data_50191 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; RBM5 RRM1-Zf1-C191G ; _BMRB_accession_number 50191 _BMRB_flat_file_name bmr50191.str _Entry_type original _Submission_date 2020-02-04 _Accession_date 2020-02-04 _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 Soni Komal . . 2 Sattler Michael . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 106 "15N chemical shifts" 106 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2020-07-13 update BMRB 'update entry citation' 2020-06-09 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 50187 'RBM5 RRM1-Zf1, wild type' stop_ _Original_release_date 2020-02-04 save_ ############################# # Citation for this entry # ############################# save_citations_1 _Saveframe_category entry_citation _Citation_full . _Citation_title ; Conformational Dynamics From Ambiguous Zinc Coordination in the RanBP2-Type Zinc Finger of RBM5 ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 32450081 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Soni Komal . . 2 Martinez-Lumbreras Santiago . . 3 Sattler Michael . . stop_ _Journal_abbreviation 'J. Mol. Biol.' _Journal_name_full 'Journal of molecular biology' _Journal_volume 432 _Journal_issue 14 _Journal_ISSN 1089-8638 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 4127 _Page_last 4138 _Year 2020 _Details . loop_ _Keyword RBM5 stop_ save_ ################################## # Molecular system description # ################################## save_assembly_1 _Saveframe_category molecular_system _Mol_system_name 'monomer RRM1-Zf1 C191G' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label RRM1-Zf1 $entity_1 Zn $entity_ZN 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_entity_1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common entity_1 _Molecular_mass . _Mol_thiol_state 'free disulfide and other bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count . _Mol_residue_sequence ; MGERESKTIMLRGLPTTITE SDIREMMESFEGPQPADVRL MKRKTGVSRGFAFVEFYHLQ DATSWMEANQKKLVIQGKHI AMHYSNPRPKFEDWLCNKCG LNNFRKRLKCFRCGADKFD ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 92 MET 2 93 GLY 3 94 GLU 4 95 ARG 5 96 GLU 6 97 SER 7 98 LYS 8 99 THR 9 100 ILE 10 101 MET 11 102 LEU 12 103 ARG 13 104 GLY 14 105 LEU 15 106 PRO 16 107 THR 17 108 THR 18 109 ILE 19 110 THR 20 111 GLU 21 112 SER 22 113 ASP 23 114 ILE 24 115 ARG 25 116 GLU 26 117 MET 27 118 MET 28 119 GLU 29 120 SER 30 121 PHE 31 122 GLU 32 123 GLY 33 124 PRO 34 125 GLN 35 126 PRO 36 127 ALA 37 128 ASP 38 129 VAL 39 130 ARG 40 131 LEU 41 132 MET 42 133 LYS 43 134 ARG 44 135 LYS 45 136 THR 46 137 GLY 47 138 VAL 48 139 SER 49 140 ARG 50 141 GLY 51 142 PHE 52 143 ALA 53 144 PHE 54 145 VAL 55 146 GLU 56 147 PHE 57 148 TYR 58 149 HIS 59 150 LEU 60 151 GLN 61 152 ASP 62 153 ALA 63 154 THR 64 155 SER 65 156 TRP 66 157 MET 67 158 GLU 68 159 ALA 69 160 ASN 70 161 GLN 71 162 LYS 72 163 LYS 73 164 LEU 74 165 VAL 75 166 ILE 76 167 GLN 77 168 GLY 78 169 LYS 79 170 HIS 80 171 ILE 81 172 ALA 82 173 MET 83 174 HIS 84 175 TYR 85 176 SER 86 177 ASN 87 178 PRO 88 179 ARG 89 180 PRO 90 181 LYS 91 182 PHE 92 183 GLU 93 184 ASP 94 185 TRP 95 186 LEU 96 187 CYS 97 188 ASN 98 189 LYS 99 190 CYS 100 191 GLY 101 192 LEU 102 193 ASN 103 194 ASN 104 195 PHE 105 196 ARG 106 197 LYS 107 198 ARG 108 199 LEU 109 200 LYS 110 201 CYS 111 202 PHE 112 203 ARG 113 204 CYS 114 205 GLY 115 206 ALA 116 207 ASP 117 208 LYS 118 209 PHE 119 210 ASP stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . 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 NCBI NP_005769.1 RBM5 . . . . . stop_ save_ ############# # Ligands # ############# save_ZN _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common "entity_ZN (ZINC ION)" _BMRB_code ZN _PDB_code ZN _Molecular_mass 65.409 _Mol_charge 2 _Mol_paramagnetic . _Mol_aromatic no _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons ZN ZN ZN . 2 . ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source_1 _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $entity_1 Human 9606 Eukaryota Metazoa Homo sapiens stop_ save_ ######################### # Experimental source # ######################### save_experimental_source_1 _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_type _Vector_name $entity_1 'recombinant technology' . Escherichia coli 'BL21 (DE3)' plasmid pET28a 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 $entity_1 . mM [U-15] MES 20 mM 'natural abundance' 'sodium chloride' 400 mM 'natural abundance' DTT 1 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_software_1_Analysis _Saveframe_category software _Name Analysis _Version . loop_ _Vendor _Address _Electronic_address CCPN . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1_800 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details . save_ save_NMR_spectrometer_2_600 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _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_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.4 . M pH 6.5 . pH pressure 1 . atm temperature 298 . K stop_ save_ #################### # NMR parameters # #################### ############################## # Assigned chemical shifts # ############################## ################################ # Chemical shift referencing # ################################ save_chem_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 water C 13 protons ppm 4.7 internal direct . . . 1 water H 1 protons ppm 4.7 internal direct . . . 1 water N 15 protons ppm 4.7 internal direct . . . 1 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_chemical_shifts_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 $chem_shift_reference_1 _Mol_system_component_name RRM1-Zf1 _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 95 4 ARG H H 8.391 0.000 . 2 95 4 ARG N N 122.537 0.000 . 3 96 5 GLU H H 8.171 0.000 . 4 96 5 GLU N N 120.931 0.000 . 5 97 6 SER H H 6.459 0.000 . 6 97 6 SER N N 116.051 0.000 . 7 98 7 LYS H H 7.973 0.000 . 8 98 7 LYS N N 116.443 0.000 . 9 99 8 THR H H 8.405 0.000 . 10 99 8 THR N N 115.645 0.000 . 11 100 9 ILE H H 9.316 0.000 . 12 100 9 ILE N N 125.804 0.000 . 13 101 10 MET H H 9.320 0.000 . 14 101 10 MET N N 126.015 0.000 . 15 102 11 LEU H H 8.942 0.000 . 16 102 11 LEU N N 125.265 0.000 . 17 103 12 ARG H H 8.685 0.000 . 18 103 12 ARG N N 119.875 0.000 . 19 104 13 GLY H H 8.215 0.000 . 20 104 13 GLY N N 109.192 0.000 . 21 105 14 LEU H H 8.084 0.000 . 22 105 14 LEU N N 119.226 0.000 . 23 107 16 THR H H 8.881 0.000 . 24 107 16 THR N N 116.062 0.000 . 25 108 17 THR H H 7.086 0.000 . 26 108 17 THR N N 106.745 0.000 . 27 109 18 ILE H H 6.936 0.000 . 28 109 18 ILE N N 121.262 0.000 . 29 110 19 THR H H 9.056 0.000 . 30 110 19 THR N N 118.700 0.000 . 31 111 20 GLU H H 9.256 0.000 . 32 111 20 GLU N N 121.038 0.000 . 33 112 21 SER H H 8.270 0.000 . 34 112 21 SER N N 113.668 0.000 . 35 113 22 ASP H H 7.616 0.000 . 36 113 22 ASP N N 121.925 0.000 . 37 114 23 ILE H H 7.654 0.000 . 38 114 23 ILE N N 119.304 0.000 . 39 115 24 ARG H H 8.159 0.000 . 40 115 24 ARG N N 120.003 0.000 . 41 116 25 GLU H H 8.155 0.000 . 42 116 25 GLU N N 118.690 0.000 . 43 117 26 MET H H 7.841 0.000 . 44 117 26 MET N N 119.254 0.000 . 45 118 27 MET H H 7.980 0.000 . 46 118 27 MET N N 117.140 0.000 . 47 119 28 GLU H H 7.761 0.000 . 48 119 28 GLU N N 118.845 0.000 . 49 120 29 SER H H 7.645 0.000 . 50 120 29 SER N N 112.916 0.000 . 51 121 30 PHE H H 7.496 0.000 . 52 121 30 PHE N N 122.207 0.000 . 53 122 31 GLU H H 8.445 0.000 . 54 122 31 GLU N N 121.479 0.000 . 55 123 32 GLY H H 8.025 0.000 . 56 123 32 GLY N N 108.625 0.000 . 57 125 34 GLN H H 8.400 0.000 . 58 125 34 GLN N N 120.052 0.000 . 59 127 36 ALA H H 8.504 0.000 . 60 127 36 ALA N N 123.567 0.000 . 61 128 37 ASP H H 7.412 0.000 . 62 128 37 ASP N N 113.262 0.000 . 63 129 38 VAL H H 7.798 0.000 . 64 129 38 VAL N N 121.852 0.000 . 65 130 39 ARG H H 8.887 0.000 . 66 130 39 ARG N N 125.036 0.000 . 67 131 40 LEU H H 9.405 0.000 . 68 131 40 LEU N N 127.374 0.000 . 69 132 41 MET H H 8.112 0.000 . 70 132 41 MET N N 125.159 0.000 . 71 133 42 LYS H H 8.435 0.000 . 72 133 42 LYS N N 121.478 0.000 . 73 134 43 ARG H H 8.747 0.000 . 74 134 43 ARG N N 120.397 0.000 . 75 136 45 THR H H 7.200 0.000 . 76 136 45 THR N N 106.719 0.000 . 77 137 46 GLY H H 8.174 0.000 . 78 137 46 GLY N N 109.467 0.000 . 79 138 47 VAL H H 7.163 0.000 . 80 138 47 VAL N N 118.814 0.000 . 81 139 48 SER H H 8.632 0.000 . 82 139 48 SER N N 119.478 0.000 . 83 140 49 ARG H H 8.673 0.000 . 84 140 49 ARG N N 122.110 0.000 . 85 141 50 GLY H H 8.910 0.000 . 86 141 50 GLY N N 106.798 0.000 . 87 143 52 ALA H H 8.554 0.000 . 88 143 52 ALA N N 120.296 0.000 . 89 144 53 PHE H H 8.988 0.000 . 90 144 53 PHE N N 118.185 0.000 . 91 145 54 VAL H H 9.480 0.000 . 92 145 54 VAL N N 124.268 0.000 . 93 146 55 GLU H H 8.277 0.000 . 94 146 55 GLU N N 126.011 0.000 . 95 147 56 PHE H H 8.969 0.000 . 96 147 56 PHE N N 123.046 0.000 . 97 148 57 TYR H H 9.725 0.000 . 98 148 57 TYR N N 118.787 0.000 . 99 149 58 HIS H H 7.324 0.000 . 100 149 58 HIS N N 111.072 0.000 . 101 151 60 GLN H H 9.238 0.000 . 102 151 60 GLN N N 115.983 0.000 . 103 152 61 ASP H H 7.215 0.000 . 104 152 61 ASP N N 119.542 0.000 . 105 153 62 ALA H H 6.902 0.000 . 106 153 62 ALA N N 122.186 0.000 . 107 154 63 THR H H 8.518 0.000 . 108 154 63 THR N N 109.504 0.000 . 109 155 64 SER H H 7.850 0.000 . 110 155 64 SER N N 118.776 0.000 . 111 156 65 TRP H H 8.155 0.000 . 112 156 65 TRP N N 124.961 0.000 . 113 157 66 MET H H 8.717 0.000 . 114 157 66 MET N N 119.635 0.000 . 115 158 67 GLU H H 8.168 0.000 . 116 158 67 GLU N N 117.584 0.000 . 117 159 68 ALA H H 7.607 0.000 . 118 159 68 ALA N N 118.550 0.000 . 119 161 70 GLN H H 8.076 0.000 . 120 161 70 GLN N N 120.284 0.000 . 121 162 71 LYS H H 8.532 0.000 . 122 162 71 LYS N N 114.918 0.000 . 123 163 72 LYS H H 7.607 0.000 . 124 163 72 LYS N N 117.861 0.000 . 125 164 73 LEU H H 7.988 0.000 . 126 164 73 LEU N N 121.893 0.000 . 127 165 74 VAL H H 8.090 0.000 . 128 165 74 VAL N N 127.568 0.000 . 129 166 75 ILE H H 8.479 0.000 . 130 166 75 ILE N N 124.906 0.000 . 131 167 76 GLN H H 9.437 0.000 . 132 167 76 GLN N N 126.886 0.000 . 133 168 77 GLY H H 8.242 0.000 . 134 168 77 GLY N N 102.699 0.000 . 135 169 78 LYS H H 7.861 0.000 . 136 169 78 LYS N N 121.462 0.000 . 137 170 79 HIS H H 8.821 0.000 . 138 170 79 HIS N N 122.964 0.000 . 139 171 80 ILE H H 8.249 0.000 . 140 171 80 ILE N N 127.028 0.000 . 141 172 81 ALA H H 8.159 0.000 . 142 172 81 ALA N N 130.240 0.000 . 143 173 82 MET H H 8.060 0.000 . 144 173 82 MET N N 117.677 0.000 . 145 174 83 HIS H H 8.343 0.000 . 146 174 83 HIS N N 117.117 0.000 . 147 175 84 TYR H H 8.815 0.000 . 148 175 84 TYR N N 122.421 0.000 . 149 176 85 SER H H 8.638 0.000 . 150 176 85 SER N N 114.477 0.000 . 151 177 86 ASN H H 9.196 0.000 . 152 177 86 ASN N N 125.675 0.000 . 153 179 88 ARG H H 8.928 0.000 . 154 179 88 ARG N N 124.413 0.000 . 155 181 90 LYS H H 8.421 0.000 . 156 181 90 LYS N N 122.530 0.000 . 157 182 91 PHE H H 8.482 0.000 . 158 182 91 PHE N N 117.544 0.000 . 159 183 92 GLU H H 7.145 0.000 . 160 183 92 GLU N N 116.878 0.000 . 161 184 93 ASP H H 8.421 0.000 . 162 184 93 ASP N N 123.240 0.000 . 163 185 94 TRP H H 8.231 0.000 . 164 185 94 TRP N N 116.003 0.000 . 165 186 95 LEU H H 9.345 0.000 . 166 186 95 LEU N N 122.125 0.000 . 167 187 96 CYS H H 8.795 0.000 . 168 187 96 CYS N N 129.828 0.000 . 169 188 97 ASN H H 9.150 0.000 . 170 188 97 ASN N N 127.879 0.000 . 171 189 98 LYS H H 9.439 0.000 . 172 189 98 LYS N N 122.844 0.000 . 173 190 99 CYS H H 9.010 0.000 . 174 190 99 CYS N N 119.807 0.000 . 175 191 100 GLY H H 7.430 0.000 . 176 191 100 GLY N N 112.604 0.000 . 177 192 101 LEU H H 8.163 0.000 . 178 192 101 LEU N N 123.466 0.000 . 179 193 102 ASN H H 8.462 0.000 . 180 193 102 ASN N N 124.185 0.000 . 181 194 103 ASN H H 9.009 0.000 . 182 194 103 ASN N N 126.030 0.000 . 183 195 104 PHE H H 7.793 0.000 . 184 195 104 PHE N N 119.114 0.000 . 185 196 105 ARG H H 8.037 0.000 . 186 196 105 ARG N N 122.956 0.000 . 187 198 107 ARG H H 8.462 0.000 . 188 198 107 ARG N N 118.909 0.000 . 189 199 108 LEU H H 9.024 0.000 . 190 199 108 LEU N N 123.315 0.000 . 191 200 109 LYS H H 7.666 0.000 . 192 200 109 LYS N N 117.037 0.000 . 193 201 110 CYS H H 9.811 0.000 . 194 201 110 CYS N N 126.283 0.000 . 195 202 111 PHE H H 9.249 0.000 . 196 202 111 PHE N N 131.712 0.000 . 197 203 112 ARG H H 8.847 0.000 . 198 203 112 ARG N N 120.849 0.000 . 199 204 113 CYS H H 8.418 0.000 . 200 204 113 CYS N N 118.433 0.000 . 201 205 114 GLY H H 7.620 0.000 . 202 205 114 GLY N N 112.153 0.000 . 203 206 115 ALA H H 8.921 0.000 . 204 206 115 ALA N N 125.801 0.000 . 205 207 116 ASP H H 8.651 0.000 . 206 207 116 ASP N N 121.365 0.000 . 207 208 117 LYS H H 7.479 0.000 . 208 208 117 LYS N N 124.563 0.000 . 209 209 118 PHE H H 8.472 0.000 . 210 209 118 PHE N N 115.902 0.000 . 211 210 119 ASP H H 7.319 0.000 . 212 210 119 ASP N N 125.419 0.000 . stop_ save_