BMRB Entry 26774

Name: 1H, 13C, and 15N Resonance Assignments for the Ribosomal Protein S1 280-438 from Mycobacterium tuberculosis
Published: 2017-08-24

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR26774

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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 for the Ribosomal Protein S1 280-438 from Mycobacterium tuberculosis

Deposition date:

2016-04-11

Original release date:

2017-08-24

Authors:

Fu, Jinglin; Liao, Xinli; Huang, Biling; Lin, Donghai

Citation:

Citation: Fu, Jinglin; Huang, Biling; Lin, Donghai; Liao, Xinli. "Chemical shift assignments of Ribosomal protein S1 from Mycobacterium tuberculosis" Biomol. NMR Assign. 11, 133-136 (2017).
PubMed: 28258550

Assembly members:

Assembly members:
Mtb_ribosomal_S1, polymer, 168 residues, Formula weight is not available

Natural source:

Natural source: Common Name: high GC Gram+ Taxonomy ID: 83332 Superkingdom: not available Kingdom: not available Genus/species: Mycobacterium tuberculosis

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET-22b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Mtb_ribosomal_S1: MQEDPWRHFARTHAIGQIVP GKVTKLVPFGAFVRVEEGIE GLVHISELAERHVEVPDQVV AVGDDAMVKVIDIDLERRRI SLSLKQANEDYTEEFDPAKY GMADSYDEQGNYIFPEGFDA ETNEWLEGFEKQRAEWEARY AEAERRHKMHTAQMEKFAAA LEHHHHHH

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	662
15N chemical shifts	157
1H chemical shifts	1054

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	S1-like domains	1

Entities:

Entity 1, S1-like domains 168 residues - Formula weight is not available

1

MET

GLN

GLU

ASP

PRO

TRP

ARG

HIS

PHE

ALA

2

ARG

THR

HIS

ALA

ILE

GLY

GLN

ILE

VAL

PRO

3

GLY

LYS

VAL

THR

LYS

LEU

VAL

PRO

PHE

GLY

4

ALA

PHE

VAL

ARG

VAL

GLU

GLY

ILE

GLU

5

GLY

LEU

VAL

HIS

ILE

SER

GLU

LEU

ALA

GLU

6

ARG

HIS

VAL

GLU

VAL

PRO

ASP

GLN

VAL

7

ALA

VAL

GLY

ASP

ALA

MET

VAL

LYS

VAL

8

ILE

ASP

ILE

ASP

LEU

GLU

ARG

ILE

9

SER

LEU

SER

LEU

LYS

GLN

ALA

ASN

GLU

ASP

10

TYR

THR

GLU

PHE

ASP

PRO

ALA

LYS

TYR

11

GLY

MET

ALA

ASP

SER

TYR

ASP

GLU

GLN

GLY

12

ASN

TYR

ILE

PHE

PRO

GLU

GLY

PHE

ASP

ALA

13

GLU

THR

ASN

GLU

TRP

LEU

GLU

GLY

PHE

GLU

14

LYS

GLN

ARG

ALA

GLU

TRP

GLU

ALA

ARG

TYR

15

ALA

GLU

ALA

GLU

ARG

HIS

LYS

MET

HIS

16

THR

ALA

GLN

MET

GLU

LYS

PHE

ALA

17

LEU

GLU

HIS

Samples:

sample_1: Mtb ribosomal S1, [U-13C; U-15N], 0.5 mM; H2O 90%; D2O 10%; Na2HPO4 20 mM; NaCl 150 mM; PMSF 1 mM; NaN3 0.02%

sample_conditions_1: ionic strength: 150 mM; pH: 6.3; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D H(CCO)NH	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCO	sample_1	isotropic	sample_conditions_1
3D HCACO	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 HN(CO)CA	sample_1	isotropic	sample_conditions_1
3D HNCA	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_1	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1

Software:

CCPN vV2.4, CCPN - chemical shift assignment

NMR spectrometers:

Bruker Avance 850 MHz

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