data_17642 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Solution structure of the N-terminal domain of huntingtin (htt17) in 50 % TFE ; _BMRB_accession_number 17642 _BMRB_flat_file_name bmr17642.str _Entry_type original _Submission_date 2011-05-13 _Accession_date 2011-05-13 _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 Salnikov Evgeniy S. . 3 Werten Sebastiaan . . 4 Bechinger Burkhard . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 66 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2013-08-13 update author 'update entry citation' 2012-08-30 original author 'original release' stop_ loop_ _Related_BMRB_accession_number _Relationship 17644 'htt17 in DPC micelles' stop_ save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title 'Structure and Topology of the Huntingtin 1-17 Membrane Anchor by a Combined Solution and Solid-State NMR Approach' _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 23931318 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Michalek Matthias . . 2 Salnikov Evgeniy S. . 3 Bechinger Burkhard . . stop_ _Journal_abbreviation 'Biophys. J.' _Journal_volume 105 _Journal_issue 3 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 699 _Page_last 710 _Year 2013 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name htt17 _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label htt17 $htt17 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_htt17 _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common htt17 _Molecular_mass 1977.422 _Mol_thiol_state 'not present' _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 17 _Mol_residue_sequence MATLEKLMKAFESLKSF loop_ _Residue_seq_code _Residue_label 1 MET 2 ALA 3 THR 4 LEU 5 GLU 6 LYS 7 LEU 8 MET 9 LYS 10 ALA 11 PHE 12 GLU 13 SER 14 LEU 15 LYS 16 SER 17 PHE stop_ _Sequence_homology_query_date . _Sequence_homology_query_revised_last_date 2015-08-12 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 17644 htt17 100.00 17 100.00 100.00 1.00e+00 BMRB 25146 httNTQ30P10K2 100.00 59 100.00 100.00 1.08e-02 PDB 2LD0 "Solution Structure Of The N-terminal Domain Of Huntingtin (htt17) In 50 % Tfe" 100.00 18 100.00 100.00 9.83e-01 PDB 2LD2 "Solution Structure Of The N-terminal Domain Of Huntingtin (htt17) In Presence Of Dpc Micelles" 100.00 18 100.00 100.00 9.83e-01 PDB 3IO4 "Huntingtin Amino-Terminal Region With 17 Gln Residues - Crystal C90" 100.00 449 100.00 100.00 8.56e-01 PDB 3IO6 "Huntingtin Amino-Terminal Region With 17 Gln Residues - Crystal C92-A" 100.00 449 100.00 100.00 8.56e-01 PDB 3IOR "Huntingtin Amino-terminal Region With 17 Gln Residues - Crystal C95" 100.00 449 100.00 100.00 8.56e-01 PDB 3IOT "Huntingtin Amino-terminal Region With 17 Gln Residues - Crystal C92-b" 100.00 449 100.00 100.00 8.56e-01 PDB 3IOU "Huntingtin Amino-terminal Region With 17 Gln Residues - Crystal C94" 100.00 449 100.00 100.00 8.56e-01 PDB 3IOV "Huntingtin Amino-terminal Region With 17 Gln Residues - Crystal C99" 100.00 449 100.00 100.00 8.56e-01 PDB 3IOW "Huntingtin Amino-terminal Region With 17 Gln Residues - Crystal C99-hg" 100.00 449 100.00 100.00 8.56e-01 PDB 4FE8 "Crystal Structure Of Htt36q3h-ex1-x1-c1(alpha)" 100.00 452 100.00 100.00 6.38e-01 PDB 4FEB "Crystal Structure Of Htt36q3h-ex1-x1-c2(beta)" 100.00 452 100.00 100.00 6.38e-01 PDB 4FEC "Crystal Structure Of Htt36q3h" 100.00 452 100.00 100.00 6.38e-01 PDB 4FED "Crystal Structure Of Htt36q3h" 100.00 452 100.00 100.00 6.38e-01 PDB 4RAV "Crystal Structure Of Scfvc4 In Complex With The First 17 Aa Of Huntingtin" 100.00 17 100.00 100.00 1.00e+00 DBJ BAA36752 "huntingtin [Sus scrofa]" 100.00 3139 100.00 100.00 1.35e+00 DBJ BAA36753 "huntingtin [Homo sapiens]" 100.00 3144 100.00 100.00 2.48e+00 DBJ BAH03657 "huntingtin [Callithrix jacchus]" 100.00 3131 100.00 100.00 2.48e+00 EMBL CAA12281 "huntingtin [Rattus norvegicus]" 100.00 67 100.00 100.00 1.36e-02 GB AAA89100 "Huntington's Disease gene homologue [Mus musculus]" 100.00 3119 100.00 100.00 2.05e+00 GB AAB38240 "Huntington's Disease protein [Homo sapiens]" 100.00 3144 100.00 100.00 2.45e+00 GB AAC52218 "huntingtin [Mus musculus]" 100.00 3119 100.00 100.00 2.13e+00 GB AAI72756 "huntingtin [synthetic construct]" 100.00 3144 100.00 100.00 2.45e+00 GB AAR34461 "huntingtin [Rattus norvegicus]" 100.00 158 100.00 100.00 1.80e-01 REF NP_001136110 "huntingtin [Ovis aries]" 100.00 3127 100.00 100.00 1.89e+00 REF NP_001254674 "huntingtin [Callithrix jacchus]" 100.00 3131 100.00 100.00 2.48e+00 REF NP_002102 "huntingtin [Homo sapiens]" 100.00 3144 100.00 100.00 2.45e+00 REF NP_034544 "huntingtin [Mus musculus]" 100.00 3120 100.00 100.00 2.02e+00 REF NP_077333 "huntingtin [Rattus norvegicus]" 100.00 3120 100.00 100.00 2.21e+00 SP P42858 "RecName: Full=Huntingtin; AltName: Full=Huntington disease protein; Short=HD protein" 100.00 3142 100.00 100.00 2.48e+00 SP P42859 "RecName: Full=Huntingtin; AltName: Full=Huntington disease protein homolog; Short=HD protein homolog" 100.00 3119 100.00 100.00 2.05e+00 TPG DAA28444 "TPA: huntingtin [Bos taurus]" 100.00 3131 100.00 100.00 2.11e+00 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 $htt17 Human 9606 Eukaryota Metazoa Homo sapiens 'huntingtin (HTT)' 'N-terminal domain of huntingtin (htt17)' 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 _Details $htt17 'chemical synthesis' . . . . . 'C-terminally amidated peptide' stop_ save_ ##################################### # Sample contents and methodology # ##################################### ######################## # Sample description # ######################## save_htt_tfe _Saveframe_category sample _Sample_type solution _Details 'peptide after disaggregation' loop_ _Mol_label _Concentration_value _Concentration_value_units _Concentration_min_value _Concentration_max_value _Isotopic_labeling $htt17 . mM 0.2 0.3 '15N labeled at PHE11' D2O 10 % . . 'natural abundance' TFE 50 % . . d3 PBS 40 % . . 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_X-PLOR_NIH _Saveframe_category software _Name X-PLOR_NIH _Version . loop_ _Vendor _Address _Electronic_address 'Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax' . . 'Johnson, One Moon Scientific' . . 'Schwieters, Kuszewski, Tjandra and Clore' . . 'Koradi, Billeter and Wuthrich' . . 'Bhattacharya and Montelione' . . stop_ loop_ _Task processing 'chemical shift assignment' 'data analysis' 'structure solution' 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_ ############################# # NMR applied experiments # ############################# save_2D_1H-1H_TOCSY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H TOCSY' _Sample_label $htt_tfe save_ save_2D_1H-1H_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H TOCSY' _Sample_label $htt_tfe save_ save_2D_1H-1H_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label $htt_tfe save_ save_2D_1H-1H_NOESY_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label $htt_tfe save_ ####################### # Sample conditions # ####################### save_sample_conditions_1 _Saveframe_category sample_conditions _Details . loop_ _Variable_type _Variable_value _Variable_value_error _Variable_value_units temperature 273 . K pH 7.2 . pH pressure 1 . atm 'ionic strength' 0.15 . M 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 4.773 na direct . . . 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 TOCSY' '2D 1H-1H NOESY' stop_ loop_ _Sample_label $htt_tfe stop_ _Sample_conditions_label $sample_conditions_1 _Chem_shift_reference_set_label $chemical_shift_reference_1 _Mol_system_component_name htt17 _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 3 THR H H 7.4261 . 1 2 3 3 THR HA H 4.5359 . 1 3 3 3 THR HB H 4.3750 . 1 4 3 3 THR HG2 H 1.4925 . 1 5 4 4 LEU H H 8.3521 . 1 6 4 4 LEU HA H 4.3660 . 1 7 4 4 LEU HB3 H 1.8934 . 2 8 4 4 LEU HG H 1.7188 . 1 9 4 4 LEU HD1 H 1.1435 . 2 10 5 5 GLU H H 8.1983 . 1 11 5 5 GLU HA H 4.1952 . 1 12 5 5 GLU HB2 H 2.2704 . 2 13 5 5 GLU HB3 H 2.3606 . 2 14 5 5 GLU HG3 H 2.5452 . 2 15 6 6 LYS H H 7.8994 . 1 16 6 6 LYS HA H 4.2038 . 1 17 6 6 LYS HB3 H 2.7591 . 2 18 6 6 LYS HG3 H 1.8099 . 2 19 7 7 LEU H H 8.1377 . 1 20 7 7 LEU HA H 4.2624 . 1 21 7 7 LEU HB3 H 2.0042 . 2 22 7 7 LEU HG H 1.8651 . 1 23 7 7 LEU HD1 H 1.0551 . 2 24 8 8 MET H H 8.6460 . 1 25 8 8 MET HA H 4.4874 . 1 26 8 8 MET HB3 H 2.4575 . 2 27 8 8 MET HG3 H 2.8206 . 2 28 9 9 LYS H H 8.2325 . 1 29 9 9 LYS HA H 4.3607 . 1 30 9 9 LYS HB2 H 2.1665 . 2 31 9 9 LYS HB3 H 2.2257 . 2 32 9 9 LYS HG3 H 1.7509 . 2 33 9 9 LYS HD3 H 2.3425 . 2 34 10 10 ALA H H 8.4028 . 1 35 10 10 ALA HA H 4.3502 . 1 36 10 10 ALA HB H 1.7267 . 1 37 11 11 PHE H H 8.6854 . 1 38 11 11 PHE HA H 4.5939 . 1 39 11 11 PHE HB3 H 3.4861 . 2 40 11 11 PHE HE2 H 7.4693 . 3 41 12 12 GLU H H 8.8410 . 1 42 12 12 GLU HA H 4.5920 . 1 43 12 12 GLU HB2 H 2.4169 . 2 44 12 12 GLU HB3 H 3.0811 . 2 45 12 12 GLU HG2 H 2.6071 . 2 46 12 12 GLU HG3 H 2.6875 . 2 47 13 13 SER H H 8.6378 . 1 48 13 13 SER HA H 4.2021 . 1 49 14 14 LEU H H 8.2859 . 1 50 14 14 LEU HA H 4.4890 . 1 51 14 14 LEU HG H 2.4246 . 1 52 15 15 LYS H H 8.2515 . 1 53 15 15 LYS HA H 4.4096 . 1 54 15 15 LYS HB2 H 2.0279 . 2 55 15 15 LYS HB3 H 2.0643 . 2 56 15 15 LYS HG3 H 1.3330 . 2 57 15 15 LYS HD3 H 1.8357 . 2 58 16 16 SER H H 8.1464 . 1 59 16 16 SER HA H 4.2772 . 1 60 16 16 SER HB3 H 4.0260 . 2 61 17 17 PHE H H 7.9867 . 1 62 17 17 PHE HA H 4.5152 . 1 63 17 17 PHE HB2 H 3.3103 . 2 64 17 17 PHE HB3 H 3.4616 . 2 65 17 17 PHE HD1 H 7.4748 . 3 66 17 17 PHE HE1 H 7.5267 . 3 stop_ save_