data_50129 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone assignments of Tau fragment (225-324) ; _BMRB_accession_number 50129 _BMRB_flat_file_name bmr50129.str _Entry_type original _Submission_date 2019-12-15 _Accession_date 2019-12-15 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details . loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kawawsaki Ryosuke . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 92 "13C chemical shifts" 422 "15N chemical shifts" 101 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2020-08-03 original BMRB . stop_ loop_ _Related_BMRB_accession_number _Relationship 50130 'Tau fragment (224-325) with P301L mutation' stop_ _Original_release_date 2019-12-16 save_ ############################# # Citation for this entry # ############################# save_citations_1 _Saveframe_category entry_citation _Citation_full . _Citation_title ; Impact of the Hereditary P301L Mutation on the Correlated Conformational Dynamics of Human Tau Protein Revealed by the Paramagnetic Relaxation Enhancement NMR Experiments ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 32486218 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kawasaki Ryosuke . . 2 Tate Shin-Ichi I. . stop_ _Journal_abbreviation 'Int. J. Mol. Sci.' _Journal_name_full 'International journal of molecular sciences' _Journal_volume 21 _Journal_issue 11 _Journal_ISSN 1422-0067 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year 2020 _Details . save_ ################################## # Molecular system description # ################################## save_assembly_1 _Saveframe_category molecular_system _Mol_system_name 'Tau fragment in monomer state' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'TauF4d fragment' $entity_1 stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_entity_1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common entity_1 _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 104 _Mol_residue_sequence ; GSHMKVAVVRTPPKSPSSAK SRLQTAPVPMPDLKNVKSKI GSTENLKHQPGGGKVQIINK KLDLSNVQSKCGSKDNIKHV PGGGSVQIVYKPVDLSKVTS KCGS ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 SER 3 HIS 4 MET 5 LYS 6 VAL 7 ALA 8 VAL 9 VAL 10 ARG 11 THR 12 PRO 13 PRO 14 LYS 15 SER 16 PRO 17 SER 18 SER 19 ALA 20 LYS 21 SER 22 ARG 23 LEU 24 GLN 25 THR 26 ALA 27 PRO 28 VAL 29 PRO 30 MET 31 PRO 32 ASP 33 LEU 34 LYS 35 ASN 36 VAL 37 LYS 38 SER 39 LYS 40 ILE 41 GLY 42 SER 43 THR 44 GLU 45 ASN 46 LEU 47 LYS 48 HIS 49 GLN 50 PRO 51 GLY 52 GLY 53 GLY 54 LYS 55 VAL 56 GLN 57 ILE 58 ILE 59 ASN 60 LYS 61 LYS 62 LEU 63 ASP 64 LEU 65 SER 66 ASN 67 VAL 68 GLN 69 SER 70 LYS 71 CYS 72 GLY 73 SER 74 LYS 75 ASP 76 ASN 77 ILE 78 LYS 79 HIS 80 VAL 81 PRO 82 GLY 83 GLY 84 GLY 85 SER 86 VAL 87 GLN 88 ILE 89 VAL 90 TYR 91 LYS 92 PRO 93 VAL 94 ASP 95 LEU 96 SER 97 LYS 98 VAL 99 THR 100 SER 101 LYS 102 CYS 103 GLY 104 SER stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ #################### # Natural source # #################### save_natural_source_1 _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $entity_1 Human 9606 Eukaryota Metazoa Homo sapiens stop_ save_ ######################### # Experimental source # ######################### save_experimental_source_1 _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name $entity_1 'recombinant technology' . Escherichia coli . plasmid pET28a stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details '13C 15N WT tauF4d' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $entity_1 0.5 mM '[U-100% 13C; U-100% 15N]' TRIS 50 mM 'natural abundance' DTT 1 mM 'natural abundance' 'sodium azide' 0.03 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_software_1 _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details 'MagRO module' save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 700 _Details 'Avance II' 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_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HN(CA)CO_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CA)CO' _Sample_label $sample_1 save_ save_3D_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_(H)CC(CO)NNH_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D (H)CC(CO)NNH' _Sample_label $sample_1 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.8 . pH pressure 1 . atm temperature 285 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_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 water C 13 'water proton' ppm 4.931 internal indirect . . . 0.251449530 water H 1 'water proton' ppm 4.931 internal direct . . . 1 water N 15 'water proton' ppm 4.931 internal 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_chemical_shifts_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCO' '3D HN(CA)CO' '3D HNCACB' '3D (H)CC(CO)NNH' stop_ loop_ _Sample_label $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chem_shift_reference_1 _Mol_system_component_name 'TauF4d fragment' _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 3 HIS C C 177.103 0.300 1 2 3 3 HIS CA C 55.004 0.300 1 3 3 3 HIS CB C 31.706 0.300 1 4 4 4 MET H H 8.398 0.030 1 5 4 4 MET C C 175.738 0.300 1 6 4 4 MET CA C 54.828 0.300 1 7 4 4 MET CB C 32.761 0.300 1 8 4 4 MET CG C 31.460 0.300 1 9 4 4 MET N N 120.850 0.300 1 10 5 5 LYS H H 8.384 0.030 1 11 5 5 LYS C C 176.430 0.300 1 12 5 5 LYS CA C 56.411 0.300 1 13 5 5 LYS CB C 32.812 0.300 1 14 5 5 LYS CG C 24.778 0.300 1 15 5 5 LYS CD C 29.013 0.300 1 16 5 5 LYS CE C 42.095 0.300 1 17 5 5 LYS N N 122.849 0.300 1 18 6 6 VAL H H 8.234 0.030 1 19 6 6 VAL C C 175.719 0.300 1 20 6 6 VAL CA C 62.038 0.300 1 21 6 6 VAL CB C 32.810 0.300 1 22 6 6 VAL CG1 C 20.825 0.300 1 23 6 6 VAL CG2 C 20.825 0.300 1 24 6 6 VAL N N 122.386 0.300 1 25 7 7 ALA H H 8.493 0.030 1 26 7 7 ALA C C 177.465 0.300 1 27 7 7 ALA CA C 52.323 0.300 1 28 7 7 ALA CB C 19.266 0.300 1 29 7 7 ALA N N 128.951 0.300 1 30 8 8 VAL H H 8.269 0.030 1 31 8 8 VAL C C 176.119 0.300 1 32 8 8 VAL CA C 62.345 0.300 1 33 8 8 VAL CB C 32.893 0.300 1 34 8 8 VAL CG1 C 21.014 0.300 1 35 8 8 VAL CG2 C 21.014 0.300 1 36 8 8 VAL N N 121.304 0.300 1 37 9 9 VAL H H 8.427 0.030 1 38 9 9 VAL C C 175.980 0.300 1 39 9 9 VAL CA C 62.301 0.300 1 40 9 9 VAL CB C 32.761 0.300 1 41 9 9 VAL CG1 C 20.920 0.300 1 42 9 9 VAL CG2 C 20.920 0.300 1 43 9 9 VAL N N 126.345 0.300 1 44 10 10 ARG H H 8.632 0.030 1 45 10 10 ARG C C 176.072 0.300 1 46 10 10 ARG CA C 55.752 0.300 1 47 10 10 ARG CB C 30.871 0.300 1 48 10 10 ARG CG C 27.225 0.300 1 49 10 10 ARG CD C 43.224 0.300 1 50 10 10 ARG N N 126.660 0.300 1 51 11 11 THR H H 8.379 0.030 1 52 11 11 THR C C 172.318 0.300 1 53 11 11 THR CA C 59.928 0.300 1 54 11 11 THR CB C 69.686 0.300 1 55 11 11 THR N N 119.440 0.300 1 56 12 12 PRO C C 174.627 0.300 1 57 12 12 PRO N N 140.753 0.300 1 58 13 13 PRO C C 176.798 0.300 1 59 13 13 PRO CA C 62.829 0.300 1 60 13 13 PRO CB C 32.146 0.300 1 61 13 13 PRO CG C 27.319 0.300 1 62 13 13 PRO CD C 50.470 0.300 1 63 13 13 PRO N N 135.767 0.300 1 64 14 14 LYS H H 8.515 0.030 1 65 14 14 LYS C C 176.655 0.300 1 66 14 14 LYS CA C 56.235 0.300 1 67 14 14 LYS CB C 33.157 0.300 1 68 14 14 LYS CG C 24.778 0.300 1 69 14 14 LYS CD C 29.107 0.300 1 70 14 14 LYS CE C 42.189 0.300 1 71 14 14 LYS N N 122.011 0.300 1 72 15 15 SER H H 8.533 0.030 1 73 15 15 SER C C 172.873 0.300 1 74 15 15 SER CA C 56.323 0.300 1 75 15 15 SER CB C 63.268 0.300 1 76 15 15 SER N N 119.152 0.300 1 77 16 16 PRO C C 177.184 0.300 1 78 16 16 PRO CA C 63.458 0.300 1 79 16 16 PRO CB C 32.119 0.300 1 80 16 16 PRO CG C 27.319 0.300 1 81 16 16 PRO CD C 50.941 0.300 1 82 16 16 PRO N N 138.218 0.300 1 83 17 17 SER H H 8.510 0.030 1 84 17 17 SER C C 174.935 0.300 1 85 17 17 SER CA C 58.554 0.300 1 86 17 17 SER CB C 63.909 0.300 1 87 17 17 SER N N 116.182 0.300 1 88 18 18 SER H H 8.417 0.030 1 89 18 18 SER C C 174.517 0.300 1 90 18 18 SER CA C 58.407 0.300 1 91 18 18 SER CB C 64.018 0.300 1 92 18 18 SER N N 118.350 0.300 1 93 19 19 ALA H H 8.374 0.030 1 94 19 19 ALA C C 178.088 0.300 1 95 19 19 ALA CA C 52.982 0.300 1 96 19 19 ALA CB C 18.958 0.300 1 97 19 19 ALA N N 126.080 0.300 1 98 20 20 LYS H H 8.317 0.030 1 99 20 20 LYS C C 177.019 0.300 1 100 20 20 LYS CA C 56.543 0.300 1 101 20 20 LYS CB C 32.981 0.300 1 102 20 20 LYS CG C 24.872 0.300 1 103 20 20 LYS CD C 29.201 0.300 1 104 20 20 LYS CE C 42.000 0.300 1 105 20 20 LYS N N 120.340 0.300 1 106 21 21 SER H H 8.301 0.030 1 107 21 21 SER C C 174.706 0.300 1 108 21 21 SER CA C 58.565 0.300 1 109 21 21 SER CB C 63.752 0.300 1 110 21 21 SER N N 116.929 0.300 1 111 22 22 ARG H H 8.417 0.030 1 112 22 22 ARG C C 176.304 0.300 1 113 22 22 ARG CA C 56.323 0.300 1 114 22 22 ARG CB C 30.695 0.300 1 115 22 22 ARG CG C 27.131 0.300 1 116 22 22 ARG CD C 43.318 0.300 1 117 22 22 ARG N N 123.209 0.300 1 118 23 23 LEU H H 8.254 0.030 1 119 23 23 LEU C C 177.364 0.300 1 120 23 23 LEU CA C 55.268 0.300 1 121 23 23 LEU CB C 42.344 0.300 1 122 23 23 LEU CG C 27.037 0.300 1 123 23 23 LEU CD1 C 24.778 0.300 2 124 23 23 LEU CD2 C 23.461 0.300 2 125 23 23 LEU N N 123.077 0.300 1 126 24 24 GLN H H 8.471 0.030 1 127 24 24 GLN C C 175.998 0.300 1 128 24 24 GLN CA C 55.708 0.300 1 129 24 24 GLN CB C 29.552 0.300 1 130 24 24 GLN CG C 33.813 0.300 1 131 24 24 GLN N N 121.879 0.300 1 132 25 25 THR H H 8.215 0.030 1 133 25 25 THR C C 173.916 0.300 1 134 25 25 THR CA C 61.642 0.300 1 135 25 25 THR CB C 69.953 0.300 1 136 25 25 THR CG2 C 21.767 0.300 1 137 25 25 THR N N 116.175 0.300 1 138 26 26 ALA H H 8.407 0.030 1 139 26 26 ALA C C 175.392 0.300 1 140 26 26 ALA CA C 50.696 0.300 1 141 26 26 ALA CB C 18.167 0.300 1 142 26 26 ALA N N 128.260 0.300 1 143 27 27 PRO C C 176.689 0.300 1 144 27 27 PRO CA C 62.741 0.300 1 145 27 27 PRO CB C 32.058 0.300 1 146 27 27 PRO CG C 27.319 0.300 1 147 27 27 PRO CD C 50.565 0.300 1 148 27 27 PRO N N 135.692 0.300 1 149 28 28 VAL H H 8.351 0.030 1 150 28 28 VAL C C 174.620 0.300 1 151 28 28 VAL CA C 60.016 0.300 1 152 28 28 VAL CB C 32.673 0.300 1 153 28 28 VAL N N 122.529 0.300 1 154 29 29 PRO C C 176.622 0.300 1 155 29 29 PRO CA C 63.005 0.300 1 156 29 29 PRO CB C 32.146 0.300 1 157 29 29 PRO CG C 27.413 0.300 1 158 29 29 PRO CD C 50.847 0.300 1 159 29 29 PRO N N 139.570 0.300 1 160 30 30 MET H H 8.531 0.030 1 161 30 30 MET C C 174.538 0.300 1 162 30 30 MET CA C 53.334 0.300 1 163 30 30 MET CB C 32.321 0.300 1 164 30 30 MET N N 122.331 0.300 1 165 31 31 PRO C C 176.314 0.300 1 166 31 31 PRO CA C 63.093 0.300 1 167 31 31 PRO CB C 32.233 0.300 1 168 31 31 PRO CG C 27.413 0.300 1 169 31 31 PRO CD C 50.753 0.300 1 170 31 31 PRO N N 137.082 0.300 1 171 32 32 ASP H H 8.514 0.030 1 172 32 32 ASP C C 176.618 0.300 1 173 32 32 ASP CA C 54.081 0.300 1 174 32 32 ASP CB C 40.981 0.300 1 175 32 32 ASP N N 120.899 0.300 1 176 33 33 LEU H H 8.372 0.030 1 177 33 33 LEU C C 177.870 0.300 1 178 33 33 LEU CA C 55.532 0.300 1 179 33 33 LEU CB C 41.773 0.300 1 180 33 33 LEU CG C 26.849 0.300 1 181 33 33 LEU CD1 C 25.060 0.300 2 182 33 33 LEU CD2 C 23.084 0.300 2 183 33 33 LEU N N 124.005 0.300 1 184 34 34 LYS H H 8.364 0.030 1 185 34 34 LYS C C 176.636 0.300 1 186 34 34 LYS CA C 56.894 0.300 1 187 34 34 LYS CB C 32.541 0.300 1 188 34 34 LYS CG C 24.872 0.300 1 189 34 34 LYS CD C 29.013 0.300 1 190 34 34 LYS CE C 42.000 0.300 1 191 34 34 LYS N N 120.529 0.300 1 192 35 35 ASN H H 8.322 0.030 1 193 35 35 ASN C C 175.190 0.300 1 194 35 35 ASN CA C 53.290 0.300 1 195 35 35 ASN CB C 38.739 0.300 1 196 35 35 ASN N N 118.722 0.300 1 197 36 36 VAL H H 8.042 0.030 1 198 36 36 VAL C C 176.382 0.300 1 199 36 36 VAL CA C 62.653 0.300 1 200 36 36 VAL CB C 32.585 0.300 1 201 36 36 VAL CG1 C 20.920 0.300 1 202 36 36 VAL CG2 C 20.920 0.300 1 203 36 36 VAL N N 120.676 0.300 1 204 37 37 LYS H H 8.498 0.030 1 205 37 37 LYS C C 176.743 0.300 1 206 37 37 LYS CA C 56.411 0.300 1 207 37 37 LYS CB C 32.893 0.300 1 208 37 37 LYS CG C 24.872 0.300 1 209 37 37 LYS CD C 28.919 0.300 1 210 37 37 LYS CE C 42.095 0.300 1 211 37 37 LYS N N 125.214 0.300 1 212 38 38 SER H H 8.338 0.030 1 213 38 38 SER C C 174.524 0.300 1 214 38 38 SER CA C 58.433 0.300 1 215 38 38 SER CB C 63.910 0.300 1 216 38 38 SER N N 117.302 0.300 1 217 39 39 LYS H H 8.484 0.030 1 218 39 39 LYS C C 176.692 0.300 1 219 39 39 LYS CA C 56.323 0.300 1 220 39 39 LYS CB C 32.893 0.300 1 221 39 39 LYS CG C 24.778 0.300 1 222 39 39 LYS CD C 29.013 0.300 1 223 39 39 LYS CE C 42.095 0.300 1 224 39 39 LYS N N 123.803 0.300 1 225 40 40 ILE H H 8.256 0.030 1 226 40 40 ILE C C 176.889 0.300 1 227 40 40 ILE CA C 61.598 0.300 1 228 40 40 ILE CB C 38.520 0.300 1 229 40 40 ILE CG1 C 27.413 0.300 1 230 40 40 ILE CG2 C 17.437 0.300 1 231 40 40 ILE CD1 C 12.826 0.300 1 232 40 40 ILE N N 122.664 0.300 1 233 41 41 GLY H H 8.631 0.030 1 234 41 41 GLY C C 174.178 0.300 1 235 41 41 GLY CA C 45.245 0.300 1 236 41 41 GLY N N 113.727 0.300 1 237 42 42 SER H H 8.310 0.030 1 238 42 42 SER C C 175.311 0.300 1 239 42 42 SER CA C 58.301 0.300 1 240 42 42 SER CB C 64.016 0.300 1 241 42 42 SER N N 115.759 0.300 1 242 43 43 THR H H 8.420 0.030 1 243 43 43 THR C C 174.957 0.300 1 244 43 43 THR CA C 62.126 0.300 1 245 43 43 THR CB C 69.511 0.300 1 246 43 43 THR CG2 C 21.672 0.300 1 247 43 43 THR N N 115.978 0.300 1 248 44 44 GLU H H 8.463 0.030 1 249 44 44 GLU C C 176.269 0.300 1 250 44 44 GLU CA C 56.982 0.300 1 251 44 44 GLU CB C 30.123 0.300 1 252 44 44 GLU CG C 36.166 0.300 1 253 44 44 GLU N N 123.160 0.300 1 254 45 45 ASN H H 8.522 0.030 1 255 45 45 ASN C C 175.317 0.300 1 256 45 45 ASN CA C 53.334 0.300 1 257 45 45 ASN CB C 38.651 0.300 1 258 45 45 ASN N N 119.537 0.300 1 259 46 46 LEU H H 8.223 0.030 1 260 46 46 LEU C C 177.516 0.300 1 261 46 46 LEU CA C 55.532 0.300 1 262 46 46 LEU CB C 42.300 0.300 1 263 46 46 LEU CG C 26.943 0.300 1 264 46 46 LEU CD1 C 25.060 0.300 2 265 46 46 LEU CD2 C 23.272 0.300 2 266 46 46 LEU N N 122.463 0.300 1 267 47 47 LYS H H 8.242 0.030 1 268 47 47 LYS C C 176.336 0.300 1 269 47 47 LYS CA C 56.499 0.300 1 270 47 47 LYS CB C 32.761 0.300 1 271 47 47 LYS CG C 24.778 0.300 1 272 47 47 LYS CD C 29.107 0.300 1 273 47 47 LYS CE C 42.095 0.300 1 274 47 47 LYS N N 121.277 0.300 1 275 48 48 HIS H H 8.217 0.030 1 276 48 48 HIS C C 175.130 0.300 1 277 48 48 HIS CA C 56.191 0.300 1 278 48 48 HIS CB C 30.959 0.300 1 279 48 48 HIS N N 120.449 0.300 1 280 49 49 GLN H H 8.359 0.030 1 281 49 49 GLN C C 173.841 0.300 1 282 49 49 GLN CA C 53.422 0.300 1 283 49 49 GLN CB C 28.893 0.300 1 284 49 49 GLN N N 123.282 0.300 1 285 50 50 PRO C C 177.780 0.300 1 286 50 50 PRO CA C 63.444 0.300 1 287 50 50 PRO CB C 31.970 0.300 1 288 50 50 PRO CG C 27.413 0.300 1 289 50 50 PRO CD C 50.753 0.300 1 290 50 50 PRO N N 137.683 0.300 1 291 51 51 GLY H H 8.707 0.030 1 292 51 51 GLY C C 175.020 0.300 1 293 51 51 GLY CA C 45.421 0.300 1 294 51 51 GLY N N 110.279 0.300 1 295 52 52 GLY H H 8.409 0.030 1 296 52 52 GLY C C 174.810 0.300 1 297 52 52 GLY CA C 45.465 0.300 1 298 52 52 GLY N N 108.853 0.300 1 299 53 53 GLY H H 8.396 0.030 1 300 53 53 GLY C C 174.026 0.300 1 301 53 53 GLY CA C 45.245 0.300 1 302 53 53 GLY N N 108.739 0.300 1 303 54 54 LYS H H 8.229 0.030 1 304 54 54 LYS C C 176.707 0.300 1 305 54 54 LYS CA C 56.235 0.300 1 306 54 54 LYS CB C 32.981 0.300 1 307 54 54 LYS CG C 24.778 0.300 1 308 54 54 LYS CD C 29.107 0.300 1 309 54 54 LYS CE C 42.095 0.300 1 310 54 54 LYS N N 120.925 0.300 1 311 55 55 VAL H H 8.274 0.030 1 312 55 55 VAL C C 175.992 0.300 1 313 55 55 VAL CA C 62.389 0.300 1 314 55 55 VAL CB C 32.761 0.300 1 315 55 55 VAL CG1 C 21.014 0.300 1 316 55 55 VAL CG2 C 21.014 0.300 1 317 55 55 VAL N N 122.455 0.300 1 318 56 56 GLN H H 8.598 0.030 1 319 56 56 GLN C C 175.554 0.300 1 320 56 56 GLN CA C 55.576 0.300 1 321 56 56 GLN CB C 29.640 0.300 1 322 56 56 GLN CG C 33.625 0.300 1 323 56 56 GLN N N 125.570 0.300 1 324 57 57 ILE H H 8.437 0.030 1 325 57 57 ILE C C 176.108 0.300 1 326 57 57 ILE CA C 61.026 0.300 1 327 57 57 ILE CB C 38.564 0.300 1 328 57 57 ILE CG1 C 27.319 0.300 1 329 57 57 ILE CG2 C 17.532 0.300 1 330 57 57 ILE CD1 C 12.732 0.300 1 331 57 57 ILE N N 124.463 0.300 1 332 58 58 ILE H H 8.414 0.030 1 333 58 58 ILE C C 175.710 0.300 1 334 58 58 ILE CA C 60.851 0.300 1 335 58 58 ILE CB C 38.651 0.300 1 336 58 58 ILE CG1 C 27.319 0.300 1 337 58 58 ILE CG2 C 17.343 0.300 1 338 58 58 ILE CD1 C 12.732 0.300 1 339 58 58 ILE N N 126.477 0.300 1 340 59 59 ASN H H 8.654 0.030 1 341 59 59 ASN C C 175.023 0.300 1 342 59 59 ASN CA C 53.026 0.300 1 343 59 59 ASN CB C 39.003 0.300 1 344 59 59 ASN N N 124.280 0.300 1 345 60 60 LYS H H 8.450 0.030 1 346 60 60 LYS C C 176.398 0.300 1 347 60 60 LYS CA C 56.558 0.300 1 348 60 60 LYS CB C 32.849 0.300 1 349 60 60 LYS CG C 24.778 0.300 1 350 60 60 LYS CD C 29.107 0.300 1 351 60 60 LYS CE C 42.095 0.300 1 352 60 60 LYS N N 123.207 0.300 1 353 61 61 LYS H H 8.392 0.030 1 354 61 61 LYS C C 176.487 0.300 1 355 61 61 LYS CA C 56.499 0.300 1 356 61 61 LYS CB C 32.862 0.300 1 357 61 61 LYS CG C 24.872 0.300 1 358 61 61 LYS CD C 29.107 0.300 1 359 61 61 LYS CE C 42.189 0.300 1 360 61 61 LYS N N 122.918 0.300 1 361 62 62 LEU H H 8.266 0.030 1 362 62 62 LEU C C 176.757 0.300 1 363 62 62 LEU CA C 55.092 0.300 1 364 62 62 LEU CB C 42.476 0.300 1 365 62 62 LEU CG C 27.037 0.300 1 366 62 62 LEU CD1 C 24.684 0.300 2 367 62 62 LEU CD2 C 23.649 0.300 2 368 62 62 LEU N N 123.951 0.300 1 369 63 63 ASP H H 8.433 0.030 1 370 63 63 ASP C C 176.461 0.300 1 371 63 63 ASP CA C 53.993 0.300 1 372 63 63 ASP CB C 41.069 0.300 1 373 63 63 ASP N N 122.262 0.300 1 374 64 64 LEU H H 8.460 0.030 1 375 64 64 LEU C C 177.923 0.300 1 376 64 64 LEU CA C 55.224 0.300 1 377 64 64 LEU CB C 41.729 0.300 1 378 64 64 LEU CG C 26.943 0.300 1 379 64 64 LEU CD1 C 25.155 0.300 2 380 64 64 LEU CD2 C 22.990 0.300 2 381 64 64 LEU N N 124.199 0.300 1 382 65 65 SER H H 8.432 0.030 1 383 65 65 SER C C 174.635 0.300 1 384 65 65 SER CA C 59.532 0.300 1 385 65 65 SER CB C 63.532 0.300 1 386 65 65 SER N N 116.181 0.300 1 387 66 66 ASN H H 8.371 0.030 1 388 66 66 ASN C C 175.364 0.300 1 389 66 66 ASN CA C 53.334 0.300 1 390 66 66 ASN CB C 38.827 0.300 1 391 66 66 ASN N N 120.476 0.300 1 392 67 67 VAL H H 8.026 0.030 1 393 67 67 VAL C C 176.497 0.300 1 394 67 67 VAL CA C 62.917 0.300 1 395 67 67 VAL CB C 32.541 0.300 1 396 67 67 VAL CG1 C 20.920 0.300 1 397 67 67 VAL CG2 C 20.920 0.300 1 398 67 67 VAL N N 120.347 0.300 1 399 68 68 GLN H H 8.532 0.030 1 400 68 68 GLN C C 176.256 0.300 1 401 68 68 GLN CA C 56.059 0.300 1 402 68 68 GLN CB C 29.332 0.300 1 403 68 68 GLN CG C 33.813 0.300 1 404 68 68 GLN N N 123.883 0.300 1 405 69 69 SER H H 8.410 0.030 1 406 69 69 SER C C 174.786 0.300 1 407 69 69 SER CA C 58.521 0.300 1 408 69 69 SER CB C 63.840 0.300 1 409 69 69 SER N N 117.424 0.300 1 410 70 70 LYS H H 8.495 0.030 1 411 70 70 LYS C C 176.701 0.300 1 412 70 70 LYS CA C 56.587 0.300 1 413 70 70 LYS CB C 32.810 0.300 1 414 70 70 LYS CG C 24.872 0.300 1 415 70 70 LYS CD C 29.013 0.300 1 416 70 70 LYS CE C 42.095 0.300 1 417 70 70 LYS N N 123.479 0.300 1 418 71 71 CYS H H 8.418 0.030 1 419 71 71 CYS C C 175.315 0.300 1 420 71 71 CYS CA C 59.092 0.300 1 421 71 71 CYS CB C 28.145 0.300 1 422 71 71 CYS N N 120.361 0.300 1 423 72 72 GLY H H 8.587 0.030 1 424 72 72 GLY C C 174.223 0.300 1 425 72 72 GLY CA C 45.421 0.300 1 426 72 72 GLY N N 111.939 0.300 1 427 73 73 SER H H 8.346 0.030 1 428 73 73 SER C C 175.090 0.300 1 429 73 73 SER CA C 58.565 0.300 1 430 73 73 SER CB C 63.928 0.300 1 431 73 73 SER N N 116.041 0.300 1 432 74 74 LYS H H 8.558 0.030 1 433 74 74 LYS C C 176.425 0.300 1 434 74 74 LYS CA C 56.587 0.300 1 435 74 74 LYS CB C 32.761 0.300 1 436 74 74 LYS CG C 24.684 0.300 1 437 74 74 LYS CD C 29.013 0.300 1 438 74 74 LYS CE C 42.189 0.300 1 439 74 74 LYS N N 123.297 0.300 1 440 75 75 ASP H H 8.272 0.030 1 441 75 75 ASP C C 175.901 0.300 1 442 75 75 ASP CA C 54.565 0.300 1 443 75 75 ASP CB C 41.157 0.300 1 444 75 75 ASP N N 120.524 0.300 1 445 76 76 ASN H H 8.363 0.030 1 446 76 76 ASN C C 175.092 0.300 1 447 76 76 ASN CA C 53.334 0.300 1 448 76 76 ASN CB C 38.827 0.300 1 449 76 76 ASN N N 118.791 0.300 1 450 77 77 ILE H H 8.064 0.030 1 451 77 77 ILE C C 176.092 0.300 1 452 77 77 ILE CA C 61.290 0.300 1 453 77 77 ILE CB C 38.520 0.300 1 454 77 77 ILE CG1 C 27.319 0.300 1 455 77 77 ILE CG2 C 17.532 0.300 1 456 77 77 ILE CD1 C 13.014 0.300 1 457 77 77 ILE N N 121.195 0.300 1 458 78 78 LYS H H 8.404 0.030 1 459 78 78 LYS C C 176.007 0.300 1 460 78 78 LYS CA C 56.015 0.300 1 461 78 78 LYS CB C 33.025 0.300 1 462 78 78 LYS CG C 24.684 0.300 1 463 78 78 LYS CD C 29.013 0.300 1 464 78 78 LYS CE C 42.095 0.300 1 465 78 78 LYS N N 125.575 0.300 1 466 79 79 HIS H H 8.402 0.030 1 467 79 79 HIS C C 175.050 0.300 1 468 79 79 HIS CA C 56.323 0.300 1 469 79 79 HIS CB C 31.047 0.300 1 470 79 79 HIS N N 122.436 0.300 1 471 80 80 VAL H H 8.217 0.030 1 472 80 80 VAL C C 174.194 0.300 1 473 80 80 VAL CA C 59.576 0.300 1 474 80 80 VAL CB C 32.761 0.300 1 475 80 80 VAL N N 124.661 0.300 1 476 81 81 PRO C C 177.684 0.300 1 477 81 81 PRO CA C 63.620 0.300 1 478 81 81 PRO CB C 32.146 0.300 1 479 81 81 PRO CG C 27.507 0.300 1 480 81 81 PRO CD C 50.941 0.300 1 481 81 81 PRO N N 139.673 0.300 1 482 82 82 GLY H H 8.692 0.030 1 483 82 82 GLY C C 174.994 0.300 1 484 82 82 GLY CA C 45.377 0.300 1 485 82 82 GLY N N 110.505 0.300 1 486 83 83 GLY H H 8.433 0.030 1 487 83 83 GLY C C 174.820 0.300 1 488 83 83 GLY CA C 45.333 0.300 1 489 83 83 GLY N N 108.933 0.300 1 490 84 84 GLY H H 8.429 0.030 1 491 84 84 GLY C C 174.178 0.300 1 492 84 84 GLY CA C 45.267 0.300 1 493 84 84 GLY N N 108.975 0.300 1 494 85 85 SER H H 8.311 0.030 1 495 85 85 SER C C 174.550 0.300 1 496 85 85 SER CA C 58.275 0.300 1 497 85 85 SER CB C 64.001 0.300 1 498 85 85 SER N N 115.752 0.300 1 499 86 86 VAL H H 8.263 0.030 1 500 86 86 VAL C C 175.969 0.300 1 501 86 86 VAL CA C 62.301 0.300 1 502 86 86 VAL CB C 32.849 0.300 1 503 86 86 VAL CG1 C 20.920 0.300 1 504 86 86 VAL CG2 C 20.920 0.300 1 505 86 86 VAL N N 122.092 0.300 1 506 87 87 GLN H H 8.531 0.030 1 507 87 87 GLN C C 175.594 0.300 1 508 87 87 GLN CA C 55.620 0.300 1 509 87 87 GLN CB C 29.420 0.300 1 510 87 87 GLN CG C 33.719 0.300 1 511 87 87 GLN N N 125.082 0.300 1 512 88 88 ILE H H 8.373 0.030 1 513 88 88 ILE C C 175.758 0.300 1 514 88 88 ILE CA C 60.983 0.300 1 515 88 88 ILE CB C 38.695 0.300 1 516 88 88 ILE CG1 C 27.507 0.300 1 517 88 88 ILE CG2 C 17.343 0.300 1 518 88 88 ILE CD1 C 12.732 0.300 1 519 88 88 ILE N N 124.526 0.300 1 520 89 89 VAL H H 8.291 0.030 1 521 89 89 VAL C C 175.507 0.300 1 522 89 89 VAL CA C 61.818 0.300 1 523 89 89 VAL CB C 32.893 0.300 1 524 89 89 VAL CG1 C 20.920 0.300 1 525 89 89 VAL CG2 C 20.920 0.300 1 526 89 89 VAL N N 126.040 0.300 1 527 90 90 TYR H H 8.547 0.030 1 528 90 90 TYR C C 175.063 0.300 1 529 90 90 TYR CA C 57.993 0.300 1 530 90 90 TYR CB C 38.959 0.300 1 531 90 90 TYR N N 126.611 0.300 1 532 91 91 LYS H H 8.241 0.030 1 533 91 91 LYS C C 173.529 0.300 1 534 91 91 LYS CA C 53.685 0.300 1 535 91 91 LYS CB C 32.937 0.300 1 536 91 91 LYS N N 126.310 0.300 1 537 92 92 PRO C C 176.878 0.300 1 538 92 92 PRO CA C 62.917 0.300 1 539 92 92 PRO CB C 32.058 0.300 1 540 92 92 PRO CG C 27.225 0.300 1 541 92 92 PRO CD C 50.659 0.300 1 542 92 92 PRO N N 136.791 0.300 1 543 93 93 VAL H H 8.278 0.030 1 544 93 93 VAL C C 175.673 0.300 1 545 93 93 VAL CA C 62.565 0.300 1 546 93 93 VAL CB C 32.805 0.300 1 547 93 93 VAL CG1 C 20.920 0.300 1 548 93 93 VAL CG2 C 20.920 0.300 1 549 93 93 VAL N N 120.839 0.300 1 550 94 94 ASP H H 8.472 0.030 1 551 94 94 ASP C C 176.673 0.300 1 552 94 94 ASP CA C 53.510 0.300 1 553 94 94 ASP CB C 40.937 0.300 1 554 94 94 ASP N N 124.604 0.300 1 555 95 95 LEU H H 8.630 0.030 1 556 95 95 LEU C C 178.079 0.300 1 557 95 95 LEU CA C 55.532 0.300 1 558 95 95 LEU CB C 41.685 0.300 1 559 95 95 LEU CG C 27.037 0.300 1 560 95 95 LEU CD1 C 25.060 0.300 2 561 95 95 LEU CD2 C 22.990 0.300 2 562 95 95 LEU N N 125.572 0.300 1 563 96 96 SER H H 8.485 0.030 1 564 96 96 SER C C 174.941 0.300 1 565 96 96 SER CA C 59.708 0.300 1 566 96 96 SER CB C 63.334 0.300 1 567 96 96 SER N N 116.285 0.300 1 568 97 97 LYS H H 8.023 0.030 1 569 97 97 LYS C C 176.638 0.300 1 570 97 97 LYS CA C 56.059 0.300 1 571 97 97 LYS CB C 32.849 0.300 1 572 97 97 LYS CG C 24.778 0.300 1 573 97 97 LYS CD C 29.013 0.300 1 574 97 97 LYS CE C 42.189 0.300 1 575 97 97 LYS N N 122.231 0.300 1 576 98 98 VAL H H 8.019 0.030 1 577 98 98 VAL C C 176.564 0.300 1 578 98 98 VAL CA C 62.741 0.300 1 579 98 98 VAL CB C 32.717 0.300 1 580 98 98 VAL CG1 C 21.014 0.300 1 581 98 98 VAL CG2 C 21.014 0.300 1 582 98 98 VAL N N 121.344 0.300 1 583 99 99 THR H H 8.346 0.030 1 584 99 99 THR C C 174.549 0.300 1 585 99 99 THR CA C 61.818 0.300 1 586 99 99 THR CB C 69.906 0.300 1 587 99 99 THR CG2 C 21.672 0.300 1 588 99 99 THR N N 118.372 0.300 1 589 100 100 SER H H 8.380 0.030 1 590 100 100 SER C C 174.473 0.300 1 591 100 100 SER CA C 58.213 0.300 1 592 100 100 SER CB C 64.104 0.300 1 593 100 100 SER N N 118.663 0.300 1 594 101 101 LYS H H 8.524 0.030 1 595 101 101 LYS C C 176.591 0.300 1 596 101 101 LYS CA C 56.411 0.300 1 597 101 101 LYS CB C 32.810 0.300 1 598 101 101 LYS CG C 24.684 0.300 1 599 101 101 LYS CD C 29.107 0.300 1 600 101 101 LYS CE C 42.095 0.300 1 601 101 101 LYS N N 123.698 0.300 1 602 102 102 CYS H H 8.515 0.030 1 603 102 102 CYS C C 175.137 0.300 1 604 102 102 CYS CA C 58.829 0.300 1 605 102 102 CYS CB C 28.057 0.300 1 606 102 102 CYS N N 120.912 0.300 1 607 103 103 GLY H H 8.572 0.030 1 608 103 103 GLY C C 173.296 0.300 1 609 103 103 GLY CA C 45.377 0.300 1 610 103 103 GLY N N 112.454 0.300 1 611 104 104 SER H H 7.992 0.030 1 612 104 104 SER C C 178.773 0.300 1 613 104 104 SER CA C 60.016 0.300 1 614 104 104 SER CB C 65.027 0.300 1 615 104 104 SER N N 121.499 0.300 1 stop_ save_