BMRB Entry 19088

Title:
Backbone chemical shift assignment of Rv2140c, a phosphatidylethanolamine binding protein from Mycobacterium tuberculosis
Deposition date:
2013-03-13
Original release date:
2013-08-14
Authors:
Eulenberg, Georg; Higman, Victoria; Diehl, Anne; Wilmanns, Matthias; Holton, Simon
Citation:

Citation: Eulenburg, Georg; Higman, Victoria; Diehl, Anne; Wilmanns, Matthias; Holton, Simon. "Structural and biochemical characterization of Rv2140c, a phosphatidylethanolamine-binding protein from Mycobacterium tuberculosis."  FEBS Lett. 587, 2936-2942 (2013).
PubMed: 23907008

Assembly members:

Assembly members:
Rv2140c, polymer, 176 residues, 18603.878 Da.

Natural source:

Natural source:   Common Name: Mycobacterium tuberculosis   Taxonomy ID: 1773   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Mycobacterium tuberculosis

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pETM-11

Data sets:
Data typeCount
13C chemical shifts308
15N chemical shifts155
1H chemical shifts155

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Rv2140c1

Entities:

Entity 1, Rv2140c 176 residues - 18603.878 Da.

1   METALATHRSERPROASPPROTYRALAALA
2   LEUPROLYSLEUPROSERPHESERLEUTHR
3   SERTHRSERILETHRASPGLYGLNPROLEU
4   ALATHRPROGLNVALSERGLYILEMETGLY
5   ALAGLYGLYALAASPALASERPROGLNLEU
6   ARGTRPSERGLYPHEPROSERGLUTHRARG
7   SERPHEALAVALTHRVALTYRASPPROASP
8   ALAPROTHRLEUSERGLYPHETRPHISTRP
9   ALAVALALAASNLEUPROALAASNVALTHR
10   GLULEUPROGLUGLYVALGLYASPGLYARG
11   GLULEUPROGLYGLYALALEUTHRLEUVAL
12   ASNASPALAGLYMETARGARGTYRVALGLY
13   ALAALAPROPROPROGLYHISGLYVALHIS
14   ARGTYRTYRVALALAVALHISALAVALLYS
15   VALGLULYSLEUASPLEUPROGLUASPALA
16   SERPROALATYRLEUGLYPHEASNLEUPHE
17   GLNHISALAILEALAARGALAVALILEPHE
18   GLYTHRTYRGLUGLNARG

Samples:

Rv2140c_1: Rv2140c, [[U-95% 13C; U-95% 15N]], 0.36 mM; Sodium Chloride 50.00 mM; Phophate buffer 20.00 mM

CondSet1: pH: 7.000; temperature: 300 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCRv2140c_1isotropicCondSet1
3D HNCARv2140c_1isotropicCondSet1
3D HN(CO)CARv2140c_1isotropicCondSet1
3D HNCORv2140c_1isotropicCondSet1
3D HN(CA)CORv2140c_1isotropicCondSet1

Software:

ANALYSIS v2.1, CCPN - resonance assignment

XWIN-NMR v3.5, Bruker Biospin - data acquisition, data processing

NMR spectrometers:

  • Bruker DMX 750 MHz

Related Database Links:

PDB
DBJ BAH26435 BAL66151 BAQ06208 GAA45837
EMBL CAL72145 CCC27222 CCC44496 CCC64734 CCE37614
GB AAK46482 ABQ73916 ABR06501 ACT24902 AEB03982
REF NP_216656 NP_855813 WP_003411119 WP_003903767 WP_003904790
SP P67227 P9WFN0 P9WFN1
AlphaFold P67227 P9WFN1 P9WFN0

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