data_25727 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C, and 15N Chemical Shift Assignments for Histamine-Binding Protein (D24R) bound to histamine ; _BMRB_accession_number 25727 _BMRB_flat_file_name bmr25727.str _Entry_type original _Submission_date 2015-07-27 _Accession_date 2015-07-27 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'For method development in conformational entropy' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Lim Jackwee . . 2 Valentine Kathleen G. . 3 Kasinath Vignesh . . 4 Harpole Kyle W. . 5 Sharp Kim A. . 6 Wand Joshua A. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 S2_parameters 2 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 229 "13C chemical shifts" 381 "15N chemical shifts" 160 "order parameters" 210 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2017-06-27 original BMRB . stop_ loop_ _Related_BMRB_accession_number _Relationship 25728 'HBPd24r (apo form)' stop_ _Original_release_date 2015-07-27 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Entropy in molecular recognition by proteins ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 28584100 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Caro Jose A. . 2 Harpole Kyle W. . 3 Kasinath Vignesh . . 4 Lim Jackwee . . 5 Granja Jeffrey . . 6 Valentine Kathleen G. . 7 Sharp Kim A. . 8 Wand 'A Joshua' J. . stop_ _Journal_abbreviation 'Proc. Natl. Acad. Sci. U.S.A.' _Journal_name_full 'Proceedings of the National Academy of Sciences of the United States of America' _Journal_volume 114 _Journal_issue 25 _Journal_ISSN 1091-6490 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 6563 _Page_last 6568 _Year 2017 _Details . loop_ _Keyword 'Binding Affinities' Entropy Ligand Protein stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'HBPd24r bound to histamine' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label HBPd24r $HBP(d24r) histamine $entity_HSM stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . loop_ _Biological_function 'Overcome host inflammatory and immune responses' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_HBP(d24r) _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common HBP(d24r) _Molecular_mass . _Mol_thiol_state 'all disulfide bound' loop_ _Biological_function Histamine-binding Serotonin-binding stop_ _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 173 _Mol_residue_sequence ; GSNQPDWADEAANGAHQDAW KSLKARVENVYYMVKATYKN DPVWGNDFTCVGVMANDVNE DEKSIQAEFLFMNNADTNMQ FATEKVTAVKMYGYNRENAF RYETEDGQVFTDVIAYSDDN CDVIYVPGTDGNEEGYELWT TDYDNIPANCLNKFNEYAVG RETRDVFTSACLE ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -1 GLY 2 0 SER 3 1 ASN 4 2 GLN 5 3 PRO 6 4 ASP 7 5 TRP 8 6 ALA 9 7 ASP 10 8 GLU 11 9 ALA 12 10 ALA 13 11 ASN 14 12 GLY 15 13 ALA 16 14 HIS 17 15 GLN 18 16 ASP 19 17 ALA 20 18 TRP 21 19 LYS 22 20 SER 23 21 LEU 24 22 LYS 25 23 ALA 26 24 ARG 27 25 VAL 28 26 GLU 29 27 ASN 30 28 VAL 31 29 TYR 32 30 TYR 33 31 MET 34 32 VAL 35 33 LYS 36 34 ALA 37 35 THR 38 36 TYR 39 37 LYS 40 38 ASN 41 39 ASP 42 40 PRO 43 41 VAL 44 42 TRP 45 43 GLY 46 44 ASN 47 45 ASP 48 46 PHE 49 47 THR 50 48 CYS 51 49 VAL 52 50 GLY 53 51 VAL 54 52 MET 55 53 ALA 56 54 ASN 57 55 ASP 58 56 VAL 59 57 ASN 60 58 GLU 61 59 ASP 62 60 GLU 63 61 LYS 64 62 SER 65 63 ILE 66 64 GLN 67 65 ALA 68 66 GLU 69 67 PHE 70 68 LEU 71 69 PHE 72 70 MET 73 71 ASN 74 72 ASN 75 73 ALA 76 74 ASP 77 75 THR 78 76 ASN 79 77 MET 80 78 GLN 81 79 PHE 82 80 ALA 83 81 THR 84 82 GLU 85 83 LYS 86 84 VAL 87 85 THR 88 86 ALA 89 87 VAL 90 88 LYS 91 89 MET 92 90 TYR 93 91 GLY 94 92 TYR 95 93 ASN 96 94 ARG 97 95 GLU 98 96 ASN 99 97 ALA 100 98 PHE 101 99 ARG 102 100 TYR 103 101 GLU 104 102 THR 105 103 GLU 106 104 ASP 107 105 GLY 108 106 GLN 109 107 VAL 110 108 PHE 111 109 THR 112 110 ASP 113 111 VAL 114 112 ILE 115 113 ALA 116 114 TYR 117 115 SER 118 116 ASP 119 117 ASP 120 118 ASN 121 119 CYS 122 120 ASP 123 121 VAL 124 122 ILE 125 123 TYR 126 124 VAL 127 125 PRO 128 126 GLY 129 127 THR 130 128 ASP 131 129 GLY 132 130 ASN 133 131 GLU 134 132 GLU 135 133 GLY 136 134 TYR 137 135 GLU 138 136 LEU 139 137 TRP 140 138 THR 141 139 THR 142 140 ASP 143 141 TYR 144 142 ASP 145 143 ASN 146 144 ILE 147 145 PRO 148 146 ALA 149 147 ASN 150 148 CYS 151 149 LEU 152 150 ASN 153 151 LYS 154 152 PHE 155 153 ASN 156 154 GLU 157 155 TYR 158 156 ALA 159 157 VAL 160 158 GLY 161 159 ARG 162 160 GLU 163 161 THR 164 162 ARG 165 163 ASP 166 164 VAL 167 165 PHE 168 166 THR 169 167 SER 170 168 ALA 171 169 CYS 172 170 LEU 173 171 GLU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ ############# # Ligands # ############# save_HSM _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common HISTAMINE _BMRB_code HSM _PDB_code HSM _Molecular_mass 111.145 _Mol_charge 0 _Mol_paramagnetic . _Mol_aromatic yes _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons N N N . 0 . ? CA CA C . 0 . ? CB CB C . 0 . ? CG CG C . 0 . ? ND1 ND1 N . 0 . ? CD2 CD2 C . 0 . ? CE1 CE1 C . 0 . ? NE2 NE2 N . 0 . ? H1 H1 H . 0 . ? H2 H2 H . 0 . ? HA1 HA1 H . 0 . ? HA2 HA2 H . 0 . ? HB1 HB1 H . 0 . ? HB2 HB2 H . 0 . ? HD2 HD2 H . 0 . ? HE1 HE1 H . 0 . ? HE2 HE2 H . 0 . ? stop_ loop_ _Bond_order _Bond_atom_one_atom_name _Bond_atom_two_atom_name _PDB_bond_atom_one_atom_name _PDB_bond_atom_two_atom_name SING N CA ? ? SING N H1 ? ? SING N H2 ? ? SING CA CB ? ? SING CA HA1 ? ? SING CA HA2 ? ? SING CB CG ? ? SING CB HB1 ? ? SING CB HB2 ? ? SING CG ND1 ? ? DOUB CG CD2 ? ? DOUB ND1 CE1 ? ? SING CD2 NE2 ? ? SING CD2 HD2 ? ? SING CE1 NE2 ? ? SING CE1 HE1 ? ? SING NE2 HE2 ? ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $HBP(d24r) 'mites and ticks' 34631 Eukaryota Metazoa Rhipicephalus appendiculatus stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Variant _Vector_name $HBP(d24r) 'recombinant technology' . Escherichia coli BL21 DE3 pET15b stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $HBP(d24r) 1.0 mM '[U-99% 13C; U-99% 15N]' $entity_HSM 1.5 mM 'natural abundance' 'potassium phosphate' 50 mM 'natural abundance' D2O 5 % 'natural abundance' 'sodium azide' 0.02 % 'natural abundance' H2O 95 % 'natuarl abundance' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details 'A NMR mixture of [15N-labeled] and [13C, 55% 2H-labeled] protein' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $HBP(d24r) 1.5 mM '[U-99% 15N]' $HBP(d24r) 1.5 mM '[U-99% 13C; U-55% 2H]' $entity_HSM 2.5 mM 'natural abundance' D2O 5 % [U-2H] 'potassium phosphate' 50 mM 'natural abundance' 'sodium azide' 0.02 % 'natural abundance' H2O 95 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_Felix _Saveframe_category software _Name Felix _Version . loop_ _Vendor _Address _Electronic_address 'Accelrys Software Inc.' . . stop_ loop_ _Task processing stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 500 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 750 _Details 'Second magnetic field for collecting data for order parameters' save_ ############################# # NMR applied experiments # ############################# save_2D_1H-15N_HSQC_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCO_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HNCA_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNCACB_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_HCACO_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCACO' _Sample_label $sample_1 save_ save_3D_HCCH-TOCSY_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HCCH-TOCSY' _Sample_label $sample_1 save_ save_2D_1H-13C_HSQC_aliphatic_9 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC aliphatic' _Sample_label $sample_1 save_ save_3D_1H-15N_TOCSY_10 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N TOCSY' _Sample_label $sample_1 save_ save_2D_1H-15N_HSQC_11 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N HSQC' _Sample_label $sample_2 save_ save_2D_1H-13C_HSQC_12 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _Sample_label $sample_2 save_ save_N_T1_relaxation_13 _Saveframe_category NMR_applied_experiment _Experiment_name 'N T1 relaxation' _Sample_label $sample_2 save_ save_N_T2_relaxation_14 _Saveframe_category NMR_applied_experiment _Experiment_name 'N T2 relaxation' _Sample_label $sample_2 save_ save_N_NOE_relaxation_15 _Saveframe_category NMR_applied_experiment _Experiment_name 'N NOE relaxation' _Sample_label $sample_2 save_ save_Dz_(IzCz)_compensated_relaxation_16 _Saveframe_category NMR_applied_experiment _Experiment_name 'Dz (IzCz) compensated relaxation' _Sample_label $sample_2 save_ save_Dy_(IzCz)_compensated_relaxation_17 _Saveframe_category NMR_applied_experiment _Experiment_name 'Dy (IzCz) compensated relaxation' _Sample_label $sample_2 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details '50 mM KPi pH 7.3' loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.05 . M pH 7.3 . pH pressure 1 . atm temperature 298 . K stop_ save_ save_sample_conditions_2 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 50 . mM pH 7.3 . pH pressure 1 . atm temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details . loop_ _Mol_common_name _Atom_type _Atom_isotope_number _Atom_group _Chem_shift_units _Chem_shift_value _Reference_method _Reference_type _External_reference_sample_geometry _External_reference_location _External_reference_axis _Indirect_shift_ratio DSS C 13 'methyl protons' ppm 0.00 na indirect . . . 0.251449530 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na indirect . . . 0.101329118 DSS P 31 'methyl protons' ppm 0.00 na indirect . . . 0.404808636 stop_ save_ ################################### # Assigned chemical shift lists # ################################### ################################################################### # Chemical Shift Ambiguity Index Value Definitions # # # # The values other than 1 are used for those atoms with different # # chemical shifts that cannot be assigned to stereospecific atoms # # or to specific residues or chains. # # # # Index Value Definition # # # # 1 Unique (including isolated methyl protons, # # geminal atoms, and geminal methyl # # groups with identical chemical shifts) # # (e.g. ILE HD11, HD12, HD13 protons) # # 2 Ambiguity of geminal atoms or geminal methyl # # proton groups (e.g. ASP HB2 and HB3 # # protons, LEU CD1 and CD2 carbons, or # # LEU HD11, HD12, HD13 and HD21, HD22, # # HD23 methyl protons) # # 3 Aromatic atoms on opposite sides of # # symmetrical rings (e.g. TYR HE1 and HE2 # # protons) # # 4 Intraresidue ambiguities (e.g. LYS HG and # # HD protons or TRP HZ2 and HZ3 protons) # # 5 Interresidue ambiguities (LYS 12 vs. LYS 27) # # 6 Intermolecular ambiguities (e.g. ASP 31 CA # # in monomer 1 and ASP 31 CA in monomer 2 # # of an asymmetrical homodimer, duplex # # DNA assignments, or other assignments # # that may apply to atoms in one or more # # molecule in the molecular assembly) # # 9 Ambiguous, specific ambiguity not defined # # # ################################################################### save_assigned_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '3D CBCA(CO)NH' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name HBPd24r _Text_data_format . _Text_data . loop_ _Atom_shift_assign_ID _Residue_author_seq_code _Residue_seq_code _Residue_label _Atom_name _Atom_type _Chem_shift_value _Chem_shift_value_error _Chem_shift_ambiguity_code 1 3 5 PRO CA C 62.111 0.3 . 2 3 5 PRO CB C 31.283 0.3 . 3 4 6 ASP H H 8.497000 0.03 . 4 4 6 ASP CA C 56.749 0.3 . 5 4 6 ASP CB C 40.252 0.3 . 6 4 6 ASP N N 121.534000 0.3 . 7 5 7 TRP H H 6.142000 0.03 . 8 5 7 TRP CA C 54.102 0.3 . 9 5 7 TRP CB C 28.643 0.3 . 10 5 7 TRP N N 110.754000 0.3 . 11 6 8 ALA H H 7.292000 0.03 . 12 6 8 ALA HB H 0.752000 0.03 . 13 6 8 ALA CA C 51.528 0.3 . 14 6 8 ALA CB C 15.415 0.3 . 15 6 8 ALA N N 130.922000 0.3 . 16 7 9 ASP H H 7.757000 0.03 . 17 7 9 ASP CA C 52.751 0.3 . 18 7 9 ASP CB C 42.115 0.3 . 19 7 9 ASP N N 124.687000 0.3 . 20 8 10 GLU H H 8.960000 0.03 . 21 8 10 GLU CA C 60.34 0.3 . 22 8 10 GLU CB C 28.687 0.3 . 23 8 10 GLU N N 128.733000 0.3 . 24 9 11 ALA H H 8.228000 0.03 . 25 9 11 ALA HB H 1.381000 0.03 . 26 9 11 ALA CA C 55.006 0.3 . 27 9 11 ALA CB C 18.007 0.3 . 28 9 11 ALA N N 122.046000 0.3 . 29 10 12 ALA H H 7.600000 0.03 . 30 10 12 ALA HB H 1.277000 0.03 . 31 10 12 ALA CA C 54.362 0.3 . 32 10 12 ALA CB C 19.653 0.3 . 33 10 12 ALA N N 117.900000 0.3 . 34 11 13 ASN H H 8.517000 0.03 . 35 11 13 ASN CA C 53.925 0.3 . 36 11 13 ASN CB C 41.941 0.3 . 37 11 13 ASN N N 112.240000 0.3 . 38 12 14 GLY H H 8.686000 0.03 . 39 12 14 GLY CA C 48.678 0.3 . 40 12 14 GLY N N 111.464000 0.3 . 41 13 15 ALA H H 8.454000 0.03 . 42 13 15 ALA HB H 1.221000 0.03 . 43 13 15 ALA CA C 54.369 0.3 . 44 13 15 ALA CB C 18.173 0.3 . 45 13 15 ALA N N 122.599000 0.3 . 46 14 16 HIS H H 8.113000 0.03 . 47 14 16 HIS CA C 53.322 0.3 . 48 14 16 HIS CB C 29.776 0.3 . 49 14 16 HIS N N 113.744000 0.3 . 50 15 17 GLN H H 7.619000 0.03 . 51 15 17 GLN CA C 53.814 0.3 . 52 15 17 GLN CB C 29.684 0.3 . 53 15 17 GLN N N 119.675000 0.3 . 54 16 18 ASP H H 8.290000 0.03 . 55 16 18 ASP CA C 53.322 0.3 . 56 16 18 ASP CB C 40.705 0.3 . 57 16 18 ASP N N 121.562000 0.3 . 58 17 19 ALA H H 8.344000 0.03 . 59 17 19 ALA HB H 1.246000 0.03 . 60 17 19 ALA CA C 55.265 0.3 . 61 17 19 ALA CB C 20.482 0.3 . 62 17 19 ALA N N 127.557000 0.3 . 63 18 20 TRP H H 9.168000 0.03 . 64 18 20 TRP CA C 58.239 0.3 . 65 18 20 TRP CB C 30.776 0.3 . 66 18 20 TRP N N 119.128000 0.3 . 67 19 21 LYS CA C 59.902 0.3 . 68 19 21 LYS CB C 32.537 0.3 . 69 20 22 SER H H 7.273000 0.03 . 70 20 22 SER CA C 62.335 0.3 . 71 20 22 SER CB C 62.335 0.3 . 72 20 22 SER N N 113.957000 0.3 . 73 21 23 LEU H H 8.314000 0.03 . 74 21 23 LEU HD1 H 0.160000 0.03 . 75 21 23 LEU HD2 H -0.301000 0.03 . 76 21 23 LEU CA C 57.801 0.3 . 77 21 23 LEU CB C 40.553 0.3 . 78 21 23 LEU CD1 C 23.439 0.3 . 79 21 23 LEU CD2 C 22.12 0.3 . 80 21 23 LEU N N 122.978000 0.3 . 81 22 24 LYS H H 7.594000 0.03 . 82 22 24 LYS CA C 59.45 0.3 . 83 22 24 LYS CB C 30.679 0.3 . 84 22 24 LYS N N 116.265000 0.3 . 85 23 25 ALA H H 7.577000 0.03 . 86 23 25 ALA HB H 1.581000 0.03 . 87 23 25 ALA CA C 54.932 0.3 . 88 23 25 ALA CB C 18.492 0.3 . 89 23 25 ALA N N 123.011000 0.3 . 90 24 26 ARG H H 6.940000 0.03 . 91 24 26 ARG CA C 57.024 0.3 . 92 24 26 ARG CB C 28.96 0.3 . 93 24 26 ARG N N 115.724000 0.3 . 94 25 27 VAL H H 7.597000 0.03 . 95 25 27 VAL HG1 H 0.683000 0.03 . 96 25 27 VAL HG2 H 0.822000 0.03 . 97 25 27 VAL CA C 63.402 0.3 . 98 25 27 VAL CB C 31.821 0.3 . 99 25 27 VAL CG1 C 22.875 0.3 . 100 25 27 VAL CG2 C 21.033 0.3 . 101 25 27 VAL N N 119.961000 0.3 . 102 26 28 GLU H H 7.051000 0.03 . 103 26 28 GLU CA C 57.07 0.3 . 104 26 28 GLU CB C 31.206 0.3 . 105 26 28 GLU N N 116.593000 0.3 . 106 27 29 ASN H H 7.716000 0.03 . 107 27 29 ASN CA C 52.364 0.3 . 108 27 29 ASN CB C 43.747 0.3 . 109 27 29 ASN N N 115.377000 0.3 . 110 28 30 VAL H H 7.839000 0.03 . 111 28 30 VAL HG1 H 0.830000 0.03 . 112 28 30 VAL HG2 H 0.082000 0.03 . 113 28 30 VAL CA C 62.367 0.3 . 114 28 30 VAL CB C 32.263 0.3 . 115 28 30 VAL CG1 C 22.455 0.3 . 116 28 30 VAL CG2 C 20.55 0.3 . 117 28 30 VAL N N 119.077000 0.3 . 118 29 31 TYR H H 8.535000 0.03 . 119 29 31 TYR CA C 57.105 0.3 . 120 29 31 TYR CB C 41.955 0.3 . 121 29 31 TYR N N 125.254000 0.3 . 122 30 32 TYR H H 9.036000 0.03 . 123 30 32 TYR CA C 56.449 0.3 . 124 30 32 TYR CB C 40.472 0.3 . 125 30 32 TYR N N 120.390000 0.3 . 126 31 33 MET H H 8.723000 0.03 . 127 31 33 MET CA C 54.66 0.3 . 128 31 33 MET CB C 31.919 0.3 . 129 31 33 MET N N 125.579000 0.3 . 130 32 34 VAL H H 8.592000 0.03 . 131 32 34 VAL HG1 H 1.048000 0.03 . 132 32 34 VAL HG2 H 0.873000 0.03 . 133 32 34 VAL CA C 63.426 0.3 . 134 32 34 VAL CB C 31.919 0.3 . 135 32 34 VAL CG1 C 22.999 0.3 . 136 32 34 VAL CG2 C 20.216 0.3 . 137 32 34 VAL N N 121.425000 0.3 . 138 33 35 LYS H H 7.440000 0.03 . 139 33 35 LYS CA C 54.462 0.3 . 140 33 35 LYS CB C 39.686 0.3 . 141 33 35 LYS N N 117.788000 0.3 . 142 34 36 ALA H H 8.533000 0.03 . 143 34 36 ALA HB H 1.430000 0.03 . 144 34 36 ALA CA C 51.518 0.3 . 145 34 36 ALA CB C 23.675 0.3 . 146 34 36 ALA N N 118.377000 0.3 . 147 35 37 THR H H 8.412000 0.03 . 148 35 37 THR HG2 H 1.311000 0.03 . 149 35 37 THR CA C 61.041 0.3 . 150 35 37 THR CB C 69.505 0.3 . 151 35 37 THR CG2 C 22.52 0.3 . 152 35 37 THR N N 105.176000 0.3 . 153 36 38 TYR H H 7.064000 0.03 . 154 36 38 TYR CA C 54.842 0.3 . 155 36 38 TYR CB C 40.516 0.3 . 156 36 38 TYR N N 116.520000 0.3 . 157 37 39 LYS H H 8.941000 0.03 . 158 37 39 LYS CA C 59.014 0.3 . 159 37 39 LYS CB C 35.093 0.3 . 160 37 39 LYS N N 120.620000 0.3 . 161 38 40 ASN H H 8.343000 0.03 . 162 38 40 ASN CA C 51.664 0.3 . 163 38 40 ASN CB C 41.595 0.3 . 164 38 40 ASN N N 115.615000 0.3 . 165 39 41 ASP H H 8.844000 0.03 . 166 39 41 ASP CA C 51.201 0.3 . 167 39 41 ASP CB C 48.582 0.3 . 168 39 41 ASP N N 122.652000 0.3 . 169 40 42 PRO CA C 65.065 0.3 . 170 40 42 PRO CB C 32.539 0.3 . 171 41 43 VAL H H 7.902000 0.03 . 172 41 43 VAL HG1 H 0.385000 0.03 . 173 41 43 VAL HG2 H 0.418000 0.03 . 174 41 43 VAL CA C 63.645 0.3 . 175 41 43 VAL CB C 32.313 0.3 . 176 41 43 VAL CG1 C 20.98 0.3 . 177 41 43 VAL CG2 C 19.867 0.3 . 178 41 43 VAL N N 116.843000 0.3 . 179 42 44 TRP H H 8.753000 0.03 . 180 42 44 TRP CA C 56.672 0.3 . 181 42 44 TRP CB C 27.255 0.3 . 182 42 44 TRP N N 120.725000 0.3 . 183 43 45 GLY CA C 44.16 0.3 . 184 44 46 ASN H H 8.839000 0.03 . 185 44 46 ASN CA C 52.893 0.3 . 186 44 46 ASN CB C 38.737 0.3 . 187 44 46 ASN N N 118.105000 0.3 . 188 45 47 ASP H H 8.645000 0.03 . 189 45 47 ASP CA C 55.231 0.3 . 190 45 47 ASP CB C 38.977 0.3 . 191 45 47 ASP N N 122.876000 0.3 . 192 46 48 PHE H H 6.985000 0.03 . 193 46 48 PHE CA C 57.625 0.3 . 194 46 48 PHE CB C 39.436 0.3 . 195 46 48 PHE N N 113.395000 0.3 . 196 47 49 THR H H 9.128000 0.03 . 197 47 49 THR HG2 H 1.081000 0.03 . 198 47 49 THR CA C 60.13 0.3 . 199 47 49 THR CB C 73.466 0.3 . 200 47 49 THR CG2 C 20.45 0.3 . 201 47 49 THR N N 111.153000 0.3 . 202 48 50 CYS CA C 55.086 0.3 . 203 48 50 CYS CB C 35.155 0.3 . 204 49 51 VAL H H 6.060000 0.03 . 205 49 51 VAL HG1 H 0.174000 0.03 . 206 49 51 VAL HG2 H -0.003000 0.03 . 207 49 51 VAL CA C 62.092 0.3 . 208 49 51 VAL CB C 31.827 0.3 . 209 49 51 VAL CG1 C 21.663 0.3 . 210 49 51 VAL CG2 C 20.935 0.3 . 211 49 51 VAL N N 115.065000 0.3 . 212 50 52 GLY H H 8.920000 0.03 . 213 50 52 GLY CA C 44.384 0.3 . 214 50 52 GLY N N 115.790000 0.3 . 215 51 53 VAL H H 9.223000 0.03 . 216 51 53 VAL HG1 H -0.157000 0.03 . 217 51 53 VAL HG2 H 0.609000 0.03 . 218 51 53 VAL CA C 58.721 0.3 . 219 51 53 VAL CB C 35.871 0.3 . 220 51 53 VAL CG1 C 23.07 0.3 . 221 51 53 VAL CG2 C 20.787 0.3 . 222 51 53 VAL N N 118.850000 0.3 . 223 52 54 MET H H 8.239000 0.03 . 224 52 54 MET CA C 54.461 0.3 . 225 52 54 MET CB C 36.54 0.3 . 226 52 54 MET N N 123.623000 0.3 . 227 53 55 ALA H H 8.094000 0.03 . 228 53 55 ALA HB H 0.969000 0.03 . 229 53 55 ALA CA C 50.771 0.3 . 230 53 55 ALA CB C 23.88 0.3 . 231 53 55 ALA N N 124.715000 0.3 . 232 54 56 ASN H H 8.964000 0.03 . 233 54 56 ASN CA C 52.646 0.3 . 234 54 56 ASN CB C 41.0 0.3 . 235 54 56 ASN N N 117.040000 0.3 . 236 55 57 ASP H H 8.178000 0.03 . 237 55 57 ASP CA C 54.406 0.3 . 238 55 57 ASP CB C 40.478 0.3 . 239 55 57 ASP N N 117.184000 0.3 . 240 56 58 VAL H H 8.298000 0.03 . 241 56 58 VAL HG1 H 0.965000 0.03 . 242 56 58 VAL HG2 H 0.924000 0.03 . 243 56 58 VAL CA C 62.197 0.3 . 244 56 58 VAL CB C 34.065 0.3 . 245 56 58 VAL CG1 C 20.651 0.3 . 246 56 58 VAL CG2 C 22.757 0.3 . 247 56 58 VAL N N 119.385000 0.3 . 248 57 59 ASN H H 9.224000 0.03 . 249 57 59 ASN CA C 51.66 0.3 . 250 57 59 ASN CB C 38.746 0.3 . 251 57 59 ASN N N 126.808000 0.3 . 252 58 60 GLU H H 9.131000 0.03 . 253 58 60 GLU CA C 59.248 0.3 . 254 58 60 GLU CB C 29.751 0.3 . 255 58 60 GLU N N 124.463000 0.3 . 256 59 61 ASP H H 8.111000 0.03 . 257 59 61 ASP CA C 57.092 0.3 . 258 59 61 ASP CB C 40.6 0.3 . 259 59 61 ASP N N 118.271000 0.3 . 260 60 62 GLU H H 7.249000 0.03 . 261 60 62 GLU CA C 55.44 0.3 . 262 60 62 GLU CB C 30.838 0.3 . 263 60 62 GLU N N 116.476000 0.3 . 264 61 63 LYS H H 7.370000 0.03 . 265 61 63 LYS CA C 56.566 0.3 . 266 61 63 LYS CB C 30.327 0.3 . 267 61 63 LYS N N 115.479000 0.3 . 268 62 64 SER H H 7.832000 0.03 . 269 62 64 SER CA C 54.95 0.3 . 270 62 64 SER CB C 69.397 0.3 . 271 62 64 SER N N 110.668000 0.3 . 272 63 65 ILE H H 9.126000 0.03 . 273 63 65 ILE HG2 H 0.683000 0.03 . 274 63 65 ILE HD1 H 0.364000 0.03 . 275 63 65 ILE CA C 59.403 0.3 . 276 63 65 ILE CB C 42.56 0.3 . 277 63 65 ILE CG2 C 18.742 0.3 . 278 63 65 ILE CD1 C 14.677 0.3 . 279 63 65 ILE N N 111.781000 0.3 . 280 64 66 GLN H H 8.026000 0.03 . 281 64 66 GLN CA C 55.424 0.3 . 282 64 66 GLN CB C 29.782 0.3 . 283 64 66 GLN N N 119.873000 0.3 . 284 65 67 ALA H H 9.354000 0.03 . 285 65 67 ALA HB H 0.683000 0.03 . 286 65 67 ALA CA C 50.834 0.3 . 287 65 67 ALA CB C 22.261 0.3 . 288 65 67 ALA N N 129.253000 0.3 . 289 66 68 GLU H H 8.792000 0.03 . 290 66 68 GLU CA C 55.203 0.3 . 291 66 68 GLU CB C 31.397 0.3 . 292 66 68 GLU N N 122.443000 0.3 . 293 67 69 PHE H H 9.797000 0.03 . 294 67 69 PHE CA C 56.84 0.3 . 295 67 69 PHE CB C 42.637 0.3 . 296 67 69 PHE N N 123.589000 0.3 . 297 68 70 LEU H H 8.701000 0.03 . 298 68 70 LEU HD1 H 0.995000 0.03 . 299 68 70 LEU HD2 H 0.944000 0.03 . 300 68 70 LEU CA C 53.67 0.3 . 301 68 70 LEU CB C 44.678 0.3 . 302 68 70 LEU CD1 C 25.836 0.3 . 303 68 70 LEU CD2 C 25.699 0.3 . 304 68 70 LEU N N 121.578000 0.3 . 305 69 71 PHE H H 7.950000 0.03 . 306 69 71 PHE CA C 57.065 0.3 . 307 69 71 PHE CB C 40.406 0.3 . 308 69 71 PHE N N 112.602000 0.3 . 309 70 72 MET H H 8.481000 0.03 . 310 70 72 MET CA C 54.232 0.3 . 311 70 72 MET CB C 37.113 0.3 . 312 70 72 MET N N 116.674000 0.3 . 313 71 73 ASN H H 8.594000 0.03 . 314 71 73 ASN CA C 53.27 0.3 . 315 71 73 ASN CB C 38.773 0.3 . 316 71 73 ASN N N 115.742000 0.3 . 317 72 74 ASN H H 7.936000 0.03 . 318 72 74 ASN CA C 53.663 0.3 . 319 72 74 ASN CB C 38.248 0.3 . 320 72 74 ASN N N 111.834000 0.3 . 321 73 75 ALA H H 8.808000 0.03 . 322 73 75 ALA HB H 1.450000 0.03 . 323 73 75 ALA CA C 52.998 0.3 . 324 73 75 ALA CB C 19.452 0.3 . 325 73 75 ALA N N 122.780000 0.3 . 326 74 76 ASP H H 7.745000 0.03 . 327 74 76 ASP CA C 53.569 0.3 . 328 74 76 ASP CB C 43.929 0.3 . 329 74 76 ASP N N 117.400000 0.3 . 330 75 77 THR H H 8.385000 0.03 . 331 75 77 THR HG2 H 1.141000 0.03 . 332 75 77 THR CA C 62.467 0.3 . 333 75 77 THR CB C 68.774 0.3 . 334 75 77 THR CG2 C 21.78 0.3 . 335 75 77 THR N N 114.768000 0.3 . 336 76 78 ASN H H 8.300000 0.03 . 337 76 78 ASN CA C 52.412 0.3 . 338 76 78 ASN CB C 40.54 0.3 . 339 76 78 ASN N N 119.643000 0.3 . 340 77 79 MET H H 8.555000 0.03 . 341 77 79 MET CA C 56.354 0.3 . 342 77 79 MET CB C 40.46 0.3 . 343 77 79 MET N N 121.941000 0.3 . 344 78 80 GLN H H 8.723000 0.03 . 345 78 80 GLN CA C 54.145 0.3 . 346 78 80 GLN CB C 31.661 0.3 . 347 78 80 GLN N N 125.579000 0.3 . 348 79 81 PHE H H 7.795000 0.03 . 349 79 81 PHE CA C 55.925 0.3 . 350 79 81 PHE CB C 43.418 0.3 . 351 79 81 PHE N N 114.710000 0.3 . 352 80 82 ALA H H 8.739000 0.03 . 353 80 82 ALA HB H 1.682000 0.03 . 354 80 82 ALA CA C 52.363 0.3 . 355 80 82 ALA CB C 23.521 0.3 . 356 80 82 ALA N N 123.667000 0.3 . 357 81 83 THR H H 8.898000 0.03 . 358 81 83 THR HG2 H 1.215000 0.03 . 359 81 83 THR CA C 60.79 0.3 . 360 81 83 THR CB C 70.727 0.3 . 361 81 83 THR CG2 C 21.237 0.3 . 362 81 83 THR N N 116.815000 0.3 . 363 82 84 GLU H H 9.414000 0.03 . 364 82 84 GLU CA C 54.898 0.3 . 365 82 84 GLU CB C 33.882 0.3 . 366 82 84 GLU N N 125.356000 0.3 . 367 83 85 LYS H H 8.209000 0.03 . 368 83 85 LYS CA C 55.806 0.3 . 369 83 85 LYS CB C 34.229 0.3 . 370 83 85 LYS N N 124.041000 0.3 . 371 84 86 VAL H H 8.847000 0.03 . 372 84 86 VAL HG1 H -0.148000 0.03 . 373 84 86 VAL HG2 H 0.720000 0.03 . 374 84 86 VAL CA C 60.38 0.3 . 375 84 86 VAL CB C 33.162 0.3 . 376 84 86 VAL CG1 C 22.93 0.3 . 377 84 86 VAL CG2 C 22.008 0.3 . 378 84 86 VAL N N 125.878000 0.3 . 379 85 87 THR H H 8.682000 0.03 . 380 85 87 THR CA C 60.694 0.3 . 381 85 87 THR CB C 71.552 0.3 . 382 85 87 THR N N 122.367000 0.3 . 383 86 88 ALA H H 8.978000 0.03 . 384 86 88 ALA HB H 1.374000 0.03 . 385 86 88 ALA CA C 51.075 0.3 . 386 86 88 ALA CB C 18.079 0.3 . 387 86 88 ALA N N 129.706000 0.3 . 388 87 89 VAL H H 8.642000 0.03 . 389 87 89 VAL HG1 H 0.354000 0.03 . 390 87 89 VAL HG2 H 0.507000 0.03 . 391 87 89 VAL CA C 59.346 0.3 . 392 87 89 VAL CB C 36.328 0.3 . 393 87 89 VAL CG1 C 21.848 0.3 . 394 87 89 VAL CG2 C 19.088 0.3 . 395 87 89 VAL N N 115.774000 0.3 . 396 88 90 LYS H H 8.447000 0.03 . 397 88 90 LYS CA C 56.095 0.3 . 398 88 90 LYS CB C 33.938 0.3 . 399 88 90 LYS N N 118.823000 0.3 . 400 89 91 MET H H 9.890000 0.03 . 401 89 91 MET CA C 53.26 0.3 . 402 89 91 MET CB C 36.57 0.3 . 403 89 91 MET N N 124.667000 0.3 . 404 90 92 TYR H H 8.983000 0.03 . 405 90 92 TYR CA C 56.713 0.3 . 406 90 92 TYR CB C 34.749 0.3 . 407 90 92 TYR N N 115.071000 0.3 . 408 91 93 GLY H H 8.899000 0.03 . 409 91 93 GLY CA C 45.827 0.3 . 410 91 93 GLY N N 105.123000 0.3 . 411 92 94 TYR H H 7.448000 0.03 . 412 92 94 TYR CA C 58.96 0.3 . 413 92 94 TYR CB C 38.306 0.3 . 414 92 94 TYR N N 123.483000 0.3 . 415 93 95 ASN H H 11.194000 0.03 . 416 93 95 ASN CA C 54.879 0.3 . 417 93 95 ASN CB C 39.869 0.3 . 418 93 95 ASN N N 120.090000 0.3 . 419 94 96 ARG H H 8.642000 0.03 . 420 94 96 ARG CA C 55.335 0.3 . 421 94 96 ARG CB C 31.662 0.3 . 422 94 96 ARG N N 122.241000 0.3 . 423 95 97 GLU H H 10.040000 0.03 . 424 95 97 GLU CA C 62.47 0.3 . 425 95 97 GLU CB C 29.199 0.3 . 426 95 97 GLU N N 124.511000 0.3 . 427 96 98 ASN H H 9.384000 0.03 . 428 96 98 ASN CA C 53.464 0.3 . 429 96 98 ASN CB C 37.992 0.3 . 430 96 98 ASN N N 123.258000 0.3 . 431 97 99 ALA H H 8.667000 0.03 . 432 97 99 ALA HB H 0.979000 0.03 . 433 97 99 ALA CA C 50.872 0.3 . 434 97 99 ALA CB C 23.82 0.3 . 435 97 99 ALA N N 125.155000 0.3 . 436 98 100 PHE H H 9.277000 0.03 . 437 98 100 PHE CA C 51.819 0.3 . 438 98 100 PHE CB C 40.983 0.3 . 439 98 100 PHE N N 119.911000 0.3 . 440 99 101 ARG H H 9.519000 0.03 . 441 99 101 ARG CA C 54.326 0.3 . 442 99 101 ARG CB C 32.412 0.3 . 443 99 101 ARG N N 123.384000 0.3 . 444 100 102 TYR H H 10.405000 0.03 . 445 100 102 TYR CA C 57.152 0.3 . 446 100 102 TYR CB C 39.453 0.3 . 447 100 102 TYR N N 130.824000 0.3 . 448 101 103 GLU H H 9.543000 0.03 . 449 101 103 GLU CA C 54.662 0.3 . 450 101 103 GLU CB C 33.087 0.3 . 451 101 103 GLU N N 120.818000 0.3 . 452 102 104 THR H H 8.909000 0.03 . 453 102 104 THR HG2 H 1.174000 0.03 . 454 102 104 THR CA C 60.844 0.3 . 455 102 104 THR CB C 70.727 0.3 . 456 102 104 THR CG2 C 22.943 0.3 . 457 102 104 THR N N 116.544000 0.3 . 458 103 105 GLU H H 9.924000 0.03 . 459 103 105 GLU CA C 59.227 0.3 . 460 103 105 GLU CB C 29.596 0.3 . 461 103 105 GLU N N 122.629000 0.3 . 462 104 106 ASP H H 8.221000 0.03 . 463 104 106 ASP CA C 52.968 0.3 . 464 104 106 ASP CB C 39.982 0.3 . 465 104 106 ASP N N 114.084000 0.3 . 466 105 107 GLY H H 7.728000 0.03 . 467 105 107 GLY CA C 46.081 0.3 . 468 105 107 GLY N N 107.562000 0.3 . 469 106 108 GLN H H 7.841000 0.03 . 470 106 108 GLN CA C 55.883 0.3 . 471 106 108 GLN CB C 30.18 0.3 . 472 106 108 GLN N N 120.247000 0.3 . 473 107 109 VAL H H 7.534000 0.03 . 474 107 109 VAL HG2 H 0.664000 0.03 . 475 107 109 VAL CA C 60.298 0.3 . 476 107 109 VAL CB C 34.655 0.3 . 477 107 109 VAL CG2 C 21.209 0.3 . 478 107 109 VAL N N 121.832000 0.3 . 479 108 110 PHE H H 8.641000 0.03 . 480 108 110 PHE CA C 55.62 0.3 . 481 108 110 PHE CB C 41.84 0.3 . 482 108 110 PHE N N 124.356000 0.3 . 483 109 111 THR H H 8.931000 0.03 . 484 109 111 THR HG2 H 0.856000 0.03 . 485 109 111 THR CA C 61.864 0.3 . 486 109 111 THR CB C 68.54 0.3 . 487 109 111 THR CG2 C 21.112 0.3 . 488 109 111 THR N N 121.090000 0.3 . 489 110 112 ASP H H 8.885000 0.03 . 490 110 112 ASP CA C 52.794 0.3 . 491 110 112 ASP CB C 44.095 0.3 . 492 110 112 ASP N N 127.738000 0.3 . 493 111 113 VAL H H 9.597000 0.03 . 494 111 113 VAL HG2 H 0.853000 0.03 . 495 111 113 VAL CA C 62.326 0.3 . 496 111 113 VAL CB C 36.101 0.3 . 497 111 113 VAL CG2 C 21.752 0.3 . 498 111 113 VAL N N 119.709000 0.3 . 499 112 114 ILE H H 9.136000 0.03 . 500 112 114 ILE HG2 H 0.578000 0.03 . 501 112 114 ILE HD1 H -0.093000 0.03 . 502 112 114 ILE CA C 60.652 0.3 . 503 112 114 ILE CB C 35.491 0.3 . 504 112 114 ILE CG2 C 19.334 0.3 . 505 112 114 ILE CD1 C 9.692 0.3 . 506 112 114 ILE N N 126.054000 0.3 . 507 113 115 ALA H H 8.599000 0.03 . 508 113 115 ALA HB H 0.074000 0.03 . 509 113 115 ALA CA C 53.222 0.3 . 510 113 115 ALA CB C 17.953 0.3 . 511 113 115 ALA N N 132.60 0.3 . 512 114 116 TYR H H 8.050000 0.03 . 513 114 116 TYR CA C 59.23 0.3 . 514 114 116 TYR CB C 41.783 0.3 . 515 114 116 TYR N N 118.429000 0.3 . 516 115 117 SER H H 8.495000 0.03 . 517 115 117 SER CA C 57.105 0.3 . 518 115 117 SER CB C 64.285 0.3 . 519 115 117 SER N N 124.899000 0.3 . 520 116 118 ASP H H 9.017000 0.03 . 521 116 118 ASP CA C 52.772 0.3 . 522 116 118 ASP CB C 44.48 0.3 . 523 116 118 ASP N N 127.713000 0.3 . 524 117 119 ASP H H 8.951000 0.03 . 525 117 119 ASP CA C 57.26 0.3 . 526 117 119 ASP CB C 40.287 0.3 . 527 117 119 ASP N N 119.667000 0.3 . 528 118 120 ASN H H 8.325000 0.03 . 529 118 120 ASN CA C 52.913 0.3 . 530 118 120 ASN CB C 38.543 0.3 . 531 118 120 ASN N N 111.979000 0.3 . 532 119 121 CYS H H 8.006000 0.03 . 533 119 121 CYS CA C 54.986 0.3 . 534 119 121 CYS CB C 46.311 0.3 . 535 119 121 CYS N N 116.098000 0.3 . 536 120 122 ASP H H 9.695000 0.03 . 537 120 122 ASP CA C 53.746 0.3 . 538 120 122 ASP CB C 47.878 0.3 . 539 120 122 ASP N N 119.030000 0.3 . 540 121 123 VAL H H 10.072000 0.03 . 541 121 123 VAL HG1 H 1.221000 0.03 . 542 121 123 VAL HG2 H 1.239000 0.03 . 543 121 123 VAL CA C 62.322 0.3 . 544 121 123 VAL CB C 32.318 0.3 . 545 121 123 VAL CG1 C 22.732 0.3 . 546 121 123 VAL CG2 C 21.876 0.3 . 547 121 123 VAL N N 123.437000 0.3 . 548 122 124 ILE H H 9.622000 0.03 . 549 122 124 ILE HG2 H 0.894000 0.03 . 550 122 124 ILE HD1 H 0.295000 0.03 . 551 122 124 ILE CA C 61.17 0.3 . 552 122 124 ILE CB C 41.442 0.3 . 553 122 124 ILE CG2 C 18.535 0.3 . 554 122 124 ILE CD1 C 12.578 0.3 . 555 122 124 ILE N N 129.523000 0.3 . 556 123 125 TYR H H 10.140000 0.03 . 557 123 125 TYR CA C 54.971 0.3 . 558 123 125 TYR CB C 41.426 0.3 . 559 123 125 TYR N N 128.833000 0.3 . 560 124 126 VAL H H 8.814000 0.03 . 561 124 126 VAL HG2 H 0.656000 0.03 . 562 124 126 VAL CA C 58.251 0.3 . 563 124 126 VAL CB C 32.313 0.3 . 564 124 126 VAL CG2 C 20.894 0.3 . 565 124 126 VAL N N 131.115000 0.3 . 566 125 127 PRO CA C 64.174 0.3 . 567 125 127 PRO CB C 32.528 0.3 . 568 126 128 GLY H H 7.676000 0.03 . 569 126 128 GLY CA C 45.641 0.3 . 570 126 128 GLY N N 104.060000 0.3 . 571 127 129 THR H H 8.357000 0.03 . 572 127 129 THR HG2 H 1.011000 0.03 . 573 127 129 THR CA C 61.539 0.3 . 574 127 129 THR CB C 68.765 0.3 . 575 127 129 THR CG2 C 21.612 0.3 . 576 127 129 THR N N 109.591000 0.3 . 577 128 130 ASP CA C 54.143 0.3 . 578 128 130 ASP CB C 42.039 0.3 . 579 129 131 GLY H H 8.097000 0.03 . 580 129 131 GLY CA C 45.71 0.3 . 581 129 131 GLY N N 107.436000 0.3 . 582 130 132 ASN H H 8.270000 0.03 . 583 130 132 ASN CA C 50.392 0.3 . 584 130 132 ASN CB C 38.224 0.3 . 585 130 132 ASN N N 117.802000 0.3 . 586 131 133 GLU CA C 55.489 0.3 . 587 131 133 GLU CB C 31.433 0.3 . 588 132 134 GLU H H 8.294000 0.03 . 589 132 134 GLU CA C 54.803 0.3 . 590 132 134 GLU CB C 29.934 0.3 . 591 132 134 GLU N N 124.096000 0.3 . 592 133 135 GLY H H 8.770000 0.03 . 593 133 135 GLY CA C 46.214 0.3 . 594 133 135 GLY N N 112.682000 0.3 . 595 134 136 TYR H H 9.096000 0.03 . 596 134 136 TYR CA C 57.439 0.3 . 597 134 136 TYR CB C 45.107 0.3 . 598 134 136 TYR N N 115.140000 0.3 . 599 135 137 GLU H H 10.052000 0.03 . 600 135 137 GLU CA C 54.619 0.3 . 601 135 137 GLU CB C 36.179 0.3 . 602 135 137 GLU N N 117.832000 0.3 . 603 136 138 LEU H H 8.525000 0.03 . 604 136 138 LEU HD1 H 0.523000 0.03 . 605 136 138 LEU HD2 H 0.683000 0.03 . 606 136 138 LEU CA C 54.32 0.3 . 607 136 138 LEU CB C 44.765 0.3 . 608 136 138 LEU CD1 C 25.782 0.3 . 609 136 138 LEU CD2 C 25.366 0.3 . 610 136 138 LEU N N 124.285000 0.3 . 611 137 139 TRP H H 9.985000 0.03 . 612 137 139 TRP CA C 54.855 0.3 . 613 137 139 TRP CB C 32.041 0.3 . 614 137 139 TRP N N 127.558000 0.3 . 615 138 140 THR H H 9.821000 0.03 . 616 138 140 THR CA C 59.88 0.3 . 617 138 140 THR CB C 69.844 0.3 . 618 138 140 THR N N 114.539000 0.3 . 619 139 141 THR H H 7.353000 0.03 . 620 139 141 THR CA C 62.497 0.3 . 621 139 141 THR CB C 68.649 0.3 . 622 139 141 THR N N 113.923000 0.3 . 623 140 142 ASP H H 7.836000 0.03 . 624 140 142 ASP CA C 52.81 0.3 . 625 140 142 ASP CB C 41.615 0.3 . 626 140 142 ASP N N 122.982000 0.3 . 627 141 143 TYR H H 6.451000 0.03 . 628 141 143 TYR CA C 57.515 0.3 . 629 141 143 TYR CB C 37.28 0.3 . 630 141 143 TYR N N 118.296000 0.3 . 631 142 144 ASP H H 7.744000 0.03 . 632 142 144 ASP CA C 54.331 0.3 . 633 142 144 ASP CB C 42.157 0.3 . 634 142 144 ASP N N 121.410000 0.3 . 635 143 145 ASN H H 7.229000 0.03 . 636 143 145 ASN CA C 51.667 0.3 . 637 143 145 ASN CB C 38.925 0.3 . 638 143 145 ASN N N 120.053000 0.3 . 639 144 146 ILE H H 8.543000 0.03 . 640 144 146 ILE HG2 H 0.808000 0.03 . 641 144 146 ILE HD1 H 0.801000 0.03 . 642 144 146 ILE CA C 60.187 0.3 . 643 144 146 ILE CB C 32.358 0.3 . 644 144 146 ILE CG2 C 18.415 0.3 . 645 144 146 ILE CD1 C 13.939 0.3 . 646 144 146 ILE N N 124.881000 0.3 . 647 145 147 PRO CA C 63.814 0.3 . 648 145 147 PRO CB C 33.019 0.3 . 649 146 148 ALA H H 8.719000 0.03 . 650 146 148 ALA HB H 1.350000 0.03 . 651 146 148 ALA CA C 55.504 0.3 . 652 146 148 ALA CB C 18.644 0.3 . 653 146 148 ALA N N 128.515000 0.3 . 654 147 149 ASN H H 9.165000 0.03 . 655 147 149 ASN CA C 56.205 0.3 . 656 147 149 ASN CB C 36.88 0.3 . 657 147 149 ASN N N 114.712000 0.3 . 658 148 150 CYS H H 7.455000 0.03 . 659 148 150 CYS CA C 59.281 0.3 . 660 148 150 CYS CB C 46.546 0.3 . 661 148 150 CYS N N 114.314000 0.3 . 662 149 151 LEU H H 8.011000 0.03 . 663 149 151 LEU HD1 H 0.772000 0.03 . 664 149 151 LEU HD2 H 0.732000 0.03 . 665 149 151 LEU CA C 58.479 0.3 . 666 149 151 LEU CB C 41.671 0.3 . 667 149 151 LEU CD1 C 25.536 0.3 . 668 149 151 LEU CD2 C 23.04 0.3 . 669 149 151 LEU N N 121.781000 0.3 . 670 150 152 ASN H H 8.669000 0.03 . 671 150 152 ASN CA C 55.963 0.3 . 672 150 152 ASN CB C 37.322 0.3 . 673 150 152 ASN N N 115.910000 0.3 . 674 151 153 LYS H H 7.179000 0.03 . 675 151 153 LYS CA C 57.364 0.3 . 676 151 153 LYS CB C 31.247 0.3 . 677 151 153 LYS N N 119.447000 0.3 . 678 152 154 PHE H H 8.338000 0.03 . 679 152 154 PHE CA C 57.364 0.3 . 680 152 154 PHE CB C 39.445 0.3 . 681 152 154 PHE N N 118.921000 0.3 . 682 153 155 ASN H H 8.476000 0.03 . 683 153 155 ASN CA C 55.209 0.3 . 684 153 155 ASN CB C 37.431 0.3 . 685 153 155 ASN N N 115.548000 0.3 . 686 154 156 GLU H H 7.733000 0.03 . 687 154 156 GLU CA C 58.765 0.3 . 688 154 156 GLU CB C 29.561 0.3 . 689 154 156 GLU N N 120.482000 0.3 . 690 155 157 TYR H H 8.012000 0.03 . 691 155 157 TYR CA C 56.22 0.3 . 692 155 157 TYR CB C 35.305 0.3 . 693 155 157 TYR N N 118.162000 0.3 . 694 156 158 ALA H H 8.142000 0.03 . 695 156 158 ALA HB H 0.488000 0.03 . 696 156 158 ALA CA C 51.736 0.3 . 697 156 158 ALA CB C 17.213 0.3 . 698 156 158 ALA N N 120.098000 0.3 . 699 157 159 VAL H H 6.482000 0.03 . 700 157 159 VAL HG1 H 1.000000 0.03 . 701 157 159 VAL HG2 H 0.927000 0.03 . 702 157 159 VAL CA C 63.233 0.3 . 703 157 159 VAL CB C 31.715 0.3 . 704 157 159 VAL CG1 C 21.141 0.3 . 705 157 159 VAL CG2 C 19.573 0.3 . 706 157 159 VAL N N 118.571000 0.3 . 707 158 160 GLY H H 8.959000 0.03 . 708 158 160 GLY CA C 45.231 0.3 . 709 158 160 GLY N N 115.166000 0.3 . 710 159 161 ARG H H 7.842000 0.03 . 711 159 161 ARG CA C 54.505 0.3 . 712 159 161 ARG CB C 31.509 0.3 . 713 159 161 ARG N N 118.967000 0.3 . 714 160 162 GLU H H 8.928000 0.03 . 715 160 162 GLU CA C 56.173 0.3 . 716 160 162 GLU CB C 30.04 0.3 . 717 160 162 GLU N N 123.446000 0.3 . 718 161 163 THR H H 8.271000 0.03 . 719 161 163 THR CA C 62.155 0.3 . 720 161 163 THR CB C 70.436 0.3 . 721 161 163 THR N N 117.130000 0.3 . 722 162 164 ARG H H 8.900000 0.03 . 723 162 164 ARG CA C 53.496 0.3 . 724 162 164 ARG CB C 33.057 0.3 . 725 162 164 ARG N N 122.562000 0.3 . 726 163 165 ASP H H 8.443000 0.03 . 727 163 165 ASP CA C 54.06 0.3 . 728 163 165 ASP CB C 41.32 0.3 . 729 163 165 ASP N N 121.096000 0.3 . 730 164 166 VAL H H 7.642000 0.03 . 731 164 166 VAL HG1 H 1.063000 0.03 . 732 164 166 VAL HG2 H 0.482000 0.03 . 733 164 166 VAL CA C 64.558 0.3 . 734 164 166 VAL CB C 32.447 0.3 . 735 164 166 VAL CG1 C 22.358 0.3 . 736 164 166 VAL CG2 C 20.857 0.3 . 737 164 166 VAL N N 122.818000 0.3 . 738 165 167 PHE H H 9.109000 0.03 . 739 165 167 PHE CA C 58.45 0.3 . 740 165 167 PHE CB C 40.184 0.3 . 741 165 167 PHE N N 126.219000 0.3 . 742 166 168 THR H H 6.591000 0.03 . 743 166 168 THR CA C 59.105 0.3 . 744 166 168 THR CB C 72.847 0.3 . 745 166 168 THR N N 117.641000 0.3 . 746 167 169 SER H H 9.169000 0.03 . 747 167 169 SER CA C 61.075 0.3 . 748 167 169 SER CB C 62.348 0.3 . 749 167 169 SER N N 115.486000 0.3 . 750 168 170 ALA H H 7.500000 0.03 . 751 168 170 ALA HB H 1.143000 0.03 . 752 168 170 ALA CA C 54.04 0.3 . 753 168 170 ALA CB C 18.223 0.3 . 754 168 170 ALA N N 124.267000 0.3 . 755 169 171 CYS H H 7.621000 0.03 . 756 169 171 CYS CA C 56.724 0.3 . 757 169 171 CYS CB C 40.182 0.3 . 758 169 171 CYS N N 114.217000 0.3 . 759 170 172 LEU H H 7.200000 0.03 . 760 170 172 LEU HD1 H 0.860000 0.03 . 761 170 172 LEU HD2 H 0.824000 0.03 . 762 170 172 LEU CA C 54.233 0.3 . 763 170 172 LEU CB C 42.486 0.3 . 764 170 172 LEU CD1 C 25.379 0.3 . 765 170 172 LEU CD2 C 22.662 0.3 . 766 170 172 LEU N N 117.889000 0.3 . 767 171 173 GLU H H 7.348000 0.03 . 768 171 173 GLU CA C 58.228 0.3 . 769 171 173 GLU CB C 31.031 0.3 . 770 171 173 GLU N N 125.482000 0.3 . stop_ save_ save_order_parameter_1 _Saveframe_category S2_parameters _Details ; In all experiments used for backbone amide and sidechain order parameters for the free protein, the data was collected on the Bruker Avance 500MHz and repeated on the Bruker Avance 750MHz spectrometer. ; loop_ _Software_label $Felix stop_ loop_ _Sample_label $sample_2 stop_ _Sample_conditions_label $sample_conditions_1 _Mol_system_component_name HBPd24r _Tau_e_value_units . _Tau_s_value_units . _Text_data_format . _Text_data . loop_ _Residue_seq_code _Residue_label _Atom_name _Model_fit _S2_value _S2_value_fit_error _Tau_e_value _Tau_e_value_fit_error _S2f_value _S2f_value_fit_error _S2s_value _S2s_value_fit_error _Tau_s_value _Tau_s_value_fit_error _S2H_value _S2H_value_fit_error _S2N_value _S2N_value_fit_error 8 ALA N . 0.928 0.004 2.00E-12 8.66E-12 . . . . . . . . . . 9 ASP N . 0.638 0.005 6.98E-11 8.09E-12 . . . . . . . . . . 11 ALA N . 0.861 0.003 1.68E-12 5.87E-12 . . . . . . . . . . 12 ALA N . 0.848 0.002 3.42E-11 1.84E-11 . . . . . . . . . . 13 ASN N . 0.836 0.005 3.74E-12 9.51E-12 . . . . . . . . . . 14 GLY N . 0.874 0.007 0.00E+00 0.00E+00 . . . . . . . . . . 15 ALA N . 0.869 0.008 1.36E-11 1.94E-11 . . . . . . . . . . 16 HIS N . 0.810 0.005 1.33E-11 1.64E-11 . . . . . . . . . . 17 GLN N . 0.853 0.004 0.00E+00 0.00E+00 . . . . . . . . . . 18 ASP N . 0.820 0.004 4.56E-11 1.78E-11 . . . . . . . . . . 20 TRP N . 0.871 0.003 2.80E-13 3.09E-12 . . . . . . . . . . 21 LYS N . 0.903 0.004 0.00E+00 0.00E+00 . . . . . . . . . . 22 SER N . 0.909 0.005 1.01E-11 1.79E-11 . . . . . . . . . . 23 LEU N . 0.923 0.004 0.00E+00 0.00E+00 . . . . . . . . . . 24 LYS N . 0.891 0.004 0.00E+00 0.00E+00 . . . . . . . . . . 25 ALA N . 0.927 0.003 1.46E-11 2.42E-11 . . . . . . . . . . 26 ARG N . 0.852 0.004 0.00E+00 0.00E+00 . . . . . . . . . . 27 VAL N . 0.920 0.004 4.46E-12 1.41E-11 . . . . . . . . . . 28 GLU N . 0.848 0.004 2.36E-10 2.24E-11 . . . . . . . . . . 29 ASN N . 0.795 0.004 1.42E-10 1.67E-11 . . . . . . . . . . 30 VAL N . 0.779 0.002 7.88E-11 1.39E-11 . . . . . . . . . . 31 TYR N . 0.764 0.005 2.00E-14 4.47E-13 . . . . . . . . . . 32 TYR N . 0.878 0.006 5.10E-12 1.75E-11 . . . . . . . . . . 33 MET N . 0.863 0.006 4.00E-14 8.94E-13 . . . . . . . . . . 34 VAL N . 0.948 0.005 0.00E+00 0.00E+00 . . . . . . . . . . 35 LYS N . 0.914 0.004 0.00E+00 0.00E+00 . . . . . . . . . . 36 ALA N . 0.849 0.004 0.00E+00 0.00E+00 . . . . . . . . . . 37 THR N . 0.829 0.004 0.00E+00 0.00E+00 . . . . . . . . . . 39 LYS N . 0.815 0.006 6.81E-11 2.99E-11 . . . . . . . . . . 40 ASN N . 0.832 0.003 6.62E-12 1.18E-11 . . . . . . . . . . 41 ASP N . 0.878 0.004 1.71E-10 3.93E-11 . . . . . . . . . . 43 VAL N . 0.838 0.005 1.82E-12 6.43E-12 . . . . . . . . . . 44 TRP N . 0.843 0.006 4.00E-14 8.94E-13 . . . . . . . . . . 45 GLY N . 0.900 0.006 0.00E+00 0.00E+00 . . . . . . . . . . 46 ASN N . 0.821 0.004 2.38E-11 1.97E-11 . . . . . . . . . . 47 ASP N . 0.883 0.007 1.96E-12 7.87E-12 . . . . . . . . . . 48 PHE N . 0.843 0.004 2.04E-12 6.32E-12 . . . . . . . . . . 50 CYS N . 0.845 0.005 0.00E+00 0.00E+00 . . . . . . . . . . 51 VAL N . 0.822 0.003 2.66E-11 2.15E-11 . . . . . . . . . . 52 GLY N . 0.892 0.004 1.64E-12 7.84E-12 . . . . . . . . . . 53 VAL N . 0.891 0.004 3.86E-12 1.36E-11 . . . . . . . . . . 54 MET N . 0.878 0.004 8.76E-11 4.06E-11 . . . . . . . . . . 56 ASN N . 0.800 0.005 2.62E-10 2.41E-11 . . . . . . . . . . 58 VAL N . 0.758 0.002 1.30E-10 9.20E-12 . . . . . . . . . . 59 ASN N . 0.859 0.006 1.90E-11 2.60E-11 . . . . . . . . . . 60 GLU N . 0.772 0.007 3.29E-11 1.69E-11 . . . . . . . . . . 61 ASP N . 0.803 0.004 1.45E-10 1.27E-11 . . . . . . . . . . 62 GLU N . 0.832 0.003 9.97E-11 1.97E-11 . . . . . . . . . . 63 LYS N . 0.849 0.003 1.52E-10 3.24E-11 . . . . . . . . . . 64 SER N . 0.890 0.004 4.94E-11 3.48E-11 . . . . . . . . . . 65 ILE N . 0.871 0.006 2.58E-11 3.32E-11 . . . . . . . . . . 66 GLN N . 0.740 0.003 1.38E-10 1.20E-11 . . . . . . . . . . 67 ALA N . 0.855 0.005 4.48E-11 3.35E-11 . . . . . . . . . . 68 GLU N . 0.821 0.003 1.27E-11 1.48E-11 . . . . . . . . . . 69 PHE N . 0.839 0.005 7.75E-11 3.52E-11 . . . . . . . . . . 70 LEU N . 0.846 0.006 3.62E-11 2.96E-11 . . . . . . . . . . 71 PHE N . 0.861 0.003 1.07E-10 2.73E-11 . . . . . . . . . . 72 MET N . 0.875 0.005 8.54E-12 1.83E-11 . . . . . . . . . . 73 ASN N . 0.871 0.003 4.65E-11 2.89E-11 . . . . . . . . . . 74 ASN N . 0.799 0.005 2.33E-10 1.89E-11 . . . . . . . . . . 75 ALA N . 0.892 0.005 6.30E-12 1.76E-11 . . . . . . . . . . 76 ASP N . 0.742 0.003 1.07E-10 1.39E-11 . . . . . . . . . . 78 ASN N . 0.758 0.004 1.49E-10 1.20E-11 . . . . . . . . . . 79 MET N . 0.781 0.004 1.22E-10 1.52E-11 . . . . . . . . . . 80 GLN N . 0.836 0.008 4.72E-11 3.39E-11 . . . . . . . . . . 82 ALA N . 0.830 0.004 3.26E-12 9.47E-12 . . . . . . . . . . 83 THR N . 0.803 0.003 5.44E-11 2.13E-11 . . . . . . . . . . 84 GLU N . 0.842 0.006 1.58E-11 2.23E-11 . . . . . . . . . . 85 LYS N . 0.839 0.004 4.20E-12 1.08E-11 . . . . . . . . . . 87 THR N . 0.821 0.005 8.12E-12 1.43E-11 . . . . . . . . . . 89 VAL N . 0.783 0.004 4.24E-12 9.13E-12 . . . . . . . . . . 90 LYS N . 0.837 0.004 2.26E-11 2.32E-11 . . . . . . . . . . 91 MET N . 0.794 0.008 3.20E-13 2.81E-12 . . . . . . . . . . 92 TYR N . 0.798 0.004 6.09E-11 1.40E-11 . . . . . . . . . . 93 GLY N . 0.822 0.007 3.32E-12 9.25E-12 . . . . . . . . . . 94 TYR N . 0.871 0.005 0.00E+00 0.00E+00 . . . . . . . . . . 95 ASN N . 0.781 0.005 0.00E+00 0.00E+00 . . . . . . . . . . 97 GLU N . 0.809 0.004 1.60E-11 1.53E-11 . . . . . . . . . . 98 ASN N . 0.804 0.005 4.00E-14 6.32E-13 . . . . . . . . . . 99 ALA N . 0.896 0.006 4.40E-13 3.50E-12 . . . . . . . . . . 100 PHE N . 0.826 0.004 1.37E-11 1.76E-11 . . . . . . . . . . 101 ARG N . 0.834 0.004 1.48E-12 6.19E-12 . . . . . . . . . . 103 GLU N . 0.792 0.006 2.24E-11 1.89E-11 . . . . . . . . . . 104 THR N . 0.857 0.002 0.00E+00 0.00E+00 . . . . . . . . . . 105 GLU N . 0.851 0.004 1.04E-10 3.03E-11 . . . . . . . . . . 106 ASP N . 0.764 0.004 1.64E-10 1.74E-11 . . . . . . . . . . 107 GLY N . 0.806 0.003 2.03E-11 1.69E-11 . . . . . . . . . . 108 GLN N . 0.827 0.004 1.16E-10 2.34E-11 . . . . . . . . . . 109 VAL N . 0.789 0.002 1.36E-10 1.72E-11 . . . . . . . . . . 110 PHE N . 0.835 0.006 9.08E-12 1.70E-11 . . . . . . . . . . 111 THR N . 0.812 0.007 1.51E-11 1.91E-11 . . . . . . . . . . 113 VAL N . 0.826 0.005 0.00E+00 0.00E+00 . . . . . . . . . . 114 ILE N . 0.849 0.006 6.56E-11 3.14E-11 . . . . . . . . . . 115 ALA N . 0.959 0.008 0.00E+00 0.00E+00 . . . . . . . . . . 116 TYR N . 0.838 0.004 0.00E+00 0.00E+00 . . . . . . . . . . 119 ASP N . 0.771 0.010 1.06E-10 3.85E-11 . . . . . . . . . . 120 ASN N . 0.767 0.003 1.70E-11 1.80E-11 . . . . . . . . . . 122 ASP N . 0.831 0.007 5.28E-12 1.30E-11 . . . . . . . . . . 123 VAL N . 0.833 0.005 1.40E-13 1.61E-12 . . . . . . . . . . 124 ILE N . 0.861 0.007 1.00E-13 1.84E-12 . . . . . . . . . . 126 VAL N . 0.881 0.005 0.00E+00 0.00E+00 . . . . . . . . . . 128 GLY N . 0.829 0.006 6.00E-14 7.73E-13 . . . . . . . . . . 130 ASP N . 0.792 0.006 8.19E-11 3.02E-11 . . . . . . . . . . 131 GLY N . 0.746 0.005 9.88E-11 1.48E-11 . . . . . . . . . . 132 ASN N . 0.768 0.004 2.68E-11 1.48E-11 . . . . . . . . . . 134 GLU N . 0.800 0.005 5.23E-11 1.93E-11 . . . . . . . . . . 135 GLY N . 0.909 0.007 0.00E+00 0.00E+00 . . . . . . . . . . 136 TYR N . 0.806 0.004 5.54E-12 1.16E-11 . . . . . . . . . . 137 GLU N . 0.829 0.005 0.00E+00 0.00E+00 . . . . . . . . . . 140 THR N . 0.868 0.005 0.00E+00 0.00E+00 . . . . . . . . . . 141 THR N . 0.827 0.007 9.23E-11 2.91E-11 . . . . . . . . . . 142 ASP N . 0.805 0.003 2.44E-10 1.92E-11 . . . . . . . . . . 143 TYR N . 0.773 0.003 7.68E-11 1.40E-11 . . . . . . . . . . 144 ASP N . 0.867 0.005 1.01E-10 3.29E-11 . . . . . . . . . . 148 ALA N . 0.805 0.005 1.36E-11 1.47E-11 . . . . . . . . . . 150 CYS N . 0.773 0.011 8.06E-11 2.11E-11 . . . . . . . . . . 151 LEU N . 0.914 0.006 0.00E+00 0.00E+00 . . . . . . . . . . 152 ASN N . 0.884 0.003 2.22E-12 6.68E-12 . . . . . . . . . . 154 PHE N . 0.929 0.004 7.48E-12 2.41E-11 . . . . . . . . . . 155 ASN N . 0.893 0.003 2.12E-11 2.53E-11 . . . . . . . . . . 156 GLU N . 0.881 0.003 0.00E+00 0.00E+00 . . . . . . . . . . 157 TYR N . 0.859 0.003 4.99E-11 2.88E-11 . . . . . . . . . . 158 ALA N . 0.887 0.003 6.46E-12 1.48E-11 . . . . . . . . . . 159 VAL N . 0.809 0.003 5.53E-11 1.24E-11 . . . . . . . . . . 161 ARG N . 0.781 0.002 9.21E-11 8.01E-12 . . . . . . . . . . 162 GLU N . 0.650 0.006 1.55E-10 1.31E-11 . . . . . . . . . . 164 ARG N . 0.888 0.005 5.00E-12 1.32E-11 . . . . . . . . . . 165 ASP N . 0.830 0.004 1.54E-11 1.63E-11 . . . . . . . . . . 166 VAL N . 0.768 0.004 2.88E-11 2.01E-11 . . . . . . . . . . 167 PHE N . 0.838 0.005 1.47E-10 3.53E-11 . . . . . . . . . . 168 THR N . 0.797 0.004 7.35E-11 1.83E-11 . . . . . . . . . . 170 ALA N . 0.796 0.007 8.43E-11 1.92E-11 . . . . . . . . . . 171 CYS N . 0.855 0.004 1.94E-10 2.47E-11 . . . . . . . . . . stop_ save_ save_order_parameter_2 _Saveframe_category S2_parameters _Details ; In all experiments used for backbone amide and sidechain order parameters for the free protein, the data was collected on the Bruker Avance 500MHz and repeated on the Bruker Avance 750MHz spectrometer. ; loop_ _Software_label $Felix stop_ loop_ _Sample_label $sample_2 stop_ _Sample_conditions_label $sample_conditions_1 _Mol_system_component_name HBPd24r _Tau_e_value_units . _Tau_s_value_units . _Text_data_format . _Text_data . loop_ _Residue_seq_code _Residue_label _Atom_name _Model_fit _S2_value _S2_value_fit_error _Tau_e_value _Tau_e_value_fit_error _S2f_value _S2f_value_fit_error _S2s_value _S2s_value_fit_error _Tau_s_value _Tau_s_value_fit_error _S2H_value _S2H_value_fit_error _S2N_value _S2N_value_fit_error 8 ALA CB . 0.870 0.017 4.93E-10 1.21E-11 . . . . . . . . . . 12 ALA CB . 0.445 0.041 4.75E-10 9.15E-12 . . . . . . . . . . 15 ALA CB . 0.848 0.009 4.42E-10 6.03E-12 . . . . . . . . . . 19 ALA CB . 0.762 0.028 5.40E-10 1.21E-11 . . . . . . . . . . 23 LEU CD1 . 0.647 0.016 5.89E-10 1.57E-11 . . . . . . . . . . 23 LEU CD2 . 0.670 0.023 4.63E-10 1.73E-11 . . . . . . . . . . 25 ALA CB . 0.898 0.014 5.05E-10 9.87E-12 . . . . . . . . . . 27 VAL CG1 . 0.649 0.006 5.12E-10 6.81E-12 . . . . . . . . . . 27 VAL CG2 . 0.643 0.006 5.34E-10 6.54E-12 . . . . . . . . . . 30 VAL CG1 . 0.605 0.006 2.92E-10 5.21E-12 . . . . . . . . . . 30 VAL CG2 . 0.670 0.013 1.13E-09 1.98E-11 . . . . . . . . . . 33 MET CE . 0.580 0.004 9.24E-11 4.28E-12 . . . . . . . . . . 34 VAL CG1 . 0.658 0.015 8.75E-10 1.93E-11 . . . . . . . . . . 34 VAL CG2 . 0.457 0.015 4.41E-10 7.77E-12 . . . . . . . . . . 36 ALA CB . 0.846 0.024 1.10E-09 5.12E-11 . . . . . . . . . . 37 THR CG2 . 0.863 0.022 5.13E-10 2.36E-11 . . . . . . . . . . 43 VAL CG1 . 0.802 0.015 4.21E-10 8.91E-12 . . . . . . . . . . 43 VAL CG2 . 0.821 0.019 6.49E-10 1.46E-11 . . . . . . . . . . 49 THR CG2 . 0.877 0.020 1.30E-09 3.06E-11 . . . . . . . . . . 51 VAL CG1 . 0.803 0.021 2.14E-10 1.11E-11 . . . . . . . . . . 51 VAL CG2 . 0.777 0.018 5.63E-10 2.52E-11 . . . . . . . . . . 53 VAL CG1 . 0.885 0.062 1.22E-09 9.20E-11 . . . . . . . . . . 53 VAL CG2 . 0.886 0.030 9.81E-10 4.19E-11 . . . . . . . . . . 54 MET CE . 0.127 0.001 7.00E-11 0.00E+00 . . . . . . . . . . 55 ALA CB . 0.875 0.014 6.14E-10 1.58E-11 . . . . . . . . . . 58 VAL CG1 . 0.271 0.013 4.26E-10 6.25E-12 . . . . . . . . . . 58 VAL CG2 . 0.419 0.004 5.36E-10 6.17E-12 . . . . . . . . . . 65 ILE CG2 . 0.848 0.025 3.35E-10 7.61E-12 . . . . . . . . . . 65 ILE CD1 . 0.598 0.010 2.87E-10 1.02E-11 . . . . . . . . . . 67 ALA CB . 0.871 0.013 3.32E-10 1.07E-11 . . . . . . . . . . 70 LEU CD1 . 0.194 0.006 2.97E-10 5.06E-12 . . . . . . . . . . 70 LEU CD2 . 0.080 0.002 3.02E-10 4.25E-12 . . . . . . . . . . 72 MET CE . 0.105 0.002 1.00E-10 0.00E+00 . . . . . . . . . . 75 ALA CB . 0.637 0.012 3.24E-10 4.86E-12 . . . . . . . . . . 77 THR CG2 . 0.507 0.004 3.99E-10 3.48E-12 . . . . . . . . . . 79 MET CE . 0.028 0.014 5.25E-11 2.19E-11 . . . . . . . . . . 82 ALA CB . 0.873 0.013 4.77E-10 8.52E-12 . . . . . . . . . . 83 THR CG2 . 0.543 0.006 5.20E-10 5.45E-12 . . . . . . . . . . 86 VAL CG1 . 0.912 0.023 9.14E-10 2.66E-11 . . . . . . . . . . 86 VAL CG2 . 0.771 0.032 1.19E-09 5.42E-11 . . . . . . . . . . 87 THR CG2 . 0.820 0.016 6.59E-10 1.40E-11 . . . . . . . . . . 88 ALA CB . 0.954 0.009 4.01E-10 5.91E-12 . . . . . . . . . . 89 VAL CG1 . 0.871 0.014 1.22E-09 1.36E-11 . . . . . . . . . . 89 VAL CG2 . 0.814 0.012 8.22E-10 2.61E-11 . . . . . . . . . . 91 MET CE . 0.119 0.001 1.10E-10 0.00E+00 . . . . . . . . . . 99 ALA CB . 0.941 0.011 3.26E-10 1.20E-11 . . . . . . . . . . 109 VAL CG2 . 0.595 0.005 6.22E-10 6.04E-12 . . . . . . . . . . 111 THR CG2 . 0.713 0.012 2.03E-10 6.48E-12 . . . . . . . . . . 113 VAL CG2 . 0.488 0.022 4.60E-10 1.07E-11 . . . . . . . . . . 114 ILE CG2 . 0.798 0.021 7.69E-10 2.89E-11 . . . . . . . . . . 114 ILE CD1 . 0.253 0.003 1.43E-10 5.71E-12 . . . . . . . . . . 115 ALA CB . 0.876 0.021 5.84E-10 2.24E-11 . . . . . . . . . . 123 VAL CG1 . 0.849 0.009 4.11E-10 1.54E-11 . . . . . . . . . . 123 VAL CG2 . 0.584 0.035 4.19E-10 1.62E-11 . . . . . . . . . . 124 ILE CG2 . 0.746 0.023 7.55E-10 2.39E-11 . . . . . . . . . . 124 ILE CD1 . 0.594 0.011 1.49E-10 8.60E-12 . . . . . . . . . . 126 VAL CG1 . 0.620 0.005 4.67E-10 4.77E-12 . . . . . . . . . . 126 VAL CG2 . 0.818 0.022 2.62E-10 1.97E-11 . . . . . . . . . . 129 THR CG2 . 0.347 0.002 6.26E-10 5.04E-12 . . . . . . . . . . 138 LEU CD1 . 0.511 0.008 4.93E-10 1.05E-11 . . . . . . . . . . 138 LEU CD2 . 0.532 0.008 4.45E-10 9.02E-12 . . . . . . . . . . 140 THR CG2 . 0.562 0.010 4.40E-10 7.69E-12 . . . . . . . . . . 141 THR CG2 . 0.802 0.021 9.92E-10 3.66E-11 . . . . . . . . . . 146 ILE CG2 . 0.835 0.015 5.89E-10 2.05E-11 . . . . . . . . . . 146 ILE CD1 . 0.629 0.007 2.15E-10 5.75E-12 . . . . . . . . . . 148 ALA CB . 0.880 0.010 5.22E-10 6.20E-12 . . . . . . . . . . 151 LEU CD1 . 0.494 0.009 4.39E-10 7.16E-12 . . . . . . . . . . 151 LEU CD2 . 0.515 0.005 3.64E-10 5.33E-12 . . . . . . . . . . 158 ALA CB . 0.944 0.011 4.72E-10 9.29E-12 . . . . . . . . . . 159 VAL CG1 . 0.655 0.011 4.12E-10 7.52E-12 . . . . . . . . . . 159 VAL CG2 . 0.309 0.003 5.33E-10 4.66E-12 . . . . . . . . . . 163 THR CG2 . 0.435 0.007 8.27E-10 9.02E-12 . . . . . . . . . . 166 VAL CG1 . 0.860 0.025 6.42E-10 2.24E-11 . . . . . . . . . . 166 VAL CG2 . 0.833 0.013 4.25E-10 1.68E-11 . . . . . . . . . . 170 ALA CB . 0.775 0.008 4.42E-10 5.36E-12 . . . . . . . . . . 172 LEU CD1 . 0.278 0.004 4.64E-10 4.96E-12 . . . . . . . . . . 172 LEU CD2 . 0.304 0.002 3.41E-10 2.38E-12 . . . . . . . . . . stop_ save_