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 26518

Title: NMR solution structure of the putative transfer protein TraH from Gram-positive conjugative plasmid pIP501   PubMed: 27103580

Deposition date: 2015-02-23 Original release date: 2016-07-13

Authors: Meyer, Niels Helge; Fercher, C.; Zangger, K.; Keller, W.

Citation: Fercher, Christian; Probst, Ines; Kohler, Verena; Goessweiner-Mohr, Nikolaus; Arends, Karsten; Grohmann, Elisabeth; Zangger, Klaus; Meyer, N. Helge; Keller, Walter. "VirB8-like protein TraH is crucial for DNA transfer in Enterococcus faecalis"  Sci. Rep. 6, 24643-24643 (2016).

Assembly members:
TRAH, polymer, 128 residues, 14896.3656 Da.

Natural source:   Common Name: Enterococcus faecalis   Taxonomy ID: 1351   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Enterococcus faecalis

Experimental source:   Production method: recombinant technology   Host organism: ESCHERICHIA COLI BL21

Entity Sequences (FASTA):
TRAH: SNTNQSESEKIIKEFYKTVY NYEKSQKEISMTTVKELATD NVYQELQNEINVNNSYSPQQ NTIQKSSVNENEIKILAYES KDNSQQYLVTAPIHQVFNGT KNDFEINQLIQIKNQKITQR TTIQLGEE

Data sets:
Data typeCount
13C chemical shifts563
15N chemical shifts147
1H chemical shifts925

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1TRAH1

Entities:

Entity 1, TRAH 128 residues - 14896.3656 Da.

1   SERASNTHRASNGLNSERGLUSERGLULYS
2   ILEILELYSGLUPHETYRLYSTHRVALTYR
3   ASNTYRGLULYSSERGLNLYSGLUILESER
4   METTHRTHRVALLYSGLULEUALATHRASP
5   ASNVALTYRGLNGLULEUGLNASNGLUILE
6   ASNVALASNASNSERTYRSERPROGLNGLN
7   ASNTHRILEGLNLYSSERSERVALASNGLU
8   ASNGLUILELYSILELEUALATYRGLUSER
9   LYSASPASNSERGLNGLNTYRLEUVALTHR
10   ALAPROILEHISGLNVALPHEASNGLYTHR
11   LYSASNASPPHEGLUILEASNGLNLEUILE
12   GLNILELYSASNGLNLYSILETHRGLNARG
13   THRTHRILEGLNLEUGLYGLUGLU

Samples:

sample_1: TRAH, [U-13C; U-15N], 0.5 mM; PO4 50 mM; NaCl 100 mM

sample_conditions_1: ionic strength: 200.000 mM; pH: 6.500; pressure: 1.000 atm; temperature: 298.000 K

Experiments:

NameSampleSample stateSample conditions
NOESYsample_1solutionsample_conditions_1

Software:

AutoDep v4.3, PDBe - chemical shift assignment

CNS vany, Brunger, Adams, Clore, Gros, Nilges and Read - chemical shift assignment

CYANA vany, Guntert, Mumenthaler and Wuthrich - chemical shift assignment

RECOORD_CNS vany, A.J. NEDERVEEN, J.F. DORELEIJERS, W.F. - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 700 MHz

Related Database Links:

UNP R4CA00_ENTFL

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