data_26956 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Backbone assignment of S100A4 and C-ERMAD fragment of ezrin ; _BMRB_accession_number 26956 _BMRB_flat_file_name bmr26956.str _Entry_type original _Submission_date 2016-11-24 _Accession_date 2016-11-24 _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 Palfy Gyula . . 2 Bodor Andrea . . 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 2017-05-23 original BMRB . stop_ loop_ _Related_BMRB_accession_number _Relationship 26946 'C-terminal truncated S100A4, apo form' stop_ _Original_release_date 2016-11-28 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Ezrin interacts with S100A4 via both its N- and C-terminal domains ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 28493957 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Biri-Kovacs Beata . . 2 Kiss Bence . . 3 Vadaszi Henrietta . . 4 Gogl Gergo . . 5 Palfy Gyula . . 6 Homolya Laszlo . . 7 Bodor Andrea . . 8 Nyitray Laszlo . . stop_ _Journal_abbreviation 'PLoS ONE' _Journal_name_full 'PloS one' _Journal_volume 12 _Journal_issue 5 _Journal_ISSN 1932-6203 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first e0177489 _Page_last e0177489 _Year 2017 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Ca-S100A4d9-C-ERMAD complex' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label 'S100A4d9, 1' $S100A4d9 'S100A4d9, 2' $S100A4d9 C-ERMAD $C-ERMAD 'CALCIUM ION, 1' $entity_CA 'CALCIUM ION, 2' $entity_CA 'CALCIUM ION, 3' $entity_CA 'CALCIUM ION, 4' $entity_CA stop_ _System_molecular_weight . _System_physical_state native _System_oligomer_state ? _System_paramagnetic no _System_thiol_state . loop_ _Magnetic_equivalence_ID _Magnetically_equivalent_system_component '#1' 'S100A4d9, 1' '#2' 'S100A4d9, 2' stop_ _Database_query_date . _Details . save_ ######################## # Monomeric polymers # ######################## save_S100A4d9 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common S100A4d9 _Molecular_mass 10884.45 _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 95 _Mol_residue_sequence ; GSHMACPLEKALDVMVSTFH KYSGKEGDKFKLNKSELKEL LTRELPSFLGKRTDEAAFQK LMSNLDSNRDNEVDFQEYCV FLSCIAMMCNEFFEG ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -2 GLY 2 -1 SER 3 0 HIS 4 1 MET 5 2 ALA 6 3 CYS 7 4 PRO 8 5 LEU 9 6 GLU 10 7 LYS 11 8 ALA 12 9 LEU 13 10 ASP 14 11 VAL 15 12 MET 16 13 VAL 17 14 SER 18 15 THR 19 16 PHE 20 17 HIS 21 18 LYS 22 19 TYR 23 20 SER 24 21 GLY 25 22 LYS 26 23 GLU 27 24 GLY 28 25 ASP 29 26 LYS 30 27 PHE 31 28 LYS 32 29 LEU 33 30 ASN 34 31 LYS 35 32 SER 36 33 GLU 37 34 LEU 38 35 LYS 39 36 GLU 40 37 LEU 41 38 LEU 42 39 THR 43 40 ARG 44 41 GLU 45 42 LEU 46 43 PRO 47 44 SER 48 45 PHE 49 46 LEU 50 47 GLY 51 48 LYS 52 49 ARG 53 50 THR 54 51 ASP 55 52 GLU 56 53 ALA 57 54 ALA 58 55 PHE 59 56 GLN 60 57 LYS 61 58 LEU 62 59 MET 63 60 SER 64 61 ASN 65 62 LEU 66 63 ASP 67 64 SER 68 65 ASN 69 66 ARG 70 67 ASP 71 68 ASN 72 69 GLU 73 70 VAL 74 71 ASP 75 72 PHE 76 73 GLN 77 74 GLU 78 75 TYR 79 76 CYS 80 77 VAL 81 78 PHE 82 79 LEU 83 80 SER 84 81 CYS 85 82 ILE 86 83 ALA 87 84 MET 88 85 MET 89 86 CYS 90 87 ASN 91 88 GLU 92 89 PHE 93 90 PHE 94 91 GLU 95 92 GLY 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 P26447 . . . . . . stop_ save_ save_C-ERMAD _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common C-ERMAD _Molecular_mass 8824.83 _Mol_thiol_state 'all free' _Details . _Residue_count 74 _Mol_residue_sequence ; GSCKRITEAEKNERVQRQLL TLSSELSQARDENKRTHNDI IHNENMRQGRDKYKTLRQIR QGNTKQRIDEFEAL ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -2 GLY 2 -1 SER 3 0 CYS 4 516 LYS 5 517 ARG 6 518 ILE 7 519 THR 8 520 GLU 9 521 ALA 10 522 GLU 11 523 LYS 12 524 ASN 13 525 GLU 14 526 ARG 15 527 VAL 16 528 GLN 17 529 ARG 18 530 GLN 19 531 LEU 20 532 LEU 21 533 THR 22 534 LEU 23 535 SER 24 536 SER 25 537 GLU 26 538 LEU 27 539 SER 28 540 GLN 29 541 ALA 30 542 ARG 31 543 ASP 32 544 GLU 33 545 ASN 34 546 LYS 35 547 ARG 36 548 THR 37 549 HIS 38 550 ASN 39 551 ASP 40 552 ILE 41 553 ILE 42 554 HIS 43 555 ASN 44 556 GLU 45 557 ASN 46 558 MET 47 559 ARG 48 560 GLN 49 561 GLY 50 562 ARG 51 563 ASP 52 564 LYS 53 565 TYR 54 566 LYS 55 567 THR 56 568 LEU 57 569 ARG 58 570 GLN 59 571 ILE 60 572 ARG 61 573 GLN 62 574 GLY 63 575 ASN 64 576 THR 65 577 LYS 66 578 GLN 67 579 ARG 68 580 ILE 69 581 ASP 70 582 GLU 71 583 PHE 72 584 GLU 73 585 ALA 74 586 LEU 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 P15311 . . . . . . stop_ save_ ############# # Ligands # ############# save_CA _Saveframe_category ligand _Mol_type "non-polymer (NON-POLYMER)" _Name_common "entity_CA (CALCIUM ION)" _BMRB_code CA _PDB_code CA _Molecular_mass 40.078 _Mol_charge 2 _Mol_paramagnetic . _Mol_aromatic no _Details . loop_ _Atom_name _PDB_atom_name _Atom_type _Atom_chirality _Atom_charge _Atom_oxidation_number _Atom_unpaired_electrons CA CA CA . 2 . ? stop_ _Mol_thiol_state . _Sequence_homology_query_date . save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species $S100A4d9 'E. coli' 562 Bacteria . Escherichia coli $C-ERMAD 'E. coli' 562 Bacteria . Escherichia coli 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 $S100A4d9 'recombinant technology' . Escherichia coli . pET $C-ERMAD 'recombinant technology' . Escherichia coli . pET 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 $S100A4d9 0.4 mM '[U-100% 15N]' $C-ERMAD 0.6 mM 'natural abundance' MES 20 mM 'natural abundance' NaCl 150 mM 'natural abundance' CaCl2 10 mM 'natural abundance' TCEP 5 mM 'natural abundance' NaN3 3 mM 'natural abundance' D2O 50 uL '[U-100% 2H]' DSS 5 uL '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 stop_ _Details . save_ 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 III' _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 'ionic strength' 0.17 . M pH 6.0 . 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 0.00 internal direct . . . 1 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 'S100A4d9, 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 0 3 HIS H H 8.688 . . 2 0 3 HIS N N 121.158 . . 3 1 4 MET H H 8.409 . . 4 1 4 MET N N 122.081 . . 5 2 5 ALA H H 8.414 . . 6 2 5 ALA N N 125.472 . . 7 3 6 CYS H H 8.787 . . 8 3 6 CYS N N 120.581 . . 9 5 8 LEU H H 10.694 . . 10 5 8 LEU N N 121.858 . . 11 6 9 GLU H H 7.010 . . 12 6 9 GLU N N 116.939 . . 13 7 10 LYS H H 8.117 . . 14 7 10 LYS N N 119.703 . . 15 8 11 ALA H H 8.399 . . 16 8 11 ALA N N 122.199 . . 17 9 12 LEU H H 8.550 . . 18 9 12 LEU N N 116.834 . . 19 10 13 ASP H H 8.514 . . 20 10 13 ASP N N 118.317 . . 21 11 14 VAL H H 8.573 . . 22 11 14 VAL N N 118.777 . . 23 12 15 MET H H 8.609 . . 24 12 15 MET N N 124.549 . . 25 13 16 VAL H H 8.491 . . 26 13 16 VAL N N 121.501 . . 27 14 17 SER H H 9.173 . . 28 14 17 SER N N 115.599 . . 29 15 18 THR H H 8.710 . . 30 15 18 THR N N 118.693 . . 31 16 19 PHE H H 6.981 . . 32 16 19 PHE N N 119.357 . . 33 17 20 HIS H H 7.130 . . 34 17 20 HIS N N 115.430 . . 35 18 21 LYS H H 7.892 . . 36 18 21 LYS N N 122.008 . . 37 19 22 TYR H H 6.742 . . 38 19 22 TYR N N 113.026 . . 39 20 23 SER H H 8.549 . . 40 20 23 SER N N 114.420 . . 41 21 24 GLY H H 7.663 . . 42 21 24 GLY N N 110.023 . . 43 22 25 LYS H H 7.172 . . 44 22 25 LYS N N 121.938 . . 45 23 26 GLU H H 9.607 . . 46 23 26 GLU N N 116.499 . . 47 24 27 GLY H H 8.990 . . 48 24 27 GLY N N 113.572 . . 49 25 28 ASP H H 8.557 . . 50 25 28 ASP N N 126.120 . . 51 26 29 LYS H H 9.433 . . 52 26 29 LYS N N 132.219 . . 53 27 30 PHE H H 9.555 . . 54 27 30 PHE N N 120.304 . . 55 28 31 LYS H H 7.130 . . 56 28 31 LYS N N 115.322 . . 57 29 32 LEU H H 9.539 . . 58 29 32 LEU N N 125.802 . . 59 30 33 ASN H H 9.653 . . 60 30 33 ASN N N 124.020 . . 61 31 34 LYS H H 8.332 . . 62 31 34 LYS N N 116.421 . . 63 32 35 SER H H 7.713 . . 64 32 35 SER N N 114.828 . . 65 33 36 GLU H H 8.822 . . 66 33 36 GLU N N 124.114 . . 67 34 37 LEU H H 8.936 . . 68 34 37 LEU N N 118.473 . . 69 35 38 LYS H H 8.048 . . 70 35 38 LYS N N 118.548 . . 71 36 39 GLU H H 7.762 . . 72 36 39 GLU N N 121.256 . . 73 37 40 LEU H H 7.871 . . 74 37 40 LEU N N 121.159 . . 75 38 41 LEU H H 8.605 . . 76 38 41 LEU N N 118.398 . . 77 39 42 THR H H 7.878 . . 78 39 42 THR N N 108.535 . . 79 40 43 ARG H H 8.170 . . 80 40 43 ARG N N 116.413 . . 81 41 44 GLU H H 8.523 . . 82 41 44 GLU N N 112.926 . . 83 42 45 LEU H H 7.486 . . 84 42 45 LEU N N 118.357 . . 85 44 47 SER H H 9.702 . . 86 44 47 SER N N 116.963 . . 87 45 48 PHE H H 8.084 . . 88 45 48 PHE N N 119.837 . . 89 46 49 LEU H H 7.822 . . 90 46 49 LEU N N 119.374 . . 91 47 50 GLY H H 7.986 . . 92 47 50 GLY N N 107.019 . . 93 48 51 LYS H H 8.466 . . 94 48 51 LYS N N 120.519 . . 95 49 52 ARG H H 8.066 . . 96 49 52 ARG N N 119.805 . . 97 50 53 THR H H 7.973 . . 98 50 53 THR N N 112.426 . . 99 51 54 ASP H H 8.078 . . 100 51 54 ASP N N 123.167 . . 101 52 55 GLU H H 8.658 . . 102 52 55 GLU N N 122.166 . . 103 53 56 ALA H H 8.406 . . 104 53 56 ALA N N 122.240 . . 105 54 57 ALA H H 8.040 . . 106 54 57 ALA N N 122.056 . . 107 55 58 PHE H H 8.127 . . 108 55 58 PHE N N 118.876 . . 109 56 59 GLN H H 8.355 . . 110 56 59 GLN N N 119.553 . . 111 57 60 LYS H H 7.797 . . 112 57 60 LYS N N 120.423 . . 113 58 61 LEU H H 7.656 . . 114 58 61 LEU N N 120.648 . . 115 59 62 MET H H 8.116 . . 116 59 62 MET N N 117.187 . . 117 60 63 SER H H 7.974 . . 118 60 63 SER N N 112.429 . . 119 61 64 ASN H H 7.758 . . 120 61 64 ASN N N 118.528 . . 121 62 65 LEU H H 7.864 . . 122 62 65 LEU N N 118.671 . . 123 63 66 ASP H H 7.879 . . 124 63 66 ASP N N 117.180 . . 125 64 67 SER H H 8.245 . . 126 64 67 SER N N 122.287 . . 127 65 68 ASN H H 8.112 . . 128 65 68 ASN N N 116.601 . . 129 66 69 ARG H H 7.694 . . 130 66 69 ARG N N 115.543 . . 131 67 70 ASP H H 8.619 . . 132 67 70 ASP N N 119.401 . . 133 68 71 ASN H H 10.193 . . 134 68 71 ASN N N 116.477 . . 135 69 72 GLU H H 7.823 . . 136 69 72 GLU N N 116.555 . . 137 70 73 VAL H H 9.991 . . 138 70 73 VAL N N 126.015 . . 139 71 74 ASP H H 9.193 . . 140 71 74 ASP N N 128.821 . . 141 72 75 PHE H H 9.033 . . 142 72 75 PHE N N 118.706 . . 143 73 76 GLN H H 8.270 . . 144 73 76 GLN N N 120.593 . . 145 74 77 GLU H H 8.815 . . 146 74 77 GLU N N 120.770 . . 147 75 78 TYR H H 8.737 . . 148 75 78 TYR N N 123.459 . . 149 76 79 CYS H H 8.312 . . 150 76 79 CYS N N 120.238 . . 151 77 80 VAL H H 7.885 . . 152 77 80 VAL N N 122.151 . . 153 78 81 PHE H H 7.700 . . 154 78 81 PHE N N 121.554 . . 155 79 82 LEU H H 8.394 . . 156 79 82 LEU N N 117.893 . . 157 80 83 SER H H 8.105 . . 158 80 83 SER N N 115.194 . . 159 81 84 CYS H H 7.768 . . 160 81 84 CYS N N 121.244 . . 161 82 85 ILE H H 7.759 . . 162 82 85 ILE N N 118.526 . . 163 83 86 ALA H H 8.258 . . 164 83 86 ALA N N 122.272 . . 165 84 87 MET H H 7.794 . . 166 84 87 MET N N 120.501 . . 167 85 88 MET H H 7.819 . . 168 85 88 MET N N 119.371 . . 169 88 91 GLU H H 7.956 . . 170 88 91 GLU N N 125.228 . . 171 89 92 PHE H H 6.968 . . 172 89 92 PHE N N 114.942 . . 173 90 93 PHE H H 7.434 . . 174 90 93 PHE N N 121.333 . . 175 91 94 GLU H H 7.297 . . 176 91 94 GLU N N 115.403 . . 177 92 95 GLY H H 7.467 . . 178 92 95 GLY N N 118.236 . . stop_ save_