data_27537 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Chemical Shift Assignments for the C-terminal domain of histone H1.0 ; _BMRB_accession_number 27537 _BMRB_flat_file_name bmr27537.str _Entry_type original _Submission_date 2018-07-06 _Accession_date 2018-07-06 _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 Jimenez 'M. Angeles' . . 2 Pantoja-Uceda David . . 3 Chaves-Arquero Belen . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 heteronucl_NOE 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 55 "13C chemical shifts" 284 "15N chemical shifts" 95 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2019-01-24 update BMRB 'update entry citation' 2018-11-16 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 27538 'Chemical Shift Assignments for the triphosphorylated C-terminal domain of histone H1.0' stop_ _Original_release_date 2018-07-06 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; A CON-based NMR assignment strategy for pro-rich intrinsically disordered proteins with low signal dispersion: the C-terminal domain of histone H1.0 as a case study ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 30414042 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Chaves-Arquero Belen . . 2 Pantoja-Uceda David . . 3 Roque Alicia . . 4 Ponte Inmaculada . . 5 Suau Pedro . . 6 Jimenez 'M. Angeles' . . stop_ _Journal_abbreviation 'J. Biomol. NMR' _Journal_volume 72 _Journal_issue 3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 139 _Page_last 148 _Year 2018 _Details . loop_ _Keyword IDP 'assignment strategy' histone stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name C-H1.0 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label C-H1.0 $C-H1.0 stop_ _System_molecular_weight . _System_physical_state 'intrinsically disordered' _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_C-H1.0 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common C-H1.0 _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 105 _Mol_residue_sequence ; MDEPKRSVAFKKTKKEVKKV ATPKKAAKPKKAASKAPSKK PKATPVKKAKKKPAATPKKA KKPKVVKVKPVKASKPKKAK TVKPKAKSSAKRASKKKRSH HHHHH ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ASP 3 GLU 4 PRO 5 LYS 6 ARG 7 SER 8 VAL 9 ALA 10 PHE 11 LYS 12 LYS 13 THR 14 LYS 15 LYS 16 GLU 17 VAL 18 LYS 19 LYS 20 VAL 21 ALA 22 THR 23 PRO 24 LYS 25 LYS 26 ALA 27 ALA 28 LYS 29 PRO 30 LYS 31 LYS 32 ALA 33 ALA 34 SER 35 LYS 36 ALA 37 PRO 38 SER 39 LYS 40 LYS 41 PRO 42 LYS 43 ALA 44 THR 45 PRO 46 VAL 47 LYS 48 LYS 49 ALA 50 LYS 51 LYS 52 LYS 53 PRO 54 ALA 55 ALA 56 THR 57 PRO 58 LYS 59 LYS 60 ALA 61 LYS 62 LYS 63 PRO 64 LYS 65 VAL 66 VAL 67 LYS 68 VAL 69 LYS 70 PRO 71 VAL 72 LYS 73 ALA 74 SER 75 LYS 76 PRO 77 LYS 78 LYS 79 ALA 80 LYS 81 THR 82 VAL 83 LYS 84 PRO 85 LYS 86 ALA 87 LYS 88 SER 89 SER 90 ALA 91 LYS 92 ARG 93 ALA 94 SER 95 LYS 96 LYS 97 LYS 98 ARG 99 SER 100 HIS 101 HIS 102 HIS 103 HIS 104 HIS 105 HIS 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 $C-H1.0 Mouse 10090 Eukaryota Metazoa Mus musculus stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $C-H1.0 'recombinant technology' . Escherichia coli . pCTH1.0 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 $C-H1.0 1 mM '[U-100% 13C; U-100% 15N]' H2O 90 % 'natural abundance' D2O 10 % '[U-100% 2H]' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $C-H1.0 1 mM '[U-100% 13C; U-100% 15N]' H2O 90 % 'natural abundance' D2O 10 % '[U-100% 2H]' 'sodium phosphate' 10 mM 'natural abundance' 'sodium chloride' 10 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version 2.1 loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection 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_ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_NMRView _Saveframe_category software _Name NMRView _Version . loop_ _Vendor _Address _Electronic_address 'Johnson, One Moon Scientific' . . stop_ loop_ _Task 'chemical shift assignment' 'peak picking' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _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_2D_CON_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D CON' _Sample_label $sample_1 save_ save_3D_hacacoNcaNCO_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D hacacoNcaNCO' _Sample_label $sample_1 save_ save_3D_hacaCOncaNCO_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D hacaCOncaNCO' _Sample_label $sample_1 save_ save_3D_CBCANCO_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCANCO' _Sample_label $sample_1 save_ save_3D_HNCO_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_2D_1H-15N-HETNOE_7 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-15N-HETNOE' _Sample_label $sample_2 save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 5.5 . 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 . 'insert at center of experimental sample tube' . 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_ _Software_label $TOPSPIN $SPARKY $NMRPipe $NMRView stop_ loop_ _Experiment_label '2D 1H-15N HSQC' '2D CON' '3D hacacoNcaNCO' '3D hacaCOncaNCO' '3D CBCANCO' '3D HNCO' 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 C-H1.0 _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 1 1 MET C C 173.272 0.200 1 2 1 1 MET CA C 55.260 0.200 1 3 1 1 MET CB C 33.305 0.200 1 4 2 2 ASP C C 175.521 0.200 1 5 2 2 ASP CA C 54.668 0.200 1 6 2 2 ASP CB C 41.165 0.200 1 7 2 2 ASP N N 123.928 0.200 1 8 3 3 GLU H H 8.568 0.020 1 9 3 3 GLU C C 174.610 0.200 1 10 3 3 GLU CA C 54.771 0.200 1 11 3 3 GLU CB C 29.777 0.200 1 12 3 3 GLU N N 122.944 0.200 1 13 4 4 PRO C C 177.025 0.200 1 14 4 4 PRO CA C 63.365 0.200 1 15 4 4 PRO CB C 32.051 0.200 1 16 4 4 PRO N N 137.535 0.200 1 17 5 5 LYS C C 176.868 0.200 1 18 5 5 LYS CA C 56.560 0.200 1 19 5 5 LYS CB C 32.203 0.200 1 20 5 5 LYS N N 121.497 0.200 1 21 6 6 ARG C C 176.418 0.200 1 22 6 6 ARG CA C 56.333 0.200 1 23 6 6 ARG CB C 30.974 0.200 1 24 6 6 ARG N N 122.460 0.200 1 25 7 7 SER H H 8.401 0.020 1 26 7 7 SER C C 174.731 0.200 1 27 7 7 SER CA C 58.437 0.200 1 28 7 7 SER CB C 63.982 0.200 1 29 7 7 SER N N 117.401 0.200 1 30 8 8 VAL H H 8.177 0.020 1 31 8 8 VAL C C 175.837 0.200 1 32 8 8 VAL CA C 62.417 0.200 1 33 8 8 VAL CB C 32.908 0.200 1 34 8 8 VAL N N 121.615 0.200 1 35 9 9 ALA H H 8.272 0.020 1 36 9 9 ALA C C 177.413 0.200 1 37 9 9 ALA CA C 52.636 0.200 1 38 9 9 ALA CB C 19.098 0.200 1 39 9 9 ALA N N 126.936 0.200 1 40 10 10 PHE H H 8.129 0.020 1 41 10 10 PHE C C 175.592 0.200 1 42 10 10 PHE CA C 57.902 0.200 1 43 10 10 PHE CB C 39.621 0.200 1 44 10 10 PHE N N 119.819 0.200 1 45 11 11 LYS H H 8.151 0.020 1 46 11 11 LYS C C 176.036 0.200 1 47 11 11 LYS CA C 56.230 0.200 1 48 11 11 LYS CB C 33.214 0.200 1 49 11 11 LYS N N 123.552 0.200 1 50 12 12 LYS H H 8.338 0.020 1 51 12 12 LYS C C 176.755 0.200 1 52 12 12 LYS CA C 56.533 0.200 1 53 12 12 LYS CB C 33.097 0.200 1 54 12 12 LYS N N 123.321 0.200 1 55 13 13 THR H H 8.226 0.020 1 56 13 13 THR C C 174.395 0.200 1 57 13 13 THR CA C 62.268 0.200 1 58 13 13 THR CB C 70.451 0.200 1 59 13 13 THR N N 116.450 0.200 1 60 14 14 LYS C C 176.328 0.200 1 61 14 14 LYS CA C 56.385 0.200 1 62 14 14 LYS CB C 33.072 0.200 1 63 14 14 LYS N N 124.457 0.200 1 64 15 15 LYS C C 176.345 0.200 1 65 15 15 LYS CA C 56.602 0.200 1 66 15 15 LYS CB C 33.037 0.200 1 67 15 15 LYS N N 123.644 0.200 1 68 16 16 GLU H H 8.508 0.020 1 69 16 16 GLU C C 176.256 0.200 1 70 16 16 GLU CA C 56.405 0.200 1 71 16 16 GLU CB C 30.486 0.200 1 72 16 16 GLU N N 123.481 0.200 1 73 17 17 VAL C C 176.024 0.200 1 74 17 17 VAL CA C 62.327 0.200 1 75 17 17 VAL CB C 32.801 0.200 1 76 17 17 VAL N N 123.001 0.200 1 77 18 18 LYS H H 8.397 0.020 1 78 18 18 LYS C C 176.281 0.200 1 79 18 18 LYS CA C 56.355 0.200 1 80 18 18 LYS CB C 33.051 0.200 1 81 18 18 LYS N N 126.105 0.200 1 82 19 19 LYS H H 8.450 0.020 1 83 19 19 LYS C C 176.392 0.200 1 84 19 19 LYS CA C 56.405 0.200 1 85 19 19 LYS CB C 33.073 0.200 1 86 19 19 LYS N N 124.154 0.200 1 87 20 20 VAL H H 8.260 0.020 1 88 20 20 VAL C C 175.682 0.200 1 89 20 20 VAL CA C 62.135 0.200 1 90 20 20 VAL CB C 33.078 0.200 1 91 20 20 VAL N N 122.561 0.200 1 92 21 21 ALA H H 8.497 0.020 1 93 21 21 ALA C C 177.492 0.200 1 94 21 21 ALA CA C 52.344 0.200 1 95 21 21 ALA CB C 19.271 0.200 1 96 21 21 ALA N N 128.790 0.200 1 97 22 22 THR H H 8.282 0.020 1 98 22 22 THR C C 172.943 0.200 1 99 22 22 THR CA C 59.922 0.200 1 100 22 22 THR CB C 69.755 0.200 1 101 22 22 THR N N 117.098 0.200 1 102 23 23 PRO C C 176.891 0.200 1 103 23 23 PRO CA C 63.369 0.200 1 104 23 23 PRO CB C 32.203 0.200 1 105 23 23 PRO N N 139.269 0.200 1 106 24 24 LYS H H 8.439 0.020 1 107 24 24 LYS C C 176.729 0.200 1 108 24 24 LYS CA C 56.560 0.200 1 109 24 24 LYS CB C 33.079 0.200 1 110 24 24 LYS N N 122.407 0.200 1 111 25 25 LYS C C 176.144 0.200 1 112 25 25 LYS CA C 56.355 0.200 1 113 25 25 LYS CB C 33.086 0.200 1 114 25 25 LYS N N 123.206 0.200 1 115 26 26 ALA C C 177.268 0.200 1 116 26 26 ALA CA C 52.331 0.200 1 117 26 26 ALA CB C 19.260 0.200 1 118 26 26 ALA N N 126.237 0.200 1 119 27 27 ALA H H 8.344 0.020 1 120 27 27 ALA C C 177.536 0.200 1 121 27 27 ALA CA C 52.245 0.200 1 122 27 27 ALA CB C 19.260 0.200 1 123 27 27 ALA N N 124.345 0.200 1 124 28 28 LYS H H 8.393 0.020 1 125 28 28 LYS C C 174.615 0.200 1 126 28 28 LYS CA C 54.313 0.200 1 127 28 28 LYS CB C 32.430 0.200 1 128 28 28 LYS N N 122.480 0.200 1 129 29 29 PRO C C 176.885 0.200 1 130 29 29 PRO CA C 63.256 0.200 1 131 29 29 PRO CB C 32.373 0.200 1 132 29 29 PRO N N 137.353 0.200 1 133 30 30 LYS C C 176.725 0.200 1 134 30 30 LYS CA C 56.404 0.200 1 135 30 30 LYS CB C 33.249 0.200 1 136 30 30 LYS N N 122.443 0.200 1 137 31 31 LYS C C 176.216 0.200 1 138 31 31 LYS CA C 56.376 0.200 1 139 31 31 LYS CB C 33.178 0.200 1 140 31 31 LYS N N 123.321 0.200 1 141 32 32 ALA C C 177.428 0.200 1 142 32 32 ALA CA C 52.432 0.200 1 143 32 32 ALA CB C 19.233 0.200 1 144 32 32 ALA N N 126.444 0.200 1 145 33 33 ALA H H 8.397 0.020 1 146 33 33 ALA C C 177.885 0.200 1 147 33 33 ALA CA C 52.622 0.200 1 148 33 33 ALA CB C 19.190 0.200 1 149 33 33 ALA N N 124.112 0.200 1 150 34 34 SER H H 8.352 0.020 1 151 34 34 SER C C 174.455 0.200 1 152 34 34 SER CA C 58.339 0.200 1 153 34 34 SER CB C 64.098 0.200 1 154 34 34 SER N N 115.762 0.200 1 155 35 35 LYS C C 175.976 0.200 1 156 35 35 LYS CA C 56.231 0.200 1 157 35 35 LYS CB C 33.103 0.200 1 158 35 35 LYS N N 123.604 0.200 1 159 36 36 ALA H H 8.398 0.020 1 160 36 36 ALA C C 175.539 0.200 1 161 36 36 ALA CA C 50.588 0.200 1 162 36 36 ALA CB C 18.002 0.200 1 163 36 36 ALA N N 127.225 0.200 1 164 37 37 PRO C C 177.063 0.200 1 165 37 37 PRO CA C 63.066 0.200 1 166 37 37 PRO CB C 32.094 0.200 1 167 37 37 PRO N N 135.823 0.200 1 168 38 38 SER H H 8.471 0.020 1 169 38 38 SER C C 174.670 0.200 1 170 38 38 SER CA C 58.506 0.200 1 171 38 38 SER CB C 64.088 0.200 1 172 38 38 SER N N 116.689 0.200 1 173 39 39 LYS C C 176.315 0.200 1 174 39 39 LYS CA C 56.355 0.200 1 175 39 39 LYS CB C 33.084 0.200 1 176 39 39 LYS N N 123.699 0.200 1 177 40 40 LYS C C 174.538 0.200 1 178 40 40 LYS CA C 54.296 0.200 1 179 40 40 LYS CB C 32.375 0.200 1 180 40 40 LYS N N 124.432 0.200 1 181 41 41 PRO C C 176.850 0.200 1 182 41 41 PRO CA C 63.143 0.200 1 183 41 41 PRO CB C 32.147 0.200 1 184 41 41 PRO N N 137.414 0.200 1 185 42 42 LYS C C 176.368 0.200 1 186 42 42 LYS CA C 56.362 0.200 1 187 42 42 LYS CB C 33.221 0.200 1 188 42 42 LYS N N 122.219 0.200 1 189 43 43 ALA C C 177.552 0.200 1 190 43 43 ALA CA C 52.204 0.200 1 191 43 43 ALA CB C 19.234 0.200 1 192 43 43 ALA N N 126.023 0.200 1 193 44 44 THR H H 8.322 0.020 1 194 44 44 THR C C 172.928 0.200 1 195 44 44 THR CA C 60.068 0.200 1 196 44 44 THR CB C 69.811 0.200 1 197 44 44 THR N N 117.317 0.200 1 198 45 45 PRO C C 176.834 0.200 1 199 45 45 PRO CA C 63.226 0.200 1 200 45 45 PRO CB C 32.121 0.200 1 201 45 45 PRO N N 139.279 0.200 1 202 46 46 VAL H H 8.297 0.020 1 203 46 46 VAL C C 176.234 0.200 1 204 46 46 VAL CA C 62.652 0.200 1 205 46 46 VAL CB C 32.914 0.200 1 206 46 46 VAL N N 121.403 0.200 1 207 47 47 LYS C C 176.340 0.200 1 208 47 47 LYS CA C 56.397 0.200 1 209 47 47 LYS CB C 33.028 0.200 1 210 47 47 LYS N N 126.175 0.200 1 211 48 48 LYS H H 8.402 0.020 1 212 48 48 LYS C C 176.172 0.200 1 213 48 48 LYS CA C 56.334 0.200 1 214 48 48 LYS CB C 33.274 0.200 1 215 48 48 LYS N N 124.009 0.200 1 216 49 49 ALA C C 177.618 0.200 1 217 49 49 ALA CA C 52.295 0.200 1 218 49 49 ALA CB C 19.284 0.200 1 219 49 49 ALA N N 126.285 0.200 1 220 50 50 LYS H H 8.402 0.020 1 221 50 50 LYS C C 176.582 0.200 1 222 50 50 LYS CA C 56.411 0.200 1 223 50 50 LYS CB C 33.038 0.200 1 224 50 50 LYS N N 121.854 0.200 1 225 51 51 LYS H H 8.444 0.020 1 226 51 51 LYS C C 176.335 0.200 1 227 51 51 LYS CA C 56.342 0.200 1 228 51 51 LYS CB C 33.151 0.200 1 229 51 51 LYS N N 123.663 0.200 1 230 52 52 LYS H H 8.500 0.020 1 231 52 52 LYS C C 174.537 0.200 1 232 52 52 LYS N N 125.092 0.200 1 233 53 53 PRO C C 176.582 0.200 1 234 53 53 PRO CA C 63.077 0.200 1 235 53 53 PRO CB C 32.156 0.200 1 236 53 53 PRO N N 137.419 0.200 1 237 54 54 ALA H H 8.429 0.020 1 238 54 54 ALA C C 177.465 0.200 1 239 54 54 ALA CA C 52.324 0.200 1 240 54 54 ALA CB C 19.254 0.200 1 241 54 54 ALA N N 124.806 0.200 1 242 55 55 ALA H H 8.365 0.020 1 243 55 55 ALA C C 177.657 0.200 1 244 55 55 ALA CA C 52.191 0.200 1 245 55 55 ALA CB C 19.191 0.200 1 246 55 55 ALA N N 123.921 0.200 1 247 56 56 THR H H 8.294 0.020 1 248 56 56 THR C C 172.948 0.200 1 249 56 56 THR CA C 60.007 0.200 1 250 56 56 THR CB C 69.857 0.200 1 251 56 56 THR N N 116.814 0.200 1 252 57 57 PRO C C 176.867 0.200 1 253 57 57 PRO CA C 63.200 0.200 1 254 57 57 PRO CB C 32.175 0.200 1 255 57 57 PRO N N 139.343 0.200 1 256 58 58 LYS H H 8.468 0.020 1 257 58 58 LYS C C 176.704 0.200 1 258 58 58 LYS CA C 56.460 0.200 1 259 58 58 LYS CB C 33.095 0.200 1 260 58 58 LYS N N 122.407 0.200 1 261 59 59 LYS C C 176.161 0.200 1 262 59 59 LYS CA C 56.341 0.200 1 263 59 59 LYS CB C 33.143 0.200 1 264 59 59 LYS N N 123.332 0.200 1 265 60 60 ALA C C 177.592 0.200 1 266 60 60 ALA CA C 52.333 0.200 1 267 60 60 ALA CB C 19.276 0.200 1 268 60 60 ALA N N 126.287 0.200 1 269 61 61 LYS H H 8.392 0.020 1 270 61 61 LYS C C 176.466 0.200 1 271 61 61 LYS CA C 56.410 0.200 1 272 61 61 LYS CB C 33.103 0.200 1 273 61 61 LYS N N 121.821 0.200 1 274 62 62 LYS H H 8.429 0.020 1 275 62 62 LYS C C 174.500 0.200 1 276 62 62 LYS CA C 54.299 0.200 1 277 62 62 LYS CB C 32.542 0.200 1 278 62 62 LYS N N 124.659 0.200 1 279 63 63 PRO C C 176.665 0.200 1 280 63 63 PRO CA C 63.168 0.200 1 281 63 63 PRO CB C 32.140 0.200 1 282 63 63 PRO N N 137.254 0.200 1 283 64 64 LYS C C 176.561 0.200 1 284 64 64 LYS CA C 56.526 0.200 1 285 64 64 LYS CB C 32.888 0.200 1 286 64 64 LYS N N 122.462 0.200 1 287 65 65 VAL H H 8.380 0.020 1 288 65 65 VAL C C 175.890 0.200 1 289 65 65 VAL CA C 62.429 0.200 1 290 65 65 VAL CB C 32.873 0.200 1 291 65 65 VAL N N 123.196 0.200 1 292 66 66 VAL C C 175.827 0.200 1 293 66 66 VAL CA C 62.222 0.200 1 294 66 66 VAL CB C 32.786 0.200 1 295 66 66 VAL N N 126.088 0.200 1 296 67 67 LYS H H 8.482 0.020 1 297 67 67 LYS C C 176.214 0.200 1 298 67 67 LYS CA C 56.362 0.200 1 299 67 67 LYS CB C 33.030 0.200 1 300 67 67 LYS N N 126.682 0.200 1 301 68 68 VAL H H 8.235 0.020 1 302 68 68 VAL C C 175.757 0.200 1 303 68 68 VAL CA C 62.316 0.200 1 304 68 68 VAL CB C 32.881 0.200 1 305 68 68 VAL N N 122.768 0.200 1 306 69 69 LYS H H 8.475 0.020 1 307 69 69 LYS C C 174.426 0.200 1 308 69 69 LYS CA C 54.289 0.200 1 309 69 69 LYS CB C 32.458 0.200 1 310 69 69 LYS N N 127.502 0.200 1 311 70 70 PRO C C 176.843 0.200 1 312 70 70 PRO CA C 62.994 0.200 1 313 70 70 PRO CB C 32.030 0.200 1 314 70 70 PRO N N 137.078 0.200 1 315 71 71 VAL H H 8.294 0.020 1 316 71 71 VAL C C 176.275 0.200 1 317 71 71 VAL CA C 62.259 0.200 1 318 71 71 VAL CB C 32.885 0.200 1 319 71 71 VAL N N 121.180 0.200 1 320 72 72 LYS H H 8.450 0.020 1 321 72 72 LYS C C 176.046 0.200 1 322 72 72 LYS CA C 56.399 0.200 1 323 72 72 LYS CB C 33.066 0.200 1 324 72 72 LYS N N 125.921 0.200 1 325 73 73 ALA C C 177.647 0.200 1 326 73 73 ALA CA C 52.450 0.200 1 327 73 73 ALA CB C 19.223 0.200 1 328 73 73 ALA N N 126.556 0.200 1 329 74 74 SER H H 8.387 0.020 1 330 74 74 SER C C 174.199 0.200 1 331 74 74 SER CA C 58.217 0.200 1 332 74 74 SER CB C 64.152 0.200 1 333 74 74 SER N N 116.353 0.200 1 334 75 75 LYS C C 174.501 0.200 1 335 75 75 LYS CA C 54.440 0.200 1 336 75 75 LYS CB C 32.514 0.200 1 337 75 75 LYS N N 124.540 0.200 1 338 76 76 PRO C C 176.874 0.200 1 339 76 76 PRO CA C 63.256 0.200 1 340 76 76 PRO CB C 32.175 0.200 1 341 76 76 PRO N N 137.423 0.200 1 342 77 77 LYS C C 176.723 0.200 1 343 77 77 LYS CA C 56.454 0.200 1 344 77 77 LYS CB C 33.086 0.200 1 345 77 77 LYS N N 122.488 0.200 1 346 78 78 LYS C C 176.186 0.200 1 347 78 78 LYS CA C 56.447 0.200 1 348 78 78 LYS CB C 33.277 0.200 1 349 78 78 LYS N N 123.421 0.200 1 350 79 79 ALA C C 177.643 0.200 1 351 79 79 ALA CA C 52.443 0.200 1 352 79 79 ALA CB C 19.338 0.200 1 353 79 79 ALA N N 126.460 0.200 1 354 80 80 LYS H H 8.431 0.020 1 355 80 80 LYS C C 176.794 0.200 1 356 80 80 LYS CA C 56.536 0.200 1 357 80 80 LYS CB C 33.017 0.200 1 358 80 80 LYS N N 121.610 0.200 1 359 81 81 THR H H 8.283 0.020 1 360 81 81 THR C C 174.305 0.200 1 361 81 81 THR CA C 61.999 0.200 1 362 81 81 THR CB C 70.021 0.200 1 363 81 81 THR N N 117.212 0.200 1 364 82 82 VAL H H 8.336 0.020 1 365 82 82 VAL C C 175.828 0.200 1 366 82 82 VAL CA C 62.220 0.200 1 367 82 82 VAL CB C 32.842 0.200 1 368 82 82 VAL N N 124.064 0.200 1 369 83 83 LYS H H 8.497 0.020 1 370 83 83 LYS C C 174.402 0.200 1 371 83 83 LYS CA C 54.186 0.200 1 372 83 83 LYS CB C 32.542 0.200 1 373 83 83 LYS N N 127.495 0.200 1 374 84 84 PRO C C 176.864 0.200 1 375 84 84 PRO CA C 63.171 0.200 1 376 84 84 PRO CB C 32.203 0.200 1 377 84 84 PRO N N 137.168 0.200 1 378 85 85 LYS C C 176.529 0.200 1 379 85 85 LYS CA C 56.506 0.200 1 380 85 85 LYS CB C 32.995 0.200 1 381 85 85 LYS N N 122.244 0.200 1 382 86 86 ALA C C 177.813 0.200 1 383 86 86 ALA CA C 52.710 0.200 1 384 86 86 ALA CB C 19.227 0.200 1 385 86 86 ALA N N 126.033 0.200 1 386 87 87 LYS H H 8.458 0.020 1 387 87 87 LYS C C 176.914 0.200 1 388 87 87 LYS CA C 56.645 0.200 1 389 87 87 LYS CB C 32.866 0.200 1 390 87 87 LYS N N 121.459 0.200 1 391 88 88 SER H H 8.498 0.020 1 392 88 88 SER C C 174.842 0.200 1 393 88 88 SER CA C 58.475 0.200 1 394 88 88 SER CB C 64.096 0.200 1 395 88 88 SER N N 117.539 0.200 1 396 89 89 SER H H 8.453 0.020 1 397 89 89 SER C C 174.476 0.200 1 398 89 89 SER CA C 58.434 0.200 1 399 89 89 SER CB C 63.952 0.200 1 400 89 89 SER N N 118.426 0.200 1 401 90 90 ALA H H 8.337 0.020 1 402 90 90 ALA C C 177.879 0.200 1 403 90 90 ALA CA C 52.757 0.200 1 404 90 90 ALA CB C 19.029 0.200 1 405 90 90 ALA N N 126.229 0.200 1 406 91 91 LYS H H 8.306 0.020 1 407 91 91 LYS C C 176.825 0.200 1 408 91 91 LYS CA C 56.523 0.200 1 409 91 91 LYS CB C 32.675 0.200 1 410 91 91 LYS N N 120.849 0.200 1 411 92 92 ARG H H 8.374 0.020 1 412 92 92 ARG C C 176.188 0.200 1 413 92 92 ARG CA C 56.162 0.200 1 414 92 92 ARG CB C 30.811 0.200 1 415 92 92 ARG N N 122.777 0.200 1 416 93 93 ALA H H 8.429 0.020 1 417 93 93 ALA C C 177.872 0.200 1 418 93 93 ALA CA C 52.532 0.200 1 419 93 93 ALA CB C 19.217 0.200 1 420 93 93 ALA N N 125.787 0.200 1 421 94 94 SER H H 8.372 0.020 1 422 94 94 SER C C 174.794 0.200 1 423 94 94 SER CA C 58.750 0.200 1 424 94 94 SER CB C 64.150 0.200 1 425 94 94 SER N N 115.804 0.200 1 426 95 95 LYS C C 176.647 0.200 1 427 95 95 LYS CA C 56.559 0.200 1 428 95 95 LYS CB C 32.655 0.200 1 429 95 95 LYS N N 123.812 0.200 1 430 96 96 LYS H H 8.334 0.020 1 431 96 96 LYS C C 176.565 0.200 1 432 96 96 LYS N N 122.799 0.200 1 433 98 98 ARG H H 8.435 0.020 1 434 99 99 SER H H 8.473 0.020 1 stop_ save_ save_heteronuclear_noe_list_1 _Saveframe_category heteronuclear_NOE _Details . loop_ _Software_label $TOPSPIN $SPARKY $NMRPipe $NMRView stop_ loop_ _Experiment_label '2D 1H-15N-HETNOE' stop_ loop_ _Sample_label . stop_ _Sample_conditions_label $sample_conditions_1 _Spectrometer_frequency_1H 800 _Mol_system_component_name C-H1.0 _Atom_one_atom_name N _Atom_two_atom_name H _Heteronuclear_NOE_value_type 'peak height' _NOE_reference_value 0.87 _NOE_reference_description . _Text_data_format . _Text_data . loop_ _Residue_seq_code _Residue_label _Heteronuclear_NOE_value _Heteronuclear_NOE_value_error 3 GLU -0.586 0.009 7 SER 0.135 0.013 8 VAL 0.143 0.011 9 ALA -0.139 0.010 10 PHE 0.189 0.010 11 LYS 0.174 0.011 12 LYS 0.027 0.012 13 THR 0.071 0.014 16 GLU -0.065 0.010 18 LYS 0.120 0.006 19 LYS 0.067 0.011 20 VAL -0.170 0.013 21 ALA -0.159 0.010 22 THR -0.140 0.011 24 LYS 0.120 0.012 27 ALA -0.102 0.010 28 LYS 0.092 0.012 33 ALA 0.000 0.009 34 SER -0.115 0.011 36 ALA -0.044 0.009 38 SER -0.150 0.010 44 THR -0.137 0.012 46 VAL -0.162 0.012 48 LYS 0.130 0.012 50 LYS 0.089 0.015 51 LYS 0.170 0.014 52 LYS -0.100 0.012 54 ALA -0.031 0.010 55 ALA 0.019 0.010 56 THR -0.127 0.013 58 LYS -0.091 0.005 61 LYS 0.089 0.011 62 LYS 0.109 0.013 65 VAL 0.086 0.007 67 LYS -0.088 0.014 68 VAL -0.015 0.014 69 LYS -0.080 0.011 71 VAL -0.153 0.013 72 LYS 0.042 0.006 74 SER -0.141 0.013 80 LYS 0.062 0.012 81 THR -0.086 0.014 82 VAL 0.020 0.012 83 LYS -0.103 0.011 87 LYS -0.105 0.006 88 SER 0.176 0.017 89 SER 0.180 0.023 90 ALA 0.075 0.011 91 LYS -0.087 0.011 92 ARG 0.118 0.012 93 ALA 0.087 0.006 94 SER 0.103 0.013 96 LYS 0.127 0.014 98 ARG 0.059 0.014 99 SER 0.029 0.017 stop_ save_