data_25728 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 13C, and 15N Chemical Shift Assignments for Histamine-Binding Protein (D24R) apo ; _BMRB_accession_number 25728 _BMRB_flat_file_name bmr25728.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" 217 "13C chemical shifts" 360 "15N chemical shifts" 151 "order parameters" 211 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2017-06-27 original BMRB . stop_ loop_ _Related_BMRB_accession_number _Relationship 25727 'HBPd24r (bound to histamine)' 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 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label HBPd24r $HBPd24r_mutant 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_HBPd24r_mutant _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common HBPd24r_mutant _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_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $HBPd24r_mutant '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 $HBPd24r_mutant '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 $HBPd24r_mutant 1.0 mM '[U-99% 13C; U-99% 15N]' 'potassium phosphate' 50 mM 'natural abundance' D2O 10 % 'natural abundance' 'sodium azide' 0.02 % [U-2H] H2O 95 % 'natural 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 $HBPd24r_mutant 1.5 mM '[U-99% 15N]' $HBPd24r_mutant 1.5 mM '[U-99% 13C; U-55% 2H]' D2O 5 % [U-2H] 'potassium phosphate' 50 mM 'natural abundance' 'sodium azide' 0.02 % '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 'peak picking' 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 750 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 500 _Details . 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_aliphatic_12 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC aliphatic' _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 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 61.935 0.3 . 2 3 5 PRO CB C 31.335 0.3 . 3 4 6 ASP CA C 56.758 0.3 . 4 4 6 ASP CB C 40.333 0.3 . 5 5 7 TRP H H 6.139000 0.03 . 6 5 7 TRP CA C 54.055 0.3 . 7 5 7 TRP CB C 28.601 0.3 . 8 5 7 TRP N N 110.709000 0.3 . 9 6 8 ALA H H 7.292000 0.03 . 10 6 8 ALA HB H 0.747000 0.03 . 11 6 8 ALA CA C 51.528 0.3 . 12 6 8 ALA CB C 15.446 0.3 . 13 6 8 ALA N N 130.912000 0.3 . 14 9 11 ALA H H 8.269000 0.03 . 15 9 11 ALA HB H 1.381000 0.03 . 16 9 11 ALA CA C 54.375 0.3 . 17 9 11 ALA CB C 18.032 0.3 . 18 9 11 ALA N N 121.745000 0.3 . 19 10 12 ALA H H 7.601000 0.03 . 20 10 12 ALA HB H 1.276000 0.03 . 21 10 12 ALA CA C 53.895 0.3 . 22 10 12 ALA CB C 19.673 0.3 . 23 10 12 ALA N N 117.875000 0.3 . 24 11 13 ASN H H 8.515000 0.03 . 25 11 13 ASN CA C 53.738 0.3 . 26 11 13 ASN CB C 41.937 0.3 . 27 11 13 ASN N N 112.189000 0.3 . 28 12 14 GLY H H 8.681000 0.03 . 29 12 14 GLY CA C 48.664 0.3 . 30 12 14 GLY N N 111.403000 0.3 . 31 13 15 ALA H H 8.451000 0.03 . 32 13 15 ALA HB H 1.221000 0.03 . 33 13 15 ALA CA C 54.572 0.3 . 34 13 15 ALA CB C 18.188 0.3 . 35 13 15 ALA N N 122.521000 0.3 . 36 14 16 HIS H H 8.106000 0.03 . 37 14 16 HIS CA C 54.572 0.3 . 38 14 16 HIS CB C 29.831 0.3 . 39 14 16 HIS N N 113.719000 0.3 . 40 15 17 GLN H H 7.620000 0.03 . 41 15 17 GLN CA C 53.74 0.3 . 42 15 17 GLN CB C 28.526 0.3 . 43 15 17 GLN N N 119.642000 0.3 . 44 16 18 ASP H H 8.281000 0.03 . 45 16 18 ASP CA C 53.363 0.3 . 46 16 18 ASP CB C 40.68 0.3 . 47 16 18 ASP N N 121.165000 0.3 . 48 17 19 ALA H H 8.336000 0.03 . 49 17 19 ALA HB H 1.225000 0.03 . 50 17 19 ALA CA C 55.245 0.3 . 51 17 19 ALA CB C 20.475 0.3 . 52 17 19 ALA N N 127.472000 0.3 . 53 19 21 LYS CA C 59.866 0.3 . 54 19 21 LYS CB C 32.537 0.3 . 55 20 22 SER H H 7.246000 0.03 . 56 20 22 SER CA C 62.324 0.3 . 57 20 22 SER CB C 62.324 0.3 . 58 20 22 SER N N 113.739000 0.3 . 59 21 23 LEU H H 8.326000 0.03 . 60 21 23 LEU HD1 H 0.141000 0.03 . 61 21 23 LEU HD2 H -0.281000 0.03 . 62 21 23 LEU CA C 57.752 0.3 . 63 21 23 LEU CB C 40.537 0.3 . 64 21 23 LEU CD1 C 23.377 0.3 . 65 21 23 LEU CD2 C 22.184 0.3 . 66 21 23 LEU N N 122.874000 0.3 . 67 22 24 LYS H H 7.580000 0.03 . 68 22 24 LYS CA C 59.428 0.3 . 69 22 24 LYS CB C 30.738 0.3 . 70 22 24 LYS N N 116.170000 0.3 . 71 23 25 ALA H H 7.553000 0.03 . 72 23 25 ALA HB H 1.570000 0.03 . 73 23 25 ALA CA C 54.941 0.3 . 74 23 25 ALA CB C 18.522 0.3 . 75 23 25 ALA N N 122.870000 0.3 . 76 24 26 ARG H H 6.926000 0.03 . 77 24 26 ARG CA C 57.002 0.3 . 78 24 26 ARG CB C 28.76 0.3 . 79 24 26 ARG N N 115.751000 0.3 . 80 25 27 VAL H H 7.566000 0.03 . 81 25 27 VAL HG1 H 0.822000 0.03 . 82 25 27 VAL HG2 H 0.670000 0.03 . 83 25 27 VAL CA C 63.271 0.3 . 84 25 27 VAL CB C 31.814 0.3 . 85 25 27 VAL CG1 C 21.046 0.3 . 86 25 27 VAL CG2 C 22.783 0.3 . 87 25 27 VAL N N 119.555000 0.3 . 88 26 28 GLU H H 7.027000 0.03 . 89 26 28 GLU CA C 57.049 0.3 . 90 26 28 GLU CB C 31.169 0.3 . 91 26 28 GLU N N 116.531000 0.3 . 92 27 29 ASN H H 7.724000 0.03 . 93 27 29 ASN CA C 52.314 0.3 . 94 27 29 ASN CB C 43.904 0.3 . 95 27 29 ASN N N 115.421000 0.3 . 96 28 30 VAL H H 7.853000 0.03 . 97 28 30 VAL HG1 H 0.855000 0.03 . 98 28 30 VAL HG2 H 0.142000 0.03 . 99 28 30 VAL CA C 62.367 0.3 . 100 28 30 VAL CB C 32.403 0.3 . 101 28 30 VAL CG1 C 22.461 0.3 . 102 28 30 VAL CG2 C 20.527 0.3 . 103 28 30 VAL N N 119.071000 0.3 . 104 29 31 TYR H H 8.399000 0.03 . 105 29 31 TYR CA C 57.012 0.3 . 106 29 31 TYR CB C 42.256 0.3 . 107 29 31 TYR N N 124.882000 0.3 . 108 30 32 TYR H H 9.047000 0.03 . 109 30 32 TYR CA C 56.456 0.3 . 110 30 32 TYR CB C 40.572 0.3 . 111 30 32 TYR N N 119.601000 0.3 . 112 32 34 VAL H H 8.577000 0.03 . 113 32 34 VAL HG1 H 1.065000 0.03 . 114 32 34 VAL HG2 H 0.870000 0.03 . 115 32 34 VAL CA C 63.589 0.3 . 116 32 34 VAL CB C 31.865 0.3 . 117 32 34 VAL CG1 C 23.041 0.3 . 118 32 34 VAL CG2 C 20.223 0.3 . 119 32 34 VAL N N 121.521000 0.3 . 120 33 35 LYS H H 7.466000 0.03 . 121 33 35 LYS CA C 54.439 0.3 . 122 33 35 LYS CB C 39.649 0.3 . 123 33 35 LYS N N 117.543000 0.3 . 124 34 36 ALA H H 8.550000 0.03 . 125 34 36 ALA HB H 1.430000 0.03 . 126 34 36 ALA CA C 51.619 0.3 . 127 34 36 ALA CB C 23.517 0.3 . 128 34 36 ALA N N 118.294000 0.3 . 129 35 37 THR H H 8.456000 0.03 . 130 35 37 THR HG2 H 1.315000 0.03 . 131 35 37 THR CA C 61.022 0.3 . 132 35 37 THR CB C 69.498 0.3 . 133 35 37 THR CG2 C 22.51 0.3 . 134 35 37 THR N N 105.214000 0.3 . 135 36 38 TYR H H 7.064000 0.03 . 136 36 38 TYR N N 116.479000 0.3 . 137 37 39 LYS CA C 58.95 0.3 . 138 37 39 LYS CB C 35.07 0.3 . 139 38 40 ASN H H 8.295000 0.03 . 140 38 40 ASN CA C 51.593 0.3 . 141 38 40 ASN CB C 41.747 0.3 . 142 38 40 ASN N N 115.259000 0.3 . 143 39 41 ASP H H 8.786000 0.03 . 144 39 41 ASP CA C 51.368 0.3 . 145 39 41 ASP CB C 48.464 0.3 . 146 39 41 ASP N N 122.614000 0.3 . 147 43 45 GLY CA C 43.665 0.3 . 148 44 46 ASN H H 8.926000 0.03 . 149 44 46 ASN CA C 52.922 0.3 . 150 44 46 ASN CB C 38.496 0.3 . 151 44 46 ASN N N 118.171000 0.3 . 152 45 47 ASP H H 8.620000 0.03 . 153 45 47 ASP CA C 55.192 0.3 . 154 45 47 ASP CB C 38.977 0.3 . 155 45 47 ASP N N 123.620000 0.3 . 156 46 48 PHE H H 6.990000 0.03 . 157 46 48 PHE CA C 57.58 0.3 . 158 46 48 PHE CB C 40.012 0.3 . 159 46 48 PHE N N 113.512000 0.3 . 160 47 49 THR H H 9.184000 0.03 . 161 47 49 THR HG2 H 1.093000 0.03 . 162 47 49 THR CA C 60.234 0.3 . 163 47 49 THR CB C 73.538 0.3 . 164 47 49 THR CG2 C 20.559 0.3 . 165 47 49 THR N N 110.937000 0.3 . 166 48 50 CYS CA C 55.089 0.3 . 167 48 50 CYS CB C 35.188 0.3 . 168 49 51 VAL H H 6.120000 0.03 . 169 49 51 VAL HG1 H 0.262000 0.03 . 170 49 51 VAL HG2 H 0.151000 0.03 . 171 49 51 VAL CA C 61.954 0.3 . 172 49 51 VAL CB C 31.673 0.3 . 173 49 51 VAL CG1 C 21.45 0.3 . 174 49 51 VAL CG2 C 21.154 0.3 . 175 49 51 VAL N N 115.073000 0.3 . 176 50 52 GLY H H 8.962000 0.03 . 177 50 52 GLY CA C 44.421 0.3 . 178 50 52 GLY N N 115.223000 0.3 . 179 51 53 VAL H H 9.210000 0.03 . 180 51 53 VAL HG1 H -0.166000 0.03 . 181 51 53 VAL HG2 H 0.609000 0.03 . 182 51 53 VAL CA C 58.739 0.3 . 183 51 53 VAL CB C 35.726 0.3 . 184 51 53 VAL CG1 C 22.631 0.3 . 185 51 53 VAL CG2 C 20.787 0.3 . 186 51 53 VAL N N 118.333000 0.3 . 187 52 54 MET H H 8.193000 0.03 . 188 52 54 MET CA C 54.552 0.3 . 189 52 54 MET CB C 36.452 0.3 . 190 52 54 MET N N 123.390000 0.3 . 191 53 55 ALA H H 8.087000 0.03 . 192 53 55 ALA HB H 0.969000 0.03 . 193 53 55 ALA CA C 50.752 0.3 . 194 53 55 ALA CB C 23.909 0.3 . 195 53 55 ALA N N 124.793000 0.3 . 196 54 56 ASN H H 8.949000 0.03 . 197 54 56 ASN CA C 52.643 0.3 . 198 54 56 ASN CB C 41.024 0.3 . 199 54 56 ASN N N 116.996000 0.3 . 200 55 57 ASP H H 8.209000 0.03 . 201 55 57 ASP CA C 54.46 0.3 . 202 55 57 ASP CB C 40.478 0.3 . 203 55 57 ASP N N 117.120000 0.3 . 204 56 58 VAL H H 8.290000 0.03 . 205 56 58 VAL CB C 33.865 0.3 . 206 56 58 VAL HG1 H 0.967000 0.03 . 207 56 58 VAL HG2 H 0.924000 0.03 . 208 56 58 VAL CA C 62.197 0.3 . 209 56 58 VAL CG1 C 20.777 0.3 . 210 56 58 VAL CG2 C 22.908 0.3 . 211 56 58 VAL N N 119.385000 0.3 . 212 57 59 ASN H H 9.218000 0.03 . 213 57 59 ASN CA C 51.658 0.3 . 214 57 59 ASN CB C 38.762 0.3 . 215 57 59 ASN N N 126.852000 0.3 . 216 58 60 GLU H H 9.131000 0.03 . 217 58 60 GLU CA C 59.237 0.3 . 218 58 60 GLU CB C 29.726 0.3 . 219 58 60 GLU N N 124.374000 0.3 . 220 59 61 ASP H H 8.108000 0.03 . 221 59 61 ASP CA C 57.087 0.3 . 222 59 61 ASP CB C 40.595 0.3 . 223 59 61 ASP N N 118.239000 0.3 . 224 60 62 GLU H H 7.253000 0.03 . 225 60 62 GLU CA C 55.379 0.3 . 226 60 62 GLU CB C 30.726 0.3 . 227 60 62 GLU N N 116.375000 0.3 . 228 61 63 LYS H H 7.370000 0.03 . 229 61 63 LYS CA C 56.566 0.3 . 230 61 63 LYS CB C 30.362 0.3 . 231 61 63 LYS N N 115.491000 0.3 . 232 62 64 SER H H 7.825000 0.03 . 233 62 64 SER CA C 54.935 0.3 . 234 62 64 SER CB C 69.417 0.3 . 235 62 64 SER N N 110.632000 0.3 . 236 63 65 ILE H H 9.105000 0.03 . 237 63 65 ILE HG2 H 0.672000 0.03 . 238 63 65 ILE HD1 H 0.360000 0.03 . 239 63 65 ILE CA C 59.389 0.3 . 240 63 65 ILE CB C 42.573 0.3 . 241 63 65 ILE CG2 C 18.854 0.3 . 242 63 65 ILE CD1 C 14.653 0.3 . 243 63 65 ILE N N 111.702000 0.3 . 244 64 66 GLN H H 8.053000 0.03 . 245 64 66 GLN CA C 54.994 0.3 . 246 64 66 GLN CB C 29.79 0.3 . 247 64 66 GLN N N 119.783000 0.3 . 248 65 67 ALA H H 9.265000 0.03 . 249 65 67 ALA CA C 50.864 0.3 . 250 65 67 ALA CB C 22.606 0.3 . 251 65 67 ALA N N 129.200000 0.3 . 252 66 68 GLU H H 8.609000 0.03 . 253 66 68 GLU CA C 55.335 0.3 . 254 66 68 GLU CB C 31.418 0.3 . 255 66 68 GLU N N 121.896000 0.3 . 256 67 69 PHE H H 9.804000 0.03 . 257 67 69 PHE CA C 56.797 0.3 . 258 67 69 PHE CB C 42.74 0.3 . 259 67 69 PHE N N 123.751000 0.3 . 260 68 70 LEU H H 8.595000 0.03 . 261 68 70 LEU HD1 H 0.994000 0.03 . 262 68 70 LEU HD2 H 0.945000 0.03 . 263 68 70 LEU CA C 53.52 0.3 . 264 68 70 LEU CB C 44.751 0.3 . 265 68 70 LEU CD1 C 25.75 0.3 . 266 68 70 LEU CD2 C 25.778 0.3 . 267 68 70 LEU N N 121.914000 0.3 . 268 69 71 PHE H H 7.904000 0.03 . 269 69 71 PHE CA C 57.041 0.3 . 270 69 71 PHE CB C 40.59 0.3 . 271 69 71 PHE N N 112.658000 0.3 . 272 70 72 MET H H 8.495000 0.03 . 273 70 72 MET CA C 54.031 0.3 . 274 70 72 MET CB C 36.975 0.3 . 275 70 72 MET N N 116.572000 0.3 . 276 71 73 ASN CA C 53.257 0.3 . 277 71 73 ASN CB C 38.652 0.3 . 278 72 74 ASN H H 7.908000 0.03 . 279 72 74 ASN CA C 53.663 0.3 . 280 72 74 ASN CB C 38.254 0.3 . 281 72 74 ASN N N 111.413000 0.3 . 282 73 75 ALA H H 8.868000 0.03 . 283 73 75 ALA HB H 1.469000 0.03 . 284 73 75 ALA CA C 52.856 0.3 . 285 73 75 ALA CB C 19.489 0.3 . 286 73 75 ALA N N 122.605000 0.3 . 287 74 76 ASP H H 7.721000 0.03 . 288 74 76 ASP CA C 52.976 0.3 . 289 74 76 ASP CB C 44.139 0.3 . 290 74 76 ASP N N 116.801000 0.3 . 291 75 77 THR H H 8.394000 0.03 . 292 75 77 THR HG2 H 1.140000 0.03 . 293 75 77 THR CA C 62.462 0.3 . 294 75 77 THR CB C 68.757 0.3 . 295 75 77 THR CG2 C 21.794 0.3 . 296 75 77 THR N N 114.635000 0.3 . 297 76 78 ASN H H 8.278000 0.03 . 298 76 78 ASN CA C 52.383 0.3 . 299 76 78 ASN CB C 40.537 0.3 . 300 76 78 ASN N N 119.592000 0.3 . 301 77 79 MET H H 8.560000 0.03 . 302 77 79 MET CA C 56.32 0.3 . 303 77 79 MET CB C 40.623 0.3 . 304 77 79 MET N N 121.847000 0.3 . 305 78 80 GLN H H 8.752000 0.03 . 306 78 80 GLN CA C 54.202 0.3 . 307 78 80 GLN CB C 31.78 0.3 . 308 78 80 GLN N N 125.686000 0.3 . 309 79 81 PHE H H 7.791000 0.03 . 310 79 81 PHE CA C 55.987 0.3 . 311 79 81 PHE CB C 43.447 0.3 . 312 79 81 PHE N N 114.563000 0.3 . 313 80 82 ALA H H 8.858000 0.03 . 314 80 82 ALA HB H 1.717000 0.03 . 315 80 82 ALA CA C 52.075 0.3 . 316 80 82 ALA CB C 23.686 0.3 . 317 80 82 ALA N N 123.551000 0.3 . 318 81 83 THR H H 8.952000 0.03 . 319 81 83 THR HG2 H 1.206000 0.03 . 320 81 83 THR CA C 60.742 0.3 . 321 81 83 THR CB C 70.483 0.3 . 322 81 83 THR CG2 C 21.237 0.3 . 323 81 83 THR N N 117.520000 0.3 . 324 82 84 GLU H H 9.368000 0.03 . 325 82 84 GLU CA C 54.901 0.3 . 326 82 84 GLU CB C 33.759 0.3 . 327 82 84 GLU N N 125.007000 0.3 . 328 83 85 LYS H H 8.134000 0.03 . 329 83 85 LYS CA C 55.847 0.3 . 330 83 85 LYS CB C 34.506 0.3 . 331 83 85 LYS N N 124.061000 0.3 . 332 84 86 VAL H H 8.825000 0.03 . 333 84 86 VAL HG1 H -0.148000 0.03 . 334 84 86 VAL HG2 H 0.711000 0.03 . 335 84 86 VAL CA C 60.359 0.3 . 336 84 86 VAL CB C 33.116 0.3 . 337 84 86 VAL CG1 C 22.93 0.3 . 338 84 86 VAL CG2 C 22.008 0.3 . 339 84 86 VAL N N 125.893000 0.3 . 340 85 87 THR H H 8.708000 0.03 . 341 85 87 THR CA C 60.666 0.3 . 342 85 87 THR CB C 71.552 0.3 . 343 85 87 THR N N 122.301000 0.3 . 344 86 88 ALA H H 9.011000 0.03 . 345 86 88 ALA HB H 1.374000 0.03 . 346 86 88 ALA CA C 51.063 0.3 . 347 86 88 ALA CB C 18.099 0.3 . 348 86 88 ALA N N 129.721000 0.3 . 349 87 89 VAL H H 8.639000 0.03 . 350 87 89 VAL HG1 H 0.341000 0.03 . 351 87 89 VAL HG2 H 0.490000 0.03 . 352 87 89 VAL CA C 59.346 0.3 . 353 87 89 VAL CB C 36.328 0.3 . 354 87 89 VAL CG1 C 21.848 0.3 . 355 87 89 VAL CG2 C 19.088 0.3 . 356 87 89 VAL N N 115.738000 0.3 . 357 88 90 LYS H H 8.463000 0.03 . 358 88 90 LYS CA C 56.073 0.3 . 359 88 90 LYS CB C 33.883 0.3 . 360 88 90 LYS N N 118.841000 0.3 . 361 89 91 MET H H 9.901000 0.03 . 362 89 91 MET CA C 53.237 0.3 . 363 89 91 MET CB C 36.467 0.3 . 364 89 91 MET N N 124.667000 0.3 . 365 90 92 TYR H H 8.986000 0.03 . 366 90 92 TYR CA C 56.79 0.3 . 367 90 92 TYR CB C 34.749 0.3 . 368 90 92 TYR N N 115.073000 0.3 . 369 91 93 GLY H H 8.987000 0.03 . 370 91 93 GLY CA C 45.827 0.3 . 371 91 93 GLY N N 105.113000 0.3 . 372 92 94 TYR H H 7.452000 0.03 . 373 92 94 TYR CA C 58.951 0.3 . 374 92 94 TYR CB C 38.306 0.3 . 375 92 94 TYR N N 123.439000 0.3 . 376 93 95 ASN H H 11.200000 0.03 . 377 93 95 ASN CA C 54.867 0.3 . 378 93 95 ASN CB C 39.869 0.3 . 379 93 95 ASN N N 119.963000 0.3 . 380 94 96 ARG H H 8.641000 0.03 . 381 94 96 ARG CA C 55.335 0.3 . 382 94 96 ARG CB C 31.662 0.3 . 383 94 96 ARG N N 122.342000 0.3 . 384 95 97 GLU H H 10.045000 0.03 . 385 95 97 GLU CA C 55.416 0.3 . 386 95 97 GLU CB C 29.179 0.3 . 387 95 97 GLU N N 124.503000 0.3 . 388 96 98 ASN H H 9.399000 0.03 . 389 96 98 ASN CA C 53.438 0.3 . 390 96 98 ASN CB C 37.955 0.3 . 391 96 98 ASN N N 123.118000 0.3 . 392 97 99 ALA H H 8.674000 0.03 . 393 97 99 ALA HB H 0.979000 0.03 . 394 97 99 ALA CA C 50.821 0.3 . 395 97 99 ALA CB C 23.874 0.3 . 396 97 99 ALA N N 125.066000 0.3 . 397 98 100 PHE H H 9.299000 0.03 . 398 98 100 PHE CA C 51.787 0.3 . 399 98 100 PHE CB C 41.085 0.3 . 400 98 100 PHE N N 119.886000 0.3 . 401 99 101 ARG H H 9.528000 0.03 . 402 99 101 ARG CA C 54.326 0.3 . 403 99 101 ARG CB C 32.412 0.3 . 404 99 101 ARG N N 123.301000 0.3 . 405 100 102 TYR H H 10.423000 0.03 . 406 100 102 TYR CA C 57.091 0.3 . 407 100 102 TYR CB C 39.45 0.3 . 408 100 102 TYR N N 131.047000 0.3 . 409 101 103 GLU H H 9.510000 0.03 . 410 101 103 GLU CA C 57.097 0.3 . 411 101 103 GLU CB C 33.009 0.3 . 412 101 103 GLU N N 120.857000 0.3 . 413 102 104 THR H H 8.909000 0.03 . 414 102 104 THR HG2 H 1.172000 0.03 . 415 102 104 THR CA C 60.844 0.3 . 416 102 104 THR CB C 70.766 0.3 . 417 102 104 THR CG2 C 22.943 0.3 . 418 102 104 THR N N 116.529000 0.3 . 419 103 105 GLU H H 9.717000 0.03 . 420 103 105 GLU CA C 59.158 0.3 . 421 103 105 GLU CB C 29.603 0.3 . 422 103 105 GLU N N 122.174000 0.3 . 423 104 106 ASP H H 8.189000 0.03 . 424 104 106 ASP CA C 52.967 0.3 . 425 104 106 ASP CB C 40.03 0.3 . 426 104 106 ASP N N 114.145000 0.3 . 427 105 107 GLY H H 7.716000 0.03 . 428 105 107 GLY CA C 46.099 0.3 . 429 105 107 GLY N N 107.513000 0.3 . 430 106 108 GLN H H 7.714000 0.03 . 431 106 108 GLN CA C 55.773 0.3 . 432 106 108 GLN CB C 30.265 0.3 . 433 106 108 GLN N N 119.979000 0.3 . 434 107 109 VAL H H 7.555000 0.03 . 435 107 109 VAL HG2 H 0.611000 0.03 . 436 107 109 VAL CA C 60.322 0.3 . 437 107 109 VAL CB C 34.403 0.3 . 438 107 109 VAL CG2 C 21.209 0.3 . 439 107 109 VAL N N 121.208000 0.3 . 440 108 110 PHE H H 8.667000 0.03 . 441 108 110 PHE CA C 55.648 0.3 . 442 108 110 PHE CB C 41.87 0.3 . 443 108 110 PHE N N 124.321000 0.3 . 444 109 111 THR H H 8.892000 0.03 . 445 109 111 THR HG2 H 0.856000 0.03 . 446 109 111 THR CA C 55.648 0.3 . 447 109 111 THR CB C 68.491 0.3 . 448 109 111 THR CG2 C 21.112 0.3 . 449 109 111 THR N N 120.952000 0.3 . 450 110 112 ASP H H 8.886000 0.03 . 451 110 112 ASP CA C 52.673 0.3 . 452 110 112 ASP CB C 43.658 0.3 . 453 110 112 ASP N N 127.898000 0.3 . 454 111 113 VAL H H 9.656000 0.03 . 455 111 113 VAL HG2 H 0.853000 0.03 . 456 111 113 VAL CA C 62.409 0.3 . 457 111 113 VAL CB C 36.063 0.3 . 458 111 113 VAL CG2 C 21.752 0.3 . 459 111 113 VAL N N 119.986000 0.3 . 460 112 114 ILE H H 9.145000 0.03 . 461 112 114 ILE HG2 H 0.591000 0.03 . 462 112 114 ILE HD1 H -0.074000 0.03 . 463 112 114 ILE CA C 61.082 0.3 . 464 112 114 ILE CB C 35.728 0.3 . 465 112 114 ILE CG2 C 19.334 0.3 . 466 112 114 ILE CD1 C 9.692 0.3 . 467 112 114 ILE N N 126.224000 0.3 . 468 113 115 ALA H H 8.614000 0.03 . 469 113 115 ALA HB H 0.089000 0.03 . 470 113 115 ALA CA C 53.162 0.3 . 471 113 115 ALA CB C 18.02 0.3 . 472 113 115 ALA N N 132.293000 0.3 . 473 114 116 TYR H H 8.117000 0.03 . 474 114 116 TYR CA C 59.248 0.3 . 475 114 116 TYR CB C 41.835 0.3 . 476 114 116 TYR N N 118.633000 0.3 . 477 115 117 SER H H 8.552000 0.03 . 478 115 117 SER CA C 57.089 0.3 . 479 115 117 SER CB C 64.242 0.3 . 480 115 117 SER N N 124.863000 0.3 . 481 116 118 ASP H H 9.018000 0.03 . 482 116 118 ASP CA C 52.77 0.3 . 483 116 118 ASP CB C 44.561 0.3 . 484 116 118 ASP N N 127.696000 0.3 . 485 117 119 ASP H H 8.938000 0.03 . 486 117 119 ASP CA C 57.18 0.3 . 487 117 119 ASP CB C 40.287 0.3 . 488 117 119 ASP N N 119.625000 0.3 . 489 118 120 ASN H H 8.318000 0.03 . 490 118 120 ASN CA C 52.902 0.3 . 491 118 120 ASN CB C 38.567 0.3 . 492 118 120 ASN N N 111.865000 0.3 . 493 119 121 CYS H H 8.009000 0.03 . 494 119 121 CYS CA C 54.974 0.3 . 495 119 121 CYS CB C 46.217 0.3 . 496 119 121 CYS N N 116.099000 0.3 . 497 120 122 ASP H H 9.722000 0.03 . 498 120 122 ASP CA C 53.703 0.3 . 499 120 122 ASP CB C 47.92 0.3 . 500 120 122 ASP N N 119.108000 0.3 . 501 121 123 VAL H H 10.128000 0.03 . 502 121 123 VAL HG1 H 1.219000 0.03 . 503 121 123 VAL HG2 H 1.241000 0.03 . 504 121 123 VAL CA C 62.432 0.3 . 505 121 123 VAL CB C 32.284 0.3 . 506 121 123 VAL CG1 C 22.732 0.3 . 507 121 123 VAL CG2 C 21.876 0.3 . 508 121 123 VAL N N 123.586000 0.3 . 509 122 124 ILE H H 9.663000 0.03 . 510 122 124 ILE HG2 H 0.948000 0.03 . 511 122 124 ILE HD1 H 0.375000 0.03 . 512 122 124 ILE CA C 61.176 0.3 . 513 122 124 ILE CB C 41.639 0.3 . 514 122 124 ILE CG2 C 18.535 0.3 . 515 122 124 ILE CD1 C 12.578 0.3 . 516 122 124 ILE N N 129.314000 0.3 . 517 123 125 TYR H H 10.063000 0.03 . 518 123 125 TYR CA C 54.927 0.3 . 519 123 125 TYR CB C 41.477 0.3 . 520 123 125 TYR N N 128.717000 0.3 . 521 124 126 VAL H H 8.897000 0.03 . 522 124 126 VAL HG2 H 0.656000 0.03 . 523 124 126 VAL CA C 58.354 0.3 . 524 124 126 VAL CB C 32.213 0.3 . 525 124 126 VAL CG2 C 20.894 0.3 . 526 124 126 VAL N N 130.972000 0.3 . 527 126 128 GLY H H 7.719000 0.03 . 528 126 128 GLY CA C 45.774 0.3 . 529 126 128 GLY N N 105.086000 0.3 . 530 127 129 THR H H 8.369000 0.03 . 531 127 129 THR HG2 H 1.011000 0.03 . 532 127 129 THR CA C 61.422 0.3 . 533 127 129 THR CB C 68.711 0.3 . 534 127 129 THR CG2 C 21.612 0.3 . 535 127 129 THR N N 109.368000 0.3 . 536 128 130 ASP CA C 54.143 0.3 . 537 128 130 ASP CB C 42.039 0.3 . 538 129 131 GLY H H 8.119000 0.03 . 539 129 131 GLY CA C 45.777 0.3 . 540 129 131 GLY N N 107.444000 0.3 . 541 130 132 ASN H H 8.293000 0.03 . 542 130 132 ASN CA C 50.557 0.3 . 543 130 132 ASN CB C 38.2 0.3 . 544 130 132 ASN N N 117.749000 0.3 . 545 131 133 GLU CA C 55.66 0.3 . 546 131 133 GLU CB C 31.412 0.3 . 547 132 134 GLU H H 8.353000 0.03 . 548 132 134 GLU CA C 54.839 0.3 . 549 132 134 GLU CB C 30.08 0.3 . 550 132 134 GLU N N 124.414000 0.3 . 551 133 135 GLY H H 8.833000 0.03 . 552 133 135 GLY CA C 46.217 0.3 . 553 133 135 GLY N N 112.505000 0.3 . 554 134 136 TYR H H 9.125000 0.03 . 555 134 136 TYR CA C 57.361 0.3 . 556 134 136 TYR CB C 45.028 0.3 . 557 134 136 TYR N N 115.156000 0.3 . 558 135 137 GLU H H 9.998000 0.03 . 559 135 137 GLU CA C 54.652 0.3 . 560 135 137 GLU CB C 36.072 0.3 . 561 135 137 GLU N N 117.580000 0.3 . 562 136 138 LEU H H 8.497000 0.03 . 563 136 138 LEU HD1 H 0.521000 0.03 . 564 136 138 LEU HD2 H 0.709000 0.03 . 565 136 138 LEU CA C 54.3 0.3 . 566 136 138 LEU CB C 45.078 0.3 . 567 136 138 LEU CD1 C 25.782 0.3 . 568 136 138 LEU CD2 C 25.366 0.3 . 569 136 138 LEU N N 124.453000 0.3 . 570 137 139 TRP H H 9.983000 0.03 . 571 137 139 TRP CA C 54.818 0.3 . 572 137 139 TRP CB C 32.16 0.3 . 573 137 139 TRP N N 127.170000 0.3 . 574 138 140 THR H H 9.755000 0.03 . 575 138 140 THR CA C 59.877 0.3 . 576 138 140 THR CB C 69.832 0.3 . 577 138 140 THR N N 114.166000 0.3 . 578 139 141 THR H H 7.345000 0.03 . 579 139 141 THR CA C 62.519 0.3 . 580 139 141 THR CB C 68.649 0.3 . 581 139 141 THR N N 113.709000 0.3 . 582 140 142 ASP H H 7.821000 0.03 . 583 140 142 ASP CA C 52.808 0.3 . 584 140 142 ASP CB C 41.606 0.3 . 585 140 142 ASP N N 122.877000 0.3 . 586 141 143 TYR H H 6.440000 0.03 . 587 141 143 TYR CA C 57.528 0.3 . 588 141 143 TYR CB C 37.307 0.3 . 589 141 143 TYR N N 118.300000 0.3 . 590 142 144 ASP H H 7.745000 0.03 . 591 142 144 ASP CA C 54.301 0.3 . 592 142 144 ASP CB C 42.157 0.3 . 593 142 144 ASP N N 121.346000 0.3 . 594 143 145 ASN H H 7.232000 0.03 . 595 143 145 ASN CA C 51.667 0.3 . 596 143 145 ASN CB C 39.003 0.3 . 597 143 145 ASN N N 120.047000 0.3 . 598 144 146 ILE H H 8.560000 0.03 . 599 144 146 ILE HG2 H 0.809000 0.03 . 600 144 146 ILE HD1 H 0.802000 0.03 . 601 144 146 ILE CA C 60.141 0.3 . 602 144 146 ILE CG2 C 18.415 0.3 . 603 144 146 ILE CD1 C 13.939 0.3 . 604 144 146 ILE N N 124.893000 0.3 . 605 145 147 PRO CA C 63.8 0.3 . 606 145 147 PRO CB C 33.027 0.3 . 607 146 148 ALA H H 8.723000 0.03 . 608 146 148 ALA HB H 1.351000 0.03 . 609 146 148 ALA CA C 55.504 0.3 . 610 146 148 ALA CB C 18.644 0.3 . 611 146 148 ALA N N 128.354000 0.3 . 612 147 149 ASN H H 9.166000 0.03 . 613 147 149 ASN CA C 56.15 0.3 . 614 147 149 ASN CB C 36.88 0.3 . 615 147 149 ASN N N 114.651000 0.3 . 616 148 150 CYS H H 7.461000 0.03 . 617 148 150 CYS CA C 59.281 0.3 . 618 148 150 CYS CB C 46.449 0.3 . 619 148 150 CYS N N 114.308000 0.3 . 620 149 151 LEU H H 8.022000 0.03 . 621 149 151 LEU HD1 H 0.774000 0.03 . 622 149 151 LEU HD2 H 0.734000 0.03 . 623 149 151 LEU CA C 58.343 0.3 . 624 149 151 LEU CB C 41.661 0.3 . 625 149 151 LEU CD1 C 25.536 0.3 . 626 149 151 LEU CD2 C 23.04 0.3 . 627 149 151 LEU N N 121.719000 0.3 . 628 150 152 ASN H H 8.666000 0.03 . 629 150 152 ASN CA C 55.947 0.3 . 630 150 152 ASN CB C 37.322 0.3 . 631 150 152 ASN N N 115.858000 0.3 . 632 151 153 LYS H H 7.183000 0.03 . 633 151 153 LYS CA C 57.345 0.3 . 634 151 153 LYS CB C 31.256 0.3 . 635 151 153 LYS N N 119.363000 0.3 . 636 152 154 PHE H H 8.240000 0.03 . 637 152 154 PHE CA C 62.234 0.3 . 638 152 154 PHE CB C 39.402 0.3 . 639 152 154 PHE N N 118.961000 0.3 . 640 153 155 ASN H H 8.477000 0.03 . 641 153 155 ASN CA C 55.209 0.3 . 642 153 155 ASN CB C 37.422 0.3 . 643 153 155 ASN N N 115.514000 0.3 . 644 154 156 GLU H H 7.731000 0.03 . 645 154 156 GLU CA C 58.755 0.3 . 646 154 156 GLU CB C 29.586 0.3 . 647 154 156 GLU N N 120.322000 0.3 . 648 155 157 TYR H H 8.006000 0.03 . 649 155 157 TYR CA C 56.205 0.3 . 650 155 157 TYR CB C 35.348 0.3 . 651 155 157 TYR N N 118.154000 0.3 . 652 156 158 ALA H H 8.137000 0.03 . 653 156 158 ALA HB H 0.479000 0.03 . 654 156 158 ALA CA C 51.719 0.3 . 655 156 158 ALA CB C 17.213 0.3 . 656 156 158 ALA N N 120.028000 0.3 . 657 157 159 VAL H H 6.476000 0.03 . 658 157 159 VAL HG1 H 0.997000 0.03 . 659 157 159 VAL HG2 H 0.923000 0.03 . 660 157 159 VAL CA C 63.193 0.3 . 661 157 159 VAL CB C 31.72 0.3 . 662 157 159 VAL CG1 C 21.141 0.3 . 663 157 159 VAL CG2 C 19.573 0.3 . 664 157 159 VAL N N 118.449000 0.3 . 665 158 160 GLY H H 8.962000 0.03 . 666 158 160 GLY CA C 45.234 0.3 . 667 158 160 GLY N N 115.223000 0.3 . 668 159 161 ARG H H 7.855000 0.03 . 669 159 161 ARG CA C 54.45 0.3 . 670 159 161 ARG CB C 31.422 0.3 . 671 159 161 ARG N N 119.085000 0.3 . 672 160 162 GLU H H 8.938000 0.03 . 673 160 162 GLU CA C 56.116 0.3 . 674 160 162 GLU CB C 30.006 0.3 . 675 160 162 GLU N N 123.383000 0.3 . 676 161 163 THR H H 8.287000 0.03 . 677 161 163 THR CA C 62.261 0.3 . 678 161 163 THR CB C 70.276 0.3 . 679 161 163 THR N N 117.401000 0.3 . 680 162 164 ARG H H 8.900000 0.03 . 681 162 164 ARG CA C 53.475 0.3 . 682 162 164 ARG CB C 33.025 0.3 . 683 162 164 ARG N N 122.726000 0.3 . 684 163 165 ASP H H 8.447000 0.03 . 685 163 165 ASP CA C 54.082 0.3 . 686 163 165 ASP CB C 41.25 0.3 . 687 163 165 ASP N N 121.091000 0.3 . 688 164 166 VAL H H 7.704000 0.03 . 689 164 166 VAL HG1 H 1.063000 0.03 . 690 164 166 VAL HG2 H 0.473000 0.03 . 691 164 166 VAL CA C 64.527 0.3 . 692 164 166 VAL CB C 32.483 0.3 . 693 164 166 VAL CG1 C 22.358 0.3 . 694 164 166 VAL CG2 C 20.857 0.3 . 695 164 166 VAL N N 122.778000 0.3 . 696 165 167 PHE H H 9.096000 0.03 . 697 165 167 PHE CA C 58.448 0.3 . 698 165 167 PHE CB C 40.192 0.3 . 699 165 167 PHE N N 126.274000 0.3 . 700 166 168 THR H H 6.607000 0.03 . 701 166 168 THR CA C 59.092 0.3 . 702 166 168 THR CB C 72.856 0.3 . 703 166 168 THR N N 117.610000 0.3 . 704 167 169 SER H H 9.190000 0.03 . 705 167 169 SER CA C 61.042 0.3 . 706 167 169 SER CB C 62.342 0.3 . 707 167 169 SER N N 115.468000 0.3 . 708 168 170 ALA H H 7.500000 0.03 . 709 168 170 ALA HB H 1.143000 0.03 . 710 168 170 ALA CA C 54.04 0.3 . 711 168 170 ALA CB C 18.228 0.3 . 712 168 170 ALA N N 124.267000 0.3 . 713 169 171 CYS H H 7.622000 0.03 . 714 169 171 CYS CA C 56.742 0.3 . 715 169 171 CYS CB C 40.154 0.3 . 716 169 171 CYS N N 114.198000 0.3 . 717 170 172 LEU H H 7.205000 0.03 . 718 170 172 LEU HD1 H 0.862000 0.03 . 719 170 172 LEU HD2 H 0.826000 0.03 . 720 170 172 LEU CA C 54.229 0.3 . 721 170 172 LEU CB C 42.425 0.3 . 722 170 172 LEU CD1 C 25.379 0.3 . 723 170 172 LEU CD2 C 22.793 0.3 . 724 170 172 LEU N N 117.971000 0.3 . 725 171 173 GLU H H 7.351000 0.03 . 726 171 173 GLU CA C 58.228 0.3 . 727 171 173 GLU CB C 31.035 0.3 . 728 171 173 GLU N N 125.457000 0.3 . stop_ save_ save_order_parameter_list_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_2 _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 . 0.946 0.018 4.76E-10 1.94E-11 . . . . . . . . . . 12 ALA CB . 0.553 0.037 4.92E-10 6.65E-12 . . . . . . . . . . 15 ALA CB . 0.840 0.007 4.50E-10 7.04E-12 . . . . . . . . . . 19 ALA CB . 0.792 0.023 5.22E-10 1.31E-11 . . . . . . . . . . 23 LEU CD1 . 0.701 0.020 5.89E-10 3.17E-11 . . . . . . . . . . 23 LEU CD2 . 0.709 0.035 3.87E-10 3.70E-11 . . . . . . . . . . 25 ALA CB . 0.939 0.015 5.13E-10 1.39E-11 . . . . . . . . . . 27 VAL CG1 . 0.661 0.008 4.97E-10 1.13E-11 . . . . . . . . . . 27 VAL CG2 . 0.645 0.005 5.30E-10 5.11E-12 . . . . . . . . . . 30 VAL CG1 . 0.665 0.007 2.91E-10 5.57E-12 . . . . . . . . . . 30 VAL CG2 . 0.678 0.010 1.13E-09 2.20E-11 . . . . . . . . . . 33 MET CE . 0.602 0.005 8.97E-11 1.65E-12 . . . . . . . . . . 34 VAL CG1 . 0.672 0.017 8.61E-10 1.41E-11 . . . . . . . . . . 34 VAL CG2 . 0.468 0.023 4.37E-10 1.11E-11 . . . . . . . . . . 36 ALA CB . 0.911 0.034 1.18E-09 5.05E-11 . . . . . . . . . . 37 THR CG2 . 0.850 0.035 5.05E-10 2.76E-11 . . . . . . . . . . 43 VAL CG1 . 0.855 0.033 3.66E-10 2.15E-11 . . . . . . . . . . 49 THR CG2 . 0.885 0.042 1.38E-09 6.80E-11 . . . . . . . . . . 51 VAL CG2 . 0.828 0.019 4.03E-10 3.09E-11 . . . . . . . . . . 53 VAL CG2 . 0.859 0.031 1.01E-09 6.11E-11 . . . . . . . . . . 54 MET CE . 0.127 0.002 7.00E-11 0.00E+00 . . . . . . . . . . 55 ALA CB . 0.887 0.016 7.05E-10 1.92E-11 . . . . . . . . . . 58 VAL CG1 . 0.352 0.006 4.78E-10 6.90E-12 . . . . . . . . . . 58 VAL CG2 . 0.424 0.004 5.53E-10 6.33E-12 . . . . . . . . . . 65 ILE CG2 . 0.895 0.013 3.73E-10 1.66E-11 . . . . . . . . . . 65 ILE CD1 . 0.597 0.006 2.51E-10 9.51E-12 . . . . . . . . . . 67 ALA CB . 0.767 0.016 3.63E-10 2.20E-11 . . . . . . . . . . 70 LEU CD1 . 0.181 0.004 2.98E-10 6.04E-12 . . . . . . . . . . 70 LEU CD2 . 0.084 0.003 3.01E-10 4.28E-12 . . . . . . . . . . 72 MET CE . 0.131 0.005 1.00E-10 6.32E-13 . . . . . . . . . . 75 ALA CB . 0.738 0.010 3.14E-10 6.63E-12 . . . . . . . . . . 77 THR CG2 . 0.535 0.010 4.07E-10 4.95E-12 . . . . . . . . . . 82 ALA CB . 0.922 0.015 5.18E-10 1.47E-11 . . . . . . . . . . 83 THR CG2 . 0.587 0.008 5.39E-10 6.74E-12 . . . . . . . . . . 86 VAL CG2 . 0.869 0.059 1.31E-09 6.85E-11 . . . . . . . . . . 87 THR CG2 . 0.889 0.017 6.58E-10 1.16E-11 . . . . . . . . . . 88 ALA CB . 0.967 0.009 3.93E-10 4.74E-12 . . . . . . . . . . 89 VAL CG1 . 0.939 0.017 1.06E-09 3.17E-11 . . . . . . . . . . 89 VAL CG2 . 0.882 0.016 7.98E-10 2.64E-11 . . . . . . . . . . 91 MET CE . 0.118 0.006 1.06E-10 4.95E-12 . . . . . . . . . . 99 ALA CB . 0.945 0.012 2.98E-10 1.01E-11 . . . . . . . . . . 109 VAL CG2 . 0.593 0.004 6.29E-10 7.31E-12 . . . . . . . . . . 111 THR CG2 . 0.705 0.015 2.28E-10 1.57E-11 . . . . . . . . . . 113 VAL CG2 . 0.505 0.023 4.52E-10 7.62E-12 . . . . . . . . . . 114 ILE CG2 . 0.785 0.025 7.80E-10 2.63E-11 . . . . . . . . . . 114 ILE CD1 . 0.235 0.004 1.44E-10 5.97E-12 . . . . . . . . . . 115 ALA CB . 0.929 0.015 6.11E-10 2.88E-11 . . . . . . . . . . 123 VAL CG1 . 0.910 0.019 3.89E-10 1.91E-11 . . . . . . . . . . 123 VAL CG2 . 0.841 0.027 4.12E-10 2.53E-11 . . . . . . . . . . 124 ILE CG2 . 0.781 0.025 6.16E-10 3.45E-11 . . . . . . . . . . 126 VAL CG1 . 0.593 0.005 5.05E-10 8.42E-12 . . . . . . . . . . 126 VAL CG2 . 0.783 0.022 3.17E-10 2.22E-11 . . . . . . . . . . 129 THR CG2 . 0.348 0.002 6.20E-10 6.32E-13 . . . . . . . . . . 138 LEU CD1 . 0.479 0.011 5.14E-10 1.47E-11 . . . . . . . . . . 138 LEU CD2 . 0.508 0.009 4.60E-10 1.59E-11 . . . . . . . . . . 140 THR CG2 . 0.587 0.011 4.50E-10 1.12E-11 . . . . . . . . . . 141 THR CG2 . 0.866 0.022 9.06E-10 2.56E-11 . . . . . . . . . . 146 ILE CG2 . 0.837 0.013 6.09E-10 1.62E-11 . . . . . . . . . . 146 ILE CD1 . 0.642 0.007 2.16E-10 6.97E-12 . . . . . . . . . . 148 ALA CB . 0.895 0.011 5.20E-10 1.07E-11 . . . . . . . . . . 151 LEU CD1 . 0.493 0.009 4.22E-10 1.09E-11 . . . . . . . . . . 151 LEU CD2 . 0.522 0.005 3.73E-10 7.49E-12 . . . . . . . . . . 158 ALA CB . 0.930 0.012 4.57E-10 1.35E-11 . . . . . . . . . . 159 VAL CG1 . 0.703 0.017 4.01E-10 1.13E-11 . . . . . . . . . . 159 VAL CG2 . 0.326 0.003 5.28E-10 4.01E-12 . . . . . . . . . . 163 THR CG2 . 0.475 0.010 8.13E-10 9.97E-12 . . . . . . . . . . 166 VAL CG1 . 0.859 0.026 6.86E-10 2.27E-11 . . . . . . . . . . 166 VAL CG2 . 0.873 0.013 5.23E-10 1.68E-11 . . . . . . . . . . 170 ALA CB . 0.795 0.006 4.65E-10 5.81E-12 . . . . . . . . . . 172 LEU CD1 . 0.275 0.003 4.65E-10 6.15E-12 . . . . . . . . . . 172 LEU CD2 . 0.290 0.002 3.52E-10 4.01E-12 . . . . . . . . . . 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_2 _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 7 TRP N . 0.830 0.007 3.20E-13 3.02E-12 . . . . . . . . . . 8 ALA N . 0.930 0.008 1.20E-13 2.00E-12 . . . . . . . . . . 9 ASP N . 0.647 0.006 3.42E-11 7.80E-12 . . . . . . . . . . 10 GLU N . 0.869 0.010 6.76E-11 2.93E-11 . . . . . . . . . . 11 ALA N . 0.852 0.004 8.00E-13 4.27E-12 . . . . . . . . . . 12 ALA N . 0.855 0.004 5.55E-11 1.91E-11 . . . . . . . . . . 13 ASN N . 0.841 0.011 5.63E-11 2.80E-11 . . . . . . . . . . 14 GLY N . 0.867 0.009 7.68E-11 3.15E-11 . . . . . . . . . . 16 HIS N . 0.793 0.007 3.70E-11 1.53E-11 . . . . . . . . . . 17 GLN N . 0.840 0.008 8.52E-12 1.18E-11 . . . . . . . . . . 18 ASP N . 0.819 0.006 1.97E-11 1.63E-11 . . . . . . . . . . 19 ALA N . 0.844 0.007 2.60E-13 2.22E-12 . . . . . . . . . . 20 TRP N . 0.864 0.005 1.78E-12 6.51E-12 . . . . . . . . . . 21 LYS N . 0.916 0.008 0.00E+00 0.00E+00 . . . . . . . . . . 22 SER N . 0.895 0.009 1.50E-12 6.30E-12 . . . . . . . . . . 23 LEU N . 0.950 0.007 3.11E-11 5.21E-11 . . . . . . . . . . 24 LYS N . 0.907 0.005 1.63E-11 2.56E-11 . . . . . . . . . . 25 ALA N . 0.915 0.004 1.60E-13 2.45E-12 . . . . . . . . . . 26 ARG N . 0.895 0.005 3.61E-11 3.18E-11 . . . . . . . . . . 27 VAL N . 0.974 0.005 0.00E+00 0.00E+00 . . . . . . . . . . 28 GLU N . 0.821 0.004 2.16E-10 1.93E-11 . . . . . . . . . . 29 ASN N . 0.801 0.003 1.46E-10 1.73E-11 . . . . . . . . . . 30 VAL N . 0.756 0.006 2.26E-10 1.68E-11 . . . . . . . . . . 31 TYR N . 0.849 0.009 6.38E-12 1.48E-11 . . . . . . . . . . 32 TYR N . 0.843 0.009 1.96E-11 2.15E-11 . . . . . . . . . . 33 MET N . 0.858 0.008 2.12E-11 2.14E-11 . . . . . . . . . . 34 VAL N . 0.857 0.005 8.82E-11 2.21E-11 . . . . . . . . . . 35 LYS N . 0.928 0.007 3.96E-12 1.49E-11 . . . . . . . . . . 36 ALA N . 0.887 0.005 1.70E-12 6.50E-12 . . . . . . . . . . 37 THR N . 0.832 0.007 1.49E-11 1.80E-11 . . . . . . . . . . 38 TYR N . 0.892 0.007 3.42E-10 4.94E-11 . . . . . . . . . . 39 LYS N . 0.861 0.010 1.63E-10 4.71E-11 . . . . . . . . . . 40 ASN N . 0.826 0.008 7.05E-11 2.89E-11 . . . . . . . . . . 41 ASP N . 0.819 0.006 1.40E-13 1.48E-12 . . . . . . . . . . 46 ASN N . 0.869 0.007 4.39E-11 3.31E-11 . . . . . . . . . . 47 ASP N . 0.852 0.010 1.84E-12 7.51E-12 . . . . . . . . . . 48 PHE N . 0.857 0.009 8.12E-11 3.28E-11 . . . . . . . . . . 49 THR N . 0.880 0.011 2.13E-11 3.94E-11 . . . . . . . . . . 50 CYS N . 0.862 0.010 1.71E-11 2.30E-11 . . . . . . . . . . 51 VAL N . 0.802 0.010 6.70E-12 1.20E-11 . . . . . . . . . . 52 GLY N . 0.910 0.008 1.49E-11 3.08E-11 . . . . . . . . . . 53 VAL N . 0.909 0.007 3.49E-11 4.53E-11 . . . . . . . . . . 54 MET N . 0.855 0.005 1.02E-10 2.99E-11 . . . . . . . . . . 55 ALA N . 0.849 0.005 1.67E-10 2.73E-11 . . . . . . . . . . 56 ASN N . 0.774 0.003 2.15E-10 1.64E-11 . . . . . . . . . . 58 VAL N . 0.783 0.004 6.75E-11 1.31E-11 . . . . . . . . . . 59 ASN N . 0.842 0.006 2.19E-11 2.26E-11 . . . . . . . . . . 60 GLU N . 0.772 0.008 8.90E-12 1.17E-11 . . . . . . . . . . 61 ASP N . 0.803 0.007 1.27E-10 1.28E-11 . . . . . . . . . . 62 GLU N . 0.807 0.005 8.10E-11 1.66E-11 . . . . . . . . . . 63 LYS N . 0.860 0.005 8.47E-11 2.43E-11 . . . . . . . . . . 64 SER N . 0.883 0.006 0.00E+00 0.00E+00 . . . . . . . . . . 65 ILE N . 0.877 0.009 6.28E-12 1.63E-11 . . . . . . . . . . 66 GLN N . 0.870 0.006 9.00E-12 1.80E-11 . . . . . . . . . . 67 ALA N . 0.876 0.006 6.80E-11 4.14E-11 . . . . . . . . . . 68 GLU N . 0.820 0.005 4.00E-12 8.47E-12 . . . . . . . . . . 69 PHE N . 0.905 0.010 4.66E-12 1.65E-11 . . . . . . . . . . 71 PHE N . 0.832 0.006 1.04E-10 2.45E-11 . . . . . . . . . . 72 MET N . 0.863 0.008 8.33E-11 3.92E-11 . . . . . . . . . . 73 ASN N . 0.858 0.009 1.93E-10 4.54E-11 . . . . . . . . . . 74 ASN N . 0.813 0.009 2.91E-10 3.14E-11 . . . . . . . . . . 75 ALA N . 0.889 0.006 8.80E-13 8.38E-12 . . . . . . . . . . 76 ASP N . 0.754 0.006 1.47E-10 1.23E-11 . . . . . . . . . . 78 ASN N . 0.735 0.007 1.60E-10 1.28E-11 . . . . . . . . . . 79 MET N . 0.797 0.004 1.46E-10 1.42E-11 . . . . . . . . . . 80 GLN N . 0.854 0.010 2.00E-14 4.47E-13 . . . . . . . . . . 81 PHE N . 0.788 0.005 1.16E-10 1.74E-11 . . . . . . . . . . 82 ALA N . 0.832 0.006 3.19E-11 2.49E-11 . . . . . . . . . . 83 THR N . 0.812 0.007 1.20E-10 2.61E-11 . . . . . . . . . . 84 GLU N . 0.863 0.009 2.70E-11 3.40E-11 . . . . . . . . . . 85 LYS N . 0.835 0.008 5.15E-11 3.05E-11 . . . . . . . . . . 86 VAL N . 0.826 0.006 3.04E-11 2.62E-11 . . . . . . . . . . 87 THR N . 0.867 0.007 1.13E-10 4.11E-11 . . . . . . . . . . 88 ALA N . 0.910 0.005 6.82E-12 1.65E-11 . . . . . . . . . . 90 LYS N . 0.853 0.008 7.29E-11 3.27E-11 . . . . . . . . . . 91 MET N . 0.809 0.010 7.40E-13 3.86E-12 . . . . . . . . . . 92 TYR N . 0.790 0.006 6.60E-11 1.44E-11 . . . . . . . . . . 94 TYR N . 0.886 0.008 0.00E+00 0.00E+00 . . . . . . . . . . 95 ASN N . 0.787 0.006 5.35E-11 2.27E-11 . . . . . . . . . . 97 GLU N . 0.817 0.007 2.73E-11 1.92E-11 . . . . . . . . . . 98 ASN N . 0.834 0.008 7.40E-13 4.53E-12 . . . . . . . . . . 99 ALA N . 0.908 0.009 7.00E-11 4.82E-11 . . . . . . . . . . 100 PHE N . 0.855 0.005 7.56E-12 1.66E-11 . . . . . . . . . . 101 ARG N . 0.820 0.006 4.94E-11 4.14E-11 . . . . . . . . . . 102 TYR N . 0.917 0.011 1.50E-12 1.04E-11 . . . . . . . . . . 103 GLU N . 0.837 0.007 6.23E-11 2.95E-11 . . . . . . . . . . 104 THR N . 0.844 0.006 3.06E-11 2.39E-11 . . . . . . . . . . 105 GLU N . 0.859 0.008 8.38E-11 4.23E-11 . . . . . . . . . . 106 ASP N . 0.727 0.006 1.70E-10 1.60E-11 . . . . . . . . . . 107 GLY N . 0.811 0.007 1.27E-10 1.88E-11 . . . . . . . . . . 108 GLN N . 0.837 0.006 1.96E-10 2.86E-11 . . . . . . . . . . 109 VAL N . 0.797 0.005 9.56E-11 2.04E-11 . . . . . . . . . . 110 PHE N . 0.856 0.010 9.00E-13 5.35E-12 . . . . . . . . . . 111 THR N . 0.792 0.012 1.19E-11 1.68E-11 . . . . . . . . . . 113 VAL N . 0.840 0.005 0.00E+00 0.00E+00 . . . . . . . . . . 114 ILE N . 0.860 0.006 1.08E-11 1.93E-11 . . . . . . . . . . 115 ALA N . 0.964 0.008 5.40E-13 8.99E-12 . . . . . . . . . . 116 TYR N . 0.905 0.015 5.42E-11 8.13E-11 . . . . . . . . . . 117 SER N . 0.801 0.006 8.35E-11 1.03E-11 . . . . . . . . . . 118 ASP N . 0.851 0.009 4.16E-11 3.60E-11 . . . . . . . . . . 120 ASN N . 0.800 0.010 1.47E-10 2.87E-11 . . . . . . . . . . 121 CYS N . 0.852 0.017 9.06E-11 3.19E-11 . . . . . . . . . . 122 ASP N . 0.900 0.025 6.87E-11 6.48E-11 . . . . . . . . . . 123 VAL N . 0.800 0.007 4.80E-13 3.19E-12 . . . . . . . . . . 124 ILE N . 0.918 0.008 0.00E+00 0.00E+00 . . . . . . . . . . 125 TYR N . 0.895 0.013 7.40E-13 6.04E-12 . . . . . . . . . . 126 VAL N . 0.877 0.011 8.06E-12 2.11E-11 . . . . . . . . . . 128 GLY N . 0.869 0.013 1.29E-10 5.80E-11 . . . . . . . . . . 129 THR N . 0.781 0.013 1.43E-10 3.24E-11 . . . . . . . . . . 130 ASP N . 0.748 0.014 1.03E-10 2.16E-11 . . . . . . . . . . 132 ASN N . 0.800 0.010 5.78E-11 2.12E-11 . . . . . . . . . . 134 GLU N . 0.813 0.011 1.23E-10 2.67E-11 . . . . . . . . . . 135 GLY N . 0.857 0.009 7.60E-13 4.89E-12 . . . . . . . . . . 136 TYR N . 0.821 0.006 2.92E-11 2.76E-11 . . . . . . . . . . 137 GLU N . 0.844 0.012 1.22E-11 2.29E-11 . . . . . . . . . . 138 LEU N . 0.874 0.011 3.06E-12 1.10E-11 . . . . . . . . . . 139 TRP N . 0.875 0.008 1.50E-11 2.87E-11 . . . . . . . . . . 140 THR N . 0.909 0.006 1.26E-12 7.42E-12 . . . . . . . . . . 141 THR N . 1.000 0.000 2.20E-09 4.20E-10 . . . . . . . . . . 142 ASP N . 0.841 0.006 2.50E-10 2.77E-11 . . . . . . . . . . 143 TYR N . 0.806 0.006 1.37E-10 1.76E-11 . . . . . . . . . . 144 ASP N . 0.870 0.006 3.23E-11 2.39E-11 . . . . . . . . . . 145 ASN N . 0.690 0.004 2.26E-10 8.52E-12 . . . . . . . . . . 148 ALA N . 0.824 0.009 3.56E-12 8.83E-12 . . . . . . . . . . 150 CYS N . 0.844 0.013 2.10E-10 4.14E-11 . . . . . . . . . . 151 LEU N . 0.867 0.006 3.28E-12 9.52E-12 . . . . . . . . . . 152 ASN N . 0.902 0.005 1.59E-11 1.91E-11 . . . . . . . . . . 154 PHE N . 0.907 0.009 1.81E-11 2.96E-11 . . . . . . . . . . 155 ASN N . 0.925 0.005 3.42E-11 3.69E-11 . . . . . . . . . . 156 GLU N . 0.912 0.003 0.00E+00 0.00E+00 . . . . . . . . . . 157 TYR N . 0.896 0.007 2.80E-13 2.60E-12 . . . . . . . . . . 158 ALA N . 0.868 0.004 5.76E-11 2.39E-11 . . . . . . . . . . 159 VAL N . 0.815 0.006 1.05E-10 1.21E-11 . . . . . . . . . . 161 ARG N . 0.774 0.006 1.22E-10 8.85E-12 . . . . . . . . . . 164 ARG N . 0.843 0.004 9.27E-11 2.45E-11 . . . . . . . . . . 165 ASP N . 0.864 0.007 6.07E-11 2.49E-11 . . . . . . . . . . 166 VAL N . 0.781 0.006 3.00E-13 2.63E-12 . . . . . . . . . . 167 PHE N . 0.818 0.008 1.52E-10 3.21E-11 . . . . . . . . . . 168 THR N . 0.805 0.007 1.72E-10 1.96E-11 . . . . . . . . . . 171 CYS N . 0.827 0.005 1.49E-10 1.57E-11 . . . . . . . . . . stop_ save_