data_25475 ####################### # Entry information # ####################### save_entry_information _Saveframe_category entry_information _Entry_title ; Structure of Tau(267-312) bound to Microtubules ; _BMRB_accession_number 25475 _BMRB_flat_file_name bmr25475.str _Entry_type original _Submission_date 2015-02-06 _Accession_date 2015-02-06 _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 Kadavath Harindranath . . 2 Jaremko Mariusz . . 3 Jaremko Lukasz . . 4 Zweckstetter Markus . . stop_ loop_ _Saveframe_category_type _Saveframe_category_type_count assigned_chemical_shifts 1 stop_ loop_ _Data_type _Data_type_count "1H chemical shifts" 43 stop_ loop_ _Revision_date _Revision_keyword _Revision_author _Revision_detail 2016-02-11 update BMRB 'update entry citation' 2015-07-13 original author 'original release' stop_ _Original_release_date 2015-07-13 save_ ############################# # Citation for this entry # ############################# save_entry_citation _Saveframe_category entry_citation _Citation_full . _Citation_title ; Folding of the Tau Protein on Microtubules ; _Citation_status published _Citation_type journal _CAS_abstract_code . _MEDLINE_UI_code . _PubMed_ID 26094605 loop_ _Author_ordinal _Author_family_name _Author_given_name _Author_middle_initials _Author_family_title 1 Kadavath Harindranath . . 2 Jaremko Mariusz . . 3 Jaremko Lukasz . . 4 Biernat Jacek . . 5 Mandelkow Eckhard . . 6 Zweckstetter Markus . . stop_ _Journal_abbreviation 'Angew. Chem. Int. Ed. Engl.' _Journal_volume 54 _Journal_issue 35 _Journal_CSD . _Book_chapter_title . _Book_volume . _Book_series . _Book_ISBN . _Conference_state_province . _Conference_abstract_number . _Page_first 10347 _Page_last 10351 _Year 2015 _Details . save_ ################################## # Molecular system description # ################################## save_assembly _Saveframe_category molecular_system _Mol_system_name 'Tau(267-312) bound to Microtubules' _Enzyme_commission_number . loop_ _Mol_system_component_name _Mol_label entity $entity 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_entity _Saveframe_category monomeric_polymer _Mol_type polymer _Mol_polymer_class protein _Name_common entity _Molecular_mass 4892.728 _Mol_thiol_state . _Details . ############################## # Polymer residue sequence # ############################## _Residue_count 46 _Mol_residue_sequence ; KHQPGGGKVQIINKKLDLSN VQSKCGSKDNIKHVPGGGSV QIVYKP ; loop_ _Residue_seq_code _Residue_author_seq_code _Residue_label 1 267 LYS 2 268 HIS 3 269 GLN 4 270 PRO 5 271 GLY 6 272 GLY 7 273 GLY 8 274 LYS 9 275 VAL 10 276 GLN 11 277 ILE 12 278 ILE 13 279 ASN 14 280 LYS 15 281 LYS 16 282 LEU 17 283 ASP 18 284 LEU 19 285 SER 20 286 ASN 21 287 VAL 22 288 GLN 23 289 SER 24 290 LYS 25 291 CYS 26 292 GLY 27 293 SER 28 294 LYS 29 295 ASP 30 296 ASN 31 297 ILE 32 298 LYS 33 299 HIS 34 300 VAL 35 301 PRO 36 302 GLY 37 303 GLY 38 304 GLY 39 305 SER 40 306 VAL 41 307 GLN 42 308 ILE 43 309 VAL 44 310 TYR 45 311 LYS 46 312 PRO 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 $entity 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 $entity 'chemical synthesis' . . . . . 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 'sodium phosphate' 50 mM 'natural abundance' $entity 1 mM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ save_sample_2 _Saveframe_category sample _Sample_type solution _Details . loop_ _Mol_label _Concentration_value _Concentration_value_units _Isotopic_labeling 'sodium phosphate' 50 mM 'natural abundance' $entity 1 mM 'natural abundance' microtubules 50 uM 'natural abundance' H2O 90 % 'natural abundance' D2O 10 % 'natural abundance' stop_ save_ ############################ # Computer software used # ############################ save_X-PLOR_NIH _Saveframe_category software _Name X-PLOR_NIH _Version 2.33 loop_ _Vendor _Address _Electronic_address 'Schwieters, Kuszewski, Tjandra and Clore' . . stop_ loop_ _Task refinement stop_ _Details . save_ save_CYANA _Saveframe_category software _Name CYANA _Version 3.0 loop_ _Vendor _Address _Electronic_address 'Guntert, Mumenthaler and Wuthrich' . . stop_ loop_ _Task 'chemical shift assignment' 'structure solution' stop_ _Details . save_ save_SPARKY _Saveframe_category software _Name SPARKY _Version . loop_ _Vendor _Address _Electronic_address Goddard . . stop_ loop_ _Task 'data analysis' 'peak picking' stop_ _Details . save_ save_TOPSPIN _Saveframe_category software _Name TOPSPIN _Version 3.0 loop_ _Vendor _Address _Electronic_address 'Bruker Biospin' . . stop_ loop_ _Task collection processing stop_ _Details . save_ ######################### # Experimental detail # ######################### ################################## # NMR Spectrometer definitions # ################################## save_spectrometer_1 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 900 _Details . save_ save_spectrometer_2 _Saveframe_category NMR_spectrometer _Manufacturer Bruker _Model Avance _Field_strength 700 _Details . save_ ############################# # NMR applied experiments # ############################# save_2D_1H-1H_NOESY_1 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label $sample_2 save_ save_2D_1H-1H_TOCSY_2 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H TOCSY' _Sample_label $sample_1 save_ save_2D_1H-1H_NOESY_3 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-1H NOESY' _Sample_label $sample_1 save_ save_2D_1H-13C_HSQC_aliphatic_4 _Saveframe_category NMR_applied_experiment _Experiment_name '2D 1H-13C HSQC aliphatic' _Sample_label $sample_1 save_ save_2D_1H-15N_HSQC_5 _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 . M pH 6.8 . pH pressure 1 . atm temperature 278 . 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 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' '2D 1H-1H TOCSY' '2D 1H-13C HSQC aliphatic' '2D 1H-15N HSQC' 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 entity _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 1 267 1 LYS H H 8.399 0.001 . 2 268 2 HIS H H 8.586 0.002 . 3 269 3 GLN H H 8.478 0.002 . 4 271 5 GLY H H 8.808 0.001 . 5 272 6 GLY H H 8.702 0 . 6 273 7 GLY H H 8.438 0.002 . 7 274 8 LYS H H 8.267 0.001 . 8 275 9 VAL H H 8.312 0.002 . 9 276 10 GLN H H 8.624 0.002 . 10 277 11 ILE H H 8.479 0.002 . 11 278 12 ILE H H 8.447 0.001 . 12 279 13 ASN H H 8.691 0.002 . 13 280 14 LYS H H 8.499 0.002 . 14 281 15 LYS H H 8.407 0.001 . 15 282 16 LEU H H 8.257 0.003 . 16 283 17 ASP H H 8.44 0.003 . 17 284 18 LEU H H 8.496 0.002 . 18 285 19 SER H H 8.439 0.002 . 19 286 20 ASN H H 8.37 0.003 . 20 287 21 VAL H H 8.036 0.002 . 21 288 22 GLN H H 8.556 0.002 . 22 289 23 SER H H 8.442 0.002 . 23 290 24 LYS H H 8.523 0.001 . 24 291 25 CYS H H 8.464 0.001 . 25 292 26 GLY H H 8.63 0.001 . 26 293 27 SER H H 8.363 0.002 . 27 294 28 LYS H H 8.593 0.002 . 28 295 29 ASP H H 8.282 0.001 . 29 296 30 ASN H H 8.372 0.003 . 30 297 31 ILE H H 8.08 0.001 . 31 298 32 LYS H H 8.428 0.002 . 32 299 33 HIS H H 8.512 0.009 . 33 300 34 VAL H H 8.319 0.007 . 34 302 36 GLY H H 8.794 0.001 . 35 303 37 GLY H H 8.461 0.001 . 36 304 38 GLY H H 8.465 0.001 . 37 305 39 SER H H 8.344 0.001 . 38 306 40 VAL H H 8.291 0.002 . 39 307 41 GLN H H 8.559 0.001 . 40 308 42 ILE H H 8.415 0.002 . 41 309 43 VAL H H 8.336 0.001 . 42 310 44 TYR H H 8.598 0.002 . 43 311 45 LYS H H 8.291 0.001 . stop_ save_