BMRB Entry 19907

Name: NMR resonance assignment of the archaeal ribosomal protein L7Ae
Published: 2019-07-12

Chem Shift validation: AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR19907

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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:

NMR resonance assignment of the archaeal ribosomal protein L7Ae

Deposition date:

2014-04-11

Original release date:

2019-07-12

Authors:

Moschen, Thomas; Wunderlich, Christoph; Kreutz, Christoph; Tollinger, Martin

Citation:

Citation: Moschen, Thomas; Wunderlich, Christoph; Kreutz, Christoph; Tollinger, Martin. "NMR resonance assignments of the archaeal ribosomal protein L7Ae in the apo form and bound to a 25 nt RNA" Biomol. NMR Assign. 9, 177-180 (2015).
PubMed: 25030110

Assembly members:

Assembly members:
L7Ae_apo, polymer, 121 residues, 13123.3 Da.

Natural source:

Natural source: Common Name: euryarchaeotes Taxonomy ID: 2190 Superkingdom: Archaea Kingdom: not available Genus/species: Methanococcus jannaschii

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: pET28a

Entity Sequences (FASTA):

Entity Sequences (FASTA):
L7Ae_apo: RGSHMAVYVKFKVPEEIQKE LLDAVAKAQKIKKGANEVTK AVERGIAKLVIIAEDVKPEE VVAHLPYLCEEKGIPYAYVA SKQDLGKAAGLEVAASSVAI INEGDAEELKVLIEKVNVLK Q

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_L7Ae

Data type	Count
13C chemical shifts	338
15N chemical shifts	111
1H chemical shifts	232

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	L7Ae apo	1

Entities:

Entity 1, L7Ae apo 121 residues - 13123.3 Da.

first 4 residues are left from cleavage with thrombin

1

ARG

GLY

SER

HIS

MET

ALA

VAL

TYR

VAL

LYS

2

PHE

LYS

VAL

PRO

GLU

ILE

GLN

LYS

GLU

3

LEU

ASP

ALA

VAL

ALA

LYS

ALA

GLN

LYS

4

ILE

LYS

GLY

ALA

ASN

GLU

VAL

THR

LYS

5

ALA

VAL

GLU

ARG

GLY

ILE

ALA

LYS

LEU

VAL

6

ILE

ALA

GLU

ASP

VAL

LYS

PRO

GLU

7

VAL

ALA

HIS

LEU

PRO

TYR

LEU

CYS

GLU

8

GLU

LYS

GLY

ILE

PRO

TYR

ALA

TYR

VAL

ALA

9

SER

LYS

GLN

ASP

LEU

GLY

LYS

ALA

GLY

10

LEU

GLU

VAL

ALA

SER

VAL

ALA

ILE

11

ILE

ASN

GLU

GLY

ASP

ALA

GLU

LEU

LYS

12

VAL

LEU

ILE

GLU

LYS

VAL

ASN

VAL

LEU

LYS

13

GLN

Samples:

sample: L7Ae, [U-100% 13C; U-100% 15N], 1 mM; D2O, [U-100% 2H], 10%; sodium chloride 50 mM; sodium cacodylate 10 mM; H2O 90%

sample_conditions: pH: 6.5; temperature: 273 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample	isotropic	sample_conditions
2D 1H-13C HSQC	sample	isotropic	sample_conditions
3D HNCO	sample	isotropic	sample_conditions
3D HN(CO)CA	sample	isotropic	sample_conditions
3D HNCA	sample	isotropic	sample_conditions
3D HNCACB	sample	isotropic	sample_conditions
3D CBCA(CO)NH	sample	isotropic	sample_conditions
3D 15N-TOCSY-HSQC	sample	isotropic	sample_conditions

Software:

CCPN, CCPN - chemical shift assignment

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

TALOS, Cornilescu, Delaglio and Bax - data analysis

NMR spectrometers:

Varian Unity 500 MHz
Bruker Avance 600 MHz

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