data_36072 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; C-terminal zinc finger of RING finger protein 141 ; _BMRB_accession_number 36072 _BMRB_flat_file_name bmr36072.str _Entry_type original _Submission_date 2017-04-05 _Accession_date 2017-06-19 _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 Miyamoto K. . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 41 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2019-03-08 update BMRB 'update entry citation' 2018-04-30 original author 'original release' stop_ _Original_release_date 2017-06-19 save_ ############################# # Citation for this entry # ############################# save_citation_1 _Saveframe_category entry_citation _Citation_full . _Citation_title ; The zinc finger domain of RING finger protein 141 reveals a unique RING fold. ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 28547869 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Miyamoto Kazuhide . . 2 Uechi Airi . . 3 Saito Kazuki . . stop_ _Journal_abbreviation 'Protein Sci.' _Journal_name_full 'Protein science : a publication of the Protein Society' _Journal_volume 26 _Journal_issue 8 _Journal_ISSN 1469-896X _Journal_CSD 0353 _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1681 _Page_last 1686 _Year 2017 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Synaptotagmin-like protein 4' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label entity_1 $entity_1 entity_ZN_1 $entity_ZN entity_ZN_2 $entity_ZN stop_ _System_molecular_weight . _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 'RING finger protein 141' _Molecular_mass 4920.788 _Mol_thiol_state 'free and other bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 42 _Mol_residue_sequence ; EEECCICMDGRADLILPCAH SFCQKCIDKWSDRHRNCPIC RL ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 GLU 2 2 GLU 3 3 GLU 4 4 CYS 5 5 CYS 6 6 ILE 7 7 CYS 8 8 MET 9 9 ASP 10 10 GLY 11 11 ARG 12 12 ALA 13 13 ASP 14 14 LEU 15 15 ILE 16 16 LEU 17 17 PRO 18 18 CYS 19 19 ALA 20 20 HIS 21 21 SER 22 22 PHE 23 23 CYS 24 24 GLN 25 25 LYS 26 26 CYS 27 27 ILE 28 28 ASP 29 29 LYS 30 30 TRP 31 31 SER 32 32 ASP 33 33 ARG 34 34 HIS 35 35 ARG 36 36 ASN 37 37 CYS 38 38 PRO 39 39 ILE 40 40 CYS 41 41 ARG 42 42 LEU stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ ############# # Ligands # ############# save_ZN _Saveframe_category ligand _Mol_type non-polymer _Name_common 'ZINC ION' _BMRB_code . _PDB_code ZN _Molecular_mass 65.409 _Mol_charge . _Mol_paramagnetic . _Mol_aromatic . _Details . _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _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 _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Vector_name $entity_1 'chemical synthesis' . . . . . stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details '1.0 mM [U-13C; U-15N] RING finger protein 141, 90% H2O/10% D2O' loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $entity_1 1.0 mM '[U-13C; U-15N]' Tris-HCl 20 mM 'natural abundance' NaCl 50 mM 'natural abundance' dithiothreitol 1 mM 'natural abundance' ZnCl2 50 uM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % U-2H stop_ save_ ############################ # Computer software used # ############################ save_software_1 _Saveframe_category software _Name CYANA _Version 2.1 loop_ _Vendor _Address _Electronic_address 'Guntert, Mumenthaler and Wuthrich' . . stop_ loop_ _Task 'chemical shift assignment' 'peak picking' refinement stop_ _Details . save_ save_software_2 _Saveframe_category software _Name 'Discovery Studio' _Version 2.1 loop_ _Vendor _Address _Electronic_address 'Accelrys Software Inc.' . . stop_ loop_ _Task 'structure calculation' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details . save_ ############################# # NMR applied experiments # ############################# save_3D_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '3D NOESY' _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' 70 . mM pH 6.9 . pH pressure 1 . atm temperature 293 . 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 DSS H 1 'methyl protons' ppm 0.000 internal direct . . . 1.0 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 '3D NOESY' 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 entity_1 _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 2 2 GLU HA H 4.13 0.03 1 2 3 3 GLU HA H 4.22 0.03 1 3 4 4 CYS HA H 4.68 0.03 1 4 5 5 CYS HA H 4.42 0.03 1 5 6 6 ILE HA H 4.23 0.03 1 6 7 7 CYS HA H 4.45 0.03 1 7 8 8 MET HA H 4.10 0.03 1 8 9 9 ASP HA H 4.69 0.03 1 9 10 10 GLY HA2 H 3.99 0.03 2 10 10 10 GLY HA3 H 3.99 0.03 2 11 11 11 ARG HA H 4.15 0.03 1 12 12 12 ALA HA H 3.78 0.03 1 13 13 13 ASP HA H 3.99 0.03 1 14 14 14 LEU HA H 4.59 0.03 1 15 15 15 ILE HA H 4.21 0.03 1 16 16 16 LEU HA H 4.63 0.03 1 17 17 17 PRO HA H 4.15 0.03 1 18 18 18 CYS HA H 4.35 0.03 1 19 19 19 ALA HA H 3.88 0.03 1 20 20 20 HIS HA H 4.55 0.03 1 21 21 21 SER HA H 4.99 0.03 1 22 22 22 PHE HA H 4.85 0.03 1 23 23 23 CYS HA H 4.87 0.03 1 24 24 24 GLN HA H 3.98 0.03 1 25 25 25 LYS HA H 4.31 0.03 1 26 26 26 CYS HA H 4.06 0.03 1 27 27 27 ILE HA H 3.35 0.03 1 28 28 28 ASP HA H 4.35 0.03 1 29 29 29 LYS HA H 3.89 0.03 1 30 30 30 TRP HA H 4.86 0.03 1 31 31 31 SER HA H 4.36 0.03 1 32 32 32 ASP HA H 4.23 0.03 1 33 33 33 ARG HA H 3.87 0.03 1 34 34 34 HIS HA H 4.40 0.03 1 35 35 35 ARG HA H 3.84 0.03 1 36 36 36 ASN HA H 4.51 0.03 1 37 37 37 CYS HA H 3.89 0.03 1 38 38 38 PRO HA H 4.36 0.03 1 39 39 39 ILE HA H 3.81 0.03 1 40 40 40 CYS HA H 3.93 0.03 1 41 41 41 ARG HA H 4.33 0.03 1 stop_ save_