BMRB Entry 17615

Name: Solution Structure of RfaH carboxyterminal domain
Published: 2012-07-30

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PDB ID: 2lcl
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_full, LACS, SPARTA
BMRB Entry DOI: doi:10.13018/BMR17615
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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:

Solution Structure of RfaH carboxyterminal domain

Deposition date:

2011-05-02

Original release date:

2012-07-30

Authors:

Burmann, Bjoern; Schweimer, Kristian; Roesch, Paul

Citation:

Citation: Burmann, Bjoern; Schweimer, Kristian; Roesch, Paul; Knauer, Stefan; Mooney, Rachel; Sevostyanova, Anastasia; Landick, Robert; Artsimovitch, Irina. "An alpha-helix to beta-barrel domain switch transforms the transcription factor RfaH into a translation factor" Cell 150, 291-303 (2012).
PubMed: 22817892

Assembly members:

Assembly members:
entity, polymer, 66 residues, 7269.401 Da.

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: BL21-DE3

Entity Sequences (FASTA):

Entity Sequences (FASTA):
entity: GAMGPKDIVDPATPYPGDKV IITEGAFEGFQAIFTEPDGE ARSMLLLNLINKEIKHSVKN TEFRKL

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	211
15N chemical shifts	62
1H chemical shifts	473

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
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Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	RfaH	1

Entities:

Entity 1, RfaH 66 residues - 7269.401 Da.

1

GLY

ALA

MET

GLY

PRO

LYS

ASP

ILE

VAL

ASP

2

PRO

ALA

THR

PRO

TYR

PRO

GLY

ASP

LYS

VAL

3

ILE

THR

GLU

GLY

ALA

PHE

GLU

GLY

PHE

4

GLN

ALA

ILE

PHE

THR

GLU

PRO

ASP

GLY

GLU

5

ALA

ARG

SER

MET

LEU

ASN

LEU

ILE

6

ASN

LYS

GLU

ILE

LYS

HIS

SER

VAL

LYS

ASN

7

THR

GLU

PHE

ARG

LYS

LEU

Samples:

sample_1: RfaH-CTD, [U-99% 13C; U-99% 15N], 0.5 mM; HEPES 0.025 mM; NaCl 0.05 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 75 mM; pH: 7.5; pressure: 1 atm; temperature: 298 K

Experiments:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_1	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_1	isotropic	sample_conditions_1
3D HNCACB	sample_1	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_1	isotropic	sample_conditions_1
3D C(CO)NH	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aliphatic	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY aromatic	sample_1	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1

Software:

NMRView, Johnson, One Moon Scientific - chemical shift assignment, data analysis, peak picking

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - structure solution

NMR spectrometers:

Bruker Avance 600 MHz
Bruker Avance 800 MHz

PDB	2LCL 2OUG
DBJ	BAB38193 BAE77461 BAG79652 BAI27905 BAI33028
EMBL	CAA46147 CAP78305 CAQ34199 CAR00816 CAR05481
GB	AAA67638 AAA91060 AAC76845 AAG10071 AAG59036
REF	NP_312797 NP_418284 NP_709646 WP_001161073 WP_001192387
SP	P0AFW0 P0AFW1 Q0TAL4 Q8FBI4
AlphaFold	P0AFW0 P0AFW1 Q0TAL4 Q8FBI4