? F NA . ? B NA 1260 ? 1_555 O ? B LYS 236 ? B LYS 236 ? 1_555 78.7 ? 5 O ? H HOH . ? B HOH 2061 ? 1_555 NA ? F NA . ? B NA 1260 ? 1_555 O ? B LYS 236 ? B LYS 236 ? 1_555 166.0 ? 6 O ? H HOH . ? B HOH 2050 ? 1_555 NA ? F NA . ? B NA 1260 ? 1_555 O ? B LYS 236 ? B LYS 236 ? 1_555 83.0 ? 7 O ? H HOH . ? B HOH 2054 ? 1_555 NA ? F NA . ? B NA 1260 ? 1_555 O ? H HOH . ? B HOH 2049 ? 1_555 107.9 ? 8 O ? H HOH . ? B HOH 2061 ? 1_555 NA ? F NA . ? B NA 1260 ? 1_555 O ? H HOH . ? B HOH 2049 ? 1_555 95.2 ? 9 O ? H HOH . ? B HOH 2050 ? 1_555 NA ? F NA . ? B NA 1260 ? 1_555 O ? H HOH . ? B HOH 2049 ? 1_555 77.2 ? 10 O ? B LYS 236 ? B LYS 236 ? 1_555 NA ? F NA . ? B NA 1260 ? 1_555 O ? H HOH . ? B HOH 2049 ? 1_555 71.3 ? 11 O ? H HOH . ? B HOH 2054 ? 1_555 NA ? F NA . ? B NA 1260 ? 1_555 O ? B ARG 233 ? B ARG 233 ? 1_555 92.1 ? 12 O ? H HOH . ? B HOH 2061 ? 1_555 NA ? F NA . ? B NA 1260 ? 1_555 O ? B ARG 233 ? B ARG 233 ? 1_555 97.5 ? 13 O ? H HOH . ? B HOH 2050 ? 1_555 NA ? F NA . ? B NA 1260 ? 1_555 O ? B ARG 233 ? B ARG 233 ? 1_555 76.7 ? 14 O ? B LYS 236 ? B LYS 236 ? 1_555 NA ? F NA . ? B NA 1260 ? 1_555 O ? B ARG 233 ? B ARG 233 ? 1_555 92.9 ? 15 O ? H HOH . ? B HOH 2049 ? 1_555 NA ? F NA . ? B NA 1260 ? 1_555 O ? B ARG 233 ? B ARG 233 ? 1_555 150.9 ? # loop_ _pdbx_audit_revision_history.ordinal _pdbx_audit_revision_history.data_content_type _pdbx_audit_revision_history.major_revision _pdbx_audit_revision_history.minor_revision _pdbx_audit_revision_history.revision_date 1 'Structure model' 1 0 2012-08-15 2 'Structure model' 1 1 2013-08-07 3 'Structure model' 1 2 2017-06-28 # _pdbx_audit_revision_details.ordinal 1 _pdbx_audit_revision_details.revision_ordinal 1 _pdbx_audit_revision_details.data_content_type 'Structure model' _pdbx_audit_revision_details.provider repository _pdbx_audit_revision_details.type 'Initial release' _pdbx_audit_revision_details.description ? # loop_ _pdbx_audit_revision_group.ordinal _pdbx_audit_revision_group.revision_ordinal _pdbx_audit_revision_group.data_content_type _pdbx_audit_revision_group.group 1 2 'Structure model' Other 2 3 'Structure model' 'Data collection' # _pdbx_audit_revision_category.ordinal 1 _pdbx_audit_revision_category.revision_ordinal 3 _pdbx_audit_revision_category.data_content_type 'Structure model' _pdbx_audit_revision_category.category diffrn_source # loop_ _pdbx_audit_revision_item.ordinal _pdbx_audit_revision_item.revision_ordinal _pdbx_audit_revision_item.data_content_type _pdbx_audit_revision_item.item 1 3 'Structure model' '_diffrn_source.pdbx_wavelength_list' 2 3 'Structure model' '_diffrn_source.type' # loop_ _software.name _software.classification _software.version _software.citation_id _software.pdbx_ordinal _software.date _software.type _software.location _software.language REFMAC refinement 5.7.0025 ? 1 ? ? ? ? XDS 'data reduction' . ? 2 ? ? ? ? XDS 'data scaling' . ? 3 ? ? ? ? AMoRE phasing . ? 4 ? ? ? ? # _pdbx_database_remark.id 700 _pdbx_database_remark.text ; SHEET DETERMINATION METHOD: DSSP THE SHEETS PRESENTED AS "BB" IN EACH CHAIN ON SHEET RECORDS BELOW IS ACTUALLY AN 6-STRANDED BARREL THIS IS REPRESENTED BY A 7-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS ARE IDENTICAL. ; # _pdbx_entry_details.entry_id 4AYY _pdbx_entry_details.compound_details ? _pdbx_entry_details.source_details ? _pdbx_entry_details.nonpolymer_details ? _pdbx_entry_details.sequence_details ;THE N-TERMINAL RESIDUE IS MODIFIED IN CHAIN D. PLEASE REFER TO THE CITATION FOR FURTHER DETAILS. ; # 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 PHE A 15 ? ? -124.84 -87.95 2 1 ILE A 33 ? ? -115.29 55.37 3 1 ASN B 53 ? ? -154.47 78.91 4 1 SER B 112 ? ? -163.42 -167.15 5 1 VAL B 152 ? ? -132.73 -69.86 6 1 LYS B 154 ? ? -66.76 -70.02 # loop_ _pdbx_entity_nonpoly.entity_id _pdbx_entity_nonpoly.name _pdbx_entity_nonpoly.comp_id 4 ;(R)-1-[(S)-3-[((S)-1-Carbamimidoyl-piperidin-3-ylmethyl)-carbamoyl]-2-(naphthalene-2-sulfonylamino)-propionyl]-4-methyl-piperidine-2-carboxylic acid ; 9MX 5 N-ACETYL-D-GLUCOSAMINE NAG 6 'SODIUM ION' NA 7 water HOH #