data_27109 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution-state NMR assignment of the flexible C-terminal domain of the human eye lens molecular chaperone alphaA-crystallin ; _BMRB_accession_number 27109 _BMRB_flat_file_name bmr27109.str _Entry_type original _Submission_date 2017-05-18 _Accession_date 2017-05-18 _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 Stavropoulou Maria . . 2 Asami Sam . . 3 Kaiser Christoph . . 4 Haslbeck Martin . . 5 Buchner Johannes . . 6 Weinkauf Sevil . . 7 Reif Bernd . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 87 "13C chemical shifts" 81 "15N chemical shifts" 22 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2020-03-04 update BMRB 'update entry citation' 2019-10-04 original author 'original release' stop_ _Original_release_date 2017-05-19 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; The structure and oxidation of the eye lens chaperone alphaA-crystallin ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 31792453 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kaiser Christoph J.O. . 2 Peters Carsten . . 3 Schmid Philipp W.N. . 4 Stavropoulou Maria . . 5 Zou Juan . . 6 Dahiya Vinay . . 7 Mymrikov Evgeny V. . 8 Rockel Beate . . 9 Asami Sam . . 10 Haslbeck Martin . . 11 Rappsilber Juri . . 12 Reif Bernd . . 13 Zacharias Martin . . 14 Buchner Johannes . . 15 Weinkauf Sevil . . stop_ _Journal_abbreviation 'Nat. Struct. Mol. Biol.' _Journal_name_full 'Nature structural & molecular biology' _Journal_volume 26 _Journal_issue 12 _Journal_ISSN 1545-9985 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 1141 _Page_last 1150 _Year 2019 _Details . loop_ _Keyword 'NMR assignment' alphaA-crystallin 'human eye lens' 'molecular chaperone' 'small heat shock proteins' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'alphaA-crystallin (or HSPB1)' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'alphaA-crystallin (or HSPB1)' $alphaA-crystallin_or_HspB1 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_alphaA-crystallin_or_HspB1 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common alphaA-crystallin_or_HspB1 _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 173 _Mol_residue_sequence ; MDVTIQHPWFKRTLGPFYPS RLFDQFFGEGLFEYDLLPFL SSTISPYYRQSLFRTVLDSG ISEVRSDRDKFVIFLDVKHF SPEDLTVKVQDDFVEIHGKH NERQDDHGYISREFHRRYRL PSNVDQSALSCSLSADGMLT FCGPKIQTGLDATHAERAIP VSREEKPTSAPSS ; loop_ _Residue_seq_code _Residue_label 1 MET 2 ASP 3 VAL 4 THR 5 ILE 6 GLN 7 HIS 8 PRO 9 TRP 10 PHE 11 LYS 12 ARG 13 THR 14 LEU 15 GLY 16 PRO 17 PHE 18 TYR 19 PRO 20 SER 21 ARG 22 LEU 23 PHE 24 ASP 25 GLN 26 PHE 27 PHE 28 GLY 29 GLU 30 GLY 31 LEU 32 PHE 33 GLU 34 TYR 35 ASP 36 LEU 37 LEU 38 PRO 39 PHE 40 LEU 41 SER 42 SER 43 THR 44 ILE 45 SER 46 PRO 47 TYR 48 TYR 49 ARG 50 GLN 51 SER 52 LEU 53 PHE 54 ARG 55 THR 56 VAL 57 LEU 58 ASP 59 SER 60 GLY 61 ILE 62 SER 63 GLU 64 VAL 65 ARG 66 SER 67 ASP 68 ARG 69 ASP 70 LYS 71 PHE 72 VAL 73 ILE 74 PHE 75 LEU 76 ASP 77 VAL 78 LYS 79 HIS 80 PHE 81 SER 82 PRO 83 GLU 84 ASP 85 LEU 86 THR 87 VAL 88 LYS 89 VAL 90 GLN 91 ASP 92 ASP 93 PHE 94 VAL 95 GLU 96 ILE 97 HIS 98 GLY 99 LYS 100 HIS 101 ASN 102 GLU 103 ARG 104 GLN 105 ASP 106 ASP 107 HIS 108 GLY 109 TYR 110 ILE 111 SER 112 ARG 113 GLU 114 PHE 115 HIS 116 ARG 117 ARG 118 TYR 119 ARG 120 LEU 121 PRO 122 SER 123 ASN 124 VAL 125 ASP 126 GLN 127 SER 128 ALA 129 LEU 130 SER 131 CYS 132 SER 133 LEU 134 SER 135 ALA 136 ASP 137 GLY 138 MET 139 LEU 140 THR 141 PHE 142 CYS 143 GLY 144 PRO 145 LYS 146 ILE 147 GLN 148 THR 149 GLY 150 LEU 151 ASP 152 ALA 153 THR 154 HIS 155 ALA 156 GLU 157 ARG 158 ALA 159 ILE 160 PRO 161 VAL 162 SER 163 ARG 164 GLU 165 GLU 166 LYS 167 PRO 168 THR 169 SER 170 ALA 171 PRO 172 SER 173 SER 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 $alphaA-crystallin_or_HspB1 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 $alphaA-crystallin_or_HspB1 'recombinant technology' . Escherichia coli . pET28b+ 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 $alphaA-crystallin_or_HspB1 3 mM '[U-100% 13C; U-100% 15N]' HEPES 10 mM 'natural abundance' EDTA 1 mM 'natural abundance' DTT 2 mM 'natural abundance' 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_NMR-STAR _Saveframe_category software _Name NMR-STAR _Version . loop_ _Vendor _Address _Electronic_address CCPN . . stop_ loop_ _Task 'chemical shift assignment' 'peak picking' stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 950 _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_2D_1H-13C_HSQC_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC' _Sample_label $sample_1 save_ save_3D_CBCA(CO)NH_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D CBCA(CO)NH' _Sample_label $sample_1 save_ save_3D_HNCO_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCO' _Sample_label $sample_1 save_ save_3D_HNCA_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCA' _Sample_label $sample_1 save_ save_3D_HNCACB_6 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACB' _Sample_label $sample_1 save_ save_3D_1H-15N_NOESY_7 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_1 save_ save_3D_H(CCO)NH_8 _Saveframe_category NMR_applied_experiment _Experiment_name '3D H(CCO)NH' _Sample_label $sample_1 save_ save_3D_HNCACO_9 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNCACO' _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 7.4 . pH pressure 1 . atm temperature 300 . 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 -0.075 internal direct . . . 1.000000000 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' '2D 1H-13C HSQC' '3D CBCA(CO)NH' '3D HNCO' '3D HNCA' '3D HNCACB' '3D 1H-15N NOESY' '3D H(CCO)NH' '3D HNCACO' 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 'alphaA-crystallin (or HSPB1)' _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 1 149 149 GLY H H 8.423 0.000 1 2 149 149 GLY HA2 H 3.900 0.000 1 3 149 149 GLY C C 171.590 0.000 1 4 149 149 GLY CA C 42.795 0.000 1 5 149 149 GLY N N 110.798 0.000 1 6 150 150 LEU H H 8.070 0.000 1 7 150 150 LEU HA H 4.255 0.000 1 8 150 150 LEU HB2 H 1.538 0.000 2 9 150 150 LEU HB3 H 1.487 0.000 2 10 150 150 LEU HG H 1.098 0.000 1 11 150 150 LEU HD1 H 0.758 0.000 2 12 150 150 LEU HD2 H 0.811 0.000 2 13 150 150 LEU C C 174.522 0.000 1 14 150 150 LEU CA C 52.599 0.000 1 15 150 150 LEU CB C 39.704 0.004 1 16 150 150 LEU CG C 24.297 0.000 1 17 150 150 LEU CD1 C 20.669 0.000 2 18 150 150 LEU CD2 C 22.249 0.000 2 19 150 150 LEU N N 121.530 0.000 1 20 151 151 ASP H H 8.296 0.000 1 21 151 151 ASP HA H 4.483 0.000 1 22 151 151 ASP HB2 H 2.598 0.023 1 23 151 151 ASP C C 173.546 0.000 1 24 151 151 ASP CA C 51.543 0.000 1 25 151 151 ASP CB C 38.423 0.003 1 26 151 151 ASP N N 120.728 0.000 1 27 152 152 ALA H H 8.188 0.000 1 28 152 152 ALA HA H 4.237 0.000 1 29 152 152 ALA HB H 1.309 0.000 1 30 152 152 ALA C C 175.518 0.000 1 31 152 152 ALA CA C 50.277 0.000 1 32 152 152 ALA CB C 16.460 0.000 1 33 152 152 ALA N N 124.490 0.000 1 34 153 153 THR H H 8.079 0.000 1 35 153 153 THR HA H 4.139 0.000 1 36 153 153 THR HB H 4.100 0.000 1 37 153 153 THR HG2 H 1.083 0.000 1 38 153 153 THR C C 172.113 0.000 1 39 153 153 THR CA C 59.949 0.000 1 40 153 153 THR CB C 66.932 0.000 1 41 153 153 THR CG2 C 18.935 0.000 1 42 153 153 THR N N 112.134 0.000 1 43 154 154 HIS H H 8.090 0.000 1 44 154 154 HIS HA H 4.516 0.000 1 45 154 154 HIS HB2 H 3.120 0.000 2 46 154 154 HIS HB3 H 3.004 0.000 2 47 154 154 HIS C C 172.373 0.000 1 48 154 154 HIS CA C 53.653 0.000 1 49 154 154 HIS CB C 27.500 0.000 1 50 154 154 HIS N N 120.933 0.000 1 51 155 155 ALA H H 8.059 0.000 1 52 155 155 ALA HA H 4.196 0.000 1 53 155 155 ALA HB H 1.291 0.000 1 54 155 155 ALA C C 175.079 0.000 1 55 155 155 ALA CA C 50.111 0.000 1 56 155 155 ALA CB C 16.570 0.000 1 57 155 155 ALA N N 124.629 0.000 1 58 156 156 GLU H H 8.365 0.000 1 59 156 156 GLU HA H 4.163 0.000 1 60 156 156 GLU HB2 H 1.887 0.000 1 61 156 156 GLU HG2 H 2.209 0.000 1 62 156 156 GLU C C 173.841 0.000 1 63 156 156 GLU CA C 54.041 0.000 1 64 156 156 GLU CB C 27.404 0.000 1 65 156 156 GLU CG C 33.497 0.000 1 66 156 156 GLU N N 119.921 0.000 1 67 157 157 ARG H H 8.139 0.000 1 68 157 157 ARG HA H 4.239 0.000 1 69 157 157 ARG HB2 H 1.793 0.000 1 70 157 157 ARG HG2 H 1.547 0.000 1 71 157 157 ARG HD2 H 3.116 0.000 1 72 157 157 ARG C C 173.007 0.000 1 73 157 157 ARG CA C 53.207 0.000 1 74 157 157 ARG CB C 28.202 0.000 1 75 157 157 ARG CG C 24.373 0.000 1 76 157 157 ARG CD C 40.664 0.000 1 77 157 157 ARG N N 121.609 0.000 1 78 158 158 ALA H H 8.162 0.000 1 79 158 158 ALA HA H 4.247 0.000 1 80 158 158 ALA HB H 1.269 0.000 1 81 158 158 ALA C C 174.558 0.000 1 82 158 158 ALA CA C 49.533 0.000 1 83 158 158 ALA CB C 16.508 0.000 1 84 158 158 ALA N N 125.276 0.000 1 85 159 159 ILE H H 8.047 0.000 1 86 159 159 ILE HA H 4.355 0.000 1 87 159 159 ILE HB H 1.773 0.000 1 88 159 159 ILE HG12 H 0.808 0.000 1 89 159 159 ILE HG2 H 0.874 0.000 1 90 159 159 ILE HD1 H 0.785 0.000 1 91 159 159 ILE C C 171.948 0.000 1 92 159 159 ILE CA C 55.893 0.000 1 93 159 159 ILE CB C 35.935 0.000 1 94 159 159 ILE CG1 C 14.735 0.000 1 95 159 159 ILE CG2 C 14.312 0.000 1 96 159 159 ILE CD1 C 10.018 0.000 1 97 159 159 ILE N N 122.171 0.000 1 98 161 161 VAL H H 8.150 0.000 1 99 161 161 VAL HA H 4.023 0.000 1 100 161 161 VAL HB H 1.979 0.000 1 101 161 161 VAL HG1 H 0.892 0.000 2 102 161 161 VAL HG2 H 0.876 0.000 2 103 161 161 VAL C C 173.586 0.000 1 104 161 161 VAL CA C 59.566 0.000 1 105 161 161 VAL CB C 30.181 0.000 1 106 161 161 VAL N N 120.523 0.000 1 107 162 162 SER H H 8.320 0.000 1 108 162 162 SER HA H 4.397 0.000 1 109 162 162 SER HB2 H 3.806 0.000 1 110 162 162 SER C C 171.720 0.000 1 111 162 162 SER CA C 55.367 0.000 1 112 162 162 SER CB C 61.300 0.000 1 113 162 162 SER N N 119.611 0.000 1 114 163 163 ARG H H 8.407 0.000 1 115 163 163 ARG HA H 4.299 0.000 1 116 163 163 ARG HB2 H 1.674 0.000 1 117 163 163 ARG HG2 H 1.448 0.000 1 118 163 163 ARG HD2 H 3.116 0.000 1 119 163 163 ARG C C 173.277 0.000 1 120 163 163 ARG CA C 53.281 0.000 1 121 163 163 ARG CB C 28.205 0.000 1 122 163 163 ARG CG C 24.295 0.000 1 123 163 163 ARG CD C 40.566 0.000 1 124 163 163 ARG N N 123.635 0.000 1 125 164 164 GLU H H 8.329 0.000 1 126 164 164 GLU HA H 4.209 0.000 1 127 164 164 GLU HB2 H 1.827 0.000 1 128 164 164 GLU HG2 H 2.137 0.000 1 129 164 164 GLU C C 173.408 0.000 1 130 164 164 GLU CA C 53.628 0.000 1 131 164 164 GLU CB C 27.735 0.000 1 132 164 164 GLU CG C 33.498 0.000 1 133 164 164 GLU N N 122.025 0.000 1 134 165 165 GLU H H 8.383 0.000 1 135 165 165 GLU HA H 4.210 0.000 1 136 165 165 GLU HB2 H 1.938 0.000 1 137 165 165 GLU HG2 H 2.176 0.000 1 138 165 165 GLU C C 173.383 0.000 1 139 165 165 GLU CA C 53.545 0.000 1 140 165 165 GLU CB C 27.735 0.000 1 141 165 165 GLU CG C 33.536 0.000 1 142 165 165 GLU N N 123.113 0.000 1 143 166 166 LYS H H 8.325 0.000 1 144 166 166 LYS HA H 4.552 0.000 1 145 166 166 LYS HB2 H 1.648 0.000 2 146 166 166 LYS HB3 H 1.742 0.000 2 147 166 166 LYS HG2 H 1.394 0.000 2 148 166 166 LYS HG3 H 1.371 0.000 2 149 166 166 LYS C C 171.660 0.000 1 150 166 166 LYS CA C 51.327 0.000 1 151 166 166 LYS CB C 29.854 0.000 1 152 166 166 LYS CG C 21.815 0.000 1 153 166 166 LYS N N 123.773 0.000 1 154 168 168 THR H H 8.283 0.000 1 155 168 168 THR HA H 4.261 0.000 1 156 168 168 THR HB H 4.164 0.000 1 157 168 168 THR HG2 H 1.167 0.000 1 158 168 168 THR C C 171.866 0.000 1 159 168 168 THR CA C 59.251 0.000 1 160 168 168 THR CB C 67.142 0.000 1 161 168 168 THR CG2 C 18.760 0.000 1 162 168 168 THR N N 114.742 0.000 1 163 169 169 SER H H 8.171 0.000 1 164 169 169 SER HA H 4.398 0.000 1 165 169 169 SER HB2 H 3.771 0.000 1 166 169 169 SER C C 170.897 0.005 1 167 169 169 SER CA C 55.303 0.000 1 168 169 169 SER CB C 61.300 0.000 1 169 169 169 SER N N 117.914 0.000 1 170 170 170 ALA H H 8.261 0.000 1 171 170 170 ALA HA H 4.548 0.000 1 172 170 170 ALA HB H 1.288 0.000 1 173 170 170 ALA C C 172.716 0.000 1 174 170 170 ALA CA C 47.814 0.000 1 175 170 170 ALA CB C 15.484 0.000 1 176 170 170 ALA N N 127.108 0.000 1 177 172 172 SER H H 8.405 0.000 1 178 172 172 SER HA H 4.396 0.000 1 179 172 172 SER HB2 H 3.851 0.000 1 180 172 172 SER C C 171.072 0.000 1 181 172 172 SER CA C 55.596 0.000 1 182 172 172 SER CB C 61.243 0.000 1 183 172 172 SER N N 116.550 0.000 1 184 173 173 SER H H 7.903 0.001 1 185 173 173 SER HA H 4.198 0.000 1 186 173 173 SER HB2 H 3.783 0.000 1 187 173 173 SER C C 175.826 0.000 1 188 173 173 SER CA C 57.268 0.000 1 189 173 173 SER CB C 62.130 0.000 1 190 173 173 SER N N 122.842 0.003 1 stop_ save_