BMRB Entry 19088

Name: Backbone chemical shift assignment of Rv2140c, a phosphatidylethanolamine binding protein from Mycobacterium tuberculosis
Published: 2013-08-14

Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR19088

NMR-STAR file interactive viewer.
NMR-STAR v3 text file.
XML gzip file.
RDF gzip file.
All files associated with the entry

Nicholas Rego and David Koes
3Dmol.js: molecular visualization with WebGL
Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

Select model:

I am color blind

Download raw data. Direct link to this display. Help

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

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Rv2140c: MATSPDPYAALPKLPSFSLT STSITDGQPLATPQVSGIMG AGGADASPQLRWSGFPSETR SFAVTVYDPDAPTLSGFWHW AVANLPANVTELPEGVGDGR ELPGGALTLVNDAGMRRYVG AAPPPGHGVHRYYVAVHAVK VEKLDLPEDASPAYLGFNLF QHAIARAVIFGTYEQR

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list

Data type	Count
13C chemical shifts	308
15N chemical shifts	155
1H chemical shifts	155

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Rv2140c	1

Entities:

Entity 1, Rv2140c 176 residues - 18603.878 Da.

1

MET

ALA

THR

SER

PRO

ASP

PRO

TYR

ALA

2

LEU

PRO

LYS

LEU

PRO

SER

PHE

SER

LEU

THR

3

SER

THR

SER

ILE

THR

ASP

GLY

GLN

PRO

LEU

4

ALA

THR

PRO

GLN

VAL

SER

GLY

ILE

MET

GLY

5

ALA

GLY

ALA

ASP

ALA

SER

PRO

GLN

LEU

6

ARG

TRP

SER

GLY

PHE

PRO

SER

GLU

THR

ARG

7

SER

PHE

ALA

VAL

THR

VAL

TYR

ASP

PRO

ASP

8

ALA

PRO

THR

LEU

SER

GLY

PHE

TRP

HIS

TRP

9

ALA

VAL

ALA

ASN

LEU

PRO

ALA

ASN

VAL

THR

10

GLU

LEU

PRO

GLU

GLY

VAL

GLY

ASP

GLY

ARG

11

GLU

LEU

PRO

GLY

ALA

LEU

THR

LEU

VAL

12

ASN

ASP

ALA

GLY

MET

ARG

TYR

VAL

GLY

13

ALA

PRO

GLY

HIS

GLY

VAL

HIS

14

ARG

TYR

VAL

ALA

VAL

HIS

ALA

VAL

LYS

15

VAL

GLU

LYS

LEU

ASP

LEU

PRO

GLU

ASP

ALA

16

SER

PRO

ALA

TYR

LEU

GLY

PHE

ASN

LEU

PHE

17

GLN

HIS

ALA

ILE

ALA

ARG

ALA

VAL

ILE

PHE

18

GLY

THR

TYR

GLU

GLN

ARG

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:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	Rv2140c_1	isotropic	CondSet1
3D HNCA	Rv2140c_1	isotropic	CondSet1
3D HN(CO)CA	Rv2140c_1	isotropic	CondSet1
3D HNCO	Rv2140c_1	isotropic	CondSet1
3D HN(CA)CO	Rv2140c_1	isotropic	CondSet1

Software:

ANALYSIS v2.1, CCPN - resonance assignment

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

NMR spectrometers:

Bruker DMX 750 MHz

PDB	4BEG
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 P9WFN0 P9WFN1