data_26594 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 15N, 1HN, 13CA, 13CB and 13C' Chemical shift Assignments for the DNA-binding domain of Human Telomeric Repeat Binding Factor Protein (hTRF1) ; _BMRB_accession_number 26594 _BMRB_flat_file_name bmr26594.str _Entry_type original _Submission_date 2015-06-26 _Accession_date 2015-06-26 _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 Sekhar Ashok . . 2 Rosenzweig Rina . . 3 Bouvignies Guillaume . . 4 Kay Lewis E. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 48 "13C chemical shifts" 141 "15N chemical shifts" 48 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2017-01-13 update BMRB 'update entry citation' 2015-07-29 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 26595 'hTRF1 bound to ADP-DnaK' stop_ _Original_release_date 2015-07-29 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Mapping the conformation of a client protein through the Hsp70 functional cycle ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 26240333 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Sekhar Ashok . . 2 Rosenzweig Rina . . 3 Bouvignies Guillaume . . 4 Kay Lewis E. . stop_ _Journal_abbreviation 'Proc. Natl. Acad. Sci. U.S.A.' _Journal_volume 112 _Journal_issue 33 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 10395 _Page_last 10400 _Year 2015 _Details . loop_ _Keyword CEST Hsp70 NMR 'molecular chaperones' 'protein folding' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'hTRF1 monomer' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label hTRF1 $hTRF1 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_hTRF1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common hTRF1 _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 53 _Mol_residue_sequence ; RKRQAWLWEEDKNLRSGVRK YGEGNWSKILLHYKFNNRTS VMLKDRWRTMKKL ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 ARG 2 2 LYS 3 3 ARG 4 4 GLN 5 5 ALA 6 6 TRP 7 7 LEU 8 8 TRP 9 9 GLU 10 10 GLU 11 11 ASP 12 12 LYS 13 13 ASN 14 14 LEU 15 15 ARG 16 16 SER 17 17 GLY 18 18 VAL 19 19 ARG 20 20 LYS 21 21 TYR 22 22 GLY 23 23 GLU 24 24 GLY 25 25 ASN 26 26 TRP 27 27 SER 28 28 LYS 29 29 ILE 30 30 LEU 31 31 LEU 32 32 HIS 33 33 TYR 34 34 LYS 35 35 PHE 36 36 ASN 37 37 ASN 38 38 ARG 39 39 THR 40 40 SER 41 41 VAL 42 42 MET 43 43 LEU 44 44 LYS 45 45 ASP 46 46 ARG 47 47 TRP 48 48 ARG 49 49 THR 50 50 MET 51 51 LYS 52 52 LYS 53 53 LEU 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 $hTRF1 Human 9606 Eukaryota Metazoa Homo sapiens 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 $hTRF1 'recombinant technology' . Escherichia coli . pET29b 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 $hTRF1 0.8 mM '[U-99% 13C; U-99% 15N]' 'sodium acetate' 50 mM 'natural abundance' 'sodium chloride' 50 mM 'natural abundance' 'sodium azide' 1 mM 'natural abundance' EDTA 1 mM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ 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 Varian _Model INOVA _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_HNCACB_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HNCO_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _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' 0.1 . M pH 5.7 . pH pressure 1 . atm temperature 308 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chemical_shift_reference_1 _Saveframe_category chemical_shift_reference _Details '1H chemical shifts were referenced to water at the relevant temperature 273 ? K or 15N referencing' 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 protons ppm 4.677 internal indirect . . . 0.2514953 water H 1 protons ppm 4.677 internal direct . . . 1.0 water N 15 protons ppm 4.677 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_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '3D CBCA(CO)NH' '3D HNCACB' '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 hTRF1 _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 ARG C C 176.021 . 1 2 4 4 GLN H H 8.561 . 1 3 4 4 GLN C C 176.085 . 1 4 4 4 GLN CA C 55.820 . 1 5 4 4 GLN CB C 29.550 . 1 6 4 4 GLN N N 122.885 . 1 7 5 5 ALA H H 8.427 . 1 8 5 5 ALA C C 177.542 . 1 9 5 5 ALA CA C 52.770 . 1 10 5 5 ALA CB C 19.440 . 1 11 5 5 ALA N N 127.912 . 1 12 6 6 TRP H H 8.611 . 1 13 6 6 TRP C C 177.446 . 1 14 6 6 TRP CA C 58.060 . 1 15 6 6 TRP CB C 28.850 . 1 16 6 6 TRP N N 122.899 . 1 17 7 7 LEU H H 9.140 . 1 18 7 7 LEU C C 178.881 . 1 19 7 7 LEU CA C 54.050 . 1 20 7 7 LEU CB C 43.150 . 1 21 7 7 LEU N N 126.964 . 1 22 8 8 TRP H H 9.039 . 1 23 8 8 TRP C C 178.810 . 1 24 8 8 TRP CA C 61.200 . 1 25 8 8 TRP CB C 28.850 . 1 26 8 8 TRP N N 124.562 . 1 27 9 9 GLU H H 8.875 . 1 28 9 9 GLU C C 178.529 . 1 29 9 9 GLU CA C 59.910 . 1 30 9 9 GLU CB C 29.830 . 1 31 9 9 GLU N N 117.376 . 1 32 10 10 GLU H H 7.164 . 1 33 10 10 GLU C C 178.566 . 1 34 10 10 GLU CA C 60.070 . 1 35 10 10 GLU CB C 32.400 . 1 36 10 10 GLU N N 116.878 . 1 37 11 11 ASP H H 7.950 . 1 38 11 11 ASP C C 179.095 . 1 39 11 11 ASP CA C 57.800 . 1 40 11 11 ASP CB C 40.370 . 1 41 11 11 ASP N N 121.564 . 1 42 12 12 LYS H H 8.155 . 1 43 12 12 LYS C C 179.226 . 1 44 12 12 LYS CA C 59.620 . 1 45 12 12 LYS CB C 31.990 . 1 46 12 12 LYS N N 120.344 . 1 47 13 13 ASN H H 8.036 . 1 48 13 13 ASN C C 176.752 . 1 49 13 13 ASN CA C 55.240 . 1 50 13 13 ASN CB C 37.920 . 1 51 13 13 ASN N N 120.350 . 1 52 14 14 LEU H H 8.781 . 1 53 14 14 LEU C C 177.567 . 1 54 14 14 LEU CA C 58.830 . 1 55 14 14 LEU CB C 42.790 . 1 56 14 14 LEU N N 122.791 . 1 57 15 15 ARG H H 8.195 . 1 58 15 15 ARG C C 179.762 . 1 59 15 15 ARG CA C 60.600 . 1 60 15 15 ARG CB C 30.500 . 1 61 15 15 ARG N N 117.536 . 1 62 16 16 SER H H 8.500 . 1 63 16 16 SER C C 176.637 . 1 64 16 16 SER CA C 61.600 . 1 65 16 16 SER CB C 62.600 . 1 66 16 16 SER N N 116.056 . 1 67 17 17 GLY H H 8.648 . 1 68 17 17 GLY C C 175.311 . 1 69 17 17 GLY CA C 48.020 . 1 70 17 17 GLY N N 111.136 . 1 71 18 18 VAL H H 8.517 . 1 72 18 18 VAL C C 179.116 . 1 73 18 18 VAL CA C 66.600 . 1 74 18 18 VAL CB C 31.200 . 1 75 18 18 VAL N N 123.961 . 1 76 19 19 ARG H H 7.546 . 1 77 19 19 ARG C C 177.389 . 1 78 19 19 ARG CA C 59.210 . 1 79 19 19 ARG CB C 29.790 . 1 80 19 19 ARG N N 120.070 . 1 81 20 20 LYS H H 7.739 . 1 82 20 20 LYS C C 177.660 . 1 83 20 20 LYS CA C 58.980 . 1 84 20 20 LYS CB C 33.850 . 1 85 20 20 LYS N N 117.345 . 1 86 21 21 TYR H H 8.761 . 1 87 21 21 TYR C C 176.588 . 1 88 21 21 TYR CA C 58.830 . 1 89 21 21 TYR CB C 39.410 . 1 90 21 21 TYR N N 114.146 . 1 91 22 22 GLY H H 7.863 . 1 92 22 22 GLY C C 173.076 . 1 93 22 22 GLY CA C 44.440 . 1 94 22 22 GLY N N 110.723 . 1 95 23 23 GLU H H 8.353 . 1 96 23 23 GLU CA C 57.670 . 1 97 23 23 GLU CB C 29.910 . 1 98 23 23 GLU N N 120.586 . 1 99 24 24 GLY C C 173.765 . 1 100 24 24 GLY CA C 45.160 . 1 101 25 25 ASN H H 7.050 . 1 102 25 25 ASN C C 175.727 . 1 103 25 25 ASN CA C 51.690 . 1 104 25 25 ASN CB C 37.180 . 1 105 25 25 ASN N N 121.441 . 1 106 26 26 TRP H H 6.629 . 1 107 26 26 TRP C C 177.956 . 1 108 26 26 TRP CA C 58.590 . 1 109 26 26 TRP CB C 30.450 . 1 110 26 26 TRP N N 118.150 . 1 111 27 27 SER H H 8.737 . 1 112 27 27 SER C C 176.309 . 1 113 27 27 SER CA C 61.990 . 1 114 27 27 SER N N 113.050 . 1 115 28 28 LYS H H 7.269 . 1 116 28 28 LYS C C 178.755 . 1 117 28 28 LYS CA C 59.180 . 1 118 28 28 LYS CB C 32.460 . 1 119 28 28 LYS N N 121.358 . 1 120 29 29 ILE H H 7.477 . 1 121 29 29 ILE C C 177.521 . 1 122 29 29 ILE CA C 66.860 . 1 123 29 29 ILE CB C 38.650 . 1 124 29 29 ILE N N 119.844 . 1 125 30 30 LEU H H 7.993 . 1 126 30 30 LEU C C 177.393 . 1 127 30 30 LEU CA C 57.730 . 1 128 30 30 LEU CB C 43.070 . 1 129 30 30 LEU N N 118.620 . 1 130 31 31 LEU H H 7.227 . 1 131 31 31 LEU C C 178.718 . 1 132 31 31 LEU CA C 56.080 . 1 133 31 31 LEU CB C 43.040 . 1 134 31 31 LEU N N 113.516 . 1 135 32 32 HIS H H 7.652 . 1 136 32 32 HIS C C 173.256 . 1 137 32 32 HIS CA C 57.500 . 1 138 32 32 HIS CB C 31.390 . 1 139 32 32 HIS N N 114.730 . 1 140 33 33 TYR H H 7.855 . 1 141 33 33 TYR C C 173.394 . 1 142 33 33 TYR CA C 56.550 . 1 143 33 33 TYR CB C 41.780 . 1 144 33 33 TYR N N 117.198 . 1 145 34 34 LYS H H 7.884 . 1 146 34 34 LYS C C 175.606 . 1 147 34 34 LYS CA C 56.520 . 1 148 34 34 LYS CB C 32.770 . 1 149 34 34 LYS N N 119.614 . 1 150 35 35 PHE H H 8.450 . 1 151 35 35 PHE C C 174.837 . 1 152 35 35 PHE CA C 57.220 . 1 153 35 35 PHE CB C 42.100 . 1 154 35 35 PHE N N 123.369 . 1 155 36 36 ASN H H 9.436 . 1 156 36 36 ASN C C 173.516 . 1 157 36 36 ASN CA C 51.950 . 1 158 36 36 ASN CB C 37.410 . 1 159 36 36 ASN N N 122.067 . 1 160 37 37 ASN H H 8.401 . 1 161 37 37 ASN C C 174.522 . 1 162 37 37 ASN CA C 54.130 . 1 163 37 37 ASN CB C 37.410 . 1 164 37 37 ASN N N 120.696 . 1 165 38 38 ARG H H 7.991 . 1 166 38 38 ARG C C 175.705 . 1 167 38 38 ARG CA C 52.250 . 1 168 38 38 ARG CB C 31.540 . 1 169 38 38 ARG N N 114.135 . 1 170 39 39 THR H H 7.099 . 1 171 39 39 THR C C 176.048 . 1 172 39 39 THR CA C 59.160 . 1 173 39 39 THR CB C 71.760 . 1 174 39 39 THR N N 108.622 . 1 175 40 40 SER H H 9.245 . 1 176 40 40 SER C C 175.971 . 1 177 40 40 SER CA C 63.030 . 1 178 40 40 SER N N 117.466 . 1 179 41 41 VAL H H 7.463 . 1 180 41 41 VAL C C 176.975 . 1 181 41 41 VAL CA C 65.390 . 1 182 41 41 VAL CB C 31.950 . 1 183 41 41 VAL N N 119.670 . 1 184 42 42 MET H H 7.332 . 1 185 42 42 MET C C 179.317 . 1 186 42 42 MET CA C 59.130 . 1 187 42 42 MET CB C 33.470 . 1 188 42 42 MET N N 118.232 . 1 189 43 43 LEU H H 7.516 . 1 190 43 43 LEU C C 176.447 . 1 191 43 43 LEU CA C 58.890 . 1 192 43 43 LEU CB C 41.510 . 1 193 43 43 LEU N N 119.373 . 1 194 44 44 LYS H H 6.839 . 1 195 44 44 LYS C C 178.676 . 1 196 44 44 LYS CA C 58.950 . 1 197 44 44 LYS CB C 31.400 . 1 198 44 44 LYS N N 119.552 . 1 199 45 45 ASP H H 7.997 . 1 200 45 45 ASP C C 178.680 . 1 201 45 45 ASP CA C 57.050 . 1 202 45 45 ASP CB C 40.540 . 1 203 45 45 ASP N N 118.382 . 1 204 46 46 ARG H H 7.916 . 1 205 46 46 ARG CA C 56.970 . 1 206 46 46 ARG CB C 29.840 . 1 207 46 46 ARG N N 121.974 . 1 208 47 47 TRP C C 177.142 . 1 209 48 48 ARG H H 7.536 . 1 210 48 48 ARG C C 178.391 . 1 211 48 48 ARG CA C 59.180 . 1 212 48 48 ARG CB C 29.950 . 1 213 48 48 ARG N N 115.701 . 1 214 49 49 THR H H 7.374 . 1 215 49 49 THR C C 175.597 . 1 216 49 49 THR CA C 64.090 . 1 217 49 49 THR CB C 69.460 . 1 218 49 49 THR N N 110.472 . 1 219 50 50 MET H H 7.710 . 1 220 50 50 MET C C 176.567 . 1 221 50 50 MET CA C 57.120 . 1 222 50 50 MET CB C 33.430 . 1 223 50 50 MET N N 121.343 . 1 224 51 51 LYS H H 7.651 . 1 225 51 51 LYS C C 176.184 . 1 226 51 51 LYS CA C 56.940 . 1 227 51 51 LYS CB C 32.180 . 1 228 51 51 LYS N N 120.098 . 1 229 52 52 LYS H H 7.788 . 1 230 52 52 LYS C C 175.341 . 1 231 52 52 LYS CA C 57.120 . 1 232 52 52 LYS CB C 33.300 . 1 233 52 52 LYS N N 121.614 . 1 234 53 53 LEU H H 7.586 . 1 235 53 53 LEU CA C 56.600 . 1 236 53 53 LEU CB C 43.490 . 1 237 53 53 LEU N N 128.302 . 1 stop_ save_