BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
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BMRB Entry 15616

Title: NMR Structure of the F1 domain (residues 86-202) of the Talin FERM domain

Deposition date: 2008-01-04 Original release date: 2010-02-18

Authors: Goult, Benjamin; Elliott, Paul; Critchley, David; Barsukov, Igor

Citation: Goult, Benjamin; Elliott, Paul; Roberts, Gordon; Critchley, David; Barsukov, Igor. "The NMR Structure of the F0F1 double domain (Residues 1-202) from the talin FERM domain"  . ., .-..

Assembly members:
F1, polymer, 128 residues, 15001.2 Da.

Natural source:   Common Name: 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):
F1: SSGLVPRGSHMRPLKIRMLD GTVKTIMVDDSKTVTDMLMT ICARIGITNHDEYSLVRELM EEKKDEGTGTLRKDKTLLRD EKKMEKLKQKLHTDDELNWL DHGRTLREQGVEEHETLLLR RKFFYSDQ

Data sets:
Data typeCount
13C chemical shifts517
15N chemical shifts132
1H chemical shifts804

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1F11

Entities:

Entity 1, F1 128 residues - 15001.2 Da.

Residues 75 to 85 (SSGLVPRGSHM) represent a non-native expression tag

1   SERSERGLYLEUVALPROARGGLYSERHIS
2   METARGPROLEULYSILEARGMETLEUASP
3   GLYTHRVALLYSTHRILEMETVALASPASP
4   SERLYSTHRVALTHRASPMETLEUMETTHR
5   ILECYSALAARGILEGLYILETHRASNHIS
6   ASPGLUTYRSERLEUVALARGGLULEUMET
7   GLUGLULYSLYSASPGLUGLYTHRGLYTHR
8   LEUARGLYSASPLYSTHRLEULEUARGASP
9   GLULYSLYSMETGLULYSLEULYSGLNLYS
10   LEUHISTHRASPASPGLULEUASNTRPLEU
11   ASPHISGLYARGTHRLEUARGGLUGLNGLY
12   VALGLUGLUHISGLUTHRLEULEULEUARG
13   ARGLYSPHEPHETYRSERASPGLN

Samples:

unlabelled: F1 1 ± 0.05 mM; sodium chloride 50 ± 0.05 mM; DTT 2 ± 0.05 mM; sodium phosphate 20 ± 0.05 mM; H2O 90%; D2O 10%

15n: F1, [U-100% 15N], 1 ± 0.05 mM; sodium chloride 50 ± 0.05 mM; DTT 2 ± 0.05 mM; H2O 90%; D2O 10%

double: F1, [U-100% 13C; U-100% 15N], 1 ± 0.05 mM; sodium chloride 50 ± 0.05 mM; DTT 2 ± 0.05 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQC15nisotropicsample_conditions_1
2D 1H-13C HSQCdoubleisotropicsample_conditions_1
3D CBCA(CO)NHdoubleisotropicsample_conditions_1
3D HNCOdoubleisotropicsample_conditions_1
3D HNCAdoubleisotropicsample_conditions_1
3D HNCACBdoubleisotropicsample_conditions_1
3D HCCH-TOCSYdoubleisotropicsample_conditions_1
3D 1H-13C NOESYdoubleisotropicsample_conditions_1
3D 1H-15N NOESY15nisotropicsample_conditions_1

Software:

TOPSPIN v2.0, Bruker Biospin - collection, processing

Analysis v1.015, CCPN - chemical shift assignment, data analysis, peak picking

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

ARIA v1.2, Linge, O, . - refinement

NMR spectrometers:

  • Bruker DRX 600 MHz
  • Bruker DRX 600 MHz
  • Bruker DRX 800 MHz

Related Database Links:

BMRB 15615
PDB
DBJ BAA82979 BAC30516 BAC65702 BAE27781 BAG09941
EMBL CAA39588
GB AAD13152 AAF23322 AAF27330 AAH42923 AAI50811
PRF 1617167A
REF NP_001034114 NP_006280 NP_035732 XP_001084941 XP_001504543
SP P26039 Q9Y490

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