BMRB Entry 15813

Name: 1H, 13C and 15N resonance assignments of the ribosome binding domain of E. coli Trigger Factor
Published: 2008-11-25

Chem Shift validation: AVS_anomalous, AVS_full, LACS
BMRB Entry DOI: doi:10.13018/BMR15813

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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 the ribosome binding domain of E. coli Trigger Factor

Deposition date:

2008-06-21

Original release date:

2008-11-25

Authors:

Hsu, Shang-Te Danny; Cabrita, Lisa; Christodoulou, John; Dobson, Christopher

Citation:

Citation: Hsu, Shang-Te; Dobson, Christopher. "1H, 15N and 13C assignments of the dimeric ribosome binding domain of trigger factor from Escherichia coli" Biomol. NMR Assignments 3, 17-20 (2009).
PubMed: 19636937

Assembly members:

Assembly members:
E._coli_TF-RBD, polymer, 117 residues, Formula weight is not available

Natural source:

Natural source: Common Name: E. coli Taxonomy ID: 562 Superkingdom: Bacteria Kingdom: not available Genus/species: Escherichia coli

Experimental source:

Experimental source: Production method: recombinant technology Host organism: Escherichia coli Vector: N/A

Entity Sequences (FASTA):

Entity Sequences (FASTA):
E._coli_TF-RBD: MQVSVETTQGLGRRVTITIA ADSIETAVKSELVNVAKKVR IDGFRKGKVPMNIVAQRYGA SVRQDVLGDLMSRNFIDAII KEKINPAGAPTYVPGEYKLG EDFTYSVEFEVYPEVEL

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	469
15N chemical shifts	115
1H chemical shifts	781

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	E. coli TF-RBD, chain 1	1
2	E. coli TF-RBD, chain 2	1

Entities:

Entity 1, E. coli TF-RBD, chain 1 117 residues - Formula weight is not available

1

MET

GLN

VAL

SER

VAL

GLU

THR

GLN

GLY

2

LEU

GLY

ARG

VAL

THR

ILE

THR

ILE

ALA

3

ALA

ASP

SER

ILE

GLU

THR

ALA

VAL

LYS

SER

4

GLU

LEU

VAL

ASN

VAL

ALA

LYS

VAL

ARG

5

ILE

ASP

GLY

PHE

ARG

LYS

GLY

LYS

VAL

PRO

6

MET

ASN

ILE

VAL

ALA

GLN

ARG

TYR

GLY

ALA

7

SER

VAL

ARG

GLN

ASP

VAL

LEU

GLY

ASP

LEU

8

MET

SER

ARG

ASN

PHE

ILE

ASP

ALA

ILE

9

LYS

GLU

LYS

ILE

ASN

PRO

ALA

GLY

ALA

PRO

10

THR

TYR

VAL

PRO

GLY

GLU

TYR

LYS

LEU

GLY

11

GLU

ASP

PHE

THR

TYR

SER

VAL

GLU

PHE

GLU

12

VAL

TYR

PRO

GLU

VAL

GLU

LEU

Samples:

13C_15N_TF-RBD: E. coli TF-RBD, [U-98% 13C; U-98% 15N], 0.2 mM; Tris 10 uM; (NH4)2.SO4 200 mM; H2O 90%; D2O, [U-100% 2H], 10%

298K: ionic strength: 0.2 M; pH: 7.35; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	13C_15N_TF-RBD	isotropic	298K
2D 1H-13C HSQC	13C_15N_TF-RBD	isotropic	298K
3D HNCO	13C_15N_TF-RBD	isotropic	298K
3D HNCA	13C_15N_TF-RBD	isotropic	298K
3D HNCACB	13C_15N_TF-RBD	isotropic	298K
3D CBCA(CO)NH	13C_15N_TF-RBD	isotropic	298K
3D HN(CO)CA	13C_15N_TF-RBD	isotropic	298K
3D HBHA(CO)NH	13C_15N_TF-RBD	isotropic	298K
3D 1H-15N NOESY	13C_15N_TF-RBD	isotropic	298K
3D 1H-15N TOCSY	13C_15N_TF-RBD	isotropic	298K
3D 1H-13C NOESY	13C_15N_TF-RBD	isotropic	298K
3D HCCH-COSY	13C_15N_TF-RBD	isotropic	298K
3D H(CCO)NH	13C_15N_TF-RBD	isotropic	298K
3D HNHA	13C_15N_TF-RBD	isotropic	298K

Software:

SPARKY v3.1, Goddard - data analysis

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

NMR spectrometers:

Bruker Avance 700 MHz
Bruker Avance 500 MHz

PDB	1OMS 1P9Y 1W26 1W2B 2MLX 2MLY 2MLZ 2VRH
DBJ	BAB33913 BAD98926 BAE76216 BAG75986 BAI23810
EMBL	CAA35634 CAD08906 CAP74970 CAQ30908 CAQ97312
GB	AAA62791 AAB40192 AAC73539 AAG54786 AAL19402
PIR	AB0558
REF	NP_308517 NP_414970 NP_455044 NP_459443 NP_706330
SP	A1A8A5 A7ZIJ4 A7ZX94 A9MM24 A9MWX9
AlphaFold	A1A8A5 A7ZIJ4 A7ZX94 A9MM24 A9MWX9