data_18918 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Chemical shifts assignment for the unfolded state of the N-terminal domain of ribosomal protein L9 (NTL9) V3AI4A double mutant in 8.3 M urea ; _BMRB_accession_number 18918 _BMRB_flat_file_name bmr18918.str _Entry_type original _Submission_date 2012-12-22 _Accession_date 2012-12-22 _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 Meng Wenli . . 2 Raleigh Daniel P. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 54 "13C chemical shifts" 160 "15N chemical shifts" 54 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2013-05-30 original author . stop_ _Original_release_date 2013-05-30 save_ ############################# # Citation for this entry # ############################# save_citation_1 _Saveframe_category entry_citation _Citation_full . _Citation_title 'The denatured state ensemble contains significant local and long-range structure under native conditions: analysis of the N-terminal domain of ribosomal protein L9.' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 23480024 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Meng Wenli . . 2 Luan Bowu . . 3 Lyle Nicholas . . 4 Pappu Rohit V. . 5 Raleigh Daniel P. . stop_ _Journal_abbreviation Biochemistry _Journal_name_full Biochemistry _Journal_volume 52 _Journal_issue 15 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 2662 _Page_last 2671 _Year 2013 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name NTL9_V3AI4A _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label NTL9_V3AI4A $NTL9_V3AI4A_double_mutant stop_ _System_molecular_weight . _System_physical_state unfolded _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_NTL9_V3AI4A_double_mutant _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common NTL9_V3AI4A_double_mutant _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 56 _Mol_residue_sequence ; MKAAFLKDVKGKGKKGEIKN VADGYANNFLFKQGLAIEAT PANLKALEAQKQKEQR ; loop_ _Residue_seq_code _Residue_label 1 MET 2 LYS 3 ALA 4 ALA 5 PHE 6 LEU 7 LYS 8 ASP 9 VAL 10 LYS 11 GLY 12 LYS 13 GLY 14 LYS 15 LYS 16 GLY 17 GLU 18 ILE 19 LYS 20 ASN 21 VAL 22 ALA 23 ASP 24 GLY 25 TYR 26 ALA 27 ASN 28 ASN 29 PHE 30 LEU 31 PHE 32 LYS 33 GLN 34 GLY 35 LEU 36 ALA 37 ILE 38 GLU 39 ALA 40 THR 41 PRO 42 ALA 43 ASN 44 LEU 45 LYS 46 ALA 47 LEU 48 GLU 49 ALA 50 GLN 51 LYS 52 GLN 53 LYS 54 GLU 55 GLN 56 ARG stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-05-12 loop_ _Database_name _Database_accession_code _Database_entry_mol_name _Sequence_query_to_submitted_percentage _Sequence_subject_length _Sequence_identity _Sequence_positive _Sequence_homology_expectation_value BMRB 17675 NTL9_V3AI4A 100.00 56 100.00 100.00 1.90e-29 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $NTL9_V3AI4A_double_mutant 'Geobacillus stearothermophilus' 1422 Bacteria . Geobacillus stearothermophilus 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 $NTL9_V3AI4A_double_mutant 'recombinant technology' . Escherichia coli . pET3a 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 $NTL9_V3AI4A_double_mutant 0.5 mM '[U-99% 13C; U-99% 15N]' urea 8.3 M 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRView _Saveframe_category software _Name NMRView _Version . loop_ _Vendor _Address _Electronic_address 'Johnson, One Moon Scientific' . . 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_ ######################### # 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_HNCACB_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCO_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_NMR_spectrometer_expt _Saveframe_category NMR_applied_experiment _Experiment_name . _BMRB_pulse_sequence_accession_number . _Details . 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' 0.12 . M pH 5.5 . pH pressure 1 . atm temperature 285 . 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 internal indirect . . . 0.251449519 DSS H 1 'methyl protons' ppm 0 internal direct . . . 1 DSS N 15 'methyl protons' ppm 0 internal indirect . . . 0.101329112 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 HNCACB' '3D CBCA(CO)NH' '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 NTL9_V3AI4A _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 172.70 0.20 1 2 1 1 MET CA C 55.05 0.20 1 3 1 1 MET CB C 33.04 0.20 1 4 2 2 LYS H H 8.94 0.03 1 5 2 2 LYS C C 176.07 0.20 1 6 2 2 LYS CA C 55.45 0.20 1 7 2 2 LYS CB C 33.34 0.20 1 8 2 2 LYS N N 125.48 0.20 1 9 3 3 ALA H H 8.62 0.03 1 10 3 3 ALA C C 177.48 0.20 1 11 3 3 ALA CA C 52.32 0.20 1 12 3 3 ALA CB C 19.26 0.20 1 13 3 3 ALA N N 126.95 0.20 1 14 4 4 ALA H H 8.45 0.03 1 15 4 4 ALA C C 177.53 0.20 1 16 4 4 ALA CA C 52.33 0.20 1 17 4 4 ALA CB C 19.18 0.20 1 18 4 4 ALA N N 124.27 0.20 1 19 5 5 PHE H H 8.29 0.03 1 20 5 5 PHE C C 175.73 0.20 1 21 5 5 PHE CA C 57.55 0.20 1 22 5 5 PHE CB C 39.60 0.20 1 23 5 5 PHE N N 119.80 0.20 1 24 6 6 LEU H H 8.39 0.03 1 25 6 6 LEU C C 177.09 0.20 1 26 6 6 LEU CA C 55.36 0.20 1 27 6 6 LEU CB C 42.32 0.20 1 28 6 6 LEU N N 125.14 0.20 1 29 7 7 LYS H H 8.50 0.03 1 30 7 7 LYS C C 176.42 0.20 1 31 7 7 LYS CA C 56.45 0.20 1 32 7 7 LYS CB C 33.35 0.20 1 33 7 7 LYS N N 123.11 0.20 1 34 8 8 ASP H H 8.57 0.03 1 35 8 8 ASP C C 176.42 0.20 1 36 8 8 ASP CA C 54.27 0.20 1 37 8 8 ASP CB C 41.23 0.20 1 38 8 8 ASP N N 122.31 0.20 1 39 9 9 VAL H H 8.27 0.03 1 40 9 9 VAL C C 176.52 0.20 1 41 9 9 VAL CA C 62.31 0.20 1 42 9 9 VAL CB C 32.12 0.20 1 43 9 9 VAL N N 121.13 0.20 1 44 10 10 LYS H H 8.53 0.03 1 45 10 10 LYS C C 177.44 0.20 1 46 10 10 LYS CA C 56.59 0.20 1 47 10 10 LYS CB C 33.04 0.20 1 48 10 10 LYS N N 125.16 0.20 1 49 11 11 GLY H H 8.52 0.03 1 50 11 11 GLY C C 174.25 0.20 1 51 11 11 GLY CA C 45.12 0.20 1 52 11 11 GLY N N 110.45 0.20 1 53 12 12 LYS H H 8.39 0.03 1 54 12 12 LYS C C 177.45 0.20 1 55 12 12 LYS CA C 56.43 0.20 1 56 12 12 LYS CB C 33.49 0.20 1 57 12 12 LYS N N 121.01 0.20 1 58 13 13 GLY H H 8.57 0.03 1 59 13 13 GLY C C 174.14 0.20 1 60 13 13 GLY CA C 45.02 0.20 1 61 13 13 GLY N N 110.19 0.20 1 62 14 14 LYS H H 8.43 0.03 1 63 14 14 LYS C C 177.11 0.20 1 64 14 14 LYS CA C 56.34 0.20 1 65 14 14 LYS CB C 33.55 0.20 1 66 14 14 LYS N N 121.58 0.20 1 67 15 15 LYS H H 8.67 0.03 1 68 15 15 LYS C C 177.42 0.20 1 69 15 15 LYS CA C 56.80 0.20 1 70 15 15 LYS CB C 33.21 0.20 1 71 15 15 LYS N N 123.79 0.20 1 72 16 16 GLY H H 8.59 0.03 1 73 16 16 GLY C C 173.99 0.20 1 74 16 16 GLY CA C 45.05 0.20 1 75 16 16 GLY N N 110.95 0.20 1 76 17 17 GLU H H 8.35 0.03 1 77 17 17 GLU C C 176.51 0.20 1 78 17 17 GLU CA C 56.26 0.20 1 79 17 17 GLU CB C 30.57 0.20 1 80 17 17 GLU N N 121.01 0.20 1 81 18 18 ILE H H 8.50 0.03 1 82 18 18 ILE C C 176.37 0.20 1 83 18 18 ILE CA C 60.92 0.20 1 84 18 18 ILE CB C 38.57 0.20 1 85 18 18 ILE N N 123.61 0.20 1 86 19 19 LYS H H 8.63 0.03 1 87 19 19 LYS C C 176.31 0.20 1 88 19 19 LYS CA C 56.04 0.20 1 89 19 19 LYS CB C 33.53 0.20 1 90 19 19 LYS N N 126.79 0.20 1 91 20 20 ASN H H 8.72 0.03 1 92 20 20 ASN C C 175.54 0.20 1 93 20 20 ASN CA C 53.19 0.20 1 94 20 20 ASN CB C 38.99 0.20 1 95 20 20 ASN N N 121.62 0.20 1 96 21 21 VAL H H 8.31 0.03 1 97 21 21 VAL C C 176.06 0.20 1 98 21 21 VAL CA C 62.29 0.20 1 99 21 21 VAL CB C 33.01 0.20 1 100 21 21 VAL N N 121.03 0.20 1 101 22 22 ALA H H 8.47 0.03 1 102 22 22 ALA C C 177.62 0.20 1 103 22 22 ALA CA C 52.56 0.20 1 104 22 22 ALA CB C 19.14 0.20 1 105 22 22 ALA N N 127.31 0.20 1 106 23 23 ASP H H 8.31 0.03 1 107 23 23 ASP C C 176.99 0.20 1 108 23 23 ASP CA C 54.45 0.20 1 109 23 23 ASP CB C 41.23 0.20 1 110 23 23 ASP N N 120.02 0.20 1 111 24 24 GLY H H 8.35 0.03 1 112 24 24 GLY C C 174.22 0.20 1 113 24 24 GLY CA C 45.46 0.20 1 114 24 24 GLY N N 109.08 0.20 1 115 25 25 TYR H H 8.16 0.03 1 116 25 25 TYR C C 176.05 0.20 1 117 25 25 TYR CA C 58.07 0.20 1 118 25 25 TYR CB C 38.98 0.20 1 119 25 25 TYR N N 120.22 0.20 1 120 26 26 ALA H H 8.34 0.03 1 121 26 26 ALA C C 177.48 0.20 1 122 26 26 ALA CA C 52.50 0.20 1 123 26 26 ALA CB C 19.17 0.20 1 124 26 26 ALA N N 125.15 0.20 1 125 27 27 ASN H H 8.39 0.03 1 126 27 27 ASN C C 175.26 0.20 1 127 27 27 ASN CA C 53.17 0.20 1 128 27 27 ASN CB C 38.82 0.20 1 129 27 27 ASN N N 117.99 0.20 1 130 28 28 ASN H H 8.40 0.03 1 131 28 28 ASN C C 175.21 0.20 1 132 28 28 ASN CA C 53.20 0.20 1 133 28 28 ASN CB C 38.73 0.20 1 134 28 28 ASN N N 119.29 0.20 1 135 29 29 PHE H H 8.24 0.03 1 136 29 29 PHE C C 175.68 0.20 1 137 29 29 PHE CA C 58.08 0.20 1 138 29 29 PHE CB C 39.48 0.20 1 139 29 29 PHE N N 120.59 0.20 1 140 30 30 LEU H H 8.14 0.03 1 141 30 30 LEU C C 176.94 0.20 1 142 30 30 LEU CA C 54.95 0.20 1 143 30 30 LEU CB C 42.42 0.20 1 144 30 30 LEU N N 123.50 0.20 1 145 31 31 PHE H H 8.32 0.03 1 146 31 31 PHE C C 175.97 0.20 1 147 31 31 PHE CA C 57.63 0.20 1 148 31 31 PHE CB C 39.59 0.20 1 149 31 31 PHE N N 121.82 0.20 1 150 32 32 LYS H H 8.50 0.03 1 151 32 32 LYS C C 176.38 0.20 1 152 32 32 LYS CA C 56.41 0.20 1 153 32 32 LYS CB C 33.21 0.20 1 154 32 32 LYS N N 124.10 0.20 1 155 33 33 GLN H H 8.55 0.03 1 156 33 33 GLN C C 176.65 0.20 1 157 33 33 GLN CA C 55.91 0.20 1 158 33 33 GLN CB C 29.75 0.20 1 159 33 33 GLN N N 122.37 0.20 1 160 34 34 GLY H H 8.57 0.03 1 161 34 34 GLY C C 173.96 0.20 1 162 34 34 GLY CA C 45.15 0.20 1 163 34 34 GLY N N 110.61 0.20 1 164 35 35 LEU H H 8.20 0.03 1 165 35 35 LEU C C 177.35 0.20 1 166 35 35 LEU CA C 54.81 0.20 1 167 35 35 LEU CB C 42.83 0.20 1 168 35 35 LEU N N 121.88 0.20 1 169 36 36 ALA H H 8.54 0.03 1 170 36 36 ALA C C 177.87 0.20 1 171 36 36 ALA CA C 52.21 0.20 1 172 36 36 ALA CB C 18.95 0.20 1 173 36 36 ALA N N 125.89 0.20 1 174 37 37 ILE H H 8.27 0.03 1 175 37 37 ILE C C 176.57 0.20 1 176 37 37 ILE CA C 61.23 0.20 1 177 37 37 ILE CB C 38.75 0.20 1 178 37 37 ILE N N 121.14 0.20 1 179 38 38 GLU H H 8.60 0.03 1 180 38 38 GLU C C 176.13 0.20 1 181 38 38 GLU CA C 56.16 0.20 1 182 38 38 GLU CB C 30.27 0.20 1 183 38 38 GLU N N 125.29 0.20 1 184 39 39 ALA H H 8.46 0.03 1 185 39 39 ALA C C 177.77 0.20 1 186 39 39 ALA CA C 52.38 0.20 1 187 39 39 ALA CB C 19.28 0.20 1 188 39 39 ALA N N 126.02 0.20 1 189 40 40 THR H H 8.32 0.03 1 190 40 40 THR CA C 59.88 0.20 1 191 40 40 THR CB C 69.57 0.20 1 192 40 40 THR N N 116.32 0.20 1 193 41 41 PRO C C 176.96 0.20 1 194 41 41 PRO CA C 63.31 0.20 1 195 41 41 PRO CB C 32.11 0.20 1 196 42 42 ALA H H 8.54 0.03 1 197 42 42 ALA C C 177.91 0.20 1 198 42 42 ALA CA C 52.84 0.20 1 199 42 42 ALA CB C 19.08 0.20 1 200 42 42 ALA N N 124.53 0.20 1 201 43 43 ASN H H 8.51 0.03 1 202 43 43 ASN C C 175.58 0.20 1 203 43 43 ASN CA C 53.15 0.20 1 204 43 43 ASN CB C 38.47 0.20 1 205 43 43 ASN N N 117.69 0.20 1 206 44 44 LEU H H 8.26 0.03 1 207 44 44 LEU C C 177.79 0.20 1 208 44 44 LEU CA C 55.37 0.20 1 209 44 44 LEU CB C 42.26 0.20 1 210 44 44 LEU N N 123.00 0.20 1 211 45 45 LYS H H 8.43 0.03 1 212 45 45 LYS C C 176.90 0.20 1 213 45 45 LYS CA C 56.75 0.20 1 214 45 45 LYS CB C 33.06 0.20 1 215 45 45 LYS N N 122.49 0.20 1 216 46 46 ALA H H 8.35 0.03 1 217 46 46 ALA C C 178.22 0.20 1 218 46 46 ALA CA C 52.67 0.20 1 219 46 46 ALA CB C 18.98 0.20 1 220 46 46 ALA N N 125.34 0.20 1 221 47 47 LEU H H 8.31 0.03 1 222 47 47 LEU C C 177.96 0.20 1 223 47 47 LEU CA C 55.40 0.20 1 224 47 47 LEU CB C 42.30 0.20 1 225 47 47 LEU N N 121.90 0.20 1 226 48 48 GLU H H 8.51 0.03 1 227 48 48 GLU C C 176.62 0.20 1 228 48 48 GLU CA C 56.44 0.20 1 229 48 48 GLU CB C 30.22 0.20 1 230 48 48 GLU N N 121.93 0.20 1 231 49 49 ALA H H 8.41 0.03 1 232 49 49 ALA C C 178.11 0.20 1 233 49 49 ALA CA C 52.63 0.20 1 234 49 49 ALA CB C 19.04 0.20 1 235 49 49 ALA N N 125.24 0.20 1 236 50 50 GLN H H 8.47 0.03 1 237 50 50 GLN C C 176.51 0.20 1 238 50 50 GLN CA C 56.07 0.20 1 239 50 50 GLN CB C 29.52 0.20 1 240 50 50 GLN N N 120.10 0.20 1 241 51 51 LYS H H 8.51 0.03 1 242 51 51 LYS C C 177.01 0.20 1 243 51 51 LYS CA C 56.53 0.20 1 244 51 51 LYS CB C 33.22 0.20 1 245 51 51 LYS N N 123.47 0.20 1 246 52 52 GLN H H 8.64 0.03 1 247 52 52 GLN C C 176.43 0.20 1 248 52 52 GLN CA C 55.89 0.20 1 249 52 52 GLN CB C 29.51 0.20 1 250 52 52 GLN N N 122.45 0.20 1 251 53 53 LYS H H 8.62 0.03 1 252 53 53 LYS C C 176.83 0.20 1 253 53 53 LYS CA C 56.83 0.20 1 254 53 53 LYS CB C 33.19 0.20 1 255 53 53 LYS N N 123.65 0.20 1 256 54 54 GLU H H 8.67 0.03 1 257 54 54 GLU C C 176.50 0.20 1 258 54 54 GLU CA C 56.49 0.20 1 259 54 54 GLU CB C 30.30 0.20 1 260 54 54 GLU N N 122.79 0.20 1 261 55 55 GLN H H 8.60 0.03 1 262 55 55 GLN C C 175.28 0.20 1 263 55 55 GLN CA C 55.92 0.20 1 264 55 55 GLN CB C 29.75 0.20 1 265 55 55 GLN N N 122.98 0.20 1 266 56 56 ARG H H 8.28 0.03 1 267 56 56 ARG CA C 57.57 0.20 1 268 56 56 ARG N N 128.74 0.20 1 stop_ save_