BMRB Entry 15411

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR15411
MolProbity Validation Chart

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Title:
NMR structure of the talin C-terminal actin binding site
Deposition date:
2007-07-30
Original release date:
2008-01-17
Authors:
Goult, Benjamin; Gingras, Alexandre; Bate, Neil; Critchley, David; Barsukov, Igor
Citation:

Citation: Goult, Benjamin; Gingras, Alexandre; Bate, Neil; Roberts, Gordon; Critchley, David; Barsukov, Igor. "NMR assignment of the C-terminal actin-binding domain of talin"  Biomol. NMR Assignments 2, 17-19 (2008).
PubMed: 19636914

Assembly members:

Assembly members:
Talin_c-terminal_actin_binding_site_(ABS3), polymer, 189 residues, 19385.072 Da.

Natural source:

Natural source:   Common Name: not available   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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Talin_c-terminal_actin_binding_site_(ABS3): GIDPFTDPTVIAENELLGAA AAIEAAAKKLEQLKPRAKPK EADESLNFEEQILEAAKSIA AATSALVKAASAAQRELVAQ GKVGAIPANALDDGQWSQGL ISAARMVAAATNNLCEAANA AVQGHASQEKLISSAKQVAA STAQLLVACKVKADQDSEAM KRLQAAGNAVKRASDNLVKA AQKAAAFED

Data sets:
Data typeCount
13C chemical shifts774
15N chemical shifts203
1H chemical shifts1285

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Talin c-terminal acting binding domain1

Entities:

Entity 1, Talin c-terminal acting binding domain 189 residues - 19385.072 Da.

Residues 1-6 represent a non-native affinity tag

1   GLYILEASPPROPHETHRASPPROTHRVAL
2   ILEALAGLUASNGLULEULEUGLYALAALA
3   ALAALAILEGLUALAALAALALYSLYSLEU
4   GLUGLNLEULYSPROARGALALYSPROLYS
5   GLUALAASPGLUSERLEUASNPHEGLUGLU
6   GLNILELEUGLUALAALALYSSERILEALA
7   ALAALATHRSERALALEUVALLYSALAALA
8   SERALAALAGLNARGGLULEUVALALAGLN
9   GLYLYSVALGLYALAILEPROALAASNALA
10   LEUASPASPGLYGLNTRPSERGLNGLYLEU
11   ILESERALAALAARGMETVALALAALAALA
12   THRASNASNLEUCYSGLUALAALAASNALA
13   ALAVALGLNGLYHISALASERGLNGLULYS
14   LEUILESERSERALALYSGLNVALALAALA
15   SERTHRALAGLNLEULEUVALALACYSLYS
16   VALLYSALAASPGLNASPSERGLUALAMET
17   LYSARGLEUGLNALAALAGLYASNALAVAL
18   LYSARGALASERASPASNLEUVALLYSALA
19   ALAGLNLYSALAALAALAPHEGLUASP

Samples:

unlabelled: Talin c-terminal actin binding site (ABS3) 1 ± 0.1 mM; Sodium Phosphate 20 mM; NaCl 50 mM; DTT 2 mM; H2O 90%; D2O 10%

15N: Talin c-terminal actin binding site (ABS3), [U-15N], 1 ± 0.1 mM; Sodium Phosphate 20 mM; NaCl 50 mM; DTT 2 mM; H2O 90%; D2O 10%

double: Talin c-terminal actin binding site (ABS3), [U-13C; U-15N], 1 ± 0.1 mM; Sodium Phosphate 20 mM; NaCl 50 mM; DTT 2 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 50 mM; pH: 6.0; pressure: 1 atm; temperature: 318.15 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQC15Nisotropicsample_conditions_1
2D 1H-13C HSQCdoubleisotropicsample_conditions_1
3D HNCOdoubleisotropicsample_conditions_1
3D HNCAdoubleisotropicsample_conditions_1
3D CBCA(CO)NHdoubleisotropicsample_conditions_1
3D HNCACBdoubleisotropicsample_conditions_1
3D HCCH-TOCSYdoubleisotropicsample_conditions_1
3D 1H-15N NOESY15Nisotropicsample_conditions_1
3D 1H-13C NOESYdoubleisotropicsample_conditions_1
3D HBHA(CO)NHdoubleisotropicsample_conditions_1
2D 1H-1H TOCSYunlabelledisotropicsample_conditions_1
2D 1H-1H NOESYunlabelledisotropicsample_conditions_1
3D HN(CO)CAdoubleisotropicsample_conditions_1
4D 13C, 13C HMQC-NOESY-HSQCdoubleisotropicsample_conditions_1

Software:

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

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - chemical shift assignment, chemical shift calculation, structure solution

TOPSPIN, Bruker Biospin - collection, processing

ANALYSIS v11, CCPN - chemical shift assignment, peak picking

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

NMR spectrometers:

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

Related Database Links:

PDB
DBJ BAA82979 BAC65702 BAE27781 BAE41923 BAE42391
EMBL CAA39588
GB AAD13152 AAF23322 AAF27330 AAH18557 AAH42923
PRF 1617167A
REF NP_001034114 NP_001192357 NP_006280 NP_035732 XP_001504543
SP P26039 Q9Y490
TPG DAA26829
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