data_26764 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N Chemical Shift Assignments for hTRF1 in urea ; _BMRB_accession_number 26764 _BMRB_flat_file_name bmr26764.str _Entry_type original _Submission_date 2016-03-21 _Accession_date 2016-03-21 _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 . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 102 "13C chemical shifts" 139 "15N chemical shifts" 50 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2016-10-26 update BMRB 'update entry citation' 2016-05-09 original author 'original release' stop_ _Original_release_date 2016-05-09 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Hsp70 biases the folding pathways of client proteins ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 27140645 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 . . stop_ _Journal_abbreviation 'Proc. Natl. Acad. Sci. U.S.A.' _Journal_volume 113 _Journal_issue 20 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first E2794 _Page_last E2801 _Year 2016 _Details . loop_ _Keyword Hsp70 PRE 'excited states' 'molecular chaperones' 'protein folding' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name hTRF1 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label hTRF1 $human_telomeric_protein_hTRF1 stop_ _System_molecular_weight . _System_physical_state denatured _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_human_telomeric_protein_hTRF1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common human_telomeric_protein_hTRF1 _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 53 _Mol_residue_sequence ; RKRQAWLWEEDKNLRSGVRK YGEGNWSKILLHYKFNNRTS VMLKDRWRTMKCL ; 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 CYS 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 $human_telomeric_protein_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 $human_telomeric_protein_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 $human_telomeric_protein_hTRF1 0.6 mM '[U-99% 13C; U-99% 15N]' urea 3500 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 600 _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_ save_3D_HBHA(CO)NH_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HBHA(CO)NH' _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 6 . pH pressure 1 . atm temperature 273 . 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 water H 1 protons ppm 4.677 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 '2D 1H-15N HSQC' '3D CBCA(CO)NH' '3D HNCACB' '3D HNCO' '3D HBHA(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 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 HA H 4.145 . 1 2 4 4 GLN H H 8.374 . 1 3 4 4 GLN HA H 4.245 . 1 4 4 4 GLN C C 175.731 . 1 5 4 4 GLN CA C 56.404 . 1 6 4 4 GLN CB C 29.316 . 1 7 4 4 GLN N N 120.331 . 1 8 5 5 ALA H H 8.242 . 1 9 5 5 ALA HA H 4.175 . 1 10 5 5 ALA C C 177.291 . 1 11 5 5 ALA CA C 52.947 . 1 12 5 5 ALA CB C 19.309 . 1 13 5 5 ALA N N 124.665 . 1 14 6 6 TRP H H 7.945 . 1 15 6 6 TRP HA H 4.662 . 1 16 6 6 TRP C C 175.957 . 1 17 6 6 TRP CA C 57.040 . 1 18 6 6 TRP CB C 29.529 . 1 19 6 6 TRP N N 119.070 . 1 20 7 7 LEU H H 7.867 . 1 21 7 7 LEU HA H 4.248 . 1 22 7 7 LEU C C 176.729 . 1 23 7 7 LEU CA C 55.344 . 1 24 7 7 LEU CB C 42.506 . 1 25 7 7 LEU N N 123.467 . 1 26 8 8 TRP H H 7.872 . 1 27 8 8 TRP HA H 4.658 . 1 28 8 8 TRP C C 176.152 . 1 29 8 8 TRP CA C 57.378 . 1 30 8 8 TRP CB C 29.666 . 1 31 8 8 TRP N N 120.946 . 1 32 9 9 GLU H H 8.165 . 1 33 9 9 GLU HA H 4.246 . 1 34 9 9 GLU C C 176.231 . 1 35 9 9 GLU CA C 56.837 . 1 36 9 9 GLU CB C 30.725 . 1 37 9 9 GLU N N 122.169 . 1 38 10 10 GLU H H 8.233 . 1 39 10 10 GLU HA H 4.191 . 1 40 10 10 GLU C C 176.309 . 1 41 10 10 GLU CA C 56.874 . 1 42 10 10 GLU CB C 30.671 . 1 43 10 10 GLU N N 121.499 . 1 44 11 11 ASP H H 8.363 . 1 45 11 11 ASP HA H 4.599 . 1 46 11 11 ASP C C 176.942 . 1 47 11 11 ASP CA C 54.639 . 1 48 11 11 ASP CB C 41.421 . 1 49 11 11 ASP N N 121.456 . 1 50 12 12 LYS H H 8.297 . 1 51 12 12 LYS HA H 4.220 . 1 52 12 12 LYS C C 176.888 . 1 53 12 12 LYS CA C 57.274 . 1 54 12 12 LYS CB C 32.717 . 1 55 12 12 LYS N N 122.246 . 1 56 13 13 ASN H H 8.454 . 1 57 13 13 ASN HA H 4.721 . 1 58 13 13 ASN CA C 53.819 . 1 59 13 13 ASN CB C 38.898 . 1 60 13 13 ASN N N 118.113 . 1 61 14 14 LEU H H 7.988 . 1 62 14 14 LEU HA H 4.318 . 1 63 14 14 LEU C C 177.544 . 1 64 14 14 LEU CA C 55.862 . 1 65 14 14 LEU CB C 42.334 . 1 66 14 14 LEU N N 121.629 . 1 67 15 15 ARG H H 8.265 . 1 68 15 15 ARG HA H 4.393 . 1 69 15 15 ARG C C 176.452 . 1 70 15 15 ARG CA C 56.320 . 1 71 15 15 ARG CB C 30.744 . 1 72 15 15 ARG N N 120.789 . 1 73 16 16 SER H H 8.217 . 1 74 16 16 SER HA H 4.493 . 1 75 16 16 SER C C 175.060 . 1 76 16 16 SER CA C 58.604 . 1 77 16 16 SER CB C 63.997 . 1 78 16 16 SER N N 116.004 . 1 79 17 17 GLY H H 8.388 . 1 80 17 17 GLY HA2 H 4.052 . 1 81 17 17 GLY HA3 H 4.052 . 1 82 17 17 GLY C C 173.969 . 1 83 17 17 GLY CA C 45.472 . 1 84 17 17 GLY N N 110.657 . 1 85 18 18 VAL H H 7.933 . 1 86 18 18 VAL HA H 4.146 . 1 87 18 18 VAL C C 176.027 . 1 88 18 18 VAL CA C 62.400 . 1 89 18 18 VAL CB C 32.926 . 1 90 18 18 VAL N N 119.122 . 1 91 19 19 ARG H H 8.373 . 1 92 19 19 ARG HA H 4.357 . 1 93 19 19 ARG C C 175.868 . 1 94 19 19 ARG CA C 56.003 . 1 95 19 19 ARG CB C 31.052 . 1 96 19 19 ARG N N 124.947 . 1 97 20 20 LYS H H 8.329 . 1 98 20 20 LYS HA H 4.323 . 1 99 20 20 LYS C C 176.114 . 1 100 20 20 LYS CA C 56.204 . 1 101 20 20 LYS CB C 33.506 . 1 102 20 20 LYS N N 123.125 . 1 103 21 21 TYR H H 8.305 . 1 104 21 21 TYR HA H 4.582 . 1 105 21 21 TYR C C 176.351 . 1 106 21 21 TYR CA C 58.101 . 1 107 21 21 TYR CB C 39.085 . 1 108 21 21 TYR N N 121.462 . 1 109 22 22 GLY H H 8.280 . 1 110 22 22 GLY HA2 H 3.945 . 1 111 22 22 GLY HA3 H 3.945 . 1 112 22 22 GLY C C 173.885 . 1 113 22 22 GLY CA C 45.361 . 1 114 22 22 GLY N N 110.602 . 1 115 23 23 GLU H H 8.245 . 1 116 23 23 GLU HA H 4.342 . 1 117 23 23 GLU C C 176.941 . 1 118 23 23 GLU CA C 56.762 . 1 119 23 23 GLU CB C 30.644 . 1 120 23 23 GLU N N 120.441 . 1 121 24 24 GLY H H 8.329 . 1 122 24 24 GLY HA2 H 3.865 . 1 123 24 24 GLY HA3 H 3.865 . 1 124 24 24 GLY C C 173.841 . 1 125 24 24 GLY CA C 45.404 . 1 126 24 24 GLY N N 109.365 . 1 127 25 25 ASN H H 8.248 . 1 128 25 25 ASN HA H 4.714 . 1 129 25 25 ASN CA C 53.360 . 1 130 25 25 ASN CB C 38.827 . 1 131 25 25 ASN N N 118.742 . 1 132 26 26 TRP H H 8.073 . 1 133 26 26 TRP HA H 4.681 . 1 134 26 26 TRP C C 176.370 . 1 135 26 26 TRP CA C 57.678 . 1 136 26 26 TRP CB C 29.628 . 1 137 26 26 TRP N N 121.257 . 1 138 27 27 SER H H 8.079 . 1 139 27 27 SER HA H 3.787 . 1 140 27 27 SER C C 174.550 . 1 141 27 27 SER CA C 58.800 . 1 142 27 27 SER CB C 63.741 . 1 143 27 27 SER N N 116.307 . 1 144 28 28 LYS H H 8.115 . 1 145 28 28 LYS HA H 4.291 . 1 146 28 28 LYS C C 176.482 . 1 147 28 28 LYS CA C 56.831 . 1 148 28 28 LYS CB C 33.100 . 1 149 28 28 LYS N N 122.726 . 1 150 29 29 ILE H H 7.962 . 1 151 29 29 ILE HA H 4.136 . 1 152 29 29 ILE C C 176.009 . 1 153 29 29 ILE CA C 61.419 . 1 154 29 29 ILE CB C 38.771 . 1 155 29 29 ILE N N 120.896 . 1 156 30 30 LEU H H 8.153 . 1 157 30 30 LEU HA H 4.371 . 1 158 30 30 LEU C C 176.935 . 1 159 30 30 LEU CA C 55.083 . 1 160 30 30 LEU CB C 42.323 . 1 161 30 30 LEU N N 125.508 . 1 162 31 31 LEU H H 8.096 . 1 163 31 31 LEU HA H 4.307 . 1 164 31 31 LEU C C 176.941 . 1 165 31 31 LEU CA C 55.188 . 1 166 31 31 LEU CB C 42.511 . 1 167 31 31 LEU N N 122.651 . 1 168 32 32 HIS H H 8.239 . 1 169 32 32 HIS HA H 4.635 . 1 170 32 32 HIS C C 175.109 . 1 171 32 32 HIS CA C 56.023 . 1 172 32 32 HIS CB C 30.494 . 1 173 32 32 HIS N N 119.114 . 1 174 33 33 TYR H H 8.033 . 1 175 33 33 TYR HA H 4.533 . 1 176 33 33 TYR C C 175.516 . 1 177 33 33 TYR CA C 57.678 . 1 178 33 33 TYR CB C 39.059 . 1 179 33 33 TYR N N 121.318 . 1 180 34 34 LYS H H 8.217 . 1 181 34 34 LYS HA H 4.270 . 1 182 34 34 LYS C C 175.925 . 1 183 34 34 LYS CA C 56.408 . 1 184 34 34 LYS CB C 33.287 . 1 185 34 34 LYS N N 122.911 . 1 186 35 35 PHE H H 8.124 . 1 187 35 35 PHE HA H 4.652 . 1 188 35 35 PHE C C 175.452 . 1 189 35 35 PHE CA C 57.625 . 1 190 35 35 PHE CB C 39.774 . 1 191 35 35 PHE N N 120.907 . 1 192 36 36 ASN H H 8.403 . 1 193 36 36 ASN HA H 4.737 . 1 194 36 36 ASN CA C 53.194 . 1 195 36 36 ASN CB C 39.285 . 1 196 36 36 ASN N N 120.470 . 1 197 37 37 ASN H H 8.361 . 1 198 37 37 ASN HA H 4.721 . 1 199 37 37 ASN CA C 53.422 . 1 200 37 37 ASN CB C 38.996 . 1 201 37 37 ASN N N 119.585 . 1 202 38 38 ARG H H 8.337 . 1 203 38 38 ARG HA H 4.439 . 1 204 38 38 ARG C C 176.511 . 1 205 38 38 ARG CA C 56.562 . 1 206 38 38 ARG CB C 30.872 . 1 207 38 38 ARG N N 120.994 . 1 208 39 39 THR H H 8.149 . 1 209 39 39 THR HA H 4.406 . 1 210 39 39 THR C C 174.646 . 1 211 39 39 THR CA C 62.068 . 1 212 39 39 THR CB C 69.852 . 1 213 39 39 THR N N 114.494 . 1 214 40 40 SER H H 8.317 . 1 215 40 40 SER HA H 4.535 . 1 216 40 40 SER C C 174.584 . 1 217 40 40 SER CA C 58.480 . 1 218 40 40 SER CB C 63.948 . 1 219 40 40 SER N N 118.016 . 1 220 41 41 VAL H H 8.100 . 1 221 41 41 VAL HA H 4.167 . 1 222 41 41 VAL C C 175.951 . 1 223 41 41 VAL CA C 62.525 . 1 224 41 41 VAL CB C 32.874 . 1 225 41 41 VAL N N 121.402 . 1 226 42 42 MET H H 8.371 . 1 227 42 42 MET HA H 4.518 . 1 228 42 42 MET CA C 55.566 . 1 229 42 42 MET CB C 33.040 . 1 230 42 42 MET N N 123.677 . 1 231 43 43 LEU H H 8.253 . 1 232 43 43 LEU HA H 4.313 . 1 233 43 43 LEU C C 177.367 . 1 234 43 43 LEU CA C 55.459 . 1 235 43 43 LEU CB C 42.455 . 1 236 43 43 LEU N N 124.019 . 1 237 44 44 LYS H H 8.286 . 1 238 44 44 LYS C C 176.315 . 1 239 44 44 LYS CA C 56.957 . 1 240 44 44 LYS CB C 33.030 . 1 241 44 44 LYS N N 121.502 . 1 242 45 45 ASP H H 8.271 . 1 243 45 45 ASP HA H 4.609 . 1 244 45 45 ASP C C 176.527 . 1 245 45 45 ASP CA C 54.577 . 1 246 45 45 ASP CB C 41.466 . 1 247 45 45 ASP N N 120.567 . 1 248 46 46 ARG H H 8.174 . 1 249 46 46 ARG HA H 4.200 . 1 250 46 46 ARG C C 176.298 . 1 251 46 46 ARG CA C 56.978 . 1 252 46 46 ARG CB C 30.528 . 1 253 46 46 ARG N N 121.025 . 1 254 47 47 TRP H H 8.063 . 1 255 47 47 TRP HA H 4.697 . 1 256 47 47 TRP C C 176.327 . 1 257 47 47 TRP CA C 57.274 . 1 258 47 47 TRP CB C 29.723 . 1 259 47 47 TRP N N 120.192 . 1 260 48 48 ARG H H 7.966 . 1 261 48 48 ARG HA H 4.320 . 1 262 48 48 ARG C C 176.333 . 1 263 48 48 ARG CA C 56.579 . 1 264 48 48 ARG CB C 30.978 . 1 265 48 48 ARG N N 121.457 . 1 266 49 49 THR H H 8.085 . 1 267 49 49 THR HA H 4.365 . 1 268 49 49 THR C C 174.487 . 1 269 49 49 THR CA C 61.980 . 1 270 49 49 THR CB C 69.822 . 1 271 49 49 THR N N 114.097 . 1 272 50 50 MET H H 8.281 . 1 273 50 50 MET HA H 4.543 . 1 274 50 50 MET CA C 55.639 . 1 275 50 50 MET CB C 33.462 . 1 276 50 50 MET N N 122.573 . 1 277 51 51 LYS H H 8.362 . 1 278 51 51 LYS HA H 4.400 . 1 279 51 51 LYS C C 176.066 . 1 280 51 51 LYS CA C 56.392 . 1 281 51 51 LYS CB C 33.355 . 1 282 51 51 LYS N N 122.662 . 1 283 52 52 CYS H H 8.391 . 1 284 52 52 CYS HA H 4.592 . 1 285 52 52 CYS CA C 58.546 . 1 286 52 52 CYS CB C 33.339 . 1 287 52 52 CYS N N 121.256 . 1 288 53 53 LEU H H 7.912 . 1 289 53 53 LEU CA C 56.927 . 1 290 53 53 LEU CB C 43.603 . 1 291 53 53 LEU N N 129.500 . 1 stop_ save_