data_18358 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; The solution structure of the dimeric Acanthaporin ; _BMRB_accession_number 18358 _BMRB_flat_file_name bmr18358.str _Entry_type original _Submission_date 2012-03-28 _Accession_date 2012-03-28 _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 Michalek Matthias . . 2 Soennichsen Frank D. . 3 Wechselberger Rainer . . 4 Dingley Andrew J. . 5 Wienk Hans . . 6 Simanski Maren . . 7 Herbst Rosa . . 8 Lorenzen Inken . . 9 Marciano-Cabral Francine . . 10 Gelhaus Christoph . . 11 Groetzinger Joachim . . 12 Leippe Matthias . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 185 "15N chemical shifts" 43 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2012-05-01 original author . stop_ loop_ _Related_BMRB_accession_number _Relationship 18357 Acanthaporin stop_ _Original_release_date 2012-05-01 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'The solution structure of the dimeric Acanthaporin' _Citation_status submitted _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID ? loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Michalek Matthias . . 2 Soennichsen Frank D. . 3 Wechselberger Rainer . . 4 Dingley Andrew J. . 5 Wienk Hans . . 6 Simanski Maren . . 7 Herbst Rosa . . 8 Lorenzen Inken . . 9 Marciano-Cabral Francine . . 10 Gelhaus Christoph . . 11 Groetzinger Joachim . . 12 Leippe Matthias . . stop_ _Journal_abbreviation 'Not known' _Journal_volume . _Journal_issue . _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first . _Page_last . _Year . _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'dimeric Acanthaporin' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'acanthaporin_dimer, chain 1' $acanthaporin_dimer 'acanthaporin_dimer, chain 2' $acanthaporin_dimer 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_acanthaporin_dimer _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common acanthaporin_dimer _Molecular_mass 6001.235 _Mol_thiol_state 'all disulfide bound' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 61 _Mol_residue_sequence ; AMGKCSVLKKVACAAAIAGA VAACGGIDLPCVLAALKAAE GCASCFCEDHCHGVCKDLHL C ; loop_ _Residue_seq_code _Residue_label 1 ALA 2 MET 3 GLY 4 LYS 5 CYS 6 SER 7 VAL 8 LEU 9 LYS 10 LYS 11 VAL 12 ALA 13 CYS 14 ALA 15 ALA 16 ALA 17 ILE 18 ALA 19 GLY 20 ALA 21 VAL 22 ALA 23 ALA 24 CYS 25 GLY 26 GLY 27 ILE 28 ASP 29 LEU 30 PRO 31 CYS 32 VAL 33 LEU 34 ALA 35 ALA 36 LEU 37 LYS 38 ALA 39 ALA 40 GLU 41 GLY 42 CYS 43 ALA 44 SER 45 CYS 46 PHE 47 CYS 48 GLU 49 ASP 50 HIS 51 CYS 52 HIS 53 GLY 54 VAL 55 CYS 56 LYS 57 ASP 58 LEU 59 HIS 60 LEU 61 CYS stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2014-03-04 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 BMRB 16727 culbertcidin 100.00 61 100.00 100.00 6.78e-31 BMRB 16819 culbertcidin 100.00 122 100.00 100.00 1.71e-17 BMRB 18357 acanthaporin 100.00 61 100.00 100.00 6.78e-31 PDB 2LRD "The Solution Structure Of The Monomeric Acanthaporin" 100.00 61 100.00 100.00 6.78e-31 PDB 2LRE "The Solution Structure Of The Dimeric Acanthaporin" 100.00 61 100.00 100.00 6.78e-31 GB AEC33273 "acanthaporin precursor [Acanthamoeba culbertsoni]" 98.36 160 98.33 98.33 1.40e-29 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $acanthaporin_dimer 'Acanthamoeba culbertsoni' 43142 Eukaryota . Acanthamoeba culbertsoni 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 $acanthaporin_dimer 'recombinant technology' . Escherichia coli . pET32a 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 $acanthaporin_dimer 0.7 mM '[U-100% 15N]' TRIS 25 mM [U-2H] 'sodium azide' 0.001 % 'natural abundance' H2O 93 % 'natural abundance' D2O 7 % 'natural abundance' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling $acanthaporin_dimer 0.7 mM '[U-100% 15N]' TRIS 25 mM [U-2H] 'sodium azide' 0.001 % 'natural abundance' H2O 93 % 'natural abundance' D2O 7 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRPipe _Saveframe_category software _Name NMRPipe _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . stop_ loop_ _Task processing stop_ _Details . save_ save_NMRView _Saveframe_category software _Name NMRView _Version . loop_ _Vendor _Address _Electronic_address 'Johnson, One Moon Scientific' . . stop_ loop_ _Task 'chemical shift assignment' 'data analysis' 'peak picking' stop_ _Details . save_ save_CYANA _Saveframe_category software _Name CYANA _Version . loop_ _Vendor _Address _Electronic_address 'Guntert, Mumenthaler and Wuthrich' . . stop_ loop_ _Task 'structure solution' stop_ _Details . save_ save_X-PLOR_NIH _Saveframe_category software _Name 'X-PLOR NIH' _Version . loop_ _Vendor _Address _Electronic_address 'Schwieters, Kuszewski, Tjandra and Clore' . . stop_ loop_ _Task refinement stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 600 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 750 _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-1H_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H TOCSY' _Sample_label $sample_2 save_ save_2D_1H-1H_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label $sample_2 save_ save_3D_1H-15N_NOESY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_1 save_ save_3D_1H-15N_TOCSY_5 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N TOCSY' _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' 0.025 . M pH 8.0 . pH pressure 1 . atm temperature 293 . 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 water H 1 protons ppm 0 internal indirect . . . 1.0 '[15N] ammonium chloride' N 15 nitrogen ppm 0 internal indirect . . . 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_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-1H NOESY' '3D 1H-15N NOESY' stop_ loop_ _Sample_label $sample_2 $sample_1 stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name 'acanthaporin_dimer, chain 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 8 8 LEU H H 7.735 . 1 2 8 8 LEU HA H 4.121 . 1 3 8 8 LEU HB2 H 1.694 . 2 4 8 8 LEU HG H 1.492 . 1 5 8 8 LEU N N 117.542 . 1 6 9 9 LYS H H 7.831 . 1 7 9 9 LYS HA H 4.078 . 1 8 9 9 LYS HB2 H 2.161 . 2 9 9 9 LYS HB3 H 1.880 . 2 10 9 9 LYS HG2 H 1.697 . 2 11 9 9 LYS N N 123.335 . 1 12 10 10 LYS H H 8.627 . 1 13 10 10 LYS HA H 3.657 . 1 14 10 10 LYS HB2 H 2.022 . 2 15 10 10 LYS N N 121.522 . 1 16 11 11 VAL H H 7.491 . 1 17 11 11 VAL HA H 3.733 . 1 18 11 11 VAL HB H 2.157 . 1 19 11 11 VAL HG1 H 1.128 . 4 20 11 11 VAL HG1 H 0.972 . 4 21 11 11 VAL N N 117.576 . 1 22 12 12 ALA H H 7.898 . 1 23 12 12 ALA HA H 4.131 . 1 24 12 12 ALA HB H 1.586 . 1 25 12 12 ALA N N 123.018 . 1 26 13 13 CYS H H 8.394 . 1 27 13 13 CYS HA H 4.587 . 1 28 13 13 CYS HB2 H 3.057 . 2 29 13 13 CYS HB3 H 3.009 . 2 30 13 13 CYS N N 113.951 . 1 31 14 14 ALA H H 7.549 . 1 32 14 14 ALA HA H 4.027 . 1 33 14 14 ALA HB H 1.576 . 1 34 14 14 ALA N N 124.346 . 1 35 15 15 ALA HA H 4.203 . 1 36 16 16 ALA H H 8.570 . 1 37 16 16 ALA HA H 4.075 . 1 38 16 16 ALA HB H 1.407 . 1 39 16 16 ALA N N 124.554 . 1 40 17 17 ILE H H 8.475 . 1 41 17 17 ILE HA H 3.416 . 1 42 17 17 ILE HB H 1.869 . 1 43 17 17 ILE HG12 H 1.071 . 9 44 17 17 ILE HG2 H 0.948 . 4 45 17 17 ILE HD1 H 0.848 . 1 46 17 17 ILE N N 119.462 . 1 47 18 18 ALA H H 8.288 . 1 48 18 18 ALA HA H 4.069 . 1 49 18 18 ALA HB H 1.504 . 1 50 18 18 ALA N N 121.295 . 1 51 19 19 GLY H H 8.399 . 1 52 19 19 GLY HA2 H 3.883 . 2 53 19 19 GLY N N 105.669 . 1 54 20 20 ALA H H 7.972 . 1 55 20 20 ALA HA H 4.081 . 1 56 20 20 ALA HB H 1.404 . 1 57 20 20 ALA N N 127.175 . 1 58 21 21 VAL H H 8.435 . 1 59 21 21 VAL HA H 3.365 . 1 60 21 21 VAL HB H 1.978 . 1 61 21 21 VAL HG1 H 0.944 . 4 62 21 21 VAL HG1 H 0.716 . 4 63 21 21 VAL N N 118.978 . 1 64 22 22 ALA H H 7.835 . 1 65 22 22 ALA HA H 4.074 . 1 66 22 22 ALA HB H 1.456 . 1 67 22 22 ALA N N 121.005 . 1 68 23 23 ALA H H 8.062 . 1 69 23 23 ALA HA H 4.063 . 1 70 23 23 ALA HB H 1.498 . 1 71 23 23 ALA N N 121.200 . 1 72 24 24 CYS H H 8.045 . 1 73 24 24 CYS HA H 4.488 . 1 74 24 24 CYS HB2 H 3.310 . 2 75 24 24 CYS HB3 H 2.970 . 2 76 24 24 CYS N N 114.529 . 1 77 25 25 GLY H H 7.916 . 1 78 25 25 GLY HA2 H 4.075 . 2 79 25 25 GLY HA3 H 3.831 . 2 80 25 25 GLY N N 109.695 . 1 81 26 26 GLY H H 8.056 . 1 82 26 26 GLY HA2 H 4.337 . 2 83 26 26 GLY HA3 H 3.604 . 2 84 26 26 GLY N N 107.481 . 1 85 27 27 ILE H H 8.342 . 1 86 27 27 ILE HA H 3.745 . 1 87 27 27 ILE HB H 2.031 . 1 88 27 27 ILE HG12 H 1.508 . 9 89 27 27 ILE HG13 H 1.265 . 9 90 27 27 ILE HD1 H 0.678 . 1 91 27 27 ILE N N 117.952 . 1 92 28 28 ASP H H 7.060 . 1 93 28 28 ASP HB2 H 2.572 . 2 94 28 28 ASP N N 128.285 . 1 95 29 29 LEU H H 8.907 . 1 96 29 29 LEU HA H 4.002 . 1 97 29 29 LEU HB2 H 2.061 . 2 98 29 29 LEU HG H 1.636 . 1 99 29 29 LEU HD1 H 0.965 . 4 100 29 29 LEU N N 124.546 . 1 101 31 31 CYS H H 7.340 . 1 102 31 31 CYS HA H 4.167 . 1 103 31 31 CYS HB2 H 3.094 . 2 104 31 31 CYS N N 117.630 . 1 105 32 32 VAL H H 8.718 . 1 106 32 32 VAL HA H 3.178 . 1 107 32 32 VAL HB H 1.499 . 1 108 32 32 VAL HG1 H 0.698 . 4 109 32 32 VAL HG1 H -0.423 . 4 110 32 32 VAL HG2 H -0.367 . 4 111 32 32 VAL N N 124.340 . 1 112 33 33 LEU H H 8.512 . 1 113 33 33 LEU HA H 3.692 . 1 114 33 33 LEU HB2 H 1.732 . 2 115 33 33 LEU HG H 1.287 . 1 116 33 33 LEU HD1 H 0.942 . 4 117 33 33 LEU HD1 H 0.790 . 4 118 33 33 LEU HD1 H 0.942 . 4 119 33 33 LEU N N 117.743 . 1 120 34 34 ALA H H 7.508 . 1 121 34 34 ALA HA H 4.067 . 1 122 34 34 ALA HB H 1.447 . 1 123 34 34 ALA N N 120.707 . 1 124 35 35 ALA H H 7.765 . 1 125 35 35 ALA HA H 4.174 . 1 126 35 35 ALA HB H 1.511 . 1 127 35 35 ALA N N 121.539 . 1 128 36 36 LEU H H 8.322 . 1 129 36 36 LEU HA H 4.207 . 1 130 36 36 LEU HB2 H 1.657 . 2 131 36 36 LEU HD1 H 0.564 . 4 132 36 36 LEU HD1 H 0.430 . 4 133 36 36 LEU HD1 H 0.564 . 4 134 36 36 LEU N N 116.961 . 1 135 37 37 LYS H H 7.335 . 1 136 37 37 LYS HA H 3.988 . 1 137 37 37 LYS HB2 H 1.924 . 2 138 37 37 LYS HB3 H 1.818 . 2 139 37 37 LYS HG2 H 1.611 . 2 140 37 37 LYS HG3 H 1.500 . 2 141 37 37 LYS N N 121.909 . 1 142 42 42 CYS HA H 4.790 . 1 143 42 42 CYS HB2 H 3.047 . 2 144 42 42 CYS HB3 H 2.973 . 2 145 43 43 ALA HA H 3.985 . 1 146 44 44 SER HB2 H 3.869 . 2 147 45 45 CYS H H 7.104 . 1 148 45 45 CYS HA H 4.341 . 1 149 45 45 CYS HB2 H 3.133 . 2 150 45 45 CYS N N 118.951 . 1 151 46 46 PHE H H 7.984 . 1 152 46 46 PHE HA H 4.599 . 1 153 46 46 PHE HB2 H 2.958 . 2 154 46 46 PHE HD2 H 6.646 . 3 155 46 46 PHE HE2 H 7.222 . 3 156 46 46 PHE HZ H 6.978 . 1 157 46 46 PHE N N 120.196 . 1 158 47 47 CYS H H 8.773 . 1 159 47 47 CYS HA H 4.319 . 1 160 47 47 CYS HB2 H 2.725 . 2 161 47 47 CYS HB3 H 2.590 . 2 162 47 47 CYS N N 115.827 . 1 163 48 48 GLU H H 7.775 . 1 164 48 48 GLU HA H 3.929 . 1 165 48 48 GLU HB2 H 2.384 . 2 166 48 48 GLU HB3 H 2.580 . 2 167 48 48 GLU HG2 H 2.148 . 2 168 48 48 GLU N N 117.841 . 1 169 49 49 ASP H H 6.791 . 1 170 49 49 ASP HA H 4.490 . 1 171 49 49 ASP HB2 H 2.312 . 2 172 49 49 ASP N N 116.149 . 1 173 50 50 HIS H H 7.016 . 1 174 50 50 HIS HA H 4.483 . 1 175 50 50 HIS HB2 H 2.675 . 2 176 50 50 HIS HB3 H 2.234 . 2 177 50 50 HIS HD1 H 12.833 . 3 178 50 50 HIS N N 121.887 . 1 179 51 51 CYS H H 8.059 . 1 180 51 51 CYS HA H 4.490 . 1 181 51 51 CYS HB2 H 2.856 . 2 182 51 51 CYS N N 118.443 . 1 183 52 52 HIS H H 8.294 . 1 184 52 52 HIS HA H 4.581 . 1 185 52 52 HIS HB2 H 3.496 . 2 186 52 52 HIS HB3 H 2.981 . 2 187 52 52 HIS N N 123.835 . 1 188 54 54 VAL HA H 4.013 . 1 189 54 54 VAL HG1 H 1.077 . 4 190 55 55 CYS H H 7.314 . 1 191 55 55 CYS HA H 4.229 . 1 192 55 55 CYS HB2 H 3.514 . 2 193 55 55 CYS HB3 H 3.000 . 2 194 55 55 CYS N N 116.926 . 1 195 56 56 LYS H H 6.427 . 1 196 56 56 LYS HA H 4.115 . 1 197 56 56 LYS HB2 H 1.775 . 2 198 56 56 LYS HG2 H 1.346 . 2 199 56 56 LYS N N 117.865 . 1 200 57 57 ASP H H 8.415 . 1 201 57 57 ASP HA H 4.106 . 1 202 57 57 ASP HB2 H 2.520 . 2 203 57 57 ASP HB3 H 2.533 . 2 204 57 57 ASP N N 122.411 . 1 205 58 58 LEU H H 7.593 . 1 206 58 58 LEU HA H 4.212 . 1 207 58 58 LEU HB2 H 1.732 . 2 208 58 58 LEU HG H 1.583 . 1 209 58 58 LEU HD1 H 0.790 . 4 210 58 58 LEU N N 115.608 . 1 211 59 59 HIS H H 7.866 . 1 212 59 59 HIS HA H 4.316 . 1 213 59 59 HIS HB2 H 3.269 . 2 214 59 59 HIS N N 113.919 . 1 215 60 60 LEU H H 7.762 . 1 216 60 60 LEU HA H 4.291 . 1 217 60 60 LEU HB2 H 2.093 . 2 218 60 60 LEU HB3 H 1.560 . 2 219 60 60 LEU HG H 1.243 . 1 220 60 60 LEU HD1 H 0.974 . 4 221 60 60 LEU HD1 H 0.775 . 4 222 60 60 LEU HD1 H 0.974 . 4 223 60 60 LEU N N 116.798 . 1 224 61 61 CYS H H 7.627 . 1 225 61 61 CYS HA H 4.309 . 1 226 61 61 CYS HB2 H 3.096 . 2 227 61 61 CYS HB3 H 3.003 . 2 228 61 61 CYS N N 119.042 . 1 stop_ save_