data_25406 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Titin M10 H56P mutation ; _BMRB_accession_number 25406 _BMRB_flat_file_name bmr25406.str _Entry_type original _Submission_date 2014-12-29 _Accession_date 2014-12-29 _Entry_origination author _NMR_STAR_version 2.1.1 _Experimental_method NMR _Details 'titin M10 H56P HSQC coordinates at 25C' loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Wright Nathan T. . 2 Rudloff Michael . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 76 "15N chemical shifts" 76 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2015-08-25 original BMRB . stop_ loop_ _Related_BMRB_accession_number _Relationship 25301 OBSC-Ig1 25303 'titin M10-obscurin-Ig1' 25304 'obscurin Ig1 bound to titin M10' 25305 'titin M10' 25308 'obscurin Ig58' stop_ _Original_release_date 2015-08-25 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Biophysical characterization of naturally occurring titin M10 mutations ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 25739468 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Rudloff Michael W. . 2 Woosley Alec N. . 3 Wright Nathan T. . stop_ _Journal_abbreviation 'Protein Sci.' _Journal_volume 24 _Journal_issue 6 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 946 _Page_last 955 _Year 2015 _Details . loop_ _Keyword LGMD2J M10 obscurin titin stop_ save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name H56P _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label H56P $H56P 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_H56P _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common H56P _Molecular_mass . _Mol_thiol_state 'all free' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 107 _Mol_residue_sequence ; HHHHHHGSRGIPPKIEALPS DISIDEGKVLTVACAFTGEP TPEVTWSCGGRKIHSQEQGR FPIENTDDLTTLIIMDVQKQ DGGLYTLSLGNEFGSDSATV NIHIRSI ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 -5 HIS 2 -4 HIS 3 -3 HIS 4 -2 HIS 5 -1 HIS 6 0 HIS 7 1 GLY 8 2 SER 9 3 ARG 10 4 GLY 11 5 ILE 12 6 PRO 13 7 PRO 14 8 LYS 15 9 ILE 16 10 GLU 17 11 ALA 18 12 LEU 19 13 PRO 20 14 SER 21 15 ASP 22 16 ILE 23 17 SER 24 18 ILE 25 19 ASP 26 20 GLU 27 21 GLY 28 22 LYS 29 23 VAL 30 24 LEU 31 25 THR 32 26 VAL 33 27 ALA 34 28 CYS 35 29 ALA 36 30 PHE 37 31 THR 38 32 GLY 39 33 GLU 40 34 PRO 41 35 THR 42 36 PRO 43 37 GLU 44 38 VAL 45 39 THR 46 40 TRP 47 41 SER 48 42 CYS 49 43 GLY 50 44 GLY 51 45 ARG 52 46 LYS 53 47 ILE 54 48 HIS 55 49 SER 56 50 GLN 57 51 GLU 58 52 GLN 59 53 GLY 60 54 ARG 61 55 PHE 62 56 PRO 63 57 ILE 64 58 GLU 65 59 ASN 66 60 THR 67 61 ASP 68 62 ASP 69 63 LEU 70 64 THR 71 65 THR 72 66 LEU 73 67 ILE 74 68 ILE 75 69 MET 76 70 ASP 77 71 VAL 78 72 GLN 79 73 LYS 80 74 GLN 81 75 ASP 82 76 GLY 83 77 GLY 84 78 LEU 85 79 TYR 86 80 THR 87 81 LEU 88 82 SER 89 83 LEU 90 84 GLY 91 85 ASN 92 86 GLU 93 87 PHE 94 88 GLY 95 89 SER 96 90 ASP 97 91 SER 98 92 ALA 99 93 THR 100 94 VAL 101 95 ASN 102 96 ILE 103 97 HIS 104 98 ILE 105 99 ARG 106 100 SER 107 101 ILE stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-10-14 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 25303 titin_M10 94.39 101 99.01 99.01 9.01e-65 BMRB 25305 titin_M10 94.39 101 99.01 99.01 9.01e-65 PDB 2WP3 "Crystal Structure Of The Titin M10-Obscurin Like 1 Ig Complex" 93.46 102 99.00 99.00 5.14e-64 PDB 2WWK "Crystal Structure Of The Titin M10-Obscurin Like 1 Ig F17r Mutant Complex" 93.46 102 99.00 99.00 5.14e-64 PDB 2WWM "Crystal Structure Of The Titin M10-Obscurin Like 1 Ig Complex In Space Group P1" 93.46 102 99.00 99.00 5.14e-64 PDB 2Y9R "Crystal Structure Of The M10 Domain Of Titin" 93.46 102 99.00 99.00 5.14e-64 PDB 3KNB "Crystal Structure Of The Titin C-Terminus In Complex With Obscurin- Like 1" 91.59 100 98.98 98.98 3.63e-62 PDB 3Q5O "Crystal Structure Of Human Titin Domain M10" 91.59 100 98.98 98.98 3.63e-62 PDB 4C4K "Crystal Structure Of The Titin M10-obscurin Ig Domain 1 Complex" 93.46 102 99.00 99.00 5.14e-64 PDB 4UOW "Crystal Structure Of The Titin M10-obscurin Ig Domain 1 Complex" 90.65 97 98.97 98.97 8.65e-62 stop_ save_ #################### # Natural source # #################### save_natural_source _Saveframe_category natural_source loop_ _Mol_label _Organism_name_common _NCBI_taxonomy_ID _Superkingdom _Kingdom _Genus _Species _Gene_mnemonic _Details $H56P Human 9606 Eukaryota Metazoa Homo sapiens 'skeletal titin' 'Mutation of the hman M10 domain in titin' stop_ save_ ######################### # Experimental source # ######################### save_experimental_source _Saveframe_category experimental_source loop_ _Mol_label _Production_method _Host_organism_name_common _Genus _Species _Strain _Variant _Vector_name $H56P 'recombinant technology' . Escherichia coli K12 BL-21(DE3) pET24a 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 $H56P 1 mM '[U-99% 15N]' D2O 10 % [U-2H] 'sodium phosphate' 10 mM 'natural abundance' 'sodim fluoride' 50 mM 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_NMRDraw _Saveframe_category software _Name NMRDraw _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . 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 600 _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_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units 'ionic strength' 0.05 . M pH 7.2 . 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' '3D 1H-15N NOESY' 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 H56P _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 9 ARG H H 8.631 0.002 1 2 3 9 ARG N N 123.38 0.01 1 3 4 10 GLY H H 7.374 0.002 1 4 4 10 GLY N N 109.82 0.01 1 5 5 11 ILE H H 9.102 0.002 1 6 5 11 ILE N N 121.67 0.01 1 7 10 16 GLU H H 8.698 0.002 1 8 10 16 GLU N N 129.66 0.01 1 9 11 17 ALA H H 7.482 0.002 1 10 11 17 ALA N N 119.10 0.01 1 11 12 18 LEU H H 8.323 0.002 1 12 12 18 LEU N N 125.55 0.01 1 13 14 20 SER H H 8.412 0.002 1 14 14 20 SER N N 112.93 0.01 1 15 15 21 ASP H H 7.681 0.002 1 16 15 21 ASP N N 120.52 0.01 1 17 16 22 ILE H H 8.898 0.002 1 18 16 22 ILE N N 122.22 0.01 1 19 17 23 SER H H 8.470 0.002 1 20 17 23 SER N N 121.33 0.01 1 21 18 24 ILE H H 8.776 0.002 1 22 18 24 ILE N N 123.56 0.01 1 23 19 25 ASP H H 7.811 0.002 1 24 19 25 ASP N N 126.51 0.01 1 25 20 26 GLU H H 8.091 0.002 1 26 20 26 GLU N N 119.20 0.01 1 27 21 27 GLY H H 9.691 0.002 1 28 21 27 GLY N N 113.06 0.01 1 29 22 28 LYS H H 7.266 0.002 1 30 22 28 LYS N N 120.17 0.01 1 31 23 29 VAL H H 7.722 0.002 1 32 23 29 VAL N N 117.19 0.01 1 33 24 30 LEU H H 8.881 0.002 1 34 24 30 LEU N N 131.90 0.01 1 35 25 31 THR H H 8.031 0.002 1 36 25 31 THR N N 119.67 0.01 1 37 26 32 VAL H H 9.467 0.002 1 38 26 32 VAL N N 125.74 0.01 1 39 27 33 ALA H H 8.511 0.002 1 40 27 33 ALA N N 129.98 0.01 1 41 28 34 CYS H H 9.506 0.002 1 42 28 34 CYS N N 123.46 0.01 1 43 29 35 ALA H H 8.848 0.002 1 44 29 35 ALA N N 131.37 0.01 1 45 30 36 PHE H H 7.486 0.002 1 46 30 36 PHE N N 114.63 0.01 1 47 31 37 THR H H 8.423 0.002 1 48 31 37 THR N N 110.13 0.01 1 49 32 38 GLY H H 8.342 0.002 1 50 32 38 GLY N N 107.41 0.01 1 51 35 41 THR H H 8.544 0.002 1 52 35 41 THR N N 118.68 0.01 1 53 37 43 GLU H H 8.736 0.002 1 54 37 43 GLU N N 120.09 0.01 1 55 38 44 VAL H H 8.567 0.002 1 56 38 44 VAL N N 129.51 0.01 1 57 40 46 TRP H H 9.575 0.002 1 58 40 46 TRP N N 130.22 0.01 1 59 41 47 SER H H 9.446 0.002 1 60 41 47 SER N N 115.13 0.01 1 61 42 48 CYS H H 8.535 0.002 1 62 42 48 CYS N N 120.57 0.01 1 63 45 51 ARG H H 7.631 0.002 1 64 45 51 ARG N N 121.19 0.01 1 65 46 52 LYS H H 8.504 0.002 1 66 46 52 LYS N N 126.07 0.01 1 67 47 53 ILE H H 8.710 0.002 1 68 47 53 ILE N N 126.17 0.01 1 69 48 54 HIS H H 8.295 0.002 1 70 48 54 HIS N N 123.27 0.01 1 71 51 57 GLU H H 8.772 0.002 1 72 51 57 GLU N N 123.84 0.01 1 73 52 58 GLN H H 7.973 0.002 1 74 52 58 GLN N N 119.73 0.01 1 75 53 59 GLY H H 8.070 0.002 1 76 53 59 GLY N N 107.50 0.01 1 77 55 61 PHE H H 7.691 0.002 1 78 55 61 PHE N N 115.44 0.01 1 79 57 63 ILE H H 7.972 0.002 1 80 57 63 ILE N N 122.40 0.01 1 81 59 65 ASN H H 9.172 0.002 1 82 59 65 ASN N N 126.68 0.01 1 83 60 66 THR H H 9.213 0.002 1 84 60 66 THR N N 117.10 0.01 1 85 61 67 ASP H H 8.291 0.002 1 86 61 67 ASP N N 117.92 0.01 1 87 62 68 ASP H H 7.919 0.002 1 88 62 68 ASP N N 115.83 0.01 1 89 63 69 LEU H H 7.081 0.002 1 90 63 69 LEU N N 122.59 0.01 1 91 65 71 THR H H 8.631 0.002 1 92 65 71 THR N N 125.24 0.01 1 93 68 74 ILE H H 8.735 0.002 1 94 68 74 ILE N N 124.00 0.01 1 95 70 76 ASP H H 7.162 0.002 1 96 70 76 ASP N N 119.63 0.01 1 97 71 77 VAL H H 8.080 0.002 1 98 71 77 VAL N N 115.75 0.01 1 99 73 79 LYS H H 9.242 0.002 1 100 73 79 LYS N N 122.19 0.01 1 101 75 81 ASP H H 8.145 0.002 1 102 75 81 ASP N N 118.94 0.01 1 103 76 82 GLY H H 7.663 0.002 1 104 76 82 GLY N N 106.04 0.01 1 105 77 83 GLY H H 8.816 0.002 1 106 77 83 GLY N N 109.43 0.01 1 107 78 84 LEU H H 8.253 0.002 1 108 78 84 LEU N N 120.60 0.01 1 109 79 85 TYR H H 9.814 0.002 1 110 79 85 TYR N N 130.94 0.01 1 111 80 86 THR H H 9.272 0.002 1 112 80 86 THR N N 118.17 0.01 1 113 81 87 LEU H H 8.856 0.002 1 114 81 87 LEU N N 130.86 0.01 1 115 82 88 SER H H 8.792 0.002 1 116 82 88 SER N N 119.91 0.01 1 117 83 89 LEU H H 8.710 0.002 1 118 83 89 LEU N N 122.57 0.01 1 119 84 90 GLY H H 7.890 0.002 1 120 84 90 GLY N N 106.49 0.01 1 121 85 91 ASN H H 8.971 0.002 1 122 85 91 ASN N N 121.49 0.01 1 123 86 92 GLU H H 9.172 0.002 1 124 86 92 GLU N N 117.11 0.01 1 125 87 93 PHE H H 7.919 0.002 1 126 87 93 PHE N N 115.83 0.01 1 127 88 94 GLY H H 7.756 0.002 1 128 88 94 GLY N N 107.38 0.01 1 129 89 95 SER H H 8.452 0.002 1 130 89 95 SER N N 112.46 0.01 1 131 90 96 ASP H H 8.630 0.002 1 132 90 96 ASP N N 119.37 0.01 1 133 91 97 SER H H 8.211 0.002 1 134 91 97 SER N N 115.75 0.01 1 135 92 98 ALA H H 8.824 0.002 1 136 92 98 ALA N N 124.67 0.01 1 137 93 99 THR H H 8.335 0.002 1 138 93 99 THR N N 111.98 0.01 1 139 94 100 VAL H H 9.473 0.002 1 140 94 100 VAL N N 123.11 0.01 1 141 95 101 ASN H H 8.516 0.002 1 142 95 101 ASN N N 127.74 0.01 1 143 96 102 ILE H H 9.116 0.002 1 144 96 102 ILE N N 127.02 0.01 1 145 97 103 HIS H H 9.285 0.002 1 146 97 103 HIS N N 129.89 0.01 1 147 98 104 ILE H H 8.615 0.002 1 148 98 104 ILE N N 124.59 0.01 1 149 99 105 ARG H H 8.888 0.002 1 150 99 105 ARG N N 129.44 0.01 1 151 101 107 ILE H H 8.167 0.002 1 152 101 107 ILE N N 127.21 0.01 1 stop_ save_