data_26881 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 15N assignment for LC3B ; _BMRB_accession_number 26881 _BMRB_flat_file_name bmr26881.str _Entry_type original _Submission_date 2016-08-26 _Accession_date 2016-08-26 _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 Varani Luca . . 2 Simonelli Luca . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 101 "15N chemical shifts" 101 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2017-02-16 original BMRB . stop_ _Original_release_date 2016-08-26 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Translocon component Sec62 acts in endoplasmic reticulum turnover during stress recovery ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 27749824 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Fumagalli Fiorenza . . 2 Noack Julia . . 3 Bergmann Timothy J. . 4 Cebollero Eduardo . . 5 Pisoni 'Giorgia Brambilla' B. . 6 Fasana Elisa . . 7 Fregno Ilaria . . 8 Galli Carmela . . 9 Loi Marisa . . 10 Solda Tatiana . . 11 D'Antuono Rocco . . 12 Raimondi Andrea . . 13 Jung Martin . . 14 Melnyk Armin . . 15 Schorr Stefan . . 16 Schreiber Anne . . 17 Simonelli Luca . . 18 Varani Luca . . 19 Wilson-Zbinden Caroline . . 20 Zerbe Oliver . . 21 Hofmann Kay . . 22 Peter Matthias . . 23 Quadroni Manfredo . . 24 Zimmermann Richard . . 25 Molinari Maurizio . . stop_ _Journal_abbreviation 'Nat. Cell Biol.' _Journal_volume 18 _Journal_issue 11 _Journal_ISSN 1476-4679 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1173 _Page_last 1184 _Year 2016 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'LC3B monomer' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'LC3B monomer' $Microtubule-associated_proteins_1A-1B_light_chain_3B 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_Microtubule-associated_proteins_1A-1B_light_chain_3B _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Microtubule-associated_proteins_1A/1B_light_chain_3B _Molecular_mass . _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 120 _Mol_residue_sequence ; MPSEKTFKQRRTFEQRVEDV RLIREQHPTKIPVIIERYKG EKQLPVLDKTKFLVPDHVNM SELIKIIRRRLQLNANQAFF LLVNGHSMVSVSTPISEVYE SEKDEDGFLYMVYASQETFG ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 1 MET 2 2 PRO 3 3 SER 4 4 GLU 5 5 LYS 6 6 THR 7 7 PHE 8 8 LYS 9 9 GLN 10 10 ARG 11 11 ARG 12 12 THR 13 13 PHE 14 14 GLU 15 15 GLN 16 16 ARG 17 17 VAL 18 18 GLU 19 19 ASP 20 20 VAL 21 21 ARG 22 22 LEU 23 23 ILE 24 24 ARG 25 25 GLU 26 26 GLN 27 27 HIS 28 28 PRO 29 29 THR 30 30 LYS 31 31 ILE 32 32 PRO 33 33 VAL 34 34 ILE 35 35 ILE 36 36 GLU 37 37 ARG 38 38 TYR 39 39 LYS 40 40 GLY 41 41 GLU 42 42 LYS 43 43 GLN 44 44 LEU 45 45 PRO 46 46 VAL 47 47 LEU 48 48 ASP 49 49 LYS 50 50 THR 51 51 LYS 52 52 PHE 53 53 LEU 54 54 VAL 55 55 PRO 56 56 ASP 57 57 HIS 58 58 VAL 59 59 ASN 60 60 MET 61 61 SER 62 62 GLU 63 63 LEU 64 64 ILE 65 65 LYS 66 66 ILE 67 67 ILE 68 68 ARG 69 69 ARG 70 70 ARG 71 71 LEU 72 72 GLN 73 73 LEU 74 74 ASN 75 75 ALA 76 76 ASN 77 77 GLN 78 78 ALA 79 79 PHE 80 80 PHE 81 81 LEU 82 82 LEU 83 83 VAL 84 84 ASN 85 85 GLY 86 86 HIS 87 87 SER 88 88 MET 89 89 VAL 90 90 SER 91 91 VAL 92 92 SER 93 93 THR 94 94 PRO 95 95 ILE 96 96 SER 97 97 GLU 98 98 VAL 99 99 TYR 100 100 GLU 101 101 SER 102 102 GLU 103 103 LYS 104 104 ASP 105 105 GLU 106 106 ASP 107 107 GLY 108 108 PHE 109 109 LEU 110 110 TYR 111 111 MET 112 112 VAL 113 113 TYR 114 114 ALA 115 115 SER 116 116 GLN 117 117 GLU 118 118 THR 119 119 PHE 120 120 GLY stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $Microtubule-associated_proteins_1A-1B_light_chain_3B 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 $Microtubule-associated_proteins_1A-1B_light_chain_3B 'recombinant technology' . Escherichia coli . pGEX6P1 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 $Microtubule-associated_proteins_1A-1B_light_chain_3B 500 uM '[U-100% 15N]' 'sodium phosphate' 20 mM 'natural abundance' 'sodium chloride' 20 mM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'chemical shift assignment' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 700 _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 pH 6.8 . 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 DSS H 1 'methyl protons' ppm 0.00 internal direct . . . 1.000000000 DSS N 15 'methyl protons' ppm 0.00 na 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 'LC3B monomer' _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 3 3 SER H H 8.366 . 1 2 3 3 SER N N 115.6 . 1 3 5 5 LYS H H 8.28 . 1 4 5 5 LYS N N 122.3 . 1 5 6 6 THR H H 8.411 . 1 6 6 6 THR N N 114.8 . 1 7 7 7 PHE H H 10.27 . 1 8 7 7 PHE N N 125 . 1 9 8 8 LYS H H 8.701 . 1 10 8 8 LYS N N 114.3 . 1 11 9 9 GLN H H 7.361 . 1 12 9 9 GLN N N 113.3 . 1 13 10 10 ARG H H 7.856 . 1 14 10 10 ARG N N 118.2 . 1 15 11 11 ARG H H 7.333 . 1 16 11 11 ARG N N 120.2 . 1 17 12 12 THR H H 8.768 . 1 18 12 12 THR N N 115.9 . 1 19 13 13 PHE H H 9.202 . 1 20 13 13 PHE N N 122.9 . 1 21 14 14 GLU H H 8.968 . 1 22 14 14 GLU N N 115.4 . 1 23 15 15 GLN H H 7.634 . 1 24 15 15 GLN N N 118.8 . 1 25 16 16 ARG H H 8.634 . 1 26 16 16 ARG N N 121.4 . 1 27 17 17 VAL H H 8.377 . 1 28 17 17 VAL N N 118.3 . 1 29 18 18 GLU H H 7.383 . 1 30 18 18 GLU N N 120.3 . 1 31 19 19 ASP H H 8.574 . 1 32 19 19 ASP N N 121.3 . 1 33 20 20 VAL H H 7.986 . 1 34 20 20 VAL N N 119.7 . 1 35 21 21 ARG H H 8.037 . 1 36 21 21 ARG N N 121.4 . 1 37 22 22 LEU H H 8.248 . 1 38 22 22 LEU N N 119.7 . 1 39 23 23 ILE H H 8.204 . 1 40 23 23 ILE N N 121.7 . 1 41 24 24 ARG H H 8.637 . 1 42 24 24 ARG N N 118.5 . 1 43 25 25 GLU H H 7.51 . 1 44 25 25 GLU N N 116.6 . 1 45 26 26 GLN H H 7.855 . 1 46 26 26 GLN N N 116 . 1 47 27 27 HIS H H 8.7 . 1 48 27 27 HIS N N 117.2 . 1 49 30 30 LYS H H 7.425 . 1 50 30 30 LYS N N 117.4 . 1 51 31 31 ILE H H 9.347 . 1 52 31 31 ILE N N 122.7 . 1 53 33 33 VAL H H 8.921 . 1 54 33 33 VAL N N 126.2 . 1 55 34 34 ILE H H 8.785 . 1 56 34 34 ILE N N 128.2 . 1 57 35 35 ILE H H 8.794 . 1 58 35 35 ILE N N 125.3 . 1 59 37 37 ARG H H 8.839 . 1 60 37 37 ARG N N 123 . 1 61 38 38 TYR H H 8.595 . 1 62 38 38 TYR N N 128.6 . 1 63 39 39 LYS H H 8.495 . 1 64 39 39 LYS N N 130.1 . 1 65 41 41 GLU H H 7.489 . 1 66 41 41 GLU N N 122.7 . 1 67 43 43 GLN H H 8.361 . 1 68 43 43 GLN N N 119.3 . 1 69 44 44 LEU H H 9.055 . 1 70 44 44 LEU N N 120.6 . 1 71 46 46 VAL H H 8.441 . 1 72 46 46 VAL N N 118.6 . 1 73 47 47 LEU H H 7.846 . 1 74 47 47 LEU N N 128.5 . 1 75 48 48 ASP H H 8.574 . 1 76 48 48 ASP N N 121.9 . 1 77 49 49 LYS H H 7.219 . 1 78 49 49 LYS N N 118.9 . 1 79 51 51 LYS H H 7.376 . 1 80 51 51 LYS N N 121 . 1 81 52 52 PHE H H 9.745 . 1 82 52 52 PHE N N 126.6 . 1 83 53 53 LEU H H 8.54 . 1 84 53 53 LEU N N 122.3 . 1 85 54 54 VAL H H 8.802 . 1 86 54 54 VAL N N 126.7 . 1 87 56 56 ASP H H 8.437 . 1 88 56 56 ASP N N 119.5 . 1 89 57 57 HIS H H 7.406 . 1 90 57 57 HIS N N 114 . 1 91 58 58 VAL H H 7.079 . 1 92 58 58 VAL N N 117.4 . 1 93 60 60 MET H H 8.168 . 1 94 60 60 MET N N 118.4 . 1 95 61 61 SER H H 8.506 . 1 96 61 61 SER N N 114.2 . 1 97 62 62 GLU H H 7.9 . 1 98 62 62 GLU N N 122.6 . 1 99 63 63 LEU H H 7.584 . 1 100 63 63 LEU N N 120.4 . 1 101 64 64 ILE H H 8.351 . 1 102 64 64 ILE N N 118.6 . 1 103 65 65 LYS H H 7.412 . 1 104 65 65 LYS N N 118.2 . 1 105 66 66 ILE H H 7.956 . 1 106 66 66 ILE N N 120.6 . 1 107 67 67 ILE H H 8.031 . 1 108 67 67 ILE N N 120.1 . 1 109 68 68 ARG H H 8.479 . 1 110 68 68 ARG N N 118.7 . 1 111 69 69 ARG H H 7.605 . 1 112 69 69 ARG N N 116.2 . 1 113 70 70 ARG H H 8.028 . 1 114 70 70 ARG N N 122.4 . 1 115 71 71 LEU H H 7.765 . 1 116 71 71 LEU N N 116.5 . 1 117 72 72 GLN H H 7.674 . 1 118 72 72 GLN N N 114.5 . 1 119 73 73 LEU H H 7.482 . 1 120 73 73 LEU N N 115.1 . 1 121 74 74 ASN H H 8.922 . 1 122 74 74 ASN N N 121.3 . 1 123 75 75 ALA H H 8.718 . 1 124 75 75 ALA N N 123 . 1 125 76 76 ASN H H 8.32 . 1 126 76 76 ASN N N 112.1 . 1 127 77 77 GLN H H 7.487 . 1 128 77 77 GLN N N 120 . 1 129 78 78 ALA H H 8.674 . 1 130 78 78 ALA N N 130 . 1 131 79 79 PHE H H 7.562 . 1 132 79 79 PHE N N 118.6 . 1 133 80 80 PHE H H 8.461 . 1 134 80 80 PHE N N 125.2 . 1 135 81 81 LEU H H 8.298 . 1 136 81 81 LEU N N 121 . 1 137 82 82 LEU H H 9.1 . 1 138 82 82 LEU N N 123.8 . 1 139 83 83 VAL H H 9.129 . 1 140 83 83 VAL N N 125.5 . 1 141 84 84 ASN H H 9.631 . 1 142 84 84 ASN N N 125.2 . 1 143 86 86 HIS H H 7.822 . 1 144 86 86 HIS N N 116.8 . 1 145 87 87 SER H H 8.606 . 1 146 87 87 SER N N 117.4 . 1 147 88 88 MET H H 9.096 . 1 148 88 88 MET N N 125.6 . 1 149 89 89 VAL H H 8.416 . 1 150 89 89 VAL N N 121 . 1 151 90 90 SER H H 8.488 . 1 152 90 90 SER N N 118.3 . 1 153 93 93 THR H H 7.492 . 1 154 93 93 THR N N 120.2 . 1 155 95 95 ILE H H 9.249 . 1 156 95 95 ILE N N 125 . 1 157 96 96 SER H H 8.652 . 1 158 96 96 SER N N 116.8 . 1 159 97 97 GLU H H 7.19 . 1 160 97 97 GLU N N 122.7 . 1 161 98 98 VAL H H 7.468 . 1 162 98 98 VAL N N 120.5 . 1 163 99 99 TYR H H 8.923 . 1 164 99 99 TYR N N 118.7 . 1 165 100 100 GLU H H 7.482 . 1 166 100 100 GLU N N 113.8 . 1 167 101 101 SER H H 7.4 . 1 168 101 101 SER N N 108.7 . 1 169 102 102 GLU H H 8.412 . 1 170 102 102 GLU N N 116.3 . 1 171 103 103 LYS H H 7.723 . 1 172 103 103 LYS N N 118.2 . 1 173 104 104 ASP H H 8.995 . 1 174 104 104 ASP N N 123.3 . 1 175 105 105 GLU H H 8.832 . 1 176 105 105 GLU N N 125 . 1 177 106 106 ASP H H 9.896 . 1 178 106 106 ASP N N 118.5 . 1 179 107 107 GLY H H 7.946 . 1 180 107 107 GLY N N 105.7 . 1 181 108 108 PHE H H 9.769 . 1 182 108 108 PHE N N 123.6 . 1 183 109 109 LEU H H 7.957 . 1 184 109 109 LEU N N 119.3 . 1 185 110 110 TYR H H 9.436 . 1 186 110 110 TYR N N 126.5 . 1 187 111 111 MET H H 9.511 . 1 188 111 111 MET N N 118.5 . 1 189 112 112 VAL H H 8.676 . 1 190 112 112 VAL N N 118.4 . 1 191 113 113 TYR H H 8.266 . 1 192 113 113 TYR N N 119.3 . 1 193 115 115 SER H H 9.709 . 1 194 115 115 SER N N 114.3 . 1 195 116 116 GLN H H 7.280 . 1 196 116 116 GLN N N 117.4 . 1 197 117 117 GLU H H 7.961 . 1 198 117 117 GLU N N 118.2 . 1 199 118 118 THR H H 7.160 . 1 200 118 118 THR N N 110.8 . 1 201 120 120 GLY H H 7.884 . 1 202 120 120 GLY N N 116 . 1 stop_ save_