BMRB Entry 26985

Name: 1H, 13C and 15N resonance assignments of SmpB from Mycobacterium tuberculosis
Published: 2017-04-26

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26985

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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:

1H, 13C and 15N resonance assignments of SmpB from Mycobacterium tuberculosis

Deposition date:

2016-12-23

Original release date:

2017-04-26

Authors:

Yang, Juanjuan; Lin, Donghai; Liu, Yindi

Citation:

Citation: Yang, Juanjuan; Liu, Yindi; Liu, Zhao; Meng, Chun; Lin, Donghai. "Backbone and side-chain resonance assignments for the tmRNA-binding protein, SmpB, from Mycobacterium tuberculosis" Biomol. NMR Assign. ., .-. (2017).
PubMed: 28258549

Assembly members:

Assembly members:
SmpB, polymer, 151 residues, Formula weight is not available

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: pET-28(a)

Entity Sequences (FASTA):

Entity Sequences (FASTA):
SmpB: MGSSHHHHHHSSGLVPRGSH MSSRGGRQIVASNRKARHNY SIIEVFEAGVALQGTEVKSL REGQASLADSFATIDDGEVW LRNAHIPEYRHGSWTNHEPR RNRKLLLHRRQIDTLVGKIR EGNFALVPLSLYFAEGKVKV ELALARGKQAR

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	502
15N chemical shifts	130
1H chemical shifts	854

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	SmpB	1

Entities:

Entity 1, SmpB 151 residues - Formula weight is not available

1

MET

GLY

SER

HIS

2

SER

GLY

LEU

VAL

PRO

ARG

GLY

SER

HIS

3

MET

SER

ARG

GLY

ARG

GLN

ILE

VAL

4

ALA

SER

ASN

ARG

LYS

ALA

ARG

HIS

ASN

TYR

5

SER

ILE

GLU

VAL

PHE

GLU

ALA

GLY

VAL

6

ALA

LEU

GLN

GLY

THR

GLU

VAL

LYS

SER

LEU

7

ARG

GLU

GLY

GLN

ALA

SER

LEU

ALA

ASP

SER

8

PHE

ALA

THR

ILE

ASP

GLY

GLU

VAL

TRP

9

LEU

ARG

ASN

ALA

HIS

ILE

PRO

GLU

TYR

ARG

10

HIS

GLY

SER

TRP

THR

ASN

HIS

GLU

PRO

ARG

11

ARG

ASN

ARG

LYS

LEU

HIS

ARG

12

GLN

ILE

ASP

THR

LEU

VAL

GLY

LYS

ILE

ARG

13

GLU

GLY

ASN

PHE

ALA

LEU

VAL

PRO

LEU

SER

14

LEU

TYR

PHE

ALA

GLU

GLY

LYS

VAL

LYS

VAL

15

GLU

LEU

ALA

LEU

ALA

ARG

GLY

LYS

GLN

ALA

16

ARG

Samples:

sample_1: SmpB, [U-100% 13C; U-100% 15N], 1.0 mM

sample_conditions_1: ionic strength: 0.15 M; pH: 6.6; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HCACO	sample_1	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 HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1

Software:

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

SPARKY, Goddard - chemical shift assignment

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

Bruker AMX 850 MHz

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