data_50265 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; NMR backbone resonance assignment of TREM2 transmembrane helix in complex with the partner protein DAP12 ; _BMRB_accession_number 50265 _BMRB_flat_file_name bmr50265.str _Entry_type original _Submission_date 2020-05-08 _Accession_date 2020-05-08 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details '300 mM DPC' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Steiner Andrea . . 2 Hagn Franz X. . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 34 "13C chemical shifts" 91 "15N chemical shifts" 34 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2020-10-16 update BMRB 'update entry citation' 2020-06-08 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 50263 'transmembrane helix of TREM2' 50264 'TREM2 transmembrane helix K186A variant' stop_ _Original_release_date 2020-05-08 save_ ############################# # Citation for this entry # ############################# save_citations_1 _Saveframe_category entry_citation _Citation_full . _Citation_title ; gamma-Secretase cleavage of the Alzheimer risk factor TREM2 is determined by its intrinsic structural dynamics ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 32830336 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Steiner Andrea . . 2 Schlepckow Kai . . 3 Brunner Bettina . . 4 Steiner Harald . . 5 Haass Christian . . 6 Hagn Franz X. . stop_ _Journal_abbreviation 'EMBO J.' _Journal_volume 39 _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first e104247 _Page_last e104247 _Year 2020 _Details . loop_ _Keyword NMR TREM2 dynamics 'intramembrane protease' structure stop_ save_ ################################## # Molecular system description # ################################## save_assembly_1 _Saveframe_category molecular_system _Mol_system_name 'TREM2 TMH wt + DAP12' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label TREM2 $entity_1 DAP12 $entity_2 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 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 49 _Mol_residue_sequence ; GSGRSLLEGEIPFPPTSILL LLACIFLIKILAASALWAAA WHGQKPGTH ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -2 GLY 2 -1 SER 3 0 GLY 4 1 ARG 5 2 SER 6 3 LEU 7 4 LEU 8 5 GLU 9 6 GLY 10 7 GLU 11 8 ILE 12 9 PRO 13 10 PHE 14 11 PRO 15 12 PRO 16 13 THR 17 14 SER 18 15 ILE 19 16 LEU 20 17 LEU 21 18 LEU 22 19 LEU 23 20 ALA 24 21 CYS 25 22 ILE 26 23 PHE 27 24 LEU 28 25 ILE 29 26 LYS 30 27 ILE 31 28 LEU 32 29 ALA 33 30 ALA 34 31 SER 35 32 ALA 36 33 LEU 37 34 TRP 38 35 ALA 39 36 ALA 40 37 ALA 41 38 TRP 42 39 HIS 43 40 GLY 44 41 GLN 45 42 LYS 46 43 PRO 47 44 GLY 48 45 THR 49 46 HIS 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 Q9NZC2 TREM2 . . . . . stop_ save_ save_entity_2 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common entity_2 _Molecular_mass . _Mol_thiol_state 'not present' _Details 'Engineered Mutation: C33S' _Residue_count 50 _Mol_residue_sequence ; GLRPVQAQAQSDSSCSTVSP GVLAGIVMGDLVLTVLIALA VYFLGRLVPR ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 21 GLY 2 22 LEU 3 23 ARG 4 24 PRO 5 25 VAL 6 26 GLN 7 27 ALA 8 28 GLN 9 29 ALA 10 30 GLN 11 31 SER 12 32 ASP 13 33 SER 14 34 SER 15 35 CYS 16 36 SER 17 37 THR 18 38 VAL 19 39 SER 20 40 PRO 21 41 GLY 22 42 VAL 23 43 LEU 24 44 ALA 25 45 GLY 26 46 ILE 27 47 VAL 28 48 MET 29 49 GLY 30 50 ASP 31 51 LEU 32 52 VAL 33 53 LEU 34 54 THR 35 55 VAL 36 56 LEU 37 57 ILE 38 58 ALA 39 59 LEU 40 60 ALA 41 61 VAL 42 62 TYR 43 63 PHE 44 64 LEU 45 65 GLY 46 66 ARG 47 67 LEU 48 68 VAL 49 69 PRO 50 70 ARG 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 UniProt O43914 . . . . . . stop_ 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 pET15b stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_sample_1 _Saveframe_category sample _Sample_type solution _Details ; 500 uM TREM2-TMH wt + unlabelled DAP12 in 300mM DPC 20 mM NaPi pH7.0 50 mM NaCl 0.5 mM EDTA 5 mM DTT ; loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $entity_1 500 uM '[U-13C; U-15N; U-2H]' $entity_2 1000 uM 'natural abundance' DPC 300 mM 'natural abundance' NaPi 20 mM 'natural abundance' NaCl 50 mM 'natural abundance' EDTA 0.5 mM 'natural abundance' DTT 5 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_software_1 _Saveframe_category software _Name TOPSPIN _Version 3.5 loop_ _Task collection stop_ _Details . save_ save_software_2 _Saveframe_category software _Name NMRFAM-SPARKY _Version . loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_NMR_spectrometer_1 _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_ save_3D_HNCO_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HNCA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNCACB_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_HN(CO)CA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HN(CO)CA' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N 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' 0.1 . M pH 7 . pH pressure 1 . atm temperature 310 . 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 C 13 'methyl protons' ppm 0 external indirect . . . . DSS H 1 'methyl protons' ppm 0 external direct . . . 1 DSS N 15 'methyl protons' ppm 0 external indirect . . . . 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_ _Software_label $software_1 $software_2 stop_ loop_ _Experiment_label '2D 1H-15N HSQC' '3D HNCO' '3D HNCA' '3D HNCACB' '3D HN(CO)CA' '3D 1H-15N 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 TREM2 _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 4 ARG C C 175.3 0.05 1 2 2 5 SER H H 8.32 0.02 1 3 2 5 SER C C 174.3 0.05 1 4 2 5 SER CA C 56.39 0.05 1 5 2 5 SER CB C 65.4 0.05 1 6 2 5 SER N N 118.46 0.05 1 7 3 6 LEU H H 8.7 0.02 1 8 3 6 LEU C C 176.3 0.05 1 9 3 6 LEU CA C 55.08 0.05 1 10 3 6 LEU CB C 43.68 0.05 1 11 3 6 LEU N N 126.88 0.05 1 12 4 7 LEU H H 7.98 0.02 1 13 4 7 LEU C C 175.6 0.05 1 14 4 7 LEU CA C 52.92 0.05 1 15 4 7 LEU CB C 43.03 0.05 1 16 4 7 LEU N N 118.19 0.05 1 17 5 8 GLU H H 7.72 0.02 1 18 5 8 GLU C C 175.5 0.05 1 19 5 8 GLU CA C 54.33 0.05 1 20 5 8 GLU CB C 31.8 0.05 1 21 5 8 GLU N N 119.87 0.05 1 22 6 9 GLY H H 7.96 0.02 1 23 6 9 GLY C C 172.0 0.05 1 24 6 9 GLY CA C 42.89 0.05 1 25 6 9 GLY N N 110.34 0.05 1 26 7 10 GLU H H 8.03 0.02 1 27 7 10 GLU C C 174.7 0.05 1 28 7 10 GLU CA C 53.77 0.05 1 29 7 10 GLU CB C 31.56 0.05 1 30 7 10 GLU N N 121.8 0.05 1 31 8 11 ILE H H 8.17 0.02 1 32 8 11 ILE CA C 55.96 0.05 1 33 8 11 ILE CB C 40.09 0.05 1 34 8 11 ILE N N 124.97 0.05 1 35 9 12 PRO CA C 61.88 0.05 1 36 9 12 PRO CB C 33.77 0.05 1 37 10 13 PHE H H 7.68 0.02 1 38 10 13 PHE C C 178.2 0.05 1 39 10 13 PHE CA C 61.84 0.05 1 40 10 13 PHE N N 120.42 0.05 1 41 14 17 SER C C 174.4 0.05 1 42 15 18 ILE H H 7.24 0.02 1 43 15 18 ILE C C 175.9 0.05 1 44 15 18 ILE CA C 61.23 0.05 1 45 15 18 ILE CB C 38.15 0.05 1 46 15 18 ILE N N 122.12 0.05 1 47 16 19 LEU H H 7.69 0.02 1 48 16 19 LEU C C 177.0 0.05 1 49 16 19 LEU CA C 56.02 0.05 1 50 16 19 LEU CB C 42.62 0.05 1 51 16 19 LEU N N 121.22 0.05 1 52 17 20 LEU H H 8.13 0.02 1 53 17 20 LEU C C 177.4 0.05 1 54 17 20 LEU CA C 55.87 0.05 1 55 17 20 LEU CB C 42.68 0.05 1 56 17 20 LEU N N 119.32 0.05 1 57 18 21 LEU H H 7.71 0.02 1 58 18 21 LEU C C 177.2 0.05 1 59 18 21 LEU CA C 56.5 0.05 1 60 18 21 LEU CB C 42.79 0.05 1 61 18 21 LEU N N 121.74 0.05 1 62 19 22 LEU H H 8.22 0.02 1 63 19 22 LEU C C 177.7 0.05 1 64 19 22 LEU CA C 55.91 0.05 1 65 19 22 LEU CB C 42.62 0.05 1 66 19 22 LEU N N 119.47 0.05 1 67 20 23 ALA H H 8.41 0.02 1 68 20 23 ALA C C 177.6 0.05 1 69 20 23 ALA CA C 53.19 0.05 1 70 20 23 ALA CB C 19.33 0.05 1 71 20 23 ALA N N 123.04 0.05 1 72 21 24 CYS H H 8.17 0.02 1 73 21 24 CYS C C 175.3 0.05 1 74 21 24 CYS CA C 62.07 0.05 1 75 21 24 CYS CB C 28.45 0.05 1 76 21 24 CYS N N 117.18 0.05 1 77 22 25 ILE H H 8.12 0.02 1 78 22 25 ILE CA C 63.35 0.05 1 79 22 25 ILE CB C 38.56 0.05 1 80 22 25 ILE N N 120.49 0.05 1 81 24 27 LEU H H 7.93 0.02 1 82 24 27 LEU C C 174.3 0.05 1 83 24 27 LEU CA C 53.46 0.05 1 84 24 27 LEU CB C 43.89 0.05 1 85 24 27 LEU N N 121.73 0.05 1 86 25 28 ILE H H 8.14 0.02 1 87 25 28 ILE C C 176.2 0.05 1 88 25 28 ILE CA C 63.29 0.05 1 89 25 28 ILE CB C 38.09 0.05 1 90 25 28 ILE N N 120.02 0.05 1 91 26 29 LYS H H 8.13 0.02 1 92 26 29 LYS C C 177.1 0.05 1 93 26 29 LYS CA C 58.87 0.05 1 94 26 29 LYS N N 121.24 0.05 1 95 27 30 ILE H H 7.93 0.02 1 96 27 30 ILE C C 177.8 0.05 1 97 27 30 ILE CA C 62.06 0.05 1 98 27 30 ILE CB C 37.91 0.05 1 99 27 30 ILE N N 119.68 0.05 1 100 28 31 LEU H H 8.37 0.02 1 101 28 31 LEU C C 177.6 0.05 1 102 28 31 LEU CA C 56.02 0.05 1 103 28 31 LEU CB C 42.68 0.05 1 104 28 31 LEU N N 124.59 0.05 1 105 29 32 ALA H H 8.78 0.02 1 106 29 32 ALA C C 177.7 0.05 1 107 29 32 ALA CA C 53.17 0.05 1 108 29 32 ALA CB C 19.27 0.05 1 109 29 32 ALA N N 123.25 0.05 1 110 30 33 ALA H H 8.62 0.02 1 111 30 33 ALA C C 178.1 0.05 1 112 30 33 ALA CA C 53.23 0.05 1 113 30 33 ALA CB C 18.88 0.05 1 114 30 33 ALA N N 120.68 0.05 1 115 31 34 SER H H 8.27 0.02 1 116 31 34 SER C C 176.6 0.05 1 117 31 34 SER CA C 60.59 0.05 1 118 31 34 SER N N 115.25 0.05 1 119 32 35 ALA H H 8.3 0.02 1 120 32 35 ALA C C 178.4 0.05 1 121 32 35 ALA CA C 52.61 0.05 1 122 32 35 ALA N N 121.0 0.05 1 123 33 36 LEU H H 8.25 0.02 1 124 33 36 LEU C C 177.1 0.05 1 125 33 36 LEU CA C 55.83 0.05 1 126 33 36 LEU CB C 43.2 0.05 1 127 33 36 LEU N N 120.47 0.05 1 128 34 37 TRP H H 8.57 0.02 1 129 34 37 TRP C C 175.0 0.05 1 130 34 37 TRP CA C 58.55 0.05 1 131 34 37 TRP CB C 30.55 0.05 1 132 34 37 TRP N N 121.74 0.05 1 133 35 38 ALA H H 8.17 0.02 1 134 35 38 ALA C C 176.6 0.05 1 135 35 38 ALA CA C 52.78 0.05 1 136 35 38 ALA N N 126.46 0.05 1 137 36 39 ALA H H 8.29 0.02 1 138 36 39 ALA C C 177.5 0.05 1 139 36 39 ALA CA C 52.21 0.05 1 140 36 39 ALA N N 125.76 0.05 1 141 37 40 ALA H H 8.11 0.02 1 142 37 40 ALA C C 176.7 0.05 1 143 37 40 ALA CA C 51.66 0.05 1 144 37 40 ALA CB C 20.0 0.05 1 145 37 40 ALA N N 120.64 0.05 1 146 38 41 TRP H H 7.81 0.02 1 147 38 41 TRP CA C 56.08 0.05 1 148 38 41 TRP N N 118.32 0.05 1 149 39 42 HIS H H 7.76 0.02 1 150 39 42 HIS C C 174.0 0.05 1 151 39 42 HIS N N 120.17 0.05 1 152 40 43 GLY H H 7.9 0.02 1 153 40 43 GLY N N 111.97 0.05 1 154 45 48 THR C C 172.4 0.05 1 155 45 48 THR CA C 59.72 0.05 1 156 45 48 THR CB C 71.56 0.05 1 157 46 49 HIS H H 7.85 0.02 1 158 46 49 HIS CA C 55.54 0.05 1 159 46 49 HIS N N 128.43 0.05 1 stop_ save_