data_27204 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone 1H, 13C, and 15N Chemical Shift Assignments for Hs. Par3 PDZ2 domain ; _BMRB_accession_number 27204 _BMRB_flat_file_name bmr27204.str _Entry_type original _Submission_date 2017-08-07 _Accession_date 2017-08-07 _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 Wiesner Silke . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 89 "15N chemical shifts" 89 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2018-02-15 original BMRB . stop_ loop_ _Related_BMRB_accession_number _Relationship 27197 'Chemical Shift Assignments for Dm. Par3 PDZ1 domain' 27198 'Chemical Shift Assignments for Dm. Par3 PDZ3 domain' 27203 'Chemical Shift Assignments for Dm. Par3 PDZ2 domain' 27205 'Chemical Shift Assignments for Hs. Par3 PDZ3 domain' stop_ _Original_release_date 2017-08-07 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Structural basis for the interaction between the cell polarity proteins Par3 and Par6 ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 29440511 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Renschler Fabian A. . 2 Bruekner Susanne R. . 3 Salomon Paulin L. . 4 Mukherjee Amrita . . 5 Kullmann Lars . . 6 Schutz-Stoffregen Mira C. . 7 Henzler Christine . . 8 Pawson Tony . . 9 Krahn Michael P. . 10 Wiesner Silke . . stop_ _Journal_abbreviation 'Sci. Signal.' _Journal_name_full 'Science signaling' _Journal_volume 11 _Journal_issue 517 _Journal_ISSN 1937-9145 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 9899 _Page_last 9899 _Year 2018 _Details . loop_ _Keyword 'PDZ domain' 'Par proteins' Par3 Par6 'cell polarity' stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Hs. Par3 PDZ2 domain' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'Hs. Par3 PDZ2 domain' $Par3_PDZ2_domain 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_Par3_PDZ2_domain _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common Par3_PDZ2_domain _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 96 _Mol_residue_sequence ; GAMGKRLNIQLKKGTEGLGF SITSRDVTIGGSAPIYVKNI LPRGAAIQDGRLKAGDRLIE VNGVDLVGKSQEEVVSLLRS TKMEGTVSLLVFRQED ; loop_ _Residue_seq_code _Residue_label 1 GLY 2 ALA 3 MET 4 GLY 5 LYS 6 ARG 7 LEU 8 ASN 9 ILE 10 GLN 11 LEU 12 LYS 13 LYS 14 GLY 15 THR 16 GLU 17 GLY 18 LEU 19 GLY 20 PHE 21 SER 22 ILE 23 THR 24 SER 25 ARG 26 ASP 27 VAL 28 THR 29 ILE 30 GLY 31 GLY 32 SER 33 ALA 34 PRO 35 ILE 36 TYR 37 VAL 38 LYS 39 ASN 40 ILE 41 LEU 42 PRO 43 ARG 44 GLY 45 ALA 46 ALA 47 ILE 48 GLN 49 ASP 50 GLY 51 ARG 52 LEU 53 LYS 54 ALA 55 GLY 56 ASP 57 ARG 58 LEU 59 ILE 60 GLU 61 VAL 62 ASN 63 GLY 64 VAL 65 ASP 66 LEU 67 VAL 68 GLY 69 LYS 70 SER 71 GLN 72 GLU 73 GLU 74 VAL 75 VAL 76 SER 77 LEU 78 LEU 79 ARG 80 SER 81 THR 82 LYS 83 MET 84 GLU 85 GLY 86 THR 87 VAL 88 SER 89 LEU 90 LEU 91 VAL 92 PHE 93 ARG 94 GLN 95 GLU 96 ASP 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 $Par3_PDZ2_domain 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 $Par3_PDZ2_domain 'recombinant technology' . Escherichia coli . pETM-41 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 $Par3_PDZ2_domain 1 mM '[U-100% 15N]' 'sodium phosphate' 20 mM 'natural abundance' 'sodium chloride' 150 mM 'natural abundance' DTT 1 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_XEASY _Saveframe_category software _Name XEASY _Version . loop_ _Vendor _Address _Electronic_address 'Bartels et al.' . . 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 800 _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_1H-15N_NOESY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '3D 1H-15N NOESY' _Sample_label $sample_1 save_ save_3D_HNHA_3 _Saveframe_category NMR_applied_experiment _Experiment_name '3D HNHA' _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' 0.15 . M pH 6.5 . pH pressure 1 . atm temperature 303 . 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 4.8 internal indirect . . . 1 water N 15 protons ppm 0 internal 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_chem_shift_list_1 _Saveframe_category assigned_chemical_shifts _Details . loop_ _Experiment_label '2D 1H-15N HSQC' '3D 1H-15N NOESY' '3D HNHA' 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 'Hs. Par3 PDZ2 domain' _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 4 4 GLY H H 8.249 0.000 1 2 4 4 GLY N N 109.516 0.000 1 3 5 5 LYS H H 8.029 0.000 1 4 5 5 LYS N N 119.345 0.000 1 5 6 6 ARG H H 8.383 0.000 1 6 6 6 ARG N N 121.481 0.000 1 7 7 7 LEU H H 8.951 0.000 1 8 7 7 LEU N N 123.135 0.000 1 9 8 8 ASN H H 8.540 0.000 1 10 8 8 ASN N N 121.417 0.000 1 11 9 9 ILE H H 8.991 0.000 1 12 9 9 ILE N N 126.088 0.000 1 13 10 10 GLN H H 7.593 0.000 1 14 10 10 GLN N N 126.386 0.000 1 15 11 11 LEU H H 8.777 0.000 1 16 11 11 LEU N N 122.062 0.000 1 17 12 12 LYS H H 8.787 0.000 1 18 12 12 LYS N N 123.730 0.000 1 19 13 13 LYS H H 8.633 0.000 1 20 13 13 LYS N N 126.989 0.000 1 21 14 14 GLY H H 7.864 0.000 1 22 14 14 GLY N N 115.796 0.000 1 23 16 16 GLU H H 8.381 0.000 1 24 16 16 GLU N N 118.465 0.000 1 25 17 17 GLY H H 7.794 0.000 1 26 17 17 GLY N N 131.609 0.000 1 27 18 18 LEU H H 8.848 0.000 1 28 18 18 LEU N N 114.059 0.000 1 29 19 19 GLY H H 8.961 0.000 1 30 19 19 GLY N N 130.497 0.000 1 31 20 20 PHE H H 7.504 0.000 1 32 20 20 PHE N N 115.011 0.000 1 33 21 21 SER H H 8.830 0.000 1 34 21 21 SER N N 116.587 0.000 1 35 22 22 ILE H H 8.735 0.000 1 36 22 22 ILE N N 114.798 0.000 1 37 23 23 THR H H 9.058 0.000 1 38 23 23 THR N N 114.096 0.000 1 39 24 24 SER H H 8.134 0.000 1 40 24 24 SER N N 116.915 0.000 1 41 25 25 ARG H H 8.573 0.000 1 42 25 25 ARG N N 121.822 0.000 1 43 26 26 ASP H H 8.352 0.000 1 44 26 26 ASP N N 120.891 0.000 1 45 27 27 VAL H H 8.114 0.000 1 46 27 27 VAL N N 119.137 0.000 1 47 28 28 THR H H 8.262 0.000 1 48 28 28 THR N N 116.288 0.000 1 49 29 29 ILE H H 8.109 0.000 1 50 29 29 ILE N N 122.149 0.000 1 51 31 31 GLY H H 8.242 0.000 1 52 31 31 GLY N N 108.232 0.000 1 53 32 32 SER H H 8.101 0.000 1 54 32 32 SER N N 114.840 0.000 1 55 33 33 ALA H H 8.463 0.000 1 56 33 33 ALA N N 128.033 0.000 1 57 35 35 ILE H H 8.586 0.000 1 58 35 35 ILE N N 121.947 0.000 1 59 36 36 TYR H H 8.848 0.000 1 60 36 36 TYR N N 123.490 0.000 1 61 37 37 VAL H H 9.092 0.000 1 62 37 37 VAL N N 120.168 0.000 1 63 38 38 LYS H H 9.502 0.000 1 64 38 38 LYS N N 110.629 0.000 1 65 39 39 ASN H H 9.502 0.000 1 66 39 39 ASN N N 108.718 0.000 1 67 40 40 ILE H H 8.557 0.000 1 68 40 40 ILE N N 121.899 0.000 1 69 41 41 LEU H H 8.060 0.000 1 70 41 41 LEU N N 128.953 0.000 1 71 43 43 ARG H H 7.142 0.000 1 72 43 43 ARG N N 114.239 0.000 1 73 44 44 GLY H H 8.381 0.000 1 74 44 44 GLY N N 108.521 0.000 1 75 45 45 ALA H H 7.857 0.000 1 76 45 45 ALA N N 118.517 0.000 1 77 46 46 ALA H H 8.576 0.000 1 78 46 46 ALA N N 118.486 0.000 1 79 47 47 ILE H H 9.639 0.000 1 80 47 47 ILE N N 123.949 0.000 1 81 48 48 GLN H H 7.090 0.000 1 82 48 48 GLN N N 122.336 0.000 1 83 49 49 ASP H H 7.922 0.000 1 84 49 49 ASP N N 118.429 0.000 1 85 50 50 GLY H H 7.801 0.000 1 86 50 50 GLY N N 129.260 0.000 1 87 51 51 ARG H H 7.860 0.000 1 88 51 51 ARG N N 118.634 0.000 1 89 52 52 LEU H H 9.332 0.000 1 90 52 52 LEU N N 123.829 0.000 1 91 53 53 LYS H H 8.352 0.000 1 92 53 53 LYS N N 123.557 0.000 1 93 54 54 ALA H H 8.482 0.000 1 94 54 54 ALA N N 123.308 0.000 1 95 55 55 GLY H H 8.978 0.000 1 96 55 55 GLY N N 112.434 0.000 1 97 56 56 ASP H H 7.899 0.000 1 98 56 56 ASP N N 123.567 0.000 1 99 57 57 ARG H H 8.841 0.000 1 100 57 57 ARG N N 123.605 0.000 1 101 58 58 LEU H H 8.831 0.000 1 102 58 58 LEU N N 127.918 0.000 1 103 59 59 ILE H H 9.051 0.000 1 104 59 59 ILE N N 122.742 0.000 1 105 60 60 GLU H H 7.642 0.000 1 106 60 60 GLU N N 115.985 0.000 1 107 61 61 VAL H H 7.889 0.000 1 108 61 61 VAL N N 119.542 0.000 1 109 62 62 ASN H H 9.981 0.000 1 110 62 62 ASN N N 126.415 0.000 1 111 63 63 GLY H H 8.804 0.000 1 112 63 63 GLY N N 129.222 0.000 1 113 64 64 VAL H H 8.077 0.000 1 114 64 64 VAL N N 123.386 0.000 1 115 65 65 ASP H H 8.450 0.000 1 116 65 65 ASP N N 127.046 0.000 1 117 66 66 LEU H H 7.566 0.000 1 118 66 66 LEU N N 122.131 0.000 1 119 67 67 VAL H H 8.255 0.000 1 120 67 67 VAL N N 123.708 0.000 1 121 68 68 GLY H H 8.650 0.000 1 122 68 68 GLY N N 115.412 0.000 1 123 69 69 LYS H H 7.792 0.000 1 124 69 69 LYS N N 119.816 0.000 1 125 70 70 SER H H 9.122 0.000 1 126 70 70 SER N N 118.769 0.000 1 127 71 71 GLN H H 9.131 0.000 1 128 71 71 GLN N N 120.767 0.000 1 129 72 72 GLU H H 8.735 0.000 1 130 72 72 GLU N N 117.666 0.000 1 131 73 73 GLU H H 7.861 0.000 1 132 73 73 GLU N N 120.783 0.000 1 133 74 74 VAL H H 8.138 0.000 1 134 74 74 VAL N N 121.539 0.000 1 135 75 75 VAL H H 8.601 0.000 1 136 75 75 VAL N N 120.694 0.000 1 137 76 76 SER H H 7.990 0.000 1 138 76 76 SER N N 114.767 0.000 1 139 77 77 LEU H H 7.891 0.000 1 140 77 77 LEU N N 123.323 0.000 1 141 78 78 LEU H H 8.093 0.000 1 142 78 78 LEU N N 118.996 0.000 1 143 79 79 ARG H H 8.458 0.000 1 144 79 79 ARG N N 119.867 0.000 1 145 80 80 SER H H 7.699 0.000 1 146 80 80 SER N N 113.468 0.000 1 147 81 81 THR H H 7.404 0.000 1 148 81 81 THR N N 117.100 0.000 1 149 82 82 LYS H H 8.667 0.000 1 150 82 82 LYS N N 126.586 0.000 1 151 83 83 MET H H 8.487 0.000 1 152 83 83 MET N N 120.930 0.000 1 153 84 84 GLU H H 8.846 0.000 1 154 84 84 GLU N N 118.817 0.000 1 155 85 85 GLY H H 8.498 0.000 1 156 85 85 GLY N N 108.834 0.000 1 157 86 86 THR H H 8.216 0.000 1 158 86 86 THR N N 114.066 0.000 1 159 87 87 VAL H H 9.300 0.000 1 160 87 87 VAL N N 126.165 0.000 1 161 88 88 SER H H 8.738 0.000 1 162 88 88 SER N N 122.110 0.000 1 163 89 89 LEU H H 9.310 0.000 1 164 89 89 LEU N N 126.031 0.000 1 165 90 90 LEU H H 8.404 0.000 1 166 90 90 LEU N N 126.615 0.000 1 167 91 91 VAL H H 9.081 0.000 1 168 91 91 VAL N N 120.770 0.000 1 169 92 92 PHE H H 9.346 0.000 1 170 92 92 PHE N N 121.210 0.000 1 171 93 93 ARG H H 8.731 0.000 1 172 93 93 ARG N N 131.263 0.000 1 173 94 94 GLN H H 8.617 0.000 1 174 94 94 GLN N N 126.979 0.000 1 175 95 95 GLU H H 8.275 0.000 1 176 95 95 GLU N N 123.325 0.000 1 177 96 96 ASP H H 8.040 0.000 1 178 96 96 ASP N N 127.427 0.000 1 stop_ save_