BMRB Entry 17363

Title:
NMR Structure of the B domain of talin
Deposition date:
2010-12-14
Original release date:
2012-08-30
Authors:
Goult, Benjamin; Gingras, Alexandre; Bate, Neil; Barsukov, Igor; Roberts, Gordon; Critchley, David
Citation:

Citation: Goult, Benjamin; Gingras, Alexandre; Bate, Neil; Barsukov, Igor; Roberts, Gordon; Critchley, David. "The Complete Domain Structure of Talin"  .

Assembly members:

Assembly members:
DomB, polymer, 168 residues, Formula weight is not available

Natural source:

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

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: Pet 151

Data sets:
Data typeCount
13C chemical shifts647
15N chemical shifts164
1H chemical shifts1094

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1DomB1

Entities:

Entity 1, DomB 168 residues - Formula weight is not available

Residues 1-6 (1040-1045) represent a non-native affinity tag

1   GLYILEASPPROPHETHRGLYPROLEUGLU
2   METASPSERALALEUSERVALVALGLNASN
3   LEUGLULYSASPLEUGLNGLUILELYSALA
4   ALAALAARGASPGLYLYSLEULYSPROLEU
5   PROGLYGLUTHRMETGLULYSCYSTHRGLN
6   ASPLEUGLYASNSERTHRLYSALAVALSER
7   SERALAILEALALYSLEULEUGLYGLUILE
8   ALAGLNGLYASNGLUASNTYRALAGLYILE
9   ALAALAARGASPVALALAGLYGLYLEUARG
10   SERLEUALAGLNALAALAARGGLYVALALA
11   ALALEUTHRSERASPPROALAVALGLNALA
12   ILEVALLEUASPTHRALASERASPVALLEU
13   ASPLYSALASERSERLEUILEGLUGLUALA
14   LYSLYSALASERGLYHISPROGLYASPPRO
15   GLUSERGLNGLNARGLEUALAGLNVALALA
16   LYSALAVALTHRGLNALALEUASNARGCYS
17   VALSERCYSLEUPROGLYGLNARG

Samples:

15N: DomB, [U-100% 15N], 1 ± 0.01 mM; D2O, [U-100% 2H], 10 ± 0.1 %; H2O 90%; DTT 2 ± 0.1 mM; sodium chloride 50 ± 0.1 mM; sodium phosphate 20 ± 0.1 mM

double: DomB, [U-100% 13C; U-100% 15N], 1 ± 0.01 mM; D2O, [U-100% 2H], 10 ± 0.1 %; H2O 90%; DTT 2 ± 0.1 mM; sodium chloride 50 ± 0.1 mM; sodium phosphate 20 ± 0.1 mM

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 1H-15N NOESY15Nisotropicsample_conditions_1
3D 1H-13C NOESYdoubleisotropicsample_conditions_1
3D HNCOdoubleisotropicsample_conditions_1
3D HNCAdoubleisotropicsample_conditions_1
3D HNCACBdoubleisotropicsample_conditions_1
3D HCCH-TOCSYdoubleisotropicsample_conditions_1
3D HN(CO)CAdoubleisotropicsample_conditions_1
3D CBCA(CO)NHdoubleisotropicsample_conditions_1

Software:

TOPSPIN v2.1, Bruker Biospin - collection, processing

TALOS, Cornilescu, Delaglio and Bax - data analysis, geometry optimization

CYANA, Guntert, Mumenthaler and Wuthrich - chemical shift assignment, geometry optimization, structure solution

ARIA v1.2, Linge, O'Donoghue and Nilges - geometry optimization, refinement, structure solution

NMR spectrometers:

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

Related Database Links:

PDB
DBJ BAA82979 BAC65702 BAE27781 BAG09941
EMBL CAA39588
GB AAF27330 AAH42923 AAI00263 AAI50811 EAW58352
PRF 1617167A
REF NP_006280 NP_035732 XP_002819691 XP_003470907 XP_003732055
SP P26039 Q9Y490
AlphaFold P26039 Q9Y490

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