data_26576 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; 1H, 15N, resonance assignment of the aortic medial amyloid protein medin in non-denaturing conditions. ; _BMRB_accession_number 26576 _BMRB_flat_file_name bmr26576.str _Entry_type original _Submission_date 2015-05-11 _Accession_date 2015-05-11 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details ; This deposition is a development of work deposited in BMRB:25399. The 1H, 15N, 13C resonance assignment was carried out in denaturing conditions (8M Urea) and we have now carried out a urea titration to assign the non-denaturing form at a much lower protein concentration. ; loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Davies Hannah A. . 2 Phelan Marie M. . 3 Madine Jilllian . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 44 "15N chemical shifts" 44 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2016-07-12 update BMRB 'update entry citation' 2015-09-22 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 25399 '1H, 15N, 13C resonance assignment of the aortic medial amyloid protein medin in denaturing conditions.' stop_ _Original_release_date 2015-09-22 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; 1H, 15N and 13C assignment of the amyloidogenic protein medin using fast-pulsing NMR techniques ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 26377205 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Davies Hannah A. . 2 Phelan Marie M. . 3 Madine Jilllian . . stop_ _Journal_abbreviation 'Biomol. NMR Assign.' _Journal_volume 10 _Journal_issue 1 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 75 _Page_last 77 _Year 2016 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name Medin _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label Medin $Medin stop_ _System_molecular_weight . _System_physical_state 'intrinsically disordered' _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_Medin _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Medin _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 50 _Mol_residue_sequence ; RLDKQGNFNAWVAGSYGNDQ WLQVDLGSSKEVTGIITQGA RNFGSVQFVA ; loop_ _Residue_seq_code _Residue_label 1 ARG 2 LEU 3 ASP 4 LYS 5 GLN 6 GLY 7 ASN 8 PHE 9 ASN 10 ALA 11 TRP 12 VAL 13 ALA 14 GLY 15 SER 16 TYR 17 GLY 18 ASN 19 ASP 20 GLN 21 TRP 22 LEU 23 GLN 24 VAL 25 ASP 26 LEU 27 GLY 28 SER 29 SER 30 LYS 31 GLU 32 VAL 33 THR 34 GLY 35 ILE 36 ILE 37 THR 38 GLN 39 GLY 40 ALA 41 ARG 42 ASN 43 PHE 44 GLY 45 SER 46 VAL 47 GLN 48 PHE 49 VAL 50 ALA 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 UNP Q08431 Medin . . . . . stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Medin 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 $Medin 'recombinant technology' . Escherichia coli . pOPINS 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 $Medin 20 uM '[U-98% 13C; U-98% 15N]' 'sodium chloride' 20 mM 'natural abundance' 'sodium phosphate' 20 mM 'natural abundance' TSP 2 uM [U-2H] stop_ save_ ############################ # Computer software used # ############################ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version . loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection processing stop_ _Details . save_ save_Analysis _Saveframe_category software _Name Analysis _Version . loop_ _Vendor _Address _Electronic_address CCPN . . stop_ loop_ _Task 'chemical shift assignment' 'data analysis' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 800 _Details 'TCI cryoprobe' 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' 20 . mM pH 6.5 . pH pressure 1 . atm temperature 298 . 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 TSP H 1 'methyl protons' ppm 1 internal direct . . . 1 TSP N 15 'methyl protons' ppm 0.1 internal 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' 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 Medin _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 LEU H H 8.487 0.000 1 2 2 2 LEU N N 122.164 0.000 1 3 3 3 ASP H H 8.358 0.000 1 4 3 3 ASP N N 120.690 0.000 1 5 4 4 LYS H H 8.218 0.000 1 6 4 4 LYS N N 120.334 0.000 1 7 6 6 GLY H H 8.315 0.000 1 8 6 6 GLY N N 109.517 0.000 1 9 7 7 ASN H H 8.241 0.000 1 10 7 7 ASN N N 118.741 0.000 1 11 11 11 TRP H H 7.974 0.000 1 12 11 11 TRP N N 119.787 0.000 1 13 12 12 VAL H H 7.734 0.000 1 14 12 12 VAL N N 121.689 0.000 1 15 13 13 ALA H H 8.106 0.000 1 16 13 13 ALA N N 126.879 0.000 1 17 14 14 GLY H H 8.166 0.000 1 18 14 14 GLY N N 107.877 0.000 1 19 15 15 SER H H 7.985 0.000 1 20 15 15 SER N N 115.262 0.000 1 21 16 16 TYR H H 8.161 0.000 1 22 16 16 TYR N N 121.691 0.000 1 23 17 17 GLY H H 8.212 0.000 1 24 17 17 GLY N N 110.115 0.000 1 25 18 18 ASN H H 8.164 0.000 1 26 18 18 ASN N N 118.279 0.000 1 27 19 19 ASP H H 8.358 0.000 1 28 19 19 ASP N N 120.057 0.000 1 29 20 20 GLN H H 8.163 0.000 1 30 20 20 GLN N N 119.545 0.000 1 31 21 21 TRP H H 7.960 0.000 1 32 21 21 TRP N N 120.578 0.000 1 33 22 22 LEU H H 7.799 0.000 1 34 22 22 LEU N N 122.720 0.000 1 35 23 23 GLN H H 8.105 0.000 1 36 23 23 GLN N N 120.873 0.000 1 37 24 24 VAL H H 7.985 0.000 1 38 24 24 VAL N N 120.735 0.000 1 39 25 25 ASP H H 8.362 0.000 1 40 25 25 ASP N N 123.545 0.000 1 41 26 26 LEU H H 8.306 0.000 1 42 26 26 LEU N N 123.930 0.000 1 43 27 27 GLY H H 8.483 0.000 1 44 27 27 GLY N N 108.888 0.000 1 45 28 28 SER H H 8.097 0.000 1 46 28 28 SER N N 115.382 0.000 1 47 29 29 SER H H 8.309 0.000 1 48 29 29 SER N N 117.591 0.000 1 49 30 30 LYS H H 8.295 0.000 1 50 30 30 LYS N N 122.851 0.000 1 51 31 31 GLU H H 8.331 0.000 1 52 31 31 GLU N N 121.308 0.000 1 53 32 32 VAL H H 8.178 0.000 1 54 32 32 VAL N N 120.899 0.000 1 55 33 33 THR H H 8.143 0.000 1 56 33 33 THR N N 116.904 0.000 1 57 34 34 GLY H H 8.323 0.000 1 58 34 34 GLY N N 110.815 0.000 1 59 35 35 ILE H H 7.914 0.000 1 60 35 35 ILE N N 119.970 0.000 1 61 36 36 ILE H H 8.236 0.000 1 62 36 36 ILE N N 124.928 0.000 1 63 37 37 THR H H 8.201 0.000 1 64 37 37 THR N N 118.618 0.000 1 65 38 38 GLN H H 8.359 0.000 1 66 38 38 GLN N N 122.656 0.000 1 67 39 39 GLY H H 8.387 0.000 1 68 39 39 GLY N N 110.087 0.000 1 69 40 40 ALA H H 8.104 0.000 1 70 40 40 ALA N N 123.643 0.000 1 71 41 41 ARG H H 8.246 0.000 1 72 41 41 ARG N N 119.709 0.000 1 73 42 42 ASN H H 8.280 0.000 1 74 42 42 ASN N N 119.304 0.000 1 75 43 43 PHE H H 8.220 0.000 1 76 43 43 PHE N N 120.967 0.000 1 77 44 44 GLY H H 8.328 0.000 1 78 44 44 GLY N N 110.212 0.000 1 79 45 45 SER H H 8.115 0.000 1 80 45 45 SER N N 115.650 0.000 1 81 46 46 VAL H H 8.088 0.000 1 82 46 46 VAL N N 121.285 0.000 1 83 47 47 GLN H H 8.297 0.000 1 84 47 47 GLN N N 123.534 0.000 1 85 48 48 PHE H H 8.207 0.000 1 86 48 48 PHE N N 122.054 0.000 1 87 49 49 VAL H H 7.990 0.000 1 88 49 49 VAL N N 123.814 0.000 1 stop_ save_