data_27633 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Chemical shift assignments of the C-terminal domain of chicken H1.11L ; _BMRB_accession_number 27633 _BMRB_flat_file_name bmr27633.str _Entry_type original _Submission_date 2018-09-27 _Accession_date 2018-09-27 _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 Turner Abigail L. . 2 Watson Matthew . . 3 Wilkins Oscar G. . 4 Cato Laura . . 5 Travers Andrew . . 6 Thomas Jean O. . 7 Stott Katherine . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 71 "15N chemical shifts" 71 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2019-02-06 original BMRB . stop_ _Original_release_date 2018-09-27 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Highly disordered histone H1-DNA model complexes and their condensates ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 30301810 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Turner Abigail L. . 2 Watson Matthew . . 3 Wilkins Oscar G. . 4 Cato Laura . . 5 Travers Andrew . . 6 Thomas Jean O. . 7 Stott Katherine . . stop_ _Journal_abbreviation 'Proc. Natl. Acad. Sci. U.S.A.' _Journal_volume 115 _Journal_issue 47 _Journal_ISSN 1091-6490 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 11964 _Page_last 11969 _Year 2018 _Details . loop_ _Keyword chromatin 'histone H1' 'intrinsic disorder' 'phase separation' phosphorylation stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'H1 C-terminal domain' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'H1 C-terminal domain' $H1 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_H1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common H1 _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 111 _Mol_residue_sequence ; KPGEVKEKAPKKKASAAKPK KPAAKKPAAAAKKPKKAVAV KKSPKKAKKPAASATKKSAK SPKKVTKAVKPKKAVAAKSP AKAKAVKPKAAKPKAAKPKA AKAKKAAAKKK ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 115 LYS 2 116 PRO 3 117 GLY 4 118 GLU 5 119 VAL 6 120 LYS 7 121 GLU 8 122 LYS 9 123 ALA 10 124 PRO 11 125 LYS 12 126 LYS 13 127 LYS 14 128 ALA 15 129 SER 16 130 ALA 17 131 ALA 18 132 LYS 19 133 PRO 20 134 LYS 21 135 LYS 22 136 PRO 23 137 ALA 24 138 ALA 25 139 LYS 26 140 LYS 27 141 PRO 28 142 ALA 29 143 ALA 30 144 ALA 31 145 ALA 32 146 LYS 33 147 LYS 34 148 PRO 35 149 LYS 36 150 LYS 37 151 ALA 38 152 VAL 39 153 ALA 40 154 VAL 41 155 LYS 42 156 LYS 43 157 SER 44 158 PRO 45 159 LYS 46 160 LYS 47 161 ALA 48 162 LYS 49 163 LYS 50 164 PRO 51 165 ALA 52 166 ALA 53 167 SER 54 168 ALA 55 169 THR 56 170 LYS 57 171 LYS 58 172 SER 59 173 ALA 60 174 LYS 61 175 SER 62 176 PRO 63 177 LYS 64 178 LYS 65 179 VAL 66 180 THR 67 181 LYS 68 182 ALA 69 183 VAL 70 184 LYS 71 185 PRO 72 186 LYS 73 187 LYS 74 188 ALA 75 189 VAL 76 190 ALA 77 191 ALA 78 192 LYS 79 193 SER 80 194 PRO 81 195 ALA 82 196 LYS 83 197 ALA 84 198 LYS 85 199 ALA 86 200 VAL 87 201 LYS 88 202 PRO 89 203 LYS 90 204 ALA 91 205 ALA 92 206 LYS 93 207 PRO 94 208 LYS 95 209 ALA 96 210 ALA 97 211 LYS 98 212 PRO 99 213 LYS 100 214 ALA 101 215 ALA 102 216 LYS 103 217 ALA 104 218 LYS 105 219 LYS 106 220 ALA 107 221 ALA 108 222 ALA 109 223 LYS 110 224 LYS 111 225 LYS 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 _Variant $H1 chicken 9031 Eukaryota Metazoa Gallus gallus H1.11L 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 $H1 'recombinant technology' . Escherichia coli . pET13a 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 $H1 0.5 mM '[U-99% 13C; U-99% 15N]' 'sodium phosphate' 0.5 mM 'natural abundance' NaCl 0.5 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version . loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection stop_ _Details . save_ save_AZARA _Saveframe_category software _Name AZARA _Version . loop_ _Vendor _Address _Electronic_address Boucher . . stop_ loop_ _Task processing stop_ _Details . save_ save_Analysis _Saveframe_category software _Name Analysis _Version v2.4 loop_ _Vendor _Address _Electronic_address CCPN . . stop_ loop_ _Task 'chemical shift assignment' 'data analysis' 'peak picking' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model DRX _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_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.16 . M pH 6.0 . 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 H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 . 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 '2D 1H-15N HSQC' 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 'H1 C-terminal domain' _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 1 117 3 GLY H H 8.623 0.001 1 2 117 3 GLY N N 110.149 0.015 1 3 118 4 GLU H H 8.039 0.001 1 4 118 4 GLU N N 120.750 0.020 1 5 119 5 VAL H H 8.249 0.001 1 6 119 5 VAL N N 121.823 0.015 1 7 120 6 LYS H H 8.439 0.001 1 8 120 6 LYS N N 125.759 0.016 1 9 121 7 GLU H H 8.444 0.001 1 10 121 7 GLU N N 122.678 0.022 1 11 122 8 LYS H H 8.439 0.001 1 12 122 8 LYS N N 123.210 0.010 1 13 123 9 ALA H H 8.316 0.001 1 14 123 9 ALA N N 126.347 0.009 1 15 125 11 LYS H H 8.438 0.001 1 16 125 11 LYS N N 122.050 0.001 1 17 126 12 LYS H H 8.362 0.001 1 18 126 12 LYS N N 123.337 0.018 1 19 127 13 LYS H H 8.439 0.005 1 20 127 13 LYS N N 123.932 0.019 1 21 128 14 ALA H H 8.463 0.001 1 22 128 14 ALA N N 126.389 0.052 1 23 129 15 SER H H 8.352 0.001 1 24 129 15 SER N N 115.724 0.034 1 25 130 16 ALA H H 8.356 0.001 1 26 130 16 ALA N N 126.428 0.064 1 27 131 17 ALA H H 8.254 0.001 1 28 131 17 ALA N N 123.850 0.023 1 29 132 18 LYS H H 8.339 0.001 1 30 132 18 LYS N N 122.526 0.012 1 31 134 20 LYS H H 8.474 0.001 1 32 134 20 LYS N N 122.454 0.013 1 33 135 21 LYS H H 8.384 0.003 1 34 135 21 LYS N N 124.341 0.003 1 35 149 35 LYS H H 8.451 0.001 1 36 149 35 LYS N N 122.436 0.009 1 37 150 36 LYS H H 8.334 0.001 1 38 150 36 LYS N N 123.430 0.010 1 39 151 37 ALA H H 8.423 0.001 1 40 151 37 ALA N N 126.775 0.016 1 41 152 38 VAL H H 8.183 0.001 1 42 152 38 VAL N N 120.434 0.008 1 43 153 39 ALA H H 8.410 0.001 1 44 153 39 ALA N N 128.683 0.017 1 45 154 40 VAL H H 8.199 0.001 1 46 154 40 VAL N N 120.849 0.010 1 47 155 41 LYS H H 8.452 0.001 1 48 155 41 LYS N N 126.341 0.011 1 49 156 42 LYS H H 8.451 0.001 1 50 156 42 LYS N N 124.057 0.011 1 51 157 43 SER H H 8.500 0.002 1 52 157 43 SER N N 119.394 0.020 1 53 165 51 ALA H H 8.445 0.001 1 54 165 51 ALA N N 124.951 0.031 1 55 166 52 ALA H H 8.402 0.002 1 56 166 52 ALA N N 123.938 0.026 1 57 167 53 SER H H 8.310 0.001 1 58 167 53 SER N N 115.103 0.014 1 59 168 54 ALA H H 8.387 0.001 1 60 168 54 ALA N N 126.323 0.020 1 61 169 55 THR H H 8.139 0.001 1 62 169 55 THR N N 113.850 0.001 1 63 170 56 LYS H H 8.347 0.001 1 64 170 56 LYS N N 124.480 0.016 1 65 171 57 LYS H H 8.429 0.001 1 66 171 57 LYS N N 123.514 0.018 1 67 172 58 SER H H 8.381 0.001 1 68 172 58 SER N N 117.503 0.014 1 69 173 59 ALA H H 8.406 0.001 1 70 173 59 ALA N N 126.611 0.022 1 71 174 60 LYS H H 8.307 0.001 1 72 174 60 LYS N N 120.814 0.033 1 73 175 61 SER H H 8.390 0.001 1 74 175 61 SER N N 118.888 0.017 1 75 177 63 LYS H H 8.361 0.001 1 76 177 63 LYS N N 122.044 0.011 1 77 178 64 LYS H H 8.399 0.001 1 78 178 64 LYS N N 123.953 0.012 1 79 179 65 VAL H H 8.344 0.001 1 80 179 65 VAL N N 123.235 0.013 1 81 180 66 THR H H 8.378 0.001 1 82 180 66 THR N N 120.022 0.016 1 83 181 67 LYS H H 8.388 0.001 1 84 181 67 LYS N N 124.901 0.034 1 85 182 68 ALA H H 8.385 0.001 1 86 182 68 ALA N N 126.513 0.017 1 87 183 69 VAL H H 8.232 0.001 1 88 183 69 VAL N N 120.758 0.032 1 89 184 70 LYS H H 8.456 0.001 1 90 184 70 LYS N N 127.251 0.025 1 91 186 72 LYS H H 8.451 0.001 1 92 186 72 LYS N N 122.436 0.009 1 93 187 73 LYS H H 8.334 0.001 1 94 187 73 LYS N N 123.428 0.010 1 95 188 74 ALA H H 8.423 0.001 1 96 188 74 ALA N N 126.771 0.013 1 97 189 75 VAL H H 8.192 0.001 1 98 189 75 VAL N N 120.416 0.016 1 99 190 76 ALA H H 8.403 0.001 1 100 190 76 ALA N N 128.565 0.010 1 101 191 77 ALA H H 8.318 0.001 1 102 191 77 ALA N N 124.256 0.012 1 103 192 78 LYS H H 8.347 0.002 1 104 192 78 LYS N N 121.207 0.025 1 105 193 79 SER H H 8.416 0.001 1 106 193 79 SER N N 118.940 0.014 1 107 195 81 ALA H H 8.372 0.001 1 108 195 81 ALA N N 124.591 0.025 1 109 196 82 LYS H H 8.288 0.001 1 110 196 82 LYS N N 121.050 0.017 1 111 197 83 ALA H H 8.307 0.001 1 112 197 83 ALA N N 125.730 0.011 1 113 198 84 LYS H H 8.299 0.001 1 114 198 84 LYS N N 121.113 0.008 1 115 199 85 ALA H H 8.310 0.001 1 116 199 85 ALA N N 125.973 0.010 1 117 200 86 VAL H H 8.207 0.001 1 118 200 86 VAL N N 120.638 0.027 1 119 201 87 LYS H H 8.455 0.001 1 120 201 87 LYS N N 127.274 0.015 1 121 203 89 LYS H H 8.453 0.001 1 122 203 89 LYS N N 122.243 0.010 1 123 204 90 ALA H H 8.334 0.001 1 124 204 90 ALA N N 125.810 0.035 1 125 205 91 ALA H H 8.335 0.001 1 126 205 91 ALA N N 124.366 0.035 1 127 206 92 LYS H H 8.359 0.003 1 128 206 92 LYS N N 122.549 0.017 1 129 208 94 LYS H H 8.453 0.001 1 130 208 94 LYS N N 122.243 0.010 1 131 209 95 ALA H H 8.334 0.001 1 132 209 95 ALA N N 125.810 0.035 1 133 210 96 ALA H H 8.335 0.001 1 134 210 96 ALA N N 124.366 0.035 1 135 211 97 LYS H H 8.359 0.003 1 136 211 97 LYS N N 122.549 0.017 1 137 223 109 LYS H H 8.304 0.001 1 138 223 109 LYS N N 121.385 0.010 1 139 224 110 LYS H H 8.391 0.001 1 140 224 110 LYS N N 124.092 0.012 1 141 225 111 LYS H H 8.026 0.001 1 142 225 111 LYS N N 128.386 0.011 1 stop_ save_