BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 26880

Title: 1H, 13C and 15N backbone assignments of the R3 domain of talin (residues 781-911) carrying four mutations T809I, T833V, T867V and T901I (R3-IVVI)   PubMed: 29153504

Deposition date: 2016-08-23 Original release date: 2018-06-26

Authors: Baxter, Nicola; Williamson, Mike; Barsukov, Igor

Citation: Baxter, Nicola; Zacharchenko, Thomas; Barsukov, Igor; Williamson, Mike. "Pressure-Dependent Chemical Shifts in the R3 Domain of Talin Show that It Is Thermodynamically Poised for Binding to Either Vinculin or RIAM"  Structure 25, 1856-11866.e2 (2017).

Assembly members:
R3-IVVI_protein, polymer, 131 residues, Formula weight is not available

Natural source:   Common Name: house mouse   Taxonomy ID: 10090   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Mus musculus

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

Entity Sequences (FASTA):
R3-IVVI_protein: GIDPFTAHATGAGPAGRYDQ ATDTILTVIENIFSSMGDAG EMVRQARILAQAVSDLVNAI KADAEGESDLENSRKLLSAA KILADAVAKMVEAAKGAAAH PDSEEQQQRLREAAEGLRMA INAAAQNAIKK

Data sets:
Data typeCount
13C chemical shifts392
15N chemical shifts138
1H chemical shifts150

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1R3-IVVI1

Entities:

Entity 1, R3-IVVI 131 residues - Formula weight is not available

Residues 1-6 (781-786) represent a non-native affinity tag

1   GLYILEASPPROPHETHRALAHISALATHR
2   GLYALAGLYPROALAGLYARGTYRASPGLN
3   ALATHRASPTHRILELEUTHRVALILEGLU
4   ASNILEPHESERSERMETGLYASPALAGLY
5   GLUMETVALARGGLNALAARGILELEUALA
6   GLNALAVALSERASPLEUVALASNALAILE
7   LYSALAASPALAGLUGLYGLUSERASPLEU
8   GLUASNSERARGLYSLEULEUSERALAALA
9   LYSILELEUALAASPALAVALALALYSMET
10   VALGLUALAALALYSGLYALAALAALAHIS
11   PROASPSERGLUGLUGLNGLNGLNARGLEU
12   ARGGLUALAALAGLUGLYLEUARGMETALA
13   ILEASNALAALAALAGLNASNALAILELYS
14   LYS

Samples:

sample_1: R3-IVVI protein, [U-100% 13C; U-100% 15N], 0.75 mM; sodium phosphate 20 mM; sodium chloride 150 mM; TCEP 0.5 mM; TSP, [U-2H], 0.4 mM; D2O, [U-100% 2H], 10%; H2O 90%

sample_conditions_1: ionic strength: 170 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HN(CA)COsample_1isotropicsample_conditions_1
2D HN(CO)CACBsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

Felix, Accelrys Software Inc. - chemical shift assignment, data analysis, processing

NMR spectrometers:

  • Bruker Avance 800 MHz
  • Bruker DRX 500 MHz

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts