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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 15457

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PDB ID:
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15457
MolProbity Validation Chart

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Title: NMR Structure of the Talin Rod domain, 1655-1822   PubMed: 19297334

Deposition date: 2007-09-05 Original release date: 2009-03-09

Authors: Goult, Benjamin; Gingras, Alexandre; Bate, Neil; Critchley, David; Barsukov, Igor

Citation: Goult, Benjamin; Bate, Neil; Anthis, Nicholas; Wegener, Kate; Gingras, Alexandre; Patel, Bipin; Barsukov, Igor; Campbell, Iain; Roberts, Gordon; Critchley, David. "The Structure of an Interdomain Complex That Regulates Talin Activity"  J. Biol. Chem. 284, 15097-15106 (2009).

Assembly members:
1655-1822, polymer, 174 residues, 18254.602 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):
1655-1822: GIDPFTAPGQLECETAIAAL NSCLRDLDQASLAAVSQQLA PREGISQEALHTQMLTAVQE ISHLIEPLASAARAEASQLG HKVSQMAQYFEPLTLAAVGA ASKTLSHPQQMALLDQTKTL AESALQLLYTAKEAGGNPKQ AAHTQEALEEAVQMMTEAVE DLTTTLNEAASAAG

Data sets:
Data typeCount
13C chemical shifts708
15N chemical shifts172
1H chemical shifts1154

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
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Assembly:

Entity Assembly IDEntity NameEntity ID
11655-18221

Entities:

Entity 1, 1655-1822 174 residues - 18254.602 Da.

Residues 1-6 represent a non-native expression tag

1   GLYILEASPPROPHETHRALAPROGLYGLN
2   LEUGLUCYSGLUTHRALAILEALAALALEU
3   ASNSERCYSLEUARGASPLEUASPGLNALA
4   SERLEUALAALAVALSERGLNGLNLEUALA
5   PROARGGLUGLYILESERGLNGLUALALEU
6   HISTHRGLNMETLEUTHRALAVALGLNGLU
7   ILESERHISLEUILEGLUPROLEUALASER
8   ALAALAARGALAGLUALASERGLNLEUGLY
9   HISLYSVALSERGLNMETALAGLNTYRPHE
10   GLUPROLEUTHRLEUALAALAVALGLYALA
11   ALASERLYSTHRLEUSERHISPROGLNGLN
12   METALALEULEUASPGLNTHRLYSTHRLEU
13   ALAGLUSERALALEUGLNLEULEUTYRTHR
14   ALALYSGLUALAGLYGLYASNPROLYSGLN
15   ALAALAHISTHRGLNGLUALALEUGLUGLU
16   ALAVALGLNMETMETTHRGLUALAVALGLU
17   ASPLEUTHRTHRTHRLEUASNGLUALAALA
18   SERALAALAGLY

Samples:

unlabelled: 1655-1822 1 ± 0.05 mM; NaCl 50 mM

15n: 1655-1822, [U-100% 15N], 1 ± 0.05 mM; NaCl 50 mM

double: 1655-1822, [U-100% 13C; U-100% 15N], 1 ± 0.05 mM; NaCl 50 mM

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 308 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 HBHA(CO)NHdoubleisotropicsample_conditions_1
3D HN(CO)CAdoubleisotropicsample_conditions_1
3D HCCH-TOCSYdoubleisotropicsample_conditions_1
3D 1H-15N NOESY15nisotropicsample_conditions_1
3D 1H-13C NOESYdoubleisotropicsample_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:

PDB
DBJ BAA82979 BAC65702 BAE27781 BAE41923 BAE42391
EMBL CAA39588
GB AAD13152 AAF23322 AAF27330 AAH18557 AAH42923
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:
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SPARKY: Backbone or all simulated shifts