BMRB Entry 17312

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR17312
MolProbity Validation Chart

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Title:
Tah1 complexed by MEEVD
Deposition date:
2010-11-22
Original release date:
2012-01-04
Authors:
Jimenez, Beatriz; Ugwu, Francisca; Zhao, Rongmin; Orti, Leticia; Houry, Walid; Pineda-Lucena, Antonio
Citation:

Citation: Jimenez, Beatriz; Ugwu, Francisca; Zhao, Rongmin; Orti, Leticia; Makhnevych, Taras; Pineda-Lucena, Antonio; Houry, Walid. "Structure of minimal tetratricopeptide repeat domain protein Tah1 reveals mechanism of its interaction with Pih1 and Hsp90."  J. Biol. Chem. 287, 5698-5709 (2012).
PubMed: 22179618

Assembly members:

Assembly members:
Tah1, polymer, 111 residues, 12567 Da.
MEEVD, polymer, 5 residues, 12567 Da.

Natural source:

Natural source:   Common Name: Baker's yeast   Taxonomy ID: 4932   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Saccharomyces cerevisiae

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pRIL

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Tah1: MSQFEKQKEQGNSLFKQGLY REAVHCYDQLITAQPQNPVG YSNKAMALIKLGEYTQAIQM CQQGLRYTSTAEHVAIRSKL QYRLELAQGAVGSVQIPVVE VDELPEGYDRS
MEEVD: MEEVD

Data sets:
Data typeCount
13C chemical shifts537
15N chemical shifts117
1H chemical shifts839

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1molecule 11
2molecule 22

Entities:

Entity 1, molecule 1 111 residues - 12567 Da.

Tah1 is a TPR repeat-containing protein associated with Hsp90

1   METSERGLNPHEGLULYSGLNLYSGLUGLN
2   GLYASNSERLEUPHELYSGLNGLYLEUTYR
3   ARGGLUALAVALHISCYSTYRASPGLNLEU
4   ILETHRALAGLNPROGLNASNPROVALGLY
5   TYRSERASNLYSALAMETALALEUILELYS
6   LEUGLYGLUTYRTHRGLNALAILEGLNMET
7   CYSGLNGLNGLYLEUARGTYRTHRSERTHR
8   ALAGLUHISVALALAILEARGSERLYSLEU
9   GLNTYRARGLEUGLULEUALAGLNGLYALA
10   VALGLYSERVALGLNILEPROVALVALGLU
11   VALASPGLULEUPROGLUGLYTYRASPARG
12   SER

Entity 2, molecule 2 5 residues - 12567 Da.

Pentapeptide: Ac-MEEVD It is the C-terminus part of Hsp90

1   METGLUGLUVALASP

Samples:

sample_1: Tah1, [U-99% 15N], 1 mM; Ac-MEEVD 2 mM; sodium phosphate 25 mM; sodium chloride 100 mM; H2O 90%; D2O 10%

sample_2: Tah1, [U-99% 13C; U-99% 15N], 1 mM; Ac-MEEVD 2 mM; sodium phosphate 25 mM; sodium chloride 100 mM; H2O 90%; D2O 10%

sample_3: Tah1 800 uM; Ac-MEEVD 1.6 mM; sodium phosphate 25 mM; sodium chloride 100 mM; H2O 90%; D2O 10%

sample_4: Tah1, [U-98% 13C; U-98% 15N], 1 mM; Ac-MEEVD 2 mM; sodium phosphate 25 mM; sodium chloride 100 mM; D2O 100%

sample_conditions_1: ionic strength: 0.1375 M; pH: 8; pressure: 1 atm; temperature: 293 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_3isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D H(CCO)NHsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_4isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_4isotropicsample_conditions_1
2D 15N edited 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 13C-13C COSYsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_4isotropicsample_conditions_1

Software:

CARA v1.8.4, Prof. Wuthrich Group - chemical shift assignment

TOPSPIN v1.3, Bruker Biospin - collection, processing

UNIO v1.0.4, Torsten Herrmann Copyright 2002-2010 - data analysis, peak picking, structure solution

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - refinement, structure solution

AMBER v10, Case, Darden, Cheatham, III, Simmerling, Wang, Duke, Luo, ... and Kollm - refinement

TALOS voriginal, Cornilescu, Delaglio and Bax - data analysis

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 900 MHz

Related Database Links:

UNP P25638
BMRB 18445 18447
PDB
DBJ GAA21965
EMBL CAA42288 CAY78265
GB AAS56477 AHN96120 AHV79323 AHY79733 AJP37484
REF NP_009986
SP P25638
TPG DAA07534
AlphaFold D6VR65 P25638

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks