data_699 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Sequential Resonance Assignments as a Basis for the Determination of a Three-dimensional Structure of Protein E-L30 of Escherichia coli ; _BMRB_accession_number 699 _BMRB_flat_file_name bmr699.str _Entry_type update _Submission_date 1995-07-31 _Accession_date 1996-03-25 _Entry_origination BMRB _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 'van de Ven' F. J.M. . 2 Hilbers C. W. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 222 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2010-06-11 revision BMRB 'Complete natural source information' 1999-06-14 revision BMRB 'Converted to BMRB NMR-STAR V 2.1 format' 1996-03-25 reformat BMRB 'Converted to the BMRB 1996-03-01 STAR flat-file format' 1995-07-31 original BMRB 'Last release in original BMRB flat-file format' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full ; van de Ven, F. J. M., Hilbers, C. W., "Sequential Resonance Assignments as a Basis for the Determination of a Three-dimensional Structure of Protein E-L30 of Escherichia coli," J. Mol. Biol. 192, 419-441 (1986). ; _Citation_title ; Sequential Resonance Assignments as a Basis for the Determination of a Three-dimensional Structure of Protein E-L30 of Escherichia coli ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 'van de Ven' F. J.M. . 2 Hilbers C. W. . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_volume 192 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 419 _Page_last 441 _Year 1986 _Details . save_ ################################## # Molecular system description # ################################## save_system_ribosomal_protein_E-L30 _Saveframe_category molecular_system _Mol_system_name 'ribosomal protein E-L30' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'ribosomal protein E-L30' $ribosomal_protein_E-L30 stop_ _System_molecular_weight . _System_oligomer_state ? _System_paramagnetic ? _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_ribosomal_protein_E-L30 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common 'ribosomal protein E-L30' _Molecular_mass . _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 58 _Mol_residue_sequence ; AKTIKITQTXSAIGRLXXHK ATLLGLGLRRIGHTVEREDT XAIRGMINAVSFMVKVEE ; loop_ _Residue_seq_code _Residue_label 1 ALA 2 LYS 3 THR 4 ILE 5 LYS 6 ILE 7 THR 8 GLN 9 THR 10 X 11 SER 12 ALA 13 ILE 14 GLY 15 ARG 16 LEU 17 X 18 X 19 HIS 20 LYS 21 ALA 22 THR 23 LEU 24 LEU 25 GLY 26 LEU 27 GLY 28 LEU 29 ARG 30 ARG 31 ILE 32 GLY 33 HIS 34 THR 35 VAL 36 GLU 37 ARG 38 GLU 39 ASP 40 THR 41 X 42 ALA 43 ILE 44 ARG 45 GLY 46 MET 47 ILE 48 ASN 49 ALA 50 VAL 51 SER 52 PHE 53 MET 54 VAL 55 LYS 56 VAL 57 GLU 58 GLU 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 58 "ribosomal protein E-L30" 100.00 58 100.00 100.00 8.78e-28 REF WP_000574348 "50S ribosomal protein L30, partial [Escherichia sp. TW10509]" 67.24 39 97.44 97.44 7.92e-17 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $ribosomal_protein_E-L30 'E. coli' 562 Bacteria . Escherichia coli 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 $ribosomal_protein_E-L30 'not available' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_one _Saveframe_category sample _Sample_type solution _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_list _Saveframe_category NMR_spectrometer _Manufacturer unknown _Model unknown _Field_strength 0 _Details 'spectrometer information not available' save_ ############################# # NMR applied experiments # ############################# save__1 _Saveframe_category NMR_applied_experiment _Sample_label $sample_one save_ ####################### # Sample conditions # ####################### save_sample_condition_set_one _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units pH 6.8 . na temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_shift_reference_par_set_one _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_citation_label _Correction_value_citation_label TSP H . . ppm 0 . . . . . $entry_citation $entry_citation 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_chemical_shift_assignment_data_set_one _Saveframe_category assigned_chemical_shifts _Details . loop_ _Sample_label $sample_one stop_ _Sample_conditions_label $sample_condition_set_one _Chem_shift_reference_set_label $chem_shift_reference_par_set_one _Mol_system_component_name 'ribosomal protein E-L30' _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 ALA HA H 4.13 . 1 2 . 1 ALA HB H 1.58 . 1 3 . 2 LYS H H 8.78 . 1 4 . 2 LYS HA H 4.52 . 1 5 . 2 LYS HB2 H 1.97 . 1 6 . 2 LYS HB3 H 1.97 . 1 7 . 3 THR H H 8.35 . 1 8 . 3 THR HA H 4.98 . 1 9 . 3 THR HB H 4.08 . 1 10 . 3 THR HG2 H 1.06 . 1 11 . 4 ILE H H 9.2 . 1 12 . 4 ILE HA H 4.73 . 1 13 . 4 ILE HB H 1.72 . 1 14 . 4 ILE HG2 H .86 . 1 15 . 5 LYS H H 8.4 . 1 16 . 5 LYS HA H 5.25 . 1 17 . 5 LYS HB2 H 1.72 . 2 18 . 5 LYS HB3 H 1.56 . 2 19 . 6 ILE H H 9.23 . 1 20 . 6 ILE HA H 4.87 . 1 21 . 6 ILE HB H 1.63 . 1 22 . 6 ILE HG2 H .77 . 1 23 . 7 THR H H 9 . 1 24 . 7 THR HA H 5.7 . 1 25 . 7 THR HB H 3.68 . 1 26 . 7 THR HG2 H .96 . 1 27 . 8 GLN H H 8.35 . 1 28 . 8 GLN HA H 4.78 . 1 29 . 8 GLN HB2 H 2.4 . 2 30 . 8 GLN HB3 H .86 . 2 31 . 8 GLN HG2 H 1.73 . 2 32 . 8 GLN HG3 H 1.37 . 2 33 . 8 GLN HE21 H 7.65 . 2 34 . 8 GLN HE22 H 6.12 . 2 35 . 9 THR H H 9.1 . 1 36 . 9 THR HA H 4.52 . 1 37 . 9 THR HB H 4.26 . 1 38 . 9 THR HG2 H 1.05 . 1 39 . 11 SER H H 8.9 . 1 40 . 11 SER HB2 H 4.08 . 2 41 . 11 SER HB3 H 3.88 . 2 42 . 12 ALA H H 9.08 . 1 43 . 12 ALA HA H 4.31 . 1 44 . 12 ALA HB H 1.4 . 1 45 . 13 ILE H H 8.07 . 1 46 . 13 ILE HA H 3.9 . 1 47 . 13 ILE HB H 1.85 . 1 48 . 13 ILE HG2 H .93 . 1 49 . 14 GLY HA2 H 4.03 . 2 50 . 14 GLY HA3 H 3.73 . 2 51 . 15 ARG H H 7.63 . 1 52 . 15 ARG HA H 4.7 . 1 53 . 15 ARG HB2 H 2.02 . 1 54 . 15 ARG HB3 H 2.02 . 1 55 . 16 LEU H H 9.02 . 1 56 . 16 LEU HA H 4.56 . 1 57 . 16 LEU HB2 H 1.35 . 1 58 . 16 LEU HB3 H 1.35 . 1 59 . 19 HIS H H 7.44 . 1 60 . 19 HIS HA H 4.49 . 1 61 . 19 HIS HB2 H 3.57 . 2 62 . 19 HIS HB3 H 3.11 . 2 63 . 19 HIS HD2 H 7.14 . 1 64 . 19 HIS HE1 H 7.96 . 1 65 . 20 LYS H H 7.85 . 1 66 . 20 LYS HA H 3.98 . 1 67 . 20 LYS HB2 H 1.95 . 1 68 . 20 LYS HB3 H 1.95 . 1 69 . 21 ALA H H 8.35 . 1 70 . 21 ALA HA H 4.15 . 1 71 . 21 ALA HB H 1.5 . 1 72 . 22 THR H H 7.9 . 1 73 . 22 THR HA H 3.95 . 1 74 . 22 THR HB H 4.31 . 1 75 . 22 THR HG2 H 1.3 . 1 76 . 23 LEU H H 7.97 . 1 77 . 23 LEU HA H 3.88 . 1 78 . 23 LEU HB2 H 1.99 . 2 79 . 23 LEU HB3 H 1.58 . 2 80 . 24 LEU H H 7.96 . 1 81 . 24 LEU HA H 4.23 . 1 82 . 24 LEU HB2 H 1.85 . 2 83 . 24 LEU HB3 H 1.65 . 2 84 . 25 GLY H H 8.3 . 1 85 . 25 GLY HA2 H 3.43 . 1 86 . 25 GLY HA3 H 3.43 . 1 87 . 26 LEU H H 7.88 . 1 88 . 26 LEU HA H 4.12 . 1 89 . 26 LEU HB2 H 2.18 . 1 90 . 26 LEU HB3 H 2.18 . 1 91 . 27 GLY H H 7.79 . 1 92 . 27 GLY HA2 H 4.27 . 2 93 . 27 GLY HA3 H 3.63 . 2 94 . 28 LEU H H 7.51 . 1 95 . 28 LEU HA H 4.7 . 1 96 . 28 LEU HB2 H 1.7 . 1 97 . 28 LEU HB3 H 1.7 . 1 98 . 29 ARG H H 11.05 . 1 99 . 29 ARG HA H 4.46 . 1 100 . 29 ARG HB2 H 2 . 2 101 . 29 ARG HB3 H 1.45 . 2 102 . 30 ARG H H 7.31 . 1 103 . 30 ARG HA H 4.63 . 1 104 . 30 ARG HB2 H 1.62 . 1 105 . 30 ARG HB3 H 1.62 . 1 106 . 31 ILE H H 8.45 . 1 107 . 31 ILE HA H 3.43 . 1 108 . 31 ILE HB H 1.58 . 1 109 . 31 ILE HG2 H .87 . 1 110 . 32 GLY H H 9.15 . 1 111 . 32 GLY HA2 H 4.31 . 2 112 . 32 GLY HA3 H 3.58 . 2 113 . 33 HIS H H 8.02 . 1 114 . 33 HIS HA H 4.73 . 1 115 . 33 HIS HB2 H 3.52 . 2 116 . 33 HIS HB3 H 3.16 . 2 117 . 33 HIS HD2 H 7.24 . 1 118 . 33 HIS HE1 H 7.86 . 1 119 . 34 THR H H 8.12 . 1 120 . 34 THR HA H 5.42 . 1 121 . 34 THR HB H 3.7 . 1 122 . 34 THR HG2 H 1.05 . 1 123 . 35 VAL H H 8.94 . 1 124 . 35 VAL HA H 4.59 . 1 125 . 35 VAL HB H 1.96 . 1 126 . 35 VAL HG1 H .79 . 2 127 . 35 VAL HG2 H .58 . 2 128 . 36 GLU H H 8.43 . 1 129 . 36 GLU HA H 5.36 . 1 130 . 36 GLU HB2 H 1.89 . 2 131 . 36 GLU HB3 H 1.79 . 2 132 . 37 ARG H H 8.98 . 1 133 . 37 ARG HA H 4.95 . 1 134 . 37 ARG HB2 H 1.5 . 1 135 . 37 ARG HB3 H 1.5 . 1 136 . 38 GLU H H 8.88 . 1 137 . 38 GLU HA H 4.26 . 1 138 . 38 GLU HB2 H 1.97 . 1 139 . 38 GLU HB3 H 1.97 . 1 140 . 39 ASP H H 8.36 . 1 141 . 39 ASP HA H 4.45 . 1 142 . 39 ASP HB2 H 2.95 . 2 143 . 39 ASP HB3 H 2.19 . 2 144 . 40 THR H H 7.31 . 1 145 . 40 THR HA H 4.96 . 1 146 . 40 THR HB H 4.64 . 1 147 . 40 THR HG2 H 1.19 . 1 148 . 42 ALA H H 8.2 . 1 149 . 42 ALA HA H 4.17 . 1 150 . 42 ALA HB H 1.44 . 1 151 . 43 ILE H H 7.71 . 1 152 . 43 ILE HA H 3.99 . 1 153 . 43 ILE HB H 2.35 . 1 154 . 43 ILE HG2 H .96 . 1 155 . 44 ARG H H 8.69 . 1 156 . 44 ARG HA H 3.96 . 1 157 . 44 ARG HB2 H 2.14 . 1 158 . 44 ARG HB3 H 2.14 . 1 159 . 45 GLY H H 8.45 . 1 160 . 45 GLY HA2 H 3.93 . 1 161 . 45 GLY HA3 H 3.93 . 1 162 . 46 MET H H 7.43 . 1 163 . 46 MET HA H 4.1 . 1 164 . 46 MET HB2 H 2.48 . 1 165 . 46 MET HB3 H 2.48 . 1 166 . 47 ILE H H 8.25 . 1 167 . 47 ILE HA H 3.15 . 1 168 . 47 ILE HB H 1.75 . 1 169 . 47 ILE HG2 H .7 . 1 170 . 48 ASN H H 8 . 1 171 . 48 ASN HA H 4.34 . 1 172 . 48 ASN HB2 H 2.88 . 1 173 . 48 ASN HB3 H 2.88 . 1 174 . 48 ASN HD21 H 6.94 . 1 175 . 48 ASN HD22 H 6.94 . 1 176 . 49 ALA H H 7.51 . 1 177 . 49 ALA HA H 4.31 . 1 178 . 49 ALA HB H 1.73 . 1 179 . 50 VAL H H 7.28 . 1 180 . 50 VAL HA H 4.3 . 1 181 . 50 VAL HB H 2.14 . 1 182 . 50 VAL HG1 H .89 . 2 183 . 50 VAL HG2 H .7 . 2 184 . 51 SER H H 7.1 . 1 185 . 51 SER HA H 3.84 . 1 186 . 51 SER HB2 H 4.02 . 2 187 . 51 SER HB3 H 4.15 . 2 188 . 52 PHE H H 7.01 . 1 189 . 52 PHE HA H 4.64 . 1 190 . 52 PHE HB2 H 3.08 . 2 191 . 52 PHE HB3 H 3.38 . 2 192 . 52 PHE HD1 H 7.16 . 1 193 . 52 PHE HD2 H 7.16 . 1 194 . 52 PHE HE1 H 7.24 . 1 195 . 52 PHE HE2 H 7.24 . 1 196 . 52 PHE HZ H 6.68 . 1 197 . 53 MET H H 8.01 . 1 198 . 53 MET HA H 4.56 . 1 199 . 53 MET HB2 H 2.12 . 1 200 . 53 MET HB3 H 2.12 . 1 201 . 54 VAL H H 7.1 . 1 202 . 54 VAL HA H 5.55 . 1 203 . 54 VAL HB H 1.89 . 1 204 . 54 VAL HG1 H .65 . 2 205 . 54 VAL HG2 H .59 . 2 206 . 55 LYS H H 8.85 . 1 207 . 55 LYS HA H 4.75 . 1 208 . 55 LYS HB2 H 1.6 . 1 209 . 55 LYS HB3 H 1.6 . 1 210 . 56 VAL H H 8.8 . 1 211 . 56 VAL HA H 4.88 . 1 212 . 56 VAL HB H 1.96 . 1 213 . 56 VAL HG1 H .85 . 2 214 . 56 VAL HG2 H .9 . 2 215 . 57 GLU H H 9.1 . 1 216 . 57 GLU HA H 4.64 . 1 217 . 57 GLU HB2 H 2.13 . 2 218 . 57 GLU HB3 H 1.85 . 2 219 . 58 GLU H H 8.33 . 1 220 . 58 GLU HA H 4.32 . 1 221 . 58 GLU HB2 H 2.05 . 2 222 . 58 GLU HB3 H 1.94 . 2 stop_ save_