BMRB Entry 15638

Name: Backbone 1H, 15N and 13C assignment of Rv1567c, an integral membrane protein from Mycobacterium tuberculosis
Published: 2008-06-05

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PDB ID: 2n48
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full
BMRB Entry DOI: doi:10.13018/BMR15638
MolProbity Validation Chart

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

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Title:

Backbone 1H, 15N and 13C assignment of Rv1567c, an integral membrane protein from Mycobacterium tuberculosis

Deposition date:

2008-01-25

Original release date:

2008-06-05

Authors:

Nguyen, Hau; Cross, Timothy

Citation:

Citation: Nguyen, Hau; Cross, Timothy. "1H, 15N and 13C backbone resonance assignment of Rv1567c, an integral membrane protein from Mycobacterium tuberculosis" Biomol. NMR Assignments 2, 47-49 (2008).
PubMed: 19636922

Assembly members:

Assembly members:
Rv1567c, polymer, 97 residues, 10362.2 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: pET15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Rv1567c: GSHMVTMTSWPSRLFAFTDN VCPPDACPLVPFGVNYYIYP VMWGGIGAAIATAVIGPFVS MLKGWYMSFWPIISIAVITV TSIAGYAIAGFSERYWH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	166
15N chemical shifts	83
1H chemical shifts	83

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Rv1567c	1

Entities:

Entity 1, Rv1567c 97 residues - 10362.2 Da.

Residue 1 to 3 (GSH) represent cloning artifact residues

1

GLY

SER

HIS

MET

VAL

THR

MET

THR

SER

TRP

2

PRO

SER

ARG

LEU

PHE

ALA

PHE

THR

ASP

ASN

3

VAL

CYS

PRO

ASP

ALA

CYS

PRO

LEU

VAL

4

PRO

PHE

GLY

VAL

ASN

TYR

ILE

TYR

PRO

5

VAL

MET

TRP

GLY

ILE

GLY

ALA

ILE

6

ALA

THR

ALA

VAL

ILE

GLY

PRO

PHE

VAL

SER

7

MET

LEU

LYS

GLY

TRP

TYR

MET

SER

PHE

TRP

8

PRO

ILE

SER

ILE

ALA

VAL

ILE

THR

VAL

9

THR

SER

ILE

ALA

GLY

TYR

ALA

ILE

ALA

GLY

10

PHE

SER

GLU

ARG

TYR

TRP

HIS

Samples:

sample_1: Rv1567c, [U-99% 13C; U-99% 15N], 1 ± 0.2 mM

sample_2: Rv1567c, [U-99% 15N], 1 ± 0.2 mM

sample_conditions_1: ionic strength: 10 mM; pH: 4; pressure: 1 atm; temperature: 323 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

SPARKY, Goddard - data analysis, peak picking

NMR spectrometers:

Varian INOVA 600 MHz
Varian INOVA 720 MHz

GB	886349 AAB96955 AAK45885 ABQ73324 ABR05943 ACT25484
SWS	O06623
DBJ	BAH25883 BAL65539 BAQ05567 GAA45311
EMBL	CAL71607 CCC26666 CCC43922 CCC64180 CCE37081
REF	NP_216083 NP_855246 WP_003407802 WP_003911567 WP_020424437